path: root/plip/test/pdb/4pjt.pdb

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       12-MAY-14   4PJT              
TITLE     STRUCTURE OF PARP1 CATALYTIC DOMAIN BOUND TO INHIBITOR BMN 673        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 1;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: PARP1 HELICAL AND CATALYTIC DOMAINS (UNP RESIDUES 662-     
COMPND   5 1011);                                                               
COMPND   6 SYNONYM: PARP-1,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 1,ARTD1,
COMPND   7 NAD(+) ADP-RIBOSYLTRANSFERASE 1,ADPRT 1,POLY[ADP-RIBOSE] SYNTHASE 1; 
COMPND   8 EC: 2.4.2.30;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PARP1, ADPRT, PPOL;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    PARP1, INHIBITOR, COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.AOYAGI-SCHARBER,A.S.GARDBERG,T.L.ARAKAKI                            
REVDAT   1   24-SEP-14 4PJT    0                                                
JRNL        AUTH   M.AOYAGI-SCHARBER,A.S.GARDBERG,B.K.YIP,B.WANG,Y.SHEN,        
JRNL        AUTH 2 P.A.FITZPATRICK                                              
JRNL        TITL   STRUCTURAL BASIS FOR THE INHIBITION OF POLY(ADP-RIBOSE)      
JRNL        TITL 2 POLYMERASES 1 AND 2 BY BMN 673, A POTENT INHIBITOR DERIVED   
JRNL        TITL 3 FROM DIHYDROPYRIDOPHTHALAZINONE.                             
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  70  1143 2014              
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   25195882                                                     
JRNL        DOI    10.1107/S2053230X14015088                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0071                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 63499                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3387                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4577                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.44                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 232                          
REMARK   3   BIN FREE R VALUE                    : 0.2710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10173                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 205                                     
REMARK   3   SOLVENT ATOMS            : 316                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.07000                                             
REMARK   3    B33 (A**2) : 0.08000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.324         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.224         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.110        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10591 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9888 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14409 ; 1.461 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22713 ; 1.255 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1333 ; 5.775 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   425 ;37.699 ;25.294       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1709 ;14.247 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;18.128 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1669 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11892 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2239 ; 0.006 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5359 ; 2.308 ; 3.412       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5358 ; 2.307 ; 3.411       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6674 ; 3.560 ; 5.100       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6675 ; 3.560 ; 5.100       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5232 ; 2.860 ; 3.551       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5232 ; 2.859 ; 3.551       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7733 ; 4.479 ; 5.235       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 11799 ; 6.073 ;26.654       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 11720 ; 6.024 ;26.593       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   662   1010       B   662   1010   18558  0.11  0.05     
REMARK   3    2     A   662   1010       C   662   1010   19168  0.12  0.05     
REMARK   3    3     A   663   1009       D   663   1009   18422  0.09  0.05     
REMARK   3    4     B   662   1010       C   662   1010   19157  0.09  0.05     
REMARK   3    5     B   663   1009       D   663   1009   17719  0.10  0.05     
REMARK   3    6     C   663   1009       D   663   1009   18110  0.11  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   662        A  1101                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.7499   3.3550 -10.5927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0248 T22:   0.0256                                     
REMARK   3      T33:   0.0328 T12:   0.0012                                     
REMARK   3      T13:  -0.0015 T23:  -0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5187 L22:   0.4526                                     
REMARK   3      L33:   0.2806 L12:  -0.1621                                     
REMARK   3      L13:   0.1081 L23:   0.1240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0029 S12:   0.0104 S13:  -0.0019                       
REMARK   3      S21:  -0.0027 S22:   0.0208 S23:  -0.0045                       
REMARK   3      S31:   0.0175 S32:   0.0075 S33:  -0.0237                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   662        B  1101                          
REMARK   3    ORIGIN FOR THE GROUP (A): -83.8829  -3.6409   4.2278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0301 T22:   0.0513                                     
REMARK   3      T33:   0.0286 T12:  -0.0310                                     
REMARK   3      T13:  -0.0210 T23:   0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6863 L22:   0.8257                                     
REMARK   3      L33:   0.8405 L12:   0.1879                                     
REMARK   3      L13:   0.0086 L23:  -0.0585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0204 S12:   0.0022 S13:   0.0266                       
REMARK   3      S21:   0.0213 S22:   0.0753 S23:  -0.0344                       
REMARK   3      S31:   0.1358 S32:  -0.1665 S33:  -0.0957                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   662        C  1101                          
REMARK   3    ORIGIN FOR THE GROUP (A): -74.9094  33.0828 -29.1980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0295 T22:   0.0238                                     
REMARK   3      T33:   0.0226 T12:   0.0015                                     
REMARK   3      T13:   0.0138 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5665 L22:   0.2765                                     
REMARK   3      L33:   1.0166 L12:  -0.2135                                     
REMARK   3      L13:  -0.3885 L23:   0.0196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0391 S12:   0.0503 S13:   0.0568                       
REMARK   3      S21:   0.0200 S22:   0.0260 S23:   0.0032                       
REMARK   3      S31:  -0.0329 S32:  -0.0317 S33:  -0.0651                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   663        D  1101                          
REMARK   3    ORIGIN FOR THE GROUP (A):-116.4501  19.2024 -23.7033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0635 T22:   0.0636                                     
REMARK   3      T33:   0.0337 T12:  -0.0350                                     
REMARK   3      T13:   0.0419 T23:  -0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7583 L22:   0.2142                                     
REMARK   3      L33:   0.6721 L12:  -0.5210                                     
REMARK   3      L13:   0.2224 L23:  -0.0063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0188 S12:   0.1591 S13:  -0.0579                       
REMARK   3      S21:  -0.0311 S22:  -0.0650 S23:  -0.0066                       
REMARK   3      S31:   0.1355 S32:  -0.0794 S33:   0.0463                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4PJT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201517.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97648                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66890                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.940                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1UK0, 3L3M                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 100MM TRIS, PH   
REMARK 280  7.2                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       51.84500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.07500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.84500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.07500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: RUNS AS MONOMER ON SIZING EXCLUSION COLUMN                   
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   642                                                      
REMARK 465     GLY A   643                                                      
REMARK 465     SER A   644                                                      
REMARK 465     SER A   645                                                      
REMARK 465     HIS A   646                                                      
REMARK 465     HIS A   647                                                      
REMARK 465     HIS A   648                                                      
REMARK 465     HIS A   649                                                      
REMARK 465     HIS A   650                                                      
REMARK 465     HIS A   651                                                      
REMARK 465     SER A   652                                                      
REMARK 465     GLY A   653                                                      
REMARK 465     LEU A   654                                                      
REMARK 465     VAL A   655                                                      
REMARK 465     PRO A   656                                                      
REMARK 465     ARG A   657                                                      
REMARK 465     GLY A   658                                                      
REMARK 465     SER A   659                                                      
REMARK 465     HIS A   660                                                      
REMARK 465     MET A   661                                                      
REMARK 465     GLY A   723                                                      
REMARK 465     SER A   724                                                      
REMARK 465     SER A   725                                                      
REMARK 465     GLY A   745                                                      
REMARK 465     MET A   746                                                      
REMARK 465     LYS A   747                                                      
REMARK 465     GLY A   781                                                      
REMARK 465     SER A   782                                                      
REMARK 465     ASP A   783                                                      
REMARK 465     ASP A   784                                                      
REMARK 465     SER A   785                                                      
REMARK 465     THR A  1011                                                      
REMARK 465     MET B   642                                                      
REMARK 465     GLY B   643                                                      
REMARK 465     SER B   644                                                      
REMARK 465     SER B   645                                                      
REMARK 465     HIS B   646                                                      
REMARK 465     HIS B   647                                                      
REMARK 465     HIS B   648                                                      
REMARK 465     HIS B   649                                                      
REMARK 465     HIS B   650                                                      
REMARK 465     HIS B   651                                                      
REMARK 465     SER B   652                                                      
REMARK 465     GLY B   653                                                      
REMARK 465     LEU B   654                                                      
REMARK 465     VAL B   655                                                      
REMARK 465     PRO B   656                                                      
REMARK 465     ARG B   657                                                      
REMARK 465     GLY B   658                                                      
REMARK 465     SER B   659                                                      
REMARK 465     HIS B   660                                                      
REMARK 465     MET B   661                                                      
REMARK 465     GLN B   722                                                      
REMARK 465     GLY B   723                                                      
REMARK 465     SER B   724                                                      
REMARK 465     SER B   725                                                      
REMARK 465     PHE B   744                                                      
REMARK 465     GLY B   745                                                      
REMARK 465     MET B   746                                                      
REMARK 465     LYS B   747                                                      
REMARK 465     LYS B   748                                                      
REMARK 465     PRO B   749                                                      
REMARK 465     GLY B   781                                                      
REMARK 465     SER B   782                                                      
REMARK 465     ASP B   783                                                      
REMARK 465     ASP B   784                                                      
REMARK 465     SER B   785                                                      
REMARK 465     HIS B   937                                                      
REMARK 465     ILE B   938                                                      
REMARK 465     THR B  1011                                                      
REMARK 465     MET C   642                                                      
REMARK 465     GLY C   643                                                      
REMARK 465     SER C   644                                                      
REMARK 465     SER C   645                                                      
REMARK 465     HIS C   646                                                      
REMARK 465     HIS C   647                                                      
REMARK 465     HIS C   648                                                      
REMARK 465     HIS C   649                                                      
REMARK 465     HIS C   650                                                      
REMARK 465     HIS C   651                                                      
REMARK 465     SER C   652                                                      
REMARK 465     GLY C   653                                                      
REMARK 465     LEU C   654                                                      
REMARK 465     VAL C   655                                                      
REMARK 465     PRO C   656                                                      
REMARK 465     ARG C   657                                                      
REMARK 465     GLY C   658                                                      
REMARK 465     SER C   659                                                      
REMARK 465     HIS C   660                                                      
REMARK 465     MET C   661                                                      
REMARK 465     SER C   782                                                      
REMARK 465     ASP C   783                                                      
REMARK 465     ASP C   784                                                      
REMARK 465     THR C  1011                                                      
REMARK 465     MET D   642                                                      
REMARK 465     GLY D   643                                                      
REMARK 465     SER D   644                                                      
REMARK 465     SER D   645                                                      
REMARK 465     HIS D   646                                                      
REMARK 465     HIS D   647                                                      
REMARK 465     HIS D   648                                                      
REMARK 465     HIS D   649                                                      
REMARK 465     HIS D   650                                                      
REMARK 465     HIS D   651                                                      
REMARK 465     SER D   652                                                      
REMARK 465     GLY D   653                                                      
REMARK 465     LEU D   654                                                      
REMARK 465     VAL D   655                                                      
REMARK 465     PRO D   656                                                      
REMARK 465     ARG D   657                                                      
REMARK 465     GLY D   658                                                      
REMARK 465     SER D   659                                                      
REMARK 465     HIS D   660                                                      
REMARK 465     MET D   661                                                      
REMARK 465     LYS D   662                                                      
REMARK 465     GLN D   722                                                      
REMARK 465     GLY D   723                                                      
REMARK 465     SER D   724                                                      
REMARK 465     SER D   725                                                      
REMARK 465     ASP D   726                                                      
REMARK 465     SER D   727                                                      
REMARK 465     GLN D   728                                                      
REMARK 465     ILE D   729                                                      
REMARK 465     PHE D   744                                                      
REMARK 465     GLY D   745                                                      
REMARK 465     MET D   746                                                      
REMARK 465     LYS D   747                                                      
REMARK 465     LYS D   748                                                      
REMARK 465     GLY D   780                                                      
REMARK 465     GLY D   781                                                      
REMARK 465     SER D   782                                                      
REMARK 465     ASP D   783                                                      
REMARK 465     ASP D   784                                                      
REMARK 465     SER D   785                                                      
REMARK 465     SER D   786                                                      
REMARK 465     LYS D   787                                                      
REMARK 465     LYS D  1010                                                      
REMARK 465     THR D  1011                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 662    CG   CD   CE   NZ                                   
REMARK 470     LYS A 664    CG   CD   CE   NZ                                   
REMARK 470     LYS A 667    CG   CD   CE   NZ                                   
REMARK 470     LYS A 700    CG   CD   CE   NZ                                   
REMARK 470     LEU A 701    CG   CD1  CD2                                       
REMARK 470     LYS A 703    CG   CD   CE   NZ                                   
REMARK 470     ARG A 704    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 705    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 726    CG   OD1  OD2                                       
REMARK 470     GLN A 728    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 730    CG   CD1  CD2                                       
REMARK 470     ARG A 735    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 748    CG   CD   CE   NZ                                   
REMARK 470     LEU A 751    CG   CD1  CD2                                       
REMARK 470     ARG A 779    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 786    OG                                                  
REMARK 470     LYS A 787    CG   CD   CE   NZ                                   
REMARK 470     ARG A 806    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 852    CG   CD   CE   NZ                                   
REMARK 470     LYS A 940    CG   CD   CE   NZ                                   
REMARK 470     LYS A 943    CG   CD   CE   NZ                                   
REMARK 470     LYS B 662    CG   CD   CE   NZ                                   
REMARK 470     SER B 663    OG                                                  
REMARK 470     LYS B 664    CG   CD   CE   NZ                                   
REMARK 470     LYS B 667    CG   CD   CE   NZ                                   
REMARK 470     LYS B 684    CG   CD   CE   NZ                                   
REMARK 470     GLU B 690    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 694    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 695    CG   CD   CE   NZ                                   
REMARK 470     LYS B 700    CG   CD   CE   NZ                                   
REMARK 470     ARG B 704    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 705    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 718    CG   CD   OE1  NE2                                  
REMARK 470     SER B 721    OG                                                  
REMARK 470     ASP B 726    CG   OD1  OD2                                       
REMARK 470     SER B 727    OG                                                  
REMARK 470     LEU B 730    CG   CD1  CD2                                       
REMARK 470     ARG B 735    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 743    CG   OD1  OD2                                       
REMARK 470     LEU B 751    CG   CD1  CD2                                       
REMARK 470     ARG B 779    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 786    OG                                                  
REMARK 470     LYS B 787    CG   CD   CE   NZ                                   
REMARK 470     LYS B 796    CG   CD   CE   NZ                                   
REMARK 470     ARG B 806    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 912    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 933    CG   CD   CE   NZ                                   
REMARK 470     LYS B 940    CG   CD   CE   NZ                                   
REMARK 470     LYS B 953    CG   CD   CE   NZ                                   
REMARK 470     SER B 959    OG                                                  
REMARK 470     ASN B 980    CG   OD1  ND2                                       
REMARK 470     ASP B 981    CG   OD1  OD2                                       
REMARK 470     LYS B1006    CG   CD   CE   NZ                                   
REMARK 470     LYS B1010    CG   CD   CE   NZ                                   
REMARK 470     LYS C 662    CG   CD   CE   NZ                                   
REMARK 470     SER C 663    OG                                                  
REMARK 470     LYS C 664    CG   CD   CE   NZ                                   
REMARK 470     LYS C 667    CG   CD   CE   NZ                                   
REMARK 470     LYS C 695    CG   CD   CE   NZ                                   
REMARK 470     LYS C 700    CG   CD   CE   NZ                                   
REMARK 470     ARG C 704    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 728    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 731    CG   OD1  OD2                                       
REMARK 470     LYS C 747    CG   CD   CE   NZ                                   
REMARK 470     LYS C 748    CG   CD   CE   NZ                                   
REMARK 470     ARG C 779    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C 786    OG                                                  
REMARK 470     LYS C 787    CG   CD   CE   NZ                                   
REMARK 470     LYS C 798    CG   CD   CE   NZ                                   
REMARK 470     ARG C 806    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 812    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 849    CG   CD   CE   NZ                                   
REMARK 470     LYS C 852    CG   CD   CE   NZ                                   
REMARK 470     SER C 939    OG                                                  
REMARK 470     LYS C 940    CG   CD   CE   NZ                                   
REMARK 470     ASN C 980    CG   OD1  ND2                                       
REMARK 470     LYS C1006    CG   CD   CE   NZ                                   
REMARK 470     LYS C1010    CG   CD   CE   NZ                                   
REMARK 470     LYS D 664    CG   CD   CE   NZ                                   
REMARK 470     LYS D 667    CG   CD   CE   NZ                                   
REMARK 470     LYS D 674    CG   CD   CE   NZ                                   
REMARK 470     GLU D 680    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 683    CG   CD   CE   NZ                                   
REMARK 470     GLU D 690    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 692    CG   OD1  OD2                                       
REMARK 470     LEU D 693    CG   CD1  CD2                                       
REMARK 470     GLN D 694    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 695    CG   CD   CE   NZ                                   
REMARK 470     LEU D 698    CG   CD1  CD2                                       
REMARK 470     LYS D 700    CG   CD   CE   NZ                                   
REMARK 470     LEU D 701    CG   CD1  CD2                                       
REMARK 470     LYS D 703    CG   CD   CE   NZ                                   
REMARK 470     ARG D 704    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 705    CG   CD   OE1  NE2                                  
REMARK 470     LEU D 730    CG   CD1  CD2                                       
REMARK 470     ARG D 735    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO D 749    CG   CD                                             
REMARK 470     SER D 757    OG                                                  
REMARK 470     LYS D 761    CG   CD   CE   NZ                                   
REMARK 470     TYR D 775    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU D 778    CG   CD1  CD2                                       
REMARK 470     ARG D 779    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 798    CG   CD   CE   NZ                                   
REMARK 470     ASP D 805    CG   OD1  OD2                                       
REMARK 470     ARG D 806    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 807    CG   OD1  OD2                                       
REMARK 470     GLU D 809    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 816    CG   CD   CE   NZ                                   
REMARK 470     GLU D 832    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 842    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 940    CG   CD   CE   NZ                                   
REMARK 470     SER D 959    OG                                                  
REMARK 470     SER D 963    OG                                                  
REMARK 470     LYS D1006    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ   LYS D   953     O    HOH D  1201              2.06            
REMARK 500   O2   SO4 C  1101     O    HOH C  1266              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 841   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 841   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG B 841   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG B 841   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG C 841   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG C 841   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG D 841   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG D 841   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 826       66.52   -102.27                                   
REMARK 500    SER A 936      113.97   -161.38                                   
REMARK 500    HIS B 826       62.86   -104.33                                   
REMARK 500    HIS C 826       63.80   -104.43                                   
REMARK 500    SER C 939      -74.73    -98.01                                   
REMARK 500    HIS D 826       65.44   -102.69                                   
REMARK 500    SER D 936      113.64   -162.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ A 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ B 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ C 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ D 1104                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4PJV   RELATED DB: PDB                                   
DBREF  4PJT A  662  1011  UNP    P09874   PARP1_HUMAN    662   1011             
DBREF  4PJT B  662  1011  UNP    P09874   PARP1_HUMAN    662   1011             
DBREF  4PJT C  662  1011  UNP    P09874   PARP1_HUMAN    662   1011             
DBREF  4PJT D  662  1011  UNP    P09874   PARP1_HUMAN    662   1011             
SEQADV 4PJT MET A  642  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY A  643  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER A  644  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER A  645  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS A  646  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS A  647  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS A  648  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS A  649  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS A  650  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS A  651  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER A  652  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY A  653  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT LEU A  654  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT VAL A  655  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT PRO A  656  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT ARG A  657  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY A  658  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER A  659  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS A  660  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT MET A  661  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT MET B  642  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY B  643  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER B  644  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER B  645  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS B  646  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS B  647  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS B  648  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS B  649  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS B  650  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS B  651  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER B  652  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY B  653  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT LEU B  654  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT VAL B  655  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT PRO B  656  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT ARG B  657  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY B  658  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER B  659  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS B  660  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT MET B  661  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT MET C  642  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY C  643  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER C  644  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER C  645  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS C  646  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS C  647  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS C  648  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS C  649  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS C  650  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS C  651  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER C  652  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY C  653  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT LEU C  654  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT VAL C  655  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT PRO C  656  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT ARG C  657  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY C  658  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER C  659  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS C  660  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT MET C  661  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT MET D  642  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY D  643  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER D  644  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER D  645  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS D  646  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS D  647  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS D  648  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS D  649  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS D  650  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS D  651  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER D  652  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY D  653  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT LEU D  654  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT VAL D  655  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT PRO D  656  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT ARG D  657  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT GLY D  658  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT SER D  659  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT HIS D  660  UNP  P09874              EXPRESSION TAG                 
SEQADV 4PJT MET D  661  UNP  P09874              EXPRESSION TAG                 
SEQRES   1 A  370  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU          
SEQRES   2 A  370  VAL PRO ARG GLY SER HIS MET LYS SER LYS LEU PRO LYS          
SEQRES   3 A  370  PRO VAL GLN ASP LEU ILE LYS MET ILE PHE ASP VAL GLU          
SEQRES   4 A  370  SER MET LYS LYS ALA MET VAL GLU TYR GLU ILE ASP LEU          
SEQRES   5 A  370  GLN LYS MET PRO LEU GLY LYS LEU SER LYS ARG GLN ILE          
SEQRES   6 A  370  GLN ALA ALA TYR SER ILE LEU SER GLU VAL GLN GLN ALA          
SEQRES   7 A  370  VAL SER GLN GLY SER SER ASP SER GLN ILE LEU ASP LEU          
SEQRES   8 A  370  SER ASN ARG PHE TYR THR LEU ILE PRO HIS ASP PHE GLY          
SEQRES   9 A  370  MET LYS LYS PRO PRO LEU LEU ASN ASN ALA ASP SER VAL          
SEQRES  10 A  370  GLN ALA LYS VAL GLU MET LEU ASP ASN LEU LEU ASP ILE          
SEQRES  11 A  370  GLU VAL ALA TYR SER LEU LEU ARG GLY GLY SER ASP ASP          
SEQRES  12 A  370  SER SER LYS ASP PRO ILE ASP VAL ASN TYR GLU LYS LEU          
SEQRES  13 A  370  LYS THR ASP ILE LYS VAL VAL ASP ARG ASP SER GLU GLU          
SEQRES  14 A  370  ALA GLU ILE ILE ARG LYS TYR VAL LYS ASN THR HIS ALA          
SEQRES  15 A  370  THR THR HIS ASN ALA TYR ASP LEU GLU VAL ILE ASP ILE          
SEQRES  16 A  370  PHE LYS ILE GLU ARG GLU GLY GLU CYS GLN ARG TYR LYS          
SEQRES  17 A  370  PRO PHE LYS GLN LEU HIS ASN ARG ARG LEU LEU TRP HIS          
SEQRES  18 A  370  GLY SER ARG THR THR ASN PHE ALA GLY ILE LEU SER GLN          
SEQRES  19 A  370  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO VAL THR GLY          
SEQRES  20 A  370  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET VAL          
SEQRES  21 A  370  SER LYS SER ALA ASN TYR CYS HIS THR SER GLN GLY ASP          
SEQRES  22 A  370  PRO ILE GLY LEU ILE LEU LEU GLY GLU VAL ALA LEU GLY          
SEQRES  23 A  370  ASN MET TYR GLU LEU LYS HIS ALA SER HIS ILE SER LYS          
SEQRES  24 A  370  LEU PRO LYS GLY LYS HIS SER VAL LYS GLY LEU GLY LYS          
SEQRES  25 A  370  THR THR PRO ASP PRO SER ALA ASN ILE SER LEU ASP GLY          
SEQRES  26 A  370  VAL ASP VAL PRO LEU GLY THR GLY ILE SER SER GLY VAL          
SEQRES  27 A  370  ASN ASP THR SER LEU LEU TYR ASN GLU TYR ILE VAL TYR          
SEQRES  28 A  370  ASP ILE ALA GLN VAL ASN LEU LYS TYR LEU LEU LYS LEU          
SEQRES  29 A  370  LYS PHE ASN PHE LYS THR                                      
SEQRES   1 B  370  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU          
SEQRES   2 B  370  VAL PRO ARG GLY SER HIS MET LYS SER LYS LEU PRO LYS          
SEQRES   3 B  370  PRO VAL GLN ASP LEU ILE LYS MET ILE PHE ASP VAL GLU          
SEQRES   4 B  370  SER MET LYS LYS ALA MET VAL GLU TYR GLU ILE ASP LEU          
SEQRES   5 B  370  GLN LYS MET PRO LEU GLY LYS LEU SER LYS ARG GLN ILE          
SEQRES   6 B  370  GLN ALA ALA TYR SER ILE LEU SER GLU VAL GLN GLN ALA          
SEQRES   7 B  370  VAL SER GLN GLY SER SER ASP SER GLN ILE LEU ASP LEU          
SEQRES   8 B  370  SER ASN ARG PHE TYR THR LEU ILE PRO HIS ASP PHE GLY          
SEQRES   9 B  370  MET LYS LYS PRO PRO LEU LEU ASN ASN ALA ASP SER VAL          
SEQRES  10 B  370  GLN ALA LYS VAL GLU MET LEU ASP ASN LEU LEU ASP ILE          
SEQRES  11 B  370  GLU VAL ALA TYR SER LEU LEU ARG GLY GLY SER ASP ASP          
SEQRES  12 B  370  SER SER LYS ASP PRO ILE ASP VAL ASN TYR GLU LYS LEU          
SEQRES  13 B  370  LYS THR ASP ILE LYS VAL VAL ASP ARG ASP SER GLU GLU          
SEQRES  14 B  370  ALA GLU ILE ILE ARG LYS TYR VAL LYS ASN THR HIS ALA          
SEQRES  15 B  370  THR THR HIS ASN ALA TYR ASP LEU GLU VAL ILE ASP ILE          
SEQRES  16 B  370  PHE LYS ILE GLU ARG GLU GLY GLU CYS GLN ARG TYR LYS          
SEQRES  17 B  370  PRO PHE LYS GLN LEU HIS ASN ARG ARG LEU LEU TRP HIS          
SEQRES  18 B  370  GLY SER ARG THR THR ASN PHE ALA GLY ILE LEU SER GLN          
SEQRES  19 B  370  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO VAL THR GLY          
SEQRES  20 B  370  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET VAL          
SEQRES  21 B  370  SER LYS SER ALA ASN TYR CYS HIS THR SER GLN GLY ASP          
SEQRES  22 B  370  PRO ILE GLY LEU ILE LEU LEU GLY GLU VAL ALA LEU GLY          
SEQRES  23 B  370  ASN MET TYR GLU LEU LYS HIS ALA SER HIS ILE SER LYS          
SEQRES  24 B  370  LEU PRO LYS GLY LYS HIS SER VAL LYS GLY LEU GLY LYS          
SEQRES  25 B  370  THR THR PRO ASP PRO SER ALA ASN ILE SER LEU ASP GLY          
SEQRES  26 B  370  VAL ASP VAL PRO LEU GLY THR GLY ILE SER SER GLY VAL          
SEQRES  27 B  370  ASN ASP THR SER LEU LEU TYR ASN GLU TYR ILE VAL TYR          
SEQRES  28 B  370  ASP ILE ALA GLN VAL ASN LEU LYS TYR LEU LEU LYS LEU          
SEQRES  29 B  370  LYS PHE ASN PHE LYS THR                                      
SEQRES   1 C  370  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU          
SEQRES   2 C  370  VAL PRO ARG GLY SER HIS MET LYS SER LYS LEU PRO LYS          
SEQRES   3 C  370  PRO VAL GLN ASP LEU ILE LYS MET ILE PHE ASP VAL GLU          
SEQRES   4 C  370  SER MET LYS LYS ALA MET VAL GLU TYR GLU ILE ASP LEU          
SEQRES   5 C  370  GLN LYS MET PRO LEU GLY LYS LEU SER LYS ARG GLN ILE          
SEQRES   6 C  370  GLN ALA ALA TYR SER ILE LEU SER GLU VAL GLN GLN ALA          
SEQRES   7 C  370  VAL SER GLN GLY SER SER ASP SER GLN ILE LEU ASP LEU          
SEQRES   8 C  370  SER ASN ARG PHE TYR THR LEU ILE PRO HIS ASP PHE GLY          
SEQRES   9 C  370  MET LYS LYS PRO PRO LEU LEU ASN ASN ALA ASP SER VAL          
SEQRES  10 C  370  GLN ALA LYS VAL GLU MET LEU ASP ASN LEU LEU ASP ILE          
SEQRES  11 C  370  GLU VAL ALA TYR SER LEU LEU ARG GLY GLY SER ASP ASP          
SEQRES  12 C  370  SER SER LYS ASP PRO ILE ASP VAL ASN TYR GLU LYS LEU          
SEQRES  13 C  370  LYS THR ASP ILE LYS VAL VAL ASP ARG ASP SER GLU GLU          
SEQRES  14 C  370  ALA GLU ILE ILE ARG LYS TYR VAL LYS ASN THR HIS ALA          
SEQRES  15 C  370  THR THR HIS ASN ALA TYR ASP LEU GLU VAL ILE ASP ILE          
SEQRES  16 C  370  PHE LYS ILE GLU ARG GLU GLY GLU CYS GLN ARG TYR LYS          
SEQRES  17 C  370  PRO PHE LYS GLN LEU HIS ASN ARG ARG LEU LEU TRP HIS          
SEQRES  18 C  370  GLY SER ARG THR THR ASN PHE ALA GLY ILE LEU SER GLN          
SEQRES  19 C  370  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO VAL THR GLY          
SEQRES  20 C  370  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET VAL          
SEQRES  21 C  370  SER LYS SER ALA ASN TYR CYS HIS THR SER GLN GLY ASP          
SEQRES  22 C  370  PRO ILE GLY LEU ILE LEU LEU GLY GLU VAL ALA LEU GLY          
SEQRES  23 C  370  ASN MET TYR GLU LEU LYS HIS ALA SER HIS ILE SER LYS          
SEQRES  24 C  370  LEU PRO LYS GLY LYS HIS SER VAL LYS GLY LEU GLY LYS          
SEQRES  25 C  370  THR THR PRO ASP PRO SER ALA ASN ILE SER LEU ASP GLY          
SEQRES  26 C  370  VAL ASP VAL PRO LEU GLY THR GLY ILE SER SER GLY VAL          
SEQRES  27 C  370  ASN ASP THR SER LEU LEU TYR ASN GLU TYR ILE VAL TYR          
SEQRES  28 C  370  ASP ILE ALA GLN VAL ASN LEU LYS TYR LEU LEU LYS LEU          
SEQRES  29 C  370  LYS PHE ASN PHE LYS THR                                      
SEQRES   1 D  370  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU          
SEQRES   2 D  370  VAL PRO ARG GLY SER HIS MET LYS SER LYS LEU PRO LYS          
SEQRES   3 D  370  PRO VAL GLN ASP LEU ILE LYS MET ILE PHE ASP VAL GLU          
SEQRES   4 D  370  SER MET LYS LYS ALA MET VAL GLU TYR GLU ILE ASP LEU          
SEQRES   5 D  370  GLN LYS MET PRO LEU GLY LYS LEU SER LYS ARG GLN ILE          
SEQRES   6 D  370  GLN ALA ALA TYR SER ILE LEU SER GLU VAL GLN GLN ALA          
SEQRES   7 D  370  VAL SER GLN GLY SER SER ASP SER GLN ILE LEU ASP LEU          
SEQRES   8 D  370  SER ASN ARG PHE TYR THR LEU ILE PRO HIS ASP PHE GLY          
SEQRES   9 D  370  MET LYS LYS PRO PRO LEU LEU ASN ASN ALA ASP SER VAL          
SEQRES  10 D  370  GLN ALA LYS VAL GLU MET LEU ASP ASN LEU LEU ASP ILE          
SEQRES  11 D  370  GLU VAL ALA TYR SER LEU LEU ARG GLY GLY SER ASP ASP          
SEQRES  12 D  370  SER SER LYS ASP PRO ILE ASP VAL ASN TYR GLU LYS LEU          
SEQRES  13 D  370  LYS THR ASP ILE LYS VAL VAL ASP ARG ASP SER GLU GLU          
SEQRES  14 D  370  ALA GLU ILE ILE ARG LYS TYR VAL LYS ASN THR HIS ALA          
SEQRES  15 D  370  THR THR HIS ASN ALA TYR ASP LEU GLU VAL ILE ASP ILE          
SEQRES  16 D  370  PHE LYS ILE GLU ARG GLU GLY GLU CYS GLN ARG TYR LYS          
SEQRES  17 D  370  PRO PHE LYS GLN LEU HIS ASN ARG ARG LEU LEU TRP HIS          
SEQRES  18 D  370  GLY SER ARG THR THR ASN PHE ALA GLY ILE LEU SER GLN          
SEQRES  19 D  370  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO VAL THR GLY          
SEQRES  20 D  370  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET VAL          
SEQRES  21 D  370  SER LYS SER ALA ASN TYR CYS HIS THR SER GLN GLY ASP          
SEQRES  22 D  370  PRO ILE GLY LEU ILE LEU LEU GLY GLU VAL ALA LEU GLY          
SEQRES  23 D  370  ASN MET TYR GLU LEU LYS HIS ALA SER HIS ILE SER LYS          
SEQRES  24 D  370  LEU PRO LYS GLY LYS HIS SER VAL LYS GLY LEU GLY LYS          
SEQRES  25 D  370  THR THR PRO ASP PRO SER ALA ASN ILE SER LEU ASP GLY          
SEQRES  26 D  370  VAL ASP VAL PRO LEU GLY THR GLY ILE SER SER GLY VAL          
SEQRES  27 D  370  ASN ASP THR SER LEU LEU TYR ASN GLU TYR ILE VAL TYR          
SEQRES  28 D  370  ASP ILE ALA GLN VAL ASN LEU LYS TYR LEU LEU LYS LEU          
SEQRES  29 D  370  LYS PHE ASN PHE LYS THR                                      
HET    SO4  A1101       5                                                       
HET    SO4  A1102       5                                                       
HET    SO4  A1103       5                                                       
HET    SO4  A1104       5                                                       
HET    2YQ  A1105      28                                                       
HET    GOL  A1106       6                                                       
HET    GOL  A1107       6                                                       
HET    SO4  B1101       5                                                       
HET    SO4  B1102       5                                                       
HET    SO4  B1103       5                                                       
HET    SO4  B1104       5                                                       
HET    2YQ  B1105      28                                                       
HET    SO4  B1106       5                                                       
HET    SO4  C1101       5                                                       
HET    SO4  C1102       5                                                       
HET    SO4  C1103       5                                                       
HET    2YQ  C1104      28                                                       
HET    GOL  C1105       6                                                       
HET    SO4  D1101       5                                                       
HET    SO4  D1102       5                                                       
HET    SO4  D1103       5                                                       
HET    2YQ  D1104      28                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     2YQ (8S,9R)-5-FLUORO-8-(4-FLUOROPHENYL)-9-(1-METHYL-1H-1,2,          
HETNAM   2 2YQ  4-TRIAZOL-5-YL)-2,7,8,9-TETRAHYDRO-3H-PYRIDO[4,3,2-             
HETNAM   3 2YQ  DE]PHTHALAZIN-3-ONE                                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  SO4    15(O4 S 2-)                                                  
FORMUL   9  2YQ    4(C19 H14 F2 N6 O)                                           
FORMUL  10  GOL    3(C3 H8 O3)                                                  
FORMUL  27  HOH   *316(H2 O)                                                    
HELIX    1 AA1 PRO A  666  PHE A  677  1                                  12    
HELIX    2 AA2 ASP A  678  TYR A  689  1                                  12    
HELIX    3 AA3 PRO A  697  LEU A  701  5                                   5    
HELIX    4 AA4 SER A  702  GLN A  722  1                                  21    
HELIX    5 AA5 SER A  727  ILE A  740  1                                  14    
HELIX    6 AA6 ASN A  754  GLY A  780  1                                  27    
HELIX    7 AA7 ASP A  788  LEU A  797  1                                  10    
HELIX    8 AA8 SER A  808  THR A  821  1                                  14    
HELIX    9 AA9 GLY A  843  LYS A  849  1                                   7    
HELIX   10 AB1 PRO A  850  LYS A  852  5                                   3    
HELIX   11 AB2 ARG A  865  THR A  867  5                                   3    
HELIX   12 AB3 ASN A  868  GLY A  876  1                                   9    
HELIX   13 AB4 MET A  900  ASN A  906  1                                   7    
HELIX   14 AB5 TYR A  907  HIS A  909  5                                   3    
HELIX   15 AB6 PRO A  958  ASN A  961  5                                   4    
HELIX   16 AB7 ASP A  993  ALA A  995  5                                   3    
HELIX   17 AB8 PRO B  666  PHE B  677  1                                  12    
HELIX   18 AB9 ASP B  678  TYR B  689  1                                  12    
HELIX   19 AC1 PRO B  697  LEU B  701  5                                   5    
HELIX   20 AC2 SER B  702  SER B  721  1                                  20    
HELIX   21 AC3 SER B  727  ILE B  740  1                                  14    
HELIX   22 AC4 ASN B  754  GLY B  780  1                                  27    
HELIX   23 AC5 ASP B  788  LEU B  797  1                                  10    
HELIX   24 AC6 SER B  808  THR B  821  1                                  14    
HELIX   25 AC7 GLY B  843  GLN B  853  1                                  11    
HELIX   26 AC8 ARG B  865  THR B  867  5                                   3    
HELIX   27 AC9 ASN B  868  GLY B  876  1                                   9    
HELIX   28 AD1 MET B  900  ASN B  906  1                                   7    
HELIX   29 AD2 TYR B  907  HIS B  909  5                                   3    
HELIX   30 AD3 PRO B  958  ASN B  961  5                                   4    
HELIX   31 AD4 ASP B  993  ALA B  995  5                                   3    
HELIX   32 AD5 PRO C  666  PHE C  677  1                                  12    
HELIX   33 AD6 ASP C  678  TYR C  689  1                                  12    
HELIX   34 AD7 PRO C  697  LEU C  701  5                                   5    
HELIX   35 AD8 SER C  702  GLY C  723  1                                  22    
HELIX   36 AD9 SER C  725  ILE C  740  1                                  16    
HELIX   37 AE1 ASN C  754  GLY C  780  1                                  27    
HELIX   38 AE2 ASP C  788  LEU C  797  1                                  10    
HELIX   39 AE3 SER C  808  THR C  821  1                                  14    
HELIX   40 AE4 GLY C  843  LYS C  849  1                                   7    
HELIX   41 AE5 PRO C  850  LEU C  854  5                                   5    
HELIX   42 AE6 ARG C  865  THR C  867  5                                   3    
HELIX   43 AE7 ASN C  868  GLY C  876  1                                   9    
HELIX   44 AE8 MET C  900  ASN C  906  1                                   7    
HELIX   45 AE9 TYR C  907  HIS C  909  5                                   3    
HELIX   46 AF1 PRO C  958  ASN C  961  5                                   4    
HELIX   47 AF2 ASP C  993  ALA C  995  5                                   3    
HELIX   48 AF3 PRO D  666  PHE D  677  1                                  12    
HELIX   49 AF4 ASP D  678  TYR D  689  1                                  12    
HELIX   50 AF5 PRO D  697  LEU D  701  5                                   5    
HELIX   51 AF6 SER D  702  SER D  721  1                                  20    
HELIX   52 AF7 ASP D  731  ILE D  740  1                                  10    
HELIX   53 AF8 ASN D  754  ARG D  779  1                                  26    
HELIX   54 AF9 PRO D  789  LEU D  797  1                                   9    
HELIX   55 AG1 SER D  808  THR D  821  1                                  14    
HELIX   56 AG2 GLY D  843  LYS D  849  1                                   7    
HELIX   57 AG3 PRO D  850  LYS D  852  5                                   3    
HELIX   58 AG4 ARG D  865  THR D  867  5                                   3    
HELIX   59 AG5 ASN D  868  GLY D  876  1                                   9    
HELIX   60 AG6 MET D  900  ASN D  906  1                                   7    
HELIX   61 AG7 TYR D  907  HIS D  909  5                                   3    
HELIX   62 AG8 PRO D  958  ASN D  961  5                                   4    
HELIX   63 AG9 ASP D  993  ALA D  995  5                                   3    
SHEET    1 AA1 5 THR A 799  VAL A 803  0                                        
SHEET    2 AA1 5 TYR A 829  ARG A 841 -1  O  LYS A 838   N  LYS A 802           
SHEET    3 AA1 5 VAL A 997  PHE A1009 -1  O  LYS A1004   N  ILE A 834           
SHEET    4 AA1 5 ILE A 916  ALA A 925 -1  N  GLU A 923   O  ASN A 998           
SHEET    5 AA1 5 ARG A 857  GLY A 863 -1  N  ARG A 858   O  VAL A 924           
SHEET    1 AA2 4 ILE A 895  PHE A 897  0                                        
SHEET    2 AA2 4 GLU A 988  VAL A 991 -1  O  VAL A 991   N  ILE A 895           
SHEET    3 AA2 4 SER A 947  GLY A 950 -1  N  GLY A 950   O  GLU A 988           
SHEET    4 AA2 4 MET A 929  LEU A 932  1  N  TYR A 930   O  SER A 947           
SHEET    1 AA3 3 GLY A 974  SER A 976  0                                        
SHEET    2 AA3 3 GLY A 952  PRO A 956 -1  N  THR A 955   O  ILE A 975           
SHEET    3 AA3 3 LEU A 984  TYR A 986  1  O  LEU A 985   N  THR A 954           
SHEET    1 AA4 3 VAL A 967  VAL A 969  0                                        
SHEET    2 AA4 3 ILE A 962  LEU A 964 -1  N  LEU A 964   O  VAL A 967           
SHEET    3 AA4 3 SER C 936  HIS C 937  1  O  HIS C 937   N  SER A 963           
SHEET    1 AA5 5 THR B 799  VAL B 803  0                                        
SHEET    2 AA5 5 TYR B 829  ARG B 841 -1  O  LYS B 838   N  LYS B 802           
SHEET    3 AA5 5 VAL B 997  PHE B1009 -1  O  LYS B1004   N  ILE B 834           
SHEET    4 AA5 5 ILE B 916  ALA B 925 -1  N  GLU B 923   O  ASN B 998           
SHEET    5 AA5 5 ARG B 857  GLY B 863 -1  N  ARG B 858   O  VAL B 924           
SHEET    1 AA6 4 ILE B 895  PHE B 897  0                                        
SHEET    2 AA6 4 GLU B 988  VAL B 991 -1  O  TYR B 989   N  PHE B 897           
SHEET    3 AA6 4 SER B 947  GLY B 950 -1  N  VAL B 948   O  ILE B 990           
SHEET    4 AA6 4 MET B 929  LEU B 932  1  N  TYR B 930   O  SER B 947           
SHEET    1 AA7 3 GLY B 974  SER B 976  0                                        
SHEET    2 AA7 3 GLY B 952  PRO B 956 -1  N  THR B 955   O  ILE B 975           
SHEET    3 AA7 3 LEU B 984  TYR B 986  1  O  LEU B 985   N  THR B 954           
SHEET    1 AA8 2 ILE B 962  LEU B 964  0                                        
SHEET    2 AA8 2 VAL B 967  VAL B 969 -1  O  VAL B 967   N  LEU B 964           
SHEET    1 AA9 5 THR C 799  VAL C 803  0                                        
SHEET    2 AA9 5 TYR C 829  ARG C 841 -1  O  LYS C 838   N  LYS C 802           
SHEET    3 AA9 5 VAL C 997  PHE C1009 -1  O  LYS C1004   N  ILE C 834           
SHEET    4 AA9 5 ILE C 916  ALA C 925 -1  N  GLU C 923   O  ASN C 998           
SHEET    5 AA9 5 ARG C 857  GLY C 863 -1  N  ARG C 858   O  VAL C 924           
SHEET    1 AB1 4 ILE C 895  PHE C 897  0                                        
SHEET    2 AB1 4 GLU C 988  VAL C 991 -1  O  VAL C 991   N  ILE C 895           
SHEET    3 AB1 4 SER C 947  GLY C 950 -1  N  VAL C 948   O  ILE C 990           
SHEET    4 AB1 4 MET C 929  LEU C 932  1  N  TYR C 930   O  SER C 947           
SHEET    1 AB2 3 GLY C 974  SER C 976  0                                        
SHEET    2 AB2 3 GLY C 952  PRO C 956 -1  N  THR C 955   O  ILE C 975           
SHEET    3 AB2 3 LEU C 984  TYR C 986  1  O  LEU C 985   N  THR C 954           
SHEET    1 AB3 2 ILE C 962  LEU C 964  0                                        
SHEET    2 AB3 2 VAL C 967  VAL C 969 -1  O  VAL C 969   N  ILE C 962           
SHEET    1 AB4 5 THR D 799  VAL D 803  0                                        
SHEET    2 AB4 5 ASP D 830  ARG D 841 -1  O  LYS D 838   N  LYS D 802           
SHEET    3 AB4 5 VAL D 997  ASN D1008 -1  O  LYS D1004   N  ILE D 834           
SHEET    4 AB4 5 ILE D 916  ALA D 925 -1  N  GLY D 917   O  LEU D1005           
SHEET    5 AB4 5 ARG D 857  GLY D 863 -1  N  LEU D 860   O  GLY D 922           
SHEET    1 AB5 4 ILE D 895  PHE D 897  0                                        
SHEET    2 AB5 4 GLU D 988  VAL D 991 -1  O  VAL D 991   N  ILE D 895           
SHEET    3 AB5 4 SER D 947  GLY D 950 -1  N  VAL D 948   O  ILE D 990           
SHEET    4 AB5 4 MET D 929  LEU D 932  1  N  TYR D 930   O  SER D 947           
SHEET    1 AB6 3 GLY D 974  SER D 976  0                                        
SHEET    2 AB6 3 GLY D 952  PRO D 956 -1  N  THR D 955   O  ILE D 975           
SHEET    3 AB6 3 LEU D 984  TYR D 986  1  O  LEU D 985   N  THR D 954           
SHEET    1 AB7 2 ILE D 962  LEU D 964  0                                        
SHEET    2 AB7 2 VAL D 967  VAL D 969 -1  O  VAL D 967   N  LEU D 964           
SSBOND   1 CYS A  845    CYS B  845                          1555   1555  2.18  
SSBOND   2 CYS C  845    CYS D  845                          1555   1555  2.15  
SITE     1 AC1  4 LYS A 903  LEU A 984  LEU A 985  TYR A 986                    
SITE     1 AC2  3 ARG A 858  MET A 929  LYS A 949                               
SITE     1 AC3  8 ARG A 841  GLY A 843  CYS A 845  GLN A 846                    
SITE     2 AC3  8 GLY B 843  GLU B 844  CYS B 845  GLN B 846                    
SITE     1 AC4  5 SER A 808  GLU A 809  GLU A 810  HOH A1286                    
SITE     2 AC4  5 HIS C 937                                                     
SITE     1 AC5 16 GLN A 759  GLU A 763  HIS A 862  GLY A 863                    
SITE     2 AC5 16 GLY A 888  TYR A 889  TYR A 896  PHE A 897                    
SITE     3 AC5 16 ALA A 898  LYS A 903  SER A 904  TYR A 907                    
SITE     4 AC5 16 GLU A 988  HOH A1220  HOH A1231  HOH A1272                    
SITE     1 AC6  4 LYS A 933  HIS A 934  ALA A 935  SER A 936                    
SITE     1 AC7  5 GLY A 944  HIS A 946  PRO D 850  LEU D 854                    
SITE     2 AC7  5 HIS D 946                                                     
SITE     1 AC8  4 LYS B 903  LEU B 984  LEU B 985  TYR B 986                    
SITE     1 AC9  6 GLN A 846  LYS A 849  LYS B 838  ASP B 965                    
SITE     2 AC9  6 LYS B1000  HOH B1241                                          
SITE     1 AD1  3 ARG B 858  MET B 929  LYS B 949                               
SITE     1 AD2  6 LYS B 943  GLY B 944  HIS B 946  SO4 B1106                    
SITE     2 AD2  6 HOH B1234  HIS C 946                                          
SITE     1 AD3 13 HIS B 862  GLY B 863  GLY B 888  TYR B 889                    
SITE     2 AD3 13 TYR B 896  PHE B 897  ALA B 898  LYS B 903                    
SITE     3 AD3 13 SER B 904  TYR B 907  GLU B 988  HOH B1221                    
SITE     4 AD3 13 HOH B1224                                                     
SITE     1 AD4  5 LYS B 945  HIS B 946  GLN B 996  SO4 B1104                    
SITE     2 AD4  5 HOH B1213                                                     
SITE     1 AD5  5 LYS C 903  LEU C 985  TYR C 986  GOL C1105                    
SITE     2 AD5  5 HOH C1266                                                     
SITE     1 AD6  4 LYS C 838  LYS C1000  GLN D 846  LYS D 849                    
SITE     1 AD7  3 SER C 702  LYS C 703  ARG C 704                               
SITE     1 AD8 15 GLN C 759  HIS C 862  GLY C 863  GLY C 888                    
SITE     2 AD8 15 TYR C 889  TYR C 896  PHE C 897  ALA C 898                    
SITE     3 AD8 15 LYS C 903  SER C 904  TYR C 907  GLU C 988                    
SITE     4 AD8 15 GOL C1105  HOH C1224  HOH C1256                               
SITE     1 AD9  8 GLY C 888  TYR C 889  MET C 890  TYR C 896                    
SITE     2 AD9  8 GLU C 988  SO4 C1101  2YQ C1104  HOH C1215                    
SITE     1 AE1  8 GLY C 843  CYS C 845  GLN C 846  GLU D 842                    
SITE     2 AE1  8 GLY D 843  GLU D 844  CYS D 845  GLN D 846                    
SITE     1 AE2  5 LYS D 903  LEU D 984  LEU D 985  TYR D 986                    
SITE     2 AE2  5 HOH D1231                                                     
SITE     1 AE3  3 ARG D 858  MET D 929  LYS D 949                               
SITE     1 AE4 16 GLN D 759  GLU D 763  HIS D 862  GLY D 863                    
SITE     2 AE4 16 GLY D 888  TYR D 889  TYR D 896  PHE D 897                    
SITE     3 AE4 16 ALA D 898  LYS D 903  SER D 904  TYR D 907                    
SITE     4 AE4 16 GLU D 988  HOH D1212  HOH D1237  HOH D1242                    
CRYST1  103.690  108.150  142.000  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009644  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009246  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007042        0.00000                         
ATOM      1  N   LYS A 662     -64.699 -17.577 -24.714  1.00 54.01           N  
ANISOU    1  N   LYS A 662     6455   6388   7679   -136   -643   -729       N  
ATOM      2  CA  LYS A 662     -64.279 -16.248 -25.279  1.00 56.66           C  
ANISOU    2  CA  LYS A 662     6819   6787   7923    -99   -636   -726       C  
ATOM      3  C   LYS A 662     -64.604 -15.095 -24.311  1.00 56.98           C  
ANISOU    3  C   LYS A 662     6853   6852   7945   -115   -586   -669       C  
ATOM      4  O   LYS A 662     -65.661 -15.063 -23.690  1.00 54.31           O  
ANISOU    4  O   LYS A 662     6476   6497   7661   -144   -575   -653       O  
ATOM      5  CB  LYS A 662     -64.912 -15.969 -26.648  1.00 53.07           C  
ANISOU    5  CB  LYS A 662     6355   6359   7452    -69   -692   -783       C  
ATOM      6  N   SER A 663     -63.691 -14.132 -24.216  1.00 57.99           N  
ANISOU    6  N   SER A 663     7017   7020   7996    -94   -556   -642       N  
ATOM      7  CA  SER A 663     -63.817 -13.035 -23.269  1.00 58.01           C  
ANISOU    7  CA  SER A 663     7020   7046   7977   -105   -508   -590       C  
ATOM      8  C   SER A 663     -64.782 -11.948 -23.733  1.00 53.48           C  
ANISOU    8  C   SER A 663     6427   6504   7390    -92   -521   -598       C  
ATOM      9  O   SER A 663     -64.816 -11.613 -24.898  1.00 50.52           O  
ANISOU    9  O   SER A 663     6061   6154   6979    -61   -559   -634       O  
ATOM     10  CB  SER A 663     -62.435 -12.431 -23.102  1.00 58.30           C  
ANISOU   10  CB  SER A 663     7101   7110   7941    -85   -478   -564       C  
ATOM     11  OG  SER A 663     -62.527 -11.192 -22.428  1.00 63.20           O  
ANISOU   11  OG  SER A 663     7724   7758   8530    -87   -440   -524       O  
ATOM     12  N   LYS A 664     -65.540 -11.375 -22.805  1.00 53.08           N  
ANISOU   12  N   LYS A 664     6350   6454   7363   -114   -490   -565       N  
ATOM     13  CA  LYS A 664     -66.345 -10.191 -23.103  1.00 54.95           C  
ANISOU   13  CA  LYS A 664     6571   6724   7582   -100   -497   -567       C  
ATOM     14  C   LYS A 664     -65.551  -8.865 -23.041  1.00 49.91           C  
ANISOU   14  C   LYS A 664     5971   6127   6867    -76   -470   -538       C  
ATOM     15  O   LYS A 664     -66.069  -7.815 -23.416  1.00 50.53           O  
ANISOU   15  O   LYS A 664     6045   6233   6922    -58   -480   -539       O  
ATOM     16  CB  LYS A 664     -67.518 -10.134 -22.115  1.00 58.98           C  
ANISOU   16  CB  LYS A 664     7034   7220   8154   -133   -473   -547       C  
ATOM     17  N   LEU A 665     -64.310  -8.902 -22.561  1.00 45.67           N  
ANISOU   17  N   LEU A 665     5468   5590   6292    -75   -438   -511       N  
ATOM     18  CA  LEU A 665     -63.520  -7.675 -22.387  1.00 40.91           C  
ANISOU   18  CA  LEU A 665     4899   5022   5625    -57   -410   -481       C  
ATOM     19  C   LEU A 665     -63.119  -7.083 -23.725  1.00 37.36           C  
ANISOU   19  C   LEU A 665     4475   4602   5117    -21   -440   -505       C  
ATOM     20  O   LEU A 665     -62.798  -7.813 -24.643  1.00 36.00           O  
ANISOU   20  O   LEU A 665     4315   4428   4938     -7   -472   -538       O  
ATOM     21  CB  LEU A 665     -62.244  -7.960 -21.582  1.00 41.15           C  
ANISOU   21  CB  LEU A 665     4956   5044   5634    -65   -372   -452       C  
ATOM     22  CG  LEU A 665     -62.401  -8.462 -20.158  1.00 38.68           C  
ANISOU   22  CG  LEU A 665     4628   4705   5363    -98   -336   -420       C  
ATOM     23  CD1 LEU A 665     -61.077  -8.972 -19.635  1.00 40.90           C  
ANISOU   23  CD1 LEU A 665     4941   4977   5624    -99   -314   -402       C  
ATOM     24  CD2 LEU A 665     -62.929  -7.374 -19.268  1.00 38.74           C  
ANISOU   24  CD2 LEU A 665     4623   4730   5367   -105   -303   -388       C  
ATOM     25  N   PRO A 666     -63.066  -5.749 -23.816  1.00 37.15           N  
ANISOU   25  N   PRO A 666     4462   4605   5048     -4   -428   -485       N  
ATOM     26  CA  PRO A 666     -62.495  -5.102 -24.998  1.00 37.06           C  
ANISOU   26  CA  PRO A 666     4483   4624   4973     30   -448   -495       C  
ATOM     27  C   PRO A 666     -61.086  -5.599 -25.327  1.00 37.33           C  
ANISOU   27  C   PRO A 666     4553   4664   4969     39   -438   -498       C  
ATOM     28  O   PRO A 666     -60.319  -5.945 -24.414  1.00 38.45           O  
ANISOU   28  O   PRO A 666     4701   4791   5118     22   -405   -476       O  
ATOM     29  CB  PRO A 666     -62.441  -3.608 -24.602  1.00 37.14           C  
ANISOU   29  CB  PRO A 666     4504   4656   4952     37   -421   -459       C  
ATOM     30  CG  PRO A 666     -63.404  -3.452 -23.467  1.00 36.30           C  
ANISOU   30  CG  PRO A 666     4361   4535   4897     13   -403   -444       C  
ATOM     31  CD  PRO A 666     -63.396  -4.773 -22.752  1.00 37.39           C  
ANISOU   31  CD  PRO A 666     4482   4642   5084    -16   -392   -448       C  
ATOM     32  N   LYS A 667     -60.751  -5.625 -26.614  1.00 36.31           N  
ANISOU   32  N   LYS A 667     4444   4555   4796     69   -468   -525       N  
ATOM     33  CA  LYS A 667     -59.439  -6.130 -27.042  1.00 36.45           C  
ANISOU   33  CA  LYS A 667     4492   4581   4777     81   -460   -533       C  
ATOM     34  C   LYS A 667     -58.291  -5.415 -26.281  1.00 32.52           C  
ANISOU   34  C   LYS A 667     4016   4092   4248     74   -410   -490       C  
ATOM     35  O   LYS A 667     -57.420  -6.078 -25.743  1.00 29.80           O  
ANISOU   35  O   LYS A 667     3677   3734   3911     64   -390   -486       O  
ATOM     36  CB  LYS A 667     -59.249  -6.079 -28.584  1.00 36.61           C  
ANISOU   36  CB  LYS A 667     4534   4631   4743    117   -494   -565       C  
ATOM     37  N   PRO A 668     -58.311  -4.062 -26.222  1.00 30.91           N  
ANISOU   37  N   PRO A 668     3821   3909   4013     81   -392   -460       N  
ATOM     38  CA  PRO A 668     -57.230  -3.319 -25.537  1.00 30.49           C  
ANISOU   38  CA  PRO A 668     3787   3864   3934     75   -348   -423       C  
ATOM     39  C   PRO A 668     -56.995  -3.790 -24.119  1.00 28.94           C  
ANISOU   39  C   PRO A 668     3577   3641   3778     48   -320   -405       C  
ATOM     40  O   PRO A 668     -55.863  -3.897 -23.693  1.00 31.08           O  
ANISOU   40  O   PRO A 668     3863   3913   4035     45   -294   -393       O  
ATOM     41  CB  PRO A 668     -57.746  -1.874 -25.538  1.00 29.67           C  
ANISOU   41  CB  PRO A 668     3684   3774   3813     82   -342   -397       C  
ATOM     42  CG  PRO A 668     -58.638  -1.806 -26.724  1.00 29.90           C  
ANISOU   42  CG  PRO A 668     3713   3817   3831    104   -385   -422       C  
ATOM     43  CD  PRO A 668     -59.327  -3.144 -26.767  1.00 29.45           C  
ANISOU   43  CD  PRO A 668     3631   3739   3820     95   -415   -459       C  
ATOM     44  N   VAL A 669     -58.067  -4.104 -23.410  1.00 29.01           N  
ANISOU   44  N   VAL A 669     3557   3629   3836     29   -324   -405       N  
ATOM     45  CA  VAL A 669     -57.976  -4.590 -22.049  1.00 28.34           C  
ANISOU   45  CA  VAL A 669     3460   3520   3788      3   -297   -385       C  
ATOM     46  C   VAL A 669     -57.363  -5.990 -22.038  1.00 30.64           C  
ANISOU   46  C   VAL A 669     3755   3790   4097     -3   -304   -403       C  
ATOM     47  O   VAL A 669     -56.468  -6.294 -21.220  1.00 30.49           O  
ANISOU   47  O   VAL A 669     3746   3760   4077    -12   -279   -386       O  
ATOM     48  CB  VAL A 669     -59.352  -4.601 -21.374  1.00 27.70           C  
ANISOU   48  CB  VAL A 669     3345   3424   3756    -16   -299   -381       C  
ATOM     49  CG1 VAL A 669     -59.252  -5.122 -19.945  1.00 28.51           C  
ANISOU   49  CG1 VAL A 669     3437   3504   3891    -42   -267   -357       C  
ATOM     50  CG2 VAL A 669     -59.932  -3.193 -21.345  1.00 28.09           C  
ANISOU   50  CG2 VAL A 669     3389   3493   3789     -7   -293   -365       C  
ATOM     51  N   GLN A 670     -57.842  -6.846 -22.932  1.00 29.26           N  
ANISOU   51  N   GLN A 670     3572   3606   3939      3   -341   -440       N  
ATOM     52  CA  GLN A 670     -57.284  -8.197 -23.080  1.00 31.89           C  
ANISOU   52  CA  GLN A 670     3909   3916   4291      2   -354   -463       C  
ATOM     53  C   GLN A 670     -55.789  -8.167 -23.366  1.00 29.90           C  
ANISOU   53  C   GLN A 670     3687   3681   3993     19   -340   -463       C  
ATOM     54  O   GLN A 670     -55.028  -8.848 -22.709  1.00 29.15           O  
ANISOU   54  O   GLN A 670     3598   3567   3911     11   -326   -457       O  
ATOM     55  CB  GLN A 670     -57.990  -8.956 -24.201  1.00 33.64           C  
ANISOU   55  CB  GLN A 670     4119   4131   4531     12   -402   -510       C  
ATOM     56  CG  GLN A 670     -59.392  -9.388 -23.859  1.00 35.26           C  
ANISOU   56  CG  GLN A 670     4288   4309   4798    -10   -419   -517       C  
ATOM     57  CD  GLN A 670     -60.019 -10.143 -25.021  1.00 40.43           C  
ANISOU   57  CD  GLN A 670     4931   4957   5472      3   -471   -568       C  
ATOM     58  OE1 GLN A 670     -59.355 -10.913 -25.707  1.00 42.07           O  
ANISOU   58  OE1 GLN A 670     5154   5162   5669     19   -491   -600       O  
ATOM     59  NE2 GLN A 670     -61.311  -9.935 -25.233  1.00 44.71           N  
ANISOU   59  NE2 GLN A 670     5444   5497   6045     -2   -494   -581       N  
ATOM     60  N   ASP A 671     -55.384  -7.289 -24.277  1.00 32.88           N  
ANISOU   60  N   ASP A 671     4083   4094   4317     43   -341   -467       N  
ATOM     61  CA  ASP A 671     -53.973  -7.050 -24.562  1.00 34.88           C  
ANISOU   61  CA  ASP A 671     4361   4368   4523     58   -321   -463       C  
ATOM     62  C   ASP A 671     -53.158  -6.562 -23.346  1.00 30.23           C  
ANISOU   62  C   ASP A 671     3777   3775   3933     44   -280   -425       C  
ATOM     63  O   ASP A 671     -52.036  -7.010 -23.147  1.00 27.90           O  
ANISOU   63  O   ASP A 671     3493   3478   3630     48   -268   -427       O  
ATOM     64  CB  ASP A 671     -53.805  -6.104 -25.766  1.00 36.41           C  
ANISOU   64  CB  ASP A 671     4572   4601   4660     84   -326   -467       C  
ATOM     65  CG  ASP A 671     -54.231  -6.765 -27.111  1.00 44.36           C  
ANISOU   65  CG  ASP A 671     5582   5619   5655    106   -369   -513       C  
ATOM     66  OD1 ASP A 671     -54.518  -7.986 -27.119  1.00 44.60           O  
ANISOU   66  OD1 ASP A 671     5599   5623   5724    102   -394   -544       O  
ATOM     67  OD2 ASP A 671     -54.256  -6.068 -28.166  1.00 44.04           O  
ANISOU   67  OD2 ASP A 671     5557   5611   5566    130   -378   -517       O  
ATOM     68  N   LEU A 672     -53.752  -5.702 -22.520  1.00 28.68           N  
ANISOU   68  N   LEU A 672     3572   3577   3748     30   -263   -394       N  
ATOM     69  CA  LEU A 672     -53.116  -5.250 -21.284  1.00 27.91           C  
ANISOU   69  CA  LEU A 672     3478   3475   3652     17   -228   -362       C  
ATOM     70  C   LEU A 672     -52.921  -6.414 -20.305  1.00 27.81           C  
ANISOU   70  C   LEU A 672     3458   3431   3677      1   -224   -360       C  
ATOM     71  O   LEU A 672     -51.853  -6.547 -19.719  1.00 28.19           O  
ANISOU   71  O   LEU A 672     3517   3477   3717      2   -206   -350       O  
ATOM     72  CB  LEU A 672     -53.938  -4.145 -20.615  1.00 27.31           C  
ANISOU   72  CB  LEU A 672     3390   3403   3582      7   -214   -335       C  
ATOM     73  CG  LEU A 672     -53.470  -3.599 -19.278  1.00 27.70           C  
ANISOU   73  CG  LEU A 672     3442   3450   3634     -4   -182   -305       C  
ATOM     74  CD1 LEU A 672     -52.175  -2.824 -19.430  1.00 28.50           C  
ANISOU   74  CD1 LEU A 672     3562   3570   3697      7   -163   -296       C  
ATOM     75  CD2 LEU A 672     -54.517  -2.701 -18.644  1.00 30.56           C  
ANISOU   75  CD2 LEU A 672     3788   3813   4009    -13   -173   -286       C  
ATOM     76  N   ILE A 673     -53.948  -7.222 -20.116  1.00 27.61           N  
ANISOU   76  N   ILE A 673     3415   3381   3694    -12   -241   -368       N  
ATOM     77  CA  ILE A 673     -53.843  -8.369 -19.233  1.00 29.95           C  
ANISOU   77  CA  ILE A 673     3706   3643   4029    -28   -238   -363       C  
ATOM     78  C   ILE A 673     -52.739  -9.330 -19.685  1.00 30.97           C  
ANISOU   78  C   ILE A 673     3851   3764   4153    -15   -251   -386       C  
ATOM     79  O   ILE A 673     -51.983  -9.830 -18.854  1.00 27.34           O  
ANISOU   79  O   ILE A 673     3400   3288   3702    -19   -237   -372       O  
ATOM     80  CB  ILE A 673     -55.170  -9.151 -19.135  1.00 32.45           C  
ANISOU   80  CB  ILE A 673     3998   3932   4398    -47   -257   -370       C  
ATOM     81  CG1 ILE A 673     -56.283  -8.256 -18.613  1.00 34.28           C  
ANISOU   81  CG1 ILE A 673     4211   4173   4641    -60   -242   -349       C  
ATOM     82  CG2 ILE A 673     -55.039 -10.368 -18.232  1.00 32.93           C  
ANISOU   82  CG2 ILE A 673     4056   3954   4501    -65   -252   -359       C  
ATOM     83  CD1 ILE A 673     -55.889  -7.420 -17.415  1.00 36.07           C  
ANISOU   83  CD1 ILE A 673     4446   4411   4849    -65   -205   -311       C  
ATOM     84  N   LYS A 674     -52.655  -9.598 -20.984  1.00 33.28           N  
ANISOU   84  N   LYS A 674     4147   4068   4431      3   -277   -422       N  
ATOM     85  CA  LYS A 674     -51.567 -10.452 -21.521  1.00 36.92           C  
ANISOU   85  CA  LYS A 674     4622   4525   4882     21   -288   -450       C  
ATOM     86  C   LYS A 674     -50.215  -9.847 -21.253  1.00 33.46           C  
ANISOU   86  C   LYS A 674     4200   4109   4405     32   -261   -435       C  
ATOM     87  O   LYS A 674     -49.308 -10.490 -20.787  1.00 37.16           O  
ANISOU   87  O   LYS A 674     4674   4563   4881     35   -256   -437       O  
ATOM     88  CB  LYS A 674     -51.732 -10.673 -23.028  1.00 39.78           C  
ANISOU   88  CB  LYS A 674     4986   4905   5225     43   -320   -494       C  
ATOM     89  CG  LYS A 674     -52.904 -11.566 -23.381  1.00 44.53           C  
ANISOU   89  CG  LYS A 674     5570   5478   5873     35   -356   -520       C  
ATOM     90  CD  LYS A 674     -53.007 -11.750 -24.883  1.00 49.74           C  
ANISOU   90  CD  LYS A 674     6234   6159   6507     61   -390   -567       C  
ATOM     91  CE  LYS A 674     -54.336 -12.383 -25.244  1.00 55.99           C  
ANISOU   91  CE  LYS A 674     7004   6927   7345     53   -428   -594       C  
ATOM     92  NZ  LYS A 674     -54.666 -12.210 -26.688  1.00 63.99           N  
ANISOU   92  NZ  LYS A 674     8021   7969   8324     81   -461   -635       N  
ATOM     93  N   MET A 675     -50.107  -8.569 -21.524  1.00 32.77           N  
ANISOU   93  N   MET A 675     4117   4055   4279     38   -243   -421       N  
ATOM     94  CA  MET A 675     -48.878  -7.817 -21.277  1.00 33.16           C  
ANISOU   94  CA  MET A 675     4178   4126   4295     45   -215   -405       C  
ATOM     95  C   MET A 675     -48.405  -7.893 -19.813  1.00 32.67           C  
ANISOU   95  C   MET A 675     4115   4044   4252     31   -194   -377       C  
ATOM     96  O   MET A 675     -47.242  -8.145 -19.511  1.00 31.93           O  
ANISOU   96  O   MET A 675     4028   3951   4152     39   -185   -380       O  
ATOM     97  CB  MET A 675     -49.157  -6.409 -21.665  1.00 35.40           C  
ANISOU   97  CB  MET A 675     4465   4439   4547     47   -202   -388       C  
ATOM     98  CG  MET A 675     -47.946  -5.553 -21.844  1.00 44.35           C  
ANISOU   98  CG  MET A 675     5609   5599   5643     57   -176   -377       C  
ATOM     99  SD  MET A 675     -48.581  -3.930 -22.265  1.00 47.83           S  
ANISOU   99  SD  MET A 675     6053   6064   6056     57   -166   -353       S  
ATOM    100  CE  MET A 675     -47.054  -3.030 -22.158  1.00 47.52           C  
ANISOU  100  CE  MET A 675     6021   6045   5987     61   -132   -337       C  
ATOM    101  N   ILE A 676     -49.325  -7.724 -18.890  1.00 30.67           N  
ANISOU  101  N   ILE A 676     3853   3776   4024     13   -189   -353       N  
ATOM    102  CA  ILE A 676     -48.995  -7.638 -17.489  1.00 31.02           C  
ANISOU  102  CA  ILE A 676     3900   3809   4079      2   -168   -325       C  
ATOM    103  C   ILE A 676     -48.716  -9.006 -16.866  1.00 30.16           C  
ANISOU  103  C   ILE A 676     3793   3666   4002     -2   -178   -327       C  
ATOM    104  O   ILE A 676     -47.998  -9.099 -15.889  1.00 31.96           O  
ANISOU  104  O   ILE A 676     4028   3887   4230     -2   -165   -310       O  
ATOM    105  CB  ILE A 676     -50.262  -7.059 -16.825  1.00 31.74           C  
ANISOU  105  CB  ILE A 676     3979   3896   4185    -16   -160   -301       C  
ATOM    106  CG1 ILE A 676     -50.298  -5.547 -16.865  1.00 33.26           C  
ANISOU  106  CG1 ILE A 676     4171   4116   4349    -12   -143   -287       C  
ATOM    107  CG2 ILE A 676     -50.506  -7.550 -15.413  1.00 32.73           C  
ANISOU  107  CG2 ILE A 676     4101   3998   4336    -31   -147   -275       C  
ATOM    108  CD1 ILE A 676     -51.593  -5.073 -16.216  1.00 35.21           C  
ANISOU  108  CD1 ILE A 676     4403   4359   4614    -27   -136   -269       C  
ATOM    109  N   PHE A 677     -49.355 -10.047 -17.381  1.00 30.68           N  
ANISOU  109  N   PHE A 677     3852   3708   4097     -6   -203   -347       N  
ATOM    110  CA  PHE A 677     -49.134 -11.415 -16.901  1.00 31.66           C  
ANISOU  110  CA  PHE A 677     3979   3794   4256    -10   -216   -350       C  
ATOM    111  C   PHE A 677     -48.172 -12.225 -17.820  1.00 33.32           C  
ANISOU  111  C   PHE A 677     4197   4001   4463     12   -237   -389       C  
ATOM    112  O   PHE A 677     -48.157 -13.425 -17.763  1.00 37.53           O  
ANISOU  112  O   PHE A 677     4731   4500   5030     12   -257   -401       O  
ATOM    113  CB  PHE A 677     -50.479 -12.144 -16.724  1.00 30.80           C  
ANISOU  113  CB  PHE A 677     3856   3654   4195    -31   -229   -345       C  
ATOM    114  CG  PHE A 677     -51.233 -11.753 -15.456  1.00 30.32           C  
ANISOU  114  CG  PHE A 677     3787   3585   4146    -53   -204   -303       C  
ATOM    115  CD1 PHE A 677     -50.750 -12.104 -14.238  1.00 32.25           C  
ANISOU  115  CD1 PHE A 677     4043   3814   4396    -58   -188   -274       C  
ATOM    116  CD2 PHE A 677     -52.367 -10.991 -15.514  1.00 28.43           C  
ANISOU  116  CD2 PHE A 677     3532   3361   3909    -65   -196   -295       C  
ATOM    117  CE1 PHE A 677     -51.403 -11.725 -13.074  1.00 32.66           C  
ANISOU  117  CE1 PHE A 677     4090   3865   4453    -75   -163   -236       C  
ATOM    118  CE2 PHE A 677     -53.045 -10.636 -14.385  1.00 30.62           C  
ANISOU  118  CE2 PHE A 677     3801   3636   4197    -83   -171   -260       C  
ATOM    119  CZ  PHE A 677     -52.564 -11.003 -13.146  1.00 31.98           C  
ANISOU  119  CZ  PHE A 677     3986   3795   4372    -88   -153   -229       C  
ATOM    120  N   ASP A 678     -47.357 -11.537 -18.608  1.00 33.80           N  
ANISOU  120  N   ASP A 678     4263   4098   4482     32   -231   -406       N  
ATOM    121  CA  ASP A 678     -46.467 -12.136 -19.550  1.00 35.15           C  
ANISOU  121  CA  ASP A 678     4439   4275   4642     55   -246   -444       C  
ATOM    122  C   ASP A 678     -45.293 -12.797 -18.843  1.00 33.69           C  
ANISOU  122  C   ASP A 678     4261   4074   4467     64   -244   -444       C  
ATOM    123  O   ASP A 678     -44.328 -12.136 -18.434  1.00 32.98           O  
ANISOU  123  O   ASP A 678     4174   4003   4352     71   -223   -432       O  
ATOM    124  CB  ASP A 678     -45.963 -11.068 -20.537  1.00 38.53           C  
ANISOU  124  CB  ASP A 678     4870   4751   5020     70   -233   -455       C  
ATOM    125  CG  ASP A 678     -45.246 -11.665 -21.750  1.00 43.78           C  
ANISOU  125  CG  ASP A 678     5538   5430   5667     96   -248   -500       C  
ATOM    126  OD1 ASP A 678     -44.591 -12.724 -21.622  1.00 48.82           O  
ANISOU  126  OD1 ASP A 678     6178   6047   6327    107   -262   -521       O  
ATOM    127  OD2 ASP A 678     -45.338 -11.052 -22.834  1.00 53.83           O  
ANISOU  127  OD2 ASP A 678     6813   6737   6904    108   -247   -514       O  
ATOM    128  N   VAL A 679     -45.359 -14.119 -18.765  1.00 33.54           N  
ANISOU  128  N   VAL A 679     4243   4015   4486     66   -269   -460       N  
ATOM    129  CA  VAL A 679     -44.350 -14.932 -18.097  1.00 34.96           C  
ANISOU  129  CA  VAL A 679     4430   4171   4682     76   -274   -461       C  
ATOM    130  C   VAL A 679     -42.968 -14.819 -18.774  1.00 30.80           C  
ANISOU  130  C   VAL A 679     3904   3673   4125    105   -271   -492       C  
ATOM    131  O   VAL A 679     -41.943 -14.791 -18.121  1.00 28.28           O  
ANISOU  131  O   VAL A 679     3589   3356   3801    114   -262   -485       O  
ATOM    132  CB  VAL A 679     -44.820 -16.404 -18.063  1.00 39.29           C  
ANISOU  132  CB  VAL A 679     4978   4668   5282     72   -306   -475       C  
ATOM    133  CG1 VAL A 679     -43.738 -17.316 -17.539  1.00 40.70           C  
ANISOU  133  CG1 VAL A 679     5166   4819   5479     89   -317   -481       C  
ATOM    134  CG2 VAL A 679     -46.067 -16.516 -17.195  1.00 39.69           C  
ANISOU  134  CG2 VAL A 679     5026   4689   5366     42   -302   -436       C  
ATOM    135  N   GLU A 680     -42.957 -14.746 -20.083  1.00 28.69           N  
ANISOU  135  N   GLU A 680     3633   3432   3837    119   -279   -529       N  
ATOM    136  CA  GLU A 680     -41.713 -14.606 -20.811  1.00 29.70           C  
ANISOU  136  CA  GLU A 680     3759   3591   3933    145   -271   -559       C  
ATOM    137  C   GLU A 680     -41.013 -13.300 -20.443  1.00 27.58           C  
ANISOU  137  C   GLU A 680     3490   3360   3631    142   -236   -532       C  
ATOM    138  O   GLU A 680     -39.785 -13.264 -20.363  1.00 28.24           O  
ANISOU  138  O   GLU A 680     3569   3457   3703    158   -225   -543       O  
ATOM    139  CB  GLU A 680     -42.039 -14.635 -22.324  1.00 30.71           C  
ANISOU  139  CB  GLU A 680     3885   3746   4037    161   -283   -599       C  
ATOM    140  CG  GLU A 680     -40.860 -14.351 -23.228  1.00 32.74           C  
ANISOU  140  CG  GLU A 680     4140   4045   4253    187   -269   -628       C  
ATOM    141  CD  GLU A 680     -41.248 -14.310 -24.705  1.00 35.55           C  
ANISOU  141  CD  GLU A 680     4498   4433   4577    204   -279   -664       C  
ATOM    142  OE1 GLU A 680     -42.392 -14.706 -25.063  1.00 41.75           O  
ANISOU  142  OE1 GLU A 680     5285   5200   5379    198   -305   -674       O  
ATOM    143  OE2 GLU A 680     -40.414 -13.869 -25.513  1.00 34.18           O  
ANISOU  143  OE2 GLU A 680     4323   4302   4361    223   -259   -681       O  
ATOM    144  N   SER A 681     -41.775 -12.225 -20.273  1.00 25.88           N  
ANISOU  144  N   SER A 681     3274   3159   3399    123   -218   -501       N  
ATOM    145  CA  SER A 681     -41.190 -10.944 -19.844  1.00 26.58           C  
ANISOU  145  CA  SER A 681     3361   3277   3462    118   -187   -475       C  
ATOM    146  C   SER A 681     -40.609 -11.025 -18.463  1.00 25.60           C  
ANISOU  146  C   SER A 681     3238   3133   3356    113   -181   -452       C  
ATOM    147  O   SER A 681     -39.568 -10.453 -18.202  1.00 25.03           O  
ANISOU  147  O   SER A 681     3160   3079   3269    120   -164   -450       O  
ATOM    148  CB  SER A 681     -42.234  -9.836 -19.847  1.00 26.59           C  
ANISOU  148  CB  SER A 681     3363   3291   3448     99   -174   -446       C  
ATOM    149  OG  SER A 681     -42.559  -9.500 -21.141  1.00 29.84           O  
ANISOU  149  OG  SER A 681     3776   3730   3834    108   -176   -464       O  
ATOM    150  N   MET A 682     -41.293 -11.749 -17.581  1.00 28.20           N  
ANISOU  150  N   MET A 682     3573   3425   3717    102   -196   -436       N  
ATOM    151  CA  MET A 682     -40.773 -12.007 -16.252  1.00 28.46           C  
ANISOU  151  CA  MET A 682     3610   3436   3765    101   -195   -414       C  
ATOM    152  C   MET A 682     -39.399 -12.701 -16.362  1.00 28.29           C  
ANISOU  152  C   MET A 682     3587   3413   3750    126   -205   -443       C  
ATOM    153  O   MET A 682     -38.443 -12.290 -15.725  1.00 24.39           O  
ANISOU  153  O   MET A 682     3090   2929   3247    133   -195   -437       O  
ATOM    154  CB  MET A 682     -41.762 -12.854 -15.455  1.00 31.89           C  
ANISOU  154  CB  MET A 682     4052   3829   4234     86   -210   -392       C  
ATOM    155  CG  MET A 682     -43.134 -12.196 -15.159  1.00 32.78           C  
ANISOU  155  CG  MET A 682     4164   3944   4347     61   -198   -363       C  
ATOM    156  SD  MET A 682     -44.235 -13.407 -14.352  1.00 40.27           S  
ANISOU  156  SD  MET A 682     5118   4842   5343     42   -213   -340       S  
ATOM    157  CE  MET A 682     -45.855 -12.826 -14.876  1.00 38.80           C  
ANISOU  157  CE  MET A 682     4918   4664   5160     20   -208   -333       C  
ATOM    158  N   LYS A 683     -39.307 -13.755 -17.179  1.00 30.43           N  
ANISOU  158  N   LYS A 683     3858   3670   4035    140   -228   -478       N  
ATOM    159  CA  LYS A 683     -38.060 -14.551 -17.282  1.00 30.79           C  
ANISOU  159  CA  LYS A 683     3899   3709   4090    166   -241   -509       C  
ATOM    160  C   LYS A 683     -36.931 -13.786 -17.918  1.00 30.00           C  
ANISOU  160  C   LYS A 683     3785   3653   3958    181   -220   -530       C  
ATOM    161  O   LYS A 683     -35.803 -13.827 -17.405  1.00 26.81           O  
ANISOU  161  O   LYS A 683     3375   3252   3558    195   -218   -536       O  
ATOM    162  CB  LYS A 683     -38.305 -15.830 -18.057  1.00 34.12           C  
ANISOU  162  CB  LYS A 683     4323   4105   4536    179   -271   -545       C  
ATOM    163  CG  LYS A 683     -39.163 -16.823 -17.272  1.00 37.23           C  
ANISOU  163  CG  LYS A 683     4728   4444   4972    166   -295   -525       C  
ATOM    164  CD  LYS A 683     -39.740 -17.839 -18.230  1.00 42.77           C  
ANISOU  164  CD  LYS A 683     5429   5123   5699    171   -323   -561       C  
ATOM    165  CE  LYS A 683     -38.688 -18.854 -18.653  1.00 47.51           C  
ANISOU  165  CE  LYS A 683     6027   5710   6314    203   -346   -606       C  
ATOM    166  NZ  LYS A 683     -39.223 -19.672 -19.775  1.00 53.20           N  
ANISOU  166  NZ  LYS A 683     6744   6417   7051    212   -374   -650       N  
ATOM    167  N   LYS A 684     -37.254 -13.026 -18.964  1.00 30.03           N  
ANISOU  167  N   LYS A 684     3785   3693   3933    177   -203   -538       N  
ATOM    168  CA  LYS A 684     -36.270 -12.188 -19.618  1.00 33.06           C  
ANISOU  168  CA  LYS A 684     4155   4120   4285    187   -176   -551       C  
ATOM    169  C   LYS A 684     -35.680 -11.203 -18.633  1.00 31.01           C  
ANISOU  169  C   LYS A 684     3890   3871   4023    177   -155   -522       C  
ATOM    170  O   LYS A 684     -34.467 -11.030 -18.571  1.00 29.79           O  
ANISOU  170  O   LYS A 684     3721   3731   3865    190   -144   -536       O  
ATOM    171  CB  LYS A 684     -36.926 -11.385 -20.756  1.00 38.62           C  
ANISOU  171  CB  LYS A 684     4861   4858   4955    181   -160   -550       C  
ATOM    172  CG  LYS A 684     -35.982 -10.855 -21.809  1.00 43.98           C  
ANISOU  172  CG  LYS A 684     5528   5582   5600    196   -135   -572       C  
ATOM    173  CD  LYS A 684     -36.702  -9.913 -22.774  1.00 47.85           C  
ANISOU  173  CD  LYS A 684     6025   6103   6053    187   -118   -559       C  
ATOM    174  CE  LYS A 684     -35.775  -9.434 -23.899  1.00 54.85           C  
ANISOU  174  CE  LYS A 684     6901   7036   6902    202    -90   -578       C  
ATOM    175  NZ  LYS A 684     -36.393  -8.368 -24.754  1.00 57.19           N  
ANISOU  175  NZ  LYS A 684     7206   7363   7159    194    -71   -557       N  
ATOM    176  N   ALA A 685     -36.541 -10.567 -17.843  1.00 30.43           N  
ANISOU  176  N   ALA A 685     3825   3786   3951    155   -150   -484       N  
ATOM    177  CA  ALA A 685     -36.066  -9.637 -16.800  1.00 28.88           C  
ANISOU  177  CA  ALA A 685     3625   3596   3753    146   -134   -458       C  
ATOM    178  C   ALA A 685     -35.053 -10.353 -15.908  1.00 28.15           C  
ANISOU  178  C   ALA A 685     3529   3485   3681    162   -150   -468       C  
ATOM    179  O   ALA A 685     -34.028  -9.798 -15.587  1.00 25.73           O  
ANISOU  179  O   ALA A 685     3209   3195   3373    168   -138   -472       O  
ATOM    180  CB  ALA A 685     -37.246  -9.113 -15.977  1.00 28.26           C  
ANISOU  180  CB  ALA A 685     3557   3503   3676    124   -132   -420       C  
ATOM    181  N   MET A 686     -35.371 -11.576 -15.489  1.00 28.81           N  
ANISOU  181  N   MET A 686     3624   3532   3788    169   -177   -471       N  
ATOM    182  CA  MET A 686     -34.512 -12.312 -14.549  1.00 30.22           C  
ANISOU  182  CA  MET A 686     3805   3689   3988    186   -196   -475       C  
ATOM    183  C   MET A 686     -33.187 -12.702 -15.186  1.00 30.66           C  
ANISOU  183  C   MET A 686     3842   3759   4047    212   -199   -517       C  
ATOM    184  O   MET A 686     -32.140 -12.666 -14.531  1.00 28.83           O  
ANISOU  184  O   MET A 686     3601   3529   3823    226   -204   -524       O  
ATOM    185  CB  MET A 686     -35.249 -13.534 -13.973  1.00 32.30           C  
ANISOU  185  CB  MET A 686     4088   3906   4278    186   -223   -462       C  
ATOM    186  CG  MET A 686     -36.426 -13.145 -13.031  1.00 39.22           C  
ANISOU  186  CG  MET A 686     4979   4769   5153    161   -217   -416       C  
ATOM    187  SD  MET A 686     -37.446 -14.562 -12.557  1.00 49.50           S  
ANISOU  187  SD  MET A 686     6302   6017   6489    154   -242   -398       S  
ATOM    188  CE  MET A 686     -36.400 -15.235 -11.284  1.00 45.16           C  
ANISOU  188  CE  MET A 686     5764   5443   5953    176   -262   -388       C  
ATOM    189  N   VAL A 687     -33.235 -13.029 -16.472  1.00 29.89           N  
ANISOU  189  N   VAL A 687     3738   3675   3942    220   -197   -547       N  
ATOM    190  CA  VAL A 687     -32.023 -13.331 -17.195  1.00 30.21           C  
ANISOU  190  CA  VAL A 687     3760   3737   3983    245   -195   -590       C  
ATOM    191  C   VAL A 687     -31.145 -12.073 -17.279  1.00 30.86           C  
ANISOU  191  C   VAL A 687     3820   3859   4045    240   -162   -587       C  
ATOM    192  O   VAL A 687     -29.977 -12.133 -16.943  1.00 30.42           O  
ANISOU  192  O   VAL A 687     3747   3810   4002    256   -163   -605       O  
ATOM    193  CB  VAL A 687     -32.320 -13.879 -18.594  1.00 30.47           C  
ANISOU  193  CB  VAL A 687     3792   3781   4005    255   -198   -623       C  
ATOM    194  CG1 VAL A 687     -31.047 -13.890 -19.422  1.00 30.61           C  
ANISOU  194  CG1 VAL A 687     3785   3833   4012    279   -183   -665       C  
ATOM    195  CG2 VAL A 687     -32.896 -15.288 -18.485  1.00 31.82           C  
ANISOU  195  CG2 VAL A 687     3978   3906   4206    265   -236   -636       C  
ATOM    196  N   GLU A 688     -31.737 -10.934 -17.593  1.00 29.42           N  
ANISOU  196  N   GLU A 688     3639   3700   3839    218   -136   -563       N  
ATOM    197  CA  GLU A 688     -30.996  -9.676 -17.620  1.00 32.11           C  
ANISOU  197  CA  GLU A 688     3960   4073   4167    209   -104   -555       C  
ATOM    198  C   GLU A 688     -30.396  -9.287 -16.276  1.00 31.52           C  
ANISOU  198  C   GLU A 688     3880   3987   4111    207   -110   -541       C  
ATOM    199  O   GLU A 688     -29.351  -8.673 -16.241  1.00 30.37           O  
ANISOU  199  O   GLU A 688     3709   3862   3968    210    -94   -552       O  
ATOM    200  CB  GLU A 688     -31.853  -8.537 -18.161  1.00 34.14           C  
ANISOU  200  CB  GLU A 688     4224   4349   4398    185    -79   -528       C  
ATOM    201  CG  GLU A 688     -31.903  -8.569 -19.672  1.00 39.35           C  
ANISOU  201  CG  GLU A 688     4881   5040   5032    192    -63   -548       C  
ATOM    202  CD  GLU A 688     -32.910  -7.625 -20.283  1.00 44.63           C  
ANISOU  202  CD  GLU A 688     5561   5723   5672    173    -46   -521       C  
ATOM    203  OE1 GLU A 688     -33.729  -7.000 -19.565  1.00 46.97           O  
ANISOU  203  OE1 GLU A 688     5869   6004   5973    153    -48   -488       O  
ATOM    204  OE2 GLU A 688     -32.927  -7.583 -21.517  1.00 47.89           O  
ANISOU  204  OE2 GLU A 688     5974   6163   6058    180    -32   -535       O  
ATOM    205  N   TYR A 689     -31.043  -9.660 -15.174  1.00 32.44           N  
ANISOU  205  N   TYR A 689     4016   4071   4239    203   -133   -519       N  
ATOM    206  CA  TYR A 689     -30.470  -9.417 -13.848  1.00 31.99           C  
ANISOU  206  CA  TYR A 689     3956   4003   4195    207   -144   -508       C  
ATOM    207  C   TYR A 689     -29.402 -10.449 -13.483  1.00 30.62           C  
ANISOU  207  C   TYR A 689     3775   3816   4044    236   -170   -537       C  
ATOM    208  O   TYR A 689     -28.838 -10.368 -12.424  1.00 27.94           O  
ANISOU  208  O   TYR A 689     3432   3467   3715    244   -184   -533       O  
ATOM    209  CB  TYR A 689     -31.561  -9.431 -12.769  1.00 30.87           C  
ANISOU  209  CB  TYR A 689     3841   3836   4053    194   -157   -471       C  
ATOM    210  CG  TYR A 689     -32.528  -8.247 -12.780  1.00 31.11           C  
ANISOU  210  CG  TYR A 689     3877   3878   4065    167   -134   -441       C  
ATOM    211  CD1 TYR A 689     -32.075  -6.931 -12.678  1.00 30.19           C  
ANISOU  211  CD1 TYR A 689     3744   3785   3941    157   -113   -437       C  
ATOM    212  CD2 TYR A 689     -33.898  -8.459 -12.743  1.00 31.16           C  
ANISOU  212  CD2 TYR A 689     3904   3869   4066    153   -137   -417       C  
ATOM    213  CE1 TYR A 689     -32.964  -5.877 -12.585  1.00 30.05           C  
ANISOU  213  CE1 TYR A 689     3733   3774   3910    136    -96   -410       C  
ATOM    214  CE2 TYR A 689     -34.798  -7.403 -12.695  1.00 32.79           C  
ANISOU  214  CE2 TYR A 689     4115   4086   4258    132   -119   -392       C  
ATOM    215  CZ  TYR A 689     -34.328  -6.112 -12.604  1.00 33.17           C  
ANISOU  215  CZ  TYR A 689     4148   4156   4298    124    -99   -388       C  
ATOM    216  OH  TYR A 689     -35.256  -5.077 -12.524  1.00 39.20           O  
ANISOU  216  OH  TYR A 689     4917   4926   5050    105    -85   -364       O  
ATOM    217  N   GLU A 690     -29.191 -11.450 -14.336  1.00 34.11           N  
ANISOU  217  N   GLU A 690     4214   4254   4493    253   -180   -567       N  
ATOM    218  CA  GLU A 690     -28.235 -12.544 -14.095  1.00 35.29           C  
ANISOU  218  CA  GLU A 690     4355   4386   4667    284   -208   -598       C  
ATOM    219  C   GLU A 690     -28.636 -13.439 -12.914  1.00 34.38           C  
ANISOU  219  C   GLU A 690     4268   4227   4568    292   -244   -577       C  
ATOM    220  O   GLU A 690     -27.810 -14.061 -12.271  1.00 33.64           O  
ANISOU  220  O   GLU A 690     4171   4117   4494    316   -269   -590       O  
ATOM    221  CB  GLU A 690     -26.818 -12.024 -13.921  1.00 41.63           C  
ANISOU  221  CB  GLU A 690     5125   5213   5478    297   -200   -621       C  
ATOM    222  CG  GLU A 690     -26.253 -11.359 -15.157  1.00 46.18           C  
ANISOU  222  CG  GLU A 690     5673   5833   6043    293   -163   -645       C  
ATOM    223  CD  GLU A 690     -24.833 -10.912 -14.922  1.00 53.93           C  
ANISOU  223  CD  GLU A 690     6616   6834   7039    304   -155   -669       C  
ATOM    224  OE1 GLU A 690     -24.657  -9.948 -14.153  1.00 57.86           O  
ANISOU  224  OE1 GLU A 690     7107   7337   7540    290   -149   -650       O  
ATOM    225  OE2 GLU A 690     -23.895 -11.534 -15.465  1.00 63.05           O  
ANISOU  225  OE2 GLU A 690     7748   8001   8208    329   -158   -710       O  
ATOM    226  N   ILE A 691     -29.928 -13.542 -12.678  1.00 32.81           N  
ANISOU  226  N   ILE A 691     4095   4007   4363    272   -245   -543       N  
ATOM    227  CA  ILE A 691     -30.445 -14.448 -11.679  1.00 33.83           C  
ANISOU  227  CA  ILE A 691     4252   4094   4508    277   -274   -518       C  
ATOM    228  C   ILE A 691     -30.391 -15.889 -12.167  1.00 34.31           C  
ANISOU  228  C   ILE A 691     4319   4122   4594    296   -302   -543       C  
ATOM    229  O   ILE A 691     -30.572 -16.159 -13.346  1.00 32.70           O  
ANISOU  229  O   ILE A 691     4108   3927   4391    297   -296   -570       O  
ATOM    230  CB  ILE A 691     -31.863 -14.043 -11.317  1.00 34.81           C  
ANISOU  230  CB  ILE A 691     4397   4209   4619    247   -262   -475       C  
ATOM    231  CG1 ILE A 691     -31.697 -12.775 -10.513  1.00 36.76           C  
ANISOU  231  CG1 ILE A 691     4639   4480   4846    236   -244   -454       C  
ATOM    232  CG2 ILE A 691     -32.580 -15.133 -10.531  1.00 34.22           C  
ANISOU  232  CG2 ILE A 691     4351   4088   4563    247   -287   -448       C  
ATOM    233  CD1 ILE A 691     -32.922 -12.219  -9.927  1.00 40.45           C  
ANISOU  233  CD1 ILE A 691     5124   4944   5299    211   -231   -413       C  
ATOM    234  N   ASP A 692     -30.099 -16.802 -11.251  1.00 32.50           N  
ANISOU  234  N   ASP A 692     4106   3857   4387    314   -334   -534       N  
ATOM    235  CA  ASP A 692     -30.106 -18.182 -11.593  1.00 34.55           C  
ANISOU  235  CA  ASP A 692     4374   4077   4675    332   -363   -554       C  
ATOM    236  C   ASP A 692     -31.520 -18.710 -11.545  1.00 35.13           C  
ANISOU  236  C   ASP A 692     4473   4117   4759    309   -367   -522       C  
ATOM    237  O   ASP A 692     -32.020 -19.026 -10.448  1.00 33.74           O  
ANISOU  237  O   ASP A 692     4321   3908   4589    302   -378   -480       O  
ATOM    238  CB  ASP A 692     -29.224 -18.975 -10.646  1.00 34.43           C  
ANISOU  238  CB  ASP A 692     4367   4033   4682    363   -398   -555       C  
ATOM    239  CG  ASP A 692     -29.106 -20.432 -11.088  1.00 34.45           C  
ANISOU  239  CG  ASP A 692     4377   3993   4721    385   -432   -582       C  
ATOM    240  OD1 ASP A 692     -27.993 -20.921 -10.966  1.00 34.88           O  
ANISOU  240  OD1 ASP A 692     4420   4041   4791    419   -455   -611       O  
ATOM    241  OD2 ASP A 692     -30.102 -21.075 -11.558  1.00 31.82           O  
ANISOU  241  OD2 ASP A 692     4058   3631   4402    371   -437   -575       O  
ATOM    242  N   LEU A 693     -32.116 -18.887 -12.735  1.00 33.93           N  
ANISOU  242  N   LEU A 693     4314   3968   4609    300   -361   -545       N  
ATOM    243  CA  LEU A 693     -33.510 -19.331 -12.856  1.00 34.82           C  
ANISOU  243  CA  LEU A 693     4444   4052   4735    275   -364   -521       C  
ATOM    244  C   LEU A 693     -33.750 -20.751 -12.411  1.00 34.91           C  
ANISOU  244  C   LEU A 693     4475   4001   4787    284   -400   -513       C  
ATOM    245  O   LEU A 693     -34.875 -21.150 -12.100  1.00 37.22           O  
ANISOU  245  O   LEU A 693     4783   4260   5097    261   -403   -481       O  
ATOM    246  CB  LEU A 693     -34.010 -19.153 -14.297  1.00 37.76           C  
ANISOU  246  CB  LEU A 693     4803   4446   5098    268   -353   -553       C  
ATOM    247  CG  LEU A 693     -34.335 -17.728 -14.695  1.00 40.18           C  
ANISOU  247  CG  LEU A 693     5098   4803   5365    247   -316   -543       C  
ATOM    248  CD1 LEU A 693     -34.866 -17.632 -16.115  1.00 42.10           C  
ANISOU  248  CD1 LEU A 693     5333   5068   5597    244   -309   -573       C  
ATOM    249  CD2 LEU A 693     -35.383 -17.220 -13.740  1.00 45.12           C  
ANISOU  249  CD2 LEU A 693     5739   5418   5986    218   -304   -490       C  
ATOM    250  N   GLN A 694     -32.712 -21.543 -12.384  1.00 34.49           N  
ANISOU  250  N   GLN A 694     4420   3931   4755    316   -427   -543       N  
ATOM    251  CA  GLN A 694     -32.908 -22.833 -11.855  1.00 36.05           C  
ANISOU  251  CA  GLN A 694     4638   4066   4993    325   -461   -529       C  
ATOM    252  C   GLN A 694     -33.039 -22.790 -10.340  1.00 37.51           C  
ANISOU  252  C   GLN A 694     4847   4230   5174    318   -463   -471       C  
ATOM    253  O   GLN A 694     -33.902 -23.433  -9.753  1.00 40.44           O  
ANISOU  253  O   GLN A 694     5242   4557   5568    301   -472   -431       O  
ATOM    254  CB  GLN A 694     -31.768 -23.754 -12.246  1.00 35.57           C  
ANISOU  254  CB  GLN A 694     4568   3989   4958    365   -493   -579       C  
ATOM    255  CG  GLN A 694     -32.211 -25.144 -11.923  1.00 35.21           C  
ANISOU  255  CG  GLN A 694     4545   3872   4961    369   -530   -566       C  
ATOM    256  CD  GLN A 694     -31.242 -26.193 -12.273  1.00 37.83           C  
ANISOU  256  CD  GLN A 694     4871   4175   5326    409   -568   -614       C  
ATOM    257  OE1 GLN A 694     -30.025 -26.057 -12.092  1.00 39.76           O  
ANISOU  257  OE1 GLN A 694     5104   4441   5562    441   -575   -638       O  
ATOM    258  NE2 GLN A 694     -31.782 -27.310 -12.705  1.00 39.94           N  
ANISOU  258  NE2 GLN A 694     5147   4390   5637    410   -595   -628       N  
ATOM    259  N   LYS A 695     -32.124 -22.092  -9.716  1.00 39.46           N  
ANISOU  259  N   LYS A 695     5089   4508   5395    333   -456   -468       N  
ATOM    260  CA  LYS A 695     -32.000 -22.139  -8.270  1.00 42.39           C  
ANISOU  260  CA  LYS A 695     5484   4861   5759    338   -465   -421       C  
ATOM    261  C   LYS A 695     -32.968 -21.202  -7.627  1.00 42.20           C  
ANISOU  261  C   LYS A 695     5470   4858   5705    305   -433   -373       C  
ATOM    262  O   LYS A 695     -33.231 -21.316  -6.457  1.00 42.42           O  
ANISOU  262  O   LYS A 695     5523   4869   5726    302   -436   -326       O  
ATOM    263  CB  LYS A 695     -30.580 -21.774  -7.840  1.00 40.91           C  
ANISOU  263  CB  LYS A 695     5285   4700   5559    371   -476   -444       C  
ATOM    264  CG  LYS A 695     -29.536 -22.777  -8.274  1.00 42.63           C  
ANISOU  264  CG  LYS A 695     5493   4895   5809    409   -512   -490       C  
ATOM    265  CD  LYS A 695     -28.233 -22.412  -7.607  1.00 47.74           C  
ANISOU  265  CD  LYS A 695     6129   5564   6444    441   -525   -504       C  
ATOM    266  CE  LYS A 695     -27.055 -23.195  -8.157  1.00 51.01           C  
ANISOU  266  CE  LYS A 695     6524   5968   6888    481   -556   -560       C  
ATOM    267  NZ  LYS A 695     -25.802 -22.585  -7.625  1.00 52.16           N  
ANISOU  267  NZ  LYS A 695     6650   6147   7021    507   -562   -579       N  
ATOM    268  N   MET A 696     -33.466 -20.237  -8.379  1.00 47.70           N  
ANISOU  268  N   MET A 696     6148   5594   6381    282   -402   -384       N  
ATOM    269  CA  MET A 696     -34.477 -19.373  -7.831  1.00 50.00           C  
ANISOU  269  CA  MET A 696     6448   5903   6648    252   -372   -342       C  
ATOM    270  C   MET A 696     -35.569 -19.143  -8.826  1.00 50.92           C  
ANISOU  270  C   MET A 696     6553   6025   6768    223   -353   -348       C  
ATOM    271  O   MET A 696     -35.573 -18.108  -9.492  1.00 56.78           O  
ANISOU  271  O   MET A 696     7276   6811   7486    215   -330   -366       O  
ATOM    272  CB  MET A 696     -33.828 -18.058  -7.446  1.00 51.84           C  
ANISOU  272  CB  MET A 696     6668   6186   6844    256   -353   -345       C  
ATOM    273  CG  MET A 696     -34.818 -17.060  -6.913  1.00 57.34           C  
ANISOU  273  CG  MET A 696     7370   6903   7513    228   -323   -307       C  
ATOM    274  SD  MET A 696     -33.886 -15.906  -5.945  1.00 59.63           S  
ANISOU  274  SD  MET A 696     7656   7232   7769    243   -316   -304       S  
ATOM    275  CE  MET A 696     -34.862 -14.438  -6.085  1.00 58.13           C  
ANISOU  275  CE  MET A 696     7456   7080   7551    210   -277   -289       C  
ATOM    276  N   PRO A 697     -36.483 -20.117  -8.958  1.00 55.38           N  
ANISOU  276  N   PRO A 697     7130   6547   7366    209   -365   -334       N  
ATOM    277  CA  PRO A 697     -37.581 -19.966  -9.913  1.00 60.34           C  
ANISOU  277  CA  PRO A 697     7746   7179   8001    183   -352   -343       C  
ATOM    278  C   PRO A 697     -38.684 -19.051  -9.420  1.00 57.43           C  
ANISOU  278  C   PRO A 697     7379   6829   7611    152   -321   -302       C  
ATOM    279  O   PRO A 697     -38.807 -18.819  -8.238  1.00 60.47           O  
ANISOU  279  O   PRO A 697     7779   7213   7983    147   -311   -260       O  
ATOM    280  CB  PRO A 697     -38.140 -21.394 -10.047  1.00 60.18           C  
ANISOU  280  CB  PRO A 697     7737   7098   8031    179   -379   -340       C  
ATOM    281  CG  PRO A 697     -37.784 -22.072  -8.767  1.00 59.12           C  
ANISOU  281  CG  PRO A 697     7628   6928   7909    189   -394   -301       C  
ATOM    282  CD  PRO A 697     -36.458 -21.472  -8.362  1.00 58.62           C  
ANISOU  282  CD  PRO A 697     7562   6898   7813    219   -395   -315       C  
ATOM    283  N   LEU A 698     -39.501 -18.572 -10.339  1.00 63.13           N  
ANISOU  283  N   LEU A 698     8086   7570   8331    133   -307   -316       N  
ATOM    284  CA  LEU A 698     -40.606 -17.649 -10.034  1.00 68.34           C  
ANISOU  284  CA  LEU A 698     8742   8250   8973    104   -278   -284       C  
ATOM    285  C   LEU A 698     -41.463 -18.060  -8.827  1.00 71.55           C  
ANISOU  285  C   LEU A 698     9166   8626   9393     85   -271   -230       C  
ATOM    286  O   LEU A 698     -41.687 -17.264  -7.894  1.00 72.44           O  
ANISOU  286  O   LEU A 698     9285   8761   9479     77   -248   -197       O  
ATOM    287  CB  LEU A 698     -41.442 -17.511 -11.307  1.00 67.94           C  
ANISOU  287  CB  LEU A 698     8675   8208   8930     90   -277   -311       C  
ATOM    288  CG  LEU A 698     -40.754 -16.691 -12.419  1.00 68.93           C  
ANISOU  288  CG  LEU A 698     8784   8379   9026    105   -271   -353       C  
ATOM    289  CD1 LEU A 698     -41.529 -16.682 -13.723  1.00 66.15           C  
ANISOU  289  CD1 LEU A 698     8420   8035   8679     96   -275   -381       C  
ATOM    290  CD2 LEU A 698     -40.560 -15.274 -11.913  1.00 68.86           C  
ANISOU  290  CD2 LEU A 698     8773   8413   8979    100   -242   -333       C  
ATOM    291  N   GLY A 699     -41.887 -19.318  -8.815  1.00 76.99           N  
ANISOU  291  N   GLY A 699     9863   9264  10125     79   -291   -222       N  
ATOM    292  CA  GLY A 699     -42.706 -19.832  -7.720  1.00 81.24           C  
ANISOU  292  CA  GLY A 699    10417   9769  10681     58   -282   -168       C  
ATOM    293  C   GLY A 699     -42.002 -19.939  -6.372  1.00 83.99           C  
ANISOU  293  C   GLY A 699    10791  10113  11010     75   -281   -131       C  
ATOM    294  O   GLY A 699     -42.655 -20.045  -5.342  1.00 80.98           O  
ANISOU  294  O   GLY A 699    10424   9720  10626     60   -264    -81       O  
ATOM    295  N   LYS A 700     -40.670 -19.915  -6.372  1.00 86.70           N  
ANISOU  295  N   LYS A 700    11138  10467  11337    108   -300   -157       N  
ATOM    296  CA  LYS A 700     -39.900 -20.139  -5.165  1.00 88.59           C  
ANISOU  296  CA  LYS A 700    11402  10699  11560    129   -308   -129       C  
ATOM    297  C   LYS A 700     -39.582 -18.843  -4.431  1.00 88.51           C  
ANISOU  297  C   LYS A 700    11392  10740  11498    135   -286   -118       C  
ATOM    298  O   LYS A 700     -39.277 -18.874  -3.240  1.00101.43           O  
ANISOU  298  O   LYS A 700    13051  12375  13113    148   -287    -85       O  
ATOM    299  CB  LYS A 700     -38.593 -20.868  -5.504  1.00 83.69           C  
ANISOU  299  CB  LYS A 700    10784  10060  10955    164   -345   -166       C  
ATOM    300  N   LEU A 701     -39.624 -17.704  -5.117  1.00 87.94           N  
ANISOU  300  N   LEU A 701    11297  10712  11405    129   -268   -146       N  
ATOM    301  CA  LEU A 701     -39.329 -16.429  -4.455  1.00 85.37           C  
ANISOU  301  CA  LEU A 701    10970  10432  11035    134   -249   -140       C  
ATOM    302  C   LEU A 701     -40.100 -16.337  -3.143  1.00 80.66           C  
ANISOU  302  C   LEU A 701    10394   9834  10421    123   -230    -86       C  
ATOM    303  O   LEU A 701     -41.279 -16.686  -3.079  1.00 82.17           O  
ANISOU  303  O   LEU A 701    10587  10006  10628     97   -215    -57       O  
ATOM    304  CB  LEU A 701     -39.645 -15.249  -5.367  1.00 89.04           C  
ANISOU  304  CB  LEU A 701    11409  10936  11487    120   -228   -166       C  
ATOM    305  N   SER A 702     -39.410 -15.957  -2.077  1.00 76.96           N  
ANISOU  305  N   SER A 702     9940   9382   9919    144   -234    -73       N  
ATOM    306  CA  SER A 702     -40.054 -15.893  -0.776  1.00 78.43           C  
ANISOU  306  CA  SER A 702    10149   9570  10080    139   -216    -22       C  
ATOM    307  C   SER A 702     -39.881 -14.501  -0.194  1.00 75.91           C  
ANISOU  307  C   SER A 702     9824   9301   9717    146   -199    -28       C  
ATOM    308  O   SER A 702     -38.826 -13.881  -0.346  1.00 81.87           O  
ANISOU  308  O   SER A 702    10570  10079  10460    167   -213    -63       O  
ATOM    309  CB  SER A 702     -39.502 -16.955   0.176  1.00 79.27           C  
ANISOU  309  CB  SER A 702    10288   9645  10188    161   -239      8       C  
ATOM    310  OG  SER A 702     -38.621 -16.399   1.133  1.00 84.42           O  
ANISOU  310  OG  SER A 702    10952  10324  10798    191   -249      7       O  
ATOM    311  N   LYS A 703     -40.937 -14.016   0.449  1.00 66.76           N  
ANISOU  311  N   LYS A 703     8670   8157   8538    128   -169      5       N  
ATOM    312  CA  LYS A 703     -40.939 -12.706   1.057  1.00 65.24           C  
ANISOU  312  CA  LYS A 703     8473   8010   8306    134   -152      1       C  
ATOM    313  C   LYS A 703     -39.808 -12.598   2.098  1.00 65.66           C  
ANISOU  313  C   LYS A 703     8547   8076   8327    170   -174     -1       C  
ATOM    314  O   LYS A 703     -39.179 -11.556   2.200  1.00 61.66           O  
ANISOU  314  O   LYS A 703     8029   7601   7800    184   -178    -30       O  
ATOM    315  CB  LYS A 703     -42.294 -12.417   1.727  1.00 64.30           C  
ANISOU  315  CB  LYS A 703     8359   7902   8171    113   -117     40       C  
ATOM    316  N   ARG A 704     -39.553 -13.669   2.852  1.00 61.44           N  
ANISOU  316  N   ARG A 704     8041   7513   7789    185   -190     31       N  
ATOM    317  CA  ARG A 704     -38.585 -13.627   3.947  1.00 57.12           C  
ANISOU  317  CA  ARG A 704     7517   6978   7207    222   -213     34       C  
ATOM    318  C   ARG A 704     -37.157 -13.633   3.433  1.00 54.52           C  
ANISOU  318  C   ARG A 704     7174   6647   6892    247   -249    -14       C  
ATOM    319  O   ARG A 704     -36.287 -12.983   4.018  1.00 53.50           O  
ANISOU  319  O   ARG A 704     7045   6544   6737    274   -265    -34       O  
ATOM    320  CB  ARG A 704     -38.805 -14.785   4.936  1.00 57.54           C  
ANISOU  320  CB  ARG A 704     7610   7003   7252    231   -218     88       C  
ATOM    321  N   GLN A 705     -36.896 -14.355   2.344  1.00 51.78           N  
ANISOU  321  N   GLN A 705     6814   6271   6589    241   -262    -34       N  
ATOM    322  CA  GLN A 705     -35.554 -14.302   1.741  1.00 51.34           C  
ANISOU  322  CA  GLN A 705     6739   6218   6549    264   -292    -84       C  
ATOM    323  C   GLN A 705     -35.281 -12.885   1.203  1.00 48.55           C  
ANISOU  323  C   GLN A 705     6353   5906   6187    257   -278   -124       C  
ATOM    324  O   GLN A 705     -34.195 -12.352   1.375  1.00 42.88           O  
ANISOU  324  O   GLN A 705     5624   5207   5461    279   -296   -156       O  
ATOM    325  CB  GLN A 705     -35.360 -15.339   0.617  1.00 49.70           C  
ANISOU  325  CB  GLN A 705     6522   5974   6388    260   -307   -103       C  
ATOM    326  N   ILE A 706     -36.264 -12.309   0.521  1.00 45.98           N  
ANISOU  326  N   ILE A 706     6012   5591   5867    225   -247   -123       N  
ATOM    327  CA  ILE A 706     -36.078 -11.024  -0.112  1.00 51.62           C  
ANISOU  327  CA  ILE A 706     6698   6339   6578    216   -233   -156       C  
ATOM    328  C   ILE A 706     -35.827  -9.987   0.977  1.00 50.59           C  
ANISOU  328  C   ILE A 706     6571   6239   6412    230   -231   -156       C  
ATOM    329  O   ILE A 706     -34.959  -9.149   0.838  1.00 46.26           O  
ANISOU  329  O   ILE A 706     6003   5711   5863    240   -239   -190       O  
ATOM    330  CB  ILE A 706     -37.248 -10.675  -1.075  1.00 55.32           C  
ANISOU  330  CB  ILE A 706     7151   6810   7059    182   -203   -152       C  
ATOM    331  CG1 ILE A 706     -37.156 -11.559  -2.339  1.00 63.02           C  
ANISOU  331  CG1 ILE A 706     8115   7759   8069    175   -212   -171       C  
ATOM    332  CG2 ILE A 706     -37.215  -9.211  -1.483  1.00 54.25           C  
ANISOU  332  CG2 ILE A 706     6991   6707   6913    173   -186   -176       C  
ATOM    333  CD1 ILE A 706     -38.396 -11.601  -3.223  1.00 66.99           C  
ANISOU  333  CD1 ILE A 706     8610   8256   8589    145   -192   -163       C  
ATOM    334  N   GLN A 707     -36.578 -10.071   2.063  1.00 53.31           N  
ANISOU  334  N   GLN A 707     6941   6586   6729    231   -221   -117       N  
ATOM    335  CA  GLN A 707     -36.404  -9.174   3.198  1.00 50.54           C  
ANISOU  335  CA  GLN A 707     6599   6265   6339    248   -221   -117       C  
ATOM    336  C   GLN A 707     -35.001  -9.266   3.769  1.00 46.65           C  
ANISOU  336  C   GLN A 707     6110   5776   5839    284   -259   -141       C  
ATOM    337  O   GLN A 707     -34.370  -8.259   4.051  1.00 43.41           O  
ANISOU  337  O   GLN A 707     5685   5392   5418    296   -267   -171       O  
ATOM    338  CB  GLN A 707     -37.457  -9.495   4.242  1.00 58.59           C  
ANISOU  338  CB  GLN A 707     7648   7285   7329    244   -203    -68       C  
ATOM    339  CG  GLN A 707     -37.343  -8.734   5.550  1.00 67.12           C  
ANISOU  339  CG  GLN A 707     8743   8397   8361    267   -204    -64       C  
ATOM    340  CD  GLN A 707     -38.476  -9.061   6.513  1.00 70.23           C  
ANISOU  340  CD  GLN A 707     9165   8796   8723    262   -179    -13       C  
ATOM    341  OE1 GLN A 707     -39.591  -9.309   6.070  1.00 74.68           O  
ANISOU  341  OE1 GLN A 707     9724   9349   9303    232   -149     12       O  
ATOM    342  NE2 GLN A 707     -38.215  -9.009   7.816  1.00 74.40           N  
ANISOU  342  NE2 GLN A 707     9720   9342   9205    292   -189      2       N  
ATOM    343  N   ALA A 708     -34.484 -10.474   3.880  1.00 43.10           N  
ANISOU  343  N   ALA A 708     5677   5298   5400    301   -284   -131       N  
ATOM    344  CA  ALA A 708     -33.114 -10.661   4.389  1.00 40.38           C  
ANISOU  344  CA  ALA A 708     5335   4955   5053    339   -324   -156       C  
ATOM    345  C   ALA A 708     -32.075 -10.113   3.406  1.00 39.16           C  
ANISOU  345  C   ALA A 708     5140   4810   4930    340   -334   -210       C  
ATOM    346  O   ALA A 708     -31.030  -9.615   3.802  1.00 43.44           O  
ANISOU  346  O   ALA A 708     5669   5367   5467    364   -358   -242       O  
ATOM    347  CB  ALA A 708     -32.861 -12.141   4.666  1.00 40.84           C  
ANISOU  347  CB  ALA A 708     5422   4977   5120    357   -349   -130       C  
ATOM    348  N   ALA A 709     -32.366 -10.229   2.115  1.00 37.71           N  
ANISOU  348  N   ALA A 709     4935   4615   4777    314   -316   -221       N  
ATOM    349  CA  ALA A 709     -31.515  -9.695   1.068  1.00 34.04           C  
ANISOU  349  CA  ALA A 709     4431   4161   4340    310   -317   -268       C  
ATOM    350  C   ALA A 709     -31.454  -8.177   1.150  1.00 31.61           C  
ANISOU  350  C   ALA A 709     4103   3887   4023    300   -302   -287       C  
ATOM    351  O   ALA A 709     -30.388  -7.588   0.986  1.00 33.19           O  
ANISOU  351  O   ALA A 709     4275   4100   4235    311   -314   -325       O  
ATOM    352  CB  ALA A 709     -32.019 -10.144  -0.319  1.00 34.85           C  
ANISOU  352  CB  ALA A 709     4521   4249   4471    285   -298   -271       C  
ATOM    353  N   TYR A 710     -32.596  -7.536   1.378  1.00 31.81           N  
ANISOU  353  N   TYR A 710     4137   3923   4028    280   -274   -263       N  
ATOM    354  CA  TYR A 710     -32.624  -6.093   1.611  1.00 31.43           C  
ANISOU  354  CA  TYR A 710     4072   3902   3969    273   -263   -280       C  
ATOM    355  C   TYR A 710     -31.670  -5.708   2.752  1.00 32.82           C  
ANISOU  355  C   TYR A 710     4250   4092   4128    305   -293   -299       C  
ATOM    356  O   TYR A 710     -30.879  -4.777   2.634  1.00 34.55           O  
ANISOU  356  O   TYR A 710     4442   4326   4361    308   -300   -335       O  
ATOM    357  CB  TYR A 710     -34.038  -5.617   1.957  1.00 32.45           C  
ANISOU  357  CB  TYR A 710     4216   4039   4074    254   -234   -248       C  
ATOM    358  CG  TYR A 710     -34.956  -5.362   0.779  1.00 34.35           C  
ANISOU  358  CG  TYR A 710     4442   4276   4332    220   -203   -241       C  
ATOM    359  CD1 TYR A 710     -34.621  -4.461  -0.214  1.00 32.76           C  
ANISOU  359  CD1 TYR A 710     4211   4084   4151    206   -193   -269       C  
ATOM    360  CD2 TYR A 710     -36.198  -6.002   0.680  1.00 36.13           C  
ANISOU  360  CD2 TYR A 710     4685   4489   4554    203   -185   -206       C  
ATOM    361  CE1 TYR A 710     -35.489  -4.200  -1.266  1.00 35.08           C  
ANISOU  361  CE1 TYR A 710     4496   4377   4457    178   -167   -262       C  
ATOM    362  CE2 TYR A 710     -37.066  -5.757  -0.378  1.00 34.26           C  
ANISOU  362  CE2 TYR A 710     4434   4250   4332    175   -161   -203       C  
ATOM    363  CZ  TYR A 710     -36.710  -4.848  -1.347  1.00 35.24           C  
ANISOU  363  CZ  TYR A 710     4532   4385   4472    164   -153   -230       C  
ATOM    364  OH  TYR A 710     -37.579  -4.616  -2.402  1.00 37.62           O  
ANISOU  364  OH  TYR A 710     4823   4686   4785    139   -132   -226       O  
ATOM    365  N   SER A 711     -31.757  -6.407   3.871  1.00 35.39           N  
ANISOU  365  N   SER A 711     4609   4413   4425    329   -311   -275       N  
ATOM    366  CA  SER A 711     -30.898  -6.095   5.030  1.00 37.04           C  
ANISOU  366  CA  SER A 711     4824   4636   4612    364   -344   -294       C  
ATOM    367  C   SER A 711     -29.405  -6.226   4.702  1.00 37.52           C  
ANISOU  367  C   SER A 711     4858   4693   4704    383   -377   -337       C  
ATOM    368  O   SER A 711     -28.586  -5.380   5.078  1.00 40.51           O  
ANISOU  368  O   SER A 711     5216   5090   5087    398   -396   -374       O  
ATOM    369  CB  SER A 711     -31.214  -7.028   6.190  1.00 38.29           C  
ANISOU  369  CB  SER A 711     5028   4789   4733    388   -359   -255       C  
ATOM    370  OG  SER A 711     -32.542  -6.849   6.635  1.00 41.91           O  
ANISOU  370  OG  SER A 711     5509   5255   5161    372   -328   -216       O  
ATOM    371  N   ILE A 712     -29.045  -7.278   3.978  1.00 36.36           N  
ANISOU  371  N   ILE A 712     4708   4523   4583    385   -384   -337       N  
ATOM    372  CA  ILE A 712     -27.643  -7.463   3.582  1.00 37.33           C  
ANISOU  372  CA  ILE A 712     4801   4643   4738    403   -412   -380       C  
ATOM    373  C   ILE A 712     -27.174  -6.347   2.692  1.00 33.31           C  
ANISOU  373  C   ILE A 712     4247   4151   4260    382   -394   -417       C  
ATOM    374  O   ILE A 712     -26.072  -5.836   2.857  1.00 34.04           O  
ANISOU  374  O   ILE A 712     4311   4254   4370    397   -416   -457       O  
ATOM    375  CB  ILE A 712     -27.426  -8.818   2.877  1.00 40.08           C  
ANISOU  375  CB  ILE A 712     5154   4964   5111    408   -420   -374       C  
ATOM    376  CG1 ILE A 712     -27.574  -9.936   3.903  1.00 46.53           C  
ANISOU  376  CG1 ILE A 712     6016   5761   5904    436   -448   -340       C  
ATOM    377  CG2 ILE A 712     -26.045  -8.894   2.194  1.00 39.33           C  
ANISOU  377  CG2 ILE A 712     5019   4870   5055    422   -440   -423       C  
ATOM    378  CD1 ILE A 712     -27.648 -11.313   3.265  1.00 52.40           C  
ANISOU  378  CD1 ILE A 712     6770   6470   6671    437   -454   -326       C  
ATOM    379  N   LEU A 713     -28.021  -5.937   1.763  1.00 35.54           N  
ANISOU  379  N   LEU A 713     4521   4434   4549    347   -355   -405       N  
ATOM    380  CA  LEU A 713     -27.691  -4.770   0.926  1.00 35.67           C  
ANISOU  380  CA  LEU A 713     4498   4465   4590    324   -334   -433       C  
ATOM    381  C   LEU A 713     -27.503  -3.493   1.756  1.00 34.49           C  
ANISOU  381  C   LEU A 713     4339   4335   4433    327   -341   -450       C  
ATOM    382  O   LEU A 713     -26.647  -2.681   1.432  1.00 32.85           O  
ANISOU  382  O   LEU A 713     4094   4135   4253    323   -343   -485       O  
ATOM    383  CB  LEU A 713     -28.754  -4.532  -0.136  1.00 34.18           C  
ANISOU  383  CB  LEU A 713     4308   4274   4404    288   -293   -412       C  
ATOM    384  CG  LEU A 713     -28.786  -5.558  -1.257  1.00 34.47           C  
ANISOU  384  CG  LEU A 713     4343   4297   4458    281   -285   -409       C  
ATOM    385  CD1 LEU A 713     -29.868  -5.211  -2.267  1.00 34.31           C  
ANISOU  385  CD1 LEU A 713     4322   4278   4437    248   -248   -391       C  
ATOM    386  CD2 LEU A 713     -27.439  -5.621  -1.930  1.00 34.58           C  
ANISOU  386  CD2 LEU A 713     4320   4315   4504    290   -294   -449       C  
ATOM    387  N   SER A 714     -28.268  -3.350   2.833  1.00 36.86           N  
ANISOU  387  N   SER A 714     4670   4640   4695    336   -346   -427       N  
ATOM    388  CA  SER A 714     -28.086  -2.218   3.758  1.00 41.38           C  
ANISOU  388  CA  SER A 714     5237   5229   5255    347   -358   -447       C  
ATOM    389  C   SER A 714     -26.729  -2.286   4.456  1.00 40.71           C  
ANISOU  389  C   SER A 714     5139   5150   5180    381   -403   -485       C  
ATOM    390  O   SER A 714     -26.026  -1.280   4.553  1.00 39.09           O  
ANISOU  390  O   SER A 714     4901   4953   4997    381   -414   -522       O  
ATOM    391  CB  SER A 714     -29.227  -2.140   4.804  1.00 43.48           C  
ANISOU  391  CB  SER A 714     5542   5504   5472    353   -352   -414       C  
ATOM    392  OG  SER A 714     -30.444  -1.625   4.246  1.00 48.35           O  
ANISOU  392  OG  SER A 714     6162   6123   6087    321   -312   -391       O  
ATOM    393  N   GLU A 715     -26.340  -3.479   4.890  1.00 43.73           N  
ANISOU  393  N   GLU A 715     5542   5522   5551    409   -430   -476       N  
ATOM    394  CA  GLU A 715     -24.993  -3.664   5.481  1.00 47.06           C  
ANISOU  394  CA  GLU A 715     5949   5947   5985    445   -477   -514       C  
ATOM    395  C   GLU A 715     -23.877  -3.370   4.468  1.00 43.99           C  
ANISOU  395  C   GLU A 715     5507   5556   5652    434   -477   -556       C  
ATOM    396  O   GLU A 715     -22.859  -2.771   4.786  1.00 39.47           O  
ANISOU  396  O   GLU A 715     4903   4992   5102    448   -503   -599       O  
ATOM    397  CB  GLU A 715     -24.838  -5.069   6.054  1.00 47.62           C  
ANISOU  397  CB  GLU A 715     6056   6004   6034    478   -507   -492       C  
ATOM    398  CG  GLU A 715     -25.780  -5.370   7.217  1.00 54.49           C  
ANISOU  398  CG  GLU A 715     6978   6879   6847    494   -510   -449       C  
ATOM    399  CD  GLU A 715     -25.506  -6.747   7.837  1.00 63.64           C  
ANISOU  399  CD  GLU A 715     8173   8022   7986    529   -543   -426       C  
ATOM    400  OE1 GLU A 715     -26.467  -7.532   8.063  1.00 63.60           O  
ANISOU  400  OE1 GLU A 715     8209   8004   7953    525   -526   -375       O  
ATOM    401  OE2 GLU A 715     -24.306  -7.035   8.113  1.00 66.76           O  
ANISOU  401  OE2 GLU A 715     8555   8415   8397    562   -586   -459       O  
ATOM    402  N   VAL A 716     -24.088  -3.781   3.235  1.00 43.21           N  
ANISOU  402  N   VAL A 716     5396   5446   5574    409   -446   -545       N  
ATOM    403  CA  VAL A 716     -23.104  -3.502   2.190  1.00 44.56           C  
ANISOU  403  CA  VAL A 716     5517   5620   5795    396   -437   -582       C  
ATOM    404  C   VAL A 716     -22.906  -1.999   2.012  1.00 45.46           C  
ANISOU  404  C   VAL A 716     5595   5746   5930    373   -420   -605       C  
ATOM    405  O   VAL A 716     -21.767  -1.520   1.949  1.00 47.43           O  
ANISOU  405  O   VAL A 716     5803   6002   6217    378   -435   -646       O  
ATOM    406  CB  VAL A 716     -23.519  -4.120   0.846  1.00 41.53           C  
ANISOU  406  CB  VAL A 716     5130   5226   5422    372   -402   -564       C  
ATOM    407  CG1 VAL A 716     -22.673  -3.579  -0.288  1.00 42.45           C  
ANISOU  407  CG1 VAL A 716     5196   5352   5583    353   -381   -597       C  
ATOM    408  CG2 VAL A 716     -23.426  -5.628   0.896  1.00 41.74           C  
ANISOU  408  CG2 VAL A 716     5182   5236   5443    397   -423   -552       C  
ATOM    409  N   GLN A 717     -24.014  -1.268   1.929  1.00 46.44           N  
ANISOU  409  N   GLN A 717     5735   5873   6035    347   -391   -579       N  
ATOM    410  CA  GLN A 717     -23.981   0.163   1.707  1.00 47.50           C  
ANISOU  410  CA  GLN A 717     5841   6014   6192    322   -373   -595       C  
ATOM    411  C   GLN A 717     -23.225   0.820   2.844  1.00 44.61           C  
ANISOU  411  C   GLN A 717     5462   5655   5832    346   -413   -632       C  
ATOM    412  O   GLN A 717     -22.393   1.706   2.605  1.00 43.63           O  
ANISOU  412  O   GLN A 717     5295   5533   5751    336   -415   -667       O  
ATOM    413  CB  GLN A 717     -25.405   0.752   1.592  1.00 51.61           C  
ANISOU  413  CB  GLN A 717     6388   6536   6687    297   -341   -560       C  
ATOM    414  CG  GLN A 717     -25.437   2.212   1.143  1.00 54.28           C  
ANISOU  414  CG  GLN A 717     6697   6876   7053    269   -319   -573       C  
ATOM    415  CD  GLN A 717     -24.677   2.440  -0.156  1.00 62.70           C  
ANISOU  415  CD  GLN A 717     7721   7939   8163    245   -295   -586       C  
ATOM    416  OE1 GLN A 717     -25.114   2.014  -1.230  1.00 64.94           O  
ANISOU  416  OE1 GLN A 717     8009   8221   8445    226   -264   -563       O  
ATOM    417  NE2 GLN A 717     -23.528   3.129  -0.068  1.00 67.31           N  
ANISOU  417  NE2 GLN A 717     8263   8524   8788    245   -309   -625       N  
ATOM    418  N   GLN A 718     -23.500   0.385   4.068  1.00 41.67           N  
ANISOU  418  N   GLN A 718     5126   5287   5418    379   -444   -624       N  
ATOM    419  CA  GLN A 718     -22.788   0.919   5.217  1.00 46.75           C  
ANISOU  419  CA  GLN A 718     5761   5940   6062    408   -488   -661       C  
ATOM    420  C   GLN A 718     -21.275   0.618   5.150  1.00 47.96           C  
ANISOU  420  C   GLN A 718     5874   6091   6256    428   -522   -706       C  
ATOM    421  O   GLN A 718     -20.447   1.492   5.412  1.00 46.60           O  
ANISOU  421  O   GLN A 718     5664   5923   6118    430   -542   -749       O  
ATOM    422  CB  GLN A 718     -23.399   0.394   6.513  1.00 50.79           C  
ANISOU  422  CB  GLN A 718     6325   6460   6513    442   -513   -640       C  
ATOM    423  CG  GLN A 718     -22.919   1.163   7.743  1.00 61.77           C  
ANISOU  423  CG  GLN A 718     7712   7864   7893    472   -555   -677       C  
ATOM    424  CD  GLN A 718     -23.064   0.416   9.061  1.00 63.52           C  
ANISOU  424  CD  GLN A 718     7982   8098   8057    517   -592   -664       C  
ATOM    425  OE1 GLN A 718     -22.943  -0.816   9.136  1.00 68.71           O  
ANISOU  425  OE1 GLN A 718     8663   8748   8696    537   -604   -641       O  
ATOM    426  NE2 GLN A 718     -23.307   1.170  10.110  1.00 64.28           N  
ANISOU  426  NE2 GLN A 718     8091   8210   8122    536   -611   -680       N  
ATOM    427  N   ALA A 719     -20.924  -0.615   4.805  1.00 49.08           N  
ANISOU  427  N   ALA A 719     6023   6227   6399    442   -529   -697       N  
ATOM    428  CA  ALA A 719     -19.513  -1.000   4.686  1.00 51.91           C  
ANISOU  428  CA  ALA A 719     6342   6584   6798    463   -560   -739       C  
ATOM    429  C   ALA A 719     -18.790  -0.214   3.577  1.00 49.91           C  
ANISOU  429  C   ALA A 719     6027   6331   6605    429   -531   -769       C  
ATOM    430  O   ALA A 719     -17.696   0.235   3.767  1.00 49.97           O  
ANISOU  430  O   ALA A 719     5991   6342   6653    438   -556   -814       O  
ATOM    431  CB  ALA A 719     -19.397  -2.493   4.449  1.00 52.34           C  
ANISOU  431  CB  ALA A 719     6417   6628   6841    484   -569   -721       C  
ATOM    432  N   VAL A 720     -19.437  -0.006   2.449  1.00 51.28           N  
ANISOU  432  N   VAL A 720     6197   6501   6784    390   -480   -742       N  
ATOM    433  CA  VAL A 720     -18.891   0.871   1.406  1.00 54.70           C  
ANISOU  433  CA  VAL A 720     6578   6936   7269    355   -446   -761       C  
ATOM    434  C   VAL A 720     -18.682   2.323   1.873  1.00 55.69           C  
ANISOU  434  C   VAL A 720     6677   7063   7420    341   -452   -786       C  
ATOM    435  O   VAL A 720     -17.580   2.894   1.729  1.00 55.56           O  
ANISOU  435  O   VAL A 720     6607   7047   7456    336   -461   -826       O  
ATOM    436  CB  VAL A 720     -19.793   0.853   0.158  1.00 56.14           C  
ANISOU  436  CB  VAL A 720     6772   7117   7443    319   -390   -722       C  
ATOM    437  CG1 VAL A 720     -19.402   1.930  -0.846  1.00 57.96           C  
ANISOU  437  CG1 VAL A 720     6955   7349   7718    280   -352   -733       C  
ATOM    438  CG2 VAL A 720     -19.712  -0.522  -0.478  1.00 58.90           C  
ANISOU  438  CG2 VAL A 720     7132   7464   7783    331   -386   -711       C  
ATOM    439  N   SER A 721     -19.722   2.914   2.454  1.00 54.68           N  
ANISOU  439  N   SER A 721     6583   6933   7258    336   -449   -764       N  
ATOM    440  CA  SER A 721     -19.620   4.301   2.947  1.00 54.94           C  
ANISOU  440  CA  SER A 721     6596   6965   7314    325   -458   -789       C  
ATOM    441  C   SER A 721     -18.372   4.546   3.826  1.00 52.57           C  
ANISOU  441  C   SER A 721     6261   6667   7046    353   -511   -845       C  
ATOM    442  O   SER A 721     -17.799   5.622   3.761  1.00 51.53           O  
ANISOU  442  O   SER A 721     6086   6529   6964    336   -513   -877       O  
ATOM    443  CB  SER A 721     -20.906   4.724   3.661  1.00 54.67           C  
ANISOU  443  CB  SER A 721     6608   6931   7231    327   -456   -762       C  
ATOM    444  OG  SER A 721     -21.961   4.962   2.744  1.00 52.16           O  
ANISOU  444  OG  SER A 721     6306   6609   6903    293   -407   -721       O  
ATOM    445  N   GLN A 722     -17.935   3.556   4.611  1.00 56.61           N  
ANISOU  445  N   GLN A 722     6790   7186   7534    397   -555   -857       N  
ATOM    446  CA  GLN A 722     -16.570   3.595   5.213  1.00 57.96           C  
ANISOU  446  CA  GLN A 722     6920   7360   7742    425   -605   -914       C  
ATOM    447  C   GLN A 722     -15.539   2.646   4.596  1.00 62.77           C  
ANISOU  447  C   GLN A 722     7496   7969   8383    436   -610   -931       C  
ATOM    448  O   GLN A 722     -15.358   2.594   3.369  1.00 63.86           O  
ANISOU  448  O   GLN A 722     7605   8104   8553    404   -566   -921       O  
ATOM    449  CB  GLN A 722     -16.612   3.354   6.713  1.00 60.42           C  
ANISOU  449  CB  GLN A 722     7267   7680   8009    474   -663   -929       C  
ATOM    450  CG  GLN A 722     -17.138   2.018   7.203  1.00 62.61           C  
ANISOU  450  CG  GLN A 722     7603   7962   8222    508   -678   -892       C  
ATOM    451  CD  GLN A 722     -18.477   2.160   7.899  1.00 61.06           C  
ANISOU  451  CD  GLN A 722     7466   7773   7961    512   -668   -853       C  
ATOM    452  OE1 GLN A 722     -19.370   2.824   7.382  1.00 69.16           O  
ANISOU  452  OE1 GLN A 722     8498   8795   8984    476   -625   -828       O  
ATOM    453  NE2 GLN A 722     -18.628   1.542   9.070  1.00 57.40           N  
ANISOU  453  NE2 GLN A 722     7047   7319   7443    557   -709   -846       N  
ATOM    454  N   ASP A 726     -12.082  -3.977   2.462  1.00 86.95           N  
ANISOU  454  N   ASP A 726    10513  11025  11500    566   -673   -977       N  
ATOM    455  CA  ASP A 726     -12.189  -4.719   1.202  1.00 90.79           C  
ANISOU  455  CA  ASP A 726    10992  11509  11994    551   -631   -963       C  
ATOM    456  C   ASP A 726     -12.524  -6.192   1.403  1.00 94.24           C  
ANISOU  456  C   ASP A 726    11479  11929  12398    587   -657   -940       C  
ATOM    457  O   ASP A 726     -13.196  -6.803   0.576  1.00 88.42           O  
ANISOU  457  O   ASP A 726    10765  11185  11646    572   -622   -910       O  
ATOM    458  CB  ASP A 726     -10.877  -4.619   0.426  1.00 94.96           C  
ANISOU  458  CB  ASP A 726    11445  12050  12587    549   -621  -1014       C  
ATOM    459  N   SER A 727     -12.024  -6.756   2.495  1.00 94.26           N  
ANISOU  459  N   SER A 727    11496  11925  12393    635   -719   -956       N  
ATOM    460  CA  SER A 727     -12.280  -8.143   2.883  1.00 87.47           C  
ANISOU  460  CA  SER A 727    10688  11045  11504    673   -753   -932       C  
ATOM    461  C   SER A 727     -13.719  -8.379   3.379  1.00 82.49           C  
ANISOU  461  C   SER A 727    10131  10401  10810    665   -742   -868       C  
ATOM    462  O   SER A 727     -14.364  -9.344   2.968  1.00 77.41           O  
ANISOU  462  O   SER A 727     9524   9739  10149    664   -729   -834       O  
ATOM    463  CB  SER A 727     -11.269  -8.529   3.971  1.00 84.03           C  
ANISOU  463  CB  SER A 727    10245  10607  11077    728   -825   -968       C  
ATOM    464  OG  SER A 727     -11.522  -9.804   4.516  1.00 84.02           O  
ANISOU  464  OG  SER A 727    10297  10583  11044    768   -863   -941       O  
ATOM    465  N   GLN A 728     -14.207  -7.521   4.279  1.00 77.50           N  
ANISOU  465  N   GLN A 728     9521   9778  10147    659   -749   -855       N  
ATOM    466  CA  GLN A 728     -15.569  -7.653   4.813  1.00 74.07           C  
ANISOU  466  CA  GLN A 728     9154   9336   9654    651   -737   -796       C  
ATOM    467  C   GLN A 728     -16.621  -7.448   3.724  1.00 69.68           C  
ANISOU  467  C   GLN A 728     8605   8778   9093    601   -672   -761       C  
ATOM    468  O   GLN A 728     -17.671  -8.078   3.765  1.00 64.52           O  
ANISOU  468  O   GLN A 728     8002   8110   8404    595   -658   -713       O  
ATOM    469  CB  GLN A 728     -15.806  -6.669   5.955  1.00 70.72           C  
ANISOU  469  CB  GLN A 728     8745   8927   9200    657   -756   -797       C  
ATOM    470  N   ILE A 729     -16.321  -6.587   2.745  1.00 67.27           N  
ANISOU  470  N   ILE A 729     8249   8486   8825    566   -633   -785       N  
ATOM    471  CA  ILE A 729     -17.279  -6.278   1.678  1.00 65.61           C  
ANISOU  471  CA  ILE A 729     8044   8276   8609    520   -573   -755       C  
ATOM    472  C   ILE A 729     -17.411  -7.466   0.739  1.00 64.55           C  
ANISOU  472  C   ILE A 729     7918   8128   8481    521   -559   -744       C  
ATOM    473  O   ILE A 729     -18.503  -7.729   0.255  1.00 66.10           O  
ANISOU  473  O   ILE A 729     8146   8316   8654    498   -527   -704       O  
ATOM    474  CB  ILE A 729     -17.042  -4.897   0.956  1.00 68.13           C  
ANISOU  474  CB  ILE A 729     8313   8613   8961    480   -534   -776       C  
ATOM    475  CG1 ILE A 729     -16.923  -5.018  -0.561  1.00 67.70           C  
ANISOU  475  CG1 ILE A 729     8228   8563   8933    452   -487   -780       C  
ATOM    476  CG2 ILE A 729     -15.811  -4.173   1.485  1.00 70.26           C  
ANISOU  476  CG2 ILE A 729     8534   8894   9268    494   -565   -827       C  
ATOM    477  CD1 ILE A 729     -16.789  -3.661  -1.219  1.00 71.13           C  
ANISOU  477  CD1 ILE A 729     8621   9012   9394    412   -446   -790       C  
ATOM    478  N   LEU A 730     -16.321  -8.201   0.527  1.00 67.52           N  
ANISOU  478  N   LEU A 730     8265   8500   8889    550   -585   -780       N  
ATOM    479  CA  LEU A 730     -16.377  -9.467  -0.209  1.00 65.35           C  
ANISOU  479  CA  LEU A 730     8001   8209   8621    561   -583   -775       C  
ATOM    480  C   LEU A 730     -17.321 -10.449   0.469  1.00 61.92           C  
ANISOU  480  C   LEU A 730     7633   7747   8147    578   -604   -727       C  
ATOM    481  O   LEU A 730     -18.185 -10.993  -0.186  1.00 60.51           O  
ANISOU  481  O   LEU A 730     7479   7555   7957    560   -577   -698       O  
ATOM    482  CB  LEU A 730     -14.999 -10.106  -0.341  1.00 67.13           C  
ANISOU  482  CB  LEU A 730     8186   8434   8887    598   -616   -825       C  
ATOM    483  N   ASP A 731     -17.195 -10.633   1.784  1.00 59.96           N  
ANISOU  483  N   ASP A 731     7414   7492   7877    610   -650   -718       N  
ATOM    484  CA  ASP A 731     -18.079 -11.565   2.509  1.00 62.52           C  
ANISOU  484  CA  ASP A 731     7803   7790   8162    625   -668   -668       C  
ATOM    485  C   ASP A 731     -19.574 -11.167   2.425  1.00 64.67           C  
ANISOU  485  C   ASP A 731     8112   8063   8398    586   -624   -616       C  
ATOM    486  O   ASP A 731     -20.448 -12.036   2.302  1.00 56.90           O  
ANISOU  486  O   ASP A 731     7167   7054   7399    580   -615   -576       O  
ATOM    487  CB  ASP A 731     -17.639 -11.678   3.988  1.00 68.26           C  
ANISOU  487  CB  ASP A 731     8554   8516   8865    669   -723   -667       C  
ATOM    488  CG  ASP A 731     -18.806 -12.025   4.960  1.00 72.10           C  
ANISOU  488  CG  ASP A 731     9110   8990   9297    672   -726   -605       C  
ATOM    489  OD1 ASP A 731     -19.193 -13.203   5.140  1.00 71.43           O  
ANISOU  489  OD1 ASP A 731     9066   8874   9199    687   -741   -570       O  
ATOM    490  OD2 ASP A 731     -19.332 -11.080   5.582  1.00 80.70           O  
ANISOU  490  OD2 ASP A 731    10211  10099  10354    658   -714   -591       O  
ATOM    491  N   LEU A 732     -19.866  -9.861   2.505  1.00 60.26           N  
ANISOU  491  N   LEU A 732     7538   7529   7830    559   -598   -619       N  
ATOM    492  CA  LEU A 732     -21.250  -9.413   2.450  1.00 56.24           C  
ANISOU  492  CA  LEU A 732     7059   7021   7289    524   -558   -575       C  
ATOM    493  C   LEU A 732     -21.807  -9.647   1.061  1.00 50.63           C  
ANISOU  493  C   LEU A 732     6338   6304   6595    490   -515   -566       C  
ATOM    494  O   LEU A 732     -22.940 -10.106   0.915  1.00 48.12           O  
ANISOU  494  O   LEU A 732     6055   5972   6258    473   -496   -525       O  
ATOM    495  CB  LEU A 732     -21.386  -7.942   2.856  1.00 54.92           C  
ANISOU  495  CB  LEU A 732     6876   6879   7111    506   -545   -584       C  
ATOM    496  CG  LEU A 732     -21.107  -7.669   4.338  1.00 53.78           C  
ANISOU  496  CG  LEU A 732     6751   6744   6938    539   -586   -587       C  
ATOM    497  CD1 LEU A 732     -20.975  -6.168   4.570  1.00 55.38           C  
ANISOU  497  CD1 LEU A 732     6927   6971   7146    523   -577   -612       C  
ATOM    498  CD2 LEU A 732     -22.174  -8.265   5.238  1.00 52.63           C  
ANISOU  498  CD2 LEU A 732     6668   6588   6741    549   -590   -533       C  
ATOM    499  N   SER A 733     -21.004  -9.317   0.057  1.00 48.04           N  
ANISOU  499  N   SER A 733     5961   5988   6304    481   -501   -606       N  
ATOM    500  CA  SER A 733     -21.362  -9.569  -1.329  1.00 50.04           C  
ANISOU  500  CA  SER A 733     6201   6239   6572    455   -463   -606       C  
ATOM    501  C   SER A 733     -21.778 -11.037  -1.506  1.00 55.69           C  
ANISOU  501  C   SER A 733     6950   6925   7285    470   -477   -586       C  
ATOM    502  O   SER A 733     -22.815 -11.336  -2.099  1.00 54.98           O  
ANISOU  502  O   SER A 733     6881   6824   7185    446   -451   -558       O  
ATOM    503  CB  SER A 733     -20.191  -9.255  -2.246  1.00 47.44           C  
ANISOU  503  CB  SER A 733     5815   5929   6283    454   -453   -655       C  
ATOM    504  OG  SER A 733     -20.496  -8.208  -3.151  1.00 50.20           O  
ANISOU  504  OG  SER A 733     6140   6298   6636    415   -405   -655       O  
ATOM    505  N   ASN A 734     -20.965 -11.939  -0.974  1.00 58.02           N  
ANISOU  505  N   ASN A 734     7248   7203   7592    509   -521   -602       N  
ATOM    506  CA  ASN A 734     -21.217 -13.374  -1.088  1.00 56.52           C  
ANISOU  506  CA  ASN A 734     7088   6979   7407    528   -541   -586       C  
ATOM    507  C   ASN A 734     -22.428 -13.819  -0.308  1.00 52.33           C  
ANISOU  507  C   ASN A 734     6614   6426   6844    521   -543   -528       C  
ATOM    508  O   ASN A 734     -23.134 -14.710  -0.747  1.00 54.03           O  
ANISOU  508  O   ASN A 734     6852   6613   7063    514   -537   -506       O  
ATOM    509  CB  ASN A 734     -19.982 -14.180  -0.669  1.00 59.99           C  
ANISOU  509  CB  ASN A 734     7516   7406   7870    575   -591   -619       C  
ATOM    510  CG  ASN A 734     -18.809 -13.982  -1.627  1.00 62.02           C  
ANISOU  510  CG  ASN A 734     7714   7684   8168    581   -585   -678       C  
ATOM    511  OD1 ASN A 734     -18.991 -13.676  -2.805  1.00 61.66           O  
ANISOU  511  OD1 ASN A 734     7643   7652   8132    554   -544   -690       O  
ATOM    512  ND2 ASN A 734     -17.602 -14.148  -1.117  1.00 64.68           N  
ANISOU  512  ND2 ASN A 734     8027   8023   8525    619   -625   -715       N  
ATOM    513  N   ARG A 735     -22.674 -13.203   0.841  1.00 48.16           N  
ANISOU  513  N   ARG A 735     6106   5908   6284    525   -552   -506       N  
ATOM    514  CA  ARG A 735     -23.851 -13.551   1.613  1.00 44.81           C  
ANISOU  514  CA  ARG A 735     5734   5466   5824    518   -548   -449       C  
ATOM    515  C   ARG A 735     -25.094 -13.188   0.775  1.00 43.34           C  
ANISOU  515  C   ARG A 735     5551   5284   5634    472   -498   -425       C  
ATOM    516  O   ARG A 735     -26.085 -13.943   0.725  1.00 42.06           O  
ANISOU  516  O   ARG A 735     5421   5096   5466    459   -489   -386       O  
ATOM    517  CB  ARG A 735     -23.826 -12.861   2.996  1.00 47.31           C  
ANISOU  517  CB  ARG A 735     6070   5802   6104    533   -565   -435       C  
ATOM    518  N   PHE A 736     -25.032 -12.053   0.075  1.00 41.24           N  
ANISOU  518  N   PHE A 736     5249   5047   5374    446   -467   -450       N  
ATOM    519  CA  PHE A 736     -26.143 -11.633  -0.780  1.00 39.01           C  
ANISOU  519  CA  PHE A 736     4966   4770   5087    406   -423   -431       C  
ATOM    520  C   PHE A 736     -26.392 -12.642  -1.912  1.00 37.06           C  
ANISOU  520  C   PHE A 736     4718   4500   4864    399   -416   -435       C  
ATOM    521  O   PHE A 736     -27.505 -13.073  -2.133  1.00 34.10           O  
ANISOU  521  O   PHE A 736     4367   4108   4483    379   -401   -403       O  
ATOM    522  CB  PHE A 736     -25.900 -10.245  -1.374  1.00 37.14           C  
ANISOU  522  CB  PHE A 736     4691   4566   4855    383   -395   -457       C  
ATOM    523  CG  PHE A 736     -26.991  -9.797  -2.288  1.00 35.80           C  
ANISOU  523  CG  PHE A 736     4520   4401   4680    345   -353   -440       C  
ATOM    524  CD1 PHE A 736     -28.160  -9.263  -1.793  1.00 35.00           C  
ANISOU  524  CD1 PHE A 736     4443   4304   4553    325   -334   -404       C  
ATOM    525  CD2 PHE A 736     -26.859  -9.947  -3.654  1.00 36.66           C  
ANISOU  525  CD2 PHE A 736     4606   4514   4810    332   -333   -461       C  
ATOM    526  CE1 PHE A 736     -29.159  -8.833  -2.642  1.00 34.47           C  
ANISOU  526  CE1 PHE A 736     4373   4241   4482    292   -299   -390       C  
ATOM    527  CE2 PHE A 736     -27.873  -9.549  -4.507  1.00 37.51           C  
ANISOU  527  CE2 PHE A 736     4715   4627   4911    300   -299   -445       C  
ATOM    528  CZ  PHE A 736     -29.024  -8.987  -4.000  1.00 34.72           C  
ANISOU  528  CZ  PHE A 736     4384   4275   4534    280   -283   -409       C  
ATOM    529  N   TYR A 737     -25.327 -13.010  -2.606  1.00 37.65           N  
ANISOU  529  N   TYR A 737     4762   4575   4967    416   -429   -477       N  
ATOM    530  CA  TYR A 737     -25.404 -13.971  -3.713  1.00 39.90           C  
ANISOU  530  CA  TYR A 737     5043   4842   5276    416   -426   -491       C  
ATOM    531  C   TYR A 737     -25.842 -15.399  -3.289  1.00 41.84           C  
ANISOU  531  C   TYR A 737     5327   5042   5528    432   -455   -464       C  
ATOM    532  O   TYR A 737     -26.370 -16.153  -4.103  1.00 44.09           O  
ANISOU  532  O   TYR A 737     5617   5306   5828    422   -449   -463       O  
ATOM    533  CB  TYR A 737     -24.077 -14.010  -4.477  1.00 38.08           C  
ANISOU  533  CB  TYR A 737     4768   4626   5073    435   -433   -546       C  
ATOM    534  CG  TYR A 737     -23.777 -12.730  -5.253  1.00 38.23           C  
ANISOU  534  CG  TYR A 737     4747   4685   5092    411   -396   -570       C  
ATOM    535  CD1 TYR A 737     -24.689 -12.219  -6.146  1.00 39.66           C  
ANISOU  535  CD1 TYR A 737     4928   4878   5262    377   -356   -556       C  
ATOM    536  CD2 TYR A 737     -22.581 -12.038  -5.091  1.00 40.25           C  
ANISOU  536  CD2 TYR A 737     4965   4966   5362    423   -401   -604       C  
ATOM    537  CE1 TYR A 737     -24.414 -11.061  -6.855  1.00 40.60           C  
ANISOU  537  CE1 TYR A 737     5014   5031   5381    356   -323   -572       C  
ATOM    538  CE2 TYR A 737     -22.287 -10.871  -5.801  1.00 41.38           C  
ANISOU  538  CE2 TYR A 737     5071   5142   5509    400   -365   -622       C  
ATOM    539  CZ  TYR A 737     -23.217 -10.383  -6.683  1.00 41.08           C  
ANISOU  539  CZ  TYR A 737     5037   5113   5456    366   -325   -604       C  
ATOM    540  OH  TYR A 737     -22.963  -9.237  -7.430  1.00 40.71           O  
ANISOU  540  OH  TYR A 737     4958   5098   5414    342   -288   -616       O  
ATOM    541  N   THR A 738     -25.652 -15.730  -2.017  1.00 41.88           N  
ANISOU  541  N   THR A 738     5359   5032   5521    455   -485   -442       N  
ATOM    542  CA  THR A 738     -26.117 -16.986  -1.466  1.00 41.85           C  
ANISOU  542  CA  THR A 738     5396   4984   5521    468   -510   -406       C  
ATOM    543  C   THR A 738     -27.602 -16.934  -1.263  1.00 43.52           C  
ANISOU  543  C   THR A 738     5638   5185   5713    434   -482   -355       C  
ATOM    544  O   THR A 738     -28.304 -17.896  -1.547  1.00 47.78           O  
ANISOU  544  O   THR A 738     6197   5689   6269    426   -484   -333       O  
ATOM    545  CB  THR A 738     -25.419 -17.276  -0.123  1.00 43.85           C  
ANISOU  545  CB  THR A 738     5671   5229   5762    506   -551   -395       C  
ATOM    546  OG1 THR A 738     -24.027 -17.501  -0.360  1.00 42.53           O  
ANISOU  546  OG1 THR A 738     5473   5066   5620    541   -582   -446       O  
ATOM    547  CG2 THR A 738     -26.025 -18.505   0.563  1.00 44.83           C  
ANISOU  547  CG2 THR A 738     5844   5306   5885    516   -573   -346       C  
ATOM    548  N   LEU A 739     -28.097 -15.790  -0.801  1.00 45.51           N  
ANISOU  548  N   LEU A 739     5890   5468   5933    415   -457   -338       N  
ATOM    549  CA  LEU A 739     -29.531 -15.611  -0.615  1.00 44.78           C  
ANISOU  549  CA  LEU A 739     5821   5372   5822    382   -427   -292       C  
ATOM    550  C   LEU A 739     -30.274 -15.477  -1.937  1.00 41.82           C  
ANISOU  550  C   LEU A 739     5426   4998   5463    349   -396   -302       C  
ATOM    551  O   LEU A 739     -31.384 -15.977  -2.097  1.00 41.08           O  
ANISOU  551  O   LEU A 739     5350   4882   5375    327   -383   -271       O  
ATOM    552  CB  LEU A 739     -29.786 -14.357   0.191  1.00 50.92           C  
ANISOU  552  CB  LEU A 739     6599   6185   6562    374   -409   -278       C  
ATOM    553  CG  LEU A 739     -30.769 -14.454   1.329  1.00 58.65           C  
ANISOU  553  CG  LEU A 739     7617   7158   7509    368   -401   -224       C  
ATOM    554  CD1 LEU A 739     -30.447 -15.558   2.323  1.00 63.29           C  
ANISOU  554  CD1 LEU A 739     8241   7715   8092    399   -436   -196       C  
ATOM    555  CD2 LEU A 739     -30.794 -13.107   2.028  1.00 58.59           C  
ANISOU  555  CD2 LEU A 739     7604   7191   7468    367   -388   -226       C  
ATOM    556  N   ILE A 740     -29.671 -14.769  -2.881  1.00 39.36           N  
ANISOU  556  N   ILE A 740     5079   4716   5162    345   -384   -345       N  
ATOM    557  CA  ILE A 740     -30.277 -14.551  -4.195  1.00 38.53           C  
ANISOU  557  CA  ILE A 740     4955   4618   5067    318   -356   -358       C  
ATOM    558  C   ILE A 740     -29.311 -15.086  -5.225  1.00 35.82           C  
ANISOU  558  C   ILE A 740     4587   4273   4751    335   -369   -406       C  
ATOM    559  O   ILE A 740     -28.388 -14.389  -5.657  1.00 31.52           O  
ANISOU  559  O   ILE A 740     4011   3759   4208    342   -362   -442       O  
ATOM    560  CB  ILE A 740     -30.557 -13.085  -4.464  1.00 38.67           C  
ANISOU  560  CB  ILE A 740     4953   4675   5064    294   -323   -362       C  
ATOM    561  CG1 ILE A 740     -31.269 -12.473  -3.269  1.00 39.18           C  
ANISOU  561  CG1 ILE A 740     5040   4746   5100    285   -314   -323       C  
ATOM    562  CG2 ILE A 740     -31.383 -12.931  -5.752  1.00 41.65           C  
ANISOU  562  CG2 ILE A 740     5320   5057   5448    267   -296   -367       C  
ATOM    563  CD1 ILE A 740     -32.694 -12.936  -3.092  1.00 38.46           C  
ANISOU  563  CD1 ILE A 740     4975   4634   5004    263   -301   -280       C  
ATOM    564  N   PRO A 741     -29.515 -16.345  -5.599  1.00 36.17           N  
ANISOU  564  N   PRO A 741     4644   4281   4819    343   -387   -407       N  
ATOM    565  CA  PRO A 741     -28.539 -16.988  -6.475  1.00 35.14           C  
ANISOU  565  CA  PRO A 741     4491   4146   4714    367   -404   -455       C  
ATOM    566  C   PRO A 741     -28.502 -16.346  -7.836  1.00 31.76           C  
ANISOU  566  C   PRO A 741     4032   3752   4285    351   -374   -489       C  
ATOM    567  O   PRO A 741     -29.550 -16.111  -8.475  1.00 30.02           O  
ANISOU  567  O   PRO A 741     3815   3534   4056    324   -351   -476       O  
ATOM    568  CB  PRO A 741     -29.005 -18.449  -6.563  1.00 37.07           C  
ANISOU  568  CB  PRO A 741     4759   4339   4986    374   -429   -445       C  
ATOM    569  CG  PRO A 741     -30.177 -18.597  -5.652  1.00 38.15           C  
ANISOU  569  CG  PRO A 741     4931   4452   5111    354   -425   -387       C  
ATOM    570  CD  PRO A 741     -30.585 -17.257  -5.142  1.00 37.63           C  
ANISOU  570  CD  PRO A 741     4864   4424   5011    333   -395   -364       C  
ATOM    571  N   HIS A 742     -27.281 -16.068  -8.254  1.00 32.53           N  
ANISOU  571  N   HIS A 742     4096   3873   4389    371   -375   -531       N  
ATOM    572  CA  HIS A 742     -26.992 -15.506  -9.535  1.00 35.72           C  
ANISOU  572  CA  HIS A 742     4470   4313   4791    362   -347   -565       C  
ATOM    573  C   HIS A 742     -26.252 -16.522 -10.362  1.00 36.18           C  
ANISOU  573  C   HIS A 742     4513   4362   4874    390   -364   -611       C  
ATOM    574  O   HIS A 742     -25.715 -17.486  -9.841  1.00 36.22           O  
ANISOU  574  O   HIS A 742     4525   4337   4900    418   -400   -620       O  
ATOM    575  CB  HIS A 742     -26.163 -14.216  -9.363  1.00 35.82           C  
ANISOU  575  CB  HIS A 742     4452   4366   4792    358   -327   -577       C  
ATOM    576  CG  HIS A 742     -26.985 -13.036  -8.971  1.00 36.02           C  
ANISOU  576  CG  HIS A 742     4487   4407   4793    327   -301   -541       C  
ATOM    577  ND1 HIS A 742     -27.668 -12.973  -7.778  1.00 35.45           N  
ANISOU  577  ND1 HIS A 742     4443   4317   4707    322   -312   -501       N  
ATOM    578  CD2 HIS A 742     -27.262 -11.882  -9.623  1.00 36.02           C  
ANISOU  578  CD2 HIS A 742     4471   4439   4777    302   -265   -539       C  
ATOM    579  CE1 HIS A 742     -28.293 -11.814  -7.688  1.00 34.02           C  
ANISOU  579  CE1 HIS A 742     4263   4157   4507    295   -285   -480       C  
ATOM    580  NE2 HIS A 742     -28.069 -11.135  -8.796  1.00 34.74           N  
ANISOU  580  NE2 HIS A 742     4327   4275   4597    282   -257   -502       N  
ATOM    581  N   ASP A 743     -26.161 -16.245 -11.651  1.00 39.99           N  
ANISOU  581  N   ASP A 743     4971   4873   5350    383   -338   -640       N  
ATOM    582  CA  ASP A 743     -25.546 -17.127 -12.620  1.00 41.74           C  
ANISOU  582  CA  ASP A 743     5176   5093   5590    409   -349   -688       C  
ATOM    583  C   ASP A 743     -24.588 -16.261 -13.423  1.00 43.20           C  
ANISOU  583  C   ASP A 743     5319   5329   5765    410   -316   -722       C  
ATOM    584  O   ASP A 743     -24.929 -15.687 -14.453  1.00 45.49           O  
ANISOU  584  O   ASP A 743     5600   5651   6035    393   -282   -728       O  
ATOM    585  CB  ASP A 743     -26.573 -17.764 -13.547  1.00 46.24           C  
ANISOU  585  CB  ASP A 743     5763   5648   6159    399   -347   -691       C  
ATOM    586  CG  ASP A 743     -25.916 -18.666 -14.611  1.00 49.00           C  
ANISOU  586  CG  ASP A 743     6093   5999   6525    429   -359   -747       C  
ATOM    587  OD1 ASP A 743     -26.573 -19.069 -15.589  1.00 54.62           O  
ANISOU  587  OD1 ASP A 743     6812   6710   7233    424   -355   -762       O  
ATOM    588  OD2 ASP A 743     -24.715 -18.922 -14.484  1.00 48.13           O  
ANISOU  588  OD2 ASP A 743     5960   5895   6430    458   -371   -780       O  
ATOM    589  N   PHE A 744     -23.378 -16.147 -12.924  1.00 49.93           N  
ANISOU  589  N   PHE A 744     6147   6191   6633    432   -326   -744       N  
ATOM    590  CA  PHE A 744     -22.378 -15.330 -13.584  1.00 55.89           C  
ANISOU  590  CA  PHE A 744     6857   6993   7385    432   -295   -775       C  
ATOM    591  C   PHE A 744     -21.503 -16.153 -14.532  1.00 59.00           C  
ANISOU  591  C   PHE A 744     7224   7398   7795    464   -298   -831       C  
ATOM    592  O   PHE A 744     -21.842 -16.293 -15.704  1.00 61.50           O  
ANISOU  592  O   PHE A 744     7538   7732   8097    460   -277   -848       O  
ATOM    593  CB  PHE A 744     -21.530 -14.635 -12.539  1.00 53.14           C  
ANISOU  593  CB  PHE A 744     6490   6653   7047    436   -302   -772       C  
ATOM    594  CG  PHE A 744     -22.317 -13.705 -11.667  1.00 53.85           C  
ANISOU  594  CG  PHE A 744     6603   6739   7118    407   -295   -723       C  
ATOM    595  CD1 PHE A 744     -22.929 -12.585 -12.211  1.00 51.85           C  
ANISOU  595  CD1 PHE A 744     6348   6513   6842    372   -253   -702       C  
ATOM    596  CD2 PHE A 744     -22.451 -13.947 -10.310  1.00 51.08           C  
ANISOU  596  CD2 PHE A 744     6277   6359   6771    416   -329   -698       C  
ATOM    597  CE1 PHE A 744     -23.640 -11.723 -11.407  1.00 51.36           C  
ANISOU  597  CE1 PHE A 744     6303   6446   6763    348   -248   -661       C  
ATOM    598  CE2 PHE A 744     -23.148 -13.068  -9.500  1.00 49.76           C  
ANISOU  598  CE2 PHE A 744     6129   6192   6584    392   -321   -658       C  
ATOM    599  CZ  PHE A 744     -23.764 -11.972 -10.054  1.00 49.00           C  
ANISOU  599  CZ  PHE A 744     6029   6121   6469    358   -281   -641       C  
ATOM    600  N   LYS A 748     -17.279 -14.609 -13.103  1.00 62.36           N  
ANISOU  600  N   LYS A 748     7513   7890   8290    508   -300   -912       N  
ATOM    601  CA  LYS A 748     -16.728 -14.055 -11.847  1.00 67.61           C  
ANISOU  601  CA  LYS A 748     8169   8549   8972    511   -324   -904       C  
ATOM    602  C   LYS A 748     -17.712 -13.052 -11.186  1.00 67.02           C  
ANISOU  602  C   LYS A 748     8124   8469   8870    474   -312   -850       C  
ATOM    603  O   LYS A 748     -18.173 -12.116 -11.855  1.00 59.86           O  
ANISOU  603  O   LYS A 748     7213   7588   7945    440   -267   -833       O  
ATOM    604  CB  LYS A 748     -15.359 -13.386 -12.089  1.00 69.42           C  
ANISOU  604  CB  LYS A 748     8334   8815   9227    516   -304   -944       C  
ATOM    605  N   PRO A 749     -18.043 -13.244  -9.881  1.00 68.91           N  
ANISOU  605  N   PRO A 749     8397   8677   9107    482   -352   -824       N  
ATOM    606  CA  PRO A 749     -19.161 -12.476  -9.294  1.00 67.32           C  
ANISOU  606  CA  PRO A 749     8232   8470   8878    451   -341   -773       C  
ATOM    607  C   PRO A 749     -18.810 -11.021  -8.954  1.00 62.52           C  
ANISOU  607  C   PRO A 749     7596   7888   8270    428   -319   -769       C  
ATOM    608  O   PRO A 749     -17.930 -10.794  -8.131  1.00 61.08           O  
ANISOU  608  O   PRO A 749     7392   7707   8107    445   -345   -787       O  
ATOM    609  CB  PRO A 749     -19.535 -13.283  -8.033  1.00 69.71           C  
ANISOU  609  CB  PRO A 749     8577   8733   9177    473   -391   -748       C  
ATOM    610  CG  PRO A 749     -18.333 -14.109  -7.691  1.00 71.00           C  
ANISOU  610  CG  PRO A 749     8720   8886   9371    516   -431   -788       C  
ATOM    611  CD  PRO A 749     -17.408 -14.135  -8.889  1.00 70.24           C  
ANISOU  611  CD  PRO A 749     8572   8818   9297    523   -407   -838       C  
ATOM    612  N   PRO A 750     -19.500 -10.041  -9.587  1.00 59.88           N  
ANISOU  612  N   PRO A 750     7262   7572   7917    390   -275   -746       N  
ATOM    613  CA  PRO A 750     -19.201  -8.623  -9.344  1.00 58.86           C  
ANISOU  613  CA  PRO A 750     7107   7464   7792    365   -253   -742       C  
ATOM    614  C   PRO A 750     -19.298  -8.248  -7.879  1.00 55.72           C  
ANISOU  614  C   PRO A 750     6727   7051   7393    371   -287   -726       C  
ATOM    615  O   PRO A 750     -20.301  -8.558  -7.230  1.00 61.39           O  
ANISOU  615  O   PRO A 750     7491   7747   8086    371   -303   -692       O  
ATOM    616  CB  PRO A 750     -20.284  -7.858 -10.122  1.00 59.65           C  
ANISOU  616  CB  PRO A 750     7224   7576   7866    327   -210   -708       C  
ATOM    617  CG  PRO A 750     -21.075  -8.856 -10.881  1.00 57.73           C  
ANISOU  617  CG  PRO A 750     7010   7322   7605    332   -207   -700       C  
ATOM    618  CD  PRO A 750     -20.644 -10.238 -10.499  1.00 58.30           C  
ANISOU  618  CD  PRO A 750     7090   7371   7691    370   -249   -722       C  
ATOM    619  N   LEU A 751     -18.285  -7.543  -7.390  1.00 57.94           N  
ANISOU  619  N   LEU A 751     6970   7344   7699    376   -295   -752       N  
ATOM    620  CA  LEU A 751     -18.275  -7.061  -6.018  1.00 57.36           C  
ANISOU  620  CA  LEU A 751     6909   7261   7623    383   -328   -744       C  
ATOM    621  C   LEU A 751     -19.283  -5.947  -5.832  1.00 55.90           C  
ANISOU  621  C   LEU A 751     6745   7080   7416    349   -304   -708       C  
ATOM    622  O   LEU A 751     -19.373  -5.027  -6.651  1.00 51.60           O  
ANISOU  622  O   LEU A 751     6179   6551   6877    317   -262   -704       O  
ATOM    623  CB  LEU A 751     -16.875  -6.565  -5.591  1.00 59.70           C  
ANISOU  623  CB  LEU A 751     7154   7570   7958    397   -346   -787       C  
ATOM    624  N   LEU A 752     -20.067  -6.049  -4.762  1.00 56.41           N  
ANISOU  624  N   LEU A 752     6852   7127   7453    356   -329   -679       N  
ATOM    625  CA  LEU A 752     -21.024  -5.003  -4.433  1.00 56.19           C  
ANISOU  625  CA  LEU A 752     6844   7102   7404    329   -310   -649       C  
ATOM    626  C   LEU A 752     -20.320  -3.924  -3.639  1.00 60.10           C  
ANISOU  626  C   LEU A 752     7312   7606   7918    329   -325   -670       C  
ATOM    627  O   LEU A 752     -20.347  -3.957  -2.405  1.00 64.47           O  
ANISOU  627  O   LEU A 752     7885   8152   8457    351   -361   -669       O  
ATOM    628  CB  LEU A 752     -22.243  -5.599  -3.703  1.00 54.79           C  
ANISOU  628  CB  LEU A 752     6723   6907   7188    335   -325   -608       C  
ATOM    629  CG  LEU A 752     -23.015  -6.568  -4.598  1.00 55.32           C  
ANISOU  629  CG  LEU A 752     6813   6962   7244    328   -308   -588       C  
ATOM    630  CD1 LEU A 752     -24.119  -7.273  -3.830  1.00 55.11           C  
ANISOU  630  CD1 LEU A 752     6838   6914   7187    334   -324   -549       C  
ATOM    631  CD2 LEU A 752     -23.585  -5.827  -5.814  1.00 56.91           C  
ANISOU  631  CD2 LEU A 752     7002   7177   7442    292   -261   -578       C  
ATOM    632  N   ASN A 753     -19.702  -2.975  -4.358  1.00 56.09           N  
ANISOU  632  N   ASN A 753     6759   7114   7441    306   -296   -690       N  
ATOM    633  CA  ASN A 753     -18.719  -2.091  -3.755  1.00 55.66           C  
ANISOU  633  CA  ASN A 753     6665   7065   7419    309   -313   -723       C  
ATOM    634  C   ASN A 753     -18.919  -0.598  -4.034  1.00 53.99           C  
ANISOU  634  C   ASN A 753     6432   6859   7222    272   -281   -716       C  
ATOM    635  O   ASN A 753     -18.029   0.194  -3.771  1.00 51.98           O  
ANISOU  635  O   ASN A 753     6137   6609   7005    268   -288   -746       O  
ATOM    636  CB  ASN A 753     -17.321  -2.526  -4.174  1.00 57.41           C  
ANISOU  636  CB  ASN A 753     6837   7296   7682    325   -320   -766       C  
ATOM    637  CG  ASN A 753     -16.978  -2.138  -5.610  1.00 62.11           C  
ANISOU  637  CG  ASN A 753     7393   7908   8300    296   -268   -772       C  
ATOM    638  OD1 ASN A 753     -17.846  -1.854  -6.439  1.00 62.90           O  
ANISOU  638  OD1 ASN A 753     7510   8010   8378    268   -228   -740       O  
ATOM    639  ND2 ASN A 753     -15.693  -2.124  -5.898  1.00 63.48           N  
ANISOU  639  ND2 ASN A 753     7512   8093   8516    303   -268   -812       N  
ATOM    640  N   ASN A 754     -20.092  -0.225  -4.535  1.00 51.97           N  
ANISOU  640  N   ASN A 754     6206   6602   6940    245   -248   -678       N  
ATOM    641  CA  ASN A 754     -20.428   1.172  -4.755  1.00 52.32           C  
ANISOU  641  CA  ASN A 754     6237   6646   6994    212   -221   -666       C  
ATOM    642  C   ASN A 754     -21.930   1.362  -4.653  1.00 55.62           C  
ANISOU  642  C   ASN A 754     6704   7057   7372    199   -209   -624       C  
ATOM    643  O   ASN A 754     -22.700   0.391  -4.685  1.00 55.11           O  
ANISOU  643  O   ASN A 754     6677   6989   7274    210   -213   -602       O  
ATOM    644  CB  ASN A 754     -19.893   1.677  -6.090  1.00 56.46           C  
ANISOU  644  CB  ASN A 754     6723   7183   7549    183   -176   -670       C  
ATOM    645  CG  ASN A 754     -20.539   0.996  -7.280  1.00 60.36           C  
ANISOU  645  CG  ASN A 754     7236   7683   8014    175   -142   -644       C  
ATOM    646  OD1 ASN A 754     -21.611   1.395  -7.734  1.00 55.29           O  
ANISOU  646  OD1 ASN A 754     6621   7039   7348    154   -118   -610       O  
ATOM    647  ND2 ASN A 754     -19.891  -0.063  -7.777  1.00 61.52           N  
ANISOU  647  ND2 ASN A 754     7370   7839   8167    194   -144   -664       N  
ATOM    648  N   ALA A 755     -22.339   2.609  -4.478  1.00 56.28           N  
ANISOU  648  N   ALA A 755     6784   7137   7461    177   -198   -615       N  
ATOM    649  CA  ALA A 755     -23.733   2.938  -4.225  1.00 59.12           C  
ANISOU  649  CA  ALA A 755     7185   7490   7786    168   -190   -581       C  
ATOM    650  C   ALA A 755     -24.619   2.550  -5.400  1.00 58.78           C  
ANISOU  650  C   ALA A 755     7162   7451   7722    150   -155   -548       C  
ATOM    651  O   ALA A 755     -25.708   2.009  -5.222  1.00 61.51           O  
ANISOU  651  O   ALA A 755     7546   7792   8033    155   -157   -522       O  
ATOM    652  CB  ALA A 755     -23.873   4.421  -3.908  1.00 59.54           C  
ANISOU  652  CB  ALA A 755     7225   7537   7859    149   -185   -583       C  
ATOM    653  N   ASP A 756     -24.166   2.817  -6.614  1.00 63.62           N  
ANISOU  653  N   ASP A 756     7747   8071   8354    130   -122   -549       N  
ATOM    654  CA  ASP A 756     -24.984   2.464  -7.768  1.00 62.97           C  
ANISOU  654  CA  ASP A 756     7684   7993   8248    117    -91   -521       C  
ATOM    655  C   ASP A 756     -25.215   0.960  -7.918  1.00 58.81           C  
ANISOU  655  C   ASP A 756     7180   7467   7698    138   -103   -520       C  
ATOM    656  O   ASP A 756     -26.289   0.558  -8.298  1.00 62.20           O  
ANISOU  656  O   ASP A 756     7640   7894   8100    133    -95   -495       O  
ATOM    657  CB  ASP A 756     -24.447   2.999  -9.065  1.00 65.71           C  
ANISOU  657  CB  ASP A 756     8001   8352   8614     94    -52   -520       C  
ATOM    658  CG  ASP A 756     -25.556   3.137 -10.111  1.00 70.76           C  
ANISOU  658  CG  ASP A 756     8665   8995   9225     76    -21   -486       C  
ATOM    659  OD1 ASP A 756     -25.690   2.265 -11.023  1.00 66.95           O  
ANISOU  659  OD1 ASP A 756     8191   8524   8724     81     -9   -483       O  
ATOM    660  OD2 ASP A 756     -26.346   4.094  -9.952  1.00 68.55           O  
ANISOU  660  OD2 ASP A 756     8399   8707   8941     60    -15   -464       O  
ATOM    661  N   SER A 757     -24.201   0.144  -7.675  1.00 53.35           N  
ANISOU  661  N   SER A 757     6472   6778   7021    161   -124   -549       N  
ATOM    662  CA  SER A 757     -24.368  -1.312  -7.681  1.00 50.45           C  
ANISOU  662  CA  SER A 757     6126   6406   6637    185   -142   -550       C  
ATOM    663  C   SER A 757     -25.385  -1.794  -6.658  1.00 46.99           C  
ANISOU  663  C   SER A 757     5732   5952   6170    196   -167   -527       C  
ATOM    664  O   SER A 757     -26.119  -2.744  -6.907  1.00 46.57           O  
ANISOU  664  O   SER A 757     5707   5891   6098    201   -169   -510       O  
ATOM    665  CB  SER A 757     -23.058  -2.020  -7.398  1.00 51.05           C  
ANISOU  665  CB  SER A 757     6176   6483   6736    212   -167   -587       C  
ATOM    666  OG  SER A 757     -22.157  -1.681  -8.410  1.00 57.35           O  
ANISOU  666  OG  SER A 757     6932   7298   7560    201   -139   -608       O  
ATOM    667  N   VAL A 758     -25.346  -1.194  -5.483  1.00 42.13           N  
ANISOU  667  N   VAL A 758     5121   5333   5555    202   -188   -528       N  
ATOM    668  CA  VAL A 758     -26.230  -1.585  -4.422  1.00 41.54           C  
ANISOU  668  CA  VAL A 758     5085   5247   5452    215   -209   -506       C  
ATOM    669  C   VAL A 758     -27.650  -1.222  -4.828  1.00 42.08           C  
ANISOU  669  C   VAL A 758     5177   5313   5497    191   -183   -471       C  
ATOM    670  O   VAL A 758     -28.570  -2.040  -4.756  1.00 39.03           O  
ANISOU  670  O   VAL A 758     4822   4918   5089    193   -185   -447       O  
ATOM    671  CB  VAL A 758     -25.862  -0.880  -3.115  1.00 40.53           C  
ANISOU  671  CB  VAL A 758     4954   5120   5324    228   -235   -520       C  
ATOM    672  CG1 VAL A 758     -26.979  -1.049  -2.100  1.00 42.33           C  
ANISOU  672  CG1 VAL A 758     5224   5342   5516    236   -246   -491       C  
ATOM    673  CG2 VAL A 758     -24.574  -1.464  -2.597  1.00 42.11           C  
ANISOU  673  CG2 VAL A 758     5136   5321   5543    258   -270   -553       C  
ATOM    674  N   GLN A 759     -27.786   0.011  -5.297  1.00 41.06           N  
ANISOU  674  N   GLN A 759     5031   5191   5378    167   -159   -470       N  
ATOM    675  CA  GLN A 759     -29.042   0.551  -5.766  1.00 44.02           C  
ANISOU  675  CA  GLN A 759     5424   5566   5737    145   -134   -440       C  
ATOM    676  C   GLN A 759     -29.668  -0.363  -6.861  1.00 38.95           C  
ANISOU  676  C   GLN A 759     4795   4922   5082    138   -118   -425       C  
ATOM    677  O   GLN A 759     -30.855  -0.652  -6.831  1.00 40.08           O  
ANISOU  677  O   GLN A 759     4964   5059   5205    133   -115   -400       O  
ATOM    678  CB  GLN A 759     -28.790   1.968  -6.275  1.00 47.64           C  
ANISOU  678  CB  GLN A 759     5856   6029   6215    122   -112   -445       C  
ATOM    679  CG  GLN A 759     -29.836   3.046  -6.077  1.00 52.46           C  
ANISOU  679  CG  GLN A 759     6480   6637   6818    106   -101   -424       C  
ATOM    680  CD  GLN A 759     -29.181   4.447  -6.211  1.00 62.98           C  
ANISOU  680  CD  GLN A 759     7782   7969   8181     90    -91   -437       C  
ATOM    681  OE1 GLN A 759     -28.238   4.753  -5.461  1.00 69.03           O  
ANISOU  681  OE1 GLN A 759     8527   8733   8968    100   -111   -464       O  
ATOM    682  NE2 GLN A 759     -29.652   5.286  -7.158  1.00 61.24           N  
ANISOU  682  NE2 GLN A 759     7556   7746   7965     66    -63   -419       N  
ATOM    683  N   ALA A 760     -28.871  -0.798  -7.816  1.00 34.99           N  
ANISOU  683  N   ALA A 760     4273   4427   4594    140   -110   -442       N  
ATOM    684  CA  ALA A 760     -29.341  -1.672  -8.862  1.00 37.89           C  
ANISOU  684  CA  ALA A 760     4651   4795   4950    138    -99   -435       C  
ATOM    685  C   ALA A 760     -29.899  -2.980  -8.264  1.00 38.15           C  
ANISOU  685  C   ALA A 760     4713   4811   4971    155   -123   -426       C  
ATOM    686  O   ALA A 760     -30.872  -3.504  -8.793  1.00 38.23           O  
ANISOU  686  O   ALA A 760     4742   4815   4968    148   -117   -409       O  
ATOM    687  CB  ALA A 760     -28.226  -1.982  -9.857  1.00 39.18           C  
ANISOU  687  CB  ALA A 760     4786   4972   5130    143    -88   -461       C  
ATOM    688  N   LYS A 761     -29.251  -3.509  -7.213  1.00 35.10           N  
ANISOU  688  N   LYS A 761     4330   4416   4591    177   -152   -437       N  
ATOM    689  CA  LYS A 761     -29.709  -4.737  -6.559  1.00 34.30           C  
ANISOU  689  CA  LYS A 761     4257   4295   4479    194   -176   -424       C  
ATOM    690  C   LYS A 761     -30.976  -4.523  -5.774  1.00 32.49           C  
ANISOU  690  C   LYS A 761     4057   4059   4228    185   -174   -391       C  
ATOM    691  O   LYS A 761     -31.849  -5.393  -5.776  1.00 29.65           O  
ANISOU  691  O   LYS A 761     3720   3684   3860    183   -177   -370       O  
ATOM    692  CB  LYS A 761     -28.630  -5.414  -5.697  1.00 35.73           C  
ANISOU  692  CB  LYS A 761     4435   4470   4671    224   -209   -444       C  
ATOM    693  CG  LYS A 761     -27.447  -5.925  -6.495  1.00 36.76           C  
ANISOU  693  CG  LYS A 761     4537   4605   4824    237   -212   -479       C  
ATOM    694  CD  LYS A 761     -27.868  -6.983  -7.493  1.00 41.33           C  
ANISOU  694  CD  LYS A 761     5126   5173   5403    237   -207   -478       C  
ATOM    695  CE  LYS A 761     -26.739  -7.510  -8.354  1.00 43.34           C  
ANISOU  695  CE  LYS A 761     5353   5437   5679    252   -208   -515       C  
ATOM    696  NZ  LYS A 761     -27.266  -7.760  -9.723  1.00 47.04           N  
ANISOU  696  NZ  LYS A 761     5821   5912   6142    239   -184   -516       N  
ATOM    697  N   VAL A 762     -31.116  -3.357  -5.157  1.00 32.69           N  
ANISOU  697  N   VAL A 762     4079   4095   4248    177   -168   -387       N  
ATOM    698  CA  VAL A 762     -32.353  -3.026  -4.461  1.00 33.02           C  
ANISOU  698  CA  VAL A 762     4144   4134   4268    168   -162   -358       C  
ATOM    699  C   VAL A 762     -33.514  -2.962  -5.446  1.00 32.49           C  
ANISOU  699  C   VAL A 762     4081   4065   4196    145   -138   -339       C  
ATOM    700  O   VAL A 762     -34.600  -3.513  -5.217  1.00 33.01           O  
ANISOU  700  O   VAL A 762     4170   4122   4252    140   -136   -314       O  
ATOM    701  CB  VAL A 762     -32.257  -1.670  -3.733  1.00 36.38           C  
ANISOU  701  CB  VAL A 762     4560   4572   4690    166   -160   -363       C  
ATOM    702  CG1 VAL A 762     -33.609  -1.262  -3.155  1.00 36.62           C  
ANISOU  702  CG1 VAL A 762     4612   4604   4699    157   -149   -336       C  
ATOM    703  CG2 VAL A 762     -31.228  -1.737  -2.628  1.00 37.90           C  
ANISOU  703  CG2 VAL A 762     4750   4766   4883    192   -189   -383       C  
ATOM    704  N   GLU A 763     -33.276  -2.283  -6.552  1.00 36.78           N  
ANISOU  704  N   GLU A 763     4605   4620   4751    131   -119   -350       N  
ATOM    705  CA  GLU A 763     -34.301  -2.151  -7.595  1.00 41.51           C  
ANISOU  705  CA  GLU A 763     5208   5220   5345    112    -99   -335       C  
ATOM    706  C   GLU A 763     -34.610  -3.525  -8.169  1.00 36.17           C  
ANISOU  706  C   GLU A 763     4542   4531   4668    116   -106   -333       C  
ATOM    707  O   GLU A 763     -35.776  -3.841  -8.342  1.00 31.29           O  
ANISOU  707  O   GLU A 763     3939   3905   4044    106   -102   -314       O  
ATOM    708  CB  GLU A 763     -33.982  -1.069  -8.634  1.00 46.33           C  
ANISOU  708  CB  GLU A 763     5797   5845   5961     97    -77   -343       C  
ATOM    709  CG  GLU A 763     -34.251   0.307  -8.029  1.00 52.64           C  
ANISOU  709  CG  GLU A 763     6592   6648   6760     88    -70   -336       C  
ATOM    710  CD  GLU A 763     -33.870   1.454  -8.941  1.00 58.17           C  
ANISOU  710  CD  GLU A 763     7272   7358   7472     72    -50   -340       C  
ATOM    711  OE1 GLU A 763     -33.981   1.281 -10.173  1.00 60.27           O  
ANISOU  711  OE1 GLU A 763     7536   7630   7734     65    -35   -337       O  
ATOM    712  OE2 GLU A 763     -33.465   2.517  -8.409  1.00 57.94           O  
ANISOU  712  OE2 GLU A 763     7231   7329   7454     69    -49   -345       O  
ATOM    713  N   MET A 764     -33.586  -4.353  -8.360  1.00 32.05           N  
ANISOU  713  N   MET A 764     4014   4006   4158    132   -120   -355       N  
ATOM    714  CA  MET A 764     -33.804  -5.725  -8.719  1.00 33.90           C  
ANISOU  714  CA  MET A 764     4260   4224   4398    140   -132   -356       C  
ATOM    715  C   MET A 764     -34.729  -6.432  -7.736  1.00 30.33           C  
ANISOU  715  C   MET A 764     3834   3749   3940    141   -145   -329       C  
ATOM    716  O   MET A 764     -35.722  -7.003  -8.148  1.00 28.18           O  
ANISOU  716  O   MET A 764     3573   3465   3668    131   -143   -316       O  
ATOM    717  CB  MET A 764     -32.518  -6.509  -8.816  1.00 36.04           C  
ANISOU  717  CB  MET A 764     4520   4491   4683    163   -150   -385       C  
ATOM    718  CG  MET A 764     -32.784  -7.972  -9.155  1.00 37.47           C  
ANISOU  718  CG  MET A 764     4715   4650   4873    173   -166   -387       C  
ATOM    719  SD  MET A 764     -31.312  -8.944  -8.888  1.00 45.01           S  
ANISOU  719  SD  MET A 764     5661   5595   5847    205   -194   -418       S  
ATOM    720  CE  MET A 764     -31.494  -9.216  -7.103  1.00 46.12           C  
ANISOU  720  CE  MET A 764     5827   5716   5981    216   -218   -390       C  
ATOM    721  N   LEU A 765     -34.424  -6.359  -6.443  1.00 29.45           N  
ANISOU  721  N   LEU A 765     3732   3636   3823    153   -158   -321       N  
ATOM    722  CA  LEU A 765     -35.280  -6.991  -5.422  1.00 32.04           C  
ANISOU  722  CA  LEU A 765     4087   3946   4142    155   -165   -290       C  
ATOM    723  C   LEU A 765     -36.727  -6.456  -5.492  1.00 33.18           C  
ANISOU  723  C   LEU A 765     4237   4094   4276    131   -144   -264       C  
ATOM    724  O   LEU A 765     -37.683  -7.227  -5.359  1.00 32.09           O  
ANISOU  724  O   LEU A 765     4114   3938   4140    123   -143   -242       O  
ATOM    725  CB  LEU A 765     -34.698  -6.801  -4.012  1.00 32.50           C  
ANISOU  725  CB  LEU A 765     4155   4008   4187    174   -181   -285       C  
ATOM    726  CG  LEU A 765     -33.409  -7.535  -3.678  1.00 34.39           C  
ANISOU  726  CG  LEU A 765     4393   4238   4435    201   -209   -305       C  
ATOM    727  CD1 LEU A 765     -32.984  -7.268  -2.225  1.00 35.86           C  
ANISOU  727  CD1 LEU A 765     4591   4430   4603    222   -226   -299       C  
ATOM    728  CD2 LEU A 765     -33.603  -9.018  -3.905  1.00 36.94           C  
ANISOU  728  CD2 LEU A 765     4732   4532   4771    208   -223   -296       C  
ATOM    729  N   ASP A 766     -36.897  -5.151  -5.691  1.00 31.82           N  
ANISOU  729  N   ASP A 766     4052   3942   4096    120   -127   -269       N  
ATOM    730  CA  ASP A 766     -38.258  -4.588  -5.792  1.00 33.93           C  
ANISOU  730  CA  ASP A 766     4323   4214   4356    100   -108   -248       C  
ATOM    731  C   ASP A 766     -39.007  -5.228  -6.954  1.00 32.93           C  
ANISOU  731  C   ASP A 766     4194   4076   4240     87   -103   -246       C  
ATOM    732  O   ASP A 766     -40.183  -5.598  -6.828  1.00 31.44           O  
ANISOU  732  O   ASP A 766     4015   3878   4054     75    -98   -225       O  
ATOM    733  CB  ASP A 766     -38.224  -3.063  -6.031  1.00 37.05           C  
ANISOU  733  CB  ASP A 766     4702   4629   4746     92    -93   -256       C  
ATOM    734  CG  ASP A 766     -37.530  -2.274  -4.904  1.00 41.94           C  
ANISOU  734  CG  ASP A 766     5320   5260   5357    105    -99   -264       C  
ATOM    735  OD1 ASP A 766     -37.390  -2.769  -3.745  1.00 40.56           O  
ANISOU  735  OD1 ASP A 766     5159   5080   5171    120   -112   -255       O  
ATOM    736  OD2 ASP A 766     -37.118  -1.133  -5.199  1.00 40.49           O  
ANISOU  736  OD2 ASP A 766     5119   5087   5178    100    -92   -278       O  
ATOM    737  N   ASN A 767     -38.322  -5.328  -8.098  1.00 31.31           N  
ANISOU  737  N   ASN A 767     3976   3875   4044     89   -105   -270       N  
ATOM    738  CA  ASN A 767     -38.911  -5.846  -9.317  1.00 29.57           C  
ANISOU  738  CA  ASN A 767     3754   3650   3831     80   -104   -276       C  
ATOM    739  C   ASN A 767     -39.188  -7.343  -9.139  1.00 31.82           C  
ANISOU  739  C   ASN A 767     4052   3907   4131     85   -121   -271       C  
ATOM    740  O   ASN A 767     -40.245  -7.829  -9.537  1.00 29.10           O  
ANISOU  740  O   ASN A 767     3712   3550   3796     72   -121   -262       O  
ATOM    741  CB  ASN A 767     -38.001  -5.555 -10.507  1.00 30.29           C  
ANISOU  741  CB  ASN A 767     3830   3758   3922     85   -100   -303       C  
ATOM    742  CG  ASN A 767     -38.637  -5.856 -11.867  1.00 33.10           C  
ANISOU  742  CG  ASN A 767     4184   4115   4278     78    -97   -311       C  
ATOM    743  OD1 ASN A 767     -39.885  -5.893 -12.046  1.00 32.05           O  
ANISOU  743  OD1 ASN A 767     4056   3975   4145     65    -96   -297       O  
ATOM    744  ND2 ASN A 767     -37.765  -6.012 -12.865  1.00 34.68           N  
ANISOU  744  ND2 ASN A 767     4373   4327   4476     88    -96   -337       N  
ATOM    745  N   LEU A 768     -38.290  -8.046  -8.453  1.00 34.02           N  
ANISOU  745  N   LEU A 768     4337   4173   4415    102   -137   -275       N  
ATOM    746  CA  LEU A 768     -38.511  -9.459  -8.141  1.00 37.33           C  
ANISOU  746  CA  LEU A 768     4772   4561   4851    107   -156   -266       C  
ATOM    747  C   LEU A 768     -39.752  -9.670  -7.322  1.00 35.98           C  
ANISOU  747  C   LEU A 768     4615   4375   4680     92   -149   -230       C  
ATOM    748  O   LEU A 768     -40.529 -10.573  -7.591  1.00 36.69           O  
ANISOU  748  O   LEU A 768     4711   4441   4789     82   -154   -221       O  
ATOM    749  CB  LEU A 768     -37.315 -10.058  -7.377  1.00 39.10           C  
ANISOU  749  CB  LEU A 768     5003   4775   5079    132   -176   -273       C  
ATOM    750  CG  LEU A 768     -36.075 -10.355  -8.190  1.00 44.19           C  
ANISOU  750  CG  LEU A 768     5632   5424   5733    150   -188   -312       C  
ATOM    751  CD1 LEU A 768     -35.034 -11.095  -7.337  1.00 45.12           C  
ANISOU  751  CD1 LEU A 768     5758   5527   5858    176   -213   -317       C  
ATOM    752  CD2 LEU A 768     -36.430 -11.153  -9.435  1.00 47.86           C  
ANISOU  752  CD2 LEU A 768     6094   5877   6214    146   -193   -330       C  
ATOM    753  N   LEU A 769     -39.919  -8.836  -6.304  1.00 38.76           N  
ANISOU  753  N   LEU A 769     4972   4743   5013     91   -137   -211       N  
ATOM    754  CA  LEU A 769     -41.060  -8.936  -5.409  1.00 40.64           C  
ANISOU  754  CA  LEU A 769     5222   4974   5246     78   -125   -175       C  
ATOM    755  C   LEU A 769     -42.368  -8.840  -6.205  1.00 37.91           C  
ANISOU  755  C   LEU A 769     4865   4625   4912     54   -112   -170       C  
ATOM    756  O   LEU A 769     -43.241  -9.682  -6.074  1.00 36.33           O  
ANISOU  756  O   LEU A 769     4671   4402   4730     42   -111   -150       O  
ATOM    757  CB  LEU A 769     -40.986  -7.873  -4.304  1.00 46.16           C  
ANISOU  757  CB  LEU A 769     5924   5696   5917     84   -113   -164       C  
ATOM    758  CG  LEU A 769     -40.733  -8.323  -2.841  1.00 50.30           C  
ANISOU  758  CG  LEU A 769     6472   6215   6426     99   -120   -140       C  
ATOM    759  CD1 LEU A 769     -40.992  -7.093  -1.964  1.00 50.75           C  
ANISOU  759  CD1 LEU A 769     6528   6301   6454    102   -104   -133       C  
ATOM    760  CD2 LEU A 769     -41.552  -9.511  -2.343  1.00 51.80           C  
ANISOU  760  CD2 LEU A 769     6679   6377   6625     91   -118   -104       C  
ATOM    761  N   ASP A 770     -42.489  -7.846  -7.077  1.00 35.20           N  
ANISOU  761  N   ASP A 770     4507   4305   4564     48   -102   -188       N  
ATOM    762  CA  ASP A 770     -43.721  -7.679  -7.855  1.00 32.76           C  
ANISOU  762  CA  ASP A 770     4188   3995   4265     29    -94   -186       C  
ATOM    763  C   ASP A 770     -43.885  -8.779  -8.903  1.00 31.88           C  
ANISOU  763  C   ASP A 770     4073   3861   4177     26   -110   -201       C  
ATOM    764  O   ASP A 770     -45.022  -9.170  -9.250  1.00 29.56           O  
ANISOU  764  O   ASP A 770     3774   3555   3902     10   -110   -194       O  
ATOM    765  CB  ASP A 770     -43.779  -6.285  -8.500  1.00 34.80           C  
ANISOU  765  CB  ASP A 770     4432   4282   4508     26    -82   -199       C  
ATOM    766  CG  ASP A 770     -44.269  -5.178  -7.521  1.00 38.50           C  
ANISOU  766  CG  ASP A 770     4900   4767   4960     23    -64   -181       C  
ATOM    767  OD1 ASP A 770     -45.145  -5.443  -6.667  1.00 46.59           O  
ANISOU  767  OD1 ASP A 770     5930   5786   5987     15    -56   -157       O  
ATOM    768  OD2 ASP A 770     -43.826  -4.012  -7.656  1.00 40.03           O  
ANISOU  768  OD2 ASP A 770     5088   4982   5142     27    -58   -191       O  
ATOM    769  N   ILE A 771     -42.775  -9.261  -9.441  1.00 31.05           N  
ANISOU  769  N   ILE A 771     3970   3753   4075     42   -125   -226       N  
ATOM    770  CA  ILE A 771     -42.828 -10.433 -10.319  1.00 32.05           C  
ANISOU  770  CA  ILE A 771     4096   3856   4226     43   -145   -245       C  
ATOM    771  C   ILE A 771     -43.387 -11.648  -9.567  1.00 33.92           C  
ANISOU  771  C   ILE A 771     4344   4054   4489     36   -154   -221       C  
ATOM    772  O   ILE A 771     -44.249 -12.360 -10.081  1.00 37.06           O  
ANISOU  772  O   ILE A 771     4738   4431   4913     23   -163   -223       O  
ATOM    773  CB  ILE A 771     -41.458 -10.728 -10.965  1.00 33.61           C  
ANISOU  773  CB  ILE A 771     4291   4059   4420     65   -158   -278       C  
ATOM    774  CG1 ILE A 771     -41.190  -9.716 -12.075  1.00 34.07           C  
ANISOU  774  CG1 ILE A 771     4335   4151   4458     67   -147   -300       C  
ATOM    775  CG2 ILE A 771     -41.422 -12.122 -11.563  1.00 34.45           C  
ANISOU  775  CG2 ILE A 771     4400   4135   4554     72   -182   -297       C  
ATOM    776  CD1 ILE A 771     -39.728  -9.567 -12.465  1.00 35.98           C  
ANISOU  776  CD1 ILE A 771     4570   4410   4690     87   -148   -327       C  
ATOM    777  N   GLU A 772     -42.918 -11.887  -8.351  1.00 35.17           N  
ANISOU  777  N   GLU A 772     4517   4204   4641     44   -154   -199       N  
ATOM    778  CA  GLU A 772     -43.465 -12.957  -7.529  1.00 37.21           C  
ANISOU  778  CA  GLU A 772     4790   4427   4922     36   -159   -168       C  
ATOM    779  C   GLU A 772     -44.962 -12.777  -7.356  1.00 34.90           C  
ANISOU  779  C   GLU A 772     4490   4132   4640      9   -140   -142       C  
ATOM    780  O   GLU A 772     -45.707 -13.748  -7.425  1.00 35.09           O  
ANISOU  780  O   GLU A 772     4513   4122   4696     -6   -146   -131       O  
ATOM    781  CB  GLU A 772     -42.754 -12.974  -6.177  1.00 43.70           C  
ANISOU  781  CB  GLU A 772     5630   5249   5724     52   -158   -144       C  
ATOM    782  CG  GLU A 772     -43.408 -13.775  -5.058  1.00 51.88           C  
ANISOU  782  CG  GLU A 772     6685   6257   6771     42   -153    -99       C  
ATOM    783  CD  GLU A 772     -44.415 -12.972  -4.173  1.00 62.30           C  
ANISOU  783  CD  GLU A 772     8004   7598   8069     26   -122    -65       C  
ATOM    784  OE1 GLU A 772     -44.089 -11.875  -3.597  1.00 57.26           O  
ANISOU  784  OE1 GLU A 772     7367   6995   7395     36   -110    -66       O  
ATOM    785  OE2 GLU A 772     -45.560 -13.475  -4.023  1.00 64.17           O  
ANISOU  785  OE2 GLU A 772     8239   7815   8328      3   -110    -39       O  
ATOM    786  N   VAL A 773     -45.412 -11.545  -7.083  1.00 34.18           N  
ANISOU  786  N   VAL A 773     4390   4073   4523      3   -118   -134       N  
ATOM    787  CA  VAL A 773     -46.841 -11.283  -6.905  1.00 32.22           C  
ANISOU  787  CA  VAL A 773     4132   3827   4284    -21    -98   -113       C  
ATOM    788  C   VAL A 773     -47.592 -11.684  -8.160  1.00 33.42           C  
ANISOU  788  C   VAL A 773     4266   3965   4466    -35   -110   -135       C  
ATOM    789  O   VAL A 773     -48.622 -12.354  -8.100  1.00 38.07           O  
ANISOU  789  O   VAL A 773     4849   4530   5087    -54   -108   -120       O  
ATOM    790  CB  VAL A 773     -47.116  -9.811  -6.586  1.00 33.67           C  
ANISOU  790  CB  VAL A 773     4308   4050   4438    -21    -77   -110       C  
ATOM    791  CG1 VAL A 773     -48.608  -9.521  -6.672  1.00 35.22           C  
ANISOU  791  CG1 VAL A 773     4486   4248   4647    -43    -60    -98       C  
ATOM    792  CG2 VAL A 773     -46.572  -9.451  -5.207  1.00 32.28           C  
ANISOU  792  CG2 VAL A 773     4148   3886   4232     -8    -65    -88       C  
ATOM    793  N   ALA A 774     -47.069 -11.285  -9.303  1.00 32.59           N  
ANISOU  793  N   ALA A 774     4154   3876   4353    -24   -123   -171       N  
ATOM    794  CA  ALA A 774     -47.706 -11.579 -10.567  1.00 33.50           C  
ANISOU  794  CA  ALA A 774     4255   3984   4489    -31   -137   -196       C  
ATOM    795  C   ALA A 774     -47.751 -13.088 -10.806  1.00 38.83           C  
ANISOU  795  C   ALA A 774     4934   4616   5204    -34   -160   -203       C  
ATOM    796  O   ALA A 774     -48.779 -13.629 -11.198  1.00 37.51           O  
ANISOU  796  O   ALA A 774     4755   4428   5069    -51   -168   -205       O  
ATOM    797  CB  ALA A 774     -46.966 -10.883 -11.703  1.00 31.62           C  
ANISOU  797  CB  ALA A 774     4014   3775   4227    -15   -144   -231       C  
ATOM    798  N   TYR A 775     -46.631 -13.761 -10.547  1.00 40.61           N  
ANISOU  798  N   TYR A 775     5174   4826   5429    -17   -173   -208       N  
ATOM    799  CA  TYR A 775     -46.551 -15.188 -10.766  1.00 41.46           C  
ANISOU  799  CA  TYR A 775     5287   4890   5575    -16   -198   -217       C  
ATOM    800  C   TYR A 775     -47.502 -15.957  -9.844  1.00 41.63           C  
ANISOU  800  C   TYR A 775     5312   4875   5632    -39   -191   -177       C  
ATOM    801  O   TYR A 775     -48.134 -16.910 -10.279  1.00 42.04           O  
ANISOU  801  O   TYR A 775     5357   4890   5727    -52   -208   -184       O  
ATOM    802  CB  TYR A 775     -45.108 -15.703 -10.617  1.00 42.39           C  
ANISOU  802  CB  TYR A 775     5420   5000   5686     11   -214   -231       C  
ATOM    803  CG  TYR A 775     -44.927 -17.027 -11.282  1.00 41.56           C  
ANISOU  803  CG  TYR A 775     5316   4854   5619     18   -245   -257       C  
ATOM    804  CD1 TYR A 775     -44.872 -17.102 -12.650  1.00 44.40           C  
ANISOU  804  CD1 TYR A 775     5664   5224   5983     26   -262   -304       C  
ATOM    805  CD2 TYR A 775     -44.880 -18.212 -10.558  1.00 44.50           C  
ANISOU  805  CD2 TYR A 775     5703   5180   6027     16   -259   -236       C  
ATOM    806  CE1 TYR A 775     -44.755 -18.308 -13.298  1.00 45.05           C  
ANISOU  806  CE1 TYR A 775     5746   5270   6102     34   -293   -334       C  
ATOM    807  CE2 TYR A 775     -44.751 -19.447 -11.199  1.00 46.59           C  
ANISOU  807  CE2 TYR A 775     5968   5402   6333     22   -291   -263       C  
ATOM    808  CZ  TYR A 775     -44.682 -19.477 -12.577  1.00 46.66           C  
ANISOU  808  CZ  TYR A 775     5962   5422   6344     32   -308   -315       C  
ATOM    809  OH  TYR A 775     -44.539 -20.657 -13.273  1.00 51.36           O  
ANISOU  809  OH  TYR A 775     6557   5980   6979     42   -342   -349       O  
ATOM    810  N   SER A 776     -47.574 -15.561  -8.583  1.00 42.05           N  
ANISOU  810  N   SER A 776     5375   4936   5665    -44   -167   -136       N  
ATOM    811  CA  SER A 776     -48.489 -16.179  -7.632  1.00 43.41           C  
ANISOU  811  CA  SER A 776     5550   5079   5863    -67   -153    -91       C  
ATOM    812  C   SER A 776     -49.938 -16.035  -8.035  1.00 42.81           C  
ANISOU  812  C   SER A 776     5450   5002   5814    -95   -142    -89       C  
ATOM    813  O   SER A 776     -50.710 -16.975  -7.920  1.00 45.71           O  
ANISOU  813  O   SER A 776     5811   5330   6227   -117   -145    -73       O  
ATOM    814  CB  SER A 776     -48.338 -15.541  -6.254  1.00 47.66           C  
ANISOU  814  CB  SER A 776     6103   5640   6363    -63   -125    -51       C  
ATOM    815  OG  SER A 776     -47.092 -15.902  -5.700  1.00 57.93           O  
ANISOU  815  OG  SER A 776     7429   6934   7647    -38   -139    -48       O  
ATOM    816  N   LEU A 777     -50.327 -14.837  -8.446  1.00 43.28           N  
ANISOU  816  N   LEU A 777     5494   5102   5848    -96   -129   -104       N  
ATOM    817  CA  LEU A 777     -51.695 -14.596  -8.842  1.00 39.86           C  
ANISOU  817  CA  LEU A 777     5034   4671   5439   -119   -121   -105       C  
ATOM    818  C   LEU A 777     -52.037 -15.500 -10.000  1.00 41.14           C  
ANISOU  818  C   LEU A 777     5183   4802   5646   -126   -153   -138       C  
ATOM    819  O   LEU A 777     -53.079 -16.147  -9.989  1.00 37.89           O  
ANISOU  819  O   LEU A 777     4755   4362   5281   -150   -153   -128       O  
ATOM    820  CB  LEU A 777     -51.900 -13.153  -9.269  1.00 40.57           C  
ANISOU  820  CB  LEU A 777     5112   4809   5494   -113   -110   -121       C  
ATOM    821  CG  LEU A 777     -52.020 -12.112  -8.164  1.00 39.64           C  
ANISOU  821  CG  LEU A 777     4998   4723   5340   -112    -77    -92       C  
ATOM    822  CD1 LEU A 777     -52.168 -10.738  -8.812  1.00 40.39           C  
ANISOU  822  CD1 LEU A 777     5081   4859   5408   -103    -73   -114       C  
ATOM    823  CD2 LEU A 777     -53.197 -12.384  -7.231  1.00 38.09           C  
ANISOU  823  CD2 LEU A 777     4790   4516   5167   -137    -51    -54       C  
ATOM    824  N   LEU A 778     -51.120 -15.592 -10.951  1.00 40.73           N  
ANISOU  824  N   LEU A 778     5138   4755   5581   -103   -179   -178       N  
ATOM    825  CA  LEU A 778     -51.316 -16.375 -12.159  1.00 46.04           C  
ANISOU  825  CA  LEU A 778     5801   5405   6289   -102   -212   -219       C  
ATOM    826  C   LEU A 778     -51.453 -17.855 -11.868  1.00 46.96           C  
ANISOU  826  C   LEU A 778     5920   5462   6459   -114   -229   -209       C  
ATOM    827  O   LEU A 778     -52.300 -18.528 -12.448  1.00 45.25           O  
ANISOU  827  O   LEU A 778     5686   5217   6290   -130   -248   -226       O  
ATOM    828  CB  LEU A 778     -50.112 -16.156 -13.100  1.00 51.07           C  
ANISOU  828  CB  LEU A 778     6448   6064   6892    -71   -231   -261       C  
ATOM    829  CG  LEU A 778     -50.221 -16.531 -14.577  1.00 55.22           C  
ANISOU  829  CG  LEU A 778     6963   6587   7430    -60   -264   -313       C  
ATOM    830  CD1 LEU A 778     -51.475 -15.941 -15.198  1.00 56.31           C  
ANISOU  830  CD1 LEU A 778     7079   6742   7575    -75   -264   -322       C  
ATOM    831  CD2 LEU A 778     -48.980 -16.034 -15.306  1.00 58.66           C  
ANISOU  831  CD2 LEU A 778     7409   7057   7820    -30   -268   -344       C  
ATOM    832  N   ARG A 779     -50.610 -18.374 -10.979  1.00 47.99           N  
ANISOU  832  N   ARG A 779     6074   5573   6585   -105   -226   -184       N  
ATOM    833  CA  ARG A 779     -50.626 -19.812 -10.682  1.00 51.20           C  
ANISOU  833  CA  ARG A 779     6489   5921   7045   -114   -244   -172       C  
ATOM    834  C   ARG A 779     -51.781 -20.203  -9.727  1.00 51.98           C  
ANISOU  834  C   ARG A 779     6579   5990   7180   -150   -220   -121       C  
ATOM    835  O   ARG A 779     -52.279 -21.330  -9.787  1.00 53.81           O  
ANISOU  835  O   ARG A 779     6805   6169   7472   -168   -236   -116       O  
ATOM    836  CB  ARG A 779     -49.257 -20.268 -10.146  1.00 52.29           C  
ANISOU  836  CB  ARG A 779     6656   6047   7166    -88   -254   -165       C  
ATOM    837  N   GLY A 780     -52.253 -19.261  -8.905  1.00 51.94           N  
ANISOU  837  N   GLY A 780     6572   6020   7144   -160   -182    -85       N  
ATOM    838  CA  GLY A 780     -53.261 -19.564  -7.862  1.00 50.93           C  
ANISOU  838  CA  GLY A 780     6437   5872   7043   -192   -152    -32       C  
ATOM    839  C   GLY A 780     -54.716 -19.354  -8.246  1.00 48.87           C  
ANISOU  839  C   GLY A 780     6138   5612   6817   -222   -141    -36       C  
ATOM    840  O   GLY A 780     -55.040 -19.227  -9.424  1.00 47.51           O  
ANISOU  840  O   GLY A 780     5945   5445   6661   -220   -166    -83       O  
ATOM    841  N   SER A 786     -63.371 -23.070 -16.797  1.00 63.19           N  
ANISOU  841  N   SER A 786     7631   7227   9151   -357   -425   -406       N  
ATOM    842  CA  SER A 786     -64.654 -22.769 -17.410  1.00 69.31           C  
ANISOU  842  CA  SER A 786     8359   8011   9964   -370   -444   -439       C  
ATOM    843  C   SER A 786     -64.626 -21.412 -18.165  1.00 72.04           C  
ANISOU  843  C   SER A 786     8709   8429  10233   -335   -451   -468       C  
ATOM    844  O   SER A 786     -65.041 -21.336 -19.332  1.00 67.21           O  
ANISOU  844  O   SER A 786     8081   7828   9629   -318   -498   -528       O  
ATOM    845  CB  SER A 786     -65.764 -22.786 -16.341  1.00 66.51           C  
ANISOU  845  CB  SER A 786     7967   7640   9665   -417   -399   -386       C  
ATOM    846  N   LYS A 787     -64.118 -20.357 -17.507  1.00 70.34           N  
ANISOU  846  N   LYS A 787     8519   8262   9946   -323   -407   -428       N  
ATOM    847  CA  LYS A 787     -64.028 -19.009 -18.108  1.00 63.91           C  
ANISOU  847  CA  LYS A 787     7712   7512   9058   -291   -409   -447       C  
ATOM    848  C   LYS A 787     -62.761 -18.839 -18.983  1.00 58.80           C  
ANISOU  848  C   LYS A 787     7107   6889   8344   -247   -435   -480       C  
ATOM    849  O   LYS A 787     -61.771 -19.538 -18.779  1.00 56.78           O  
ANISOU  849  O   LYS A 787     6880   6610   8084   -241   -436   -474       O  
ATOM    850  CB  LYS A 787     -64.064 -17.939 -17.007  1.00 61.55           C  
ANISOU  850  CB  LYS A 787     7419   7252   8716   -297   -351   -391       C  
ATOM    851  N   ASP A 788     -62.789 -17.916 -19.950  1.00 56.10           N  
ANISOU  851  N   ASP A 788     6769   6596   7952   -217   -455   -514       N  
ATOM    852  CA  ASP A 788     -61.573 -17.537 -20.690  1.00 53.65           C  
ANISOU  852  CA  ASP A 788     6498   6319   7568   -177   -468   -537       C  
ATOM    853  C   ASP A 788     -60.490 -17.145 -19.660  1.00 51.25           C  
ANISOU  853  C   ASP A 788     6227   6028   7218   -175   -421   -486       C  
ATOM    854  O   ASP A 788     -60.772 -16.358 -18.755  1.00 47.59           O  
ANISOU  854  O   ASP A 788     5759   5582   6739   -188   -380   -442       O  
ATOM    855  CB  ASP A 788     -61.845 -16.341 -21.621  1.00 53.19           C  
ANISOU  855  CB  ASP A 788     6440   6315   7455   -149   -482   -561       C  
ATOM    856  CG  ASP A 788     -60.681 -16.050 -22.574  1.00 54.89           C  
ANISOU  856  CG  ASP A 788     6692   6564   7599   -108   -498   -590       C  
ATOM    857  OD1 ASP A 788     -60.900 -15.501 -23.689  1.00 58.81           O  
ANISOU  857  OD1 ASP A 788     7190   7094   8061    -82   -527   -625       O  
ATOM    858  OD2 ASP A 788     -59.533 -16.360 -22.219  1.00 53.97           O  
ANISOU  858  OD2 ASP A 788     6604   6442   7460   -101   -481   -576       O  
ATOM    859  N   PRO A 789     -59.264 -17.701 -19.783  1.00 47.40           N  
ANISOU  859  N   PRO A 789     5770   5530   6708   -156   -428   -495       N  
ATOM    860  CA  PRO A 789     -58.198 -17.371 -18.833  1.00 44.08           C  
ANISOU  860  CA  PRO A 789     5380   5121   6247   -152   -388   -451       C  
ATOM    861  C   PRO A 789     -57.891 -15.872 -18.696  1.00 41.33           C  
ANISOU  861  C   PRO A 789     5044   4830   5829   -137   -359   -431       C  
ATOM    862  O   PRO A 789     -57.592 -15.431 -17.618  1.00 38.56           O  
ANISOU  862  O   PRO A 789     4704   4487   5462   -145   -320   -386       O  
ATOM    863  CB  PRO A 789     -56.987 -18.122 -19.399  1.00 46.08           C  
ANISOU  863  CB  PRO A 789     5660   5363   6487   -126   -413   -482       C  
ATOM    864  CG  PRO A 789     -57.574 -19.293 -20.099  1.00 47.57           C  
ANISOU  864  CG  PRO A 789     5829   5507   6738   -133   -457   -525       C  
ATOM    865  CD  PRO A 789     -58.858 -18.790 -20.702  1.00 48.45           C  
ANISOU  865  CD  PRO A 789     5909   5635   6864   -141   -473   -546       C  
ATOM    866  N   ILE A 790     -57.980 -15.109 -19.785  1.00 41.32           N  
ANISOU  866  N   ILE A 790     5044   4867   5790   -113   -377   -463       N  
ATOM    867  CA  ILE A 790     -57.805 -13.666 -19.726  1.00 42.19           C  
ANISOU  867  CA  ILE A 790     5163   5025   5841   -101   -352   -444       C  
ATOM    868  C   ILE A 790     -58.771 -13.071 -18.706  1.00 42.23           C  
ANISOU  868  C   ILE A 790     5146   5032   5866   -126   -321   -405       C  
ATOM    869  O   ILE A 790     -58.365 -12.235 -17.898  1.00 41.44           O  
ANISOU  869  O   ILE A 790     5059   4955   5733   -126   -286   -370       O  
ATOM    870  CB  ILE A 790     -57.994 -13.007 -21.109  1.00 45.25           C  
ANISOU  870  CB  ILE A 790     5552   5450   6193    -74   -381   -483       C  
ATOM    871  CG1 ILE A 790     -56.848 -13.401 -22.045  1.00 46.35           C  
ANISOU  871  CG1 ILE A 790     5717   5598   6295    -45   -401   -517       C  
ATOM    872  CG2 ILE A 790     -58.015 -11.485 -21.005  1.00 46.00           C  
ANISOU  872  CG2 ILE A 790     5653   5588   6237    -65   -356   -458       C  
ATOM    873  CD1 ILE A 790     -57.242 -13.424 -23.512  1.00 51.82           C  
ANISOU  873  CD1 ILE A 790     6407   6309   6975    -21   -444   -567       C  
ATOM    874  N   ASP A 791     -60.026 -13.513 -18.732  1.00 39.66           N  
ANISOU  874  N   ASP A 791     4787   4684   5597   -148   -335   -413       N  
ATOM    875  CA  ASP A 791     -61.037 -13.030 -17.790  1.00 42.05           C  
ANISOU  875  CA  ASP A 791     5064   4990   5925   -172   -305   -380       C  
ATOM    876  C   ASP A 791     -60.734 -13.461 -16.356  1.00 41.59           C  
ANISOU  876  C   ASP A 791     5012   4909   5881   -195   -265   -331       C  
ATOM    877  O   ASP A 791     -61.000 -12.712 -15.405  1.00 39.90           O  
ANISOU  877  O   ASP A 791     4794   4714   5653   -203   -227   -295       O  
ATOM    878  CB  ASP A 791     -62.459 -13.516 -18.175  1.00 43.20           C  
ANISOU  878  CB  ASP A 791     5166   5113   6136   -192   -329   -403       C  
ATOM    879  CG  ASP A 791     -63.064 -12.770 -19.365  1.00 48.10           C  
ANISOU  879  CG  ASP A 791     5774   5764   6739   -171   -363   -442       C  
ATOM    880  OD1 ASP A 791     -64.281 -12.940 -19.600  1.00 54.48           O  
ANISOU  880  OD1 ASP A 791     6543   6561   7597   -185   -382   -460       O  
ATOM    881  OD2 ASP A 791     -62.352 -12.027 -20.077  1.00 54.46           O  
ANISOU  881  OD2 ASP A 791     6607   6603   7482   -140   -373   -455       O  
ATOM    882  N   VAL A 792     -60.213 -14.674 -16.192  1.00 41.57           N  
ANISOU  882  N   VAL A 792     5021   4866   5907   -202   -274   -331       N  
ATOM    883  CA  VAL A 792     -59.905 -15.167 -14.857  1.00 40.52           C  
ANISOU  883  CA  VAL A 792     4898   4710   5787   -221   -239   -283       C  
ATOM    884  C   VAL A 792     -58.802 -14.308 -14.245  1.00 37.83           C  
ANISOU  884  C   VAL A 792     4592   4404   5380   -201   -211   -258       C  
ATOM    885  O   VAL A 792     -58.899 -13.887 -13.101  1.00 37.64           O  
ANISOU  885  O   VAL A 792     4569   4390   5343   -211   -173   -216       O  
ATOM    886  CB  VAL A 792     -59.449 -16.644 -14.878  1.00 43.64           C  
ANISOU  886  CB  VAL A 792     5303   5052   6225   -229   -260   -288       C  
ATOM    887  CG1 VAL A 792     -58.953 -17.076 -13.500  1.00 42.22           C  
ANISOU  887  CG1 VAL A 792     5143   4853   6047   -242   -225   -235       C  
ATOM    888  CG2 VAL A 792     -60.582 -17.544 -15.339  1.00 46.95           C  
ANISOU  888  CG2 VAL A 792     5687   5432   6721   -254   -286   -310       C  
ATOM    889  N   ASN A 793     -57.757 -14.042 -15.020  1.00 35.53           N  
ANISOU  889  N   ASN A 793     4323   4131   5044   -172   -230   -285       N  
ATOM    890  CA  ASN A 793     -56.667 -13.223 -14.546  1.00 35.80           C  
ANISOU  890  CA  ASN A 793     4386   4196   5021   -152   -207   -267       C  
ATOM    891  C   ASN A 793     -57.036 -11.739 -14.350  1.00 33.81           C  
ANISOU  891  C   ASN A 793     4127   3987   4731   -147   -184   -255       C  
ATOM    892  O   ASN A 793     -56.551 -11.104 -13.429  1.00 32.89           O  
ANISOU  892  O   ASN A 793     4025   3889   4584   -144   -155   -226       O  
ATOM    893  CB  ASN A 793     -55.471 -13.427 -15.457  1.00 37.08           C  
ANISOU  893  CB  ASN A 793     4572   4365   5154   -125   -232   -299       C  
ATOM    894  CG  ASN A 793     -54.937 -14.854 -15.325  1.00 40.89           C  
ANISOU  894  CG  ASN A 793     5063   4802   5671   -128   -249   -304       C  
ATOM    895  OD1 ASN A 793     -54.496 -15.249 -14.262  1.00 38.64           O  
ANISOU  895  OD1 ASN A 793     4792   4499   5391   -135   -230   -271       O  
ATOM    896  ND2 ASN A 793     -55.070 -15.650 -16.372  1.00 40.61           N  
ANISOU  896  ND2 ASN A 793     5021   4746   5662   -122   -286   -346       N  
ATOM    897  N   TYR A 794     -57.889 -11.202 -15.210  1.00 33.09           N  
ANISOU  897  N   TYR A 794     4016   3912   4644   -145   -201   -279       N  
ATOM    898  CA  TYR A 794     -58.416  -9.848 -15.028  1.00 32.73           C  
ANISOU  898  CA  TYR A 794     3960   3901   4573   -141   -183   -268       C  
ATOM    899  C   TYR A 794     -59.001  -9.737 -13.640  1.00 31.87           C  
ANISOU  899  C   TYR A 794     3839   3789   4480   -162   -145   -229       C  
ATOM    900  O   TYR A 794     -58.692  -8.800 -12.918  1.00 31.57           O  
ANISOU  900  O   TYR A 794     3811   3776   4407   -155   -119   -207       O  
ATOM    901  CB  TYR A 794     -59.471  -9.536 -16.095  1.00 32.10           C  
ANISOU  901  CB  TYR A 794     3856   3831   4510   -138   -210   -299       C  
ATOM    902  CG  TYR A 794     -60.280  -8.284 -15.853  1.00 32.90           C  
ANISOU  902  CG  TYR A 794     3940   3960   4599   -137   -195   -288       C  
ATOM    903  CD1 TYR A 794     -59.726  -7.029 -16.025  1.00 32.91           C  
ANISOU  903  CD1 TYR A 794     3961   3995   4550   -116   -187   -285       C  
ATOM    904  CD2 TYR A 794     -61.602  -8.353 -15.459  1.00 32.62           C  
ANISOU  904  CD2 TYR A 794     3868   3917   4607   -158   -188   -283       C  
ATOM    905  CE1 TYR A 794     -60.465  -5.881 -15.822  1.00 32.28           C  
ANISOU  905  CE1 TYR A 794     3865   3937   4462   -113   -176   -277       C  
ATOM    906  CE2 TYR A 794     -62.347  -7.202 -15.235  1.00 32.71           C  
ANISOU  906  CE2 TYR A 794     3862   3955   4610   -154   -175   -277       C  
ATOM    907  CZ  TYR A 794     -61.778  -5.966 -15.418  1.00 31.91           C  
ANISOU  907  CZ  TYR A 794     3782   3884   4458   -130   -170   -274       C  
ATOM    908  OH  TYR A 794     -62.502  -4.806 -15.185  1.00 28.97           O  
ANISOU  908  OH  TYR A 794     3393   3534   4078   -124   -159   -269       O  
ATOM    909  N   GLU A 795     -59.863 -10.684 -13.280  1.00 33.07           N  
ANISOU  909  N   GLU A 795     3968   3910   4686   -188   -143   -220       N  
ATOM    910  CA  GLU A 795     -60.555 -10.653 -11.990  1.00 34.88           C  
ANISOU  910  CA  GLU A 795     4181   4137   4933   -210   -105   -181       C  
ATOM    911  C   GLU A 795     -59.580 -10.700 -10.825  1.00 35.18           C  
ANISOU  911  C   GLU A 795     4251   4177   4940   -206    -75   -145       C  
ATOM    912  O   GLU A 795     -59.837 -10.119  -9.772  1.00 35.05           O  
ANISOU  912  O   GLU A 795     4231   4179   4907   -211    -40   -116       O  
ATOM    913  CB  GLU A 795     -61.588 -11.775 -11.895  1.00 39.39           C  
ANISOU  913  CB  GLU A 795     4722   4671   5574   -241   -108   -178       C  
ATOM    914  CG  GLU A 795     -62.826 -11.528 -12.765  1.00 44.93           C  
ANISOU  914  CG  GLU A 795     5383   5376   6311   -248   -130   -209       C  
ATOM    915  CD  GLU A 795     -63.796 -12.719 -12.884  1.00 52.46           C  
ANISOU  915  CD  GLU A 795     6302   6287   7341   -279   -142   -215       C  
ATOM    916  OE1 GLU A 795     -63.559 -13.820 -12.316  1.00 53.40           O  
ANISOU  916  OE1 GLU A 795     6430   6369   7493   -298   -133   -192       O  
ATOM    917  OE2 GLU A 795     -64.833 -12.543 -13.559  1.00 58.37           O  
ANISOU  917  OE2 GLU A 795     7015   7039   8123   -284   -163   -243       O  
ATOM    918  N   LYS A 796     -58.457 -11.379 -11.013  1.00 34.61           N  
ANISOU  918  N   LYS A 796     4206   4087   4857   -196    -91   -150       N  
ATOM    919  CA  LYS A 796     -57.429 -11.476  -9.960  1.00 35.04           C  
ANISOU  919  CA  LYS A 796     4291   4142   4880   -188    -70   -119       C  
ATOM    920  C   LYS A 796     -56.768 -10.150  -9.614  1.00 33.27           C  
ANISOU  920  C   LYS A 796     4084   3960   4599   -166    -54   -116       C  
ATOM    921  O   LYS A 796     -56.254  -9.994  -8.513  1.00 35.44           O  
ANISOU  921  O   LYS A 796     4376   4243   4848   -162    -31    -88       O  
ATOM    922  CB  LYS A 796     -56.352 -12.460 -10.372  1.00 36.04           C  
ANISOU  922  CB  LYS A 796     4441   4240   5010   -178    -96   -132       C  
ATOM    923  CG  LYS A 796     -56.781 -13.925 -10.320  1.00 38.00           C  
ANISOU  923  CG  LYS A 796     4683   4439   5318   -200   -108   -125       C  
ATOM    924  CD  LYS A 796     -55.722 -14.786 -10.994  1.00 41.07           C  
ANISOU  924  CD  LYS A 796     5092   4803   5710   -183   -141   -151       C  
ATOM    925  CE  LYS A 796     -56.087 -16.263 -11.053  1.00 42.80           C  
ANISOU  925  CE  LYS A 796     5305   4966   5993   -203   -159   -149       C  
ATOM    926  NZ  LYS A 796     -55.123 -17.030 -11.901  1.00 44.60           N  
ANISOU  926  NZ  LYS A 796     5549   5173   6226   -183   -197   -185       N  
ATOM    927  N   LEU A 797     -56.757  -9.210 -10.562  1.00 31.88           N  
ANISOU  927  N   LEU A 797     3902   3809   4402   -151    -69   -145       N  
ATOM    928  CA  LEU A 797     -56.228  -7.857 -10.322  1.00 30.17           C  
ANISOU  928  CA  LEU A 797     3696   3628   4137   -132    -56   -144       C  
ATOM    929  C   LEU A 797     -57.121  -7.039  -9.377  1.00 30.76           C  
ANISOU  929  C   LEU A 797     3755   3724   4209   -140    -25   -123       C  
ATOM    930  O   LEU A 797     -56.652  -6.086  -8.790  1.00 30.98           O  
ANISOU  930  O   LEU A 797     3794   3775   4201   -126     -9   -115       O  
ATOM    931  CB  LEU A 797     -56.072  -7.078 -11.620  1.00 28.39           C  
ANISOU  931  CB  LEU A 797     3470   3422   3895   -116    -78   -176       C  
ATOM    932  CG  LEU A 797     -55.167  -7.694 -12.666  1.00 29.95           C  
ANISOU  932  CG  LEU A 797     3683   3609   4087   -104   -107   -202       C  
ATOM    933  CD1 LEU A 797     -55.249  -6.913 -13.962  1.00 31.86           C  
ANISOU  933  CD1 LEU A 797     3922   3872   4311    -89   -126   -229       C  
ATOM    934  CD2 LEU A 797     -53.734  -7.759 -12.176  1.00 30.02           C  
ANISOU  934  CD2 LEU A 797     3719   3620   4067    -91    -99   -194       C  
ATOM    935  N   LYS A 798     -58.399  -7.409  -9.249  1.00 32.64           N  
ANISOU  935  N   LYS A 798     3965   3952   4487   -161    -17   -116       N  
ATOM    936  CA  LYS A 798     -59.370  -6.713  -8.381  1.00 33.47           C  
ANISOU  936  CA  LYS A 798     4047   4076   4592   -168     14    -99       C  
ATOM    937  C   LYS A 798     -59.377  -5.228  -8.703  1.00 30.36           C  
ANISOU  937  C   LYS A 798     3651   3715   4167   -148     11   -116       C  
ATOM    938  O   LYS A 798     -59.337  -4.369  -7.830  1.00 28.82           O  
ANISOU  938  O   LYS A 798     3461   3544   3947   -139     35   -103       O  
ATOM    939  CB  LYS A 798     -59.054  -6.942  -6.900  1.00 37.50           C  
ANISOU  939  CB  LYS A 798     4573   4589   5084   -172     48    -61       C  
ATOM    940  CG  LYS A 798     -59.290  -8.367  -6.419  1.00 40.82           C  
ANISOU  940  CG  LYS A 798     4993   4975   5540   -195     57    -35       C  
ATOM    941  CD  LYS A 798     -59.186  -8.409  -4.906  1.00 48.65           C  
ANISOU  941  CD  LYS A 798     5998   5978   6508   -197     96      5       C  
ATOM    942  CE  LYS A 798     -59.028  -9.835  -4.379  1.00 56.28           C  
ANISOU  942  CE  LYS A 798     6977   6907   7499   -214    102     37       C  
ATOM    943  NZ  LYS A 798     -59.109  -9.903  -2.887  1.00 61.48           N  
ANISOU  943  NZ  LYS A 798     7648   7578   8133   -217    143     81       N  
ATOM    944  N   THR A 799     -59.419  -4.955  -9.987  1.00 28.13           N  
ANISOU  944  N   THR A 799     3366   3434   3889   -139    -19   -145       N  
ATOM    945  CA  THR A 799     -59.364  -3.604 -10.486  1.00 29.30           C  
ANISOU  945  CA  THR A 799     3515   3607   4011   -120    -27   -160       C  
ATOM    946  C   THR A 799     -60.312  -3.506 -11.659  1.00 29.12           C  
ANISOU  946  C   THR A 799     3468   3582   4012   -120    -54   -185       C  
ATOM    947  O   THR A 799     -60.241  -4.302 -12.603  1.00 32.37           O  
ANISOU  947  O   THR A 799     3882   3978   4441   -123    -82   -203       O  
ATOM    948  CB  THR A 799     -57.918  -3.266 -10.959  1.00 28.82           C  
ANISOU  948  CB  THR A 799     3487   3551   3911   -101    -39   -168       C  
ATOM    949  OG1 THR A 799     -57.027  -3.387  -9.849  1.00 30.97           O  
ANISOU  949  OG1 THR A 799     3779   3824   4162    -99    -18   -147       O  
ATOM    950  CG2 THR A 799     -57.842  -1.860 -11.502  1.00 27.92           C  
ANISOU  950  CG2 THR A 799     3375   3459   3772    -83    -46   -179       C  
ATOM    951  N   ASP A 800     -61.206  -2.551 -11.613  1.00 28.90           N  
ANISOU  951  N   ASP A 800     3420   3572   3990   -116    -50   -189       N  
ATOM    952  CA  ASP A 800     -62.063  -2.299 -12.755  1.00 28.31           C  
ANISOU  952  CA  ASP A 800     3325   3499   3934   -110    -80   -215       C  
ATOM    953  C   ASP A 800     -61.255  -1.521 -13.791  1.00 26.15           C  
ANISOU  953  C   ASP A 800     3077   3237   3622    -87   -104   -228       C  
ATOM    954  O   ASP A 800     -60.696  -0.501 -13.483  1.00 26.70           O  
ANISOU  954  O   ASP A 800     3163   3321   3660    -73    -92   -219       O  
ATOM    955  CB  ASP A 800     -63.297  -1.500 -12.347  1.00 29.05           C  
ANISOU  955  CB  ASP A 800     3385   3608   4046   -111    -69   -215       C  
ATOM    956  CG  ASP A 800     -64.279  -1.355 -13.497  1.00 31.49           C  
ANISOU  956  CG  ASP A 800     3669   3916   4379   -105   -104   -243       C  
ATOM    957  OD1 ASP A 800     -65.096  -2.269 -13.689  1.00 36.60           O  
ANISOU  957  OD1 ASP A 800     4288   4548   5071   -123   -114   -253       O  
ATOM    958  OD2 ASP A 800     -64.253  -0.345 -14.207  1.00 32.54           O  
ANISOU  958  OD2 ASP A 800     3809   4062   4490    -83   -124   -255       O  
ATOM    959  N   ILE A 801     -61.210  -2.024 -15.014  1.00 26.09           N  
ANISOU  959  N   ILE A 801     3073   3222   3618    -82   -137   -250       N  
ATOM    960  CA  ILE A 801     -60.506  -1.386 -16.094  1.00 25.09           C  
ANISOU  960  CA  ILE A 801     2972   3107   3454    -60   -158   -261       C  
ATOM    961  C   ILE A 801     -61.443  -1.116 -17.280  1.00 26.36           C  
ANISOU  961  C   ILE A 801     3118   3274   3624    -48   -193   -285       C  
ATOM    962  O   ILE A 801     -61.995  -2.044 -17.845  1.00 28.73           O  
ANISOU  962  O   ILE A 801     3403   3562   3952    -55   -217   -305       O  
ATOM    963  CB  ILE A 801     -59.333  -2.271 -16.581  1.00 24.03           C  
ANISOU  963  CB  ILE A 801     2863   2964   3303    -58   -166   -268       C  
ATOM    964  CG1 ILE A 801     -58.446  -2.684 -15.415  1.00 23.61           C  
ANISOU  964  CG1 ILE A 801     2823   2902   3244    -68   -137   -246       C  
ATOM    965  CG2 ILE A 801     -58.503  -1.517 -17.617  1.00 23.88           C  
ANISOU  965  CG2 ILE A 801     2871   2963   3241    -35   -179   -275       C  
ATOM    966  CD1 ILE A 801     -57.272  -3.581 -15.776  1.00 23.56           C  
ANISOU  966  CD1 ILE A 801     2840   2886   3226    -65   -144   -253       C  
ATOM    967  N   LYS A 802     -61.547   0.141 -17.687  1.00 27.54           N  
ANISOU  967  N   LYS A 802     3274   3441   3750    -29   -200   -283       N  
ATOM    968  CA  LYS A 802     -62.338   0.556 -18.829  1.00 29.22           C  
ANISOU  968  CA  LYS A 802     3478   3661   3963    -12   -236   -303       C  
ATOM    969  C   LYS A 802     -61.483   1.324 -19.821  1.00 29.35           C  
ANISOU  969  C   LYS A 802     3529   3692   3931     11   -248   -301       C  
ATOM    970  O   LYS A 802     -60.613   2.095 -19.440  1.00 27.44           O  
ANISOU  970  O   LYS A 802     3308   3456   3661     15   -226   -280       O  
ATOM    971  CB  LYS A 802     -63.467   1.491 -18.386  1.00 33.58           C  
ANISOU  971  CB  LYS A 802     4003   4220   4536     -9   -233   -301       C  
ATOM    972  CG  LYS A 802     -64.626   0.799 -17.663  1.00 39.28           C  
ANISOU  972  CG  LYS A 802     4682   4932   5311    -30   -226   -308       C  
ATOM    973  CD  LYS A 802     -65.659   1.851 -17.245  1.00 44.14           C  
ANISOU  973  CD  LYS A 802     5270   5558   5943    -22   -221   -307       C  
ATOM    974  CE  LYS A 802     -66.930   1.234 -16.649  1.00 49.26           C  
ANISOU  974  CE  LYS A 802     5869   6200   6647    -41   -214   -317       C  
ATOM    975  NZ  LYS A 802     -66.748   0.713 -15.257  1.00 48.78           N  
ANISOU  975  NZ  LYS A 802     5801   6134   6599    -66   -168   -294       N  
ATOM    976  N   VAL A 803     -61.761   1.133 -21.101  1.00 29.70           N  
ANISOU  976  N   VAL A 803     3578   3742   3963     27   -285   -322       N  
ATOM    977  CA  VAL A 803     -61.084   1.853 -22.149  1.00 29.37           C  
ANISOU  977  CA  VAL A 803     3569   3717   3874     50   -297   -317       C  
ATOM    978  C   VAL A 803     -61.672   3.254 -22.234  1.00 28.13           C  
ANISOU  978  C   VAL A 803     3410   3568   3709     66   -302   -305       C  
ATOM    979  O   VAL A 803     -62.872   3.403 -22.221  1.00 27.51           O  
ANISOU  979  O   VAL A 803     3305   3488   3661     69   -321   -317       O  
ATOM    980  CB  VAL A 803     -61.281   1.165 -23.504  1.00 29.72           C  
ANISOU  980  CB  VAL A 803     3619   3767   3904     66   -336   -346       C  
ATOM    981  CG1 VAL A 803     -60.612   1.967 -24.608  1.00 30.01           C  
ANISOU  981  CG1 VAL A 803     3692   3826   3886     91   -346   -338       C  
ATOM    982  CG2 VAL A 803     -60.711  -0.226 -23.444  1.00 31.12           C  
ANISOU  982  CG2 VAL A 803     3798   3933   4093     52   -334   -362       C  
ATOM    983  N   VAL A 804     -60.812   4.267 -22.287  1.00 27.78           N  
ANISOU  983  N   VAL A 804     3394   3531   3631     75   -286   -281       N  
ATOM    984  CA  VAL A 804     -61.244   5.618 -22.537  1.00 27.73           C  
ANISOU  984  CA  VAL A 804     3393   3529   3616     93   -295   -267       C  
ATOM    985  C   VAL A 804     -61.274   5.846 -24.037  1.00 29.40           C  
ANISOU  985  C   VAL A 804     3627   3754   3791    118   -328   -272       C  
ATOM    986  O   VAL A 804     -60.294   5.623 -24.737  1.00 29.54           O  
ANISOU  986  O   VAL A 804     3673   3781   3770    123   -324   -267       O  
ATOM    987  CB  VAL A 804     -60.319   6.631 -21.863  1.00 27.83           C  
ANISOU  987  CB  VAL A 804     3423   3538   3614     90   -262   -239       C  
ATOM    988  CG1 VAL A 804     -60.709   8.039 -22.264  1.00 27.91           C  
ANISOU  988  CG1 VAL A 804     3442   3548   3615    110   -275   -224       C  
ATOM    989  CG2 VAL A 804     -60.388   6.479 -20.340  1.00 28.07           C  
ANISOU  989  CG2 VAL A 804     3431   3559   3676     69   -232   -236       C  
ATOM    990  N   ASP A 805     -62.430   6.226 -24.548  1.00 32.06           N  
ANISOU  990  N   ASP A 805     3950   4093   4138    135   -362   -284       N  
ATOM    991  CA  ASP A 805     -62.622   6.399 -25.984  1.00 34.76           C  
ANISOU  991  CA  ASP A 805     4313   4449   4445    163   -400   -290       C  
ATOM    992  C   ASP A 805     -61.618   7.416 -26.516  1.00 32.28           C  
ANISOU  992  C   ASP A 805     4040   4142   4081    176   -385   -256       C  
ATOM    993  O   ASP A 805     -61.504   8.525 -25.977  1.00 32.66           O  
ANISOU  993  O   ASP A 805     4093   4181   4135    176   -368   -231       O  
ATOM    994  CB  ASP A 805     -64.073   6.874 -26.220  1.00 40.50           C  
ANISOU  994  CB  ASP A 805     5016   5175   5198    180   -438   -305       C  
ATOM    995  CG  ASP A 805     -64.457   6.935 -27.681  1.00 45.89           C  
ANISOU  995  CG  ASP A 805     5716   5873   5845    212   -485   -317       C  
ATOM    996  OD1 ASP A 805     -63.661   6.575 -28.573  1.00 51.51           O  
ANISOU  996  OD1 ASP A 805     6461   6600   6511    222   -488   -316       O  
ATOM    997  OD2 ASP A 805     -65.595   7.380 -27.934  1.00 57.11           O  
ANISOU  997  OD2 ASP A 805     7119   7294   7286    230   -519   -329       O  
ATOM    998  N   ARG A 806     -60.909   7.047 -27.572  1.00 32.60           N  
ANISOU  998  N   ARG A 806     4110   4200   4075    188   -392   -257       N  
ATOM    999  CA  ARG A 806     -59.879   7.902 -28.178  1.00 35.02           C  
ANISOU  999  CA  ARG A 806     4456   4516   4333    198   -374   -223       C  
ATOM   1000  C   ARG A 806     -60.374   9.274 -28.596  1.00 32.58           C  
ANISOU 1000  C   ARG A 806     4161   4204   4012    220   -390   -197       C  
ATOM   1001  O   ARG A 806     -59.601  10.237 -28.638  1.00 36.88           O  
ANISOU 1001  O   ARG A 806     4731   4746   4537    220   -366   -161       O  
ATOM   1002  CB  ARG A 806     -59.249   7.180 -29.398  1.00 39.09           C  
ANISOU 1002  CB  ARG A 806     4998   5057   4798    213   -383   -234       C  
ATOM   1003  N   ASP A 807     -61.658   9.368 -28.901  1.00 33.69           N  
ANISOU 1003  N   ASP A 807     4286   4345   4170    238   -431   -215       N  
ATOM   1004  CA  ASP A 807     -62.299  10.611 -29.376  1.00 35.30           C  
ANISOU 1004  CA  ASP A 807     4502   4544   4365    263   -457   -194       C  
ATOM   1005  C   ASP A 807     -62.933  11.431 -28.291  1.00 32.18           C  
ANISOU 1005  C   ASP A 807     4081   4126   4020    256   -450   -188       C  
ATOM   1006  O   ASP A 807     -63.506  12.456 -28.585  1.00 34.88           O  
ANISOU 1006  O   ASP A 807     4431   4461   4363    278   -472   -174       O  
ATOM   1007  CB  ASP A 807     -63.420  10.280 -30.384  1.00 38.19           C  
ANISOU 1007  CB  ASP A 807     4864   4925   4723    293   -513   -222       C  
ATOM   1008  CG  ASP A 807     -62.921   9.517 -31.597  1.00 42.74           C  
ANISOU 1008  CG  ASP A 807     5469   5528   5244    308   -527   -233       C  
ATOM   1009  OD1 ASP A 807     -61.757   9.750 -32.036  1.00 48.20           O  
ANISOU 1009  OD1 ASP A 807     6196   6230   5887    308   -499   -204       O  
ATOM   1010  OD2 ASP A 807     -63.683   8.671 -32.108  1.00 46.20           O  
ANISOU 1010  OD2 ASP A 807     5891   5977   5687    321   -567   -273       O  
ATOM   1011  N   SER A 808     -62.851  11.001 -27.036  1.00 33.38           N  
ANISOU 1011  N   SER A 808     4203   4267   4213    228   -421   -200       N  
ATOM   1012  CA  SER A 808     -63.433  11.760 -25.906  1.00 30.74           C  
ANISOU 1012  CA  SER A 808     3842   3913   3924    222   -411   -198       C  
ATOM   1013  C   SER A 808     -62.594  12.966 -25.566  1.00 31.36           C  
ANISOU 1013  C   SER A 808     3945   3978   3994    220   -384   -161       C  
ATOM   1014  O   SER A 808     -61.420  13.062 -25.928  1.00 29.64           O  
ANISOU 1014  O   SER A 808     3757   3763   3741    214   -362   -138       O  
ATOM   1015  CB  SER A 808     -63.557  10.856 -24.668  1.00 30.57           C  
ANISOU 1015  CB  SER A 808     3784   3888   3943    193   -385   -220       C  
ATOM   1016  OG  SER A 808     -62.281  10.434 -24.161  1.00 30.11           O  
ANISOU 1016  OG  SER A 808     3740   3829   3871    170   -345   -207       O  
ATOM   1017  N   GLU A 809     -63.178  13.879 -24.812  1.00 34.57           N  
ANISOU 1017  N   GLU A 809     4334   4367   4434    224   -385   -159       N  
ATOM   1018  CA  GLU A 809     -62.446  15.038 -24.318  1.00 35.07           C  
ANISOU 1018  CA  GLU A 809     4414   4412   4500    221   -361   -130       C  
ATOM   1019  C   GLU A 809     -61.486  14.601 -23.224  1.00 31.83           C  
ANISOU 1019  C   GLU A 809     3997   3999   4099    191   -317   -131       C  
ATOM   1020  O   GLU A 809     -60.398  15.162 -23.068  1.00 29.64           O  
ANISOU 1020  O   GLU A 809     3741   3712   3810    182   -292   -107       O  
ATOM   1021  CB  GLU A 809     -63.421  16.127 -23.803  1.00 40.64           C  
ANISOU 1021  CB  GLU A 809     5100   5098   5242    238   -378   -133       C  
ATOM   1022  CG  GLU A 809     -62.788  17.384 -23.174  1.00 47.58           C  
ANISOU 1022  CG  GLU A 809     5992   5952   6134    235   -358   -109       C  
ATOM   1023  CD  GLU A 809     -61.710  18.020 -24.025  1.00 51.40           C  
ANISOU 1023  CD  GLU A 809     6520   6427   6582    237   -350    -69       C  
ATOM   1024  OE1 GLU A 809     -61.645  17.708 -25.228  1.00 57.56           O  
ANISOU 1024  OE1 GLU A 809     7324   7222   7324    248   -368    -57       O  
ATOM   1025  OE2 GLU A 809     -60.961  18.870 -23.498  1.00 56.58           O  
ANISOU 1025  OE2 GLU A 809     7186   7062   7250    227   -328    -50       O  
ATOM   1026  N   GLU A 810     -61.897  13.600 -22.466  1.00 29.72           N  
ANISOU 1026  N   GLU A 810     3698   3740   3855    176   -308   -159       N  
ATOM   1027  CA  GLU A 810     -61.052  12.997 -21.444  1.00 30.27           C  
ANISOU 1027  CA  GLU A 810     3761   3809   3930    150   -271   -161       C  
ATOM   1028  C   GLU A 810     -59.715  12.569 -22.084  1.00 27.93           C  
ANISOU 1028  C   GLU A 810     3496   3520   3596    141   -255   -145       C  
ATOM   1029  O   GLU A 810     -58.628  12.927 -21.608  1.00 27.93           O  
ANISOU 1029  O   GLU A 810     3508   3513   3590    129   -227   -130       O  
ATOM   1030  CB  GLU A 810     -61.800  11.800 -20.847  1.00 32.92           C  
ANISOU 1030  CB  GLU A 810     4063   4154   4291    138   -270   -190       C  
ATOM   1031  CG  GLU A 810     -61.257  11.211 -19.558  1.00 35.11           C  
ANISOU 1031  CG  GLU A 810     4327   4430   4582    114   -234   -194       C  
ATOM   1032  CD  GLU A 810     -62.220  10.204 -18.938  1.00 36.16           C  
ANISOU 1032  CD  GLU A 810     4425   4569   4745    103   -233   -218       C  
ATOM   1033  OE1 GLU A 810     -63.082   9.628 -19.674  1.00 37.75           O  
ANISOU 1033  OE1 GLU A 810     4612   4776   4955    108   -261   -234       O  
ATOM   1034  OE2 GLU A 810     -62.123   9.989 -17.711  1.00 38.71           O  
ANISOU 1034  OE2 GLU A 810     4732   4891   5084     88   -205   -220       O  
ATOM   1035  N   ALA A 811     -59.793  11.820 -23.185  1.00 25.70           N  
ANISOU 1035  N   ALA A 811     3224   3253   3287    148   -274   -152       N  
ATOM   1036  CA  ALA A 811     -58.578  11.342 -23.848  1.00 26.08           C  
ANISOU 1036  CA  ALA A 811     3300   3313   3298    142   -259   -141       C  
ATOM   1037  C   ALA A 811     -57.728  12.510 -24.352  1.00 26.65           C  
ANISOU 1037  C   ALA A 811     3403   3379   3345    149   -247   -106       C  
ATOM   1038  O   ALA A 811     -56.497  12.471 -24.325  1.00 23.80           O  
ANISOU 1038  O   ALA A 811     3056   3019   2968    136   -219    -92       O  
ATOM   1039  CB  ALA A 811     -58.927  10.404 -24.998  1.00 26.22           C  
ANISOU 1039  CB  ALA A 811     3324   3350   3290    155   -286   -158       C  
ATOM   1040  N   GLU A 812     -58.400  13.546 -24.828  1.00 27.67           N  
ANISOU 1040  N   GLU A 812     3540   3499   3474    168   -270    -91       N  
ATOM   1041  CA  GLU A 812     -57.722  14.696 -25.384  1.00 28.19           C  
ANISOU 1041  CA  GLU A 812     3636   3555   3520    175   -262    -53       C  
ATOM   1042  C   GLU A 812     -56.901  15.391 -24.318  1.00 25.89           C  
ANISOU 1042  C   GLU A 812     3340   3242   3255    156   -229    -40       C  
ATOM   1043  O   GLU A 812     -55.757  15.797 -24.576  1.00 26.52           O  
ANISOU 1043  O   GLU A 812     3440   3319   3318    146   -205    -15       O  
ATOM   1044  CB  GLU A 812     -58.755  15.622 -26.059  1.00 30.07           C  
ANISOU 1044  CB  GLU A 812     3883   3785   3757    203   -298    -41       C  
ATOM   1045  CG  GLU A 812     -58.312  17.024 -26.425  1.00 33.32           C  
ANISOU 1045  CG  GLU A 812     4322   4175   4161    210   -294      1       C  
ATOM   1046  CD  GLU A 812     -57.213  17.062 -27.484  1.00 35.13           C  
ANISOU 1046  CD  GLU A 812     4588   4417   4341    209   -275     34       C  
ATOM   1047  OE1 GLU A 812     -56.928  16.050 -28.146  1.00 37.56           O  
ANISOU 1047  OE1 GLU A 812     4904   4754   4613    210   -274     23       O  
ATOM   1048  OE2 GLU A 812     -56.623  18.135 -27.655  1.00 40.36           O  
ANISOU 1048  OE2 GLU A 812     5271   5060   5003    207   -261     72       O  
ATOM   1049  N   ILE A 813     -57.509  15.576 -23.153  1.00 25.29           N  
ANISOU 1049  N   ILE A 813     3236   3153   3219    151   -230    -59       N  
ATOM   1050  CA  ILE A 813     -56.831  16.175 -22.014  1.00 25.22           C  
ANISOU 1050  CA  ILE A 813     3219   3125   3237    136   -204    -55       C  
ATOM   1051  C   ILE A 813     -55.570  15.345 -21.676  1.00 24.51           C  
ANISOU 1051  C   ILE A 813     3131   3046   3135    113   -172    -58       C  
ATOM   1052  O   ILE A 813     -54.472  15.887 -21.521  1.00 24.04           O  
ANISOU 1052  O   ILE A 813     3083   2976   3076    102   -150    -41       O  
ATOM   1053  CB  ILE A 813     -57.715  16.187 -20.765  1.00 26.35           C  
ANISOU 1053  CB  ILE A 813     3331   3263   3419    136   -207    -82       C  
ATOM   1054  CG1 ILE A 813     -58.986  17.026 -20.927  1.00 31.24           C  
ANISOU 1054  CG1 ILE A 813     3942   3871   4058    159   -238    -85       C  
ATOM   1055  CG2 ILE A 813     -56.973  16.706 -19.538  1.00 25.59           C  
ANISOU 1055  CG2 ILE A 813     3227   3151   3346    122   -182    -84       C  
ATOM   1056  CD1 ILE A 813     -58.715  18.471 -21.119  1.00 34.63           C  
ANISOU 1056  CD1 ILE A 813     4389   4273   4496    169   -243    -60       C  
ATOM   1057  N   ILE A 814     -55.730  14.029 -21.619  1.00 22.13           N  
ANISOU 1057  N   ILE A 814     2819   2765   2826    108   -172    -81       N  
ATOM   1058  CA  ILE A 814     -54.617  13.160 -21.288  1.00 22.14           C  
ANISOU 1058  CA  ILE A 814     2821   2775   2818     90   -147    -87       C  
ATOM   1059  C   ILE A 814     -53.493  13.187 -22.343  1.00 21.84           C  
ANISOU 1059  C   ILE A 814     2809   2746   2745     88   -134    -66       C  
ATOM   1060  O   ILE A 814     -52.316  13.248 -21.990  1.00 21.80           O  
ANISOU 1060  O   ILE A 814     2806   2738   2740     74   -107    -59       O  
ATOM   1061  CB  ILE A 814     -55.119  11.745 -21.030  1.00 21.77           C  
ANISOU 1061  CB  ILE A 814     2756   2742   2773     85   -153   -115       C  
ATOM   1062  CG1 ILE A 814     -55.891  11.748 -19.723  1.00 21.75           C  
ANISOU 1062  CG1 ILE A 814     2727   2731   2806     80   -151   -131       C  
ATOM   1063  CG2 ILE A 814     -53.939  10.777 -20.987  1.00 22.34           C  
ANISOU 1063  CG2 ILE A 814     2834   2824   2830     71   -132   -120       C  
ATOM   1064  CD1 ILE A 814     -56.615  10.469 -19.422  1.00 24.16           C  
ANISOU 1064  CD1 ILE A 814     3012   3046   3122     75   -158   -154       C  
ATOM   1065  N   ARG A 815     -53.852  13.223 -23.628  1.00 22.51           N  
ANISOU 1065  N   ARG A 815     2912   2843   2799    104   -151    -55       N  
ATOM   1066  CA  ARG A 815     -52.854  13.348 -24.704  1.00 23.29           C  
ANISOU 1066  CA  ARG A 815     3036   2954   2859    105   -137    -32       C  
ATOM   1067  C   ARG A 815     -52.138  14.676 -24.620  1.00 22.64           C  
ANISOU 1067  C   ARG A 815     2965   2851   2785     98   -117      2       C  
ATOM   1068  O   ARG A 815     -50.961  14.750 -24.905  1.00 22.09           O  
ANISOU 1068  O   ARG A 815     2906   2787   2702     87    -90     18       O  
ATOM   1069  CB  ARG A 815     -53.465  13.142 -26.098  1.00 24.70           C  
ANISOU 1069  CB  ARG A 815     3235   3152   2998    128   -162    -28       C  
ATOM   1070  CG  ARG A 815     -53.774  11.690 -26.424  1.00 27.52           C  
ANISOU 1070  CG  ARG A 815     3584   3532   3340    133   -177    -62       C  
ATOM   1071  CD  ARG A 815     -54.169  11.519 -27.891  1.00 32.13           C  
ANISOU 1071  CD  ARG A 815     4191   4139   3878    158   -201    -59       C  
ATOM   1072  NE  ARG A 815     -55.281  12.407 -28.223  1.00 32.85           N  
ANISOU 1072  NE  ARG A 815     4289   4221   3974    177   -232    -47       N  
ATOM   1073  CZ  ARG A 815     -56.563  12.055 -28.280  1.00 30.53           C  
ANISOU 1073  CZ  ARG A 815     3979   3927   3693    191   -270    -72       C  
ATOM   1074  NH1 ARG A 815     -57.460  12.977 -28.542  1.00 29.99           N  
ANISOU 1074  NH1 ARG A 815     3916   3849   3631    210   -297    -59       N  
ATOM   1075  NH2 ARG A 815     -56.942  10.810 -28.076  1.00 30.88           N  
ANISOU 1075  NH2 ARG A 815     4003   3982   3750    187   -282   -110       N  
ATOM   1076  N   LYS A 816     -52.845  15.714 -24.231  1.00 24.36           N  
ANISOU 1076  N   LYS A 816     3181   3046   3031    105   -132     11       N  
ATOM   1077  CA  LYS A 816     -52.236  17.029 -24.063  1.00 27.24           C  
ANISOU 1077  CA  LYS A 816     3553   3383   3413     98   -117     41       C  
ATOM   1078  C   LYS A 816     -51.201  16.991 -22.949  1.00 25.59           C  
ANISOU 1078  C   LYS A 816     3328   3164   3232     75    -89     31       C  
ATOM   1079  O   LYS A 816     -50.088  17.491 -23.092  1.00 25.68           O  
ANISOU 1079  O   LYS A 816     3346   3167   3245     61    -64     52       O  
ATOM   1080  CB  LYS A 816     -53.329  18.026 -23.676  1.00 32.01           C  
ANISOU 1080  CB  LYS A 816     4153   3962   4048    112   -143     43       C  
ATOM   1081  CG  LYS A 816     -53.685  19.085 -24.687  1.00 39.15           C  
ANISOU 1081  CG  LYS A 816     5084   4853   4940    129   -160     79       C  
ATOM   1082  CD  LYS A 816     -54.779  19.952 -24.077  1.00 44.17           C  
ANISOU 1082  CD  LYS A 816     5707   5462   5614    143   -187     71       C  
ATOM   1083  CE  LYS A 816     -55.241  21.032 -25.007  1.00 50.40           C  
ANISOU 1083  CE  LYS A 816     6522   6232   6395    164   -209    106       C  
ATOM   1084  NZ  LYS A 816     -56.148  20.434 -26.018  1.00 54.47           N  
ANISOU 1084  NZ  LYS A 816     7048   6774   6874    188   -239    102       N  
ATOM   1085  N   TYR A 817     -51.569  16.355 -21.844  1.00 24.20           N  
ANISOU 1085  N   TYR A 817     3128   2990   3077     71    -93     -2       N  
ATOM   1086  CA  TYR A 817     -50.668  16.252 -20.713  1.00 22.80           C  
ANISOU 1086  CA  TYR A 817     2934   2805   2923     53    -71    -16       C  
ATOM   1087  C   TYR A 817     -49.380  15.549 -21.156  1.00 23.18           C  
ANISOU 1087  C   TYR A 817     2988   2870   2949     40    -46    -12       C  
ATOM   1088  O   TYR A 817     -48.288  16.028 -20.876  1.00 23.92           O  
ANISOU 1088  O   TYR A 817     3080   2953   3056     26    -25     -3       O  
ATOM   1089  CB  TYR A 817     -51.349  15.477 -19.612  1.00 20.52           C  
ANISOU 1089  CB  TYR A 817     2624   2523   2650     54    -79    -49       C  
ATOM   1090  CG  TYR A 817     -50.763  15.595 -18.231  1.00 19.90           C  
ANISOU 1090  CG  TYR A 817     2529   2434   2598     42    -65    -66       C  
ATOM   1091  CD1 TYR A 817     -49.672  16.418 -17.933  1.00 19.14           C  
ANISOU 1091  CD1 TYR A 817     2435   2321   2519     32    -49    -56       C  
ATOM   1092  CD2 TYR A 817     -51.348  14.886 -17.188  1.00 18.93           C  
ANISOU 1092  CD2 TYR A 817     2388   2318   2485     43    -68    -92       C  
ATOM   1093  CE1 TYR A 817     -49.200  16.508 -16.631  1.00 19.43           C  
ANISOU 1093  CE1 TYR A 817     2455   2349   2578     25    -42    -75       C  
ATOM   1094  CE2 TYR A 817     -50.903  14.993 -15.913  1.00 18.58           C  
ANISOU 1094  CE2 TYR A 817     2331   2268   2459     38    -58   -107       C  
ATOM   1095  CZ  TYR A 817     -49.830  15.787 -15.631  1.00 18.79           C  
ANISOU 1095  CZ  TYR A 817     2361   2279   2500     30    -47   -101       C  
ATOM   1096  OH  TYR A 817     -49.449  15.820 -14.308  1.00 20.04           O  
ANISOU 1096  OH  TYR A 817     2506   2434   2675     27    -41   -121       O  
ATOM   1097  N   VAL A 818     -49.524  14.464 -21.912  1.00 22.90           N  
ANISOU 1097  N   VAL A 818     2959   2861   2880     46    -50    -20       N  
ATOM   1098  CA  VAL A 818     -48.347  13.736 -22.446  1.00 24.21           C  
ANISOU 1098  CA  VAL A 818     3130   3047   3022     38    -28    -20       C  
ATOM   1099  C   VAL A 818     -47.488  14.596 -23.383  1.00 26.10           C  
ANISOU 1099  C   VAL A 818     3387   3285   3245     34     -7     16       C  
ATOM   1100  O   VAL A 818     -46.287  14.703 -23.223  1.00 25.66           O  
ANISOU 1100  O   VAL A 818     3325   3228   3197     18     20     21       O  
ATOM   1101  CB  VAL A 818     -48.743  12.475 -23.203  1.00 23.37           C  
ANISOU 1101  CB  VAL A 818     3030   2968   2883     49    -40    -37       C  
ATOM   1102  CG1 VAL A 818     -47.539  11.860 -23.889  1.00 22.83           C  
ANISOU 1102  CG1 VAL A 818     2968   2921   2787     45    -16    -36       C  
ATOM   1103  CG2 VAL A 818     -49.395  11.469 -22.259  1.00 22.46           C  
ANISOU 1103  CG2 VAL A 818     2894   2852   2786     48    -54    -69       C  
ATOM   1104  N   LYS A 819     -48.139  15.281 -24.304  1.00 27.54           N  
ANISOU 1104  N   LYS A 819     3589   3465   3409     47    -20     41       N  
ATOM   1105  CA  LYS A 819     -47.444  16.084 -25.286  1.00 29.42           C  
ANISOU 1105  CA  LYS A 819     3848   3703   3629     44      0     81       C  
ATOM   1106  C   LYS A 819     -46.724  17.302 -24.689  1.00 29.22           C  
ANISOU 1106  C   LYS A 819     3816   3644   3644     26     19    103       C  
ATOM   1107  O   LYS A 819     -45.598  17.588 -25.031  1.00 29.69           O  
ANISOU 1107  O   LYS A 819     3877   3705   3701     11     50    123       O  
ATOM   1108  CB  LYS A 819     -48.443  16.553 -26.344  1.00 30.71           C  
ANISOU 1108  CB  LYS A 819     4037   3870   3763     66    -24    104       C  
ATOM   1109  CG  LYS A 819     -47.843  17.142 -27.598  1.00 33.40           C  
ANISOU 1109  CG  LYS A 819     4405   4219   4067     69     -4    148       C  
ATOM   1110  CD  LYS A 819     -48.882  18.052 -28.242  1.00 37.27           C  
ANISOU 1110  CD  LYS A 819     4919   4695   4547     89    -32    177       C  
ATOM   1111  CE  LYS A 819     -48.548  18.422 -29.672  1.00 42.38           C  
ANISOU 1111  CE  LYS A 819     5600   5360   5142    100    -19    221       C  
ATOM   1112  NZ  LYS A 819     -47.801  19.696 -29.743  1.00 44.55           N  
ANISOU 1112  NZ  LYS A 819     5885   5605   5438     83      9    269       N  
ATOM   1113  N   ASN A 820     -47.416  18.044 -23.846  1.00 27.95           N  
ANISOU 1113  N   ASN A 820     3646   3453   3520     27      0     97       N  
ATOM   1114  CA  ASN A 820     -46.884  19.278 -23.328  1.00 26.95           C  
ANISOU 1114  CA  ASN A 820     3515   3291   3436     13     10    116       C  
ATOM   1115  C   ASN A 820     -45.837  19.127 -22.273  1.00 25.22           C  
ANISOU 1115  C   ASN A 820     3270   3063   3248     -7     29     93       C  
ATOM   1116  O   ASN A 820     -45.082  20.061 -22.081  1.00 25.41           O  
ANISOU 1116  O   ASN A 820     3289   3061   3304    -23     44    111       O  
ATOM   1117  CB  ASN A 820     -48.006  20.103 -22.733  1.00 27.66           C  
ANISOU 1117  CB  ASN A 820     3602   3352   3556     26    -20    111       C  
ATOM   1118  CG  ASN A 820     -48.908  20.673 -23.779  1.00 29.13           C  
ANISOU 1118  CG  ASN A 820     3813   3533   3721     45    -40    141       C  
ATOM   1119  OD1 ASN A 820     -48.590  20.665 -24.963  1.00 31.69           O  
ANISOU 1119  OD1 ASN A 820     4161   3872   4008     48    -29    172       O  
ATOM   1120  ND2 ASN A 820     -50.023  21.244 -23.343  1.00 31.00           N  
ANISOU 1120  ND2 ASN A 820     4047   3749   3981     61    -70    132       N  
ATOM   1121  N   THR A 821     -45.806  18.005 -21.547  1.00 22.94           N  
ANISOU 1121  N   THR A 821     2966   2795   2957     -7     27     56       N  
ATOM   1122  CA  THR A 821     -44.899  17.904 -20.405  1.00 22.16           C  
ANISOU 1122  CA  THR A 821     2843   2688   2889    -22     39     32       C  
ATOM   1123  C   THR A 821     -43.729  16.935 -20.661  1.00 23.55           C  
ANISOU 1123  C   THR A 821     3012   2890   3047    -32     63     23       C  
ATOM   1124  O   THR A 821     -43.082  16.487 -19.744  1.00 22.69           O  
ANISOU 1124  O   THR A 821     2883   2781   2955    -40     68     -3       O  
ATOM   1125  CB  THR A 821     -45.644  17.547 -19.130  1.00 21.84           C  
ANISOU 1125  CB  THR A 821     2788   2644   2867    -14     18     -3       C  
ATOM   1126  OG1 THR A 821     -46.096  16.180 -19.165  1.00 21.74           O  
ANISOU 1126  OG1 THR A 821     2775   2661   2826     -5     11    -24       O  
ATOM   1127  CG2 THR A 821     -46.844  18.503 -18.911  1.00 21.40           C  
ANISOU 1127  CG2 THR A 821     2736   2565   2829     -1     -6      2       C  
ATOM   1128  N   HIS A 822     -43.455  16.637 -21.928  1.00 25.31           N  
ANISOU 1128  N   HIS A 822     3250   3134   3233    -30     78     45       N  
ATOM   1129  CA  HIS A 822     -42.258  15.899 -22.294  1.00 27.59           C  
ANISOU 1129  CA  HIS A 822     3531   3446   3506    -40    105     39       C  
ATOM   1130  C   HIS A 822     -41.085  16.868 -22.157  1.00 29.56           C  
ANISOU 1130  C   HIS A 822     3767   3675   3789    -61    131     57       C  
ATOM   1131  O   HIS A 822     -41.079  17.891 -22.789  1.00 30.06           O  
ANISOU 1131  O   HIS A 822     3843   3722   3857    -67    141     94       O  
ATOM   1132  CB  HIS A 822     -42.318  15.368 -23.731  1.00 28.02           C  
ANISOU 1132  CB  HIS A 822     3606   3533   3508    -29    115     56       C  
ATOM   1133  CG  HIS A 822     -41.230  14.389 -24.036  1.00 28.80           C  
ANISOU 1133  CG  HIS A 822     3694   3661   3589    -33    138     40       C  
ATOM   1134  ND1 HIS A 822     -41.487  13.103 -24.456  1.00 31.59           N  
ANISOU 1134  ND1 HIS A 822     4053   4044   3907    -17    129     16       N  
ATOM   1135  CD2 HIS A 822     -39.890  14.472 -23.893  1.00 28.58           C  
ANISOU 1135  CD2 HIS A 822     3647   3633   3578    -49    168     39       C  
ATOM   1136  CE1 HIS A 822     -40.356  12.434 -24.560  1.00 29.68           C  
ANISOU 1136  CE1 HIS A 822     3797   3821   3660    -23    152      1       C  
ATOM   1137  NE2 HIS A 822     -39.369  13.246 -24.233  1.00 29.16           N  
ANISOU 1137  NE2 HIS A 822     3715   3739   3625    -42    177     15       N  
ATOM   1138  N   ALA A 823     -40.127  16.576 -21.290  1.00 31.31           N  
ANISOU 1138  N   ALA A 823     3964   3895   4039    -73    140     32       N  
ATOM   1139  CA  ALA A 823     -39.049  17.514 -21.011  1.00 32.90           C  
ANISOU 1139  CA  ALA A 823     4146   4071   4281    -95    161     43       C  
ATOM   1140  C   ALA A 823     -38.074  17.631 -22.187  1.00 35.95           C  
ANISOU 1140  C   ALA A 823     4534   4474   4652   -108    199     73       C  
ATOM   1141  O   ALA A 823     -37.794  16.638 -22.859  1.00 35.82           O  
ANISOU 1141  O   ALA A 823     4521   4494   4596   -100    212     66       O  
ATOM   1142  CB  ALA A 823     -38.287  17.092 -19.762  1.00 31.00           C  
ANISOU 1142  CB  ALA A 823     3877   3827   4073   -101    156      3       C  
ATOM   1143  N   THR A 824     -37.548  18.846 -22.389  1.00 38.66           N  
ANISOU 1143  N   THR A 824     4873   4789   5028   -127    217    104       N  
ATOM   1144  CA  THR A 824     -36.578  19.124 -23.481  1.00 40.50           C  
ANISOU 1144  CA  THR A 824     5104   5034   5250   -143    260    139       C  
ATOM   1145  C   THR A 824     -35.307  18.305 -23.378  1.00 37.04           C  
ANISOU 1145  C   THR A 824     4637   4622   4815   -152    286    113       C  
ATOM   1146  O   THR A 824     -34.739  18.011 -24.400  1.00 39.32           O  
ANISOU 1146  O   THR A 824     4929   4940   5072   -155    319    132       O  
ATOM   1147  CB  THR A 824     -36.119  20.602 -23.578  1.00 40.32           C  
ANISOU 1147  CB  THR A 824     5076   4970   5274   -168    278    178       C  
ATOM   1148  OG1 THR A 824     -35.418  20.976 -22.382  1.00 43.34           O  
ANISOU 1148  OG1 THR A 824     5425   5324   5720   -185    271    148       O  
ATOM   1149  CG2 THR A 824     -37.308  21.525 -23.817  1.00 40.95           C  
ANISOU 1149  CG2 THR A 824     5186   5020   5352   -158    254    209       C  
ATOM   1150  N   THR A 825     -34.861  17.941 -22.169  1.00 34.24           N  
ANISOU 1150  N   THR A 825     4255   4259   4496   -155    270     70       N  
ATOM   1151  CA  THR A 825     -33.632  17.140 -21.995  1.00 35.18           C  
ANISOU 1151  CA  THR A 825     4343   4401   4622   -161    289     41       C  
ATOM   1152  C   THR A 825     -33.807  15.636 -22.067  1.00 33.37           C  
ANISOU 1152  C   THR A 825     4119   4210   4349   -138    279      9       C  
ATOM   1153  O   THR A 825     -32.838  14.904 -21.937  1.00 31.98           O  
ANISOU 1153  O   THR A 825     3920   4053   4178   -139    292    -17       O  
ATOM   1154  CB  THR A 825     -32.953  17.426 -20.644  1.00 37.50           C  
ANISOU 1154  CB  THR A 825     4604   4669   4977   -172    275      8       C  
ATOM   1155  OG1 THR A 825     -33.836  17.039 -19.580  1.00 38.91           O  
ANISOU 1155  OG1 THR A 825     4791   4839   5154   -154    233    -23       O  
ATOM   1156  CG2 THR A 825     -32.591  18.922 -20.538  1.00 39.44           C  
ANISOU 1156  CG2 THR A 825     4838   4872   5276   -198    286     34       C  
ATOM   1157  N   HIS A 826     -35.038  15.160 -22.227  1.00 34.20           N  
ANISOU 1157  N   HIS A 826     4254   4324   4418   -118    254      8       N  
ATOM   1158  CA  HIS A 826     -35.303  13.725 -22.360  1.00 33.58           C  
ANISOU 1158  CA  HIS A 826     4182   4277   4300    -97    241    -21       C  
ATOM   1159  C   HIS A 826     -35.548  13.426 -23.841  1.00 37.32           C  
ANISOU 1159  C   HIS A 826     4679   4782   4719    -86    260      3       C  
ATOM   1160  O   HIS A 826     -36.645  13.033 -24.245  1.00 42.24           O  
ANISOU 1160  O   HIS A 826     5327   5414   5307    -68    238      4       O  
ATOM   1161  CB  HIS A 826     -36.481  13.311 -21.491  1.00 30.74           C  
ANISOU 1161  CB  HIS A 826     3833   3905   3939    -82    201    -41       C  
ATOM   1162  CG  HIS A 826     -36.224  13.505 -20.028  1.00 31.85           C  
ANISOU 1162  CG  HIS A 826     3955   4022   4126    -87    183    -67       C  
ATOM   1163  ND1 HIS A 826     -37.211  13.851 -19.133  1.00 27.52           N  
ANISOU 1163  ND1 HIS A 826     3413   3451   3591    -82    154    -73       N  
ATOM   1164  CD2 HIS A 826     -35.071  13.442 -19.317  1.00 29.36           C  
ANISOU 1164  CD2 HIS A 826     3610   3702   3843    -97    190    -89       C  
ATOM   1165  CE1 HIS A 826     -36.672  13.991 -17.936  1.00 28.70           C  
ANISOU 1165  CE1 HIS A 826     3542   3585   3776    -86    145    -97       C  
ATOM   1166  NE2 HIS A 826     -35.381  13.737 -18.021  1.00 27.57           N  
ANISOU 1166  NE2 HIS A 826     3377   3451   3646    -95    164   -108       N  
ATOM   1167  N   ASN A 827     -34.501  13.591 -24.630  1.00 38.18           N  
ANISOU 1167  N   ASN A 827     4777   4910   4821    -97    299     18       N  
ATOM   1168  CA  ASN A 827     -34.593  13.503 -26.086  1.00 42.04           C  
ANISOU 1168  CA  ASN A 827     5288   5430   5255    -88    323     46       C  
ATOM   1169  C   ASN A 827     -34.368  12.149 -26.701  1.00 37.93           C  
ANISOU 1169  C   ASN A 827     4769   4953   4691    -67    327     16       C  
ATOM   1170  O   ASN A 827     -34.432  12.038 -27.913  1.00 39.97           O  
ANISOU 1170  O   ASN A 827     5047   5242   4900    -56    346     35       O  
ATOM   1171  CB  ASN A 827     -33.506  14.343 -26.726  1.00 47.97           C  
ANISOU 1171  CB  ASN A 827     6025   6184   6017   -110    372     80       C  
ATOM   1172  CG  ASN A 827     -33.573  15.782 -26.331  1.00 55.94           C  
ANISOU 1172  CG  ASN A 827     7033   7150   7072   -133    374    115       C  
ATOM   1173  OD1 ASN A 827     -32.783  16.240 -25.505  1.00 66.56           O  
ANISOU 1173  OD1 ASN A 827     8346   8469   8473   -154    381    105       O  
ATOM   1174  ND2 ASN A 827     -34.518  16.514 -26.902  1.00 61.90           N  
ANISOU 1174  ND2 ASN A 827     7821   7892   7806   -128    366    154       N  
ATOM   1175  N   ALA A 828     -34.030  11.164 -25.889  1.00 35.39           N  
ANISOU 1175  N   ALA A 828     4427   4633   4387    -61    310    -29       N  
ATOM   1176  CA  ALA A 828     -33.809   9.821 -26.366  1.00 34.84           C  
ANISOU 1176  CA  ALA A 828     4357   4598   4283    -40    309    -62       C  
ATOM   1177  C   ALA A 828     -35.042   9.179 -27.050  1.00 35.57           C  
ANISOU 1177  C   ALA A 828     4483   4706   4327    -15    282    -66       C  
ATOM   1178  O   ALA A 828     -34.878   8.210 -27.798  1.00 36.35           O  
ANISOU 1178  O   ALA A 828     4586   4838   4387      3    285    -88       O  
ATOM   1179  CB  ALA A 828     -33.333   8.940 -25.215  1.00 32.97           C  
ANISOU 1179  CB  ALA A 828     4095   4351   4081    -38    289   -107       C  
ATOM   1180  N   TYR A 829     -36.250   9.711 -26.812  1.00 32.97           N  
ANISOU 1180  N   TYR A 829     4175   4354   3999    -15    254    -49       N  
ATOM   1181  CA  TYR A 829     -37.465   9.130 -27.394  1.00 33.03           C  
ANISOU 1181  CA  TYR A 829     4210   4373   3968      8    224    -55       C  
ATOM   1182  C   TYR A 829     -38.607  10.148 -27.479  1.00 33.73           C  
ANISOU 1182  C   TYR A 829     4321   4440   4055      7    207    -21       C  
ATOM   1183  O   TYR A 829     -38.532  11.216 -26.879  1.00 35.10           O  
ANISOU 1183  O   TYR A 829     4488   4585   4264    -11    212      2       O  
ATOM   1184  CB  TYR A 829     -37.914   7.917 -26.565  1.00 32.21           C  
ANISOU 1184  CB  TYR A 829     4098   4261   3879     18    189    -99       C  
ATOM   1185  CG  TYR A 829     -38.165   8.233 -25.096  1.00 30.25           C  
ANISOU 1185  CG  TYR A 829     3837   3977   3682      4    171   -104       C  
ATOM   1186  CD1 TYR A 829     -39.348   8.833 -24.695  1.00 28.90           C  
ANISOU 1186  CD1 TYR A 829     3678   3782   3521      3    147    -90       C  
ATOM   1187  CD2 TYR A 829     -37.193   7.995 -24.126  1.00 29.47           C  
ANISOU 1187  CD2 TYR A 829     3711   3867   3619     -6    178   -124       C  
ATOM   1188  CE1 TYR A 829     -39.575   9.157 -23.372  1.00 28.75           C  
ANISOU 1188  CE1 TYR A 829     3646   3733   3544     -7    132    -95       C  
ATOM   1189  CE2 TYR A 829     -37.416   8.322 -22.807  1.00 29.18           C  
ANISOU 1189  CE2 TYR A 829     3664   3800   3623    -16    161   -129       C  
ATOM   1190  CZ  TYR A 829     -38.635   8.883 -22.436  1.00 28.49           C  
ANISOU 1190  CZ  TYR A 829     3591   3693   3541    -16    139   -115       C  
ATOM   1191  OH  TYR A 829     -38.893   9.288 -21.141  1.00 27.71           O  
ANISOU 1191  OH  TYR A 829     3483   3567   3479    -23    124   -120       O  
ATOM   1192  N   ASP A 830     -39.613   9.848 -28.298  1.00 34.50           N  
ANISOU 1192  N   ASP A 830     4444   4553   4111     27    185    -20       N  
ATOM   1193  CA  ASP A 830     -40.916  10.503 -28.246  1.00 34.77           C  
ANISOU 1193  CA  ASP A 830     4497   4567   4147     33    155     -1       C  
ATOM   1194  C   ASP A 830     -41.905   9.512 -27.753  1.00 31.69           C  
ANISOU 1194  C   ASP A 830     4105   4172   3763     45    116    -38       C  
ATOM   1195  O   ASP A 830     -41.692   8.328 -27.881  1.00 31.94           O  
ANISOU 1195  O   ASP A 830     4131   4223   3782     55    110    -71       O  
ATOM   1196  CB  ASP A 830     -41.474  10.798 -29.641  1.00 40.92           C  
ANISOU 1196  CB  ASP A 830     5308   5370   4871     52    154     25       C  
ATOM   1197  CG  ASP A 830     -40.733  11.821 -30.370  1.00 48.25           C  
ANISOU 1197  CG  ASP A 830     6246   6305   5782     42    192     70       C  
ATOM   1198  OD1 ASP A 830     -40.198  12.756 -29.730  1.00 54.92           O  
ANISOU 1198  OD1 ASP A 830     7076   7120   6669     18    211     93       O  
ATOM   1199  OD2 ASP A 830     -40.691  11.679 -31.604  1.00 54.56           O  
ANISOU 1199  OD2 ASP A 830     7067   7138   6525     60    203     83       O  
ATOM   1200  N   LEU A 831     -43.037  10.005 -27.305  1.00 30.82           N  
ANISOU 1200  N   LEU A 831     4000   4038   3670     46     88    -30       N  
ATOM   1201  CA  LEU A 831     -44.031   9.154 -26.789  1.00 31.11           C  
ANISOU 1201  CA  LEU A 831     4033   4069   3719     55     53    -61       C  
ATOM   1202  C   LEU A 831     -45.244   9.202 -27.673  1.00 31.43           C  
ANISOU 1202  C   LEU A 831     4094   4119   3729     75     24    -56       C  
ATOM   1203  O   LEU A 831     -45.640  10.256 -28.136  1.00 31.90           O  
ANISOU 1203  O   LEU A 831     4169   4173   3778     78     23    -23       O  
ATOM   1204  CB  LEU A 831     -44.436   9.573 -25.389  1.00 30.17           C  
ANISOU 1204  CB  LEU A 831     3897   3916   3649     41     42    -64       C  
ATOM   1205  CG  LEU A 831     -43.392   9.281 -24.314  1.00 31.92           C  
ANISOU 1205  CG  LEU A 831     4097   4128   3903     25     60    -79       C  
ATOM   1206  CD1 LEU A 831     -43.750   9.966 -23.011  1.00 33.13           C  
ANISOU 1206  CD1 LEU A 831     4237   4251   4098     14     52    -76       C  
ATOM   1207  CD2 LEU A 831     -43.204   7.765 -24.083  1.00 33.57           C  
ANISOU 1207  CD2 LEU A 831     4296   4349   4110     31     50   -116       C  
ATOM   1208  N   GLU A 832     -45.891   8.057 -27.792  1.00 30.08           N  
ANISOU 1208  N   GLU A 832     3921   3958   3551     88     -3    -90       N  
ATOM   1209  CA  GLU A 832     -47.135   7.962 -28.478  1.00 32.88           C  
ANISOU 1209  CA  GLU A 832     4289   4318   3885    107    -37    -95       C  
ATOM   1210  C   GLU A 832     -48.100   7.175 -27.607  1.00 30.07           C  
ANISOU 1210  C   GLU A 832     3915   3944   3565    105    -67   -125       C  
ATOM   1211  O   GLU A 832     -47.801   6.054 -27.179  1.00 26.14           O  
ANISOU 1211  O   GLU A 832     3403   3447   3080    100    -68   -155       O  
ATOM   1212  CB  GLU A 832     -46.870   7.259 -29.806  1.00 36.33           C  
ANISOU 1212  CB  GLU A 832     4743   4792   4268    128    -38   -108       C  
ATOM   1213  CG  GLU A 832     -48.083   6.762 -30.536  1.00 42.26           C  
ANISOU 1213  CG  GLU A 832     5505   5554   4998    152    -81   -128       C  
ATOM   1214  CD  GLU A 832     -47.738   6.114 -31.876  1.00 50.27           C  
ANISOU 1214  CD  GLU A 832     6539   6608   5955    176    -82   -144       C  
ATOM   1215  OE1 GLU A 832     -46.572   5.650 -32.096  1.00 51.02           O  
ANISOU 1215  OE1 GLU A 832     6632   6722   6033    174    -52   -152       O  
ATOM   1216  OE2 GLU A 832     -48.676   6.065 -32.705  1.00 61.00           O  
ANISOU 1216  OE2 GLU A 832     7912   7979   7285    199   -115   -151       O  
ATOM   1217  N   VAL A 833     -49.273   7.763 -27.352  1.00 29.90           N  
ANISOU 1217  N   VAL A 833     3892   3907   3561    107    -91   -117       N  
ATOM   1218  CA  VAL A 833     -50.283   7.099 -26.527  1.00 28.24           C  
ANISOU 1218  CA  VAL A 833     3662   3680   3386    104   -116   -143       C  
ATOM   1219  C   VAL A 833     -50.972   6.074 -27.382  1.00 27.37           C  
ANISOU 1219  C   VAL A 833     3555   3587   3258    121   -147   -173       C  
ATOM   1220  O   VAL A 833     -51.516   6.400 -28.417  1.00 28.83           O  
ANISOU 1220  O   VAL A 833     3756   3786   3411    140   -167   -167       O  
ATOM   1221  CB  VAL A 833     -51.303   8.112 -25.956  1.00 27.17           C  
ANISOU 1221  CB  VAL A 833     3520   3524   3278    102   -129   -127       C  
ATOM   1222  CG1 VAL A 833     -52.399   7.412 -25.166  1.00 26.91           C  
ANISOU 1222  CG1 VAL A 833     3465   3479   3282     98   -152   -153       C  
ATOM   1223  CG2 VAL A 833     -50.586   9.123 -25.068  1.00 27.43           C  
ANISOU 1223  CG2 VAL A 833     3549   3539   3334     86   -101   -103       C  
ATOM   1224  N   ILE A 834     -50.996   4.839 -26.933  1.00 28.87           N  
ANISOU 1224  N   ILE A 834     3729   3772   3467    115   -155   -204       N  
ATOM   1225  CA  ILE A 834     -51.676   3.779 -27.682  1.00 29.40           C  
ANISOU 1225  CA  ILE A 834     3796   3849   3525    130   -188   -238       C  
ATOM   1226  C   ILE A 834     -53.066   3.596 -27.130  1.00 31.55           C  
ANISOU 1226  C   ILE A 834     4048   4102   3836    126   -217   -250       C  
ATOM   1227  O   ILE A 834     -54.027   3.717 -27.862  1.00 37.37           O  
ANISOU 1227  O   ILE A 834     4788   4846   4564    142   -248   -258       O  
ATOM   1228  CB  ILE A 834     -50.896   2.453 -27.602  1.00 28.97           C  
ANISOU 1228  CB  ILE A 834     3735   3797   3473    127   -182   -267       C  
ATOM   1229  CG1 ILE A 834     -49.558   2.605 -28.288  1.00 30.44           C  
ANISOU 1229  CG1 ILE A 834     3939   4008   3618    134   -154   -259       C  
ATOM   1230  CG2 ILE A 834     -51.678   1.313 -28.262  1.00 28.73           C  
ANISOU 1230  CG2 ILE A 834     3701   3771   3443    141   -221   -307       C  
ATOM   1231  CD1 ILE A 834     -48.636   1.436 -27.991  1.00 34.28           C  
ANISOU 1231  CD1 ILE A 834     4416   4494   4115    130   -144   -286       C  
ATOM   1232  N   ASP A 835     -53.162   3.277 -25.834  1.00 31.78           N  
ANISOU 1232  N   ASP A 835     4056   4109   3910    105   -206   -252       N  
ATOM   1233  CA  ASP A 835     -54.437   3.118 -25.146  1.00 30.61           C  
ANISOU 1233  CA  ASP A 835     3885   3943   3804     97   -225   -261       C  
ATOM   1234  C   ASP A 835     -54.446   3.907 -23.844  1.00 28.69           C  
ANISOU 1234  C   ASP A 835     3629   3682   3588     80   -201   -238       C  
ATOM   1235  O   ASP A 835     -53.428   4.025 -23.156  1.00 25.24           O  
ANISOU 1235  O   ASP A 835     3197   3242   3152     69   -173   -226       O  
ATOM   1236  CB  ASP A 835     -54.695   1.658 -24.796  1.00 33.50           C  
ANISOU 1236  CB  ASP A 835     4234   4297   4199     87   -237   -291       C  
ATOM   1237  CG  ASP A 835     -54.900   0.778 -26.023  1.00 39.32           C  
ANISOU 1237  CG  ASP A 835     4977   5047   4917    104   -268   -323       C  
ATOM   1238  OD1 ASP A 835     -54.260  -0.314 -26.059  1.00 40.89           O  
ANISOU 1238  OD1 ASP A 835     5176   5242   5118    102   -267   -343       O  
ATOM   1239  OD2 ASP A 835     -55.684   1.165 -26.935  1.00 35.92           O  
ANISOU 1239  OD2 ASP A 835     4551   4628   4469    123   -296   -329       O  
ATOM   1240  N   ILE A 836     -55.635   4.382 -23.484  1.00 27.64           N  
ANISOU 1240  N   ILE A 836     3480   3541   3479     80   -215   -236       N  
ATOM   1241  CA  ILE A 836     -55.881   5.019 -22.208  1.00 25.48           C  
ANISOU 1241  CA  ILE A 836     3192   3253   3236     67   -197   -222       C  
ATOM   1242  C   ILE A 836     -56.938   4.208 -21.483  1.00 24.98           C  
ANISOU 1242  C   ILE A 836     3100   3179   3213     56   -207   -240       C  
ATOM   1243  O   ILE A 836     -58.023   4.015 -21.984  1.00 26.24           O  
ANISOU 1243  O   ILE A 836     3246   3339   3384     63   -234   -254       O  
ATOM   1244  CB  ILE A 836     -56.363   6.452 -22.389  1.00 24.89           C  
ANISOU 1244  CB  ILE A 836     3122   3178   3157     79   -202   -203       C  
ATOM   1245  CG1 ILE A 836     -55.345   7.251 -23.199  1.00 25.30           C  
ANISOU 1245  CG1 ILE A 836     3203   3239   3170     88   -192   -181       C  
ATOM   1246  CG2 ILE A 836     -56.538   7.115 -21.039  1.00 26.02           C  
ANISOU 1246  CG2 ILE A 836     3250   3308   3329     68   -183   -193       C  
ATOM   1247  CD1 ILE A 836     -55.839   8.621 -23.622  1.00 24.93           C  
ANISOU 1247  CD1 ILE A 836     3166   3189   3116    103   -202   -161       C  
ATOM   1248  N   PHE A 837     -56.624   3.790 -20.270  1.00 24.21           N  
ANISOU 1248  N   PHE A 837     2992   3070   3136     39   -183   -236       N  
ATOM   1249  CA  PHE A 837     -57.543   3.077 -19.444  1.00 23.33           C  
ANISOU 1249  CA  PHE A 837     2854   2948   3063     25   -184   -245       C  
ATOM   1250  C   PHE A 837     -57.893   3.887 -18.206  1.00 22.83           C  
ANISOU 1250  C   PHE A 837     2777   2880   3016     19   -163   -231       C  
ATOM   1251  O   PHE A 837     -57.029   4.448 -17.546  1.00 21.24           O  
ANISOU 1251  O   PHE A 837     2587   2679   2803     17   -140   -216       O  
ATOM   1252  CB  PHE A 837     -56.909   1.738 -19.031  1.00 24.42           C  
ANISOU 1252  CB  PHE A 837     2993   3076   3209     11   -175   -253       C  
ATOM   1253  CG  PHE A 837     -56.490   0.866 -20.197  1.00 24.48           C  
ANISOU 1253  CG  PHE A 837     3013   3088   3201     19   -196   -272       C  
ATOM   1254  CD1 PHE A 837     -57.402   0.011 -20.806  1.00 24.52           C  
ANISOU 1254  CD1 PHE A 837     3003   3087   3226     19   -224   -296       C  
ATOM   1255  CD2 PHE A 837     -55.188   0.887 -20.656  1.00 24.67           C  
ANISOU 1255  CD2 PHE A 837     3061   3121   3192     27   -186   -269       C  
ATOM   1256  CE1 PHE A 837     -57.016  -0.811 -21.845  1.00 25.62           C  
ANISOU 1256  CE1 PHE A 837     3153   3230   3350     29   -246   -319       C  
ATOM   1257  CE2 PHE A 837     -54.783   0.049 -21.693  1.00 26.21           C  
ANISOU 1257  CE2 PHE A 837     3266   3321   3370     36   -204   -291       C  
ATOM   1258  CZ  PHE A 837     -55.706  -0.795 -22.292  1.00 26.00           C  
ANISOU 1258  CZ  PHE A 837     3227   3290   3361     39   -234   -316       C  
ATOM   1259  N   LYS A 838     -59.158   3.828 -17.829  1.00 24.95           N  
ANISOU 1259  N   LYS A 838     3018   3146   3315     15   -169   -238       N  
ATOM   1260  CA  LYS A 838     -59.629   4.329 -16.553  1.00 27.01           C  
ANISOU 1260  CA  LYS A 838     3262   3405   3596      8   -147   -229       C  
ATOM   1261  C   LYS A 838     -59.647   3.196 -15.566  1.00 25.39           C  
ANISOU 1261  C   LYS A 838     3044   3193   3411    -12   -128   -228       C  
ATOM   1262  O   LYS A 838     -60.234   2.144 -15.842  1.00 27.73           O  
ANISOU 1262  O   LYS A 838     3326   3481   3730    -22   -140   -239       O  
ATOM   1263  CB  LYS A 838     -61.021   4.915 -16.702  1.00 31.27           C  
ANISOU 1263  CB  LYS A 838     3775   3948   4159     16   -163   -238       C  
ATOM   1264  CG  LYS A 838     -61.459   5.880 -15.596  1.00 33.75           C  
ANISOU 1264  CG  LYS A 838     4075   4265   4485     19   -143   -231       C  
ATOM   1265  CD  LYS A 838     -62.624   6.753 -16.080  1.00 39.62           C  
ANISOU 1265  CD  LYS A 838     4799   5012   5243     36   -165   -241       C  
ATOM   1266  CE  LYS A 838     -62.778   8.085 -15.333  1.00 44.08           C  
ANISOU 1266  CE  LYS A 838     5360   5579   5810     48   -153   -235       C  
ATOM   1267  NZ  LYS A 838     -62.468   8.043 -13.876  1.00 47.96           N  
ANISOU 1267  NZ  LYS A 838     5845   6073   6304     37   -117   -229       N  
ATOM   1268  N   ILE A 839     -59.000   3.368 -14.425  1.00 23.16           N  
ANISOU 1268  N   ILE A 839     2768   2910   3121    -17   -100   -214       N  
ATOM   1269  CA  ILE A 839     -58.869   2.248 -13.462  1.00 24.12           C  
ANISOU 1269  CA  ILE A 839     2885   3025   3256    -34    -80   -207       C  
ATOM   1270  C   ILE A 839     -59.432   2.564 -12.060  1.00 23.92           C  
ANISOU 1270  C   ILE A 839     2842   3004   3241    -40    -53   -196       C  
ATOM   1271  O   ILE A 839     -59.282   3.671 -11.571  1.00 24.85           O  
ANISOU 1271  O   ILE A 839     2964   3132   3347    -29    -43   -193       O  
ATOM   1272  CB  ILE A 839     -57.401   1.788 -13.330  1.00 23.31           C  
ANISOU 1272  CB  ILE A 839     2810   2917   3130    -35    -73   -201       C  
ATOM   1273  CG1 ILE A 839     -56.479   2.928 -12.974  1.00 22.72           C  
ANISOU 1273  CG1 ILE A 839     2753   2851   3030    -24    -61   -193       C  
ATOM   1274  CG2 ILE A 839     -56.937   1.157 -14.632  1.00 24.62           C  
ANISOU 1274  CG2 ILE A 839     2988   3078   3287    -32    -97   -214       C  
ATOM   1275  CD1 ILE A 839     -55.072   2.453 -12.643  1.00 23.69           C  
ANISOU 1275  CD1 ILE A 839     2896   2970   3135    -25    -52   -188       C  
ATOM   1276  N   GLU A 840     -60.052   1.579 -11.436  1.00 24.38           N  
ANISOU 1276  N   GLU A 840     2883   3056   3324    -57    -40   -191       N  
ATOM   1277  CA  GLU A 840     -60.552   1.707 -10.082  1.00 27.39           C  
ANISOU 1277  CA  GLU A 840     3249   3445   3711    -63     -9   -179       C  
ATOM   1278  C   GLU A 840     -60.127   0.456  -9.323  1.00 27.01           C  
ANISOU 1278  C   GLU A 840     3209   3386   3666    -79      8   -162       C  
ATOM   1279  O   GLU A 840     -60.676  -0.642  -9.536  1.00 27.39           O  
ANISOU 1279  O   GLU A 840     3243   3420   3745    -97      5   -160       O  
ATOM   1280  CB  GLU A 840     -62.090   1.813 -10.048  1.00 30.04           C  
ANISOU 1280  CB  GLU A 840     3545   3786   4081    -68     -7   -186       C  
ATOM   1281  CG  GLU A 840     -62.668   2.958 -10.861  1.00 34.67           C  
ANISOU 1281  CG  GLU A 840     4121   4381   4670    -51    -30   -204       C  
ATOM   1282  CD  GLU A 840     -64.208   2.899 -11.024  1.00 43.13           C  
ANISOU 1282  CD  GLU A 840     5150   5455   5782    -56    -35   -216       C  
ATOM   1283  OE1 GLU A 840     -64.869   1.901 -10.618  1.00 46.46           O  
ANISOU 1283  OE1 GLU A 840     5548   5871   6233    -77    -22   -212       O  
ATOM   1284  OE2 GLU A 840     -64.773   3.862 -11.575  1.00 47.39           O  
ANISOU 1284  OE2 GLU A 840     5679   6001   6325    -39    -54   -230       O  
ATOM   1285  N   ARG A 841     -59.145   0.604  -8.459  1.00 25.15           N  
ANISOU 1285  N   ARG A 841     2997   3156   3403    -73     25   -149       N  
ATOM   1286  CA  ARG A 841     -58.736  -0.501  -7.600  1.00 26.51           C  
ANISOU 1286  CA  ARG A 841     3180   3319   3575    -85     42   -129       C  
ATOM   1287  C   ARG A 841     -59.731  -0.722  -6.439  1.00 27.36           C  
ANISOU 1287  C   ARG A 841     3266   3434   3694    -96     74   -112       C  
ATOM   1288  O   ARG A 841     -60.114   0.192  -5.768  1.00 28.34           O  
ANISOU 1288  O   ARG A 841     3381   3580   3807    -86     91   -112       O  
ATOM   1289  CB  ARG A 841     -57.349  -0.234  -6.994  1.00 25.44           C  
ANISOU 1289  CB  ARG A 841     3075   3188   3402    -72     47   -123       C  
ATOM   1290  CG  ARG A 841     -56.191  -0.179  -7.977  1.00 24.99           C  
ANISOU 1290  CG  ARG A 841     3039   3123   3332    -63     23   -136       C  
ATOM   1291  CD  ARG A 841     -54.948  -0.842  -7.369  1.00 28.25           C  
ANISOU 1291  CD  ARG A 841     3478   3530   3728    -60     26   -126       C  
ATOM   1292  NE  ARG A 841     -54.704  -0.265  -6.098  1.00 29.68           N  
ANISOU 1292  NE  ARG A 841     3665   3725   3886    -51     46   -116       N  
ATOM   1293  CZ  ARG A 841     -54.767  -0.827  -4.907  1.00 27.13           C  
ANISOU 1293  CZ  ARG A 841     3347   3404   3556    -53     66    -97       C  
ATOM   1294  NH1 ARG A 841     -54.861  -2.122  -4.699  1.00 25.84           N  
ANISOU 1294  NH1 ARG A 841     3188   3223   3406    -67     69    -79       N  
ATOM   1295  NH2 ARG A 841     -54.600  -0.006  -3.895  1.00 28.48           N  
ANISOU 1295  NH2 ARG A 841     3523   3595   3702    -40     80    -95       N  
ATOM   1296  N   GLU A 842     -60.105  -1.964  -6.212  1.00 29.52           N  
ANISOU 1296  N   GLU A 842     3532   3691   3993   -117     83    -96       N  
ATOM   1297  CA  GLU A 842     -60.911  -2.362  -5.090  1.00 33.14           C  
ANISOU 1297  CA  GLU A 842     3974   4156   4463   -131    118    -72       C  
ATOM   1298  C   GLU A 842     -60.332  -1.852  -3.780  1.00 31.36           C  
ANISOU 1298  C   GLU A 842     3769   3952   4194   -116    145    -56       C  
ATOM   1299  O   GLU A 842     -59.148  -2.056  -3.476  1.00 29.40           O  
ANISOU 1299  O   GLU A 842     3553   3700   3918   -106    139    -49       O  
ATOM   1300  CB  GLU A 842     -60.931  -3.898  -5.094  1.00 41.12           C  
ANISOU 1300  CB  GLU A 842     4986   5136   5501   -154    119    -53       C  
ATOM   1301  CG  GLU A 842     -61.780  -4.659  -4.078  1.00 50.95           C  
ANISOU 1301  CG  GLU A 842     6214   6378   6768   -176    155    -21       C  
ATOM   1302  CD  GLU A 842     -62.209  -6.082  -4.613  1.00 65.28           C  
ANISOU 1302  CD  GLU A 842     8015   8154   8635   -205    144    -14       C  
ATOM   1303  OE1 GLU A 842     -62.525  -6.202  -5.829  1.00 72.74           O  
ANISOU 1303  OE1 GLU A 842     8944   9084   9611   -209    112    -42       O  
ATOM   1304  OE2 GLU A 842     -62.268  -7.102  -3.852  1.00 71.37           O  
ANISOU 1304  OE2 GLU A 842     8792   8907   9419   -223    166     20       O  
ATOM   1305  N   GLY A 843     -61.160  -1.139  -3.024  1.00 28.12           N  
ANISOU 1305  N   GLY A 843     3339   3568   3779   -111    171    -55       N  
ATOM   1306  CA  GLY A 843     -60.752  -0.694  -1.710  1.00 27.81           C  
ANISOU 1306  CA  GLY A 843     3316   3552   3698    -96    198    -42       C  
ATOM   1307  C   GLY A 843     -60.033   0.634  -1.697  1.00 27.03           C  
ANISOU 1307  C   GLY A 843     3232   3470   3567    -68    184    -66       C  
ATOM   1308  O   GLY A 843     -59.876   1.236  -0.632  1.00 28.58           O  
ANISOU 1308  O   GLY A 843     3436   3691   3732    -51    203    -64       O  
ATOM   1309  N   GLU A 844     -59.654   1.149  -2.854  1.00 25.85           N  
ANISOU 1309  N   GLU A 844     3086   3310   3427    -62    151    -88       N  
ATOM   1310  CA  GLU A 844     -58.860   2.369  -2.844  1.00 26.65           C  
ANISOU 1310  CA  GLU A 844     3202   3422   3502    -39    138   -108       C  
ATOM   1311  C   GLU A 844     -59.668   3.616  -2.527  1.00 26.09           C  
ANISOU 1311  C   GLU A 844     3110   3372   3431    -24    147   -125       C  
ATOM   1312  O   GLU A 844     -59.150   4.529  -1.891  1.00 27.51           O  
ANISOU 1312  O   GLU A 844     3302   3566   3586     -4    149   -135       O  
ATOM   1313  CB  GLU A 844     -58.093   2.541  -4.152  1.00 27.45           C  
ANISOU 1313  CB  GLU A 844     3315   3504   3609    -37    104   -122       C  
ATOM   1314  CG  GLU A 844     -56.748   3.190  -3.960  1.00 29.16           C  
ANISOU 1314  CG  GLU A 844     3559   3724   3798    -20     93   -130       C  
ATOM   1315  CD  GLU A 844     -55.939   3.266  -5.258  1.00 29.55           C  
ANISOU 1315  CD  GLU A 844     3620   3757   3852    -20     65   -141       C  
ATOM   1316  OE1 GLU A 844     -56.433   3.960  -6.182  1.00 28.05           O  
ANISOU 1316  OE1 GLU A 844     3418   3564   3675    -18     51   -153       O  
ATOM   1317  OE2 GLU A 844     -54.818   2.681  -5.321  1.00 28.40           O  
ANISOU 1317  OE2 GLU A 844     3495   3602   3695    -20     57   -137       O  
ATOM   1318  N   CYS A 845     -60.904   3.673  -2.988  1.00 25.80           N  
ANISOU 1318  N   CYS A 845     3041   3337   3426    -32    149   -130       N  
ATOM   1319  CA  CYS A 845     -61.773   4.808  -2.701  1.00 29.04           C  
ANISOU 1319  CA  CYS A 845     3428   3767   3841    -17    157   -148       C  
ATOM   1320  C   CYS A 845     -61.941   4.957  -1.189  1.00 27.03           C  
ANISOU 1320  C   CYS A 845     3171   3539   3559     -8    193   -141       C  
ATOM   1321  O   CYS A 845     -61.832   6.029  -0.644  1.00 24.83           O  
ANISOU 1321  O   CYS A 845     2896   3278   3263     15    195   -158       O  
ATOM   1322  CB  CYS A 845     -63.163   4.634  -3.368  1.00 29.73           C  
ANISOU 1322  CB  CYS A 845     3475   3851   3969    -29    155   -155       C  
ATOM   1323  SG  CYS A 845     -64.424   5.832  -2.901  1.00 35.40           S  
ANISOU 1323  SG  CYS A 845     4156   4595   4700    -11    169   -177       S  
ATOM   1324  N   GLN A 846     -62.242   3.847  -0.545  1.00 28.42           N  
ANISOU 1324  N   GLN A 846     3345   3719   3735    -25    221   -115       N  
ATOM   1325  CA  GLN A 846     -62.434   3.832   0.892  1.00 30.39           C  
ANISOU 1325  CA  GLN A 846     3595   3996   3954    -17    259   -102       C  
ATOM   1326  C   GLN A 846     -61.164   4.236   1.583  1.00 27.04           C  
ANISOU 1326  C   GLN A 846     3209   3581   3485      5    252   -105       C  
ATOM   1327  O   GLN A 846     -61.181   5.003   2.548  1.00 26.34           O  
ANISOU 1327  O   GLN A 846     3122   3518   3367     28    267   -117       O  
ATOM   1328  CB  GLN A 846     -62.942   2.442   1.355  1.00 32.63           C  
ANISOU 1328  CB  GLN A 846     3871   4277   4248    -43    290    -66       C  
ATOM   1329  CG  GLN A 846     -63.342   2.350   2.815  1.00 36.03           C  
ANISOU 1329  CG  GLN A 846     4300   4741   4648    -37    336    -47       C  
ATOM   1330  CD  GLN A 846     -64.553   3.222   3.183  1.00 41.56           C  
ANISOU 1330  CD  GLN A 846     4961   5472   5357    -26    361    -67       C  
ATOM   1331  OE1 GLN A 846     -65.490   3.422   2.382  1.00 39.79           O  
ANISOU 1331  OE1 GLN A 846     4700   5240   5177    -36    353    -82       O  
ATOM   1332  NE2 GLN A 846     -64.542   3.746   4.411  1.00 44.73           N  
ANISOU 1332  NE2 GLN A 846     5369   5910   5715     -3    389    -68       N  
ATOM   1333  N   ARG A 847     -60.049   3.717   1.109  1.00 26.85           N  
ANISOU 1333  N   ARG A 847     3213   3533   3455      0    228    -98       N  
ATOM   1334  CA  ARG A 847     -58.760   4.048   1.732  1.00 27.80           C  
ANISOU 1334  CA  ARG A 847     3368   3658   3537     20    218   -103       C  
ATOM   1335  C   ARG A 847     -58.422   5.522   1.517  1.00 25.87           C  
ANISOU 1335  C   ARG A 847     3123   3419   3289     43    197   -138       C  
ATOM   1336  O   ARG A 847     -57.901   6.181   2.400  1.00 25.42           O  
ANISOU 1336  O   ARG A 847     3079   3379   3201     66    199   -151       O  
ATOM   1337  CB  ARG A 847     -57.691   3.137   1.143  1.00 30.77           C  
ANISOU 1337  CB  ARG A 847     3769   4007   3916      9    196    -90       C  
ATOM   1338  CG  ARG A 847     -56.332   3.299   1.765  1.00 32.41           C  
ANISOU 1338  CG  ARG A 847     4008   4217   4087     28    184    -94       C  
ATOM   1339  CD  ARG A 847     -55.346   2.391   1.075  1.00 32.63           C  
ANISOU 1339  CD  ARG A 847     4056   4218   4124     17    162    -85       C  
ATOM   1340  NE  ARG A 847     -54.910   2.917  -0.220  1.00 34.46           N  
ANISOU 1340  NE  ARG A 847     4284   4433   4378     14    133   -106       N  
ATOM   1341  CZ  ARG A 847     -53.928   2.386  -0.958  1.00 35.15           C  
ANISOU 1341  CZ  ARG A 847     4385   4499   4471      9    111   -106       C  
ATOM   1342  NH1 ARG A 847     -53.285   1.315  -0.531  1.00 37.37           N  
ANISOU 1342  NH1 ARG A 847     4685   4771   4741      7    112    -89       N  
ATOM   1343  NH2 ARG A 847     -53.576   2.929  -2.103  1.00 35.08           N  
ANISOU 1343  NH2 ARG A 847     4372   4478   4478      8     90   -124       N  
ATOM   1344  N   TYR A 848     -58.750   6.059   0.344  1.00 24.64           N  
ANISOU 1344  N   TYR A 848     2950   3246   3164     38    176   -153       N  
ATOM   1345  CA  TYR A 848     -58.438   7.461   0.020  1.00 24.11           C  
ANISOU 1345  CA  TYR A 848     2883   3177   3100     57    154   -182       C  
ATOM   1346  C   TYR A 848     -59.347   8.476   0.748  1.00 25.44           C  
ANISOU 1346  C   TYR A 848     3030   3370   3267     77    169   -203       C  
ATOM   1347  O   TYR A 848     -59.024   9.653   0.826  1.00 25.40           O  
ANISOU 1347  O   TYR A 848     3028   3365   3259     97    154   -228       O  
ATOM   1348  CB  TYR A 848     -58.508   7.647  -1.492  1.00 23.14           C  
ANISOU 1348  CB  TYR A 848     2754   3030   3009     47    127   -187       C  
ATOM   1349  CG  TYR A 848     -58.088   8.986  -2.031  1.00 22.71           C  
ANISOU 1349  CG  TYR A 848     2702   2965   2961     62    102   -210       C  
ATOM   1350  CD1 TYR A 848     -56.760   9.388  -1.977  1.00 22.24           C  
ANISOU 1350  CD1 TYR A 848     2667   2896   2887     70     87   -216       C  
ATOM   1351  CD2 TYR A 848     -59.003   9.837  -2.635  1.00 22.46           C  
ANISOU 1351  CD2 TYR A 848     2650   2931   2954     69     92   -223       C  
ATOM   1352  CE1 TYR A 848     -56.351  10.593  -2.477  1.00 22.32           C  
ANISOU 1352  CE1 TYR A 848     2680   2893   2907     80     67   -233       C  
ATOM   1353  CE2 TYR A 848     -58.590  11.071  -3.156  1.00 23.13           C  
ANISOU 1353  CE2 TYR A 848     2740   3001   3046     82     69   -240       C  
ATOM   1354  CZ  TYR A 848     -57.267  11.447  -3.060  1.00 22.19           C  
ANISOU 1354  CZ  TYR A 848     2645   2872   2915     87     58   -243       C  
ATOM   1355  OH  TYR A 848     -56.796  12.625  -3.601  1.00 23.12           O  
ANISOU 1355  OH  TYR A 848     2769   2972   3045     96     36   -255       O  
ATOM   1356  N   LYS A 849     -60.470   8.017   1.257  1.00 28.72           N  
ANISOU 1356  N   LYS A 849     3422   3804   3685     71    199   -193       N  
ATOM   1357  CA  LYS A 849     -61.549   8.874   1.812  1.00 33.35           C  
ANISOU 1357  CA  LYS A 849     3981   4416   4276     88    216   -213       C  
ATOM   1358  C   LYS A 849     -61.090   9.975   2.760  1.00 33.06           C  
ANISOU 1358  C   LYS A 849     3955   4397   4211    120    215   -240       C  
ATOM   1359  O   LYS A 849     -61.490  11.117   2.593  1.00 35.01           O  
ANISOU 1359  O   LYS A 849     4186   4644   4472    138    202   -268       O  
ATOM   1360  CB  LYS A 849     -62.608   7.982   2.480  1.00 34.89           C  
ANISOU 1360  CB  LYS A 849     4153   4633   4471     75    257   -192       C  
ATOM   1361  CG  LYS A 849     -63.865   8.666   2.970  1.00 41.09           C  
ANISOU 1361  CG  LYS A 849     4902   5446   5266     89    280   -211       C  
ATOM   1362  CD  LYS A 849     -64.832   7.606   3.528  1.00 46.27           C  
ANISOU 1362  CD  LYS A 849     5534   6121   5925     68    325   -183       C  
ATOM   1363  CE  LYS A 849     -66.124   8.185   4.119  1.00 51.40           C  
ANISOU 1363  CE  LYS A 849     6142   6803   6583     81    356   -201       C  
ATOM   1364  NZ  LYS A 849     -66.752   9.191   3.226  1.00 54.15           N  
ANISOU 1364  NZ  LYS A 849     6463   7141   6971     93    327   -235       N  
ATOM   1365  N   PRO A 850     -60.236   9.652   3.737  1.00 33.54           N  
ANISOU 1365  N   PRO A 850     4043   4471   4231    129    224   -233       N  
ATOM   1366  CA  PRO A 850     -59.747  10.709   4.611  1.00 35.44           C  
ANISOU 1366  CA  PRO A 850     4294   4728   4445    160    218   -264       C  
ATOM   1367  C   PRO A 850     -59.015  11.841   3.880  1.00 37.55           C  
ANISOU 1367  C   PRO A 850     4568   4967   4733    170    177   -291       C  
ATOM   1368  O   PRO A 850     -58.989  12.976   4.368  1.00 41.53           O  
ANISOU 1368  O   PRO A 850     5068   5478   5233    196    168   -324       O  
ATOM   1369  CB  PRO A 850     -58.805   9.983   5.565  1.00 35.19           C  
ANISOU 1369  CB  PRO A 850     4293   4709   4368    165    226   -248       C  
ATOM   1370  CG  PRO A 850     -59.194   8.542   5.481  1.00 36.17           C  
ANISOU 1370  CG  PRO A 850     4417   4832   4492    138    251   -205       C  
ATOM   1371  CD  PRO A 850     -59.704   8.328   4.098  1.00 34.25           C  
ANISOU 1371  CD  PRO A 850     4154   4561   4298    112    238   -198       C  
ATOM   1372  N   PHE A 851     -58.460  11.552   2.708  1.00 35.56           N  
ANISOU 1372  N   PHE A 851     4324   4682   4505    150    154   -278       N  
ATOM   1373  CA  PHE A 851     -57.695  12.543   1.972  1.00 34.81           C  
ANISOU 1373  CA  PHE A 851     4237   4559   4429    156    120   -297       C  
ATOM   1374  C   PHE A 851     -58.511  13.220   0.862  1.00 32.11           C  
ANISOU 1374  C   PHE A 851     3874   4199   4127    152    105   -303       C  
ATOM   1375  O   PHE A 851     -58.066  14.189   0.273  1.00 31.36           O  
ANISOU 1375  O   PHE A 851     3783   4081   4050    159     79   -317       O  
ATOM   1376  CB  PHE A 851     -56.404  11.875   1.468  1.00 33.54           C  
ANISOU 1376  CB  PHE A 851     4102   4379   4264    140    104   -279       C  
ATOM   1377  CG  PHE A 851     -55.518  11.409   2.585  1.00 33.58           C  
ANISOU 1377  CG  PHE A 851     4128   4400   4231    150    111   -278       C  
ATOM   1378  CD1 PHE A 851     -54.788  12.320   3.335  1.00 36.10           C  
ANISOU 1378  CD1 PHE A 851     4457   4724   4537    173     97   -308       C  
ATOM   1379  CD2 PHE A 851     -55.430  10.067   2.917  1.00 34.02           C  
ANISOU 1379  CD2 PHE A 851     4195   4465   4266    137    128   -250       C  
ATOM   1380  CE1 PHE A 851     -53.966  11.901   4.381  1.00 34.15           C  
ANISOU 1380  CE1 PHE A 851     4230   4492   4252    186     99   -309       C  
ATOM   1381  CE2 PHE A 851     -54.639   9.641   3.970  1.00 33.16           C  
ANISOU 1381  CE2 PHE A 851     4108   4371   4120    149    132   -247       C  
ATOM   1382  CZ  PHE A 851     -53.905  10.558   4.703  1.00 33.44           C  
ANISOU 1382  CZ  PHE A 851     4152   4413   4138    175    117   -278       C  
ATOM   1383  N   LYS A 852     -59.694  12.697   0.594  1.00 32.13           N  
ANISOU 1383  N   LYS A 852     3853   4211   4142    142    121   -292       N  
ATOM   1384  CA  LYS A 852     -60.534  13.151  -0.517  1.00 37.27           C  
ANISOU 1384  CA  LYS A 852     4484   4846   4831    139    105   -296       C  
ATOM   1385  C   LYS A 852     -60.850  14.644  -0.528  1.00 36.70           C  
ANISOU 1385  C   LYS A 852     4402   4767   4777    164     88   -326       C  
ATOM   1386  O   LYS A 852     -61.091  15.209  -1.583  1.00 39.41           O  
ANISOU 1386  O   LYS A 852     4740   5087   5148    163     64   -328       O  
ATOM   1387  CB  LYS A 852     -61.862  12.342  -0.588  1.00 38.66           C  
ANISOU 1387  CB  LYS A 852     4630   5038   5020    126    128   -284       C  
ATOM   1388  N   GLN A 853     -60.827  15.257   0.642  1.00 36.81           N  
ANISOU 1388  N   GLN A 853     4413   4800   4773    187     98   -350       N  
ATOM   1389  CA  GLN A 853     -61.069  16.677   0.839  1.00 39.88           C  
ANISOU 1389  CA  GLN A 853     4793   5183   5178    214     82   -384       C  
ATOM   1390  C   GLN A 853     -59.902  17.458   1.411  1.00 36.26           C  
ANISOU 1390  C   GLN A 853     4357   4714   4708    230     66   -405       C  
ATOM   1391  O   GLN A 853     -60.081  18.605   1.817  1.00 35.91           O  
ANISOU 1391  O   GLN A 853     4305   4666   4675    255     54   -437       O  
ATOM   1392  CB  GLN A 853     -62.326  16.839   1.745  1.00 45.66           C  
ANISOU 1392  CB  GLN A 853     5494   5949   5906    233    109   -404       C  
ATOM   1393  CG  GLN A 853     -63.590  16.393   1.030  1.00 48.46           C  
ANISOU 1393  CG  GLN A 853     5818   6307   6287    221    116   -392       C  
ATOM   1394  CD  GLN A 853     -64.838  16.953   1.666  1.00 58.16           C  
ANISOU 1394  CD  GLN A 853     7010   7562   7525    244    133   -420       C  
ATOM   1395  OE1 GLN A 853     -65.568  17.754   1.070  1.00 61.55           O  
ANISOU 1395  OE1 GLN A 853     7419   7978   7990    258    113   -438       O  
ATOM   1396  NE2 GLN A 853     -65.106  16.515   2.894  1.00 63.06           N  
ANISOU 1396  NE2 GLN A 853     7624   8222   8115    251    172   -423       N  
ATOM   1397  N   LEU A 854     -58.700  16.875   1.448  1.00 36.69           N  
ANISOU 1397  N   LEU A 854     4436   4761   4742    216     63   -389       N  
ATOM   1398  CA  LEU A 854     -57.484  17.670   1.593  1.00 33.08           C  
ANISOU 1398  CA  LEU A 854     3998   4283   4287    225     38   -407       C  
ATOM   1399  C   LEU A 854     -57.466  18.575   0.381  1.00 30.89           C  
ANISOU 1399  C   LEU A 854     3719   3966   4052    220     10   -406       C  
ATOM   1400  O   LEU A 854     -57.908  18.214  -0.708  1.00 29.78           O  
ANISOU 1400  O   LEU A 854     3574   3814   3927    204      8   -382       O  
ATOM   1401  CB  LEU A 854     -56.247  16.764   1.602  1.00 36.83           C  
ANISOU 1401  CB  LEU A 854     4497   4755   4741    207     39   -386       C  
ATOM   1402  CG  LEU A 854     -54.986  17.138   2.368  1.00 36.15           C  
ANISOU 1402  CG  LEU A 854     4428   4666   4640    219     25   -407       C  
ATOM   1403  CD1 LEU A 854     -55.305  17.534   3.803  1.00 39.23           C  
ANISOU 1403  CD1 LEU A 854     4814   5088   5004    250     35   -439       C  
ATOM   1404  CD2 LEU A 854     -54.028  15.957   2.356  1.00 37.16           C  
ANISOU 1404  CD2 LEU A 854     4576   4798   4745    201     30   -382       C  
ATOM   1405  N   HIS A 855     -56.886  19.733   0.543  1.00 29.84           N  
ANISOU 1405  N   HIS A 855     3590   3811   3936    235    -12   -431       N  
ATOM   1406  CA  HIS A 855     -56.711  20.633  -0.570  1.00 28.52           C  
ANISOU 1406  CA  HIS A 855     3425   3603   3808    230    -38   -426       C  
ATOM   1407  C   HIS A 855     -55.478  20.220  -1.400  1.00 29.26           C  
ANISOU 1407  C   HIS A 855     3540   3675   3903    204    -46   -398       C  
ATOM   1408  O   HIS A 855     -54.726  19.285  -1.040  1.00 28.46           O  
ANISOU 1408  O   HIS A 855     3450   3589   3775    192    -34   -389       O  
ATOM   1409  CB  HIS A 855     -56.519  22.047  -0.036  1.00 28.88           C  
ANISOU 1409  CB  HIS A 855     3468   3629   3878    254    -59   -463       C  
ATOM   1410  CG  HIS A 855     -55.288  22.213   0.815  1.00 27.78           C  
ANISOU 1410  CG  HIS A 855     3341   3488   3726    259    -66   -483       C  
ATOM   1411  ND1 HIS A 855     -55.088  21.531   2.001  1.00 30.02           N  
ANISOU 1411  ND1 HIS A 855     3628   3810   3969    269    -49   -497       N  
ATOM   1412  CD2 HIS A 855     -54.185  22.969   0.640  1.00 27.79           C  
ANISOU 1412  CD2 HIS A 855     3352   3455   3752    255    -89   -493       C  
ATOM   1413  CE1 HIS A 855     -53.927  21.880   2.534  1.00 27.43           C  
ANISOU 1413  CE1 HIS A 855     3310   3471   3639    273    -64   -517       C  
ATOM   1414  NE2 HIS A 855     -53.363  22.754   1.729  1.00 27.85           N  
ANISOU 1414  NE2 HIS A 855     3366   3481   3736    264    -88   -516       N  
ATOM   1415  N   ASN A 856     -55.290  20.899  -2.528  1.00 28.80           N  
ANISOU 1415  N   ASN A 856     3486   3581   3875    195    -65   -385       N  
ATOM   1416  CA  ASN A 856     -54.131  20.687  -3.366  1.00 27.34           C  
ANISOU 1416  CA  ASN A 856     3318   3375   3694    173    -70   -361       C  
ATOM   1417  C   ASN A 856     -53.991  19.204  -3.804  1.00 26.95           C  
ANISOU 1417  C   ASN A 856     3276   3347   3617    152    -53   -332       C  
ATOM   1418  O   ASN A 856     -52.964  18.531  -3.602  1.00 26.44           O  
ANISOU 1418  O   ASN A 856     3222   3288   3535    140    -47   -327       O  
ATOM   1419  CB  ASN A 856     -52.892  21.194  -2.650  1.00 28.93           C  
ANISOU 1419  CB  ASN A 856     3526   3564   3901    175    -79   -381       C  
ATOM   1420  CG  ASN A 856     -51.675  21.223  -3.551  1.00 30.66           C  
ANISOU 1420  CG  ASN A 856     3757   3758   4134    152    -85   -359       C  
ATOM   1421  OD1 ASN A 856     -51.793  21.211  -4.775  1.00 32.89           O  
ANISOU 1421  OD1 ASN A 856     4046   4025   4426    138    -86   -330       O  
ATOM   1422  ND2 ASN A 856     -50.502  21.213  -2.951  1.00 31.76           N  
ANISOU 1422  ND2 ASN A 856     3900   3894   4272    149    -88   -374       N  
ATOM   1423  N   ARG A 857     -55.040  18.732  -4.465  1.00 25.82           N  
ANISOU 1423  N   ARG A 857     3125   3212   3472    148    -48   -317       N  
ATOM   1424  CA  ARG A 857     -55.082  17.430  -5.084  1.00 24.55           C  
ANISOU 1424  CA  ARG A 857     2969   3065   3293    129    -37   -292       C  
ATOM   1425  C   ARG A 857     -54.675  17.541  -6.537  1.00 23.51           C  
ANISOU 1425  C   ARG A 857     2849   2910   3172    115    -50   -267       C  
ATOM   1426  O   ARG A 857     -55.219  18.336  -7.265  1.00 22.24           O  
ANISOU 1426  O   ARG A 857     2687   2734   3031    122    -64   -263       O  
ATOM   1427  CB  ARG A 857     -56.459  16.830  -4.940  1.00 25.05           C  
ANISOU 1427  CB  ARG A 857     3015   3151   3352    133    -26   -291       C  
ATOM   1428  CG  ARG A 857     -56.625  16.287  -3.541  1.00 27.81           C  
ANISOU 1428  CG  ARG A 857     3357   3529   3680    140     -4   -305       C  
ATOM   1429  CD  ARG A 857     -58.020  16.066  -3.042  1.00 28.62           C  
ANISOU 1429  CD  ARG A 857     3436   3655   3782    149     11   -313       C  
ATOM   1430  NE  ARG A 857     -59.005  16.234  -4.064  1.00 35.65           N  
ANISOU 1430  NE  ARG A 857     4313   4537   4697    148     -1   -307       N  
ATOM   1431  CZ  ARG A 857     -59.913  17.190  -4.088  1.00 39.95           C  
ANISOU 1431  CZ  ARG A 857     4839   5077   5263    167    -10   -324       C  
ATOM   1432  NH1 ARG A 857     -60.019  18.077  -3.099  1.00 47.09           N  
ANISOU 1432  NH1 ARG A 857     5736   5987   6169    189     -8   -352       N  
ATOM   1433  NH2 ARG A 857     -60.729  17.249  -5.126  1.00 42.04           N  
ANISOU 1433  NH2 ARG A 857     5093   5333   5548    165    -25   -316       N  
ATOM   1434  N   ARG A 858     -53.737  16.691  -6.964  1.00 23.84           N  
ANISOU 1434  N   ARG A 858     2904   2954   3198     98    -43   -251       N  
ATOM   1435  CA  ARG A 858     -53.136  16.842  -8.276  1.00 24.93           C  
ANISOU 1435  CA  ARG A 858     3056   3075   3342     86    -52   -230       C  
ATOM   1436  C   ARG A 858     -53.054  15.502  -9.009  1.00 22.74           C  
ANISOU 1436  C   ARG A 858     2785   2811   3044     71    -45   -212       C  
ATOM   1437  O   ARG A 858     -52.733  14.464  -8.398  1.00 21.22           O  
ANISOU 1437  O   ARG A 858     2592   2634   2834     65    -33   -216       O  
ATOM   1438  CB  ARG A 858     -51.733  17.405  -8.117  1.00 27.80           C  
ANISOU 1438  CB  ARG A 858     3429   3421   3713     80    -53   -232       C  
ATOM   1439  CG  ARG A 858     -51.425  18.485  -9.113  1.00 34.78           C  
ANISOU 1439  CG  ARG A 858     4320   4276   4619     77    -64   -217       C  
ATOM   1440  CD  ARG A 858     -50.147  19.291  -8.822  1.00 38.08           C  
ANISOU 1440  CD  ARG A 858     4741   4672   5057     71    -66   -223       C  
ATOM   1441  NE  ARG A 858     -50.350  20.365  -7.841  1.00 45.99           N  
ANISOU 1441  NE  ARG A 858     5733   5659   6081     86    -77   -249       N  
ATOM   1442  CZ  ARG A 858     -49.458  21.316  -7.543  1.00 44.74           C  
ANISOU 1442  CZ  ARG A 858     5573   5474   5951     84    -85   -260       C  
ATOM   1443  NH1 ARG A 858     -48.282  21.366  -8.159  1.00 45.62           N  
ANISOU 1443  NH1 ARG A 858     5691   5572   6072     65    -80   -244       N  
ATOM   1444  NH2 ARG A 858     -49.747  22.217  -6.605  1.00 40.39           N  
ANISOU 1444  NH2 ARG A 858     5013   4913   5421    102    -97   -290       N  
ATOM   1445  N   LEU A 859     -53.305  15.554 -10.323  1.00 21.10           N  
ANISOU 1445  N   LEU A 859     2584   2596   2837     67    -54   -195       N  
ATOM   1446  CA  LEU A 859     -53.138  14.424 -11.191  1.00 20.34           C  
ANISOU 1446  CA  LEU A 859     2495   2510   2722     56    -52   -181       C  
ATOM   1447  C   LEU A 859     -51.690  14.383 -11.691  1.00 19.69           C  
ANISOU 1447  C   LEU A 859     2428   2421   2632     45    -46   -171       C  
ATOM   1448  O   LEU A 859     -51.265  15.198 -12.517  1.00 21.33           O  
ANISOU 1448  O   LEU A 859     2645   2613   2845     43    -51   -157       O  
ATOM   1449  CB  LEU A 859     -54.139  14.488 -12.338  1.00 22.21           C  
ANISOU 1449  CB  LEU A 859     2732   2746   2960     61    -67   -171       C  
ATOM   1450  CG  LEU A 859     -54.381  13.157 -13.072  1.00 21.51           C  
ANISOU 1450  CG  LEU A 859     2645   2672   2855     53    -68   -166       C  
ATOM   1451  CD1 LEU A 859     -55.240  12.234 -12.224  1.00 21.63           C  
ANISOU 1451  CD1 LEU A 859     2642   2701   2874     51    -61   -179       C  
ATOM   1452  CD2 LEU A 859     -55.024  13.388 -14.428  1.00 21.51           C  
ANISOU 1452  CD2 LEU A 859     2651   2669   2852     60    -87   -156       C  
ATOM   1453  N   LEU A 860     -50.966  13.366 -11.254  1.00 18.98           N  
ANISOU 1453  N   LEU A 860     2339   2342   2529     36    -35   -175       N  
ATOM   1454  CA  LEU A 860     -49.525  13.259 -11.478  1.00 18.73           C  
ANISOU 1454  CA  LEU A 860     2316   2307   2493     27    -28   -172       C  
ATOM   1455  C   LEU A 860     -49.125  11.894 -12.015  1.00 17.89           C  
ANISOU 1455  C   LEU A 860     2216   2214   2368     19    -23   -168       C  
ATOM   1456  O   LEU A 860     -49.855  10.903 -11.858  1.00 18.55           O  
ANISOU 1456  O   LEU A 860     2295   2308   2443     19    -24   -171       O  
ATOM   1457  CB  LEU A 860     -48.809  13.500 -10.172  1.00 19.39           C  
ANISOU 1457  CB  LEU A 860     2395   2389   2584     29    -23   -189       C  
ATOM   1458  CG  LEU A 860     -49.018  14.879  -9.539  1.00 19.68           C  
ANISOU 1458  CG  LEU A 860     2425   2410   2643     38    -30   -199       C  
ATOM   1459  CD1 LEU A 860     -48.441  14.889  -8.133  1.00 20.66           C  
ANISOU 1459  CD1 LEU A 860     2544   2539   2768     44    -28   -221       C  
ATOM   1460  CD2 LEU A 860     -48.381  15.982 -10.377  1.00 19.52           C  
ANISOU 1460  CD2 LEU A 860     2410   2367   2641     33    -33   -186       C  
ATOM   1461  N   TRP A 861     -47.976  11.855 -12.663  1.00 17.42           N  
ANISOU 1461  N   TRP A 861     2164   2153   2304     12    -17   -162       N  
ATOM   1462  CA  TRP A 861     -47.475  10.650 -13.310  1.00 17.79           C  
ANISOU 1462  CA  TRP A 861     2216   2212   2333      7    -13   -161       C  
ATOM   1463  C   TRP A 861     -46.724   9.732 -12.346  1.00 17.39           C  
ANISOU 1463  C   TRP A 861     2162   2167   2280      5     -8   -174       C  
ATOM   1464  O   TRP A 861     -46.035  10.204 -11.436  1.00 17.34           O  
ANISOU 1464  O   TRP A 861     2150   2155   2283      6     -5   -183       O  
ATOM   1465  CB  TRP A 861     -46.516  11.008 -14.451  1.00 18.33           C  
ANISOU 1465  CB  TRP A 861     2291   2279   2394      1     -5   -148       C  
ATOM   1466  CG  TRP A 861     -47.102  11.867 -15.518  1.00 18.53           C  
ANISOU 1466  CG  TRP A 861     2325   2299   2416      4    -10   -130       C  
ATOM   1467  CD1 TRP A 861     -46.897  13.213 -15.699  1.00 19.62           C  
ANISOU 1467  CD1 TRP A 861     2465   2420   2568      3     -8   -116       C  
ATOM   1468  CD2 TRP A 861     -47.980  11.450 -16.563  1.00 18.20           C  
ANISOU 1468  CD2 TRP A 861     2291   2267   2356     10    -20   -123       C  
ATOM   1469  NE1 TRP A 861     -47.596  13.648 -16.803  1.00 18.92           N  
ANISOU 1469  NE1 TRP A 861     2388   2331   2469      8    -15    -97       N  
ATOM   1470  CE2 TRP A 861     -48.261  12.580 -17.352  1.00 18.69           C  
ANISOU 1470  CE2 TRP A 861     2363   2320   2418     14    -24   -102       C  
ATOM   1471  CE3 TRP A 861     -48.539  10.227 -16.913  1.00 18.37           C  
ANISOU 1471  CE3 TRP A 861     2313   2302   2363     14    -29   -132       C  
ATOM   1472  CZ2 TRP A 861     -49.089  12.520 -18.476  1.00 18.89           C  
ANISOU 1472  CZ2 TRP A 861     2399   2353   2424     24    -37    -92       C  
ATOM   1473  CZ3 TRP A 861     -49.325  10.149 -18.025  1.00 18.80           C  
ANISOU 1473  CZ3 TRP A 861     2376   2364   2402     22    -42   -126       C  
ATOM   1474  CH2 TRP A 861     -49.628  11.309 -18.790  1.00 19.41           C  
ANISOU 1474  CH2 TRP A 861     2464   2435   2476     28    -47   -106       C  
ATOM   1475  N   HIS A 862     -46.836   8.421 -12.586  1.00 16.68           N  
ANISOU 1475  N   HIS A 862     2074   2086   2178      4     -9   -177       N  
ATOM   1476  CA  HIS A 862     -45.915   7.480 -11.990  1.00 17.10           C  
ANISOU 1476  CA  HIS A 862     2128   2143   2228      3     -6   -187       C  
ATOM   1477  C   HIS A 862     -45.589   6.389 -12.992  1.00 17.34           C  
ANISOU 1477  C   HIS A 862     2163   2179   2247      2     -8   -189       C  
ATOM   1478  O   HIS A 862     -46.478   5.634 -13.388  1.00 18.08           O  
ANISOU 1478  O   HIS A 862     2259   2275   2337      2    -15   -188       O  
ATOM   1479  CB  HIS A 862     -46.487   6.875 -10.722  1.00 16.73           C  
ANISOU 1479  CB  HIS A 862     2078   2096   2182      7     -8   -192       C  
ATOM   1480  CG  HIS A 862     -45.556   5.939 -10.059  1.00 18.48           C  
ANISOU 1480  CG  HIS A 862     2302   2319   2400      9     -8   -200       C  
ATOM   1481  ND1 HIS A 862     -44.659   6.355  -9.096  1.00 20.25           N  
ANISOU 1481  ND1 HIS A 862     2526   2543   2627     14     -7   -209       N  
ATOM   1482  CD2 HIS A 862     -45.343   4.615 -10.219  1.00 19.71           C  
ANISOU 1482  CD2 HIS A 862     2463   2475   2550      8    -11   -201       C  
ATOM   1483  CE1 HIS A 862     -43.959   5.314  -8.673  1.00 21.16           C  
ANISOU 1483  CE1 HIS A 862     2644   2658   2736     18    -10   -214       C  
ATOM   1484  NE2 HIS A 862     -44.357   4.249  -9.335  1.00 20.67           N  
ANISOU 1484  NE2 HIS A 862     2586   2596   2671     14    -12   -209       N  
ATOM   1485  N   GLY A 863     -44.317   6.276 -13.347  1.00 17.50           N  
ANISOU 1485  N   GLY A 863     2183   2202   2264      1     -1   -194       N  
ATOM   1486  CA  GLY A 863     -43.827   5.232 -14.222  1.00 17.79           C  
ANISOU 1486  CA  GLY A 863     2223   2246   2289      3     -2   -201       C  
ATOM   1487  C   GLY A 863     -43.152   4.103 -13.474  1.00 19.42           C  
ANISOU 1487  C   GLY A 863     2428   2451   2499      6     -6   -214       C  
ATOM   1488  O   GLY A 863     -42.591   4.313 -12.408  1.00 20.91           O  
ANISOU 1488  O   GLY A 863     2613   2635   2696      8     -5   -218       O  
ATOM   1489  N   SER A 864     -43.233   2.886 -14.021  1.00 20.46           N  
ANISOU 1489  N   SER A 864     2564   2585   2625      9    -13   -222       N  
ATOM   1490  CA  SER A 864     -42.640   1.691 -13.423  1.00 20.41           C  
ANISOU 1490  CA  SER A 864     2559   2574   2624     15    -20   -234       C  
ATOM   1491  C   SER A 864     -42.495   0.649 -14.521  1.00 21.77           C  
ANISOU 1491  C   SER A 864     2735   2749   2789     19    -26   -246       C  
ATOM   1492  O   SER A 864     -43.132   0.758 -15.572  1.00 24.09           O  
ANISOU 1492  O   SER A 864     3031   3049   3072     19    -28   -245       O  
ATOM   1493  CB  SER A 864     -43.542   1.145 -12.344  1.00 20.10           C  
ANISOU 1493  CB  SER A 864     2523   2522   2592     13    -27   -226       C  
ATOM   1494  OG  SER A 864     -42.890   0.189 -11.539  1.00 19.36           O  
ANISOU 1494  OG  SER A 864     2433   2421   2502     19    -33   -232       O  
ATOM   1495  N   ARG A 865     -41.647  -0.338 -14.312  1.00 22.40           N  
ANISOU 1495  N   ARG A 865     2814   2825   2873     27    -32   -260       N  
ATOM   1496  CA  ARG A 865     -41.458  -1.418 -15.282  1.00 25.45           C  
ANISOU 1496  CA  ARG A 865     3202   3213   3255     34    -40   -278       C  
ATOM   1497  C   ARG A 865     -42.770  -2.193 -15.446  1.00 24.39           C  
ANISOU 1497  C   ARG A 865     3075   3067   3127     31    -55   -276       C  
ATOM   1498  O   ARG A 865     -43.517  -2.383 -14.491  1.00 24.12           O  
ANISOU 1498  O   ARG A 865     3042   3018   3106     24    -60   -263       O  
ATOM   1499  CB  ARG A 865     -40.369  -2.395 -14.835  1.00 27.67           C  
ANISOU 1499  CB  ARG A 865     3480   3487   3545     45    -47   -294       C  
ATOM   1500  CG  ARG A 865     -38.955  -1.880 -14.886  1.00 30.53           C  
ANISOU 1500  CG  ARG A 865     3832   3862   3905     50    -35   -304       C  
ATOM   1501  CD  ARG A 865     -38.019  -2.818 -14.108  1.00 34.57           C  
ANISOU 1501  CD  ARG A 865     4341   4363   4430     63    -47   -319       C  
ATOM   1502  NE  ARG A 865     -36.740  -2.186 -13.838  1.00 37.45           N  
ANISOU 1502  NE  ARG A 865     4690   4738   4799     66    -37   -328       N  
ATOM   1503  CZ  ARG A 865     -35.695  -2.229 -14.643  1.00 37.23           C  
ANISOU 1503  CZ  ARG A 865     4650   4726   4770     73    -27   -347       C  
ATOM   1504  NH1 ARG A 865     -34.602  -1.567 -14.323  1.00 40.07           N  
ANISOU 1504  NH1 ARG A 865     4992   5094   5140     73    -18   -354       N  
ATOM   1505  NH2 ARG A 865     -35.744  -2.892 -15.779  1.00 41.93           N  
ANISOU 1505  NH2 ARG A 865     5246   5329   5354     80    -27   -360       N  
ATOM   1506  N   THR A 866     -43.009  -2.638 -16.665  1.00 23.04           N  
ANISOU 1506  N   THR A 866     2905   2903   2947     36    -63   -290       N  
ATOM   1507  CA  THR A 866     -44.211  -3.380 -17.026  1.00 22.99           C  
ANISOU 1507  CA  THR A 866     2901   2885   2950     33    -81   -294       C  
ATOM   1508  C   THR A 866     -44.448  -4.585 -16.156  1.00 22.14           C  
ANISOU 1508  C   THR A 866     2794   2750   2867     30    -94   -295       C  
ATOM   1509  O   THR A 866     -45.595  -4.866 -15.764  1.00 24.10           O  
ANISOU 1509  O   THR A 866     3040   2984   3132     19   -101   -285       O  
ATOM   1510  CB  THR A 866     -44.147  -3.776 -18.503  1.00 23.14           C  
ANISOU 1510  CB  THR A 866     2923   2917   2952     44    -90   -316       C  
ATOM   1511  OG1 THR A 866     -43.961  -2.593 -19.251  1.00 27.12           O  
ANISOU 1511  OG1 THR A 866     3428   3445   3430     46    -75   -308       O  
ATOM   1512  CG2 THR A 866     -45.437  -4.422 -18.978  1.00 24.58           C  
ANISOU 1512  CG2 THR A 866     3106   3089   3146     41   -112   -325       C  
ATOM   1513  N   THR A 867     -43.371  -5.272 -15.808  1.00 21.68           N  
ANISOU 1513  N   THR A 867     2737   2685   2813     39    -96   -306       N  
ATOM   1514  CA  THR A 867     -43.446  -6.465 -14.975  1.00 21.52           C  
ANISOU 1514  CA  THR A 867     2721   2637   2817     38   -109   -304       C  
ATOM   1515  C   THR A 867     -43.840  -6.198 -13.533  1.00 22.15           C  
ANISOU 1515  C   THR A 867     2804   2707   2906     28   -101   -276       C  
ATOM   1516  O   THR A 867     -44.068  -7.130 -12.765  1.00 27.21           O  
ANISOU 1516  O   THR A 867     3451   3324   3565     25   -109   -267       O  
ATOM   1517  CB  THR A 867     -42.108  -7.221 -15.017  1.00 21.53           C  
ANISOU 1517  CB  THR A 867     2724   2635   2821     54   -116   -324       C  
ATOM   1518  OG1 THR A 867     -41.031  -6.328 -14.715  1.00 20.53           O  
ANISOU 1518  OG1 THR A 867     2593   2527   2680     60   -101   -323       O  
ATOM   1519  CG2 THR A 867     -41.873  -7.859 -16.423  1.00 19.55           C  
ANISOU 1519  CG2 THR A 867     2471   2390   2565     66   -128   -357       C  
ATOM   1520  N   ASN A 868     -43.931  -4.935 -13.149  1.00 22.67           N  
ANISOU 1520  N   ASN A 868     2867   2789   2957     23    -85   -262       N  
ATOM   1521  CA  ASN A 868     -44.440  -4.574 -11.854  1.00 22.73           C  
ANISOU 1521  CA  ASN A 868     2876   2792   2968     16    -76   -238       C  
ATOM   1522  C   ASN A 868     -45.959  -4.368 -11.805  1.00 22.24           C  
ANISOU 1522  C   ASN A 868     2809   2727   2915      2    -72   -224       C  
ATOM   1523  O   ASN A 868     -46.517  -4.264 -10.728  1.00 20.31           O  
ANISOU 1523  O   ASN A 868     2565   2477   2673     -4    -64   -204       O  
ATOM   1524  CB  ASN A 868     -43.797  -3.305 -11.355  1.00 23.66           C  
ANISOU 1524  CB  ASN A 868     2992   2927   3070     20    -62   -234       C  
ATOM   1525  CG  ASN A 868     -42.318  -3.439 -11.075  1.00 25.41           C  
ANISOU 1525  CG  ASN A 868     3215   3152   3289     33    -65   -246       C  
ATOM   1526  OD1 ASN A 868     -41.581  -2.470 -11.255  1.00 28.97           O  
ANISOU 1526  OD1 ASN A 868     3658   3617   3730     36    -56   -253       O  
ATOM   1527  ND2 ASN A 868     -41.870  -4.580 -10.621  1.00 25.48           N  
ANISOU 1527  ND2 ASN A 868     3230   3144   3306     41    -77   -250       N  
ATOM   1528  N   PHE A 869     -46.625  -4.265 -12.951  1.00 23.67           N  
ANISOU 1528  N   PHE A 869     2984   2912   3097     -2    -79   -234       N  
ATOM   1529  CA  PHE A 869     -48.003  -3.722 -12.958  1.00 23.74           C  
ANISOU 1529  CA  PHE A 869     2983   2923   3112    -13    -75   -223       C  
ATOM   1530  C   PHE A 869     -49.086  -4.639 -12.408  1.00 25.87           C  
ANISOU 1530  C   PHE A 869     3248   3173   3409    -26    -79   -212       C  
ATOM   1531  O   PHE A 869     -50.143  -4.156 -11.949  1.00 25.62           O  
ANISOU 1531  O   PHE A 869     3206   3144   3383    -35    -69   -199       O  
ATOM   1532  CB  PHE A 869     -48.372  -3.168 -14.302  1.00 23.64           C  
ANISOU 1532  CB  PHE A 869     2967   2924   3090    -10    -83   -236       C  
ATOM   1533  CG  PHE A 869     -48.025  -1.730 -14.426  1.00 24.15           C  
ANISOU 1533  CG  PHE A 869     3032   3009   3134     -5    -70   -230       C  
ATOM   1534  CD1 PHE A 869     -46.759  -1.337 -14.740  1.00 23.16           C  
ANISOU 1534  CD1 PHE A 869     2914   2895   2993      4    -64   -236       C  
ATOM   1535  CD2 PHE A 869     -48.958  -0.760 -14.135  1.00 25.59           C  
ANISOU 1535  CD2 PHE A 869     3208   3197   3318    -10    -64   -218       C  
ATOM   1536  CE1 PHE A 869     -46.427   0.000 -14.813  1.00 23.77           C  
ANISOU 1536  CE1 PHE A 869     2990   2985   3056      5    -51   -228       C  
ATOM   1537  CE2 PHE A 869     -48.617   0.586 -14.189  1.00 25.48           C  
ANISOU 1537  CE2 PHE A 869     3196   3196   3291     -6    -54   -211       C  
ATOM   1538  CZ  PHE A 869     -47.350   0.959 -14.525  1.00 23.39           C  
ANISOU 1538  CZ  PHE A 869     2938   2939   3011      1    -48   -216       C  
ATOM   1539  N   ALA A 870     -48.843  -5.931 -12.412  1.00 24.62           N  
ANISOU 1539  N   ALA A 870     3094   2992   3267    -27    -91   -217       N  
ATOM   1540  CA  ALA A 870     -49.796  -6.819 -11.764  1.00 25.69           C  
ANISOU 1540  CA  ALA A 870     3225   3105   3432    -42    -91   -202       C  
ATOM   1541  C   ALA A 870     -49.789  -6.565 -10.295  1.00 23.50           C  
ANISOU 1541  C   ALA A 870     2952   2829   3147    -45    -70   -174       C  
ATOM   1542  O   ALA A 870     -50.821  -6.563  -9.651  1.00 25.96           O  
ANISOU 1542  O   ALA A 870     3255   3137   3472    -59    -57   -155       O  
ATOM   1543  CB  ALA A 870     -49.474  -8.280 -12.062  1.00 27.28           C  
ANISOU 1543  CB  ALA A 870     3432   3278   3657    -42   -110   -213       C  
ATOM   1544  N   GLY A 871     -48.605  -6.363  -9.752  1.00 22.67           N  
ANISOU 1544  N   GLY A 871     2862   2731   3022    -32    -67   -172       N  
ATOM   1545  CA  GLY A 871     -48.441  -6.078  -8.356  1.00 21.53           C  
ANISOU 1545  CA  GLY A 871     2725   2592   2864    -29    -50   -149       C  
ATOM   1546  C   GLY A 871     -49.068  -4.726  -8.044  1.00 22.28           C  
ANISOU 1546  C   GLY A 871     2810   2710   2944    -31    -33   -144       C  
ATOM   1547  O   GLY A 871     -49.786  -4.596  -7.052  1.00 24.58           O  
ANISOU 1547  O   GLY A 871     3099   3005   3234    -37    -17   -123       O  
ATOM   1548  N   ILE A 872     -48.781  -3.715  -8.854  1.00 20.31           N  
ANISOU 1548  N   ILE A 872     2556   2479   2684    -25    -36   -161       N  
ATOM   1549  CA  ILE A 872     -49.327  -2.378  -8.615  1.00 20.74           C  
ANISOU 1549  CA  ILE A 872     2600   2551   2727    -25    -24   -158       C  
ATOM   1550  C   ILE A 872     -50.856  -2.372  -8.699  1.00 21.51           C  
ANISOU 1550  C   ILE A 872     2682   2648   2842    -38    -18   -151       C  
ATOM   1551  O   ILE A 872     -51.492  -1.786  -7.882  1.00 21.68           O  
ANISOU 1551  O   ILE A 872     2697   2680   2860    -39     -2   -140       O  
ATOM   1552  CB  ILE A 872     -48.766  -1.367  -9.608  1.00 21.04           C  
ANISOU 1552  CB  ILE A 872     2638   2604   2755    -17    -29   -175       C  
ATOM   1553  CG1 ILE A 872     -47.272  -1.132  -9.311  1.00 20.96           C  
ANISOU 1553  CG1 ILE A 872     2637   2598   2729     -5    -30   -183       C  
ATOM   1554  CG2 ILE A 872     -49.526  -0.049  -9.566  1.00 20.40           C  
ANISOU 1554  CG2 ILE A 872     2546   2536   2669    -18    -21   -173       C  
ATOM   1555  CD1 ILE A 872     -46.553  -0.449 -10.446  1.00 19.94           C  
ANISOU 1555  CD1 ILE A 872     2507   2478   2593     -1    -34   -198       C  
ATOM   1556  N   LEU A 873     -51.440  -3.025  -9.690  1.00 22.92           N  
ANISOU 1556  N   LEU A 873     2853   2816   3041    -46    -31   -159       N  
ATOM   1557  CA  LEU A 873     -52.849  -3.040  -9.774  1.00 23.64           C  
ANISOU 1557  CA  LEU A 873     2925   2905   3153    -59    -28   -155       C  
ATOM   1558  C   LEU A 873     -53.465  -3.806  -8.636  1.00 24.55           C  
ANISOU 1558  C   LEU A 873     3036   3009   3284    -72    -12   -132       C  
ATOM   1559  O   LEU A 873     -54.465  -3.369  -8.067  1.00 22.61           O  
ANISOU 1559  O   LEU A 873     2775   2773   3044    -78      5   -122       O  
ATOM   1560  CB  LEU A 873     -53.326  -3.562 -11.140  1.00 25.15           C  
ANISOU 1560  CB  LEU A 873     3107   3086   3362    -63    -51   -174       C  
ATOM   1561  CG  LEU A 873     -52.959  -2.627 -12.284  1.00 26.08           C  
ANISOU 1561  CG  LEU A 873     3229   3220   3461    -50    -63   -192       C  
ATOM   1562  CD1 LEU A 873     -53.493  -3.214 -13.574  1.00 28.00           C  
ANISOU 1562  CD1 LEU A 873     3464   3456   3718    -51    -87   -211       C  
ATOM   1563  CD2 LEU A 873     -53.498  -1.209 -12.108  1.00 25.49           C  
ANISOU 1563  CD2 LEU A 873     3145   3163   3376    -46    -53   -187       C  
ATOM   1564  N   SER A 874     -52.903  -4.950  -8.274  1.00 25.30           N  
ANISOU 1564  N   SER A 874     3144   3084   3385    -75    -15   -123       N  
ATOM   1565  CA  SER A 874     -53.536  -5.713  -7.217  1.00 26.48           C  
ANISOU 1565  CA  SER A 874     3291   3221   3550    -88      3    -96       C  
ATOM   1566  C   SER A 874     -53.250  -5.116  -5.842  1.00 26.56           C  
ANISOU 1566  C   SER A 874     3312   3250   3530    -79     26    -76       C  
ATOM   1567  O   SER A 874     -54.109  -5.204  -4.966  1.00 26.08           O  
ANISOU 1567  O   SER A 874     3243   3194   3474    -89     49    -54       O  
ATOM   1568  CB  SER A 874     -53.166  -7.201  -7.267  1.00 29.30           C  
ANISOU 1568  CB  SER A 874     3658   3545   3929    -95    -10    -89       C  
ATOM   1569  OG  SER A 874     -51.875  -7.401  -6.773  1.00 31.00           O  
ANISOU 1569  OG  SER A 874     3899   3759   4121    -80    -14    -85       O  
ATOM   1570  N   GLN A 875     -52.096  -4.483  -5.637  1.00 26.19           N  
ANISOU 1570  N   GLN A 875     3282   3217   3453    -60     21    -85       N  
ATOM   1571  CA  GLN A 875     -51.766  -3.984  -4.275  1.00 29.46           C  
ANISOU 1571  CA  GLN A 875     3708   3649   3837    -48     39    -70       C  
ATOM   1572  C   GLN A 875     -51.580  -2.478  -4.168  1.00 27.59           C  
ANISOU 1572  C   GLN A 875     3467   3438   3578    -34     43    -86       C  
ATOM   1573  O   GLN A 875     -51.395  -1.966  -3.087  1.00 27.77           O  
ANISOU 1573  O   GLN A 875     3497   3477   3577    -23     56    -79       O  
ATOM   1574  CB  GLN A 875     -50.490  -4.636  -3.769  1.00 33.89           C  
ANISOU 1574  CB  GLN A 875     4294   4200   4383    -35     29    -65       C  
ATOM   1575  CG  GLN A 875     -50.476  -6.140  -3.795  1.00 38.13           C  
ANISOU 1575  CG  GLN A 875     4840   4706   4942    -45     22    -48       C  
ATOM   1576  CD  GLN A 875     -49.316  -6.736  -3.023  1.00 46.67           C  
ANISOU 1576  CD  GLN A 875     5947   5779   6006    -29     13    -38       C  
ATOM   1577  OE1 GLN A 875     -48.389  -6.037  -2.586  1.00 52.43           O  
ANISOU 1577  OE1 GLN A 875     6686   6527   6707     -9      9    -49       O  
ATOM   1578  NE2 GLN A 875     -49.327  -8.051  -2.922  1.00 49.21           N  
ANISOU 1578  NE2 GLN A 875     6278   6071   6348    -37      7    -20       N  
ATOM   1579  N   GLY A 876     -51.613  -1.768  -5.285  1.00 25.34           N  
ANISOU 1579  N   GLY A 876     3172   3156   3301    -34     31   -107       N  
ATOM   1580  CA  GLY A 876     -51.442  -0.303  -5.262  1.00 24.15           C  
ANISOU 1580  CA  GLY A 876     3017   3025   3135    -22     33   -121       C  
ATOM   1581  C   GLY A 876     -49.970   0.067  -5.160  1.00 22.83           C  
ANISOU 1581  C   GLY A 876     2864   2860   2949     -7     22   -133       C  
ATOM   1582  O   GLY A 876     -49.119  -0.805  -5.001  1.00 21.56           O  
ANISOU 1582  O   GLY A 876     2717   2689   2785     -4     14   -130       O  
ATOM   1583  N   LEU A 877     -49.681   1.352  -5.297  1.00 21.34           N  
ANISOU 1583  N   LEU A 877     2672   2683   2754      1     20   -147       N  
ATOM   1584  CA  LEU A 877     -48.337   1.846  -5.127  1.00 20.56           C  
ANISOU 1584  CA  LEU A 877     2582   2587   2642     14     12   -160       C  
ATOM   1585  C   LEU A 877     -47.974   1.709  -3.646  1.00 22.09           C  
ANISOU 1585  C   LEU A 877     2787   2789   2817     26     18   -154       C  
ATOM   1586  O   LEU A 877     -48.798   1.975  -2.773  1.00 21.67           O  
ANISOU 1586  O   LEU A 877     2732   2747   2755     28     32   -146       O  
ATOM   1587  CB  LEU A 877     -48.231   3.282  -5.577  1.00 19.18           C  
ANISOU 1587  CB  LEU A 877     2399   2418   2469     18     10   -174       C  
ATOM   1588  CG  LEU A 877     -48.406   3.492  -7.058  1.00 18.74           C  
ANISOU 1588  CG  LEU A 877     2338   2357   2427      9      3   -178       C  
ATOM   1589  CD1 LEU A 877     -48.349   4.949  -7.412  1.00 18.29           C  
ANISOU 1589  CD1 LEU A 877     2274   2303   2372     13      2   -186       C  
ATOM   1590  CD2 LEU A 877     -47.378   2.713  -7.841  1.00 20.13           C  
ANISOU 1590  CD2 LEU A 877     2521   2526   2603      8     -6   -183       C  
ATOM   1591  N   ARG A 878     -46.762   1.253  -3.395  1.00 22.46           N  
ANISOU 1591  N   ARG A 878     2846   2831   2856     35      6   -159       N  
ATOM   1592  CA  ARG A 878     -46.287   0.998  -2.046  1.00 25.95           C  
ANISOU 1592  CA  ARG A 878     3302   3280   3276     50      6   -154       C  
ATOM   1593  C   ARG A 878     -44.976   1.715  -1.804  1.00 24.36           C  
ANISOU 1593  C   ARG A 878     3103   3084   3069     65     -8   -176       C  
ATOM   1594  O   ARG A 878     -44.365   2.218  -2.714  1.00 21.51           O  
ANISOU 1594  O   ARG A 878     2732   2719   2722     61    -16   -192       O  
ATOM   1595  CB  ARG A 878     -46.106  -0.503  -1.825  1.00 29.65           C  
ANISOU 1595  CB  ARG A 878     3785   3736   3745     48      3   -135       C  
ATOM   1596  CG  ARG A 878     -47.421  -1.251  -1.596  1.00 34.03           C  
ANISOU 1596  CG  ARG A 878     4340   4286   4305     34     20   -109       C  
ATOM   1597  CD  ARG A 878     -47.384  -2.600  -2.302  1.00 39.84           C  
ANISOU 1597  CD  ARG A 878     5079   4997   5062     22     12    -99       C  
ATOM   1598  NE  ARG A 878     -47.308  -2.395  -3.760  1.00 45.10           N  
ANISOU 1598  NE  ARG A 878     5732   5656   5749     13      1   -119       N  
ATOM   1599  CZ  ARG A 878     -46.739  -3.223  -4.647  1.00 47.74           C  
ANISOU 1599  CZ  ARG A 878     6068   5972   6098     11    -15   -127       C  
ATOM   1600  NH1 ARG A 878     -46.163  -4.369  -4.273  1.00 49.71           N  
ANISOU 1600  NH1 ARG A 878     6333   6206   6351     16    -24   -119       N  
ATOM   1601  NH2 ARG A 878     -46.736  -2.877  -5.924  1.00 46.21           N  
ANISOU 1601  NH2 ARG A 878     5864   5779   5916      6    -21   -145       N  
ATOM   1602  N   ILE A 879     -44.583   1.764  -0.544  1.00 25.25           N  
ANISOU 1602  N   ILE A 879     3227   3209   3160     83    -12   -178       N  
ATOM   1603  CA  ILE A 879     -43.354   2.417  -0.113  1.00 25.38           C  
ANISOU 1603  CA  ILE A 879     3243   3229   3170    100    -29   -202       C  
ATOM   1604  C   ILE A 879     -42.297   1.328   0.206  1.00 24.30           C  
ANISOU 1604  C   ILE A 879     3120   3085   3027    111    -45   -200       C  
ATOM   1605  O   ILE A 879     -42.614   0.266   0.723  1.00 22.46           O  
ANISOU 1605  O   ILE A 879     2903   2848   2781    114    -43   -177       O  
ATOM   1606  CB  ILE A 879     -43.678   3.276   1.132  1.00 27.12           C  
ANISOU 1606  CB  ILE A 879     3467   3470   3368    117    -25   -210       C  
ATOM   1607  CG1 ILE A 879     -44.586   4.455   0.754  1.00 27.66           C  
ANISOU 1607  CG1 ILE A 879     3519   3542   3447    108    -13   -217       C  
ATOM   1608  CG2 ILE A 879     -42.419   3.746   1.812  1.00 27.48           C  
ANISOU 1608  CG2 ILE A 879     3515   3521   3406    137    -47   -236       C  
ATOM   1609  CD1 ILE A 879     -45.141   5.181   1.956  1.00 28.59           C  
ANISOU 1609  CD1 ILE A 879     3640   3681   3542    125     -6   -225       C  
ATOM   1610  N   ALA A 880     -41.045   1.604  -0.090  1.00 24.43           N  
ANISOU 1610  N   ALA A 880     3129   3098   3055    118    -63   -224       N  
ATOM   1611  CA  ALA A 880     -39.951   0.691   0.235  1.00 24.74           C  
ANISOU 1611  CA  ALA A 880     3178   3132   3091    133    -83   -228       C  
ATOM   1612  C   ALA A 880     -39.953   0.240   1.703  1.00 25.98           C  
ANISOU 1612  C   ALA A 880     3357   3298   3216    156    -90   -217       C  
ATOM   1613  O   ALA A 880     -40.216   1.034   2.587  1.00 26.49           O  
ANISOU 1613  O   ALA A 880     3425   3380   3261    167    -88   -223       O  
ATOM   1614  CB  ALA A 880     -38.629   1.355  -0.100  1.00 24.68           C  
ANISOU 1614  CB  ALA A 880     3153   3124   3102    139    -99   -260       C  
ATOM   1615  N   PRO A 881     -39.597  -1.020   1.970  1.00 28.30           N  
ANISOU 1615  N   PRO A 881     3668   3581   3503    165   -101   -201       N  
ATOM   1616  CA  PRO A 881     -39.608  -1.486   3.355  1.00 30.54           C  
ANISOU 1616  CA  PRO A 881     3978   3874   3753    187   -108   -185       C  
ATOM   1617  C   PRO A 881     -38.477  -0.906   4.212  1.00 31.92           C  
ANISOU 1617  C   PRO A 881     4154   4063   3912    216   -135   -214       C  
ATOM   1618  O   PRO A 881     -37.458  -0.449   3.689  1.00 30.73           O  
ANISOU 1618  O   PRO A 881     3983   3908   3785    218   -152   -246       O  
ATOM   1619  CB  PRO A 881     -39.471  -3.011   3.233  1.00 30.65           C  
ANISOU 1619  CB  PRO A 881     4009   3866   3772    187   -115   -160       C  
ATOM   1620  CG  PRO A 881     -38.920  -3.274   1.898  1.00 31.18           C  
ANISOU 1620  CG  PRO A 881     4057   3915   3875    174   -122   -178       C  
ATOM   1621  CD  PRO A 881     -39.207  -2.080   1.018  1.00 30.55           C  
ANISOU 1621  CD  PRO A 881     3951   3844   3812    156   -108   -197       C  
ATOM   1622  N   PRO A 882     -38.642  -0.933   5.528  1.00 34.07           N  
ANISOU 1622  N   PRO A 882     4448   4352   4145    239   -139   -205       N  
ATOM   1623  CA  PRO A 882     -37.594  -0.481   6.494  1.00 35.45           C  
ANISOU 1623  CA  PRO A 882     4627   4542   4300    271   -170   -233       C  
ATOM   1624  C   PRO A 882     -36.209  -1.085   6.242  1.00 34.52           C  
ANISOU 1624  C   PRO A 882     4505   4409   4201    285   -203   -252       C  
ATOM   1625  O   PRO A 882     -35.195  -0.405   6.380  1.00 33.18           O  
ANISOU 1625  O   PRO A 882     4319   4246   4042    299   -227   -291       O  
ATOM   1626  CB  PRO A 882     -38.128  -0.948   7.853  1.00 37.56           C  
ANISOU 1626  CB  PRO A 882     4928   4826   4515    294   -166   -205       C  
ATOM   1627  CG  PRO A 882     -39.610  -1.131   7.658  1.00 40.29           C  
ANISOU 1627  CG  PRO A 882     5279   5174   4857    269   -126   -169       C  
ATOM   1628  CD  PRO A 882     -39.860  -1.425   6.187  1.00 37.28           C  
ANISOU 1628  CD  PRO A 882     4876   4767   4522    235   -113   -165       C  
ATOM   1629  N   GLU A 883     -36.169  -2.354   5.854  1.00 35.70           N  
ANISOU 1629  N   GLU A 883     4667   4538   4359    280   -203   -227       N  
ATOM   1630  CA  GLU A 883     -34.910  -3.061   5.635  1.00 39.82           C  
ANISOU 1630  CA  GLU A 883     5185   5045   4900    296   -235   -243       C  
ATOM   1631  C   GLU A 883     -34.116  -2.576   4.423  1.00 38.87           C  
ANISOU 1631  C   GLU A 883     5028   4916   4823    281   -238   -279       C  
ATOM   1632  O   GLU A 883     -32.891  -2.830   4.313  1.00 40.32           O  
ANISOU 1632  O   GLU A 883     5199   5095   5025    297   -266   -305       O  
ATOM   1633  CB  GLU A 883     -35.180  -4.561   5.453  1.00 43.51           C  
ANISOU 1633  CB  GLU A 883     5674   5488   5369    294   -233   -207       C  
ATOM   1634  CG  GLU A 883     -35.865  -5.234   6.636  1.00 47.04           C  
ANISOU 1634  CG  GLU A 883     6161   5940   5774    308   -229   -164       C  
ATOM   1635  CD  GLU A 883     -37.386  -5.174   6.624  1.00 49.64           C  
ANISOU 1635  CD  GLU A 883     6497   6272   6092    282   -188   -128       C  
ATOM   1636  OE1 GLU A 883     -37.970  -5.478   7.692  1.00 57.10           O  
ANISOU 1636  OE1 GLU A 883     7470   7227   6997    293   -179    -95       O  
ATOM   1637  OE2 GLU A 883     -38.003  -4.822   5.589  1.00 46.27           O  
ANISOU 1637  OE2 GLU A 883     6047   5839   5693    252   -166   -133       O  
ATOM   1638  N   ALA A 884     -34.807  -1.942   3.482  1.00 36.20           N  
ANISOU 1638  N   ALA A 884     4672   4578   4505    251   -210   -278       N  
ATOM   1639  CA  ALA A 884     -34.147  -1.482   2.284  1.00 34.80           C  
ANISOU 1639  CA  ALA A 884     4462   4395   4365    235   -208   -306       C  
ATOM   1640  C   ALA A 884     -33.220  -0.322   2.608  1.00 33.77           C  
ANISOU 1640  C   ALA A 884     4309   4277   4246    246   -224   -344       C  
ATOM   1641  O   ALA A 884     -33.577   0.529   3.426  1.00 33.55           O  
ANISOU 1641  O   ALA A 884     4286   4263   4199    253   -225   -350       O  
ATOM   1642  CB  ALA A 884     -35.171  -1.063   1.243  1.00 35.39           C  
ANISOU 1642  CB  ALA A 884     4527   4466   4453    203   -176   -292       C  
ATOM   1643  N   PRO A 885     -32.055  -0.251   1.923  1.00 32.63           N  
ANISOU 1643  N   PRO A 885     4137   4126   4133    245   -236   -374       N  
ATOM   1644  CA  PRO A 885     -31.229   0.935   2.034  1.00 35.48           C  
ANISOU 1644  CA  PRO A 885     4469   4495   4515    247   -247   -410       C  
ATOM   1645  C   PRO A 885     -31.962   2.173   1.531  1.00 36.97           C  
ANISOU 1645  C   PRO A 885     4646   4687   4714    221   -220   -408       C  
ATOM   1646  O   PRO A 885     -32.730   2.071   0.573  1.00 41.35           O  
ANISOU 1646  O   PRO A 885     5202   5236   5274    197   -193   -387       O  
ATOM   1647  CB  PRO A 885     -30.006   0.636   1.144  1.00 34.79           C  
ANISOU 1647  CB  PRO A 885     4352   4400   4465    244   -254   -434       C  
ATOM   1648  CG  PRO A 885     -30.174  -0.739   0.625  1.00 34.26           C  
ANISOU 1648  CG  PRO A 885     4301   4323   4394    246   -250   -413       C  
ATOM   1649  CD  PRO A 885     -31.535  -1.221   0.945  1.00 33.15           C  
ANISOU 1649  CD  PRO A 885     4194   4179   4222    241   -236   -374       C  
ATOM   1650  N   VAL A 886     -31.745   3.297   2.196  1.00 36.93           N  
ANISOU 1650  N   VAL A 886     4630   4690   4713    228   -231   -432       N  
ATOM   1651  CA  VAL A 886     -32.374   4.570   1.840  1.00 40.45           C  
ANISOU 1651  CA  VAL A 886     5063   5134   5171    207   -211   -434       C  
ATOM   1652  C   VAL A 886     -31.602   5.239   0.711  1.00 40.84           C  
ANISOU 1652  C   VAL A 886     5078   5173   5266    184   -202   -451       C  
ATOM   1653  O   VAL A 886     -32.129   6.131   0.025  1.00 43.81           O  
ANISOU 1653  O   VAL A 886     5445   5544   5658    161   -180   -443       O  
ATOM   1654  CB  VAL A 886     -32.425   5.527   3.045  1.00 40.91           C  
ANISOU 1654  CB  VAL A 886     5125   5203   5217    225   -230   -457       C  
ATOM   1655  CG1 VAL A 886     -31.024   5.961   3.433  1.00 41.67           C  
ANISOU 1655  CG1 VAL A 886     5195   5297   5340    239   -262   -499       C  
ATOM   1656  CG2 VAL A 886     -33.287   6.753   2.723  1.00 44.77           C  
ANISOU 1656  CG2 VAL A 886     5606   5688   5718    206   -210   -454       C  
ATOM   1657  N   THR A 887     -30.378   4.781   0.494  1.00 43.26           N  
ANISOU 1657  N   THR A 887     5366   5478   5594    191   -216   -471       N  
ATOM   1658  CA  THR A 887     -29.505   5.320  -0.546  1.00 45.36           C  
ANISOU 1658  CA  THR A 887     5595   5736   5903    171   -205   -487       C  
ATOM   1659  C   THR A 887     -30.232   5.338  -1.901  1.00 37.89           C  
ANISOU 1659  C   THR A 887     4650   4786   4960    142   -168   -458       C  
ATOM   1660  O   THR A 887     -30.876   4.382  -2.304  1.00 36.36           O  
ANISOU 1660  O   THR A 887     4477   4594   4745    141   -157   -434       O  
ATOM   1661  CB  THR A 887     -28.117   4.595  -0.590  1.00 46.53           C  
ANISOU 1661  CB  THR A 887     5722   5886   6071    185   -225   -512       C  
ATOM   1662  OG1 THR A 887     -27.287   5.142   0.456  1.00 52.25           O  
ANISOU 1662  OG1 THR A 887     6432   6613   6809    205   -258   -548       O  
ATOM   1663  CG2 THR A 887     -27.426   4.811  -1.917  1.00 46.32           C  
ANISOU 1663  CG2 THR A 887     5662   5855   6081    161   -201   -518       C  
ATOM   1664  N   GLY A 888     -30.121   6.461  -2.583  1.00 32.78           N  
ANISOU 1664  N   GLY A 888     3981   4133   4342    119   -150   -461       N  
ATOM   1665  CA  GLY A 888     -30.825   6.670  -3.835  1.00 28.24           C  
ANISOU 1665  CA  GLY A 888     3408   3554   3767     94   -118   -433       C  
ATOM   1666  C   GLY A 888     -32.134   7.407  -3.663  1.00 25.45           C  
ANISOU 1666  C   GLY A 888     3073   3197   3400     87   -109   -414       C  
ATOM   1667  O   GLY A 888     -32.575   8.034  -4.594  1.00 25.68           O  
ANISOU 1667  O   GLY A 888     3098   3220   3438     66    -86   -398       O  
ATOM   1668  N   TYR A 889     -32.764   7.314  -2.494  1.00 25.50           N  
ANISOU 1668  N   TYR A 889     3100   3208   3381    105   -125   -415       N  
ATOM   1669  CA  TYR A 889     -33.997   8.046  -2.227  1.00 27.56           C  
ANISOU 1669  CA  TYR A 889     3375   3467   3629    101   -117   -401       C  
ATOM   1670  C   TYR A 889     -33.753   9.472  -1.797  1.00 25.77           C  
ANISOU 1670  C   TYR A 889     3132   3232   3429     99   -126   -423       C  
ATOM   1671  O   TYR A 889     -33.562   9.764  -0.631  1.00 27.47           O  
ANISOU 1671  O   TYR A 889     3349   3451   3638    118   -149   -447       O  
ATOM   1672  CB  TYR A 889     -34.843   7.350  -1.165  1.00 28.71           C  
ANISOU 1672  CB  TYR A 889     3548   3624   3735    121   -126   -392       C  
ATOM   1673  CG  TYR A 889     -35.565   6.144  -1.672  1.00 29.76           C  
ANISOU 1673  CG  TYR A 889     3700   3760   3847    117   -112   -363       C  
ATOM   1674  CD1 TYR A 889     -35.033   4.864  -1.531  1.00 33.86           C  
ANISOU 1674  CD1 TYR A 889     4228   4282   4355    128   -122   -361       C  
ATOM   1675  CD2 TYR A 889     -36.782   6.280  -2.294  1.00 33.94           C  
ANISOU 1675  CD2 TYR A 889     4238   4288   4369    102    -91   -338       C  
ATOM   1676  CE1 TYR A 889     -35.715   3.751  -2.006  1.00 35.64           C  
ANISOU 1676  CE1 TYR A 889     4471   4506   4567    124   -112   -335       C  
ATOM   1677  CE2 TYR A 889     -37.487   5.177  -2.755  1.00 32.60           C  
ANISOU 1677  CE2 TYR A 889     4083   4119   4184     97    -81   -314       C  
ATOM   1678  CZ  TYR A 889     -36.940   3.925  -2.626  1.00 33.60           C  
ANISOU 1678  CZ  TYR A 889     4218   4246   4304    107    -91   -313       C  
ATOM   1679  OH  TYR A 889     -37.657   2.853  -3.091  1.00 39.08           O  
ANISOU 1679  OH  TYR A 889     4926   4937   4988    101    -83   -291       O  
ATOM   1680  N   MET A 890     -33.809  10.367  -2.760  1.00 25.88           N  
ANISOU 1680  N   MET A 890     3131   3232   3470     76   -108   -415       N  
ATOM   1681  CA  MET A 890     -33.501  11.756  -2.559  1.00 24.85           C  
ANISOU 1681  CA  MET A 890     2981   3085   3374     69   -115   -434       C  
ATOM   1682  C   MET A 890     -34.331  12.382  -1.451  1.00 23.94           C  
ANISOU 1682  C   MET A 890     2880   2972   3245     86   -130   -446       C  
ATOM   1683  O   MET A 890     -33.834  13.241  -0.709  1.00 28.78           O  
ANISOU 1683  O   MET A 890     3479   3576   3880     94   -151   -477       O  
ATOM   1684  CB  MET A 890     -33.715  12.490  -3.866  1.00 25.28           C  
ANISOU 1684  CB  MET A 890     3028   3126   3454     41    -89   -411       C  
ATOM   1685  CG  MET A 890     -33.328  13.944  -3.801  1.00 29.87           C  
ANISOU 1685  CG  MET A 890     3588   3683   4079     30    -95   -427       C  
ATOM   1686  SD  MET A 890     -33.219  14.692  -5.426  1.00 34.79           S  
ANISOU 1686  SD  MET A 890     4199   4288   4733     -4    -63   -395       S  
ATOM   1687  CE  MET A 890     -32.632  16.332  -4.922  1.00 37.45           C  
ANISOU 1687  CE  MET A 890     4508   4592   5128    -13    -78   -421       C  
ATOM   1688  N   PHE A 891     -35.599  12.011  -1.342  1.00 22.08           N  
ANISOU 1688  N   PHE A 891     2669   2747   2976     91   -120   -424       N  
ATOM   1689  CA  PHE A 891     -36.461  12.583  -0.303  1.00 21.87           C  
ANISOU 1689  CA  PHE A 891     2653   2725   2932    109   -130   -435       C  
ATOM   1690  C   PHE A 891     -37.006  11.551   0.654  1.00 21.14           C  
ANISOU 1690  C   PHE A 891     2585   2657   2792    131   -134   -430       C  
ATOM   1691  O   PHE A 891     -38.096  11.692   1.207  1.00 21.24           O  
ANISOU 1691  O   PHE A 891     2611   2679   2780    141   -129   -424       O  
ATOM   1692  CB  PHE A 891     -37.562  13.403  -0.939  1.00 22.81           C  
ANISOU 1692  CB  PHE A 891     2774   2832   3059     95   -113   -417       C  
ATOM   1693  CG  PHE A 891     -37.048  14.546  -1.759  1.00 23.26           C  
ANISOU 1693  CG  PHE A 891     2810   2863   3164     75   -110   -420       C  
ATOM   1694  CD1 PHE A 891     -36.466  15.633  -1.156  1.00 23.68           C  
ANISOU 1694  CD1 PHE A 891     2847   2901   3250     79   -130   -453       C  
ATOM   1695  CD2 PHE A 891     -37.105  14.515  -3.128  1.00 24.85           C  
ANISOU 1695  CD2 PHE A 891     3009   3055   3377     51    -88   -391       C  
ATOM   1696  CE1 PHE A 891     -35.968  16.705  -1.892  1.00 23.29           C  
ANISOU 1696  CE1 PHE A 891     2778   2822   3250     58   -126   -453       C  
ATOM   1697  CE2 PHE A 891     -36.605  15.585  -3.883  1.00 26.54           C  
ANISOU 1697  CE2 PHE A 891     3205   3244   3635     31    -83   -389       C  
ATOM   1698  CZ  PHE A 891     -36.038  16.682  -3.251  1.00 25.02           C  
ANISOU 1698  CZ  PHE A 891     2996   3032   3479     33   -101   -418       C  
ATOM   1699  N   GLY A 892     -36.244  10.493   0.850  1.00 20.90           N  
ANISOU 1699  N   GLY A 892     2558   2635   2749    139   -143   -431       N  
ATOM   1700  CA  GLY A 892     -36.695   9.408   1.692  1.00 22.81           C  
ANISOU 1700  CA  GLY A 892     2825   2896   2946    159   -145   -419       C  
ATOM   1701  C   GLY A 892     -37.625   8.415   1.025  1.00 22.58           C  
ANISOU 1701  C   GLY A 892     2812   2870   2899    147   -122   -380       C  
ATOM   1702  O   GLY A 892     -38.001   8.539  -0.158  1.00 23.01           O  
ANISOU 1702  O   GLY A 892     2858   2913   2970    124   -103   -363       O  
ATOM   1703  N   LYS A 893     -37.978   7.426   1.804  1.00 22.95           N  
ANISOU 1703  N   LYS A 893     2879   2930   2910    162   -123   -367       N  
ATOM   1704  CA  LYS A 893     -38.828   6.359   1.359  1.00 24.48           C  
ANISOU 1704  CA  LYS A 893     3089   3126   3089    152   -104   -333       C  
ATOM   1705  C   LYS A 893     -40.226   6.858   1.266  1.00 24.66           C  
ANISOU 1705  C   LYS A 893     3113   3152   3104    143    -84   -318       C  
ATOM   1706  O   LYS A 893     -40.806   7.166   2.252  1.00 26.77           O  
ANISOU 1706  O   LYS A 893     3389   3434   3350    158    -83   -321       O  
ATOM   1707  CB  LYS A 893     -38.707   5.182   2.291  1.00 24.12           C  
ANISOU 1707  CB  LYS A 893     3064   3089   3010    171   -113   -321       C  
ATOM   1708  CG  LYS A 893     -37.334   4.499   2.199  1.00 25.87           C  
ANISOU 1708  CG  LYS A 893     3283   3304   3242    180   -135   -334       C  
ATOM   1709  CD  LYS A 893     -37.211   3.400   3.257  1.00 28.66           C  
ANISOU 1709  CD  LYS A 893     3662   3667   3561    204   -148   -322       C  
ATOM   1710  CE  LYS A 893     -35.791   2.819   3.334  1.00 30.47           C  
ANISOU 1710  CE  LYS A 893     3887   3889   3800    219   -176   -340       C  
ATOM   1711  NZ  LYS A 893     -35.841   1.580   4.158  1.00 35.94           N  
ANISOU 1711  NZ  LYS A 893     4609   4585   4460    239   -185   -318       N  
ATOM   1712  N   GLY A 894     -40.741   6.981   0.046  1.00 23.17           N  
ANISOU 1712  N   GLY A 894     2915   2952   2935    121    -68   -304       N  
ATOM   1713  CA  GLY A 894     -42.090   7.422  -0.167  1.00 21.13           C  
ANISOU 1713  CA  GLY A 894     2657   2697   2676    113    -51   -290       C  
ATOM   1714  C   GLY A 894     -42.527   6.969  -1.550  1.00 21.22           C  
ANISOU 1714  C   GLY A 894     2663   2696   2701     91    -39   -270       C  
ATOM   1715  O   GLY A 894     -41.812   6.191  -2.202  1.00 20.73           O  
ANISOU 1715  O   GLY A 894     2602   2628   2646     84    -42   -266       O  
ATOM   1716  N   ILE A 895     -43.660   7.496  -2.017  1.00 18.81           N  
ANISOU 1716  N   ILE A 895     2353   2390   2402     81    -27   -261       N  
ATOM   1717  CA  ILE A 895     -44.099   7.262  -3.361  1.00 19.52           C  
ANISOU 1717  CA  ILE A 895     2439   2471   2506     64    -19   -246       C  
ATOM   1718  C   ILE A 895     -43.857   8.547  -4.130  1.00 19.57           C  
ANISOU 1718  C   ILE A 895     2434   2467   2535     57    -21   -254       C  
ATOM   1719  O   ILE A 895     -44.333   9.597  -3.729  1.00 19.60           O  
ANISOU 1719  O   ILE A 895     2433   2470   2545     62    -22   -263       O  
ATOM   1720  CB  ILE A 895     -45.592   6.878  -3.432  1.00 19.53           C  
ANISOU 1720  CB  ILE A 895     2441   2477   2500     58     -6   -228       C  
ATOM   1721  CG1 ILE A 895     -45.888   5.715  -2.501  1.00 19.19           C  
ANISOU 1721  CG1 ILE A 895     2410   2443   2437     64     -1   -215       C  
ATOM   1722  CG2 ILE A 895     -45.972   6.503  -4.842  1.00 19.82           C  
ANISOU 1722  CG2 ILE A 895     2475   2506   2549     42     -3   -216       C  
ATOM   1723  CD1 ILE A 895     -47.369   5.530  -2.263  1.00 20.09           C  
ANISOU 1723  CD1 ILE A 895     2522   2566   2547     60     15   -201       C  
ATOM   1724  N   TYR A 896     -43.151   8.421  -5.249  1.00 18.56           N  
ANISOU 1724  N   TYR A 896     2302   2331   2419     45    -20   -251       N  
ATOM   1725  CA  TYR A 896     -42.668   9.515  -6.029  1.00 18.63           C  
ANISOU 1725  CA  TYR A 896     2302   2328   2449     37    -20   -255       C  
ATOM   1726  C   TYR A 896     -43.498   9.679  -7.302  1.00 18.50           C  
ANISOU 1726  C   TYR A 896     2286   2308   2436     26    -12   -236       C  
ATOM   1727  O   TYR A 896     -43.822   8.691  -7.966  1.00 19.55           O  
ANISOU 1727  O   TYR A 896     2425   2446   2558     21     -9   -225       O  
ATOM   1728  CB  TYR A 896     -41.195   9.243  -6.424  1.00 20.08           C  
ANISOU 1728  CB  TYR A 896     2479   2509   2642     33    -22   -263       C  
ATOM   1729  CG  TYR A 896     -40.199   9.423  -5.328  1.00 19.22           C  
ANISOU 1729  CG  TYR A 896     2364   2401   2539     44    -35   -286       C  
ATOM   1730  CD1 TYR A 896     -40.194   8.593  -4.241  1.00 19.54           C  
ANISOU 1730  CD1 TYR A 896     2413   2451   2559     59    -44   -292       C  
ATOM   1731  CD2 TYR A 896     -39.248  10.433  -5.384  1.00 20.11           C  
ANISOU 1731  CD2 TYR A 896     2461   2502   2678     40    -39   -301       C  
ATOM   1732  CE1 TYR A 896     -39.306   8.765  -3.211  1.00 19.82           C  
ANISOU 1732  CE1 TYR A 896     2445   2489   2596     73    -59   -315       C  
ATOM   1733  CE2 TYR A 896     -38.316  10.600  -4.346  1.00 19.88           C  
ANISOU 1733  CE2 TYR A 896     2424   2474   2656     52    -55   -327       C  
ATOM   1734  CZ  TYR A 896     -38.351   9.755  -3.285  1.00 19.65           C  
ANISOU 1734  CZ  TYR A 896     2406   2457   2602     70    -66   -335       C  
ATOM   1735  OH  TYR A 896     -37.500   9.889  -2.233  1.00 19.41           O  
ANISOU 1735  OH  TYR A 896     2370   2430   2573     86    -86   -361       O  
ATOM   1736  N   PHE A 897     -43.761  10.930  -7.668  1.00 18.07           N  
ANISOU 1736  N   PHE A 897     2226   2242   2397     23    -12   -234       N  
ATOM   1737  CA  PHE A 897     -44.532  11.315  -8.831  1.00 17.62           C  
ANISOU 1737  CA  PHE A 897     2172   2180   2343     16     -8   -217       C  
ATOM   1738  C   PHE A 897     -43.921  12.531  -9.502  1.00 17.48           C  
ANISOU 1738  C   PHE A 897     2149   2146   2345      8     -6   -212       C  
ATOM   1739  O   PHE A 897     -43.247  13.320  -8.863  1.00 18.22           O  
ANISOU 1739  O   PHE A 897     2235   2229   2458      9    -10   -225       O  
ATOM   1740  CB  PHE A 897     -45.951  11.732  -8.437  1.00 17.71           C  
ANISOU 1740  CB  PHE A 897     2183   2192   2354     23    -11   -215       C  
ATOM   1741  CG  PHE A 897     -46.736  10.646  -7.761  1.00 18.39           C  
ANISOU 1741  CG  PHE A 897     2271   2293   2422     28     -9   -216       C  
ATOM   1742  CD1 PHE A 897     -46.668  10.477  -6.413  1.00 17.94           C  
ANISOU 1742  CD1 PHE A 897     2214   2244   2358     38     -9   -228       C  
ATOM   1743  CD2 PHE A 897     -47.582   9.796  -8.508  1.00 19.05           C  
ANISOU 1743  CD2 PHE A 897     2357   2382   2498     23     -7   -203       C  
ATOM   1744  CE1 PHE A 897     -47.419   9.504  -5.787  1.00 17.53           C  
ANISOU 1744  CE1 PHE A 897     2164   2205   2290     41     -3   -223       C  
ATOM   1745  CE2 PHE A 897     -48.337   8.821  -7.894  1.00 17.88           C  
ANISOU 1745  CE2 PHE A 897     2208   2244   2341     24     -3   -201       C  
ATOM   1746  CZ  PHE A 897     -48.217   8.656  -6.533  1.00 18.87           C  
ANISOU 1746  CZ  PHE A 897     2335   2377   2458     33      0   -209       C  
ATOM   1747  N   ALA A 898     -44.168  12.670 -10.791  1.00 16.59           N  
ANISOU 1747  N   ALA A 898     2043   2031   2230      1     -1   -192       N  
ATOM   1748  CA  ALA A 898     -43.670  13.796 -11.579  1.00 17.01           C  
ANISOU 1748  CA  ALA A 898     2093   2067   2300     -8      4   -179       C  
ATOM   1749  C   ALA A 898     -44.854  14.538 -12.219  1.00 17.01           C  
ANISOU 1749  C   ALA A 898     2101   2059   2302     -5     -2   -162       C  
ATOM   1750  O   ALA A 898     -45.939  13.936 -12.405  1.00 15.37           O  
ANISOU 1750  O   ALA A 898     1899   1863   2078      2     -7   -160       O  
ATOM   1751  CB  ALA A 898     -42.798  13.284 -12.684  1.00 17.56           C  
ANISOU 1751  CB  ALA A 898     2166   2146   2360    -18     17   -167       C  
ATOM   1752  N   ASP A 899     -44.655  15.819 -12.530  1.00 17.61           N  
ANISOU 1752  N   ASP A 899     2176   2113   2400     -9     -2   -152       N  
ATOM   1753  CA  ASP A 899     -45.610  16.564 -13.356  1.00 18.47           C  
ANISOU 1753  CA  ASP A 899     2296   2212   2512     -5     -8   -131       C  
ATOM   1754  C   ASP A 899     -45.137  16.640 -14.794  1.00 19.18           C  
ANISOU 1754  C   ASP A 899     2397   2302   2589    -14      4   -102       C  
ATOM   1755  O   ASP A 899     -45.864  17.164 -15.649  1.00 19.47           O  
ANISOU 1755  O   ASP A 899     2446   2332   2621    -10     -2    -80       O  
ATOM   1756  CB  ASP A 899     -45.981  17.924 -12.796  1.00 19.23           C  
ANISOU 1756  CB  ASP A 899     2387   2281   2639      1    -20   -135       C  
ATOM   1757  CG  ASP A 899     -44.779  18.849 -12.565  1.00 21.23           C  
ANISOU 1757  CG  ASP A 899     2632   2509   2924    -11    -15   -137       C  
ATOM   1758  OD1 ASP A 899     -43.702  18.660 -13.163  1.00 23.86           O  
ANISOU 1758  OD1 ASP A 899     2964   2844   3257    -26      1   -125       O  
ATOM   1759  OD2 ASP A 899     -44.929  19.768 -11.721  1.00 22.03           O  
ANISOU 1759  OD2 ASP A 899     2725   2590   3054     -5    -27   -154       O  
ATOM   1760  N   MET A 900     -43.951  16.093 -15.082  1.00 19.94           N  
ANISOU 1760  N   MET A 900     2489   2408   2678    -26     20   -102       N  
ATOM   1761  CA  MET A 900     -43.459  15.960 -16.453  1.00 20.91           C  
ANISOU 1761  CA  MET A 900     2623   2541   2782    -33     36    -77       C  
ATOM   1762  C   MET A 900     -43.513  14.482 -16.858  1.00 20.60           C  
ANISOU 1762  C   MET A 900     2587   2531   2708    -28     38    -86       C  
ATOM   1763  O   MET A 900     -42.818  13.662 -16.272  1.00 19.62           O  
ANISOU 1763  O   MET A 900     2453   2418   2585    -30     43   -106       O  
ATOM   1764  CB  MET A 900     -42.009  16.474 -16.582  1.00 24.10           C  
ANISOU 1764  CB  MET A 900     3016   2935   3207    -50     57    -70       C  
ATOM   1765  CG  MET A 900     -41.812  17.924 -16.140  1.00 27.65           C  
ANISOU 1765  CG  MET A 900     3458   3349   3699    -58     53    -64       C  
ATOM   1766  SD  MET A 900     -42.451  19.088 -17.304  1.00 32.46           S  
ANISOU 1766  SD  MET A 900     4087   3937   4309    -59     54    -21       S  
ATOM   1767  CE  MET A 900     -41.183  19.091 -18.591  1.00 28.61           C  
ANISOU 1767  CE  MET A 900     3602   3459   3809    -78     90     12       C  
ATOM   1768  N   VAL A 901     -44.268  14.162 -17.910  1.00 19.33           N  
ANISOU 1768  N   VAL A 901     2442   2384   2519    -20     34    -72       N  
ATOM   1769  CA  VAL A 901     -44.456  12.774 -18.319  1.00 18.82           C  
ANISOU 1769  CA  VAL A 901     2382   2344   2426    -13     31    -84       C  
ATOM   1770  C   VAL A 901     -43.146  12.031 -18.528  1.00 20.04           C  
ANISOU 1770  C   VAL A 901     2530   2513   2572    -20     50    -93       C  
ATOM   1771  O   VAL A 901     -43.024  10.872 -18.149  1.00 21.32           O  
ANISOU 1771  O   VAL A 901     2687   2687   2727    -16     45   -114       O  
ATOM   1772  CB  VAL A 901     -45.358  12.651 -19.574  1.00 18.57           C  
ANISOU 1772  CB  VAL A 901     2368   2325   2365     -2     22    -69       C  
ATOM   1773  CG1 VAL A 901     -44.707  13.229 -20.822  1.00 18.55           C  
ANISOU 1773  CG1 VAL A 901     2378   2327   2343     -5     39    -41       C  
ATOM   1774  CG2 VAL A 901     -45.751  11.227 -19.825  1.00 19.32           C  
ANISOU 1774  CG2 VAL A 901     2464   2440   2438      5     12    -88       C  
ATOM   1775  N   SER A 902     -42.161  12.683 -19.126  1.00 21.12           N  
ANISOU 1775  N   SER A 902     2666   2649   2712    -30     71    -76       N  
ATOM   1776  CA  SER A 902     -40.909  12.012 -19.466  1.00 20.70           C  
ANISOU 1776  CA  SER A 902     2604   2613   2650    -35     91    -84       C  
ATOM   1777  C   SER A 902     -40.073  11.663 -18.242  1.00 21.13           C  
ANISOU 1777  C   SER A 902     2636   2660   2730    -40     90   -111       C  
ATOM   1778  O   SER A 902     -39.431  10.626 -18.204  1.00 21.60           O  
ANISOU 1778  O   SER A 902     2689   2735   2782    -37     94   -130       O  
ATOM   1779  CB  SER A 902     -40.102  12.872 -20.442  1.00 21.56           C  
ANISOU 1779  CB  SER A 902     2714   2722   2756    -46    118    -56       C  
ATOM   1780  OG  SER A 902     -39.774  14.140 -19.894  1.00 21.80           O  
ANISOU 1780  OG  SER A 902     2735   2724   2824    -60    123    -43       O  
ATOM   1781  N   LYS A 903     -40.135  12.491 -17.195  1.00 21.99           N  
ANISOU 1781  N   LYS A 903     2737   2747   2872    -45     82   -115       N  
ATOM   1782  CA  LYS A 903     -39.436  12.182 -15.952  1.00 20.55           C  
ANISOU 1782  CA  LYS A 903     2537   2559   2711    -46     76   -142       C  
ATOM   1783  C   LYS A 903     -39.925  10.870 -15.396  1.00 20.44           C  
ANISOU 1783  C   LYS A 903     2528   2558   2681    -33     61   -162       C  
ATOM   1784  O   LYS A 903     -39.129  10.042 -14.948  1.00 20.01           O  
ANISOU 1784  O   LYS A 903     2463   2511   2627    -30     61   -181       O  
ATOM   1785  CB  LYS A 903     -39.624  13.299 -14.927  1.00 21.35           C  
ANISOU 1785  CB  LYS A 903     2632   2636   2846    -49     65   -145       C  
ATOM   1786  CG  LYS A 903     -38.843  13.066 -13.651  1.00 22.27           C  
ANISOU 1786  CG  LYS A 903     2730   2748   2981    -47     57   -174       C  
ATOM   1787  CD  LYS A 903     -38.630  14.360 -12.866  1.00 22.27           C  
ANISOU 1787  CD  LYS A 903     2720   2724   3020    -52     50   -181       C  
ATOM   1788  CE  LYS A 903     -37.765  14.113 -11.639  1.00 22.45           C  
ANISOU 1788  CE  LYS A 903     2725   2745   3059    -48     39   -213       C  
ATOM   1789  NZ  LYS A 903     -37.717  15.327 -10.750  1.00 24.20           N  
ANISOU 1789  NZ  LYS A 903     2937   2942   3316    -48     26   -226       N  
ATOM   1790  N   SER A 904     -41.246  10.646 -15.445  1.00 21.86           N  
ANISOU 1790  N   SER A 904     2720   2738   2845    -25     47   -156       N  
ATOM   1791  CA  SER A 904     -41.822   9.375 -14.997  1.00 22.41           C  
ANISOU 1791  CA  SER A 904     2794   2818   2902    -16     35   -171       C  
ATOM   1792  C   SER A 904     -41.599   8.260 -16.004  1.00 21.51           C  
ANISOU 1792  C   SER A 904     2686   2721   2765    -12     38   -174       C  
ATOM   1793  O   SER A 904     -41.340   7.131 -15.613  1.00 21.73           O  
ANISOU 1793  O   SER A 904     2712   2755   2790     -7     32   -191       O  
ATOM   1794  CB  SER A 904     -43.308   9.512 -14.657  1.00 22.14           C  
ANISOU 1794  CB  SER A 904     2767   2778   2866    -10     20   -166       C  
ATOM   1795  OG  SER A 904     -43.469  10.149 -13.392  1.00 21.24           O  
ANISOU 1795  OG  SER A 904     2646   2652   2771     -9     15   -174       O  
ATOM   1796  N   ALA A 905     -41.758   8.558 -17.285  1.00 21.85           N  
ANISOU 1796  N   ALA A 905     2739   2774   2791    -13     46   -159       N  
ATOM   1797  CA  ALA A 905     -41.626   7.549 -18.340  1.00 21.67           C  
ANISOU 1797  CA  ALA A 905     2723   2770   2742     -6     48   -165       C  
ATOM   1798  C   ALA A 905     -40.242   6.922 -18.348  1.00 21.82           C  
ANISOU 1798  C   ALA A 905     2729   2798   2762     -6     61   -181       C  
ATOM   1799  O   ALA A 905     -40.097   5.774 -18.698  1.00 20.08           O  
ANISOU 1799  O   ALA A 905     2511   2589   2528      2     56   -197       O  
ATOM   1800  CB  ALA A 905     -41.919   8.158 -19.695  1.00 22.45           C  
ANISOU 1800  CB  ALA A 905     2834   2878   2817     -4     56   -144       C  
ATOM   1801  N   ASN A 906     -39.227   7.679 -17.926  1.00 23.20           N  
ANISOU 1801  N   ASN A 906     2891   2967   2958    -16     76   -178       N  
ATOM   1802  CA  ASN A 906     -37.875   7.119 -17.800  1.00 22.99           C  
ANISOU 1802  CA  ASN A 906     2848   2948   2938    -16     86   -197       C  
ATOM   1803  C   ASN A 906     -37.823   5.907 -16.866  1.00 23.17           C  
ANISOU 1803  C   ASN A 906     2867   2968   2966     -6     67   -222       C  
ATOM   1804  O   ASN A 906     -37.025   5.009 -17.088  1.00 23.91           O  
ANISOU 1804  O   ASN A 906     2955   3073   3057      1     70   -240       O  
ATOM   1805  CB  ASN A 906     -36.870   8.164 -17.337  1.00 23.11           C  
ANISOU 1805  CB  ASN A 906     2845   2954   2983    -28    101   -194       C  
ATOM   1806  CG  ASN A 906     -36.574   9.210 -18.392  1.00 23.44           C  
ANISOU 1806  CG  ASN A 906     2886   2999   3021    -40    126   -167       C  
ATOM   1807  OD1 ASN A 906     -36.823   9.015 -19.576  1.00 23.28           O  
ANISOU 1807  OD1 ASN A 906     2879   2996   2970    -36    137   -155       O  
ATOM   1808  ND2 ASN A 906     -36.050  10.342 -17.957  1.00 24.70           N  
ANISOU 1808  ND2 ASN A 906     3032   3141   3212    -54    135   -159       N  
ATOM   1809  N   TYR A 907     -38.697   5.857 -15.871  1.00 20.65           N  
ANISOU 1809  N   TYR A 907     2555   2635   2655     -4     49   -222       N  
ATOM   1810  CA  TYR A 907     -38.736   4.741 -14.952  1.00 20.06           C  
ANISOU 1810  CA  TYR A 907     2481   2556   2585      5     32   -239       C  
ATOM   1811  C   TYR A 907     -39.528   3.531 -15.457  1.00 20.80           C  
ANISOU 1811  C   TYR A 907     2587   2653   2662     13     21   -243       C  
ATOM   1812  O   TYR A 907     -39.629   2.513 -14.780  1.00 20.39           O  
ANISOU 1812  O   TYR A 907     2537   2594   2614     19      7   -253       O  
ATOM   1813  CB  TYR A 907     -39.252   5.211 -13.622  1.00 19.44           C  
ANISOU 1813  CB  TYR A 907     2404   2464   2520      4     22   -236       C  
ATOM   1814  CG  TYR A 907     -38.287   6.157 -12.976  1.00 19.09           C  
ANISOU 1814  CG  TYR A 907     2345   2414   2496      0     27   -241       C  
ATOM   1815  CD1 TYR A 907     -37.126   5.683 -12.378  1.00 19.74           C  
ANISOU 1815  CD1 TYR A 907     2415   2497   2588      6     23   -261       C  
ATOM   1816  CD2 TYR A 907     -38.504   7.530 -12.963  1.00 19.15           C  
ANISOU 1816  CD2 TYR A 907     2348   2412   2514     -9     33   -229       C  
ATOM   1817  CE1 TYR A 907     -36.222   6.546 -11.792  1.00 19.39           C  
ANISOU 1817  CE1 TYR A 907     2353   2447   2566      3     24   -270       C  
ATOM   1818  CE2 TYR A 907     -37.614   8.408 -12.347  1.00 18.74           C  
ANISOU 1818  CE2 TYR A 907     2282   2353   2487    -13     35   -238       C  
ATOM   1819  CZ  TYR A 907     -36.468   7.907 -11.773  1.00 19.49           C  
ANISOU 1819  CZ  TYR A 907     2363   2450   2593     -8     31   -259       C  
ATOM   1820  OH  TYR A 907     -35.578   8.742 -11.148  1.00 19.65           O  
ANISOU 1820  OH  TYR A 907     2365   2461   2640    -12     29   -271       O  
ATOM   1821  N   CYS A 908     -40.034   3.607 -16.680  1.00 21.75           N  
ANISOU 1821  N   CYS A 908     2716   2785   2765     13     25   -236       N  
ATOM   1822  CA  CYS A 908     -40.581   2.425 -17.325  1.00 22.82           C  
ANISOU 1822  CA  CYS A 908     2859   2924   2887     21     12   -247       C  
ATOM   1823  C   CYS A 908     -39.465   1.451 -17.745  1.00 24.74           C  
ANISOU 1823  C   CYS A 908     3097   3177   3126     31     15   -269       C  
ATOM   1824  O   CYS A 908     -39.712   0.260 -17.895  1.00 24.93           O  
ANISOU 1824  O   CYS A 908     3126   3198   3149     39      0   -285       O  
ATOM   1825  CB  CYS A 908     -41.434   2.802 -18.521  1.00 23.12           C  
ANISOU 1825  CB  CYS A 908     2908   2973   2905     22     12   -236       C  
ATOM   1826  SG  CYS A 908     -42.905   3.783 -18.145  1.00 23.44           S  
ANISOU 1826  SG  CYS A 908     2954   3001   2951     15      4   -214       S  
ATOM   1827  N   HIS A 909     -38.259   1.983 -17.962  1.00 26.54           N  
ANISOU 1827  N   HIS A 909     3312   3415   3355     29     34   -271       N  
ATOM   1828  CA  HIS A 909     -37.095   1.244 -18.421  1.00 27.46           C  
ANISOU 1828  CA  HIS A 909     3419   3546   3469     39     41   -294       C  
ATOM   1829  C   HIS A 909     -37.425   0.490 -19.699  1.00 28.91           C  
ANISOU 1829  C   HIS A 909     3613   3746   3627     50     39   -305       C  
ATOM   1830  O   HIS A 909     -37.118  -0.689 -19.843  1.00 26.93           O  
ANISOU 1830  O   HIS A 909     3360   3495   3376     63     27   -330       O  
ATOM   1831  CB  HIS A 909     -36.543   0.313 -17.340  1.00 28.61           C  
ANISOU 1831  CB  HIS A 909     3558   3677   3636     47     25   -313       C  
ATOM   1832  CG  HIS A 909     -35.977   1.037 -16.160  1.00 32.42           C  
ANISOU 1832  CG  HIS A 909     4029   4149   4139     40     27   -308       C  
ATOM   1833  ND1 HIS A 909     -34.774   1.711 -16.208  1.00 35.07           N  
ANISOU 1833  ND1 HIS A 909     4345   4494   4487     36     44   -313       N  
ATOM   1834  CD2 HIS A 909     -36.455   1.218 -14.905  1.00 32.37           C  
ANISOU 1834  CD2 HIS A 909     4028   4126   4146     37     13   -300       C  
ATOM   1835  CE1 HIS A 909     -34.550   2.299 -15.047  1.00 33.27           C  
ANISOU 1835  CE1 HIS A 909     4110   4253   4278     32     38   -311       C  
ATOM   1836  NE2 HIS A 909     -35.539   1.991 -14.230  1.00 32.77           N  
ANISOU 1836  NE2 HIS A 909     4063   4176   4214     34     19   -304       N  
ATOM   1837  N   THR A 910     -38.054   1.187 -20.641  1.00 29.68           N  
ANISOU 1837  N   THR A 910     3721   3856   3702     47     47   -288       N  
ATOM   1838  CA  THR A 910     -38.306   0.600 -21.915  1.00 31.65           C  
ANISOU 1838  CA  THR A 910     3980   4125   3921     60     45   -300       C  
ATOM   1839  C   THR A 910     -37.013   0.671 -22.749  1.00 32.38           C  
ANISOU 1839  C   THR A 910     4062   4245   3997     67     73   -309       C  
ATOM   1840  O   THR A 910     -36.057   1.294 -22.357  1.00 33.81           O  
ANISOU 1840  O   THR A 910     4227   4427   4193     57     94   -302       O  
ATOM   1841  CB  THR A 910     -39.452   1.291 -22.643  1.00 31.90           C  
ANISOU 1841  CB  THR A 910     4029   4162   3931     58     41   -279       C  
ATOM   1842  OG1 THR A 910     -39.219   2.703 -22.658  1.00 29.97           O  
ANISOU 1842  OG1 THR A 910     3783   3920   3686     46     64   -248       O  
ATOM   1843  CG2 THR A 910     -40.748   0.968 -21.984  1.00 31.38           C  
ANISOU 1843  CG2 THR A 910     3969   4073   3881     55     13   -277       C  
ATOM   1844  N   SER A 911     -37.002  -0.008 -23.885  1.00 36.15           N  
ANISOU 1844  N   SER A 911     4546   4744   4444     83     72   -328       N  
ATOM   1845  CA  SER A 911     -35.823  -0.055 -24.771  1.00 36.94           C  
ANISOU 1845  CA  SER A 911     4635   4876   4523     92    101   -340       C  
ATOM   1846  C   SER A 911     -36.302  -0.346 -26.174  1.00 39.24           C  
ANISOU 1846  C   SER A 911     4945   5196   4770    110    100   -347       C  
ATOM   1847  O   SER A 911     -37.491  -0.565 -26.406  1.00 36.75           O  
ANISOU 1847  O   SER A 911     4647   4873   4444    115     74   -347       O  
ATOM   1848  CB  SER A 911     -34.852  -1.144 -24.311  1.00 38.15           C  
ANISOU 1848  CB  SER A 911     4770   5026   4698    104     95   -376       C  
ATOM   1849  OG  SER A 911     -35.519  -2.407 -24.238  1.00 42.20           O  
ANISOU 1849  OG  SER A 911     5294   5525   5216    118     60   -403       O  
ATOM   1850  N   GLN A 912     -35.390  -0.317 -27.132  1.00 44.90           N  
ANISOU 1850  N   GLN A 912     5656   5948   5458    120    129   -355       N  
ATOM   1851  CA  GLN A 912     -35.751  -0.553 -28.531  1.00 44.45           C  
ANISOU 1851  CA  GLN A 912     5617   5924   5349    140    131   -363       C  
ATOM   1852  C   GLN A 912     -36.305  -1.951 -28.713  1.00 40.32           C  
ANISOU 1852  C   GLN A 912     5100   5395   4824    162     92   -407       C  
ATOM   1853  O   GLN A 912     -37.217  -2.151 -29.474  1.00 41.92           O  
ANISOU 1853  O   GLN A 912     5323   5607   4998    175     73   -412       O  
ATOM   1854  CB  GLN A 912     -34.560  -0.272 -29.442  1.00 51.68           C  
ANISOU 1854  CB  GLN A 912     6522   6880   6233    147    175   -363       C  
ATOM   1855  CG  GLN A 912     -34.527   1.208 -29.793  1.00 57.92           C  
ANISOU 1855  CG  GLN A 912     7320   7681   7008    129    209   -312       C  
ATOM   1856  CD  GLN A 912     -33.162   1.813 -30.039  1.00 64.37           C  
ANISOU 1856  CD  GLN A 912     8113   8520   7825    119    260   -299       C  
ATOM   1857  OE1 GLN A 912     -32.565   2.399 -29.120  1.00 76.70           O  
ANISOU 1857  OE1 GLN A 912     9653  10060   9431     96    273   -285       O  
ATOM   1858  NE2 GLN A 912     -32.672   1.729 -31.278  1.00 66.04           N  
ANISOU 1858  NE2 GLN A 912     8329   8777   7987    135    291   -302       N  
ATOM   1859  N   GLY A 913     -35.778  -2.893 -27.958  1.00 39.90           N  
ANISOU 1859  N   GLY A 913     5032   5324   4807    165     79   -436       N  
ATOM   1860  CA  GLY A 913     -36.246  -4.266 -27.968  1.00 43.54           C  
ANISOU 1860  CA  GLY A 913     5496   5769   5277    183     40   -477       C  
ATOM   1861  C   GLY A 913     -37.554  -4.506 -27.263  1.00 48.75           C  
ANISOU 1861  C   GLY A 913     6167   6391   5964    172      3   -468       C  
ATOM   1862  O   GLY A 913     -38.244  -5.470 -27.596  1.00 47.11           O  
ANISOU 1862  O   GLY A 913     5968   6174   5757    186    -29   -497       O  
ATOM   1863  N   ASP A 914     -37.890  -3.649 -26.281  1.00 52.35           N  
ANISOU 1863  N   ASP A 914     6622   6826   6445    148      8   -432       N  
ATOM   1864  CA  ASP A 914     -39.233  -3.616 -25.675  1.00 49.44           C  
ANISOU 1864  CA  ASP A 914     6262   6426   6095    136    -19   -417       C  
ATOM   1865  C   ASP A 914     -39.729  -2.165 -25.468  1.00 42.37           C  
ANISOU 1865  C   ASP A 914     5373   5531   5194    118     -4   -374       C  
ATOM   1866  O   ASP A 914     -39.607  -1.612 -24.370  1.00 36.97           O  
ANISOU 1866  O   ASP A 914     4680   4827   4538    101      4   -353       O  
ATOM   1867  CB  ASP A 914     -39.264  -4.390 -24.355  1.00 55.80           C  
ANISOU 1867  CB  ASP A 914     7059   7194   6947    128    -38   -424       C  
ATOM   1868  CG  ASP A 914     -40.708  -4.725 -23.918  1.00 67.92           C  
ANISOU 1868  CG  ASP A 914     8602   8700   8503    119    -69   -418       C  
ATOM   1869  OD1 ASP A 914     -40.872  -5.523 -22.975  1.00 70.61           O  
ANISOU 1869  OD1 ASP A 914     8940   9011   8879    114    -86   -424       O  
ATOM   1870  OD2 ASP A 914     -41.690  -4.227 -24.552  1.00 65.85           O  
ANISOU 1870  OD2 ASP A 914     8350   8447   8222    118    -76   -408       O  
ATOM   1871  N   PRO A 915     -40.282  -1.554 -26.528  1.00 34.40           N  
ANISOU 1871  N   PRO A 915     4378   4544   4147    124      0   -362       N  
ATOM   1872  CA  PRO A 915     -40.585  -0.140 -26.543  1.00 33.16           C  
ANISOU 1872  CA  PRO A 915     4227   4389   3981    111     17   -321       C  
ATOM   1873  C   PRO A 915     -42.007   0.264 -26.091  1.00 32.04           C  
ANISOU 1873  C   PRO A 915     4093   4225   3855    102     -8   -304       C  
ATOM   1874  O   PRO A 915     -42.395   1.421 -26.248  1.00 33.18           O  
ANISOU 1874  O   PRO A 915     4245   4372   3990     95      1   -272       O  
ATOM   1875  CB  PRO A 915     -40.400   0.199 -28.023  1.00 32.12           C  
ANISOU 1875  CB  PRO A 915     4111   4297   3797    127     32   -317       C  
ATOM   1876  CG  PRO A 915     -40.941  -1.027 -28.718  1.00 31.61           C  
ANISOU 1876  CG  PRO A 915     4054   4241   3717    150      0   -357       C  
ATOM   1877  CD  PRO A 915     -40.642  -2.184 -27.818  1.00 32.61           C  
ANISOU 1877  CD  PRO A 915     4164   4342   3885    148    -16   -387       C  
ATOM   1878  N   ILE A 916     -42.769  -0.667 -25.562  1.00 32.74           N  
ANISOU 1878  N   ILE A 916     4179   4292   3970    102    -38   -323       N  
ATOM   1879  CA  ILE A 916     -44.091  -0.375 -25.066  1.00 34.64           C  
ANISOU 1879  CA  ILE A 916     4420   4511   4229     93    -59   -310       C  
ATOM   1880  C   ILE A 916     -44.019  -0.371 -23.552  1.00 32.60           C  
ANISOU 1880  C   ILE A 916     4149   4224   4012     75    -55   -301       C  
ATOM   1881  O   ILE A 916     -43.570  -1.328 -22.951  1.00 34.13           O  
ANISOU 1881  O   ILE A 916     4335   4406   4227     75    -60   -319       O  
ATOM   1882  CB  ILE A 916     -45.102  -1.410 -25.552  1.00 40.49           C  
ANISOU 1882  CB  ILE A 916     5164   5247   4973    104    -94   -338       C  
ATOM   1883  CG1 ILE A 916     -45.229  -1.330 -27.080  1.00 44.76           C  
ANISOU 1883  CG1 ILE A 916     5720   5820   5466    125   -101   -349       C  
ATOM   1884  CG2 ILE A 916     -46.464  -1.136 -24.981  1.00 40.10           C  
ANISOU 1884  CG2 ILE A 916     5111   5177   4949     93   -114   -326       C  
ATOM   1885  CD1 ILE A 916     -46.228  -2.301 -27.685  1.00 50.13           C  
ANISOU 1885  CD1 ILE A 916     6402   6497   6147    139   -140   -382       C  
ATOM   1886  N   GLY A 917     -44.449   0.730 -22.954  1.00 29.68           N  
ANISOU 1886  N   GLY A 917     3778   3846   3653     63    -47   -273       N  
ATOM   1887  CA  GLY A 917     -44.467   0.882 -21.520  1.00 28.89           C  
ANISOU 1887  CA  GLY A 917     3668   3723   3585     48    -44   -263       C  
ATOM   1888  C   GLY A 917     -45.838   1.227 -20.967  1.00 28.00           C  
ANISOU 1888  C   GLY A 917     3554   3595   3491     41    -58   -251       C  
ATOM   1889  O   GLY A 917     -46.756   1.612 -21.705  1.00 29.17           O  
ANISOU 1889  O   GLY A 917     3708   3750   3627     46    -70   -246       O  
ATOM   1890  N   LEU A 918     -45.932   1.126 -19.647  1.00 25.51           N  
ANISOU 1890  N   LEU A 918     3229   3261   3203     31    -56   -246       N  
ATOM   1891  CA  LEU A 918     -47.088   1.470 -18.918  1.00 25.75           C  
ANISOU 1891  CA  LEU A 918     3254   3279   3252     23    -64   -235       C  
ATOM   1892  C   LEU A 918     -46.768   2.577 -17.914  1.00 26.37           C  
ANISOU 1892  C   LEU A 918     3329   3352   3339     16    -47   -217       C  
ATOM   1893  O   LEU A 918     -45.739   2.531 -17.182  1.00 24.23           O  
ANISOU 1893  O   LEU A 918     3055   3078   3073     13    -35   -218       O  
ATOM   1894  CB  LEU A 918     -47.622   0.246 -18.184  1.00 26.75           C  
ANISOU 1894  CB  LEU A 918     3374   3387   3401     18    -76   -246       C  
ATOM   1895  CG  LEU A 918     -48.154  -0.903 -19.032  1.00 26.29           C  
ANISOU 1895  CG  LEU A 918     3316   3327   3345     23    -98   -267       C  
ATOM   1896  CD1 LEU A 918     -48.556  -2.092 -18.169  1.00 24.96           C  
ANISOU 1896  CD1 LEU A 918     3140   3136   3207     14   -107   -272       C  
ATOM   1897  CD2 LEU A 918     -49.316  -0.447 -19.872  1.00 27.56           C  
ANISOU 1897  CD2 LEU A 918     3476   3495   3500     27   -113   -267       C  
ATOM   1898  N   ILE A 919     -47.676   3.564 -17.859  1.00 24.09           N  
ANISOU 1898  N   ILE A 919     3039   3062   3054     14    -49   -203       N  
ATOM   1899  CA  ILE A 919     -47.536   4.672 -16.953  1.00 22.74           C  
ANISOU 1899  CA  ILE A 919     2864   2884   2893     10    -37   -190       C  
ATOM   1900  C   ILE A 919     -48.878   5.016 -16.303  1.00 22.16           C  
ANISOU 1900  C   ILE A 919     2783   2803   2836      8    -45   -185       C  
ATOM   1901  O   ILE A 919     -49.947   4.921 -16.931  1.00 21.47           O  
ANISOU 1901  O   ILE A 919     2693   2717   2748     11    -59   -187       O  
ATOM   1902  CB  ILE A 919     -46.934   5.870 -17.708  1.00 24.10           C  
ANISOU 1902  CB  ILE A 919     3042   3061   3052     11    -27   -176       C  
ATOM   1903  CG1 ILE A 919     -46.484   6.941 -16.756  1.00 24.64           C  
ANISOU 1903  CG1 ILE A 919     3106   3120   3136      6    -15   -168       C  
ATOM   1904  CG2 ILE A 919     -47.936   6.473 -18.650  1.00 25.21           C  
ANISOU 1904  CG2 ILE A 919     3190   3207   3183     18    -38   -166       C  
ATOM   1905  CD1 ILE A 919     -45.521   7.903 -17.406  1.00 26.38           C  
ANISOU 1905  CD1 ILE A 919     3331   3343   3350      4     -1   -155       C  
ATOM   1906  N   LEU A 920     -48.829   5.417 -15.045  1.00 20.25           N  
ANISOU 1906  N   LEU A 920     2533   2553   2606      4    -36   -182       N  
ATOM   1907  CA  LEU A 920     -50.028   5.748 -14.290  1.00 19.74           C  
ANISOU 1907  CA  LEU A 920     2458   2484   2556      4    -39   -180       C  
ATOM   1908  C   LEU A 920     -50.279   7.246 -14.182  1.00 19.22           C  
ANISOU 1908  C   LEU A 920     2392   2416   2495      8    -37   -172       C  
ATOM   1909  O   LEU A 920     -49.346   8.029 -14.113  1.00 19.34           O  
ANISOU 1909  O   LEU A 920     2411   2428   2508      8    -29   -167       O  
ATOM   1910  CB  LEU A 920     -49.914   5.213 -12.877  1.00 19.52           C  
ANISOU 1910  CB  LEU A 920     2425   2453   2537      0    -30   -182       C  
ATOM   1911  CG  LEU A 920     -49.853   3.720 -12.749  1.00 20.76           C  
ANISOU 1911  CG  LEU A 920     2584   2607   2697     -5    -33   -187       C  
ATOM   1912  CD1 LEU A 920     -49.317   3.320 -11.379  1.00 22.11           C  
ANISOU 1912  CD1 LEU A 920     2756   2775   2869     -6    -23   -185       C  
ATOM   1913  CD2 LEU A 920     -51.220   3.118 -12.945  1.00 21.17           C  
ANISOU 1913  CD2 LEU A 920     2626   2657   2762    -10    -42   -187       C  
ATOM   1914  N   LEU A 921     -51.556   7.629 -14.162  1.00 19.52           N  
ANISOU 1914  N   LEU A 921     2420   2453   2543     12    -46   -171       N  
ATOM   1915  CA  LEU A 921     -51.942   8.931 -13.638  1.00 17.79           C  
ANISOU 1915  CA  LEU A 921     2197   2229   2336     18    -44   -167       C  
ATOM   1916  C   LEU A 921     -52.663   8.700 -12.340  1.00 17.46           C  
ANISOU 1916  C   LEU A 921     2140   2189   2305     17    -37   -174       C  
ATOM   1917  O   LEU A 921     -53.616   7.959 -12.273  1.00 18.92           O  
ANISOU 1917  O   LEU A 921     2314   2377   2497     15    -40   -177       O  
ATOM   1918  CB  LEU A 921     -52.822   9.675 -14.583  1.00 17.83           C  
ANISOU 1918  CB  LEU A 921     2201   2231   2342     26    -59   -162       C  
ATOM   1919  CG  LEU A 921     -52.111  10.308 -15.762  1.00 18.51           C  
ANISOU 1919  CG  LEU A 921     2304   2315   2414     29    -62   -148       C  
ATOM   1920  CD1 LEU A 921     -53.135  10.692 -16.807  1.00 19.23           C  
ANISOU 1920  CD1 LEU A 921     2398   2407   2502     39    -82   -143       C  
ATOM   1921  CD2 LEU A 921     -51.306  11.524 -15.356  1.00 18.98           C  
ANISOU 1921  CD2 LEU A 921     2368   2362   2482     28    -53   -140       C  
ATOM   1922  N   GLY A 922     -52.154   9.308 -11.277  1.00 17.80           N  
ANISOU 1922  N   GLY A 922     2183   2230   2351     20    -27   -178       N  
ATOM   1923  CA  GLY A 922     -52.735   9.195  -9.949  1.00 17.60           C  
ANISOU 1923  CA  GLY A 922     2146   2211   2331     23    -18   -184       C  
ATOM   1924  C   GLY A 922     -53.230  10.531  -9.458  1.00 17.40           C  
ANISOU 1924  C   GLY A 922     2112   2182   2316     35    -19   -191       C  
ATOM   1925  O   GLY A 922     -52.587  11.571  -9.685  1.00 18.09           O  
ANISOU 1925  O   GLY A 922     2207   2260   2408     39    -24   -192       O  
ATOM   1926  N   GLU A 923     -54.349  10.514  -8.772  1.00 17.41           N  
ANISOU 1926  N   GLU A 923     2098   2192   2324     39    -14   -197       N  
ATOM   1927  CA  GLU A 923     -54.775  11.679  -8.015  1.00 19.52           C  
ANISOU 1927  CA  GLU A 923     2356   2460   2600     53    -12   -209       C  
ATOM   1928  C   GLU A 923     -54.002  11.592  -6.691  1.00 19.23           C  
ANISOU 1928  C   GLU A 923     2325   2431   2551     57      0   -217       C  
ATOM   1929  O   GLU A 923     -54.127  10.605  -5.960  1.00 19.05           O  
ANISOU 1929  O   GLU A 923     2300   2421   2516     53     14   -214       O  
ATOM   1930  CB  GLU A 923     -56.277  11.666  -7.742  1.00 21.12           C  
ANISOU 1930  CB  GLU A 923     2537   2673   2815     59     -9   -214       C  
ATOM   1931  CG  GLU A 923     -56.760  12.896  -6.989  1.00 23.47           C  
ANISOU 1931  CG  GLU A 923     2823   2972   3123     77     -9   -231       C  
ATOM   1932  CD  GLU A 923     -58.221  12.805  -6.536  1.00 26.40           C  
ANISOU 1932  CD  GLU A 923     3168   3359   3505     83      0   -239       C  
ATOM   1933  OE1 GLU A 923     -59.027  12.209  -7.268  1.00 27.30           O  
ANISOU 1933  OE1 GLU A 923     3270   3474   3630     76     -5   -233       O  
ATOM   1934  OE2 GLU A 923     -58.578  13.411  -5.506  1.00 28.54           O  
ANISOU 1934  OE2 GLU A 923     3428   3640   3776     98     10   -255       O  
ATOM   1935  N   VAL A 924     -53.181  12.600  -6.420  1.00 18.80           N  
ANISOU 1935  N   VAL A 924     2277   2367   2500     65     -6   -227       N  
ATOM   1936  CA  VAL A 924     -52.372  12.615  -5.243  1.00 19.98           C  
ANISOU 1936  CA  VAL A 924     2431   2523   2637     71      0   -238       C  
ATOM   1937  C   VAL A 924     -52.808  13.770  -4.338  1.00 19.95           C  
ANISOU 1937  C   VAL A 924     2419   2522   2641     90     -1   -260       C  
ATOM   1938  O   VAL A 924     -52.861  14.927  -4.755  1.00 19.73           O  
ANISOU 1938  O   VAL A 924     2387   2476   2633     96    -14   -267       O  
ATOM   1939  CB  VAL A 924     -50.891  12.793  -5.609  1.00 20.51           C  
ANISOU 1939  CB  VAL A 924     2511   2576   2706     65     -7   -238       C  
ATOM   1940  CG1 VAL A 924     -50.014  12.690  -4.349  1.00 21.31           C  
ANISOU 1940  CG1 VAL A 924     2617   2686   2794     74     -5   -253       C  
ATOM   1941  CG2 VAL A 924     -50.459  11.732  -6.617  1.00 19.48           C  
ANISOU 1941  CG2 VAL A 924     2389   2444   2568     50     -6   -220       C  
ATOM   1942  N   ALA A 925     -53.109  13.454  -3.093  1.00 21.06           N  
ANISOU 1942  N   ALA A 925     2555   2683   2763    100     12   -270       N  
ATOM   1943  CA  ALA A 925     -53.568  14.473  -2.160  1.00 22.12           C  
ANISOU 1943  CA  ALA A 925     2680   2824   2900    122     11   -295       C  
ATOM   1944  C   ALA A 925     -52.348  15.093  -1.470  1.00 21.34           C  
ANISOU 1944  C   ALA A 925     2591   2719   2799    132      0   -315       C  
ATOM   1945  O   ALA A 925     -51.869  14.572  -0.472  1.00 21.27           O  
ANISOU 1945  O   ALA A 925     2590   2727   2764    139      7   -321       O  
ATOM   1946  CB  ALA A 925     -54.507  13.862  -1.145  1.00 21.94           C  
ANISOU 1946  CB  ALA A 925     2648   2831   2857    130     33   -296       C  
ATOM   1947  N   LEU A 926     -51.866  16.195  -2.013  1.00 20.79           N  
ANISOU 1947  N   LEU A 926     2521   2622   2755    132    -18   -324       N  
ATOM   1948  CA  LEU A 926     -50.585  16.762  -1.585  1.00 21.93           C  
ANISOU 1948  CA  LEU A 926     2672   2755   2907    136    -32   -342       C  
ATOM   1949  C   LEU A 926     -50.731  17.685  -0.390  1.00 22.70           C  
ANISOU 1949  C   LEU A 926     2763   2858   3004    162    -39   -378       C  
ATOM   1950  O   LEU A 926     -49.796  17.811   0.393  1.00 24.17           O  
ANISOU 1950  O   LEU A 926     2954   3046   3183    170    -48   -398       O  
ATOM   1951  CB  LEU A 926     -49.950  17.550  -2.710  1.00 21.13           C  
ANISOU 1951  CB  LEU A 926     2571   2619   2838    123    -46   -334       C  
ATOM   1952  CG  LEU A 926     -49.655  16.759  -3.956  1.00 20.82           C  
ANISOU 1952  CG  LEU A 926     2540   2575   2796    101    -40   -302       C  
ATOM   1953  CD1 LEU A 926     -49.360  17.694  -5.095  1.00 21.98           C  
ANISOU 1953  CD1 LEU A 926     2688   2691   2973     91    -50   -290       C  
ATOM   1954  CD2 LEU A 926     -48.484  15.829  -3.727  1.00 20.81           C  
ANISOU 1954  CD2 LEU A 926     2547   2582   2779     92    -36   -300       C  
ATOM   1955  N   GLY A 927     -51.887  18.322  -0.254  1.00 21.74           N  
ANISOU 1955  N   GLY A 927     2630   2739   2891    176    -38   -388       N  
ATOM   1956  CA  GLY A 927     -52.113  19.242   0.853  1.00 22.53           C  
ANISOU 1956  CA  GLY A 927     2723   2846   2992    203    -45   -427       C  
ATOM   1957  C   GLY A 927     -51.047  20.328   0.872  1.00 22.15           C  
ANISOU 1957  C   GLY A 927     2676   2766   2974    206    -71   -450       C  
ATOM   1958  O   GLY A 927     -50.668  20.829  -0.166  1.00 22.63           O  
ANISOU 1958  O   GLY A 927     2738   2793   3068    190    -82   -435       O  
ATOM   1959  N   ASN A 928     -50.584  20.663   2.054  1.00 22.34           N  
ANISOU 1959  N   ASN A 928     2701   2801   2986    227    -80   -485       N  
ATOM   1960  CA  ASN A 928     -49.459  21.575   2.248  1.00 24.86           C  
ANISOU 1960  CA  ASN A 928     3020   3092   3335    230   -106   -512       C  
ATOM   1961  C   ASN A 928     -48.123  20.896   2.001  1.00 23.29           C  
ANISOU 1961  C   ASN A 928     2830   2888   3132    211   -109   -498       C  
ATOM   1962  O   ASN A 928     -47.714  19.962   2.743  1.00 21.96           O  
ANISOU 1962  O   ASN A 928     2670   2749   2926    217   -102   -500       O  
ATOM   1963  CB  ASN A 928     -49.467  22.088   3.677  1.00 26.30           C  
ANISOU 1963  CB  ASN A 928     3199   3293   3501    264   -117   -561       C  
ATOM   1964  CG  ASN A 928     -50.693  22.857   3.997  1.00 27.32           C  
ANISOU 1964  CG  ASN A 928     3316   3427   3636    287   -116   -582       C  
ATOM   1965  OD1 ASN A 928     -51.157  23.661   3.174  1.00 31.66           O  
ANISOU 1965  OD1 ASN A 928     3858   3945   4226    281   -125   -577       O  
ATOM   1966  ND2 ASN A 928     -51.216  22.679   5.215  1.00 28.34           N  
ANISOU 1966  ND2 ASN A 928     3446   3597   3726    316   -107   -609       N  
ATOM   1967  N   MET A 929     -47.459  21.378   0.966  1.00 23.02           N  
ANISOU 1967  N   MET A 929     2792   2816   3137    189   -118   -484       N  
ATOM   1968  CA  MET A 929     -46.228  20.762   0.488  1.00 24.78           C  
ANISOU 1968  CA  MET A 929     3020   3033   3364    167   -118   -467       C  
ATOM   1969  C   MET A 929     -45.026  21.330   1.217  1.00 25.33           C  
ANISOU 1969  C   MET A 929     3083   3090   3452    174   -141   -504       C  
ATOM   1970  O   MET A 929     -44.908  22.535   1.386  1.00 23.77           O  
ANISOU 1970  O   MET A 929     2876   2864   3292    181   -160   -530       O  
ATOM   1971  CB  MET A 929     -46.089  21.017  -0.992  1.00 25.61           C  
ANISOU 1971  CB  MET A 929     3123   3107   3499    140   -113   -433       C  
ATOM   1972  CG  MET A 929     -47.190  20.366  -1.809  1.00 25.54           C  
ANISOU 1972  CG  MET A 929     3121   3112   3472    132    -94   -398       C  
ATOM   1973  SD  MET A 929     -47.129  20.756  -3.547  1.00 27.81           S  
ANISOU 1973  SD  MET A 929     3411   3366   3788    107    -91   -360       S  
ATOM   1974  CE  MET A 929     -47.180  22.533  -3.548  1.00 28.93           C  
ANISOU 1974  CE  MET A 929     3545   3466   3982    114   -112   -378       C  
ATOM   1975  N   TYR A 930     -44.156  20.436   1.648  1.00 24.40           N  
ANISOU 1975  N   TYR A 930     2969   2990   3310    173   -141   -506       N  
ATOM   1976  CA  TYR A 930     -42.848  20.793   2.160  1.00 25.05           C  
ANISOU 1976  CA  TYR A 930     3044   3061   3414    176   -163   -537       C  
ATOM   1977  C   TYR A 930     -41.967  20.945   0.930  1.00 24.55           C  
ANISOU 1977  C   TYR A 930     2971   2965   3390    143   -160   -513       C  
ATOM   1978  O   TYR A 930     -41.608  19.966   0.306  1.00 24.54           O  
ANISOU 1978  O   TYR A 930     2975   2974   3374    127   -144   -484       O  
ATOM   1979  CB  TYR A 930     -42.369  19.677   3.107  1.00 23.57           C  
ANISOU 1979  CB  TYR A 930     2867   2910   3179    192   -165   -546       C  
ATOM   1980  CG  TYR A 930     -41.111  19.922   3.889  1.00 24.55           C  
ANISOU 1980  CG  TYR A 930     2983   3030   3315    203   -193   -586       C  
ATOM   1981  CD1 TYR A 930     -40.686  21.202   4.235  1.00 25.35           C  
ANISOU 1981  CD1 TYR A 930     3069   3104   3460    210   -220   -627       C  
ATOM   1982  CD2 TYR A 930     -40.377  18.844   4.379  1.00 24.54           C  
ANISOU 1982  CD2 TYR A 930     2990   3053   3281    210   -197   -586       C  
ATOM   1983  CE1 TYR A 930     -39.527  21.392   4.971  1.00 25.08           C  
ANISOU 1983  CE1 TYR A 930     3024   3067   3438    221   -249   -666       C  
ATOM   1984  CE2 TYR A 930     -39.221  19.024   5.117  1.00 25.94           C  
ANISOU 1984  CE2 TYR A 930     3159   3229   3468    223   -226   -624       C  
ATOM   1985  CZ  TYR A 930     -38.810  20.297   5.419  1.00 26.98           C  
ANISOU 1985  CZ  TYR A 930     3273   3334   3644    229   -253   -666       C  
ATOM   1986  OH  TYR A 930     -37.681  20.448   6.194  1.00 28.08           O  
ANISOU 1986  OH  TYR A 930     3401   3473   3793    244   -285   -708       O  
ATOM   1987  N   GLU A 931     -41.630  22.182   0.589  1.00 25.56           N  
ANISOU 1987  N   GLU A 931     3086   3054   3572    134   -174   -525       N  
ATOM   1988  CA  GLU A 931     -40.915  22.460  -0.635  1.00 27.41           C  
ANISOU 1988  CA  GLU A 931     3312   3257   3846    103   -165   -498       C  
ATOM   1989  C   GLU A 931     -39.418  22.411  -0.405  1.00 26.62           C  
ANISOU 1989  C   GLU A 931     3196   3149   3771     93   -178   -518       C  
ATOM   1990  O   GLU A 931     -38.900  23.110   0.427  1.00 26.02           O  
ANISOU 1990  O   GLU A 931     3107   3059   3720    105   -203   -560       O  
ATOM   1991  CB  GLU A 931     -41.297  23.815  -1.174  1.00 29.59           C  
ANISOU 1991  CB  GLU A 931     3582   3492   4171     95   -172   -494       C  
ATOM   1992  CG  GLU A 931     -42.801  23.946  -1.306  1.00 34.97           C  
ANISOU 1992  CG  GLU A 931     4275   4181   4831    109   -165   -481       C  
ATOM   1993  CD  GLU A 931     -43.237  25.104  -2.197  1.00 38.72           C  
ANISOU 1993  CD  GLU A 931     4748   4613   5350     98   -168   -463       C  
ATOM   1994  OE1 GLU A 931     -42.403  25.966  -2.531  1.00 44.32           O  
ANISOU 1994  OE1 GLU A 931     5446   5282   6110     82   -178   -465       O  
ATOM   1995  OE2 GLU A 931     -44.404  25.108  -2.606  1.00 42.96           O  
ANISOU 1995  OE2 GLU A 931     5294   5155   5872    105   -160   -444       O  
ATOM   1996  N   LEU A 932     -38.722  21.572  -1.143  1.00 25.22           N  
ANISOU 1996  N   LEU A 932     3017   2979   3586     73   -161   -492       N  
ATOM   1997  CA  LEU A 932     -37.289  21.374  -0.903  1.00 24.85           C  
ANISOU 1997  CA  LEU A 932     2952   2929   3560     66   -171   -512       C  
ATOM   1998  C   LEU A 932     -36.559  21.535  -2.206  1.00 25.87           C  
ANISOU 1998  C   LEU A 932     3068   3035   3725     32   -152   -481       C  
ATOM   1999  O   LEU A 932     -37.043  21.096  -3.278  1.00 27.03           O  
ANISOU 1999  O   LEU A 932     3228   3189   3855     18   -126   -438       O  
ATOM   2000  CB  LEU A 932     -37.048  19.984  -0.312  1.00 23.28           C  
ANISOU 2000  CB  LEU A 932     2764   2771   3311     82   -171   -517       C  
ATOM   2001  CG  LEU A 932     -37.652  19.762   1.068  1.00 23.17           C  
ANISOU 2001  CG  LEU A 932     2764   2784   3257    117   -188   -546       C  
ATOM   2002  CD1 LEU A 932     -37.499  18.328   1.518  1.00 23.48           C  
ANISOU 2002  CD1 LEU A 932     2817   2859   3244    130   -184   -539       C  
ATOM   2003  CD2 LEU A 932     -37.021  20.703   2.088  1.00 24.21           C  
ANISOU 2003  CD2 LEU A 932     2880   2901   3417    134   -223   -599       C  
ATOM   2004  N   LYS A 933     -35.358  22.068  -2.115  1.00 27.25           N  
ANISOU 2004  N   LYS A 933     3218   3188   3948     20   -163   -503       N  
ATOM   2005  CA  LYS A 933     -34.487  22.210  -3.279  1.00 28.83           C  
ANISOU 2005  CA  LYS A 933     3401   3369   4184    -14   -141   -475       C  
ATOM   2006  C   LYS A 933     -33.405  21.173  -3.325  1.00 27.54           C  
ANISOU 2006  C   LYS A 933     3226   3229   4011    -18   -136   -481       C  
ATOM   2007  O   LYS A 933     -32.767  21.022  -4.354  1.00 30.98           O  
ANISOU 2007  O   LYS A 933     3649   3659   4462    -43   -111   -455       O  
ATOM   2008  CB  LYS A 933     -33.851  23.576  -3.286  1.00 31.83           C  
ANISOU 2008  CB  LYS A 933     3756   3703   4636    -30   -154   -492       C  
ATOM   2009  CG  LYS A 933     -34.833  24.704  -3.447  1.00 35.68           C  
ANISOU 2009  CG  LYS A 933     4254   4158   5144    -30   -159   -482       C  
ATOM   2010  CD  LYS A 933     -34.151  26.046  -3.258  1.00 40.76           C  
ANISOU 2010  CD  LYS A 933     4871   4752   5863    -44   -177   -506       C  
ATOM   2011  CE  LYS A 933     -35.158  27.007  -2.686  1.00 47.56           C  
ANISOU 2011  CE  LYS A 933     5744   5591   6737    -24   -201   -525       C  
ATOM   2012  NZ  LYS A 933     -34.746  28.424  -2.861  1.00 51.66           N  
ANISOU 2012  NZ  LYS A 933     6242   6051   7335    -43   -214   -533       N  
ATOM   2013  N   HIS A 934     -33.154  20.465  -2.224  1.00 26.00           N  
ANISOU 2013  N   HIS A 934     3031   3059   3787      8   -158   -515       N  
ATOM   2014  CA  HIS A 934     -32.050  19.501  -2.166  1.00 25.98           C  
ANISOU 2014  CA  HIS A 934     3015   3076   3779      8   -159   -526       C  
ATOM   2015  C   HIS A 934     -32.432  18.294  -1.350  1.00 23.98           C  
ANISOU 2015  C   HIS A 934     2785   2861   3465     38   -170   -534       C  
ATOM   2016  O   HIS A 934     -33.394  18.319  -0.647  1.00 24.81           O  
ANISOU 2016  O   HIS A 934     2912   2977   3539     59   -179   -539       O  
ATOM   2017  CB  HIS A 934     -30.796  20.167  -1.558  1.00 28.20           C  
ANISOU 2017  CB  HIS A 934     3261   3338   4115      6   -185   -570       C  
ATOM   2018  CG  HIS A 934     -30.469  21.499  -2.165  1.00 29.21           C  
ANISOU 2018  CG  HIS A 934     3366   3422   4311    -23   -178   -565       C  
ATOM   2019  ND1 HIS A 934     -29.862  21.618  -3.396  1.00 29.51           N  
ANISOU 2019  ND1 HIS A 934     3386   3446   4380    -57   -146   -532       N  
ATOM   2020  CD2 HIS A 934     -30.689  22.765  -1.732  1.00 30.32           C  
ANISOU 2020  CD2 HIS A 934     3498   3528   4493    -24   -198   -587       C  
ATOM   2021  CE1 HIS A 934     -29.718  22.897  -3.694  1.00 30.69           C  
ANISOU 2021  CE1 HIS A 934     3518   3553   4588    -79   -145   -530       C  
ATOM   2022  NE2 HIS A 934     -30.210  23.615  -2.699  1.00 31.11           N  
ANISOU 2022  NE2 HIS A 934     3576   3591   4652    -59   -179   -564       N  
ATOM   2023  N   ALA A 935     -31.664  17.230  -1.476  1.00 24.57           N  
ANISOU 2023  N   ALA A 935     2855   2955   3526     40   -166   -534       N  
ATOM   2024  CA  ALA A 935     -31.959  15.947  -0.844  1.00 24.81           C  
ANISOU 2024  CA  ALA A 935     2909   3018   3501     66   -174   -534       C  
ATOM   2025  C   ALA A 935     -32.237  16.112   0.650  1.00 26.27           C  
ANISOU 2025  C   ALA A 935     3105   3214   3663     98   -207   -569       C  
ATOM   2026  O   ALA A 935     -31.562  16.865   1.342  1.00 28.14           O  
ANISOU 2026  O   ALA A 935     3322   3438   3931    106   -234   -608       O  
ATOM   2027  CB  ALA A 935     -30.804  14.976  -1.067  1.00 23.87           C  
ANISOU 2027  CB  ALA A 935     2774   2910   3383     65   -175   -540       C  
ATOM   2028  N   SER A 936     -33.207  15.357   1.138  1.00 25.59           N  
ANISOU 2028  N   SER A 936     3050   3152   3522    118   -203   -554       N  
ATOM   2029  CA  SER A 936     -33.526  15.303   2.539  1.00 25.05           C  
ANISOU 2029  CA  SER A 936     2996   3101   3419    152   -228   -581       C  
ATOM   2030  C   SER A 936     -34.334  14.028   2.766  1.00 24.75           C  
ANISOU 2030  C   SER A 936     2991   3092   3322    165   -215   -551       C  
ATOM   2031  O   SER A 936     -35.456  13.897   2.270  1.00 24.64           O  
ANISOU 2031  O   SER A 936     2991   3080   3290    155   -190   -519       O  
ATOM   2032  CB  SER A 936     -34.342  16.507   2.905  1.00 24.68           C  
ANISOU 2032  CB  SER A 936     2952   3043   3383    156   -233   -594       C  
ATOM   2033  OG  SER A 936     -34.450  16.583   4.307  1.00 26.69           O  
ANISOU 2033  OG  SER A 936     3217   3317   3608    191   -260   -629       O  
ATOM   2034  N   HIS A 937     -33.755  13.104   3.509  1.00 24.07           N  
ANISOU 2034  N   HIS A 937     2913   3024   3208    187   -233   -562       N  
ATOM   2035  CA  HIS A 937     -34.343  11.812   3.766  1.00 24.66           C  
ANISOU 2035  CA  HIS A 937     3016   3121   3231    199   -222   -533       C  
ATOM   2036  C   HIS A 937     -35.418  11.919   4.850  1.00 23.66           C  
ANISOU 2036  C   HIS A 937     2915   3015   3059    223   -223   -533       C  
ATOM   2037  O   HIS A 937     -35.157  11.741   6.023  1.00 24.22           O  
ANISOU 2037  O   HIS A 937     2998   3105   3101    253   -247   -555       O  
ATOM   2038  CB  HIS A 937     -33.277  10.781   4.168  1.00 26.01           C  
ANISOU 2038  CB  HIS A 937     3189   3302   3390    216   -243   -542       C  
ATOM   2039  CG  HIS A 937     -32.289  10.449   3.095  1.00 29.64           C  
ANISOU 2039  CG  HIS A 937     3627   3748   3889    194   -238   -539       C  
ATOM   2040  ND1 HIS A 937     -32.227  11.092   1.872  1.00 35.63           N  
ANISOU 2040  ND1 HIS A 937     4363   4487   4689    162   -215   -529       N  
ATOM   2041  CD2 HIS A 937     -31.258   9.580   3.100  1.00 33.74           C  
ANISOU 2041  CD2 HIS A 937     4139   4271   4411    203   -252   -547       C  
ATOM   2042  CE1 HIS A 937     -31.239  10.590   1.150  1.00 33.23           C  
ANISOU 2042  CE1 HIS A 937     4040   4178   4407    151   -212   -530       C  
ATOM   2043  NE2 HIS A 937     -30.636   9.670   1.875  1.00 34.69           N  
ANISOU 2043  NE2 HIS A 937     4233   4376   4573    176   -235   -543       N  
ATOM   2044  N   ILE A 938     -36.639  12.187   4.434  1.00 23.07           N  
ANISOU 2044  N   ILE A 938     2848   2940   2978    211   -197   -509       N  
ATOM   2045  CA  ILE A 938     -37.722  12.451   5.346  1.00 24.25           C  
ANISOU 2045  CA  ILE A 938     3014   3109   3092    231   -193   -511       C  
ATOM   2046  C   ILE A 938     -38.071  11.169   6.067  1.00 23.52           C  
ANISOU 2046  C   ILE A 938     2949   3042   2944    249   -187   -488       C  
ATOM   2047  O   ILE A 938     -38.243  10.153   5.419  1.00 24.40           O  
ANISOU 2047  O   ILE A 938     3068   3151   3050    233   -170   -454       O  
ATOM   2048  CB  ILE A 938     -38.953  12.897   4.576  1.00 25.13           C  
ANISOU 2048  CB  ILE A 938     3123   3211   3212    211   -165   -487       C  
ATOM   2049  CG1 ILE A 938     -38.658  14.145   3.747  1.00 25.56           C  
ANISOU 2049  CG1 ILE A 938     3154   3235   3322    191   -168   -501       C  
ATOM   2050  CG2 ILE A 938     -40.102  13.137   5.519  1.00 26.17           C  
ANISOU 2050  CG2 ILE A 938     3270   3366   3308    232   -157   -490       C  
ATOM   2051  CD1 ILE A 938     -38.151  15.330   4.550  1.00 27.64           C  
ANISOU 2051  CD1 ILE A 938     3404   3491   3607    208   -197   -549       C  
ATOM   2052  N   SER A 939     -38.068  11.203   7.400  1.00 23.51           N  
ANISOU 2052  N   SER A 939     2963   3065   2905    282   -204   -509       N  
ATOM   2053  CA ASER A 939     -38.606  10.113   8.224  0.50 23.91           C  
ANISOU 2053  CA ASER A 939     3044   3144   2899    301   -194   -483       C  
ATOM   2054  CA BSER A 939     -38.612  10.143   8.247  0.50 23.21           C  
ANISOU 2054  CA BSER A 939     2955   3055   2809    301   -194   -484       C  
ATOM   2055  C   SER A 939     -39.942  10.527   8.803  1.00 23.95           C  
ANISOU 2055  C   SER A 939     3059   3169   2873    311   -172   -477       C  
ATOM   2056  O   SER A 939     -40.772   9.690   9.011  1.00 26.13           O  
ANISOU 2056  O   SER A 939     3353   3460   3114    310   -147   -441       O  
ATOM   2057  CB ASER A 939     -37.633   9.677   9.334  0.50 24.75           C  
ANISOU 2057  CB ASER A 939     3164   3266   2974    335   -227   -504       C  
ATOM   2058  CB BSER A 939     -37.728   9.951   9.458  0.50 23.35           C  
ANISOU 2058  CB BSER A 939     2985   3091   2796    338   -228   -511       C  
ATOM   2059  OG ASER A 939     -36.463   9.098   8.770  0.50 24.80           O  
ANISOU 2059  OG ASER A 939     3161   3255   3007    326   -245   -505       O  
ATOM   2060  OG BSER A 939     -38.133   8.849  10.252  0.50 21.81           O  
ANISOU 2060  OG BSER A 939     2823   2921   2545    357   -219   -481       O  
ATOM   2061  N   LYS A 940     -40.126  11.816   9.098  1.00 25.20           N  
ANISOU 2061  N   LYS A 940     3203   3327   3045    320   -182   -514       N  
ATOM   2062  CA  LYS A 940     -41.432  12.336   9.465  1.00 26.10           C  
ANISOU 2062  CA  LYS A 940     3320   3457   3140    327   -160   -512       C  
ATOM   2063  C   LYS A 940     -41.517  13.737   8.930  1.00 26.63           C  
ANISOU 2063  C   LYS A 940     3363   3501   3257    317   -168   -542       C  
ATOM   2064  O   LYS A 940     -40.586  14.524   9.107  1.00 28.57           O  
ANISOU 2064  O   LYS A 940     3594   3731   3529    326   -199   -582       O  
ATOM   2065  CB  LYS A 940     -41.706  12.364  10.989  1.00 27.25           C  
ANISOU 2065  CB  LYS A 940     3486   3642   3226    368   -166   -531       C  
ATOM   2066  N   LEU A 941     -42.631  14.051   8.285  1.00 24.65           N  
ANISOU 2066  N   LEU A 941     3104   3243   3020    300   -142   -523       N  
ATOM   2067  CA  LEU A 941     -42.873  15.380   7.777  1.00 25.21           C  
ANISOU 2067  CA  LEU A 941     3154   3290   3136    292   -148   -547       C  
ATOM   2068  C   LEU A 941     -43.029  16.382   8.916  1.00 26.21           C  
ANISOU 2068  C   LEU A 941     3279   3430   3249    327   -167   -595       C  
ATOM   2069  O   LEU A 941     -43.449  16.015   9.984  1.00 26.94           O  
ANISOU 2069  O   LEU A 941     3387   3559   3289    354   -161   -600       O  
ATOM   2070  CB  LEU A 941     -44.140  15.394   6.926  1.00 24.60           C  
ANISOU 2070  CB  LEU A 941     3071   3206   3069    272   -117   -515       C  
ATOM   2071  CG  LEU A 941     -44.010  14.725   5.563  1.00 26.58           C  
ANISOU 2071  CG  LEU A 941     3318   3435   3345    237   -104   -475       C  
ATOM   2072  CD1 LEU A 941     -45.380  14.632   4.878  1.00 26.03           C  
ANISOU 2072  CD1 LEU A 941     3245   3366   3278    222    -76   -446       C  
ATOM   2073  CD2 LEU A 941     -43.045  15.504   4.689  1.00 26.18           C  
ANISOU 2073  CD2 LEU A 941     3251   3349   3347    219   -122   -488       C  
ATOM   2074  N   PRO A 942     -42.719  17.659   8.666  1.00 26.84           N  
ANISOU 2074  N   PRO A 942     3339   3481   3377    325   -188   -630       N  
ATOM   2075  CA  PRO A 942     -43.086  18.659   9.644  1.00 28.30           C  
ANISOU 2075  CA  PRO A 942     3521   3678   3554    357   -204   -677       C  
ATOM   2076  C   PRO A 942     -44.582  18.604   9.873  1.00 30.07           C  
ANISOU 2076  C   PRO A 942     3751   3928   3748    367   -173   -662       C  
ATOM   2077  O   PRO A 942     -45.349  18.408   8.913  1.00 31.24           O  
ANISOU 2077  O   PRO A 942     3893   4064   3912    341   -147   -625       O  
ATOM   2078  CB  PRO A 942     -42.689  19.992   8.978  1.00 28.06           C  
ANISOU 2078  CB  PRO A 942     3467   3601   3595    343   -227   -705       C  
ATOM   2079  CG  PRO A 942     -41.637  19.624   7.992  1.00 28.60           C  
ANISOU 2079  CG  PRO A 942     3527   3640   3701    310   -231   -682       C  
ATOM   2080  CD  PRO A 942     -41.927  18.214   7.551  1.00 27.14           C  
ANISOU 2080  CD  PRO A 942     3358   3475   3480    295   -201   -630       C  
ATOM   2081  N   LYS A 943     -45.002  18.787  11.123  1.00 29.88           N  
ANISOU 2081  N   LYS A 943     3735   3940   3677    405   -175   -692       N  
ATOM   2082  CA  LYS A 943     -46.413  18.742  11.474  1.00 31.03           C  
ANISOU 2082  CA  LYS A 943     3884   4116   3790    417   -142   -682       C  
ATOM   2083  C   LYS A 943     -47.102  19.808  10.628  1.00 29.63           C  
ANISOU 2083  C   LYS A 943     3683   3906   3668    404   -141   -690       C  
ATOM   2084  O   LYS A 943     -46.585  20.924  10.439  1.00 28.63           O  
ANISOU 2084  O   LYS A 943     3544   3745   3590    406   -172   -727       O  
ATOM   2085  CB  LYS A 943     -46.592  18.965  12.994  1.00 33.14           C  
ANISOU 2085  CB  LYS A 943     4162   4428   4000    465   -149   -722       C  
ATOM   2086  N   GLY A 944     -48.226  19.442  10.028  1.00 27.61           N  
ANISOU 2086  N   GLY A 944     3423   3655   3411    387   -108   -653       N  
ATOM   2087  CA  GLY A 944     -48.930  20.349   9.144  1.00 26.54           C  
ANISOU 2087  CA  GLY A 944     3268   3488   3327    375   -107   -655       C  
ATOM   2088  C   GLY A 944     -48.627  20.227   7.666  1.00 26.58           C  
ANISOU 2088  C   GLY A 944     3268   3453   3380    335   -107   -618       C  
ATOM   2089  O   GLY A 944     -49.365  20.767   6.836  1.00 30.04           O  
ANISOU 2089  O   GLY A 944     3693   3869   3853    323   -102   -608       O  
ATOM   2090  N   LYS A 945     -47.569  19.517   7.315  1.00 25.88           N  
ANISOU 2090  N   LYS A 945     3188   3354   3292    315   -114   -599       N  
ATOM   2091  CA  LYS A 945     -47.222  19.239   5.906  1.00 26.04           C  
ANISOU 2091  CA  LYS A 945     3205   3341   3349    278   -110   -561       C  
ATOM   2092  C   LYS A 945     -47.698  17.833   5.540  1.00 24.79           C  
ANISOU 2092  C   LYS A 945     3057   3204   3159    261    -80   -514       C  
ATOM   2093  O   LYS A 945     -47.613  16.932   6.367  1.00 24.74           O  
ANISOU 2093  O   LYS A 945     3064   3229   3107    273    -71   -508       O  
ATOM   2094  CB  LYS A 945     -45.718  19.294   5.714  1.00 27.03           C  
ANISOU 2094  CB  LYS A 945     3329   3443   3497    267   -134   -571       C  
ATOM   2095  CG  LYS A 945     -45.128  20.652   6.068  1.00 27.21           C  
ANISOU 2095  CG  LYS A 945     3340   3440   3559    281   -167   -619       C  
ATOM   2096  CD  LYS A 945     -45.481  21.661   5.017  1.00 27.54           C  
ANISOU 2096  CD  LYS A 945     3368   3440   3655    263   -169   -612       C  
ATOM   2097  CE  LYS A 945     -44.686  22.930   5.210  1.00 26.97           C  
ANISOU 2097  CE  LYS A 945     3282   3332   3633    268   -202   -654       C  
ATOM   2098  NZ  LYS A 945     -45.051  23.916   4.186  1.00 28.14           N  
ANISOU 2098  NZ  LYS A 945     3420   3437   3835    251   -205   -642       N  
ATOM   2099  N   HIS A 946     -48.177  17.650   4.313  1.00 24.28           N  
ANISOU 2099  N   HIS A 946     2986   3121   3118    235    -68   -481       N  
ATOM   2100  CA  HIS A 946     -48.688  16.340   3.908  1.00 23.64           C  
ANISOU 2100  CA  HIS A 946     2913   3057   3014    219    -42   -440       C  
ATOM   2101  C   HIS A 946     -47.908  15.695   2.791  1.00 23.52           C  
ANISOU 2101  C   HIS A 946     2901   3020   3016    190    -45   -412       C  
ATOM   2102  O   HIS A 946     -48.140  14.532   2.469  1.00 22.23           O  
ANISOU 2102  O   HIS A 946     2745   2866   2835    177    -28   -381       O  
ATOM   2103  CB  HIS A 946     -50.132  16.474   3.489  1.00 24.76           C  
ANISOU 2103  CB  HIS A 946     3043   3203   3162    215    -24   -427       C  
ATOM   2104  CG  HIS A 946     -50.959  17.228   4.463  1.00 26.45           C  
ANISOU 2104  CG  HIS A 946     3248   3437   3364    244    -20   -457       C  
ATOM   2105  ND1 HIS A 946     -51.191  18.578   4.322  1.00 28.78           N  
ANISOU 2105  ND1 HIS A 946     3530   3710   3693    255    -38   -486       N  
ATOM   2106  CD2 HIS A 946     -51.551  16.856   5.617  1.00 26.31           C  
ANISOU 2106  CD2 HIS A 946     3234   3458   3305    265     -2   -465       C  
ATOM   2107  CE1 HIS A 946     -51.914  19.004   5.341  1.00 27.85           C  
ANISOU 2107  CE1 HIS A 946     3407   3620   3557    284    -31   -514       C  
ATOM   2108  NE2 HIS A 946     -52.143  17.977   6.139  1.00 28.06           N  
ANISOU 2108  NE2 HIS A 946     3442   3684   3534    290     -8   -501       N  
ATOM   2109  N   SER A 947     -46.958  16.429   2.214  1.00 21.64           N  
ANISOU 2109  N   SER A 947     2657   2752   2813    181    -64   -423       N  
ATOM   2110  CA  SER A 947     -46.166  15.901   1.130  1.00 21.32           C  
ANISOU 2110  CA  SER A 947     2619   2693   2788    156    -64   -399       C  
ATOM   2111  C   SER A 947     -44.890  16.697   0.947  1.00 21.65           C  
ANISOU 2111  C   SER A 947     2654   2710   2864    151    -85   -419       C  
ATOM   2112  O   SER A 947     -44.728  17.771   1.538  1.00 23.58           O  
ANISOU 2112  O   SER A 947     2889   2943   3125    166   -102   -452       O  
ATOM   2113  CB  SER A 947     -46.965  15.985  -0.148  1.00 21.54           C  
ANISOU 2113  CB  SER A 947     2642   2707   2834    137    -53   -372       C  
ATOM   2114  OG  SER A 947     -47.295  17.316  -0.458  1.00 20.01           O  
ANISOU 2114  OG  SER A 947     2439   2491   2674    140    -63   -385       O  
ATOM   2115  N   VAL A 948     -43.973  16.159   0.167  1.00 19.94           N  
ANISOU 2115  N   VAL A 948     2437   2483   2658    132    -84   -403       N  
ATOM   2116  CA  VAL A 948     -42.815  16.899  -0.260  1.00 20.04           C  
ANISOU 2116  CA  VAL A 948     2438   2469   2709    121    -98   -415       C  
ATOM   2117  C   VAL A 948     -42.955  17.265  -1.727  1.00 20.21           C  
ANISOU 2117  C   VAL A 948     2455   2466   2758     96    -87   -387       C  
ATOM   2118  O   VAL A 948     -43.379  16.427  -2.549  1.00 19.66           O  
ANISOU 2118  O   VAL A 948     2393   2405   2672     85    -71   -357       O  
ATOM   2119  CB  VAL A 948     -41.519  16.109  -0.054  1.00 19.53           C  
ANISOU 2119  CB  VAL A 948     2373   2410   2638    119   -105   -421       C  
ATOM   2120  CG1 VAL A 948     -40.358  16.767  -0.792  1.00 20.40           C  
ANISOU 2120  CG1 VAL A 948     2466   2492   2792    100   -112   -426       C  
ATOM   2121  CG2 VAL A 948     -41.173  16.039   1.422  1.00 20.51           C  
ANISOU 2121  CG2 VAL A 948     2501   2553   2739    146   -123   -455       C  
ATOM   2122  N   LYS A 949     -42.586  18.497  -2.061  1.00 20.04           N  
ANISOU 2122  N   LYS A 949     2422   2414   2777     89    -97   -396       N  
ATOM   2123  CA  LYS A 949     -42.367  18.881  -3.463  1.00 20.56           C  
ANISOU 2123  CA  LYS A 949     2486   2456   2871     65    -87   -368       C  
ATOM   2124  C   LYS A 949     -40.903  19.224  -3.663  1.00 21.07           C  
ANISOU 2124  C   LYS A 949     2537   2502   2969     50    -93   -377       C  
ATOM   2125  O   LYS A 949     -40.394  20.159  -3.036  1.00 22.19           O  
ANISOU 2125  O   LYS A 949     2665   2623   3142     55   -111   -406       O  
ATOM   2126  CB  LYS A 949     -43.175  20.105  -3.813  1.00 20.40           C  
ANISOU 2126  CB  LYS A 949     2463   2409   2877     66    -92   -364       C  
ATOM   2127  CG  LYS A 949     -42.964  20.553  -5.235  1.00 20.76           C  
ANISOU 2127  CG  LYS A 949     2510   2431   2949     43    -83   -331       C  
ATOM   2128  CD  LYS A 949     -43.810  21.739  -5.570  1.00 21.73           C  
ANISOU 2128  CD  LYS A 949     2633   2526   3097     47    -91   -325       C  
ATOM   2129  CE  LYS A 949     -43.585  22.142  -6.999  1.00 23.56           C  
ANISOU 2129  CE  LYS A 949     2869   2734   3348     25    -80   -286       C  
ATOM   2130  NZ  LYS A 949     -44.254  23.410  -7.303  1.00 25.49           N  
ANISOU 2130  NZ  LYS A 949     3115   2945   3624     30    -91   -279       N  
ATOM   2131  N   GLY A 950     -40.220  18.454  -4.503  1.00 20.83           N  
ANISOU 2131  N   GLY A 950     2505   2477   2932     33    -78   -355       N  
ATOM   2132  CA  GLY A 950     -38.862  18.787  -4.915  1.00 22.46           C  
ANISOU 2132  CA  GLY A 950     2695   2666   3174     15    -77   -358       C  
ATOM   2133  C   GLY A 950     -38.978  19.842  -5.992  1.00 22.94           C  
ANISOU 2133  C   GLY A 950     2752   2695   3268     -4    -67   -333       C  
ATOM   2134  O   GLY A 950     -39.621  19.588  -6.992  1.00 24.50           O  
ANISOU 2134  O   GLY A 950     2964   2898   3449    -11    -51   -299       O  
ATOM   2135  N   LEU A 951     -38.369  21.004  -5.788  1.00 23.18           N  
ANISOU 2135  N   LEU A 951     2766   2693   3347    -12    -79   -348       N  
ATOM   2136  CA  LEU A 951     -38.544  22.150  -6.686  1.00 24.21           C  
ANISOU 2136  CA  LEU A 951     2896   2788   3515    -29    -72   -323       C  
ATOM   2137  C   LEU A 951     -37.630  22.077  -7.904  1.00 25.56           C  
ANISOU 2137  C   LEU A 951     3060   2952   3701    -57    -47   -291       C  
ATOM   2138  O   LEU A 951     -36.429  22.165  -7.768  1.00 26.06           O  
ANISOU 2138  O   LEU A 951     3101   3007   3794    -70    -46   -305       O  
ATOM   2139  CB  LEU A 951     -38.271  23.434  -5.949  1.00 24.54           C  
ANISOU 2139  CB  LEU A 951     2922   2794   3608    -26    -95   -353       C  
ATOM   2140  CG  LEU A 951     -39.213  23.676  -4.786  1.00 26.42           C  
ANISOU 2140  CG  LEU A 951     3167   3039   3832      4   -119   -387       C  
ATOM   2141  CD1 LEU A 951     -38.869  24.989  -4.084  1.00 27.86           C  
ANISOU 2141  CD1 LEU A 951     3333   3183   4069      8   -145   -423       C  
ATOM   2142  CD2 LEU A 951     -40.658  23.715  -5.254  1.00 26.70           C  
ANISOU 2142  CD2 LEU A 951     3223   3080   3842     14   -112   -362       C  
ATOM   2143  N   GLY A 952     -38.210  21.895  -9.094  1.00 26.64           N  
ANISOU 2143  N   GLY A 952     3213   3093   3815    -65    -27   -249       N  
ATOM   2144  CA  GLY A 952     -37.433  21.915 -10.343  1.00 27.25           C  
ANISOU 2144  CA  GLY A 952     3286   3166   3902    -90      0   -214       C  
ATOM   2145  C   GLY A 952     -37.155  23.318 -10.873  1.00 27.16           C  
ANISOU 2145  C   GLY A 952     3268   3109   3941   -110      5   -192       C  
ATOM   2146  O   GLY A 952     -37.802  24.272 -10.472  1.00 24.03           O  
ANISOU 2146  O   GLY A 952     2876   2685   3570   -102    -15   -199       O  
ATOM   2147  N   LYS A 953     -36.193  23.423 -11.777  1.00 28.73           N  
ANISOU 2147  N   LYS A 953     3457   3303   4158   -135     31   -166       N  
ATOM   2148  CA  LYS A 953     -35.942  24.673 -12.514  1.00 31.15           C  
ANISOU 2148  CA  LYS A 953     3760   3567   4508   -158     43   -133       C  
ATOM   2149  C   LYS A 953     -37.044  24.963 -13.538  1.00 32.68           C  
ANISOU 2149  C   LYS A 953     3985   3756   4674   -153     50    -87       C  
ATOM   2150  O   LYS A 953     -37.276  26.115 -13.907  1.00 33.33           O  
ANISOU 2150  O   LYS A 953     4073   3798   4791   -162     48    -61       O  
ATOM   2151  CB  LYS A 953     -34.589  24.609 -13.236  1.00 31.54           C  
ANISOU 2151  CB  LYS A 953     3787   3617   4578   -187     76   -114       C  
ATOM   2152  CG  LYS A 953     -33.436  24.517 -12.273  1.00 35.74           C  
ANISOU 2152  CG  LYS A 953     4284   4146   5150   -193     66   -160       C  
ATOM   2153  CD  LYS A 953     -32.060  24.486 -12.902  1.00 42.14           C  
ANISOU 2153  CD  LYS A 953     5066   4957   5989   -222     98   -147       C  
ATOM   2154  CE  LYS A 953     -31.035  24.221 -11.766  1.00 46.22           C  
ANISOU 2154  CE  LYS A 953     5546   5476   6539   -220     78   -203       C  
ATOM   2155  NZ  LYS A 953     -29.690  24.662 -12.210  1.00 52.31           N  
ANISOU 2155  NZ  LYS A 953     6281   6230   7365   -253    104   -195       N  
ATOM   2156  N   THR A 954     -37.682  23.906 -14.031  1.00 30.15           N  
ANISOU 2156  N   THR A 954     3685   3477   4293   -139     58    -76       N  
ATOM   2157  CA  THR A 954     -38.742  24.023 -15.013  1.00 30.03           C  
ANISOU 2157  CA  THR A 954     3699   3464   4246   -131     61    -37       C  
ATOM   2158  C   THR A 954     -40.005  23.419 -14.421  1.00 31.71           C  
ANISOU 2158  C   THR A 954     3925   3698   4424   -102     36    -60       C  
ATOM   2159  O   THR A 954     -39.956  22.353 -13.768  1.00 31.78           O  
ANISOU 2159  O   THR A 954     3928   3738   4407    -92     32    -90       O  
ATOM   2160  CB  THR A 954     -38.364  23.265 -16.286  1.00 30.75           C  
ANISOU 2160  CB  THR A 954     3801   3587   4296   -140     93     -3       C  
ATOM   2161  OG1 THR A 954     -37.154  23.813 -16.824  1.00 27.57           O  
ANISOU 2161  OG1 THR A 954     3382   3167   3925   -168    121     20       O  
ATOM   2162  CG2 THR A 954     -39.469  23.327 -17.340  1.00 31.65           C  
ANISOU 2162  CG2 THR A 954     3947   3708   4371   -128     92     35       C  
ATOM   2163  N   THR A 955     -41.114  24.110 -14.619  1.00 32.08           N  
ANISOU 2163  N   THR A 955     3989   3727   4473    -90     20    -45       N  
ATOM   2164  CA  THR A 955     -42.384  23.713 -14.089  1.00 35.86           C  
ANISOU 2164  CA  THR A 955     4477   4221   4926    -64     -1    -66       C  
ATOM   2165  C   THR A 955     -43.447  23.890 -15.177  1.00 42.43           C  
ANISOU 2165  C   THR A 955     5334   5055   5734    -55     -4    -29       C  
ATOM   2166  O   THR A 955     -43.300  24.752 -16.020  1.00 41.64           O  
ANISOU 2166  O   THR A 955     5245   4928   5650    -64      2      7       O  
ATOM   2167  CB  THR A 955     -42.768  24.529 -12.847  1.00 35.91           C  
ANISOU 2167  CB  THR A 955     4472   4202   4971    -52    -28   -101       C  
ATOM   2168  OG1 THR A 955     -43.962  23.985 -12.284  1.00 39.24           O  
ANISOU 2168  OG1 THR A 955     4899   4647   5363    -27    -43   -122       O  
ATOM   2169  CG2 THR A 955     -43.026  26.017 -13.157  1.00 37.25           C  
ANISOU 2169  CG2 THR A 955     4647   4322   5185    -54    -39    -81       C  
ATOM   2170  N   PRO A 956     -44.515  23.058 -15.171  1.00 47.15           N  
ANISOU 2170  N   PRO A 956     5941   5682   6293    -35    -14    -38       N  
ATOM   2171  CA  PRO A 956     -45.595  23.300 -16.133  1.00 46.24           C  
ANISOU 2171  CA  PRO A 956     5846   5564   6157    -23    -23     -9       C  
ATOM   2172  C   PRO A 956     -46.248  24.643 -15.874  1.00 41.76           C  
ANISOU 2172  C   PRO A 956     5281   4956   5629    -13    -45     -7       C  
ATOM   2173  O   PRO A 956     -46.409  25.035 -14.723  1.00 45.70           O  
ANISOU 2173  O   PRO A 956     5765   5442   6157     -5    -60    -41       O  
ATOM   2174  CB  PRO A 956     -46.570  22.155 -15.853  1.00 47.74           C  
ANISOU 2174  CB  PRO A 956     6036   5791   6311     -6    -33    -31       C  
ATOM   2175  CG  PRO A 956     -45.724  21.055 -15.302  1.00 49.40           C  
ANISOU 2175  CG  PRO A 956     6234   6029   6507    -15    -18    -54       C  
ATOM   2176  CD  PRO A 956     -44.745  21.809 -14.417  1.00 47.74           C  
ANISOU 2176  CD  PRO A 956     6008   5793   6340    -26    -16    -71       C  
ATOM   2177  N   ASP A 957     -46.549  25.365 -16.940  1.00 41.08           N  
ANISOU 2177  N   ASP A 957     5215   4851   5545    -12    -47     34       N  
ATOM   2178  CA  ASP A 957     -47.106  26.714 -16.842  1.00 39.64           C  
ANISOU 2178  CA  ASP A 957     5036   4622   5402     -2    -69     43       C  
ATOM   2179  C   ASP A 957     -48.399  26.718 -16.049  1.00 39.84           C  
ANISOU 2179  C   ASP A 957     5055   4653   5431     25    -97      8       C  
ATOM   2180  O   ASP A 957     -49.393  26.148 -16.487  1.00 36.95           O  
ANISOU 2180  O   ASP A 957     4697   4312   5031     42   -106     11       O  
ATOM   2181  CB  ASP A 957     -47.372  27.232 -18.240  1.00 41.88           C  
ANISOU 2181  CB  ASP A 957     5348   4893   5673     -1    -68     96       C  
ATOM   2182  CG  ASP A 957     -47.808  28.693 -18.260  1.00 45.43           C  
ANISOU 2182  CG  ASP A 957     5805   5288   6168      7    -90    112       C  
ATOM   2183  OD1 ASP A 957     -48.210  29.227 -17.213  1.00 42.35           O  
ANISOU 2183  OD1 ASP A 957     5399   4876   5815     19   -112     76       O  
ATOM   2184  OD2 ASP A 957     -47.770  29.291 -19.360  1.00 48.33           O  
ANISOU 2184  OD2 ASP A 957     6196   5635   6533      4    -87    163       O  
ATOM   2185  N   PRO A 958     -48.406  27.369 -14.877  1.00 45.75           N  
ANISOU 2185  N   PRO A 958     5785   5378   6219     31   -111    -28       N  
ATOM   2186  CA  PRO A 958     -49.590  27.365 -13.998  1.00 46.25           C  
ANISOU 2186  CA  PRO A 958     5837   5450   6285     58   -133    -66       C  
ATOM   2187  C   PRO A 958     -50.862  27.910 -14.637  1.00 48.55           C  
ANISOU 2187  C   PRO A 958     6142   5729   6578     81   -156    -50       C  
ATOM   2188  O   PRO A 958     -51.952  27.508 -14.254  1.00 54.03           O  
ANISOU 2188  O   PRO A 958     6827   6446   7257    102   -169    -74       O  
ATOM   2189  CB  PRO A 958     -49.171  28.268 -12.837  1.00 46.81           C  
ANISOU 2189  CB  PRO A 958     5892   5489   6405     60   -145   -101       C  
ATOM   2190  CG  PRO A 958     -47.692  28.274 -12.853  1.00 46.72           C  
ANISOU 2190  CG  PRO A 958     5876   5467   6409     32   -125    -93       C  
ATOM   2191  CD  PRO A 958     -47.266  28.080 -14.270  1.00 45.50           C  
ANISOU 2191  CD  PRO A 958     5741   5314   6234     13   -106    -39       C  
ATOM   2192  N   SER A 959     -50.731  28.799 -15.611  1.00 48.78           N  
ANISOU 2192  N   SER A 959     6190   5722   6623     77   -162     -8       N  
ATOM   2193  CA  SER A 959     -51.914  29.389 -16.217  1.00 51.27           C  
ANISOU 2193  CA  SER A 959     6518   6022   6941    102   -188      8       C  
ATOM   2194  C   SER A 959     -52.631  28.391 -17.118  1.00 48.81           C  
ANISOU 2194  C   SER A 959     6218   5752   6576    111   -187     25       C  
ATOM   2195  O   SER A 959     -53.809  28.585 -17.464  1.00 48.46           O  
ANISOU 2195  O   SER A 959     6178   5707   6527    136   -212     25       O  
ATOM   2196  CB  SER A 959     -51.573  30.693 -16.961  1.00 51.38           C  
ANISOU 2196  CB  SER A 959     6552   5981   6990     97   -196     51       C  
ATOM   2197  OG  SER A 959     -50.906  30.449 -18.178  1.00 55.02           O  
ANISOU 2197  OG  SER A 959     7036   6448   7422     78   -175    103       O  
ATOM   2198  N   ALA A 960     -51.922  27.338 -17.533  1.00 45.16           N  
ANISOU 2198  N   ALA A 960     5760   5324   6075     92   -161     36       N  
ATOM   2199  CA  ALA A 960     -52.534  26.304 -18.368  1.00 39.71           C  
ANISOU 2199  CA  ALA A 960     5079   4674   5334    100   -162     46       C  
ATOM   2200  C   ALA A 960     -53.137  25.145 -17.556  1.00 37.17           C  
ANISOU 2200  C   ALA A 960     4735   4392   4995    107   -162      3       C  
ATOM   2201  O   ALA A 960     -53.646  24.207 -18.141  1.00 37.49           O  
ANISOU 2201  O   ALA A 960     4780   4465   5000    112   -163      5       O  
ATOM   2202  CB  ALA A 960     -51.553  25.804 -19.411  1.00 38.98           C  
ANISOU 2202  CB  ALA A 960     5006   4597   5208     80   -137     82       C  
ATOM   2203  N   ASN A 961     -53.096  25.184 -16.227  1.00 35.06           N  
ANISOU 2203  N   ASN A 961     4446   4124   4753    107   -159    -36       N  
ATOM   2204  CA  ASN A 961     -53.816  24.126 -15.476  1.00 35.50           C  
ANISOU 2204  CA  ASN A 961     4481   4216   4790    115   -158    -71       C  
ATOM   2205  C   ASN A 961     -55.298  23.903 -15.853  1.00 37.81           C  
ANISOU 2205  C   ASN A 961     4769   4523   5073    137   -180    -77       C  
ATOM   2206  O   ASN A 961     -56.031  24.843 -16.026  1.00 43.81           O  
ANISOU 2206  O   ASN A 961     5530   5260   5856    156   -203    -74       O  
ATOM   2207  CB  ASN A 961     -53.823  24.417 -14.003  1.00 36.58           C  
ANISOU 2207  CB  ASN A 961     4596   4348   4953    119   -157   -111       C  
ATOM   2208  CG  ASN A 961     -52.507  24.135 -13.314  1.00 39.37           C  
ANISOU 2208  CG  ASN A 961     4946   4704   5309     99   -136   -121       C  
ATOM   2209  OD1 ASN A 961     -52.467  24.283 -12.124  1.00 47.80           O  
ANISOU 2209  OD1 ASN A 961     5997   5772   6391    105   -136   -154       O  
ATOM   2210  ND2 ASN A 961     -51.431  23.800 -14.029  1.00 39.62           N  
ANISOU 2210  ND2 ASN A 961     4990   4737   5326     78   -120    -95       N  
ATOM   2211  N   ILE A 962     -55.735  22.656 -15.916  1.00 37.47           N  
ANISOU 2211  N   ILE A 962     4718   4517   5002    136   -174    -87       N  
ATOM   2212  CA  ILE A 962     -57.115  22.296 -16.218  1.00 40.50           C  
ANISOU 2212  CA  ILE A 962     5091   4917   5380    154   -194    -98       C  
ATOM   2213  C   ILE A 962     -57.636  21.401 -15.115  1.00 42.19           C  
ANISOU 2213  C   ILE A 962     5277   5159   5594    153   -182   -133       C  
ATOM   2214  O   ILE A 962     -56.915  20.539 -14.647  1.00 45.71           O  
ANISOU 2214  O   ILE A 962     5722   5622   6025    135   -160   -138       O  
ATOM   2215  CB  ILE A 962     -57.238  21.443 -17.501  1.00 44.02           C  
ANISOU 2215  CB  ILE A 962     5552   5384   5790    152   -199    -77       C  
ATOM   2216  CG1 ILE A 962     -56.484  22.114 -18.638  1.00 49.82           C  
ANISOU 2216  CG1 ILE A 962     6318   6098   6512    149   -200    -36       C  
ATOM   2217  CG2 ILE A 962     -58.690  21.176 -17.879  1.00 45.18           C  
ANISOU 2217  CG2 ILE A 962     5686   5544   5937    173   -225    -89       C  
ATOM   2218  CD1 ILE A 962     -56.969  23.473 -19.117  1.00 56.17           C  
ANISOU 2218  CD1 ILE A 962     7135   6869   7338    168   -226    -16       C  
ATOM   2219  N   SER A 963     -58.895  21.551 -14.731  1.00 40.67           N  
ANISOU 2219  N   SER A 963     5062   4971   5418    172   -197   -154       N  
ATOM   2220  CA  SER A 963     -59.479  20.664 -13.733  1.00 40.24           C  
ANISOU 2220  CA  SER A 963     4981   4946   5363    170   -182   -183       C  
ATOM   2221  C   SER A 963     -60.085  19.537 -14.477  1.00 38.47           C  
ANISOU 2221  C   SER A 963     4752   4745   5120    166   -187   -179       C  
ATOM   2222  O   SER A 963     -60.798  19.769 -15.459  1.00 37.97           O  
ANISOU 2222  O   SER A 963     4693   4678   5058    179   -212   -170       O  
ATOM   2223  CB  SER A 963     -60.616  21.307 -12.961  1.00 39.09           C  
ANISOU 2223  CB  SER A 963     4809   4799   5245    192   -192   -211       C  
ATOM   2224  OG  SER A 963     -60.113  22.249 -12.068  1.00 43.38           O  
ANISOU 2224  OG  SER A 963     5352   5324   5806    198   -188   -224       O  
ATOM   2225  N   LEU A 964     -59.863  18.338 -13.967  1.00 36.61           N  
ANISOU 2225  N   LEU A 964     4508   4532   4869    149   -165   -188       N  
ATOM   2226  CA  LEU A 964     -60.496  17.125 -14.501  1.00 36.04           C  
ANISOU 2226  CA  LEU A 964     4426   4482   4786    142   -169   -190       C  
ATOM   2227  C   LEU A 964     -61.176  16.423 -13.356  1.00 38.77           C  
ANISOU 2227  C   LEU A 964     4742   4848   5143    138   -151   -213       C  
ATOM   2228  O   LEU A 964     -60.520  15.965 -12.410  1.00 38.01           O  
ANISOU 2228  O   LEU A 964     4645   4759   5038    125   -126   -216       O  
ATOM   2229  CB  LEU A 964     -59.462  16.230 -15.151  1.00 35.06           C  
ANISOU 2229  CB  LEU A 964     4325   4364   4634    124   -160   -173       C  
ATOM   2230  CG  LEU A 964     -59.850  14.909 -15.811  1.00 35.66           C  
ANISOU 2230  CG  LEU A 964     4396   4458   4696    116   -165   -175       C  
ATOM   2231  CD1 LEU A 964     -60.623  15.210 -17.083  1.00 38.10           C  
ANISOU 2231  CD1 LEU A 964     4709   4764   5002    133   -198   -170       C  
ATOM   2232  CD2 LEU A 964     -58.629  14.081 -16.159  1.00 33.96           C  
ANISOU 2232  CD2 LEU A 964     4201   4248   4454     99   -151   -164       C  
ATOM   2233  N   ASP A 965     -62.509  16.448 -13.396  1.00 42.04           N  
ANISOU 2233  N   ASP A 965     5128   5268   5576    150   -164   -228       N  
ATOM   2234  CA  ASP A 965     -63.359  15.885 -12.385  1.00 43.38           C  
ANISOU 2234  CA  ASP A 965     5264   5457   5760    148   -147   -248       C  
ATOM   2235  C   ASP A 965     -62.902  16.285 -10.969  1.00 41.45           C  
ANISOU 2235  C   ASP A 965     5017   5218   5516    148   -120   -258       C  
ATOM   2236  O   ASP A 965     -62.761  15.454 -10.074  1.00 45.22           O  
ANISOU 2236  O   ASP A 965     5486   5712   5984    135    -93   -262       O  
ATOM   2237  CB  ASP A 965     -63.439  14.395 -12.668  1.00 51.02           C  
ANISOU 2237  CB  ASP A 965     6227   6440   6719    127   -139   -244       C  
ATOM   2238  CG  ASP A 965     -64.116  14.072 -14.067  1.00 60.63           C  
ANISOU 2238  CG  ASP A 965     7441   7655   7939    132   -172   -243       C  
ATOM   2239  OD1 ASP A 965     -63.938  12.924 -14.583  1.00 61.68           O  
ANISOU 2239  OD1 ASP A 965     7578   7794   8062    116   -172   -239       O  
ATOM   2240  OD2 ASP A 965     -64.809  14.962 -14.659  1.00 59.87           O  
ANISOU 2240  OD2 ASP A 965     7341   7551   7856    154   -199   -247       O  
ATOM   2241  N   GLY A 966     -62.630  17.583 -10.812  1.00 38.86           N  
ANISOU 2241  N   GLY A 966     4699   4871   5197    165   -130   -262       N  
ATOM   2242  CA  GLY A 966     -62.300  18.197  -9.536  1.00 35.98           C  
ANISOU 2242  CA  GLY A 966     4329   4507   4834    173   -113   -279       C  
ATOM   2243  C   GLY A 966     -60.821  18.252  -9.212  1.00 35.82           C  
ANISOU 2243  C   GLY A 966     4336   4477   4796    161   -102   -269       C  
ATOM   2244  O   GLY A 966     -60.419  18.837  -8.201  1.00 37.58           O  
ANISOU 2244  O   GLY A 966     4559   4699   5021    169    -93   -285       O  
ATOM   2245  N   VAL A 967     -59.992  17.635 -10.035  1.00 32.07           N  
ANISOU 2245  N   VAL A 967     3883   3997   4304    143   -103   -246       N  
ATOM   2246  CA  VAL A 967     -58.539  17.550  -9.728  1.00 29.05           C  
ANISOU 2246  CA  VAL A 967     3522   3609   3906    130    -91   -238       C  
ATOM   2247  C   VAL A 967     -57.764  18.394 -10.708  1.00 27.47           C  
ANISOU 2247  C   VAL A 967     3345   3381   3710    129   -107   -220       C  
ATOM   2248  O   VAL A 967     -57.996  18.343 -11.905  1.00 30.11           O  
ANISOU 2248  O   VAL A 967     3689   3709   4042    129   -122   -202       O  
ATOM   2249  CB  VAL A 967     -58.057  16.088  -9.846  1.00 27.75           C  
ANISOU 2249  CB  VAL A 967     3364   3461   3718    109    -75   -227       C  
ATOM   2250  CG1 VAL A 967     -56.577  15.972  -9.548  1.00 25.67           C  
ANISOU 2250  CG1 VAL A 967     3121   3193   3441     98    -65   -221       C  
ATOM   2251  CG2 VAL A 967     -58.883  15.181  -8.927  1.00 27.99           C  
ANISOU 2251  CG2 VAL A 967     3372   3516   3745    107    -57   -239       C  
ATOM   2252  N   ASP A 968     -56.780  19.101 -10.235  1.00 31.44           N  
ANISOU 2252  N   ASP A 968     3859   3868   4220    128   -104   -223       N  
ATOM   2253  CA  ASP A 968     -55.918  19.826 -11.138  1.00 32.92           C  
ANISOU 2253  CA  ASP A 968     4066   4028   4412    123   -114   -201       C  
ATOM   2254  C   ASP A 968     -54.976  18.939 -11.939  1.00 28.79           C  
ANISOU 2254  C   ASP A 968     3560   3512   3865    102   -103   -179       C  
ATOM   2255  O   ASP A 968     -54.257  18.088 -11.403  1.00 27.14           O  
ANISOU 2255  O   ASP A 968     3352   3319   3642     90    -87   -184       O  
ATOM   2256  CB  ASP A 968     -55.070  20.843 -10.388  1.00 40.89           C  
ANISOU 2256  CB  ASP A 968     5078   5015   5442    125   -113   -213       C  
ATOM   2257  CG  ASP A 968     -55.873  22.093  -9.997  1.00 51.24           C  
ANISOU 2257  CG  ASP A 968     6379   6307   6783    148   -131   -230       C  
ATOM   2258  OD1 ASP A 968     -57.002  22.276 -10.532  1.00 54.30           O  
ANISOU 2258  OD1 ASP A 968     6760   6694   7177    161   -146   -227       O  
ATOM   2259  OD2 ASP A 968     -55.366  22.877  -9.150  1.00 66.63           O  
ANISOU 2259  OD2 ASP A 968     8325   8240   8751    153   -133   -250       O  
ATOM   2260  N   VAL A 969     -54.898  19.281 -13.208  1.00 26.15           N  
ANISOU 2260  N   VAL A 969     3243   3166   3529    101   -114   -154       N  
ATOM   2261  CA  VAL A 969     -53.982  18.677 -14.129  1.00 25.75           C  
ANISOU 2261  CA  VAL A 969     3209   3120   3455     86   -106   -132       C  
ATOM   2262  C   VAL A 969     -53.005  19.729 -14.607  1.00 25.54           C  
ANISOU 2262  C   VAL A 969     3199   3066   3440     80   -104   -111       C  
ATOM   2263  O   VAL A 969     -53.379  20.622 -15.367  1.00 25.22           O  
ANISOU 2263  O   VAL A 969     3168   3005   3408     89   -119    -92       O  
ATOM   2264  CB  VAL A 969     -54.770  18.118 -15.297  1.00 25.68           C  
ANISOU 2264  CB  VAL A 969     3206   3124   3427     91   -118   -119       C  
ATOM   2265  CG1 VAL A 969     -53.885  17.286 -16.165  1.00 26.09           C  
ANISOU 2265  CG1 VAL A 969     3274   3188   3450     77   -107   -103       C  
ATOM   2266  CG2 VAL A 969     -55.953  17.297 -14.768  1.00 26.58           C  
ANISOU 2266  CG2 VAL A 969     3299   3258   3542     98   -123   -141       C  
ATOM   2267  N   PRO A 970     -51.738  19.644 -14.166  1.00 26.44           N  
ANISOU 2267  N   PRO A 970     3313   3176   3556     64    -87   -113       N  
ATOM   2268  CA  PRO A 970     -50.753  20.638 -14.602  1.00 26.62           C  
ANISOU 2268  CA  PRO A 970     3347   3172   3597     55    -83    -92       C  
ATOM   2269  C   PRO A 970     -50.188  20.361 -15.989  1.00 27.61           C  
ANISOU 2269  C   PRO A 970     3491   3302   3698     44    -74    -59       C  
ATOM   2270  O   PRO A 970     -49.002  20.000 -16.140  1.00 28.66           O  
ANISOU 2270  O   PRO A 970     3626   3441   3824     27    -55    -53       O  
ATOM   2271  CB  PRO A 970     -49.671  20.515 -13.543  1.00 26.55           C  
ANISOU 2271  CB  PRO A 970     3327   3162   3599     43    -70   -113       C  
ATOM   2272  CG  PRO A 970     -49.694  19.050 -13.191  1.00 27.37           C  
ANISOU 2272  CG  PRO A 970     3425   3300   3673     41    -60   -128       C  
ATOM   2273  CD  PRO A 970     -51.119  18.600 -13.337  1.00 26.17           C  
ANISOU 2273  CD  PRO A 970     3271   3164   3510     55    -72   -132       C  
ATOM   2274  N   LEU A 971     -51.018  20.520 -17.011  1.00 27.65           N  
ANISOU 2274  N   LEU A 971     3510   3308   3689     56    -88    -39       N  
ATOM   2275  CA  LEU A 971     -50.632  20.088 -18.359  1.00 28.78           C  
ANISOU 2275  CA  LEU A 971     3672   3465   3798     51    -80    -10       C  
ATOM   2276  C   LEU A 971     -50.016  21.202 -19.190  1.00 30.61           C  
ANISOU 2276  C   LEU A 971     3922   3671   4039     45    -74     28       C  
ATOM   2277  O   LEU A 971     -49.814  21.045 -20.396  1.00 30.19           O  
ANISOU 2277  O   LEU A 971     3888   3628   3954     44    -68     57       O  
ATOM   2278  CB  LEU A 971     -51.800  19.422 -19.087  1.00 29.49           C  
ANISOU 2278  CB  LEU A 971     3768   3577   3861     67    -98    -10       C  
ATOM   2279  CG  LEU A 971     -53.155  20.092 -19.059  1.00 29.82           C  
ANISOU 2279  CG  LEU A 971     3806   3605   3918     88   -127    -14       C  
ATOM   2280  CD1 LEU A 971     -53.080  21.452 -19.715  1.00 30.53           C  
ANISOU 2280  CD1 LEU A 971     3915   3664   4022     95   -136     18       C  
ATOM   2281  CD2 LEU A 971     -54.156  19.220 -19.764  1.00 30.13           C  
ANISOU 2281  CD2 LEU A 971     3847   3671   3931    102   -144    -20       C  
ATOM   2282  N   GLY A 972     -49.668  22.310 -18.554  1.00 32.21           N  
ANISOU 2282  N   GLY A 972     4118   3839   4282     40    -75     29       N  
ATOM   2283  CA  GLY A 972     -48.957  23.377 -19.252  1.00 34.46           C  
ANISOU 2283  CA  GLY A 972     4418   4093   4581     29    -66     67       C  
ATOM   2284  C   GLY A 972     -47.598  22.943 -19.772  1.00 36.65           C  
ANISOU 2284  C   GLY A 972     4699   4384   4843      6    -33     85       C  
ATOM   2285  O   GLY A 972     -46.941  22.060 -19.189  1.00 37.76           O  
ANISOU 2285  O   GLY A 972     4823   4545   4978     -4    -19     59       O  
ATOM   2286  N   THR A 973     -47.152  23.564 -20.865  1.00 36.00           N  
ANISOU 2286  N   THR A 973     4636   4288   4753     -1    -21    129       N  
ATOM   2287  CA  THR A 973     -45.781  23.376 -21.316  1.00 37.56           C  
ANISOU 2287  CA  THR A 973     4833   4494   4944    -25     14    148       C  
ATOM   2288  C   THR A 973     -44.808  23.979 -20.300  1.00 35.18           C  
ANISOU 2288  C   THR A 973     4507   4163   4696    -45     24    132       C  
ATOM   2289  O   THR A 973     -45.120  24.909 -19.557  1.00 34.45           O  
ANISOU 2289  O   THR A 973     4407   4034   4648    -42      6    122       O  
ATOM   2290  CB  THR A 973     -45.522  24.035 -22.691  1.00 42.74           C  
ANISOU 2290  CB  THR A 973     5516   5142   5582    -29     29    205       C  
ATOM   2291  OG1 THR A 973     -46.025  25.373 -22.659  1.00 45.34           O  
ANISOU 2291  OG1 THR A 973     5855   5424   5948    -24     10    227       O  
ATOM   2292  CG2 THR A 973     -46.246  23.289 -23.830  1.00 42.69           C  
ANISOU 2292  CG2 THR A 973     5534   5173   5513     -8     22    219       C  
ATOM   2293  N   GLY A 974     -43.622  23.396 -20.248  1.00 37.73           N  
ANISOU 2293  N   GLY A 974     4817   4504   5016    -64     52    125       N  
ATOM   2294  CA  GLY A 974     -42.603  23.788 -19.282  1.00 39.92           C  
ANISOU 2294  CA  GLY A 974     5067   4758   5341    -83     60    104       C  
ATOM   2295  C   GLY A 974     -42.075  25.196 -19.440  1.00 43.72           C  
ANISOU 2295  C   GLY A 974     5548   5192   5873   -101     67    133       C  
ATOM   2296  O   GLY A 974     -41.606  25.562 -20.519  1.00 52.95           O  
ANISOU 2296  O   GLY A 974     6730   6355   7033   -114     91    179       O  
ATOM   2297  N   ILE A 975     -42.117  25.958 -18.350  1.00 41.81           N  
ANISOU 2297  N   ILE A 975     5290   4914   5683   -101     47    106       N  
ATOM   2298  CA  ILE A 975     -41.511  27.263 -18.267  1.00 41.88           C  
ANISOU 2298  CA  ILE A 975     5290   4870   5751   -120     49    124       C  
ATOM   2299  C   ILE A 975     -40.613  27.313 -17.036  1.00 41.33           C  
ANISOU 2299  C   ILE A 975     5187   4790   5727   -132     46     78       C  
ATOM   2300  O   ILE A 975     -40.591  26.394 -16.216  1.00 34.82           O  
ANISOU 2300  O   ILE A 975     4349   3996   4883   -122     39     35       O  
ATOM   2301  CB  ILE A 975     -42.563  28.386 -18.145  1.00 43.91           C  
ANISOU 2301  CB  ILE A 975     5562   5086   6037   -103     18    132       C  
ATOM   2302  CG1 ILE A 975     -43.285  28.301 -16.796  1.00 44.51           C  
ANISOU 2302  CG1 ILE A 975     5622   5162   6126    -81    -14     75       C  
ATOM   2303  CG2 ILE A 975     -43.546  28.304 -19.299  1.00 46.07           C  
ANISOU 2303  CG2 ILE A 975     5868   5373   6264    -86     14    173       C  
ATOM   2304  CD1 ILE A 975     -44.199  29.467 -16.508  1.00 44.72           C  
ANISOU 2304  CD1 ILE A 975     5656   5144   6190    -64    -46     74       C  
ATOM   2305  N   SER A 976     -39.880  28.416 -16.917  1.00 41.54           N  
ANISOU 2305  N   SER A 976     5200   4768   5813   -153     50     88       N  
ATOM   2306  CA  SER A 976     -38.940  28.603 -15.837  1.00 41.25           C  
ANISOU 2306  CA  SER A 976     5131   4717   5827   -166     45     46       C  
ATOM   2307  C   SER A 976     -39.717  28.817 -14.563  1.00 40.74           C  
ANISOU 2307  C   SER A 976     5060   4642   5777   -141      6     -5       C  
ATOM   2308  O   SER A 976     -40.700  29.552 -14.557  1.00 40.54           O  
ANISOU 2308  O   SER A 976     5050   4591   5763   -125    -17      1       O  
ATOM   2309  CB  SER A 976     -38.067  29.830 -16.106  1.00 44.58           C  
ANISOU 2309  CB  SER A 976     5539   5083   6316   -196     56     72       C  
ATOM   2310  OG  SER A 976     -37.087  29.936 -15.105  1.00 42.80           O  
ANISOU 2310  OG  SER A 976     5278   4845   6139   -209     50     27       O  
ATOM   2311  N   SER A 977     -39.296  28.140 -13.497  1.00 38.60           N  
ANISOU 2311  N   SER A 977     4769   4395   5504   -135     -3    -56       N  
ATOM   2312  CA  SER A 977     -39.948  28.268 -12.211  1.00 38.31           C  
ANISOU 2312  CA  SER A 977     4725   4355   5475   -109    -36   -106       C  
ATOM   2313  C   SER A 977     -39.390  29.451 -11.450  1.00 39.51           C  
ANISOU 2313  C   SER A 977     4856   4457   5699   -117    -56   -133       C  
ATOM   2314  O   SER A 977     -39.992  29.888 -10.479  1.00 37.86           O  
ANISOU 2314  O   SER A 977     4644   4236   5506    -95    -86   -172       O  
ATOM   2315  CB  SER A 977     -39.724  27.016 -11.367  1.00 36.57           C  
ANISOU 2315  CB  SER A 977     4494   4183   5217    -97    -38   -147       C  
ATOM   2316  OG  SER A 977     -38.330  26.817 -11.173  1.00 33.92           O  
ANISOU 2316  OG  SER A 977     4135   3849   4906   -118    -25   -160       O  
ATOM   2317  N   GLY A 978     -38.236  29.958 -11.882  1.00 41.40           N  
ANISOU 2317  N   GLY A 978     5079   4668   5983   -149    -39   -114       N  
ATOM   2318  CA  GLY A 978     -37.579  31.048 -11.181  1.00 44.86           C  
ANISOU 2318  CA  GLY A 978     5492   5054   6497   -160    -58   -142       C  
ATOM   2319  C   GLY A 978     -36.749  30.575 -10.010  1.00 45.37           C  
ANISOU 2319  C   GLY A 978     5528   5137   6573   -156    -71   -202       C  
ATOM   2320  O   GLY A 978     -36.203  31.378  -9.284  1.00 51.19           O  
ANISOU 2320  O   GLY A 978     6242   5837   7370   -162    -93   -236       O  
ATOM   2321  N   VAL A 979     -36.646  29.267  -9.829  1.00 46.51           N  
ANISOU 2321  N   VAL A 979     5674   5338   6660   -146    -61   -214       N  
ATOM   2322  CA  VAL A 979     -35.823  28.704  -8.786  1.00 44.70           C  
ANISOU 2322  CA  VAL A 979     5421   5130   6434   -141    -73   -266       C  
ATOM   2323  C   VAL A 979     -34.510  28.321  -9.448  1.00 47.31           C  
ANISOU 2323  C   VAL A 979     5730   5467   6779   -172    -42   -247       C  
ATOM   2324  O   VAL A 979     -34.507  27.406 -10.263  1.00 49.46           O  
ANISOU 2324  O   VAL A 979     6014   5775   7002   -176    -14   -215       O  
ATOM   2325  CB  VAL A 979     -36.502  27.461  -8.172  1.00 44.94           C  
ANISOU 2325  CB  VAL A 979     5466   5215   6393   -110    -80   -289       C  
ATOM   2326  CG1 VAL A 979     -35.568  26.723  -7.219  1.00 45.64           C  
ANISOU 2326  CG1 VAL A 979     5533   5330   6477   -105    -90   -334       C  
ATOM   2327  CG2 VAL A 979     -37.794  27.844  -7.444  1.00 42.39           C  
ANISOU 2327  CG2 VAL A 979     5160   4890   6058    -79   -107   -311       C  
ATOM   2328  N   ASN A 980     -33.404  28.980  -9.093  1.00 49.74           N  
ANISOU 2328  N   ASN A 980     6004   5741   7153   -192    -49   -269       N  
ATOM   2329  CA  ASN A 980     -32.068  28.653  -9.675  1.00 49.66           C  
ANISOU 2329  CA  ASN A 980     5967   5738   7164   -223    -18   -255       C  
ATOM   2330  C   ASN A 980     -31.227  27.736  -8.797  1.00 47.99           C  
ANISOU 2330  C   ASN A 980     5730   5560   6942   -213    -30   -305       C  
ATOM   2331  O   ASN A 980     -30.524  26.867  -9.330  1.00 47.53           O  
ANISOU 2331  O   ASN A 980     5663   5535   6863   -223     -3   -292       O  
ATOM   2332  CB  ASN A 980     -31.211  29.881 -10.092  1.00 53.49           C  
ANISOU 2332  CB  ASN A 980     6425   6165   7735   -260     -8   -237       C  
ATOM   2333  CG  ASN A 980     -29.865  29.467 -10.797  1.00 60.90           C  
ANISOU 2333  CG  ASN A 980     7332   7117   8690   -293     32   -218       C  
ATOM   2334  OD1 ASN A 980     -29.832  28.533 -11.632  1.00 65.87           O  
ANISOU 2334  OD1 ASN A 980     7975   7790   9265   -295     66   -186       O  
ATOM   2335  ND2 ASN A 980     -28.758  30.135 -10.434  1.00 53.82           N  
ANISOU 2335  ND2 ASN A 980     6393   6185   7873   -318     26   -242       N  
ATOM   2336  N   ASP A 981     -31.334  27.894  -7.479  1.00 43.88           N  
ANISOU 2336  N   ASP A 981     5202   5036   6433   -188    -72   -362       N  
ATOM   2337  CA  ASP A 981     -30.518  27.129  -6.531  1.00 40.46           C  
ANISOU 2337  CA  ASP A 981     4747   4631   5993   -175    -91   -414       C  
ATOM   2338  C   ASP A 981     -31.146  25.781  -6.129  1.00 36.01           C  
ANISOU 2338  C   ASP A 981     4210   4124   5347   -143    -94   -422       C  
ATOM   2339  O   ASP A 981     -31.481  25.550  -4.965  1.00 32.82           O  
ANISOU 2339  O   ASP A 981     3812   3736   4922   -112   -127   -466       O  
ATOM   2340  CB  ASP A 981     -30.257  27.988  -5.287  1.00 41.28           C  
ANISOU 2340  CB  ASP A 981     4831   4705   6150   -163   -136   -473       C  
ATOM   2341  CG  ASP A 981     -31.563  28.386  -4.541  1.00 44.30           C  
ANISOU 2341  CG  ASP A 981     5242   5083   6508   -130   -165   -492       C  
ATOM   2342  OD1 ASP A 981     -32.624  28.571  -5.178  1.00 41.20           O  
ANISOU 2342  OD1 ASP A 981     4878   4687   6090   -128   -151   -453       O  
ATOM   2343  OD2 ASP A 981     -31.527  28.487  -3.295  1.00 47.75           O  
ANISOU 2343  OD2 ASP A 981     5671   5524   6947   -103   -204   -550       O  
ATOM   2344  N   THR A 982     -31.249  24.869  -7.086  1.00 35.38           N  
ANISOU 2344  N   THR A 982     4144   4076   5221   -149    -61   -382       N  
ATOM   2345  CA  THR A 982     -31.860  23.565  -6.849  1.00 33.71           C  
ANISOU 2345  CA  THR A 982     3958   3913   4937   -123    -61   -384       C  
ATOM   2346  C   THR A 982     -31.081  22.439  -7.475  1.00 33.04           C  
ANISOU 2346  C   THR A 982     3865   3861   4827   -132    -35   -371       C  
ATOM   2347  O   THR A 982     -30.425  22.608  -8.504  1.00 35.46           O  
ANISOU 2347  O   THR A 982     4157   4160   5156   -159     -4   -342       O  
ATOM   2348  CB  THR A 982     -33.311  23.516  -7.372  1.00 35.41           C  
ANISOU 2348  CB  THR A 982     4211   4136   5108   -113    -52   -348       C  
ATOM   2349  OG1 THR A 982     -33.819  22.182  -7.283  1.00 36.98           O  
ANISOU 2349  OG1 THR A 982     4430   4379   5241    -93    -48   -346       O  
ATOM   2350  CG2 THR A 982     -33.373  23.950  -8.826  1.00 36.78           C  
ANISOU 2350  CG2 THR A 982     4391   4293   5292   -140    -18   -293       C  
ATOM   2351  N   SER A 983     -31.191  21.264  -6.864  1.00 31.64           N  
ANISOU 2351  N   SER A 983     3697   3721   4602   -107    -47   -392       N  
ATOM   2352  CA  SER A 983     -30.594  20.067  -7.391  1.00 32.63           C  
ANISOU 2352  CA  SER A 983     3819   3879   4699   -109    -27   -383       C  
ATOM   2353  C   SER A 983     -31.378  19.461  -8.569  1.00 30.73           C  
ANISOU 2353  C   SER A 983     3607   3658   4411   -113      3   -336       C  
ATOM   2354  O   SER A 983     -30.909  18.509  -9.157  1.00 32.05           O  
ANISOU 2354  O   SER A 983     3772   3851   4555   -115     22   -327       O  
ATOM   2355  CB  SER A 983     -30.494  19.001  -6.273  1.00 33.04           C  
ANISOU 2355  CB  SER A 983     3876   3961   4716    -79    -54   -420       C  
ATOM   2356  OG  SER A 983     -29.852  19.521  -5.129  1.00 34.72           O  
ANISOU 2356  OG  SER A 983     4067   4160   4965    -69    -87   -467       O  
ATOM   2357  N   LEU A 984     -32.558  19.987  -8.896  1.00 27.94           N  
ANISOU 2357  N   LEU A 984     3279   3294   4044   -112      5   -310       N  
ATOM   2358  CA  LEU A 984     -33.471  19.287  -9.774  1.00 27.23           C  
ANISOU 2358  CA  LEU A 984     3218   3226   3902   -107     23   -275       C  
ATOM   2359  C   LEU A 984     -33.787  20.091 -11.016  1.00 26.65           C  
ANISOU 2359  C   LEU A 984     3153   3134   3839   -127     48   -230       C  
ATOM   2360  O   LEU A 984     -34.107  21.282 -10.937  1.00 27.84           O  
ANISOU 2360  O   LEU A 984     3305   3251   4024   -134     40   -223       O  
ATOM   2361  CB  LEU A 984     -34.786  18.984  -9.021  1.00 27.76           C  
ANISOU 2361  CB  LEU A 984     3311   3303   3933    -81      1   -285       C  
ATOM   2362  CG  LEU A 984     -34.793  17.975  -7.870  1.00 27.27           C  
ANISOU 2362  CG  LEU A 984     3252   3267   3843    -57    -19   -318       C  
ATOM   2363  CD1 LEU A 984     -36.117  18.008  -7.143  1.00 28.38           C  
ANISOU 2363  CD1 LEU A 984     3414   3411   3957    -36    -36   -323       C  
ATOM   2364  CD2 LEU A 984     -34.524  16.573  -8.355  1.00 28.62           C  
ANISOU 2364  CD2 LEU A 984     3429   3469   3977    -54     -6   -310       C  
ATOM   2365  N   LEU A 985     -33.773  19.433 -12.154  1.00 25.40           N  
ANISOU 2365  N   LEU A 985     3005   2997   3647   -133     75   -200       N  
ATOM   2366  CA  LEU A 985     -34.258  20.056 -13.389  1.00 28.17           C  
ANISOU 2366  CA  LEU A 985     3373   3337   3993   -147     97   -153       C  
ATOM   2367  C   LEU A 985     -35.788  20.218 -13.371  1.00 26.10           C  
ANISOU 2367  C   LEU A 985     3141   3072   3703   -129     80   -141       C  
ATOM   2368  O   LEU A 985     -36.319  21.222 -13.837  1.00 27.12           O  
ANISOU 2368  O   LEU A 985     3281   3175   3847   -135     81   -114       O  
ATOM   2369  CB  LEU A 985     -33.830  19.227 -14.625  1.00 29.44           C  
ANISOU 2369  CB  LEU A 985     3538   3529   4119   -154    130   -128       C  
ATOM   2370  CG  LEU A 985     -32.309  19.130 -14.919  1.00 32.40           C  
ANISOU 2370  CG  LEU A 985     3879   3909   4521   -173    155   -133       C  
ATOM   2371  CD1 LEU A 985     -32.006  18.210 -16.111  1.00 30.92           C  
ANISOU 2371  CD1 LEU A 985     3699   3759   4291   -174    187   -113       C  
ATOM   2372  CD2 LEU A 985     -31.710  20.516 -15.172  1.00 33.83           C  
ANISOU 2372  CD2 LEU A 985     4043   4053   4760   -201    170   -113       C  
ATOM   2373  N   TYR A 986     -36.489  19.226 -12.841  1.00 24.65           N  
ANISOU 2373  N   TYR A 986     2970   2914   3481   -108     65   -160       N  
ATOM   2374  CA  TYR A 986     -37.940  19.213 -12.854  1.00 23.46           C  
ANISOU 2374  CA  TYR A 986     2844   2767   3303    -91     51   -150       C  
ATOM   2375  C   TYR A 986     -38.485  18.905 -11.466  1.00 22.29           C  
ANISOU 2375  C   TYR A 986     2695   2624   3150    -71     25   -187       C  
ATOM   2376  O   TYR A 986     -37.808  18.263 -10.643  1.00 23.07           O  
ANISOU 2376  O   TYR A 986     2782   2736   3249    -66     18   -216       O  
ATOM   2377  CB  TYR A 986     -38.434  18.196 -13.912  1.00 23.53           C  
ANISOU 2377  CB  TYR A 986     2872   2806   3262    -86     65   -128       C  
ATOM   2378  CG  TYR A 986     -37.705  18.353 -15.231  1.00 26.02           C  
ANISOU 2378  CG  TYR A 986     3187   3124   3575   -104     94    -95       C  
ATOM   2379  CD1 TYR A 986     -37.950  19.439 -16.062  1.00 27.35           C  
ANISOU 2379  CD1 TYR A 986     3366   3271   3756   -114    104    -59       C  
ATOM   2380  CD2 TYR A 986     -36.695  17.461 -15.608  1.00 29.41           C  
ANISOU 2380  CD2 TYR A 986     3605   3578   3991   -110    114   -102       C  
ATOM   2381  CE1 TYR A 986     -37.239  19.600 -17.254  1.00 28.51           C  
ANISOU 2381  CE1 TYR A 986     3514   3422   3898   -131    135    -26       C  
ATOM   2382  CE2 TYR A 986     -35.977  17.607 -16.790  1.00 28.49           C  
ANISOU 2382  CE2 TYR A 986     3486   3469   3870   -125    145    -73       C  
ATOM   2383  CZ  TYR A 986     -36.248  18.692 -17.603  1.00 29.88           C  
ANISOU 2383  CZ  TYR A 986     3673   3624   4055   -136    157    -34       C  
ATOM   2384  OH  TYR A 986     -35.529  18.840 -18.781  1.00 31.23           O  
ANISOU 2384  OH  TYR A 986     3843   3804   4218   -151    192     -2       O  
ATOM   2385  N   ASN A 987     -39.731  19.303 -11.225  1.00 20.19           N  
ANISOU 2385  N   ASN A 987     2442   2351   2877    -57     10   -184       N  
ATOM   2386  CA  ASN A 987     -40.398  18.989  -9.988  1.00 20.12           C  
ANISOU 2386  CA  ASN A 987     2435   2352   2857    -37     -9   -214       C  
ATOM   2387  C   ASN A 987     -40.514  17.487  -9.750  1.00 20.08           C  
ANISOU 2387  C   ASN A 987     2436   2382   2811    -28     -7   -222       C  
ATOM   2388  O   ASN A 987     -40.475  16.678 -10.681  1.00 19.19           O  
ANISOU 2388  O   ASN A 987     2331   2285   2674    -33      7   -203       O  
ATOM   2389  CB  ASN A 987     -41.810  19.552  -9.950  1.00 20.91           C  
ANISOU 2389  CB  ASN A 987     2548   2444   2953    -24    -21   -208       C  
ATOM   2390  CG  ASN A 987     -41.847  21.054 -10.088  1.00 21.40           C  
ANISOU 2390  CG  ASN A 987     2606   2467   3057    -29    -28   -201       C  
ATOM   2391  OD1 ASN A 987     -40.997  21.736  -9.582  1.00 22.91           O  
ANISOU 2391  OD1 ASN A 987     2782   2637   3285    -36    -34   -219       O  
ATOM   2392  ND2 ASN A 987     -42.820  21.557 -10.800  1.00 22.07           N  
ANISOU 2392  ND2 ASN A 987     2704   2541   3140    -25    -30   -177       N  
ATOM   2393  N   GLU A 988     -40.636  17.131  -8.483  1.00 19.63           N  
ANISOU 2393  N   GLU A 988     2376   2336   2748    -12    -21   -251       N  
ATOM   2394  CA  GLU A 988     -41.167  15.838  -8.114  1.00 20.19           C  
ANISOU 2394  CA  GLU A 988     2457   2434   2781     -1    -21   -254       C  
ATOM   2395  C   GLU A 988     -41.943  15.981  -6.817  1.00 19.02           C  
ANISOU 2395  C   GLU A 988     2311   2292   2625     19    -35   -276       C  
ATOM   2396  O   GLU A 988     -41.809  16.968  -6.116  1.00 18.30           O  
ANISOU 2396  O   GLU A 988     2212   2185   2557     25    -48   -296       O  
ATOM   2397  CB  GLU A 988     -40.104  14.743  -8.010  1.00 20.39           C  
ANISOU 2397  CB  GLU A 988     2478   2476   2794     -3    -17   -263       C  
ATOM   2398  CG  GLU A 988     -38.880  15.091  -7.202  1.00 20.65           C  
ANISOU 2398  CG  GLU A 988     2493   2500   2851     -2    -27   -290       C  
ATOM   2399  CD  GLU A 988     -37.776  14.073  -7.411  1.00 20.31           C  
ANISOU 2399  CD  GLU A 988     2443   2471   2801     -5    -22   -295       C  
ATOM   2400  OE1 GLU A 988     -37.541  13.232  -6.522  1.00 19.57           O  
ANISOU 2400  OE1 GLU A 988     2352   2392   2691      9    -33   -313       O  
ATOM   2401  OE2 GLU A 988     -37.154  14.078  -8.495  1.00 21.17           O  
ANISOU 2401  OE2 GLU A 988     2545   2578   2920    -21     -5   -280       O  
ATOM   2402  N   TYR A 989     -42.804  15.002  -6.573  1.00 18.53           N  
ANISOU 2402  N   TYR A 989     2259   2251   2532     28    -33   -271       N  
ATOM   2403  CA  TYR A 989     -43.744  15.065  -5.500  1.00 18.11           C  
ANISOU 2403  CA  TYR A 989     2208   2207   2466     45    -39   -285       C  
ATOM   2404  C   TYR A 989     -43.714  13.742  -4.790  1.00 17.34           C  
ANISOU 2404  C   TYR A 989     2118   2133   2337     53    -37   -289       C  
ATOM   2405  O   TYR A 989     -43.777  12.697  -5.419  1.00 18.51           O  
ANISOU 2405  O   TYR A 989     2272   2291   2471     45    -28   -272       O  
ATOM   2406  CB  TYR A 989     -45.147  15.334  -6.048  1.00 17.57           C  
ANISOU 2406  CB  TYR A 989     2144   2137   2394     46    -35   -269       C  
ATOM   2407  CG  TYR A 989     -45.272  16.591  -6.845  1.00 17.12           C  
ANISOU 2407  CG  TYR A 989     2084   2055   2365     40    -39   -260       C  
ATOM   2408  CD1 TYR A 989     -45.040  16.584  -8.188  1.00 17.25           C  
ANISOU 2408  CD1 TYR A 989     2106   2064   2386     25    -32   -234       C  
ATOM   2409  CD2 TYR A 989     -45.700  17.767  -6.262  1.00 18.00           C  
ANISOU 2409  CD2 TYR A 989     2189   2151   2498     51    -51   -276       C  
ATOM   2410  CE1 TYR A 989     -45.202  17.705  -8.945  1.00 17.98           C  
ANISOU 2410  CE1 TYR A 989     2199   2132   2502     20    -34   -220       C  
ATOM   2411  CE2 TYR A 989     -45.849  18.910  -7.000  1.00 18.80           C  
ANISOU 2411  CE2 TYR A 989     2290   2225   2629     46    -56   -265       C  
ATOM   2412  CZ  TYR A 989     -45.589  18.873  -8.350  1.00 18.31           C  
ANISOU 2412  CZ  TYR A 989     2235   2154   2569     30    -47   -234       C  
ATOM   2413  OH  TYR A 989     -45.724  19.968  -9.122  1.00 18.01           O  
ANISOU 2413  OH  TYR A 989     2199   2088   2557     25    -51   -218       O  
ATOM   2414  N   ILE A 990     -43.650  13.785  -3.483  1.00 17.44           N  
ANISOU 2414  N   ILE A 990     2131   2156   2341     69    -45   -311       N  
ATOM   2415  CA  ILE A 990     -43.546  12.584  -2.680  1.00 17.18           C  
ANISOU 2415  CA  ILE A 990     2107   2144   2277     79    -44   -312       C  
ATOM   2416  C   ILE A 990     -44.578  12.596  -1.560  1.00 18.13           C  
ANISOU 2416  C   ILE A 990     2232   2282   2375     97    -41   -319       C  
ATOM   2417  O   ILE A 990     -44.741  13.593  -0.848  1.00 16.76           O  
ANISOU 2417  O   ILE A 990     2053   2107   2208    111    -50   -341       O  
ATOM   2418  CB  ILE A 990     -42.134  12.417  -2.095  1.00 18.02           C  
ANISOU 2418  CB  ILE A 990     2210   2250   2386     85    -57   -332       C  
ATOM   2419  CG1 ILE A 990     -41.071  12.467  -3.183  1.00 17.72           C  
ANISOU 2419  CG1 ILE A 990     2163   2198   2373     67    -56   -327       C  
ATOM   2420  CG2 ILE A 990     -42.001  11.084  -1.373  1.00 18.33           C  
ANISOU 2420  CG2 ILE A 990     2262   2309   2393     96    -58   -328       C  
ATOM   2421  CD1 ILE A 990     -40.580  13.856  -3.510  1.00 17.95           C  
ANISOU 2421  CD1 ILE A 990     2177   2204   2439     59    -62   -339       C  
ATOM   2422  N   VAL A 991     -45.311  11.485  -1.437  1.00 18.87           N  
ANISOU 2422  N   VAL A 991     2335   2392   2444     96    -29   -300       N  
ATOM   2423  CA  VAL A 991     -46.142  11.245  -0.269  1.00 20.41           C  
ANISOU 2423  CA  VAL A 991     2535   2608   2613    113    -21   -303       C  
ATOM   2424  C   VAL A 991     -45.627  10.046   0.541  1.00 20.96           C  
ANISOU 2424  C   VAL A 991     2619   2693   2653    121    -21   -296       C  
ATOM   2425  O   VAL A 991     -44.993   9.156  -0.007  1.00 20.53           O  
ANISOU 2425  O   VAL A 991     2570   2632   2601    110    -23   -284       O  
ATOM   2426  CB  VAL A 991     -47.627  11.083  -0.629  1.00 20.46           C  
ANISOU 2426  CB  VAL A 991     2536   2620   2617    106     -5   -285       C  
ATOM   2427  CG1 VAL A 991     -48.161  12.370  -1.238  1.00 21.08           C  
ANISOU 2427  CG1 VAL A 991     2603   2685   2723    105     -9   -294       C  
ATOM   2428  CG2 VAL A 991     -47.861   9.899  -1.553  1.00 20.29           C  
ANISOU 2428  CG2 VAL A 991     2518   2594   2595     88      4   -258       C  
ATOM   2429  N   TYR A 992     -45.935  10.041   1.838  1.00 21.86           N  
ANISOU 2429  N   TYR A 992     2740   2827   2739    141    -19   -305       N  
ATOM   2430  CA  TYR A 992     -45.379   9.085   2.798  1.00 22.24           C  
ANISOU 2430  CA  TYR A 992     2805   2890   2755    155    -22   -301       C  
ATOM   2431  C   TYR A 992     -46.424   8.185   3.420  1.00 22.51           C  
ANISOU 2431  C   TYR A 992     2850   2944   2760    157      1   -275       C  
ATOM   2432  O   TYR A 992     -46.144   7.481   4.339  1.00 22.61           O  
ANISOU 2432  O   TYR A 992     2879   2971   2742    171      1   -268       O  
ATOM   2433  CB  TYR A 992     -44.583   9.845   3.889  1.00 21.55           C  
ANISOU 2433  CB  TYR A 992     2720   2812   2655    181    -42   -336       C  
ATOM   2434  CG  TYR A 992     -43.473  10.627   3.219  1.00 19.59           C  
ANISOU 2434  CG  TYR A 992     2458   2541   2445    173    -63   -358       C  
ATOM   2435  CD1 TYR A 992     -43.716  11.900   2.732  1.00 19.10           C  
ANISOU 2435  CD1 TYR A 992     2380   2464   2414    167    -67   -374       C  
ATOM   2436  CD2 TYR A 992     -42.228  10.047   2.958  1.00 18.06           C  
ANISOU 2436  CD2 TYR A 992     2265   2337   2258    170    -78   -360       C  
ATOM   2437  CE1 TYR A 992     -42.732  12.618   2.055  1.00 18.30           C  
ANISOU 2437  CE1 TYR A 992     2266   2339   2351    157    -82   -390       C  
ATOM   2438  CE2 TYR A 992     -41.237  10.753   2.298  1.00 17.43           C  
ANISOU 2438  CE2 TYR A 992     2170   2238   2216    160    -92   -379       C  
ATOM   2439  CZ  TYR A 992     -41.501  12.033   1.836  1.00 18.31           C  
ANISOU 2439  CZ  TYR A 992     2266   2334   2358    152    -93   -391       C  
ATOM   2440  OH  TYR A 992     -40.525  12.753   1.167  1.00 19.09           O  
ANISOU 2440  OH  TYR A 992     2348   2410   2497    139   -104   -405       O  
ATOM   2441  N   ASP A 993     -47.620   8.190   2.853  1.00 23.82           N  
ANISOU 2441  N   ASP A 993     3005   3108   2936    143     20   -260       N  
ATOM   2442  CA  ASP A 993     -48.710   7.350   3.291  1.00 23.87           C  
ANISOU 2442  CA  ASP A 993     3015   3131   2924    139     45   -233       C  
ATOM   2443  C   ASP A 993     -49.388   6.854   2.027  1.00 22.16           C  
ANISOU 2443  C   ASP A 993     2787   2897   2736    113     53   -213       C  
ATOM   2444  O   ASP A 993     -49.845   7.647   1.231  1.00 21.28           O  
ANISOU 2444  O   ASP A 993     2661   2777   2650    105     51   -222       O  
ATOM   2445  CB  ASP A 993     -49.680   8.191   4.149  1.00 25.47           C  
ANISOU 2445  CB  ASP A 993     3210   3357   3112    156     60   -247       C  
ATOM   2446  CG  ASP A 993     -50.879   7.381   4.703  1.00 27.80           C  
ANISOU 2446  CG  ASP A 993     3504   3672   3387    152     92   -218       C  
ATOM   2447  OD1 ASP A 993     -51.234   6.293   4.184  1.00 26.84           O  
ANISOU 2447  OD1 ASP A 993     3383   3540   3275    130    103   -188       O  
ATOM   2448  OD2 ASP A 993     -51.472   7.869   5.681  1.00 32.04           O  
ANISOU 2448  OD2 ASP A 993     4039   4236   3900    170    107   -229       O  
ATOM   2449  N   ILE A 994     -49.462   5.547   1.861  1.00 22.25           N  
ANISOU 2449  N   ILE A 994     2808   2903   2745    100     61   -186       N  
ATOM   2450  CA  ILE A 994     -50.011   4.946   0.635  1.00 22.49           C  
ANISOU 2450  CA  ILE A 994     2827   2915   2802     76     64   -170       C  
ATOM   2451  C   ILE A 994     -51.465   5.330   0.372  1.00 22.37           C  
ANISOU 2451  C   ILE A 994     2792   2907   2802     67     81   -167       C  
ATOM   2452  O   ILE A 994     -51.952   5.219  -0.757  1.00 23.50           O  
ANISOU 2452  O   ILE A 994     2923   3036   2971     51     77   -163       O  
ATOM   2453  CB  ILE A 994     -49.878   3.393   0.649  1.00 22.95           C  
ANISOU 2453  CB  ILE A 994     2899   2964   2857     65     68   -144       C  
ATOM   2454  CG1 ILE A 994     -50.680   2.787   1.793  1.00 24.20           C  
ANISOU 2454  CG1 ILE A 994     3062   3138   2993     68     93   -121       C  
ATOM   2455  CG2 ILE A 994     -48.412   2.990   0.778  1.00 21.98           C  
ANISOU 2455  CG2 ILE A 994     2793   2832   2725     75     48   -150       C  
ATOM   2456  CD1 ILE A 994     -50.592   1.272   1.887  1.00 25.67           C  
ANISOU 2456  CD1 ILE A 994     3263   3311   3180     57     97    -90       C  
ATOM   2457  N   ALA A 995     -52.164   5.756   1.411  1.00 22.05           N  
ANISOU 2457  N   ALA A 995     2747   2888   2743     80     98   -170       N  
ATOM   2458  CA  ALA A 995     -53.558   6.130   1.290  1.00 22.10           C  
ANISOU 2458  CA  ALA A 995     2730   2903   2763     75    116   -169       C  
ATOM   2459  C   ALA A 995     -53.776   7.485   0.638  1.00 22.00           C  
ANISOU 2459  C   ALA A 995     2702   2885   2771     81    102   -194       C  
ATOM   2460  O   ALA A 995     -54.907   7.825   0.322  1.00 21.35           O  
ANISOU 2460  O   ALA A 995     2599   2806   2706     78    110   -196       O  
ATOM   2461  CB  ALA A 995     -54.226   6.089   2.672  1.00 22.81           C  
ANISOU 2461  CB  ALA A 995     2820   3024   2824     88    143   -163       C  
ATOM   2462  N   GLN A 996     -52.716   8.279   0.498  1.00 21.93           N  
ANISOU 2462  N   GLN A 996     2703   2868   2763     92     80   -214       N  
ATOM   2463  CA  GLN A 996     -52.813   9.587  -0.149  1.00 21.97           C  
ANISOU 2463  CA  GLN A 996     2697   2861   2791     96     66   -235       C  
ATOM   2464  C   GLN A 996     -52.816   9.520  -1.701  1.00 22.27           C  
ANISOU 2464  C   GLN A 996     2730   2876   2856     78     53   -226       C  
ATOM   2465  O   GLN A 996     -52.838  10.552  -2.362  1.00 21.09           O  
ANISOU 2465  O   GLN A 996     2574   2714   2725     81     40   -237       O  
ATOM   2466  CB  GLN A 996     -51.649  10.472   0.280  1.00 23.16           C  
ANISOU 2466  CB  GLN A 996     2856   3007   2935    112     48   -258       C  
ATOM   2467  CG  GLN A 996     -51.889  11.196   1.582  1.00 24.20           C  
ANISOU 2467  CG  GLN A 996     2986   3159   3048    136     53   -281       C  
ATOM   2468  CD  GLN A 996     -50.676  11.921   2.092  1.00 22.79           C  
ANISOU 2468  CD  GLN A 996     2817   2975   2865    152     32   -307       C  
ATOM   2469  OE1 GLN A 996     -49.892  11.361   2.821  1.00 22.65           O  
ANISOU 2469  OE1 GLN A 996     2815   2968   2824    160     30   -307       O  
ATOM   2470  NE2 GLN A 996     -50.486  13.154   1.635  1.00 22.64           N  
ANISOU 2470  NE2 GLN A 996     2790   2939   2875    155     16   -327       N  
ATOM   2471  N   VAL A 997     -52.901   8.324  -2.272  1.00 22.78           N  
ANISOU 2471  N   VAL A 997     2798   2936   2923     61     56   -206       N  
ATOM   2472  CA  VAL A 997     -52.919   8.142  -3.726  1.00 22.66           C  
ANISOU 2472  CA  VAL A 997     2780   2903   2927     47     44   -199       C  
ATOM   2473  C   VAL A 997     -54.186   7.417  -4.177  1.00 22.83           C  
ANISOU 2473  C   VAL A 997     2786   2925   2961     35     52   -187       C  
ATOM   2474  O   VAL A 997     -54.534   6.376  -3.617  1.00 22.40           O  
ANISOU 2474  O   VAL A 997     2731   2878   2901     27     66   -173       O  
ATOM   2475  CB  VAL A 997     -51.754   7.258  -4.162  1.00 22.81           C  
ANISOU 2475  CB  VAL A 997     2815   2911   2940     38     36   -191       C  
ATOM   2476  CG1 VAL A 997     -51.787   7.066  -5.652  1.00 23.22           C  
ANISOU 2476  CG1 VAL A 997     2865   2950   3007     27     24   -187       C  
ATOM   2477  CG2 VAL A 997     -50.446   7.896  -3.744  1.00 24.26           C  
ANISOU 2477  CG2 VAL A 997     3010   3093   3116     49     27   -205       C  
ATOM   2478  N   ASN A 998     -54.863   7.962  -5.199  1.00 22.46           N  
ANISOU 2478  N   ASN A 998     2728   2872   2934     32     41   -191       N  
ATOM   2479  CA  ASN A 998     -55.997   7.285  -5.832  1.00 22.49           C  
ANISOU 2479  CA  ASN A 998     2716   2875   2956     21     42   -184       C  
ATOM   2480  C   ASN A 998     -55.673   7.186  -7.321  1.00 21.96           C  
ANISOU 2480  C   ASN A 998     2655   2792   2896     14     20   -183       C  
ATOM   2481  O   ASN A 998     -55.666   8.187  -8.039  1.00 23.34           O  
ANISOU 2481  O   ASN A 998     2830   2961   3076     22      6   -189       O  
ATOM   2482  CB  ASN A 998     -57.292   8.027  -5.523  1.00 23.81           C  
ANISOU 2482  CB  ASN A 998     2859   3052   3136     29     48   -193       C  
ATOM   2483  CG  ASN A 998     -58.566   7.275  -5.944  1.00 26.87           C  
ANISOU 2483  CG  ASN A 998     3223   3441   3545     16     52   -187       C  
ATOM   2484  OD1 ASN A 998     -58.569   6.067  -6.118  1.00 32.89           O  
ANISOU 2484  OD1 ASN A 998     3987   4199   4313      0     55   -175       O  
ATOM   2485  ND2 ASN A 998     -59.659   7.981  -6.041  1.00 27.13           N  
ANISOU 2485  ND2 ASN A 998     3232   3480   3595     24     50   -198       N  
ATOM   2486  N   LEU A 999     -55.357   5.968  -7.767  1.00 20.85           N  
ANISOU 2486  N   LEU A 999     2522   2646   2756      2     17   -175       N  
ATOM   2487  CA  LEU A 999     -54.993   5.733  -9.135  1.00 21.96           C  
ANISOU 2487  CA  LEU A 999     2670   2776   2899     -2     -1   -176       C  
ATOM   2488  C   LEU A 999     -56.196   5.956 -10.035  1.00 22.21           C  
ANISOU 2488  C   LEU A 999     2685   2807   2947     -2    -15   -181       C  
ATOM   2489  O   LEU A 999     -57.280   5.502  -9.717  1.00 23.21           O  
ANISOU 2489  O   LEU A 999     2792   2937   3091     -8     -9   -181       O  
ATOM   2490  CB  LEU A 999     -54.433   4.331  -9.305  1.00 21.59           C  
ANISOU 2490  CB  LEU A 999     2633   2723   2849    -13     -2   -171       C  
ATOM   2491  CG  LEU A 999     -53.128   4.082  -8.559  1.00 21.33           C  
ANISOU 2491  CG  LEU A 999     2618   2689   2799    -10      5   -168       C  
ATOM   2492  CD1 LEU A 999     -52.649   2.675  -8.858  1.00 21.35           C  
ANISOU 2492  CD1 LEU A 999     2628   2681   2803    -19      0   -164       C  
ATOM   2493  CD2 LEU A 999     -52.041   5.080  -8.922  1.00 21.30           C  
ANISOU 2493  CD2 LEU A 999     2625   2685   2784     -1     -1   -174       C  
ATOM   2494  N   LYS A1000     -56.012   6.726 -11.112  1.00 23.88           N  
ANISOU 2494  N   LYS A1000     2904   3015   3156      6    -32   -184       N  
ATOM   2495  CA  LYS A1000     -57.132   7.086 -12.018  1.00 25.61           C  
ANISOU 2495  CA  LYS A1000     3109   3233   3388     11    -50   -189       C  
ATOM   2496  C   LYS A1000     -57.005   6.517 -13.422  1.00 22.66           C  
ANISOU 2496  C   LYS A1000     2745   2857   3009     10    -71   -191       C  
ATOM   2497  O   LYS A1000     -57.971   6.004 -13.966  1.00 21.04           O  
ANISOU 2497  O   LYS A1000     2524   2651   2817      8    -85   -198       O  
ATOM   2498  CB  LYS A1000     -57.271   8.603 -12.183  1.00 27.24           C  
ANISOU 2498  CB  LYS A1000     3317   3439   3595     26    -57   -190       C  
ATOM   2499  CG  LYS A1000     -57.390   9.398 -10.910  1.00 31.73           C  
ANISOU 2499  CG  LYS A1000     3877   4010   4168     33    -41   -194       C  
ATOM   2500  CD  LYS A1000     -58.363   8.835  -9.889  1.00 35.13           C  
ANISOU 2500  CD  LYS A1000     4284   4452   4611     28    -25   -199       C  
ATOM   2501  CE  LYS A1000     -59.797   9.124 -10.243  1.00 40.54           C  
ANISOU 2501  CE  LYS A1000     4943   5141   5319     34    -35   -207       C  
ATOM   2502  NZ  LYS A1000     -60.664   8.817  -9.047  1.00 46.05           N  
ANISOU 2502  NZ  LYS A1000     5616   5852   6028     31    -12   -211       N  
ATOM   2503  N   TYR A1001     -55.829   6.669 -14.027  1.00 21.02           N  
ANISOU 2503  N   TYR A1001     2559   2647   2779     12    -73   -186       N  
ATOM   2504  CA  TYR A1001     -55.611   6.179 -15.398  1.00 20.61           C  
ANISOU 2504  CA  TYR A1001     2518   2596   2715     14    -91   -189       C  
ATOM   2505  C   TYR A1001     -54.346   5.341 -15.529  1.00 20.15           C  
ANISOU 2505  C   TYR A1001     2476   2537   2641      8    -83   -190       C  
ATOM   2506  O   TYR A1001     -53.386   5.513 -14.768  1.00 18.40           O  
ANISOU 2506  O   TYR A1001     2262   2315   2415      5    -67   -184       O  
ATOM   2507  CB  TYR A1001     -55.571   7.323 -16.409  1.00 19.90           C  
ANISOU 2507  CB  TYR A1001     2441   2508   2612     28   -104   -183       C  
ATOM   2508  CG  TYR A1001     -56.803   8.207 -16.397  1.00 21.14           C  
ANISOU 2508  CG  TYR A1001     2584   2664   2786     38   -116   -184       C  
ATOM   2509  CD1 TYR A1001     -57.956   7.857 -17.077  1.00 20.98           C  
ANISOU 2509  CD1 TYR A1001     2549   2646   2775     43   -139   -195       C  
ATOM   2510  CD2 TYR A1001     -56.818   9.374 -15.659  1.00 20.79           C  
ANISOU 2510  CD2 TYR A1001     2536   2613   2749     43   -107   -178       C  
ATOM   2511  CE1 TYR A1001     -59.084   8.687 -17.078  1.00 21.59           C  
ANISOU 2511  CE1 TYR A1001     2611   2722   2870     55   -153   -198       C  
ATOM   2512  CE2 TYR A1001     -57.921  10.208 -15.672  1.00 23.15           C  
ANISOU 2512  CE2 TYR A1001     2821   2910   3064     55   -120   -182       C  
ATOM   2513  CZ  TYR A1001     -59.053   9.864 -16.381  1.00 22.19           C  
ANISOU 2513  CZ  TYR A1001     2685   2793   2952     61   -143   -191       C  
ATOM   2514  OH  TYR A1001     -60.147  10.696 -16.316  1.00 23.40           O  
ANISOU 2514  OH  TYR A1001     2821   2944   3124     75   -156   -197       O  
ATOM   2515  N   LEU A1002     -54.366   4.461 -16.523  1.00 20.13           N  
ANISOU 2515  N   LEU A1002     2478   2537   2633      9    -99   -199       N  
ATOM   2516  CA  LEU A1002     -53.229   3.695 -16.904  1.00 20.83           C  
ANISOU 2516  CA  LEU A1002     2581   2627   2706      7    -96   -203       C  
ATOM   2517  C   LEU A1002     -53.067   3.876 -18.394  1.00 21.75           C  
ANISOU 2517  C   LEU A1002     2710   2753   2799     19   -111   -207       C  
ATOM   2518  O   LEU A1002     -53.988   3.652 -19.142  1.00 22.67           O  
ANISOU 2518  O   LEU A1002     2822   2872   2918     25   -132   -217       O  
ATOM   2519  CB  LEU A1002     -53.456   2.241 -16.548  1.00 21.57           C  
ANISOU 2519  CB  LEU A1002     2666   2711   2817     -2    -99   -214       C  
ATOM   2520  CG  LEU A1002     -52.365   1.239 -16.918  1.00 24.42           C  
ANISOU 2520  CG  LEU A1002     3040   3071   3168     -2   -100   -223       C  
ATOM   2521  CD1 LEU A1002     -51.097   1.549 -16.181  1.00 26.42           C  
ANISOU 2521  CD1 LEU A1002     3303   3326   3411     -3    -80   -214       C  
ATOM   2522  CD2 LEU A1002     -52.787  -0.152 -16.525  1.00 25.07           C  
ANISOU 2522  CD2 LEU A1002     3114   3139   3275    -12   -107   -232       C  
ATOM   2523  N   LEU A1003     -51.907   4.330 -18.829  1.00 22.86           N  
ANISOU 2523  N   LEU A1003     2867   2901   2916     23   -100   -200       N  
ATOM   2524  CA  LEU A1003     -51.656   4.533 -20.246  1.00 23.41           C  
ANISOU 2524  CA  LEU A1003     2952   2984   2957     35   -109   -200       C  
ATOM   2525  C   LEU A1003     -50.676   3.494 -20.741  1.00 24.06           C  
ANISOU 2525  C   LEU A1003     3042   3074   3024     37   -106   -214       C  
ATOM   2526  O   LEU A1003     -49.650   3.208 -20.104  1.00 25.92           O  
ANISOU 2526  O   LEU A1003     3278   3307   3264     30    -89   -214       O  
ATOM   2527  CB  LEU A1003     -51.048   5.914 -20.491  1.00 23.94           C  
ANISOU 2527  CB  LEU A1003     3031   3055   3009     39    -95   -178       C  
ATOM   2528  CG  LEU A1003     -51.985   7.108 -20.528  1.00 23.73           C  
ANISOU 2528  CG  LEU A1003     3003   3023   2990     45   -104   -164       C  
ATOM   2529  CD1 LEU A1003     -52.641   7.320 -19.176  1.00 24.07           C  
ANISOU 2529  CD1 LEU A1003     3027   3052   3065     37   -101   -166       C  
ATOM   2530  CD2 LEU A1003     -51.192   8.341 -20.942  1.00 23.83           C  
ANISOU 2530  CD2 LEU A1003     3032   3036   2988     47    -90   -140       C  
ATOM   2531  N   LYS A1004     -50.980   2.949 -21.900  1.00 25.15           N  
ANISOU 2531  N   LYS A1004     3187   3224   3146     48   -125   -229       N  
ATOM   2532  CA  LYS A1004     -50.046   2.163 -22.671  1.00 24.89           C  
ANISOU 2532  CA  LYS A1004     3165   3204   3090     56   -124   -244       C  
ATOM   2533  C   LYS A1004     -49.364   3.098 -23.650  1.00 23.59           C  
ANISOU 2533  C   LYS A1004     3017   3060   2887     66   -111   -228       C  
ATOM   2534  O   LYS A1004     -50.031   3.692 -24.489  1.00 23.49           O  
ANISOU 2534  O   LYS A1004     3014   3056   2855     78   -124   -221       O  
ATOM   2535  CB  LYS A1004     -50.797   1.067 -23.392  1.00 27.38           C  
ANISOU 2535  CB  LYS A1004     3476   3520   3405     65   -153   -272       C  
ATOM   2536  CG  LYS A1004     -49.922   0.070 -24.131  1.00 32.14           C  
ANISOU 2536  CG  LYS A1004     4088   4135   3989     75   -156   -296       C  
ATOM   2537  CD  LYS A1004     -50.793  -1.106 -24.563  1.00 37.19           C  
ANISOU 2537  CD  LYS A1004     4720   4766   4643     80   -189   -328       C  
ATOM   2538  CE  LYS A1004     -50.266  -1.799 -25.799  1.00 39.69           C  
ANISOU 2538  CE  LYS A1004     5049   5104   4928    100   -201   -356       C  
ATOM   2539  NZ  LYS A1004     -51.142  -2.944 -26.160  1.00 43.05           N  
ANISOU 2539  NZ  LYS A1004     5465   5517   5374    105   -238   -390       N  
ATOM   2540  N   LEU A1005     -48.049   3.250 -23.509  1.00 24.60           N  
ANISOU 2540  N   LEU A1005     3148   3193   3006     62    -84   -222       N  
ATOM   2541  CA  LEU A1005     -47.241   4.167 -24.325  1.00 27.78           C  
ANISOU 2541  CA  LEU A1005     3565   3613   3377     68    -64   -202       C  
ATOM   2542  C   LEU A1005     -46.195   3.461 -25.187  1.00 28.09           C  
ANISOU 2542  C   LEU A1005     3611   3676   3387     77    -53   -217       C  
ATOM   2543  O   LEU A1005     -45.566   2.510 -24.752  1.00 26.23           O  
ANISOU 2543  O   LEU A1005     3365   3436   3164     75    -50   -238       O  
ATOM   2544  CB  LEU A1005     -46.471   5.114 -23.431  1.00 31.57           C  
ANISOU 2544  CB  LEU A1005     4039   4082   3875     53    -38   -180       C  
ATOM   2545  CG  LEU A1005     -47.215   6.060 -22.491  1.00 33.72           C  
ANISOU 2545  CG  LEU A1005     4305   4333   4176     44    -42   -163       C  
ATOM   2546  CD1 LEU A1005     -46.197   6.883 -21.724  1.00 37.32           C  
ANISOU 2546  CD1 LEU A1005     4754   4779   4647     31    -17   -149       C  
ATOM   2547  CD2 LEU A1005     -48.109   6.974 -23.278  1.00 33.24           C  
ANISOU 2547  CD2 LEU A1005     4256   4275   4100     53    -54   -145       C  
ATOM   2548  N   LYS A1006     -46.063   3.899 -26.429  1.00 28.51           N  
ANISOU 2548  N   LYS A1006     3681   3753   3399     91    -48   -207       N  
ATOM   2549  CA  LYS A1006     -45.021   3.431 -27.313  1.00 29.01           C  
ANISOU 2549  CA  LYS A1006     3750   3843   3429    102    -31   -219       C  
ATOM   2550  C   LYS A1006     -43.951   4.478 -27.199  1.00 27.48           C  
ANISOU 2550  C   LYS A1006     3556   3653   3233     90      7   -188       C  
ATOM   2551  O   LYS A1006     -44.239   5.659 -27.363  1.00 24.95           O  
ANISOU 2551  O   LYS A1006     3245   3328   2907     86     14   -155       O  
ATOM   2552  CB  LYS A1006     -45.521   3.348 -28.765  1.00 33.26           C  
ANISOU 2552  CB  LYS A1006     4310   4410   3919    125    -46   -224       C  
ATOM   2553  CG  LYS A1006     -44.464   3.274 -29.871  1.00 37.00           C  
ANISOU 2553  CG  LYS A1006     4794   4919   4344    139    -20   -224       C  
ATOM   2554  CD  LYS A1006     -43.990   1.853 -30.117  1.00 40.69           C  
ANISOU 2554  CD  LYS A1006     5254   5399   4806    152    -28   -270       C  
ATOM   2555  CE  LYS A1006     -43.059   1.768 -31.330  1.00 43.97           C  
ANISOU 2555  CE  LYS A1006     5682   5857   5168    170     -3   -275       C  
ATOM   2556  NZ  LYS A1006     -43.777   2.116 -32.588  1.00 47.64           N  
ANISOU 2556  NZ  LYS A1006     6172   6348   5580    193    -18   -267       N  
ATOM   2557  N   PHE A1007     -42.742   4.028 -26.905  1.00 26.51           N  
ANISOU 2557  N   PHE A1007     3420   3535   3117     85     30   -201       N  
ATOM   2558  CA  PHE A1007     -41.570   4.853 -26.895  1.00 28.86           C  
ANISOU 2558  CA  PHE A1007     3712   3840   3415     73     67   -178       C  
ATOM   2559  C   PHE A1007     -40.910   4.719 -28.274  1.00 30.19           C  
ANISOU 2559  C   PHE A1007     3891   4046   3533     88     89   -178       C  
ATOM   2560  O   PHE A1007     -40.478   3.639 -28.637  1.00 32.59           O  
ANISOU 2560  O   PHE A1007     4191   4368   3824    102     86   -211       O  
ATOM   2561  CB  PHE A1007     -40.574   4.361 -25.841  1.00 27.24           C  
ANISOU 2561  CB  PHE A1007     3483   3622   3245     62     78   -196       C  
ATOM   2562  CG  PHE A1007     -40.986   4.606 -24.424  1.00 25.56           C  
ANISOU 2562  CG  PHE A1007     3260   3375   3076     47     65   -193       C  
ATOM   2563  CD1 PHE A1007     -42.112   3.986 -23.894  1.00 25.67           C  
ANISOU 2563  CD1 PHE A1007     3276   3373   3104     50     34   -207       C  
ATOM   2564  CD2 PHE A1007     -40.240   5.443 -23.597  1.00 25.77           C  
ANISOU 2564  CD2 PHE A1007     3272   3388   3131     31     84   -179       C  
ATOM   2565  CE1 PHE A1007     -42.485   4.219 -22.568  1.00 25.66           C  
ANISOU 2565  CE1 PHE A1007     3265   3346   3139     38     25   -203       C  
ATOM   2566  CE2 PHE A1007     -40.628   5.706 -22.276  1.00 23.83           C  
ANISOU 2566  CE2 PHE A1007     3018   3114   2920     20     71   -178       C  
ATOM   2567  CZ  PHE A1007     -41.751   5.086 -21.767  1.00 24.06           C  
ANISOU 2567  CZ  PHE A1007     3051   3131   2958     25     43   -189       C  
ATOM   2568  N   ASN A1008     -40.830   5.807 -29.029  1.00 30.73           N  
ANISOU 2568  N   ASN A1008     3974   4126   3575     87    110   -141       N  
ATOM   2569  CA  ASN A1008     -40.133   5.807 -30.331  1.00 32.68           C  
ANISOU 2569  CA  ASN A1008     4232   4413   3770    100    137   -134       C  
ATOM   2570  C   ASN A1008     -38.748   6.389 -30.184  1.00 32.91           C  
ANISOU 2570  C   ASN A1008     4244   4447   3812     82    184   -116       C  
ATOM   2571  O   ASN A1008     -38.581   7.615 -30.138  1.00 32.71           O  
ANISOU 2571  O   ASN A1008     4222   4410   3797     66    205    -74       O  
ATOM   2572  CB  ASN A1008     -40.929   6.623 -31.338  1.00 33.30           C  
ANISOU 2572  CB  ASN A1008     4341   4504   3807    112    132   -101       C  
ATOM   2573  CG  ASN A1008     -42.252   5.980 -31.657  1.00 38.18           C  
ANISOU 2573  CG  ASN A1008     4974   5123   4409    133     84   -124       C  
ATOM   2574  OD1 ASN A1008     -42.325   4.763 -31.932  1.00 45.80           O  
ANISOU 2574  OD1 ASN A1008     5936   6103   5361    150     66   -167       O  
ATOM   2575  ND2 ASN A1008     -43.315   6.758 -31.608  1.00 41.57           N  
ANISOU 2575  ND2 ASN A1008     5417   5535   4844    133     62   -100       N  
ATOM   2576  N   PHE A1009     -37.768   5.505 -30.028  1.00 34.30           N  
ANISOU 2576  N   PHE A1009     4400   4637   3996     85    197   -149       N  
ATOM   2577  CA  PHE A1009     -36.392   5.915 -29.768  1.00 38.34           C  
ANISOU 2577  CA  PHE A1009     4887   5152   4529     68    239   -140       C  
ATOM   2578  C   PHE A1009     -35.709   6.559 -30.981  1.00 40.77           C  
ANISOU 2578  C   PHE A1009     5203   5495   4793     69    284   -109       C  
ATOM   2579  O   PHE A1009     -35.978   6.201 -32.112  1.00 41.70           O  
ANISOU 2579  O   PHE A1009     5341   5647   4855     92    285   -112       O  
ATOM   2580  CB  PHE A1009     -35.582   4.729 -29.275  1.00 37.61           C  
ANISOU 2580  CB  PHE A1009     4769   5064   4456     74    237   -187       C  
ATOM   2581  CG  PHE A1009     -35.964   4.287 -27.916  1.00 38.17           C  
ANISOU 2581  CG  PHE A1009     4829   5098   4576     66    203   -207       C  
ATOM   2582  CD1 PHE A1009     -36.919   3.296 -27.739  1.00 38.86           C  
ANISOU 2582  CD1 PHE A1009     4927   5176   4661     81    162   -234       C  
ATOM   2583  CD2 PHE A1009     -35.399   4.899 -26.792  1.00 38.17           C  
ANISOU 2583  CD2 PHE A1009     4807   5071   4623     44    212   -197       C  
ATOM   2584  CE1 PHE A1009     -37.310   2.909 -26.468  1.00 37.47           C  
ANISOU 2584  CE1 PHE A1009     4743   4967   4528     74    135   -247       C  
ATOM   2585  CE2 PHE A1009     -35.776   4.504 -25.522  1.00 39.55           C  
ANISOU 2585  CE2 PHE A1009     4975   5215   4837     40    181   -214       C  
ATOM   2586  CZ  PHE A1009     -36.737   3.509 -25.362  1.00 39.26           C  
ANISOU 2586  CZ  PHE A1009     4951   5170   4795     54    145   -236       C  
ATOM   2587  N   LYS A1010     -34.860   7.552 -30.717  1.00 49.07           N  
ANISOU 2587  N   LYS A1010     6237   6536   5871     44    321    -78       N  
ATOM   2588  CA  LYS A1010     -34.039   8.217 -31.731  1.00 55.57           C  
ANISOU 2588  CA  LYS A1010     7062   7390   6664     39    373    -44       C  
ATOM   2589  C   LYS A1010     -32.594   7.695 -31.729  1.00 59.37           C  
ANISOU 2589  C   LYS A1010     7507   7894   7156     35    409    -69       C  
ATOM   2590  O   LYS A1010     -32.297   6.570 -31.268  1.00 61.97           O  
ANISOU 2590  O   LYS A1010     7819   8227   7500     47    391   -119       O  
ATOM   2591  CB  LYS A1010     -34.047   9.726 -31.462  1.00 57.22           C  
ANISOU 2591  CB  LYS A1010     7272   7566   6901     10    390     10       C  
ATOM   2592  CG  LYS A1010     -35.418  10.346 -31.676  1.00 58.89           C  
ANISOU 2592  CG  LYS A1010     7520   7761   7096     18    359     40       C  
ATOM   2593  CD  LYS A1010     -35.559  11.656 -30.922  1.00 61.82           C  
ANISOU 2593  CD  LYS A1010     7887   8085   7518    -10    359     77       C  
ATOM   2594  CE  LYS A1010     -37.025  12.038 -30.742  1.00 63.30           C  
ANISOU 2594  CE  LYS A1010     8101   8247   7702      0    315     88       C  
ATOM   2595  NZ  LYS A1010     -37.176  13.368 -30.087  1.00 60.07           N  
ANISOU 2595  NZ  LYS A1010     7689   7792   7341    -23    315    124       N  
TER    2596      LYS A1010                                                      
ATOM   2597  N   LYS B 662     -59.894 -23.541  11.761  1.00 81.72           N  
ANISOU 2597  N   LYS B 662    10650   8942  11457    906  -1213     32       N  
ATOM   2598  CA  LYS B 662     -59.621 -22.449  12.731  1.00 81.84           C  
ANISOU 2598  CA  LYS B 662    10593   9051  11452    886  -1270     58       C  
ATOM   2599  C   LYS B 662     -59.730 -21.133  11.973  1.00 82.75           C  
ANISOU 2599  C   LYS B 662    10624   9263  11554    839  -1181      3       C  
ATOM   2600  O   LYS B 662     -58.809 -20.762  11.255  1.00 83.65           O  
ANISOU 2600  O   LYS B 662    10637   9394  11754    890  -1135    -51       O  
ATOM   2601  CB  LYS B 662     -58.221 -22.604  13.352  1.00 78.66           C  
ANISOU 2601  CB  LYS B 662    10105   8631  11152    987  -1355     68       C  
ATOM   2602  N   SER B 663     -60.870 -20.454  12.108  1.00 80.97           N  
ANISOU 2602  N   SER B 663    10442   9098  11225    742  -1154     19       N  
ATOM   2603  CA  SER B 663     -61.052 -19.122  11.528  1.00 74.79           C  
ANISOU 2603  CA  SER B 663     9587   8408  10423    693  -1079    -23       C  
ATOM   2604  C   SER B 663     -60.290 -18.088  12.336  1.00 68.11           C  
ANISOU 2604  C   SER B 663     8646   7630   9604    705  -1132    -19       C  
ATOM   2605  O   SER B 663     -60.250 -18.169  13.556  1.00 64.02           O  
ANISOU 2605  O   SER B 663     8153   7116   9057    704  -1224     29       O  
ATOM   2606  CB  SER B 663     -62.541 -18.745  11.502  1.00 74.74           C  
ANISOU 2606  CB  SER B 663     9656   8443  10300    591  -1041     -2       C  
ATOM   2607  N   LYS B 664     -59.707 -17.101  11.659  1.00 67.34           N  
ANISOU 2607  N   LYS B 664     8444   7587   9555    710  -1073    -70       N  
ATOM   2608  CA  LYS B 664     -59.151 -15.928  12.343  1.00 70.32           C  
ANISOU 2608  CA  LYS B 664     8735   8037   9946    699  -1111    -73       C  
ATOM   2609  C   LYS B 664     -60.214 -14.869  12.738  1.00 65.61           C  
ANISOU 2609  C   LYS B 664     8171   7510   9247    607  -1094    -59       C  
ATOM   2610  O   LYS B 664     -59.904 -13.920  13.461  1.00 64.36           O  
ANISOU 2610  O   LYS B 664     7964   7407   9083    588  -1133    -58       O  
ATOM   2611  CB  LYS B 664     -58.084 -15.261  11.464  1.00 73.76           C  
ANISOU 2611  CB  LYS B 664     9045   8503  10479    735  -1052   -131       C  
ATOM   2612  N   LEU B 665     -61.450 -15.021  12.265  1.00 58.58           N  
ANISOU 2612  N   LEU B 665     7362   6618   8279    550  -1036    -50       N  
ATOM   2613  CA  LEU B 665     -62.475 -14.000  12.491  1.00 54.59           C  
ANISOU 2613  CA  LEU B 665     6878   6177   7686    470  -1006    -42       C  
ATOM   2614  C   LEU B 665     -62.923 -13.965  13.940  1.00 54.57           C  
ANISOU 2614  C   LEU B 665     6931   6193   7612    441  -1089      8       C  
ATOM   2615  O   LEU B 665     -63.027 -15.007  14.574  1.00 54.20           O  
ANISOU 2615  O   LEU B 665     6952   6097   7544    457  -1151     49       O  
ATOM   2616  CB  LEU B 665     -63.710 -14.263  11.629  1.00 51.04           C  
ANISOU 2616  CB  LEU B 665     6498   5723   7174    419   -930    -40       C  
ATOM   2617  CG  LEU B 665     -63.535 -14.229  10.114  1.00 47.99           C  
ANISOU 2617  CG  LEU B 665     6075   5328   6831    430   -837    -88       C  
ATOM   2618  CD1 LEU B 665     -64.764 -14.802   9.441  1.00 46.23           C  
ANISOU 2618  CD1 LEU B 665     5938   5088   6539    380   -788    -78       C  
ATOM   2619  CD2 LEU B 665     -63.265 -12.822   9.631  1.00 48.03           C  
ANISOU 2619  CD2 LEU B 665     5994   5400   6856    410   -782   -122       C  
ATOM   2620  N   PRO B 666     -63.256 -12.769  14.450  1.00 51.16           N  
ANISOU 2620  N   PRO B 666     6477   5827   7133    394  -1085      3       N  
ATOM   2621  CA  PRO B 666     -63.851 -12.675  15.785  1.00 49.06           C  
ANISOU 2621  CA  PRO B 666     6274   5585   6781    356  -1149     46       C  
ATOM   2622  C   PRO B 666     -65.112 -13.526  15.908  1.00 49.64           C  
ANISOU 2622  C   PRO B 666     6456   5636   6770    314  -1137     90       C  
ATOM   2623  O   PRO B 666     -65.850 -13.695  14.922  1.00 47.81           O  
ANISOU 2623  O   PRO B 666     6244   5397   6525    289  -1062     80       O  
ATOM   2624  CB  PRO B 666     -64.205 -11.184  15.918  1.00 50.92           C  
ANISOU 2624  CB  PRO B 666     6471   5893   6983    308  -1110     20       C  
ATOM   2625  CG  PRO B 666     -63.352 -10.474  14.903  1.00 51.42           C  
ANISOU 2625  CG  PRO B 666     6434   5967   7137    333  -1058    -32       C  
ATOM   2626  CD  PRO B 666     -63.142 -11.455  13.787  1.00 50.10           C  
ANISOU 2626  CD  PRO B 666     6267   5747   7023    371  -1017    -41       C  
ATOM   2627  N   LYS B 667     -65.379 -14.023  17.115  1.00 47.73           N  
ANISOU 2627  N   LYS B 667     6283   5387   6466    301  -1211    139       N  
ATOM   2628  CA  LYS B 667     -66.548 -14.877  17.358  1.00 49.22           C  
ANISOU 2628  CA  LYS B 667     6575   5553   6572    256  -1206    188       C  
ATOM   2629  C   LYS B 667     -67.861 -14.204  16.882  1.00 42.60           C  
ANISOU 2629  C   LYS B 667     5752   4768   5668    186  -1119    179       C  
ATOM   2630  O   LYS B 667     -68.609 -14.811  16.116  1.00 39.00           O  
ANISOU 2630  O   LYS B 667     5335   4288   5197    161  -1070    187       O  
ATOM   2631  CB  LYS B 667     -66.639 -15.324  18.837  1.00 49.89           C  
ANISOU 2631  CB  LYS B 667     6731   5636   6590    243  -1297    245       C  
ATOM   2632  N   PRO B 668     -68.112 -12.946  17.293  1.00 38.99           N  
ANISOU 2632  N   PRO B 668     5258   4380   5175    157  -1099    161       N  
ATOM   2633  CA  PRO B 668     -69.326 -12.232  16.826  1.00 37.95           C  
ANISOU 2633  CA  PRO B 668     5130   4300   4989    100  -1017    153       C  
ATOM   2634  C   PRO B 668     -69.522 -12.276  15.311  1.00 37.21           C  
ANISOU 2634  C   PRO B 668     5005   4193   4941    102   -940    125       C  
ATOM   2635  O   PRO B 668     -70.642 -12.427  14.846  1.00 37.73           O  
ANISOU 2635  O   PRO B 668     5105   4273   4959     56   -889    139       O  
ATOM   2636  CB  PRO B 668     -69.095 -10.792  17.292  1.00 37.27           C  
ANISOU 2636  CB  PRO B 668     4988   4274   4899     94  -1010    121       C  
ATOM   2637  CG  PRO B 668     -68.161 -10.931  18.453  1.00 37.33           C  
ANISOU 2637  CG  PRO B 668     5000   4272   4911    122  -1104    131       C  
ATOM   2638  CD  PRO B 668     -67.243 -12.058  18.075  1.00 37.74           C  
ANISOU 2638  CD  PRO B 668     5049   4256   5036    177  -1149    140       C  
ATOM   2639  N   VAL B 669     -68.437 -12.157  14.556  1.00 37.43           N  
ANISOU 2639  N   VAL B 669     4967   4196   5057    153   -932     85       N  
ATOM   2640  CA  VAL B 669     -68.509 -12.158  13.099  1.00 37.81           C  
ANISOU 2640  CA  VAL B 669     4986   4234   5147    156   -858     55       C  
ATOM   2641  C   VAL B 669     -68.829 -13.566  12.600  1.00 38.83           C  
ANISOU 2641  C   VAL B 669     5182   4301   5271    156   -858     74       C  
ATOM   2642  O   VAL B 669     -69.699 -13.761  11.752  1.00 39.95           O  
ANISOU 2642  O   VAL B 669     5351   4447   5383    118   -802     73       O  
ATOM   2643  CB  VAL B 669     -67.201 -11.651  12.475  1.00 35.15           C  
ANISOU 2643  CB  VAL B 669     4560   3890   4905    209   -845      7       C  
ATOM   2644  CG1 VAL B 669     -67.270 -11.698  10.965  1.00 35.56           C  
ANISOU 2644  CG1 VAL B 669     4590   3934   4989    210   -766    -24       C  
ATOM   2645  CG2 VAL B 669     -66.901 -10.238  12.932  1.00 35.75           C  
ANISOU 2645  CG2 VAL B 669     4573   4022   4987    200   -845    -13       C  
ATOM   2646  N   GLN B 670     -68.154 -14.540  13.167  1.00 41.24           N  
ANISOU 2646  N   GLN B 670     5518   4548   5604    197   -925     92       N  
ATOM   2647  CA  GLN B 670     -68.447 -15.937  12.866  1.00 43.71           C  
ANISOU 2647  CA  GLN B 670     5906   4790   5911    198   -934    114       C  
ATOM   2648  C   GLN B 670     -69.919 -16.252  13.112  1.00 40.29           C  
ANISOU 2648  C   GLN B 670     5552   4374   5382    120   -920    156       C  
ATOM   2649  O   GLN B 670     -70.551 -16.880  12.280  1.00 38.91           O  
ANISOU 2649  O   GLN B 670     5418   4172   5194     91   -880    154       O  
ATOM   2650  CB  GLN B 670     -67.558 -16.875  13.700  1.00 47.08           C  
ANISOU 2650  CB  GLN B 670     6361   5152   6376    254  -1022    139       C  
ATOM   2651  CG  GLN B 670     -66.096 -16.902  13.259  1.00 49.80           C  
ANISOU 2651  CG  GLN B 670     6629   5464   6829    338  -1034     98       C  
ATOM   2652  CD  GLN B 670     -65.266 -17.853  14.115  1.00 52.48           C  
ANISOU 2652  CD  GLN B 670     6994   5739   7208    398  -1128    130       C  
ATOM   2653  OE1 GLN B 670     -65.751 -18.893  14.540  1.00 53.25           O  
ANISOU 2653  OE1 GLN B 670     7184   5782   7268    385  -1165    176       O  
ATOM   2654  NE2 GLN B 670     -64.032 -17.478  14.396  1.00 52.63           N  
ANISOU 2654  NE2 GLN B 670     6932   5765   7301    460  -1169    111       N  
ATOM   2655  N   ASP B 671     -70.454 -15.814  14.249  1.00 39.33           N  
ANISOU 2655  N   ASP B 671     5451   4299   5194     84   -950    191       N  
ATOM   2656  CA  ASP B 671     -71.864 -16.021  14.587  1.00 40.60           C  
ANISOU 2656  CA  ASP B 671     5675   4488   5263      8   -932    233       C  
ATOM   2657  C   ASP B 671     -72.797 -15.347  13.586  1.00 40.12           C  
ANISOU 2657  C   ASP B 671     5584   4480   5181    -37   -848    211       C  
ATOM   2658  O   ASP B 671     -73.825 -15.914  13.234  1.00 41.73           O  
ANISOU 2658  O   ASP B 671     5835   4681   5339    -91   -823    234       O  
ATOM   2659  CB  ASP B 671     -72.169 -15.550  16.029  1.00 45.09           C  
ANISOU 2659  CB  ASP B 671     6263   5105   5764    -16   -973    268       C  
ATOM   2660  CG  ASP B 671     -71.592 -16.504  17.105  1.00 51.66           C  
ANISOU 2660  CG  ASP B 671     7157   5883   6590      8  -1062    311       C  
ATOM   2661  OD1 ASP B 671     -71.044 -17.576  16.730  1.00 51.94           O  
ANISOU 2661  OD1 ASP B 671     7222   5837   6676     45  -1092    317       O  
ATOM   2662  OD2 ASP B 671     -71.660 -16.170  18.326  1.00 53.59           O  
ANISOU 2662  OD2 ASP B 671     7421   6164   6778     -6  -1105    339       O  
ATOM   2663  N   LEU B 672     -72.430 -14.151  13.117  1.00 38.75           N  
ANISOU 2663  N   LEU B 672     5330   4352   5041    -16   -810    170       N  
ATOM   2664  CA  LEU B 672     -73.203 -13.453  12.088  1.00 35.04           C  
ANISOU 2664  CA  LEU B 672     4826   3930   4559    -51   -735    151       C  
ATOM   2665  C   LEU B 672     -73.218 -14.247  10.805  1.00 35.61           C  
ANISOU 2665  C   LEU B 672     4915   3957   4657    -52   -703    134       C  
ATOM   2666  O   LEU B 672     -74.271 -14.415  10.193  1.00 33.29           O  
ANISOU 2666  O   LEU B 672     4646   3684   4321   -105   -665    145       O  
ATOM   2667  CB  LEU B 672     -72.618 -12.052  11.840  1.00 34.60           C  
ANISOU 2667  CB  LEU B 672     4685   3919   4543    -22   -705    111       C  
ATOM   2668  CG  LEU B 672     -73.258 -11.211  10.758  1.00 33.48           C  
ANISOU 2668  CG  LEU B 672     4502   3823   4397    -48   -632     94       C  
ATOM   2669  CD1 LEU B 672     -74.673 -10.801  11.142  1.00 34.21           C  
ANISOU 2669  CD1 LEU B 672     4612   3973   4413   -105   -609    127       C  
ATOM   2670  CD2 LEU B 672     -72.423  -9.965  10.461  1.00 35.82           C  
ANISOU 2670  CD2 LEU B 672     4720   4143   4749    -13   -608     55       C  
ATOM   2671  N   ILE B 673     -72.052 -14.745  10.380  1.00 36.33           N  
ANISOU 2671  N   ILE B 673     4995   3989   4820      7   -718    103       N  
ATOM   2672  CA  ILE B 673     -71.983 -15.550   9.154  1.00 39.14           C  
ANISOU 2672  CA  ILE B 673     5373   4296   5201     10   -684     78       C  
ATOM   2673  C   ILE B 673     -72.865 -16.802   9.248  1.00 40.48           C  
ANISOU 2673  C   ILE B 673     5638   4422   5322    -38   -703    114       C  
ATOM   2674  O   ILE B 673     -73.541 -17.158   8.285  1.00 40.71           O  
ANISOU 2674  O   ILE B 673     5693   4446   5327    -79   -663    105       O  
ATOM   2675  CB  ILE B 673     -70.538 -15.977   8.824  1.00 42.63           C  
ANISOU 2675  CB  ILE B 673     5788   4676   5732     89   -698     40       C  
ATOM   2676  CG1 ILE B 673     -69.629 -14.761   8.647  1.00 44.06           C  
ANISOU 2676  CG1 ILE B 673     5871   4901   5967    129   -676      4       C  
ATOM   2677  CG2 ILE B 673     -70.482 -16.843   7.571  1.00 42.31           C  
ANISOU 2677  CG2 ILE B 673     5780   4582   5712     93   -658      8       C  
ATOM   2678  CD1 ILE B 673     -70.229 -13.677   7.775  1.00 45.43           C  
ANISOU 2678  CD1 ILE B 673     6003   5141   6116     90   -606    -13       C  
ATOM   2679  N   LYS B 674     -72.840 -17.479  10.390  1.00 41.47           N  
ANISOU 2679  N   LYS B 674     5815   4511   5429    -36   -766    155       N  
ATOM   2680  CA  LYS B 674     -73.697 -18.663  10.587  1.00 44.76           C  
ANISOU 2680  CA  LYS B 674     6326   4883   5797    -90   -786    195       C  
ATOM   2681  C   LYS B 674     -75.174 -18.300  10.508  1.00 42.44           C  
ANISOU 2681  C   LYS B 674     6043   4659   5424   -177   -750    222       C  
ATOM   2682  O   LYS B 674     -75.955 -18.962   9.840  1.00 43.34           O  
ANISOU 2682  O   LYS B 674     6202   4756   5510   -231   -729    228       O  
ATOM   2683  CB  LYS B 674     -73.410 -19.321  11.942  1.00 47.69           C  
ANISOU 2683  CB  LYS B 674     6750   5212   6157    -75   -862    243       C  
ATOM   2684  CG  LYS B 674     -72.063 -20.029  12.005  1.00 54.43           C  
ANISOU 2684  CG  LYS B 674     7610   5980   7091     10   -909    227       C  
ATOM   2685  CD  LYS B 674     -71.847 -20.653  13.378  1.00 59.10           C  
ANISOU 2685  CD  LYS B 674     8258   6534   7663     21   -991    284       C  
ATOM   2686  CE  LYS B 674     -70.402 -21.080  13.554  1.00 66.49           C  
ANISOU 2686  CE  LYS B 674     9174   7401   8686    118  -1045    269       C  
ATOM   2687  NZ  LYS B 674     -70.045 -21.320  14.985  1.00 69.81           N  
ANISOU 2687  NZ  LYS B 674     9628   7810   9088    136  -1132    324       N  
ATOM   2688  N   MET B 675     -75.529 -17.239  11.210  1.00 39.84           N  
ANISOU 2688  N   MET B 675     5668   4408   5061   -190   -744    238       N  
ATOM   2689  CA  MET B 675     -76.861 -16.721  11.212  1.00 41.85           C  
ANISOU 2689  CA  MET B 675     5914   4738   5248   -261   -707    262       C  
ATOM   2690  C   MET B 675     -77.374 -16.432   9.792  1.00 42.94           C  
ANISOU 2690  C   MET B 675     6021   4903   5391   -287   -648    233       C  
ATOM   2691  O   MET B 675     -78.489 -16.818   9.421  1.00 45.70           O  
ANISOU 2691  O   MET B 675     6399   5272   5693   -356   -630    255       O  
ATOM   2692  CB  MET B 675     -76.827 -15.446  12.027  1.00 47.19           C  
ANISOU 2692  CB  MET B 675     6533   5486   5910   -245   -702    262       C  
ATOM   2693  CG  MET B 675     -78.152 -14.915  12.483  1.00 49.85           C  
ANISOU 2693  CG  MET B 675     6863   5901   6175   -307   -673    295       C  
ATOM   2694  SD  MET B 675     -77.789 -13.431  13.454  1.00 48.29           S  
ANISOU 2694  SD  MET B 675     6606   5767   5975   -270   -671    281       S  
ATOM   2695  CE  MET B 675     -79.470 -12.855  13.616  1.00 50.76           C  
ANISOU 2695  CE  MET B 675     6904   6169   6214   -339   -618    311       C  
ATOM   2696  N   ILE B 676     -76.557 -15.791   8.969  1.00 43.16           N  
ANISOU 2696  N   ILE B 676     5993   4933   5474   -237   -620    185       N  
ATOM   2697  CA  ILE B 676     -77.056 -15.337   7.658  1.00 41.46           C  
ANISOU 2697  CA  ILE B 676     5745   4755   5253   -263   -564    162       C  
ATOM   2698  C   ILE B 676     -77.006 -16.419   6.596  1.00 39.34           C  
ANISOU 2698  C   ILE B 676     5528   4425   4993   -278   -555    141       C  
ATOM   2699  O   ILE B 676     -77.775 -16.361   5.639  1.00 38.04           O  
ANISOU 2699  O   ILE B 676     5364   4293   4799   -326   -521    136       O  
ATOM   2700  CB  ILE B 676     -76.434 -14.004   7.170  1.00 39.88           C  
ANISOU 2700  CB  ILE B 676     5462   4599   5094   -218   -527    127       C  
ATOM   2701  CG1 ILE B 676     -74.976 -14.123   6.801  1.00 42.03           C  
ANISOU 2701  CG1 ILE B 676     5713   4817   5439   -148   -530     83       C  
ATOM   2702  CG2 ILE B 676     -76.611 -12.919   8.227  1.00 41.87           C  
ANISOU 2702  CG2 ILE B 676     5671   4908   5331   -212   -533    146       C  
ATOM   2703  CD1 ILE B 676     -74.431 -12.744   6.447  1.00 46.67           C  
ANISOU 2703  CD1 ILE B 676     6219   5452   6064   -116   -494     55       C  
ATOM   2704  N   PHE B 677     -76.133 -17.414   6.763  1.00 40.18           N  
ANISOU 2704  N   PHE B 677     5681   4446   5140   -237   -588    127       N  
ATOM   2705  CA  PHE B 677     -76.119 -18.555   5.845  1.00 42.24           C  
ANISOU 2705  CA  PHE B 677     6005   4637   5408   -252   -581    103       C  
ATOM   2706  C   PHE B 677     -76.853 -19.798   6.378  1.00 43.89           C  
ANISOU 2706  C   PHE B 677     6306   4794   5576   -308   -621    144       C  
ATOM   2707  O   PHE B 677     -76.649 -20.901   5.880  1.00 43.27           O  
ANISOU 2707  O   PHE B 677     6295   4634   5514   -309   -628    125       O  
ATOM   2708  CB  PHE B 677     -74.689 -18.893   5.447  1.00 43.78           C  
ANISOU 2708  CB  PHE B 677     6192   4762   5680   -168   -580     54       C  
ATOM   2709  CG  PHE B 677     -74.109 -17.966   4.414  1.00 42.58           C  
ANISOU 2709  CG  PHE B 677     5967   4650   5561   -135   -524      5       C  
ATOM   2710  CD1 PHE B 677     -74.559 -17.995   3.096  1.00 43.06           C  
ANISOU 2710  CD1 PHE B 677     6039   4727   5596   -173   -474    -23       C  
ATOM   2711  CD2 PHE B 677     -73.101 -17.088   4.746  1.00 41.81           C  
ANISOU 2711  CD2 PHE B 677     5794   4575   5518    -70   -522    -11       C  
ATOM   2712  CE1 PHE B 677     -74.021 -17.147   2.139  1.00 42.57           C  
ANISOU 2712  CE1 PHE B 677     5915   4702   5559   -146   -421    -64       C  
ATOM   2713  CE2 PHE B 677     -72.542 -16.247   3.787  1.00 40.56           C  
ANISOU 2713  CE2 PHE B 677     5570   4450   5390    -45   -468    -53       C  
ATOM   2714  CZ  PHE B 677     -72.991 -16.287   2.483  1.00 40.54           C  
ANISOU 2714  CZ  PHE B 677     5582   4462   5359    -81   -415    -78       C  
ATOM   2715  N   ASP B 678     -77.752 -19.602   7.335  1.00 44.22           N  
ANISOU 2715  N   ASP B 678     6353   4884   5564   -358   -640    198       N  
ATOM   2716  CA  ASP B 678     -78.480 -20.693   7.973  1.00 47.98           C  
ANISOU 2716  CA  ASP B 678     6913   5318   5999   -419   -676    246       C  
ATOM   2717  C   ASP B 678     -79.536 -21.283   7.032  1.00 46.58           C  
ANISOU 2717  C   ASP B 678     6776   5141   5779   -504   -654    245       C  
ATOM   2718  O   ASP B 678     -80.606 -20.709   6.829  1.00 44.91           O  
ANISOU 2718  O   ASP B 678     6530   5015   5520   -567   -628    265       O  
ATOM   2719  CB  ASP B 678     -79.128 -20.186   9.268  1.00 49.78           C  
ANISOU 2719  CB  ASP B 678     7126   5611   6177   -449   -694    301       C  
ATOM   2720  CG  ASP B 678     -79.657 -21.297  10.144  1.00 52.77           C  
ANISOU 2720  CG  ASP B 678     7592   5942   6516   -502   -736    357       C  
ATOM   2721  OD1 ASP B 678     -80.138 -22.323   9.626  1.00 56.11           O  
ANISOU 2721  OD1 ASP B 678     8081   6310   6926   -556   -740    362       O  
ATOM   2722  OD2 ASP B 678     -79.619 -21.130  11.374  1.00 57.86           O  
ANISOU 2722  OD2 ASP B 678     8242   6603   7137   -496   -766    396       O  
ATOM   2723  N   VAL B 679     -79.233 -22.464   6.512  1.00 47.92           N  
ANISOU 2723  N   VAL B 679     7023   5214   5970   -507   -667    224       N  
ATOM   2724  CA  VAL B 679     -80.097 -23.168   5.562  1.00 50.12           C  
ANISOU 2724  CA  VAL B 679     7353   5477   6213   -588   -652    214       C  
ATOM   2725  C   VAL B 679     -81.456 -23.563   6.183  1.00 50.06           C  
ANISOU 2725  C   VAL B 679     7380   5501   6138   -693   -670    278       C  
ATOM   2726  O   VAL B 679     -82.496 -23.480   5.534  1.00 44.05           O  
ANISOU 2726  O   VAL B 679     6609   4795   5333   -773   -649    283       O  
ATOM   2727  CB  VAL B 679     -79.353 -24.413   5.039  1.00 52.27           C  
ANISOU 2727  CB  VAL B 679     7711   5622   6528   -559   -666    175       C  
ATOM   2728  CG1 VAL B 679     -80.262 -25.284   4.203  1.00 53.91           C  
ANISOU 2728  CG1 VAL B 679     7990   5800   6694   -653   -659    166       C  
ATOM   2729  CG2 VAL B 679     -78.135 -23.980   4.230  1.00 50.44           C  
ANISOU 2729  CG2 VAL B 679     7433   5373   6357   -465   -633    107       C  
ATOM   2730  N   GLU B 680     -81.451 -23.952   7.454  1.00 51.05           N  
ANISOU 2730  N   GLU B 680     7541   5600   6254   -694   -709    329       N  
ATOM   2731  CA  GLU B 680     -82.718 -24.281   8.123  1.00 51.54           C  
ANISOU 2731  CA  GLU B 680     7630   5699   6252   -795   -720    393       C  
ATOM   2732  C   GLU B 680     -83.614 -23.045   8.266  1.00 51.51           C  
ANISOU 2732  C   GLU B 680     7532   5833   6207   -827   -685    413       C  
ATOM   2733  O   GLU B 680     -84.834 -23.146   8.130  1.00 52.99           O  
ANISOU 2733  O   GLU B 680     7715   6075   6345   -920   -672    443       O  
ATOM   2734  CB  GLU B 680     -82.559 -25.085   9.432  1.00 53.93           C  
ANISOU 2734  CB  GLU B 680     8007   5938   6546   -799   -769    448       C  
ATOM   2735  CG  GLU B 680     -83.574 -26.246   9.471  1.00 59.20           C  
ANISOU 2735  CG  GLU B 680     8760   6562   7170   -911   -784    489       C  
ATOM   2736  CD  GLU B 680     -83.394 -27.281   8.346  1.00 58.00           C  
ANISOU 2736  CD  GLU B 680     8683   6309   7046   -929   -789    445       C  
ATOM   2737  OE1 GLU B 680     -84.393 -27.897   7.893  1.00 68.29           O  
ANISOU 2737  OE1 GLU B 680    10027   7609   8312  -1033   -785    457       O  
ATOM   2738  OE2 GLU B 680     -82.242 -27.498   7.918  1.00 55.53           O  
ANISOU 2738  OE2 GLU B 680     8387   5917   6793   -840   -795    395       O  
ATOM   2739  N   SER B 681     -83.024 -21.867   8.484  1.00 47.96           N  
ANISOU 2739  N   SER B 681     7004   5439   5781   -751   -667    395       N  
ATOM   2740  CA  SER B 681     -83.814 -20.614   8.485  1.00 46.53           C  
ANISOU 2740  CA  SER B 681     6730   5379   5568   -770   -629    406       C  
ATOM   2741  C   SER B 681     -84.428 -20.325   7.131  1.00 43.13           C  
ANISOU 2741  C   SER B 681     6263   4994   5130   -809   -596    380       C  
ATOM   2742  O   SER B 681     -85.560 -19.859   7.047  1.00 42.30           O  
ANISOU 2742  O   SER B 681     6112   4977   4985   -869   -575    408       O  
ATOM   2743  CB  SER B 681     -82.970 -19.420   8.900  1.00 44.03           C  
ANISOU 2743  CB  SER B 681     6345   5099   5284   -680   -618    384       C  
ATOM   2744  OG  SER B 681     -82.671 -19.500  10.260  1.00 45.87           O  
ANISOU 2744  OG  SER B 681     6602   5320   5507   -660   -648    417       O  
ATOM   2745  N   MET B 682     -83.674 -20.614   6.078  1.00 43.76           N  
ANISOU 2745  N   MET B 682     6364   5017   5247   -774   -591    327       N  
ATOM   2746  CA  MET B 682     -84.192 -20.477   4.713  1.00 46.84           C  
ANISOU 2746  CA  MET B 682     6735   5440   5622   -816   -565    301       C  
ATOM   2747  C   MET B 682     -85.427 -21.352   4.520  1.00 47.71           C  
ANISOU 2747  C   MET B 682     6891   5556   5680   -929   -580    333       C  
ATOM   2748  O   MET B 682     -86.466 -20.888   4.070  1.00 47.71           O  
ANISOU 2748  O   MET B 682     6842   5643   5645   -988   -564    351       O  
ATOM   2749  CB  MET B 682     -83.101 -20.826   3.678  1.00 47.22           C  
ANISOU 2749  CB  MET B 682     6815   5413   5713   -762   -556    235       C  
ATOM   2750  CG  MET B 682     -81.890 -19.878   3.670  1.00 47.78           C  
ANISOU 2750  CG  MET B 682     6827   5490   5839   -657   -536    200       C  
ATOM   2751  SD  MET B 682     -80.595 -20.447   2.550  1.00 46.13           S  
ANISOU 2751  SD  MET B 682     6657   5189   5682   -595   -520    125       S  
ATOM   2752  CE  MET B 682     -79.130 -19.815   3.320  1.00 44.48           C  
ANISOU 2752  CE  MET B 682     6399   4958   5545   -479   -524    108       C  
ATOM   2753  N   LYS B 683     -85.328 -22.616   4.912  1.00 49.40           N  
ANISOU 2753  N   LYS B 683     7199   5678   5894   -960   -612    343       N  
ATOM   2754  CA  LYS B 683     -86.476 -23.530   4.805  1.00 49.83           C  
ANISOU 2754  CA  LYS B 683     7303   5727   5901  -1076   -629    376       C  
ATOM   2755  C   LYS B 683     -87.676 -23.122   5.674  1.00 48.11           C  
ANISOU 2755  C   LYS B 683     7035   5607   5638  -1142   -624    442       C  
ATOM   2756  O   LYS B 683     -88.822 -23.202   5.229  1.00 49.07           O  
ANISOU 2756  O   LYS B 683     7135   5788   5720  -1233   -620    463       O  
ATOM   2757  CB  LYS B 683     -86.031 -24.954   5.119  1.00 53.27           C  
ANISOU 2757  CB  LYS B 683     7856   6031   6351  -1090   -665    375       C  
ATOM   2758  CG  LYS B 683     -85.087 -25.567   4.087  1.00 58.44           C  
ANISOU 2758  CG  LYS B 683     8571   6586   7046  -1045   -665    306       C  
ATOM   2759  CD  LYS B 683     -84.619 -26.921   4.606  1.00 64.60           C  
ANISOU 2759  CD  LYS B 683     9465   7230   7849  -1044   -702    313       C  
ATOM   2760  CE  LYS B 683     -83.440 -27.499   3.837  1.00 69.97           C  
ANISOU 2760  CE  LYS B 683    10202   7800   8584   -969   -700    243       C  
ATOM   2761  NZ  LYS B 683     -82.999 -28.761   4.493  1.00 73.57           N  
ANISOU 2761  NZ  LYS B 683    10764   8121   9067   -960   -740    259       N  
ATOM   2762  N   LYS B 684     -87.424 -22.701   6.910  1.00 46.52           N  
ANISOU 2762  N   LYS B 684     6813   5423   5438  -1099   -626    474       N  
ATOM   2763  CA  LYS B 684     -88.520 -22.248   7.811  1.00 49.30           C  
ANISOU 2763  CA  LYS B 684     7114   5872   5746  -1153   -612    533       C  
ATOM   2764  C   LYS B 684     -89.296 -21.112   7.163  1.00 52.39           C  
ANISOU 2764  C   LYS B 684     7398   6382   6125  -1163   -575    530       C  
ATOM   2765  O   LYS B 684     -90.533 -21.090   7.155  1.00 51.02           O  
ANISOU 2765  O   LYS B 684     7188   6284   5914  -1246   -565    568       O  
ATOM   2766  CB  LYS B 684     -88.001 -21.836   9.218  1.00 46.76           C  
ANISOU 2766  CB  LYS B 684     6787   5554   5425  -1093   -615    559       C  
ATOM   2767  N   ALA B 685     -88.549 -20.174   6.599  1.00 54.84           N  
ANISOU 2767  N   ALA B 685     7659   6707   6471  -1078   -557    486       N  
ATOM   2768  CA  ALA B 685     -89.164 -19.049   5.910  1.00 56.21           C  
ANISOU 2768  CA  ALA B 685     7735   6982   6638  -1076   -526    483       C  
ATOM   2769  C   ALA B 685     -90.087 -19.518   4.794  1.00 54.43           C  
ANISOU 2769  C   ALA B 685     7512   6783   6386  -1165   -532    486       C  
ATOM   2770  O   ALA B 685     -91.235 -19.072   4.693  1.00 52.56           O  
ANISOU 2770  O   ALA B 685     7207   6643   6122  -1218   -520    520       O  
ATOM   2771  CB  ALA B 685     -88.093 -18.156   5.349  1.00 55.61           C  
ANISOU 2771  CB  ALA B 685     7626   6897   6608   -978   -509    434       C  
ATOM   2772  N   MET B 686     -89.606 -20.472   4.002  1.00 53.02           N  
ANISOU 2772  N   MET B 686     7413   6519   6214  -1184   -554    449       N  
ATOM   2773  CA  MET B 686     -90.419 -21.047   2.921  1.00 54.13           C  
ANISOU 2773  CA  MET B 686     7571   6673   6323  -1276   -567    445       C  
ATOM   2774  C   MET B 686     -91.672 -21.782   3.445  1.00 56.60           C  
ANISOU 2774  C   MET B 686     7896   7014   6595  -1392   -585    500       C  
ATOM   2775  O   MET B 686     -92.756 -21.731   2.849  1.00 57.30           O  
ANISOU 2775  O   MET B 686     7942   7177   6652  -1473   -589    520       O  
ATOM   2776  CB  MET B 686     -89.556 -21.984   2.049  1.00 54.11           C  
ANISOU 2776  CB  MET B 686     7665   6559   6336  -1269   -583    387       C  
ATOM   2777  CG  MET B 686     -88.475 -21.240   1.281  1.00 53.05           C  
ANISOU 2777  CG  MET B 686     7507   6414   6235  -1171   -558    332       C  
ATOM   2778  SD  MET B 686     -87.292 -22.192   0.306  1.00 52.38           S  
ANISOU 2778  SD  MET B 686     7524   6202   6176  -1139   -562    255       S  
ATOM   2779  CE  MET B 686     -88.368 -22.758  -0.995  1.00 54.72           C  
ANISOU 2779  CE  MET B 686     7851   6527   6413  -1259   -576    244       C  
ATOM   2780  N   VAL B 687     -91.524 -22.491   4.554  1.00 56.54           N  
ANISOU 2780  N   VAL B 687     7947   6949   6586  -1404   -597    528       N  
ATOM   2781  CA  VAL B 687     -92.670 -23.157   5.148  1.00 59.87           C  
ANISOU 2781  CA  VAL B 687     8379   7398   6969  -1515   -608    584       C  
ATOM   2782  C   VAL B 687     -93.683 -22.097   5.569  1.00 58.42           C  
ANISOU 2782  C   VAL B 687     8076   7354   6766  -1528   -578    628       C  
ATOM   2783  O   VAL B 687     -94.862 -22.255   5.301  1.00 58.58           O  
ANISOU 2783  O   VAL B 687     8056   7444   6757  -1623   -580    660       O  
ATOM   2784  CB  VAL B 687     -92.265 -24.069   6.336  1.00 63.60           C  
ANISOU 2784  CB  VAL B 687     8941   7781   7441  -1521   -627    612       C  
ATOM   2785  CG1 VAL B 687     -93.487 -24.499   7.142  1.00 64.01           C  
ANISOU 2785  CG1 VAL B 687     8986   7885   7450  -1630   -626    681       C  
ATOM   2786  CG2 VAL B 687     -91.502 -25.292   5.826  1.00 63.27           C  
ANISOU 2786  CG2 VAL B 687     9022   7598   7419  -1527   -660    575       C  
ATOM   2787  N   GLU B 688     -93.226 -21.030   6.219  1.00 56.18           N  
ANISOU 2787  N   GLU B 688     7735   7111   6502  -1434   -549    627       N  
ATOM   2788  CA  GLU B 688     -94.135 -19.970   6.670  1.00 63.50           C  
ANISOU 2788  CA  GLU B 688     8550   8163   7415  -1433   -514    663       C  
ATOM   2789  C   GLU B 688     -94.872 -19.306   5.512  1.00 60.99           C  
ANISOU 2789  C   GLU B 688     8146   7932   7096  -1453   -507    659       C  
ATOM   2790  O   GLU B 688     -95.974 -18.828   5.684  1.00 59.15           O  
ANISOU 2790  O   GLU B 688     7827   7801   6847  -1493   -488    698       O  
ATOM   2791  CB  GLU B 688     -93.407 -18.909   7.518  1.00 67.75           C  
ANISOU 2791  CB  GLU B 688     9051   8716   7974  -1322   -485    653       C  
ATOM   2792  CG  GLU B 688     -93.263 -19.223   9.005  1.00 77.62           C  
ANISOU 2792  CG  GLU B 688    10342   9945   9205  -1321   -482    684       C  
ATOM   2793  CD  GLU B 688     -92.830 -17.987   9.817  1.00 90.54           C  
ANISOU 2793  CD  GLU B 688    11923  11625  10853  -1225   -449    675       C  
ATOM   2794  OE1 GLU B 688     -91.640 -17.899  10.202  1.00 90.55           O  
ANISOU 2794  OE1 GLU B 688    11969  11558  10878  -1149   -463    646       O  
ATOM   2795  OE2 GLU B 688     -93.675 -17.079  10.070  1.00 98.49           O  
ANISOU 2795  OE2 GLU B 688    12838  12734  11848  -1225   -410    695       O  
ATOM   2796  N   TYR B 689     -94.274 -19.295   4.326  1.00 64.29           N  
ANISOU 2796  N   TYR B 689     8587   8310   7530  -1427   -523    613       N  
ATOM   2797  CA  TYR B 689     -94.985 -18.818   3.121  1.00 63.88           C  
ANISOU 2797  CA  TYR B 689     8469   8335   7469  -1459   -527    612       C  
ATOM   2798  C   TYR B 689     -95.913 -19.845   2.483  1.00 65.28           C  
ANISOU 2798  C   TYR B 689     8675   8518   7610  -1587   -561    628       C  
ATOM   2799  O   TYR B 689     -96.537 -19.572   1.446  1.00 66.75           O  
ANISOU 2799  O   TYR B 689     8813   8767   7781  -1625   -575    629       O  
ATOM   2800  CB  TYR B 689     -93.986 -18.372   2.064  1.00 62.74           C  
ANISOU 2800  CB  TYR B 689     8340   8150   7346  -1385   -527    557       C  
ATOM   2801  CG  TYR B 689     -93.282 -17.108   2.409  1.00 58.94           C  
ANISOU 2801  CG  TYR B 689     7804   7690   6902  -1270   -493    544       C  
ATOM   2802  CD1 TYR B 689     -93.989 -15.950   2.737  1.00 56.91           C  
ANISOU 2802  CD1 TYR B 689     7440   7534   6648  -1243   -466    578       C  
ATOM   2803  CD2 TYR B 689     -91.900 -17.061   2.394  1.00 59.12           C  
ANISOU 2803  CD2 TYR B 689     7879   7628   6957  -1187   -488    497       C  
ATOM   2804  CE1 TYR B 689     -93.326 -14.787   3.054  1.00 57.31           C  
ANISOU 2804  CE1 TYR B 689     7448   7594   6734  -1141   -436    563       C  
ATOM   2805  CE2 TYR B 689     -91.234 -15.912   2.709  1.00 59.02           C  
ANISOU 2805  CE2 TYR B 689     7816   7631   6978  -1089   -459    484       C  
ATOM   2806  CZ  TYR B 689     -91.944 -14.774   3.037  1.00 56.60           C  
ANISOU 2806  CZ  TYR B 689     7413   7419   6674  -1068   -434    516       C  
ATOM   2807  OH  TYR B 689     -91.228 -13.659   3.365  1.00 52.65           O  
ANISOU 2807  OH  TYR B 689     6874   6922   6208   -973   -407    499       O  
ATOM   2808  N   GLU B 690     -95.959 -21.036   3.068  1.00 63.53           N  
ANISOU 2808  N   GLU B 690     8538   8226   7374  -1653   -579    639       N  
ATOM   2809  CA  GLU B 690     -96.809 -22.103   2.569  1.00 66.54           C  
ANISOU 2809  CA  GLU B 690     8958   8602   7723  -1784   -614    653       C  
ATOM   2810  C   GLU B 690     -96.324 -22.642   1.220  1.00 65.03           C  
ANISOU 2810  C   GLU B 690     8839   8344   7526  -1801   -643    596       C  
ATOM   2811  O   GLU B 690     -97.088 -23.219   0.443  1.00 63.77           O  
ANISOU 2811  O   GLU B 690     8691   8204   7336  -1905   -674    598       O  
ATOM   2812  CB  GLU B 690     -98.272 -21.635   2.484  1.00 62.43           C  
ANISOU 2812  CB  GLU B 690     8321   8218   7180  -1859   -610    706       C  
ATOM   2813  N   ILE B 691     -95.030 -22.498   0.972  1.00 65.40           N  
ANISOU 2813  N   ILE B 691     8938   8311   7601  -1702   -634    543       N  
ATOM   2814  CA  ILE B 691     -94.421 -23.061  -0.219  1.00 67.09           C  
ANISOU 2814  CA  ILE B 691     9232   8450   7810  -1708   -652    482       C  
ATOM   2815  C   ILE B 691     -94.283 -24.564  -0.072  1.00 70.71           C  
ANISOU 2815  C   ILE B 691     9816   8790   8261  -1779   -680    468       C  
ATOM   2816  O   ILE B 691     -93.970 -25.067   0.997  1.00 70.84           O  
ANISOU 2816  O   ILE B 691     9879   8742   8294  -1766   -680    488       O  
ATOM   2817  CB  ILE B 691     -93.065 -22.393  -0.483  1.00 63.72           C  
ANISOU 2817  CB  ILE B 691     8811   7978   7420  -1577   -625    431       C  
ATOM   2818  CG1 ILE B 691     -93.406 -20.984  -0.954  1.00 62.90           C  
ANISOU 2818  CG1 ILE B 691     8591   7993   7315  -1534   -605    445       C  
ATOM   2819  CG2 ILE B 691     -92.231 -23.144  -1.521  1.00 63.09           C  
ANISOU 2819  CG2 ILE B 691     8831   7799   7340  -1571   -635    361       C  
ATOM   2820  CD1 ILE B 691     -92.272 -20.107  -1.350  1.00 62.85           C  
ANISOU 2820  CD1 ILE B 691     8568   7970   7341  -1418   -576    404       C  
ATOM   2821  N   ASP B 692     -94.502 -25.277  -1.160  1.00 68.80           N  
ANISOU 2821  N   ASP B 692     9634   8515   7991  -1854   -707    432       N  
ATOM   2822  CA  ASP B 692     -94.342 -26.699  -1.139  1.00 71.20           C  
ANISOU 2822  CA  ASP B 692    10066   8697   8291  -1920   -733    410       C  
ATOM   2823  C   ASP B 692     -92.877 -27.089  -1.328  1.00 69.51           C  
ANISOU 2823  C   ASP B 692     9945   8351   8114  -1821   -721    344       C  
ATOM   2824  O   ASP B 692     -92.394 -27.156  -2.462  1.00 61.38           O  
ANISOU 2824  O   ASP B 692     8952   7291   7077  -1803   -718    281       O  
ATOM   2825  CB  ASP B 692     -95.180 -27.338  -2.234  1.00 74.09           C  
ANISOU 2825  CB  ASP B 692    10465   9076   8610  -2047   -767    392       C  
ATOM   2826  CG  ASP B 692     -95.220 -28.839  -2.094  1.00 76.39           C  
ANISOU 2826  CG  ASP B 692    10887   9242   8896  -2134   -797    379       C  
ATOM   2827  OD1 ASP B 692     -96.321 -29.361  -2.283  1.00 82.39           O  
ANISOU 2827  OD1 ASP B 692    11648  10037   9620  -2268   -828    407       O  
ATOM   2828  OD2 ASP B 692     -94.184 -29.481  -1.741  1.00 72.92           O  
ANISOU 2828  OD2 ASP B 692    10546   8669   8491  -2071   -790    347       O  
ATOM   2829  N   LEU B 693     -92.201 -27.404  -0.223  1.00 68.43           N  
ANISOU 2829  N   LEU B 693     9848   8137   8014  -1762   -716    360       N  
ATOM   2830  CA  LEU B 693     -90.780 -27.772  -0.261  1.00 71.93           C  
ANISOU 2830  CA  LEU B 693    10369   8457   8503  -1658   -707    304       C  
ATOM   2831  C   LEU B 693     -90.502 -29.145  -0.888  1.00 78.96           C  
ANISOU 2831  C   LEU B 693    11396   9213   9393  -1707   -729    253       C  
ATOM   2832  O   LEU B 693     -89.375 -29.427  -1.309  1.00 75.25           O  
ANISOU 2832  O   LEU B 693    10985   8649   8957  -1624   -716    191       O  
ATOM   2833  CB  LEU B 693     -90.185 -27.758   1.135  1.00 71.20           C  
ANISOU 2833  CB  LEU B 693    10281   8323   8449  -1586   -705    342       C  
ATOM   2834  CG  LEU B 693     -89.942 -26.396   1.768  1.00 70.59           C  
ANISOU 2834  CG  LEU B 693    10091   8341   8388  -1496   -677    368       C  
ATOM   2835  CD1 LEU B 693     -89.284 -26.576   3.120  1.00 70.46           C  
ANISOU 2835  CD1 LEU B 693    10101   8267   8402  -1433   -684    399       C  
ATOM   2836  CD2 LEU B 693     -89.054 -25.550   0.876  1.00 69.41           C  
ANISOU 2836  CD2 LEU B 693     9899   8209   8263  -1399   -649    309       C  
ATOM   2837  N   GLN B 694     -91.524 -29.998  -0.945  1.00 85.46           N  
ANISOU 2837  N   GLN B 694    12267  10025  10179  -1841   -760    278       N  
ATOM   2838  CA  GLN B 694     -91.409 -31.275  -1.647  1.00 87.81           C  
ANISOU 2838  CA  GLN B 694    12696  10199  10469  -1904   -782    226       C  
ATOM   2839  C   GLN B 694     -91.305 -31.017  -3.146  1.00 84.17           C  
ANISOU 2839  C   GLN B 694    12236   9766   9980  -1908   -770    153       C  
ATOM   2840  O   GLN B 694     -90.425 -31.564  -3.796  1.00 85.88           O  
ANISOU 2840  O   GLN B 694    12539   9877  10213  -1861   -760     79       O  
ATOM   2841  CB  GLN B 694     -92.586 -32.212  -1.336  1.00 88.21           C  
ANISOU 2841  CB  GLN B 694    12795  10236  10485  -2059   -819    273       C  
ATOM   2842  N   LYS B 695     -92.157 -30.146  -3.685  1.00 80.93           N  
ANISOU 2842  N   LYS B 695    11725   9498   9526  -1956   -770    173       N  
ATOM   2843  CA  LYS B 695     -92.126 -29.851  -5.124  1.00 84.85           C  
ANISOU 2843  CA  LYS B 695    12221  10033   9984  -1967   -764    112       C  
ATOM   2844  C   LYS B 695     -91.082 -28.774  -5.511  1.00 89.05           C  
ANISOU 2844  C   LYS B 695    12695  10598  10542  -1828   -719     76       C  
ATOM   2845  O   LYS B 695     -90.577 -28.769  -6.637  1.00 86.61           O  
ANISOU 2845  O   LYS B 695    12423  10269  10214  -1807   -702      7       O  
ATOM   2846  CB  LYS B 695     -93.520 -29.465  -5.625  1.00 84.94           C  
ANISOU 2846  CB  LYS B 695    12157  10179   9936  -2086   -793    152       C  
ATOM   2847  N   MET B 696     -90.763 -27.857  -4.595  1.00 88.80           N  
ANISOU 2847  N   MET B 696    12573  10617  10549  -1738   -697    121       N  
ATOM   2848  CA  MET B 696     -89.753 -26.813  -4.860  1.00 83.10           C  
ANISOU 2848  CA  MET B 696    11793   9923   9857  -1609   -655     91       C  
ATOM   2849  C   MET B 696     -88.795 -26.632  -3.699  1.00 80.26           C  
ANISOU 2849  C   MET B 696    11422   9509   9564  -1498   -637    106       C  
ATOM   2850  O   MET B 696     -88.948 -25.700  -2.906  1.00 69.82           O  
ANISOU 2850  O   MET B 696    10006   8266   8257  -1457   -628    158       O  
ATOM   2851  CB  MET B 696     -90.389 -25.460  -5.175  1.00 82.10           C  
ANISOU 2851  CB  MET B 696    11540   9949   9705  -1608   -645    130       C  
ATOM   2852  CG  MET B 696     -89.376 -24.437  -5.690  1.00 79.22           C  
ANISOU 2852  CG  MET B 696    11128   9607   9363  -1493   -602     93       C  
ATOM   2853  SD  MET B 696     -90.135 -22.932  -6.275  1.00 85.47           S  
ANISOU 2853  SD  MET B 696    11791  10562  10121  -1498   -595    135       S  
ATOM   2854  CE  MET B 696     -90.572 -22.105  -4.736  1.00 88.64           C  
ANISOU 2854  CE  MET B 696    12087  11031  10561  -1460   -592    217       C  
ATOM   2855  N   PRO B 697     -87.787 -27.507  -3.605  1.00 81.06           N  
ANISOU 2855  N   PRO B 697    11618   9476   9704  -1445   -633     58       N  
ATOM   2856  CA  PRO B 697     -86.818 -27.351  -2.531  1.00 81.59           C  
ANISOU 2856  CA  PRO B 697    11673   9492   9835  -1337   -624     73       C  
ATOM   2857  C   PRO B 697     -85.952 -26.116  -2.717  1.00 78.27           C  
ANISOU 2857  C   PRO B 697    11164   9129   9445  -1224   -584     52       C  
ATOM   2858  O   PRO B 697     -85.903 -25.540  -3.795  1.00 75.20           O  
ANISOU 2858  O   PRO B 697    10745   8794   9034  -1220   -558     16       O  
ATOM   2859  CB  PRO B 697     -85.956 -28.609  -2.650  1.00 81.27           C  
ANISOU 2859  CB  PRO B 697    11755   9293   9829  -1308   -630     18       C  
ATOM   2860  CG  PRO B 697     -86.118 -29.054  -4.058  1.00 82.70           C  
ANISOU 2860  CG  PRO B 697    11996   9455   9971  -1363   -620    -49       C  
ATOM   2861  CD  PRO B 697     -87.523 -28.698  -4.430  1.00 83.69           C  
ANISOU 2861  CD  PRO B 697    12075   9697  10028  -1484   -640     -9       C  
ATOM   2862  N   LEU B 698     -85.262 -25.744  -1.657  1.00 72.88           N  
ANISOU 2862  N   LEU B 698    10447   8432   8813  -1137   -581     77       N  
ATOM   2863  CA  LEU B 698     -84.290 -24.670  -1.692  1.00 71.75           C  
ANISOU 2863  CA  LEU B 698    10228   8324   8710  -1027   -547     56       C  
ATOM   2864  C   LEU B 698     -83.378 -24.712  -2.937  1.00 73.32           C  
ANISOU 2864  C   LEU B 698    10452   8483   8923   -977   -510    -25       C  
ATOM   2865  O   LEU B 698     -83.154 -23.692  -3.589  1.00 69.35           O  
ANISOU 2865  O   LEU B 698     9881   8054   8416   -943   -476    -41       O  
ATOM   2866  CB  LEU B 698     -83.436 -24.774  -0.440  1.00 69.64           C  
ANISOU 2866  CB  LEU B 698     9963   7998   8501   -944   -560     76       C  
ATOM   2867  CG  LEU B 698     -82.795 -23.504   0.080  1.00 69.20           C  
ANISOU 2867  CG  LEU B 698     9807   8005   8480   -853   -539     87       C  
ATOM   2868  CD1 LEU B 698     -83.708 -22.290   0.160  1.00 68.52           C  
ANISOU 2868  CD1 LEU B 698     9626   8052   8358   -886   -527    130       C  
ATOM   2869  CD2 LEU B 698     -82.215 -23.818   1.445  1.00 65.51           C  
ANISOU 2869  CD2 LEU B 698     9357   7480   8053   -799   -569    118       C  
ATOM   2870  N   GLY B 699     -82.856 -25.893  -3.258  1.00 71.78           N  
ANISOU 2870  N   GLY B 699    10358   8170   8746   -972   -514    -74       N  
ATOM   2871  CA  GLY B 699     -81.971 -26.059  -4.416  1.00 69.88           C  
ANISOU 2871  CA  GLY B 699    10151   7883   8518   -924   -472   -158       C  
ATOM   2872  C   GLY B 699     -82.608 -25.827  -5.785  1.00 68.72           C  
ANISOU 2872  C   GLY B 699    10009   7800   8300   -997   -452   -189       C  
ATOM   2873  O   GLY B 699     -81.902 -25.604  -6.761  1.00 64.89           O  
ANISOU 2873  O   GLY B 699     9527   7312   7816   -954   -408   -251       O  
ATOM   2874  N   LYS B 700     -83.936 -25.848  -5.857  1.00 70.48           N  
ANISOU 2874  N   LYS B 700    10229   8089   8461  -1109   -485   -145       N  
ATOM   2875  CA  LYS B 700     -84.642 -25.701  -7.135  1.00 73.59           C  
ANISOU 2875  CA  LYS B 700    10633   8547   8782  -1190   -480   -169       C  
ATOM   2876  C   LYS B 700     -85.053 -24.260  -7.425  1.00 74.13           C  
ANISOU 2876  C   LYS B 700    10586   8756   8824  -1184   -465   -130       C  
ATOM   2877  O   LYS B 700     -85.397 -23.950  -8.560  1.00 80.75           O  
ANISOU 2877  O   LYS B 700    11423   9652   9607  -1228   -455   -151       O  
ATOM   2878  CB  LYS B 700     -85.877 -26.612  -7.201  1.00 75.17           C  
ANISOU 2878  CB  LYS B 700    10896   8738   8928  -1324   -528   -147       C  
ATOM   2879  N   LEU B 701     -85.051 -23.393  -6.411  1.00 72.14           N  
ANISOU 2879  N   LEU B 701    10245   8557   8609  -1134   -467    -72       N  
ATOM   2880  CA  LEU B 701     -85.315 -21.967  -6.613  1.00 69.95           C  
ANISOU 2880  CA  LEU B 701     9859   8398   8319  -1112   -449    -36       C  
ATOM   2881  C   LEU B 701     -84.386 -21.397  -7.676  1.00 65.51           C  
ANISOU 2881  C   LEU B 701     9288   7843   7760  -1051   -400    -92       C  
ATOM   2882  O   LEU B 701     -83.173 -21.564  -7.598  1.00 64.34           O  
ANISOU 2882  O   LEU B 701     9160   7623   7664   -968   -368   -138       O  
ATOM   2883  CB  LEU B 701     -85.071 -21.163  -5.331  1.00 73.06           C  
ANISOU 2883  CB  LEU B 701    10172   8819   8767  -1042   -447     13       C  
ATOM   2884  CG  LEU B 701     -86.075 -21.303  -4.190  1.00 76.82           C  
ANISOU 2884  CG  LEU B 701    10625   9326   9235  -1095   -485     82       C  
ATOM   2885  CD1 LEU B 701     -85.666 -20.411  -3.031  1.00 75.13           C  
ANISOU 2885  CD1 LEU B 701    10337   9139   9070  -1015   -475    118       C  
ATOM   2886  CD2 LEU B 701     -87.472 -20.936  -4.654  1.00 77.82           C  
ANISOU 2886  CD2 LEU B 701    10708   9558   9303  -1188   -505    126       C  
ATOM   2887  N   SER B 702     -84.953 -20.689  -8.636  1.00 60.00           N  
ANISOU 2887  N   SER B 702     8554   7235   7007  -1092   -394    -82       N  
ATOM   2888  CA  SER B 702     -84.174 -20.124  -9.727  1.00 60.15           C  
ANISOU 2888  CA  SER B 702     8568   7270   7015  -1048   -345   -128       C  
ATOM   2889  C   SER B 702     -84.521 -18.645  -9.946  1.00 57.33           C  
ANISOU 2889  C   SER B 702     8111   7028   6646  -1032   -335    -77       C  
ATOM   2890  O   SER B 702     -85.675 -18.224  -9.819  1.00 54.80           O  
ANISOU 2890  O   SER B 702     7741   6787   6292  -1090   -371    -17       O  
ATOM   2891  CB  SER B 702     -84.415 -20.932 -11.011  1.00 64.16           C  
ANISOU 2891  CB  SER B 702     9168   7759   7452  -1122   -346   -183       C  
ATOM   2892  OG  SER B 702     -85.292 -20.251 -11.892  1.00 64.64           O  
ANISOU 2892  OG  SER B 702     9195   7925   7441  -1186   -360   -152       O  
ATOM   2893  N   LYS B 703     -83.505 -17.866 -10.287  1.00 60.14           N  
ANISOU 2893  N   LYS B 703     8433   7387   7032   -954   -285   -101       N  
ATOM   2894  CA  LYS B 703     -83.655 -16.444 -10.576  1.00 62.63           C  
ANISOU 2894  CA  LYS B 703     8662   7795   7341   -931   -268    -58       C  
ATOM   2895  C   LYS B 703     -84.669 -16.196 -11.702  1.00 64.00           C  
ANISOU 2895  C   LYS B 703     8839   8050   7428  -1014   -289    -35       C  
ATOM   2896  O   LYS B 703     -85.477 -15.264 -11.632  1.00 61.22           O  
ANISOU 2896  O   LYS B 703     8414   7784   7062  -1029   -309     30       O  
ATOM   2897  CB  LYS B 703     -82.281 -15.890 -10.977  1.00 66.35           C  
ANISOU 2897  CB  LYS B 703     9119   8241   7852   -847   -205   -102       C  
ATOM   2898  CG  LYS B 703     -82.085 -14.400 -10.795  1.00 73.62           C  
ANISOU 2898  CG  LYS B 703     9944   9225   8804   -795   -183    -58       C  
ATOM   2899  CD  LYS B 703     -80.598 -14.084 -10.530  1.00 76.71           C  
ANISOU 2899  CD  LYS B 703    10314   9564   9268   -701   -132    -99       C  
ATOM   2900  CE  LYS B 703     -79.636 -14.809 -11.471  1.00 82.84           C  
ANISOU 2900  CE  LYS B 703    11156  10284  10034   -687    -84   -178       C  
ATOM   2901  NZ  LYS B 703     -78.497 -13.960 -11.951  1.00 86.58           N  
ANISOU 2901  NZ  LYS B 703    11589  10767  10542   -625    -20   -202       N  
ATOM   2902  N   ARG B 704     -84.655 -17.059 -12.716  1.00 69.02           N  
ANISOU 2902  N   ARG B 704     9562   8658   8005  -1068   -286    -88       N  
ATOM   2903  CA  ARG B 704     -85.532 -16.878 -13.874  1.00 74.47           C  
ANISOU 2903  CA  ARG B 704    10265   9426   8605  -1150   -310    -72       C  
ATOM   2904  C   ARG B 704     -87.001 -17.237 -13.557  1.00 69.43           C  
ANISOU 2904  C   ARG B 704     9614   8837   7931  -1243   -380    -18       C  
ATOM   2905  O   ARG B 704     -87.916 -16.585 -14.068  1.00 68.03           O  
ANISOU 2905  O   ARG B 704     9390   8755   7705  -1289   -411     35       O  
ATOM   2906  CB  ARG B 704     -85.010 -17.668 -15.086  1.00 71.19           C  
ANISOU 2906  CB  ARG B 704     9952   8967   8130  -1180   -281   -152       C  
ATOM   2907  N   GLN B 705     -87.222 -18.252 -12.720  1.00 63.77           N  
ANISOU 2907  N   GLN B 705     8935   8056   7239  -1269   -407    -26       N  
ATOM   2908  CA  GLN B 705     -88.582 -18.595 -12.281  1.00 61.01           C  
ANISOU 2908  CA  GLN B 705     8564   7752   6865  -1357   -468     28       C  
ATOM   2909  C   GLN B 705     -89.174 -17.463 -11.444  1.00 58.63           C  
ANISOU 2909  C   GLN B 705     8144   7533   6600  -1324   -479    110       C  
ATOM   2910  O   GLN B 705     -90.315 -17.076 -11.625  1.00 60.87           O  
ANISOU 2910  O   GLN B 705     8372   7907   6848  -1382   -518    166       O  
ATOM   2911  CB  GLN B 705     -88.626 -19.907 -11.481  1.00 57.50           C  
ANISOU 2911  CB  GLN B 705     8189   7215   6444  -1391   -489      6       C  
ATOM   2912  N   ILE B 706     -88.378 -16.902 -10.546  1.00 56.05           N  
ANISOU 2912  N   ILE B 706     7774   7176   6345  -1228   -443    114       N  
ATOM   2913  CA  ILE B 706     -88.880 -15.840  -9.680  1.00 53.30           C  
ANISOU 2913  CA  ILE B 706     7321   6896   6034  -1191   -447    183       C  
ATOM   2914  C   ILE B 706     -89.214 -14.600 -10.484  1.00 50.58           C  
ANISOU 2914  C   ILE B 706     6909   6644   5665  -1179   -442    221       C  
ATOM   2915  O   ILE B 706     -90.268 -13.989 -10.297  1.00 50.01           O  
ANISOU 2915  O   ILE B 706     6761   6655   5583  -1204   -470    285       O  
ATOM   2916  CB  ILE B 706     -87.882 -15.523  -8.554  1.00 51.43           C  
ANISOU 2916  CB  ILE B 706     7063   6603   5876  -1093   -413    173       C  
ATOM   2917  CG1 ILE B 706     -87.893 -16.691  -7.573  1.00 51.62           C  
ANISOU 2917  CG1 ILE B 706     7141   6552   5921  -1115   -433    162       C  
ATOM   2918  CG2 ILE B 706     -88.260 -14.234  -7.830  1.00 48.46           C  
ANISOU 2918  CG2 ILE B 706     6582   6297   5535  -1045   -407    233       C  
ATOM   2919  CD1 ILE B 706     -86.694 -16.728  -6.652  1.00 50.34           C  
ANISOU 2919  CD1 ILE B 706     6989   6312   5828  -1025   -406    135       C  
ATOM   2920  N   GLN B 707     -88.336 -14.257 -11.411  1.00 51.98           N  
ANISOU 2920  N   GLN B 707     7115   6806   5829  -1143   -406    182       N  
ATOM   2921  CA  GLN B 707     -88.588 -13.143 -12.311  1.00 54.70           C  
ANISOU 2921  CA  GLN B 707     7411   7231   6142  -1137   -402    218       C  
ATOM   2922  C   GLN B 707     -89.907 -13.345 -13.071  1.00 51.83           C  
ANISOU 2922  C   GLN B 707     7043   6947   5702  -1236   -459    256       C  
ATOM   2923  O   GLN B 707     -90.683 -12.406 -13.220  1.00 46.92           O  
ANISOU 2923  O   GLN B 707     6344   6411   5072  -1237   -481    321       O  
ATOM   2924  CB  GLN B 707     -87.414 -13.003 -13.268  1.00 58.53           C  
ANISOU 2924  CB  GLN B 707     7947   7680   6613  -1100   -351    162       C  
ATOM   2925  CG  GLN B 707     -87.576 -11.940 -14.335  1.00 63.63           C  
ANISOU 2925  CG  GLN B 707     8561   8400   7214  -1100   -344    197       C  
ATOM   2926  CD  GLN B 707     -86.523 -12.078 -15.414  1.00 65.15           C  
ANISOU 2926  CD  GLN B 707     8822   8559   7373  -1089   -294    135       C  
ATOM   2927  OE1 GLN B 707     -86.499 -13.077 -16.140  1.00 66.42           O  
ANISOU 2927  OE1 GLN B 707     9069   8694   7474  -1146   -300     83       O  
ATOM   2928  NE2 GLN B 707     -85.689 -11.075 -15.566  1.00 64.66           N  
ANISOU 2928  NE2 GLN B 707     8726   8499   7344  -1020   -244    140       N  
ATOM   2929  N   ALA B 708     -90.163 -14.573 -13.525  1.00 50.78           N  
ANISOU 2929  N   ALA B 708     6993   6784   5518  -1318   -486    215       N  
ATOM   2930  CA  ALA B 708     -91.403 -14.877 -14.257  1.00 52.41           C  
ANISOU 2930  CA  ALA B 708     7201   7065   5649  -1423   -548    246       C  
ATOM   2931  C   ALA B 708     -92.606 -14.781 -13.333  1.00 50.98           C  
ANISOU 2931  C   ALA B 708     6937   6940   5492  -1456   -592    315       C  
ATOM   2932  O   ALA B 708     -93.687 -14.376 -13.748  1.00 51.97           O  
ANISOU 2932  O   ALA B 708     7004   7160   5582  -1507   -638    372       O  
ATOM   2933  CB  ALA B 708     -91.332 -16.265 -14.913  1.00 53.16           C  
ANISOU 2933  CB  ALA B 708     7412   7101   5684  -1506   -564    178       C  
ATOM   2934  N   ALA B 709     -92.416 -15.171 -12.076  1.00 48.35           N  
ANISOU 2934  N   ALA B 709     6599   6553   5221  -1427   -577    311       N  
ATOM   2935  CA  ALA B 709     -93.466 -15.050 -11.066  1.00 48.80           C  
ANISOU 2935  CA  ALA B 709     6575   6662   5306  -1451   -605    374       C  
ATOM   2936  C   ALA B 709     -93.831 -13.578 -10.794  1.00 47.45           C  
ANISOU 2936  C   ALA B 709     6287   6573   5170  -1383   -595    439       C  
ATOM   2937  O   ALA B 709     -95.010 -13.231 -10.675  1.00 48.83           O  
ANISOU 2937  O   ALA B 709     6381   6835   5336  -1421   -630    501       O  
ATOM   2938  CB  ALA B 709     -93.044 -15.748  -9.791  1.00 48.56           C  
ANISOU 2938  CB  ALA B 709     6574   6549   5328  -1428   -586    353       C  
ATOM   2939  N   TYR B 710     -92.828 -12.709 -10.746  1.00 46.96           N  
ANISOU 2939  N   TYR B 710     6213   6482   5146  -1285   -546    425       N  
ATOM   2940  CA  TYR B 710     -93.075 -11.268 -10.629  1.00 48.48           C  
ANISOU 2940  CA  TYR B 710     6308   6741   5370  -1219   -534    481       C  
ATOM   2941  C   TYR B 710     -93.954 -10.786 -11.759  1.00 47.63           C  
ANISOU 2941  C   TYR B 710     6164   6725   5207  -1266   -575    528       C  
ATOM   2942  O   TYR B 710     -94.921 -10.060 -11.530  1.00 48.66           O  
ANISOU 2942  O   TYR B 710     6201   6936   5352  -1261   -598    595       O  
ATOM   2943  CB  TYR B 710     -91.770 -10.459 -10.647  1.00 47.65           C  
ANISOU 2943  CB  TYR B 710     6213   6586   5308  -1120   -477    452       C  
ATOM   2944  CG  TYR B 710     -91.048 -10.323  -9.331  1.00 45.91           C  
ANISOU 2944  CG  TYR B 710     5979   6304   5159  -1047   -439    434       C  
ATOM   2945  CD1 TYR B 710     -91.652  -9.734  -8.231  1.00 43.81           C  
ANISOU 2945  CD1 TYR B 710     5635   6073   4937  -1016   -439    479       C  
ATOM   2946  CD2 TYR B 710     -89.728 -10.731  -9.215  1.00 47.76           C  
ANISOU 2946  CD2 TYR B 710     6279   6449   5418  -1004   -403    370       C  
ATOM   2947  CE1 TYR B 710     -90.980  -9.591  -7.048  1.00 44.01           C  
ANISOU 2947  CE1 TYR B 710     5655   6046   5019   -953   -408    460       C  
ATOM   2948  CE2 TYR B 710     -89.046 -10.609  -8.025  1.00 44.39           C  
ANISOU 2948  CE2 TYR B 710     5841   5970   5055   -939   -376    355       C  
ATOM   2949  CZ  TYR B 710     -89.676 -10.039  -6.955  1.00 44.80           C  
ANISOU 2949  CZ  TYR B 710     5822   6058   5140   -917   -381    400       C  
ATOM   2950  OH  TYR B 710     -88.999  -9.890  -5.788  1.00 44.81           O  
ANISOU 2950  OH  TYR B 710     5817   6011   5197   -856   -357    384       O  
ATOM   2951  N   SER B 711     -93.597 -11.172 -12.982  1.00 49.59           N  
ANISOU 2951  N   SER B 711     6487   6963   5392  -1307   -584    493       N  
ATOM   2952  CA  SER B 711     -94.346 -10.753 -14.155  1.00 53.42           C  
ANISOU 2952  CA  SER B 711     6949   7534   5812  -1356   -628    536       C  
ATOM   2953  C   SER B 711     -95.781 -11.192 -14.057  1.00 49.99           C  
ANISOU 2953  C   SER B 711     6466   7175   5352  -1443   -695    583       C  
ATOM   2954  O   SER B 711     -96.660 -10.406 -14.327  1.00 49.95           O  
ANISOU 2954  O   SER B 711     6376   7260   5342  -1445   -729    652       O  
ATOM   2955  CB  SER B 711     -93.736 -11.305 -15.452  1.00 55.50           C  
ANISOU 2955  CB  SER B 711     7318   7771   5999  -1400   -627    480       C  
ATOM   2956  OG  SER B 711     -92.455 -10.753 -15.655  1.00 57.87           O  
ANISOU 2956  OG  SER B 711     7649   8016   6322  -1319   -563    445       O  
ATOM   2957  N   ILE B 712     -96.010 -12.439 -13.667  1.00 48.06           N  
ANISOU 2957  N   ILE B 712     6271   6893   5095  -1516   -712    548       N  
ATOM   2958  CA  ILE B 712     -97.368 -12.944 -13.532  1.00 49.68           C  
ANISOU 2958  CA  ILE B 712     6429   7168   5278  -1610   -774    591       C  
ATOM   2959  C   ILE B 712     -98.147 -12.137 -12.524  1.00 49.12           C  
ANISOU 2959  C   ILE B 712     6232   7161   5271  -1565   -771    662       C  
ATOM   2960  O   ILE B 712     -99.284 -11.786 -12.756  1.00 51.77           O  
ANISOU 2960  O   ILE B 712     6482   7594   5593  -1604   -818    724       O  
ATOM   2961  CB  ILE B 712     -97.394 -14.443 -13.182  1.00 51.45           C  
ANISOU 2961  CB  ILE B 712     6737   7326   5485  -1695   -787    541       C  
ATOM   2962  CG1 ILE B 712     -96.943 -15.251 -14.403  1.00 54.03           C  
ANISOU 2962  CG1 ILE B 712     7183   7611   5734  -1760   -803    476       C  
ATOM   2963  CG2 ILE B 712     -98.779 -14.897 -12.726  1.00 52.71           C  
ANISOU 2963  CG2 ILE B 712     6832   7555   5641  -1786   -840    591       C  
ATOM   2964  CD1 ILE B 712     -96.689 -16.705 -14.095  1.00 57.94           C  
ANISOU 2964  CD1 ILE B 712     7782   8012   6220  -1825   -804    413       C  
ATOM   2965  N   LEU B 713     -97.536 -11.819 -11.398  1.00 48.75           N  
ANISOU 2965  N   LEU B 713     6169   7061   5293  -1481   -716    651       N  
ATOM   2966  CA  LEU B 713     -98.201 -10.949 -10.410  1.00 48.59           C  
ANISOU 2966  CA  LEU B 713     6032   7098   5334  -1427   -703    711       C  
ATOM   2967  C   LEU B 713     -98.537  -9.568 -10.970  1.00 46.66           C  
ANISOU 2967  C   LEU B 713     5702   6928   5099  -1367   -709    768       C  
ATOM   2968  O   LEU B 713     -99.561  -8.976 -10.622  1.00 43.96           O  
ANISOU 2968  O   LEU B 713     5252   6667   4783  -1359   -726    831       O  
ATOM   2969  CB  LEU B 713     -97.335 -10.823  -9.140  1.00 49.41           C  
ANISOU 2969  CB  LEU B 713     6149   7124   5502  -1345   -641    681       C  
ATOM   2970  CG  LEU B 713     -97.222 -12.100  -8.299  1.00 49.44           C  
ANISOU 2970  CG  LEU B 713     6216   7064   5507  -1398   -638    645       C  
ATOM   2971  CD1 LEU B 713     -96.336 -11.854  -7.083  1.00 51.53           C  
ANISOU 2971  CD1 LEU B 713     6490   7259   5830  -1310   -583    621       C  
ATOM   2972  CD2 LEU B 713     -98.595 -12.591  -7.885  1.00 47.11           C  
ANISOU 2972  CD2 LEU B 713     5859   6840   5199  -1485   -676    692       C  
ATOM   2973  N   SER B 714     -97.674  -9.061 -11.845  1.00 48.30           N  
ANISOU 2973  N   SER B 714     5958   7106   5288  -1325   -694    747       N  
ATOM   2974  CA  SER B 714     -97.932  -7.791 -12.526  1.00 52.99           C  
ANISOU 2974  CA  SER B 714     6488   7762   5884  -1274   -704    804       C  
ATOM   2975  C   SER B 714     -99.088  -7.931 -13.472  1.00 49.68           C  
ANISOU 2975  C   SER B 714     6031   7439   5405  -1357   -780    855       C  
ATOM   2976  O   SER B 714     -99.908  -7.042 -13.549  1.00 47.99           O  
ANISOU 2976  O   SER B 714     5718   7303   5211  -1329   -804    926       O  
ATOM   2977  CB  SER B 714     -96.712  -7.280 -13.323  1.00 54.15           C  
ANISOU 2977  CB  SER B 714     6704   7855   6016  -1222   -669    772       C  
ATOM   2978  OG  SER B 714     -95.792  -6.696 -12.433  1.00 58.24           O  
ANISOU 2978  OG  SER B 714     7217   8306   6604  -1127   -604    748       O  
ATOM   2979  N   GLU B 715     -99.138  -9.043 -14.204  1.00 53.24           N  
ANISOU 2979  N   GLU B 715     6562   7883   5782  -1458   -818    818       N  
ATOM   2980  CA  GLU B 715    -100.257  -9.313 -15.125  1.00 54.05           C  
ANISOU 2980  CA  GLU B 715     6637   8079   5819  -1554   -899    861       C  
ATOM   2981  C   GLU B 715    -101.543  -9.422 -14.338  1.00 52.58           C  
ANISOU 2981  C   GLU B 715     6341   7968   5671  -1589   -932    915       C  
ATOM   2982  O   GLU B 715    -102.556  -8.924 -14.759  1.00 50.91           O  
ANISOU 2982  O   GLU B 715     6038   7855   5449  -1608   -986    984       O  
ATOM   2983  CB  GLU B 715    -100.025 -10.568 -15.963  1.00 56.45           C  
ANISOU 2983  CB  GLU B 715     7060   8352   6038  -1661   -930    799       C  
ATOM   2984  CG  GLU B 715     -98.878 -10.426 -16.967  1.00 63.18           C  
ANISOU 2984  CG  GLU B 715     8016   9150   6840  -1636   -901    750       C  
ATOM   2985  CD  GLU B 715     -98.618 -11.669 -17.827  1.00 74.62           C  
ANISOU 2985  CD  GLU B 715     9590  10563   8201  -1738   -924    679       C  
ATOM   2986  OE1 GLU B 715     -99.433 -12.619 -17.806  1.00 81.03           O  
ANISOU 2986  OE1 GLU B 715    10408  11397   8980  -1842   -977    675       O  
ATOM   2987  OE2 GLU B 715     -97.591 -11.692 -18.544  1.00 80.35           O  
ANISOU 2987  OE2 GLU B 715    10408  11235   8887  -1717   -887    626       O  
ATOM   2988  N   VAL B 716    -101.496 -10.043 -13.165  1.00 53.36           N  
ANISOU 2988  N   VAL B 716     6442   8022   5813  -1594   -898    887       N  
ATOM   2989  CA  VAL B 716    -102.680 -10.114 -12.311  1.00 56.66           C  
ANISOU 2989  CA  VAL B 716     6749   8509   6268  -1623   -915    938       C  
ATOM   2990  C   VAL B 716    -103.196  -8.713 -11.964  1.00 56.49           C  
ANISOU 2990  C   VAL B 716     6598   8557   6309  -1525   -901   1009       C  
ATOM   2991  O   VAL B 716    -104.378  -8.435 -12.101  1.00 60.30           O  
ANISOU 2991  O   VAL B 716     6974   9142   6797  -1553   -948   1074       O  
ATOM   2992  CB  VAL B 716    -102.393 -10.897 -11.015  1.00 57.60           C  
ANISOU 2992  CB  VAL B 716     6901   8559   6425  -1630   -868    898       C  
ATOM   2993  CG1 VAL B 716    -103.515 -10.706 -10.015  1.00 59.91           C  
ANISOU 2993  CG1 VAL B 716     7070   8928   6766  -1636   -866    954       C  
ATOM   2994  CG2 VAL B 716    -102.199 -12.381 -11.323  1.00 61.18           C  
ANISOU 2994  CG2 VAL B 716     7468   8955   6821  -1743   -895    841       C  
ATOM   2995  N   GLN B 717    -102.297  -7.844 -11.529  1.00 57.76           N  
ANISOU 2995  N   GLN B 717     6768   8659   6519  -1410   -838    994       N  
ATOM   2996  CA  GLN B 717    -102.650  -6.489 -11.139  1.00 62.05           C  
ANISOU 2996  CA  GLN B 717     7202   9246   7126  -1307   -816   1051       C  
ATOM   2997  C   GLN B 717    -103.220  -5.723 -12.334  1.00 64.75           C  
ANISOU 2997  C   GLN B 717     7493   9667   7441  -1304   -874   1115       C  
ATOM   2998  O   GLN B 717    -104.222  -5.038 -12.195  1.00 68.41           O  
ANISOU 2998  O   GLN B 717     7838  10214   7942  -1276   -896   1183       O  
ATOM   2999  CB  GLN B 717    -101.428  -5.746 -10.570  1.00 65.42           C  
ANISOU 2999  CB  GLN B 717     7670   9583   7603  -1194   -740   1014       C  
ATOM   3000  CG  GLN B 717    -101.723  -4.323 -10.106  1.00 67.81           C  
ANISOU 3000  CG  GLN B 717     7872   9916   7977  -1084   -711   1064       C  
ATOM   3001  CD  GLN B 717    -100.620  -3.334 -10.408  1.00 75.45           C  
ANISOU 3001  CD  GLN B 717     8883  10817   8966   -991   -671   1050       C  
ATOM   3002  OE1 GLN B 717     -99.698  -3.160  -9.612  1.00 80.93           O  
ANISOU 3002  OE1 GLN B 717     9616  11433   9699   -933   -611   1003       O  
ATOM   3003  NE2 GLN B 717    -100.734  -2.641 -11.545  1.00 79.25           N  
ANISOU 3003  NE2 GLN B 717     9355  11334   9424   -979   -707   1095       N  
ATOM   3004  N   GLN B 718    -102.591  -5.864 -13.501  1.00 62.93           N  
ANISOU 3004  N   GLN B 718     7353   9411   7145  -1332   -898   1093       N  
ATOM   3005  CA  GLN B 718    -103.096  -5.257 -14.753  1.00 63.48           C  
ANISOU 3005  CA  GLN B 718     7393   9556   7171  -1344   -963   1155       C  
ATOM   3006  C   GLN B 718    -104.487  -5.799 -15.126  1.00 63.10           C  
ANISOU 3006  C   GLN B 718     7271   9617   7088  -1445  -1048   1204       C  
ATOM   3007  O   GLN B 718    -105.380  -5.019 -15.437  1.00 64.63           O  
ANISOU 3007  O   GLN B 718     7359   9898   7299  -1420  -1093   1283       O  
ATOM   3008  CB  GLN B 718    -102.120  -5.453 -15.926  1.00 57.26           C  
ANISOU 3008  CB  GLN B 718     6730   8720   6306  -1370   -967   1114       C  
ATOM   3009  N   ALA B 719    -104.690  -7.114 -15.021  1.00 59.77           N  
ANISOU 3009  N   ALA B 719     6898   9188   6624  -1555  -1070   1160       N  
ATOM   3010  CA  ALA B 719    -106.004  -7.711 -15.304  1.00 61.52           C  
ANISOU 3010  CA  ALA B 719     7049   9512   6815  -1664  -1151   1203       C  
ATOM   3011  C   ALA B 719    -107.062  -7.195 -14.340  1.00 60.63           C  
ANISOU 3011  C   ALA B 719     6780   9474   6784  -1624  -1144   1265       C  
ATOM   3012  O   ALA B 719    -108.159  -6.894 -14.747  1.00 61.55           O  
ANISOU 3012  O   ALA B 719     6790   9697   6899  -1650  -1209   1336       O  
ATOM   3013  CB  ALA B 719    -105.940  -9.231 -15.255  1.00 59.49           C  
ANISOU 3013  CB  ALA B 719     6882   9214   6505  -1789  -1166   1137       C  
ATOM   3014  N   VAL B 720    -106.733  -7.094 -13.061  1.00 62.37           N  
ANISOU 3014  N   VAL B 720     6985   9640   7072  -1560  -1065   1240       N  
ATOM   3015  CA  VAL B 720    -107.664  -6.523 -12.101  1.00 65.23           C  
ANISOU 3015  CA  VAL B 720     7202  10069   7512  -1510  -1044   1293       C  
ATOM   3016  C   VAL B 720    -107.974  -5.075 -12.497  1.00 67.32           C  
ANISOU 3016  C   VAL B 720     7373  10387   7819  -1403  -1055   1363       C  
ATOM   3017  O   VAL B 720    -109.131  -4.692 -12.611  1.00 69.08           O  
ANISOU 3017  O   VAL B 720     7467  10715   8067  -1406  -1100   1435       O  
ATOM   3018  CB  VAL B 720    -107.122  -6.637 -10.652  1.00 69.08           C  
ANISOU 3018  CB  VAL B 720     7708  10482   8056  -1456   -952   1247       C  
ATOM   3019  CG1 VAL B 720    -107.965  -5.813  -9.689  1.00 68.07           C  
ANISOU 3019  CG1 VAL B 720     7434  10419   8009  -1381   -916   1298       C  
ATOM   3020  CG2 VAL B 720    -107.079  -8.106 -10.193  1.00 69.83           C  
ANISOU 3020  CG2 VAL B 720     7876  10540   8116  -1570   -951   1196       C  
ATOM   3021  N   SER B 721    -106.930  -4.283 -12.724  1.00 70.76           N  
ANISOU 3021  N   SER B 721     7875  10748   8265  -1309  -1015   1345       N  
ATOM   3022  CA  SER B 721    -107.060  -2.885 -13.148  1.00 72.22           C  
ANISOU 3022  CA  SER B 721     7994  10960   8488  -1204  -1022   1409       C  
ATOM   3023  C   SER B 721    -107.757  -2.704 -14.497  1.00 71.65           C  
ANISOU 3023  C   SER B 721     7888  10976   8361  -1252  -1120   1476       C  
ATOM   3024  O   SER B 721    -108.667  -1.883 -14.619  1.00 66.69           O  
ANISOU 3024  O   SER B 721     7136  10428   7775  -1203  -1155   1555       O  
ATOM   3025  CB  SER B 721    -105.680  -2.237 -13.218  1.00 71.27           C  
ANISOU 3025  CB  SER B 721     7972  10731   8377  -1117   -961   1367       C  
ATOM   3026  N   ASP B 726    -111.626 -12.126 -15.673  1.00 70.26           N  
ANISOU 3026  N   ASP B 726     7895  11010   7791  -2328  -1495   1306       N  
ATOM   3027  CA  ASP B 726    -112.373 -12.879 -14.653  1.00 71.52           C  
ANISOU 3027  CA  ASP B 726     7991  11193   7992  -2404  -1480   1312       C  
ATOM   3028  C   ASP B 726    -112.043 -14.385 -14.643  1.00 72.88           C  
ANISOU 3028  C   ASP B 726     8303  11280   8107  -2538  -1487   1236       C  
ATOM   3029  O   ASP B 726    -111.532 -14.940 -13.660  1.00 69.43           O  
ANISOU 3029  O   ASP B 726     7927  10754   7701  -2531  -1416   1191       O  
ATOM   3030  CB  ASP B 726    -113.874 -12.658 -14.824  1.00 73.45           C  
ANISOU 3030  CB  ASP B 726     8060  11593   8256  -2463  -1556   1398       C  
ATOM   3031  N   SER B 727    -112.398 -15.047 -15.743  1.00 77.88           N  
ANISOU 3031  N   SER B 727     8987  11947   8658  -2665  -1578   1225       N  
ATOM   3032  CA  SER B 727    -111.837 -16.364 -16.104  1.00 74.42           C  
ANISOU 3032  CA  SER B 727     8719  11408   8149  -2779  -1591   1139       C  
ATOM   3033  C   SER B 727    -110.317 -16.254 -16.296  1.00 69.86           C  
ANISOU 3033  C   SER B 727     8296  10697   7551  -2684  -1524   1065       C  
ATOM   3034  O   SER B 727    -109.583 -17.151 -15.904  1.00 65.10           O  
ANISOU 3034  O   SER B 727     7819   9977   6941  -2711  -1479    992       O  
ATOM   3035  CB  SER B 727    -112.482 -16.908 -17.395  1.00 72.94           C  
ANISOU 3035  CB  SER B 727     8556  11289   7868  -2922  -1706   1141       C  
ATOM   3036  N   GLN B 728    -109.871 -15.152 -16.908  1.00 68.18           N  
ANISOU 3036  N   GLN B 728     8070  10505   7331  -2576  -1519   1086       N  
ATOM   3037  CA  GLN B 728    -108.458 -14.902 -17.188  1.00 67.35           C  
ANISOU 3037  CA  GLN B 728     8094  10289   7208  -2483  -1456   1023       C  
ATOM   3038  C   GLN B 728    -107.634 -14.733 -15.901  1.00 69.81           C  
ANISOU 3038  C   GLN B 728     8420  10504   7601  -2374  -1350    995       C  
ATOM   3039  O   GLN B 728    -106.528 -15.265 -15.778  1.00 64.70           O  
ANISOU 3039  O   GLN B 728     7904   9736   6942  -2354  -1298    918       O  
ATOM   3040  CB  GLN B 728    -108.293 -13.693 -18.134  1.00 64.54           C  
ANISOU 3040  CB  GLN B 728     7706   9989   6827  -2401  -1479   1066       C  
ATOM   3041  CG  GLN B 728    -108.667 -14.050 -19.560  1.00 63.56           C  
ANISOU 3041  CG  GLN B 728     7633   9923   6595  -2511  -1576   1065       C  
ATOM   3042  CD  GLN B 728    -108.576 -12.855 -20.476  1.00 62.09           C  
ANISOU 3042  CD  GLN B 728     7413   9798   6380  -2434  -1603   1119       C  
ATOM   3043  OE1 GLN B 728    -109.299 -11.880 -20.306  1.00 62.48           O  
ANISOU 3043  OE1 GLN B 728     7320   9939   6482  -2373  -1627   1207       O  
ATOM   3044  NE2 GLN B 728    -107.701 -12.931 -21.471  1.00 61.22           N  
ANISOU 3044  NE2 GLN B 728     7437   9637   6187  -2438  -1600   1067       N  
ATOM   3045  N   ILE B 729    -108.198 -14.015 -14.941  1.00 70.22           N  
ANISOU 3045  N   ILE B 729     8335  10612   7735  -2305  -1321   1056       N  
ATOM   3046  CA  ILE B 729    -107.517 -13.773 -13.670  1.00 66.55           C  
ANISOU 3046  CA  ILE B 729     7872  10069   7344  -2203  -1225   1036       C  
ATOM   3047  C   ILE B 729    -107.438 -15.065 -12.824  1.00 63.88           C  
ANISOU 3047  C   ILE B 729     7604   9656   7011  -2286  -1201    989       C  
ATOM   3048  O   ILE B 729    -106.452 -15.299 -12.126  1.00 57.22           O  
ANISOU 3048  O   ILE B 729     6844   8704   6194  -2228  -1134    938       O  
ATOM   3049  CB  ILE B 729    -108.041 -12.517 -12.905  1.00 66.96           C  
ANISOU 3049  CB  ILE B 729     7768  10196   7480  -2091  -1191   1108       C  
ATOM   3050  CG1 ILE B 729    -108.434 -12.850 -11.473  1.00 68.68           C  
ANISOU 3050  CG1 ILE B 729     7928  10409   7759  -2095  -1140   1116       C  
ATOM   3051  CG2 ILE B 729    -109.231 -11.869 -13.590  1.00 71.21           C  
ANISOU 3051  CG2 ILE B 729     8171  10873   8013  -2113  -1266   1191       C  
ATOM   3052  CD1 ILE B 729    -108.822 -11.608 -10.721  1.00 70.36           C  
ANISOU 3052  CD1 ILE B 729     8003  10682   8050  -1976  -1095   1174       C  
ATOM   3053  N   LEU B 730    -108.439 -15.929 -12.938  1.00 64.04           N  
ANISOU 3053  N   LEU B 730     7599   9731   7004  -2424  -1262   1006       N  
ATOM   3054  CA  LEU B 730    -108.323 -17.285 -12.384  1.00 65.71           C  
ANISOU 3054  CA  LEU B 730     7904   9860   7204  -2523  -1251    958       C  
ATOM   3055  C   LEU B 730    -107.120 -18.020 -12.992  1.00 65.42           C  
ANISOU 3055  C   LEU B 730     8052   9692   7115  -2534  -1241    867       C  
ATOM   3056  O   LEU B 730    -106.328 -18.628 -12.276  1.00 60.20           O  
ANISOU 3056  O   LEU B 730     7483   8916   6475  -2512  -1187    817       O  
ATOM   3057  CB  LEU B 730    -109.600 -18.094 -12.630  1.00 64.93           C  
ANISOU 3057  CB  LEU B 730     7753   9842   7074  -2686  -1328    989       C  
ATOM   3058  N   ASP B 731    -106.993 -17.976 -14.318  1.00 68.67           N  
ANISOU 3058  N   ASP B 731     8516  10121   7456  -2566  -1293    846       N  
ATOM   3059  CA  ASP B 731    -105.880 -18.650 -15.000  1.00 69.54           C  
ANISOU 3059  CA  ASP B 731     8798  10114   7511  -2576  -1280    756       C  
ATOM   3060  C   ASP B 731    -104.523 -18.061 -14.591  1.00 68.04           C  
ANISOU 3060  C   ASP B 731     8658   9831   7363  -2425  -1192    719       C  
ATOM   3061  O   ASP B 731    -103.559 -18.802 -14.463  1.00 65.25           O  
ANISOU 3061  O   ASP B 731     8432   9356   7005  -2418  -1154    646       O  
ATOM   3062  CB  ASP B 731    -106.025 -18.629 -16.529  1.00 69.51           C  
ANISOU 3062  CB  ASP B 731     8838  10159   7415  -2639  -1349    743       C  
ATOM   3063  CG  ASP B 731    -104.784 -19.214 -17.250  1.00 69.46           C  
ANISOU 3063  CG  ASP B 731     9009  10032   7352  -2632  -1321    644       C  
ATOM   3064  OD1 ASP B 731    -104.519 -20.429 -17.074  1.00 70.04           O  
ANISOU 3064  OD1 ASP B 731     9193  10009   7410  -2707  -1315    580       O  
ATOM   3065  OD2 ASP B 731    -104.080 -18.470 -17.990  1.00 66.24           O  
ANISOU 3065  OD2 ASP B 731     8629   9625   6916  -2553  -1301    631       O  
ATOM   3066  N   LEU B 732    -104.462 -16.745 -14.379  1.00 63.50           N  
ANISOU 3066  N   LEU B 732     7982   9312   6833  -2307  -1163    770       N  
ATOM   3067  CA  LEU B 732    -103.224 -16.100 -13.967  1.00 62.31           C  
ANISOU 3067  CA  LEU B 732     7867   9082   6727  -2168  -1083    740       C  
ATOM   3068  C   LEU B 732    -102.854 -16.549 -12.567  1.00 62.57           C  
ANISOU 3068  C   LEU B 732     7913   9035   6824  -2135  -1025    722       C  
ATOM   3069  O   LEU B 732    -101.704 -16.880 -12.324  1.00 61.94           O  
ANISOU 3069  O   LEU B 732     7934   8844   6756  -2083   -976    660       O  
ATOM   3070  CB  LEU B 732    -103.314 -14.567 -14.054  1.00 60.69           C  
ANISOU 3070  CB  LEU B 732     7550   8953   6557  -2056  -1069    802       C  
ATOM   3071  CG  LEU B 732    -103.376 -14.028 -15.481  1.00 61.79           C  
ANISOU 3071  CG  LEU B 732     7698   9151   6630  -2067  -1118    817       C  
ATOM   3072  CD1 LEU B 732    -103.759 -12.555 -15.485  1.00 62.30           C  
ANISOU 3072  CD1 LEU B 732     7635   9301   6736  -1970  -1117    896       C  
ATOM   3073  CD2 LEU B 732    -102.079 -14.257 -16.248  1.00 60.19           C  
ANISOU 3073  CD2 LEU B 732     7636   8855   6380  -2041  -1084    740       C  
ATOM   3074  N   SER B 733    -103.832 -16.582 -11.666  1.00 60.04           N  
ANISOU 3074  N   SER B 733     7494   8775   6542  -2168  -1033    776       N  
ATOM   3075  CA  SER B 733    -103.618 -17.126 -10.326  1.00 61.02           C  
ANISOU 3075  CA  SER B 733     7636   8832   6715  -2158   -985    765       C  
ATOM   3076  C   SER B 733    -102.970 -18.514 -10.387  1.00 62.05           C  
ANISOU 3076  C   SER B 733     7921   8841   6815  -2228   -986    692       C  
ATOM   3077  O   SER B 733    -101.995 -18.791  -9.691  1.00 61.54           O  
ANISOU 3077  O   SER B 733     7928   8671   6781  -2166   -934    651       O  
ATOM   3078  CB  SER B 733    -104.949 -17.228  -9.564  1.00 61.96           C  
ANISOU 3078  CB  SER B 733     7638   9044   6859  -2225  -1003    831       C  
ATOM   3079  OG  SER B 733    -104.937 -16.471  -8.378  1.00 62.16           O  
ANISOU 3079  OG  SER B 733     7581   9086   6951  -2128   -943    864       O  
ATOM   3080  N   ASN B 734    -103.549 -19.381 -11.212  1.00 62.21           N  
ANISOU 3080  N   ASN B 734     7988   8875   6775  -2358  -1049    678       N  
ATOM   3081  CA  ASN B 734    -103.091 -20.752 -11.339  1.00 61.16           C  
ANISOU 3081  CA  ASN B 734     8000   8627   6610  -2438  -1057    610       C  
ATOM   3082  C   ASN B 734    -101.739 -20.831 -11.985  1.00 58.37           C  
ANISOU 3082  C   ASN B 734     7770   8171   6238  -2369  -1025    532       C  
ATOM   3083  O   ASN B 734    -100.941 -21.673 -11.614  1.00 60.68           O  
ANISOU 3083  O   ASN B 734     8172   8341   6542  -2362   -996    476       O  
ATOM   3084  CB  ASN B 734    -104.088 -21.590 -12.150  1.00 65.40           C  
ANISOU 3084  CB  ASN B 734     8555   9210   7083  -2601  -1137    612       C  
ATOM   3085  CG  ASN B 734    -105.411 -21.778 -11.432  1.00 66.20           C  
ANISOU 3085  CG  ASN B 734     8546   9399   7207  -2690  -1167    683       C  
ATOM   3086  OD1 ASN B 734    -105.479 -21.746 -10.199  1.00 67.05           O  
ANISOU 3086  OD1 ASN B 734     8610   9494   7371  -2655  -1122    713       O  
ATOM   3087  ND2 ASN B 734    -106.473 -21.972 -12.199  1.00 71.06           N  
ANISOU 3087  ND2 ASN B 734     9114  10110   7776  -2808  -1242    711       N  
ATOM   3088  N   ARG B 735    -101.460 -19.943 -12.930  1.00 58.32           N  
ANISOU 3088  N   ARG B 735     7742   8213   6203  -2313  -1028    531       N  
ATOM   3089  CA  ARG B 735    -100.145 -19.909 -13.550  1.00 61.49           C  
ANISOU 3089  CA  ARG B 735     8248   8527   6588  -2241   -988    459       C  
ATOM   3090  C   ARG B 735     -99.103 -19.580 -12.466  1.00 65.90           C  
ANISOU 3090  C   ARG B 735     8811   9005   7224  -2113   -913    445       C  
ATOM   3091  O   ARG B 735     -98.018 -20.158 -12.435  1.00 62.80           O  
ANISOU 3091  O   ARG B 735     8525   8497   6839  -2076   -875    377       O  
ATOM   3092  CB  ARG B 735    -100.102 -18.879 -14.694  1.00 63.30           C  
ANISOU 3092  CB  ARG B 735     8441   8836   6774  -2203  -1002    475       C  
ATOM   3093  N   PHE B 736     -99.444 -18.661 -11.565  1.00 67.01           N  
ANISOU 3093  N   PHE B 736     8833   9206   7421  -2045   -891    509       N  
ATOM   3094  CA  PHE B 736     -98.541 -18.292 -10.489  1.00 64.99           C  
ANISOU 3094  CA  PHE B 736     8575   8885   7235  -1931   -827    500       C  
ATOM   3095  C   PHE B 736     -98.248 -19.490  -9.595  1.00 65.46           C  
ANISOU 3095  C   PHE B 736     8716   8840   7314  -1965   -816    468       C  
ATOM   3096  O   PHE B 736     -97.093 -19.777  -9.304  1.00 61.62           O  
ANISOU 3096  O   PHE B 736     8308   8249   6854  -1898   -776    416       O  
ATOM   3097  CB  PHE B 736     -99.104 -17.139  -9.644  1.00 63.63           C  
ANISOU 3097  CB  PHE B 736     8262   8800   7114  -1865   -809    572       C  
ATOM   3098  CG  PHE B 736     -98.223 -16.761  -8.492  1.00 62.80           C  
ANISOU 3098  CG  PHE B 736     8155   8631   7074  -1755   -747    562       C  
ATOM   3099  CD1 PHE B 736     -97.151 -15.887  -8.685  1.00 60.78           C  
ANISOU 3099  CD1 PHE B 736     7906   8345   6844  -1642   -704    537       C  
ATOM   3100  CD2 PHE B 736     -98.448 -17.271  -7.235  1.00 60.78           C  
ANISOU 3100  CD2 PHE B 736     7894   8348   6850  -1770   -734    577       C  
ATOM   3101  CE1 PHE B 736     -96.334 -15.531  -7.640  1.00 58.29           C  
ANISOU 3101  CE1 PHE B 736     7587   7973   6586  -1547   -654    526       C  
ATOM   3102  CE2 PHE B 736     -97.626 -16.920  -6.185  1.00 60.26           C  
ANISOU 3102  CE2 PHE B 736     7831   8227   6837  -1673   -683    567       C  
ATOM   3103  CZ  PHE B 736     -96.571 -16.045  -6.391  1.00 56.99           C  
ANISOU 3103  CZ  PHE B 736     7420   7785   6450  -1561   -646    541       C  
ATOM   3104  N   TYR B 737     -99.303 -20.167  -9.152  1.00 62.91           N  
ANISOU 3104  N   TYR B 737     8371   8550   6982  -2070   -852    504       N  
ATOM   3105  CA  TYR B 737     -99.167 -21.310  -8.248  1.00 61.63           C  
ANISOU 3105  CA  TYR B 737     8284   8293   6839  -2114   -846    487       C  
ATOM   3106  C   TYR B 737     -98.466 -22.501  -8.890  1.00 63.12           C  
ANISOU 3106  C   TYR B 737     8626   8362   6996  -2160   -857    409       C  
ATOM   3107  O   TYR B 737     -97.899 -23.333  -8.197  1.00 64.93           O  
ANISOU 3107  O   TYR B 737     8938   8481   7251  -2153   -839    382       O  
ATOM   3108  CB  TYR B 737    -100.526 -21.720  -7.701  1.00 58.65           C  
ANISOU 3108  CB  TYR B 737     7843   7987   6456  -2226   -881    548       C  
ATOM   3109  CG  TYR B 737    -101.095 -20.716  -6.725  1.00 59.06           C  
ANISOU 3109  CG  TYR B 737     7756   8133   6551  -2169   -853    618       C  
ATOM   3110  CD1 TYR B 737    -100.379 -20.354  -5.574  1.00 59.41           C  
ANISOU 3110  CD1 TYR B 737     7797   8130   6647  -2066   -798    620       C  
ATOM   3111  CD2 TYR B 737    -102.341 -20.125  -6.933  1.00 58.21           C  
ANISOU 3111  CD2 TYR B 737     7520   8162   6434  -2216   -882    681       C  
ATOM   3112  CE1 TYR B 737    -100.893 -19.447  -4.656  1.00 58.07           C  
ANISOU 3112  CE1 TYR B 737     7508   8042   6513  -2014   -768    677       C  
ATOM   3113  CE2 TYR B 737    -102.866 -19.213  -6.020  1.00 59.59           C  
ANISOU 3113  CE2 TYR B 737     7569   8420   6652  -2158   -850    741       C  
ATOM   3114  CZ  TYR B 737    -102.134 -18.882  -4.885  1.00 58.73           C  
ANISOU 3114  CZ  TYR B 737     7468   8257   6589  -2059   -790    735       C  
ATOM   3115  OH  TYR B 737    -102.635 -17.993  -3.977  1.00 59.94           O  
ANISOU 3115  OH  TYR B 737     7505   8488   6781  -2002   -755    787       O  
ATOM   3116  N   THR B 738     -98.466 -22.553 -10.212  1.00 63.82           N  
ANISOU 3116  N   THR B 738     8754   8467   7028  -2199   -884    372       N  
ATOM   3117  CA  THR B 738     -97.704 -23.554 -10.938  1.00 69.25           C  
ANISOU 3117  CA  THR B 738     9588   9041   7684  -2227   -885    288       C  
ATOM   3118  C   THR B 738     -96.223 -23.215 -10.924  1.00 66.99           C  
ANISOU 3118  C   THR B 738     9350   8671   7433  -2092   -823    234       C  
ATOM   3119  O   THR B 738     -95.398 -24.103 -10.799  1.00 65.91           O  
ANISOU 3119  O   THR B 738     9322   8410   7310  -2077   -803    174       O  
ATOM   3120  CB  THR B 738     -98.195 -23.661 -12.401  1.00 73.35           C  
ANISOU 3120  CB  THR B 738    10134   9615   8121  -2316   -932    264       C  
ATOM   3121  OG1 THR B 738     -99.542 -24.145 -12.402  1.00 76.73           O  
ANISOU 3121  OG1 THR B 738    10525  10111   8518  -2454   -995    308       O  
ATOM   3122  CG2 THR B 738     -97.321 -24.607 -13.230  1.00 72.19           C  
ANISOU 3122  CG2 THR B 738    10143   9350   7936  -2333   -922    165       C  
ATOM   3123  N   LEU B 739     -95.892 -21.937 -11.086  1.00 67.79           N  
ANISOU 3123  N   LEU B 739     9368   8840   7550  -1995   -794    256       N  
ATOM   3124  CA  LEU B 739     -94.502 -21.494 -11.052  1.00 72.50           C  
ANISOU 3124  CA  LEU B 739     9993   9369   8184  -1868   -734    211       C  
ATOM   3125  C   LEU B 739     -93.954 -21.592  -9.636  1.00 69.28           C  
ANISOU 3125  C   LEU B 739     9578   8895   7852  -1794   -702    223       C  
ATOM   3126  O   LEU B 739     -92.808 -21.936  -9.441  1.00 67.94           O  
ANISOU 3126  O   LEU B 739     9475   8623   7715  -1724   -667    171       O  
ATOM   3127  CB  LEU B 739     -94.368 -20.047 -11.525  1.00 72.57           C  
ANISOU 3127  CB  LEU B 739     9910   9469   8193  -1791   -714    241       C  
ATOM   3128  CG  LEU B 739     -93.257 -19.701 -12.494  1.00 74.48           C  
ANISOU 3128  CG  LEU B 739    10203   9678   8418  -1726   -674    182       C  
ATOM   3129  CD1 LEU B 739     -93.254 -20.565 -13.740  1.00 78.47           C  
ANISOU 3129  CD1 LEU B 739    10815  10154   8846  -1809   -695    120       C  
ATOM   3130  CD2 LEU B 739     -93.415 -18.238 -12.875  1.00 74.80           C  
ANISOU 3130  CD2 LEU B 739    10142   9821   8456  -1670   -665    232       C  
ATOM   3131  N   ILE B 740     -94.773 -21.236  -8.662  1.00 66.14           N  
ANISOU 3131  N   ILE B 740     9091   8560   7479  -1808   -714    293       N  
ATOM   3132  CA  ILE B 740     -94.363 -21.260  -7.277  1.00 65.49           C  
ANISOU 3132  CA  ILE B 740     8997   8429   7457  -1745   -687    312       C  
ATOM   3133  C   ILE B 740     -95.348 -22.177  -6.522  1.00 64.58           C  
ANISOU 3133  C   ILE B 740     8893   8311   7334  -1850   -721    351       C  
ATOM   3134  O   ILE B 740     -96.384 -21.729  -6.030  1.00 55.40           O  
ANISOU 3134  O   ILE B 740     7635   7245   6170  -1887   -733    416       O  
ATOM   3135  CB  ILE B 740     -94.351 -19.851  -6.665  1.00 63.44           C  
ANISOU 3135  CB  ILE B 740     8619   8248   7236  -1652   -657    360       C  
ATOM   3136  CG1 ILE B 740     -93.638 -18.850  -7.585  1.00 63.10           C  
ANISOU 3136  CG1 ILE B 740     8553   8230   7192  -1572   -630    334       C  
ATOM   3137  CG2 ILE B 740     -93.684 -19.893  -5.307  1.00 66.78           C  
ANISOU 3137  CG2 ILE B 740     9048   8608   7716  -1578   -627    364       C  
ATOM   3138  CD1 ILE B 740     -92.138 -19.032  -7.686  1.00 62.55           C  
ANISOU 3138  CD1 ILE B 740     8558   8055   7152  -1486   -591    267       C  
ATOM   3139  N   PRO B 741     -95.031 -23.476  -6.460  1.00 67.44           N  
ANISOU 3139  N   PRO B 741     9372   8560   7690  -1900   -734    310       N  
ATOM   3140  CA  PRO B 741     -95.950 -24.442  -5.860  1.00 71.24           C  
ANISOU 3140  CA  PRO B 741     9879   9029   8159  -2014   -768    345       C  
ATOM   3141  C   PRO B 741     -96.159 -24.194  -4.379  1.00 70.89           C  
ANISOU 3141  C   PRO B 741     9777   9003   8155  -1983   -749    405       C  
ATOM   3142  O   PRO B 741     -95.196 -23.986  -3.646  1.00 73.95           O  
ANISOU 3142  O   PRO B 741    10181   9331   8587  -1881   -717    394       O  
ATOM   3143  CB  PRO B 741     -95.287 -25.804  -6.098  1.00 71.27           C  
ANISOU 3143  CB  PRO B 741    10034   8885   8160  -2046   -777    281       C  
ATOM   3144  CG  PRO B 741     -94.054 -25.553  -6.886  1.00 73.20           C  
ANISOU 3144  CG  PRO B 741    10327   9073   8413  -1949   -746    209       C  
ATOM   3145  CD  PRO B 741     -93.787 -24.088  -6.955  1.00 70.41           C  
ANISOU 3145  CD  PRO B 741     9863   8813   8075  -1850   -715    231       C  
ATOM   3146  N   HIS B 742     -97.425 -24.191  -3.975  1.00 70.55           N  
ANISOU 3146  N   HIS B 742     9662   9048   8095  -2073   -770    468       N  
ATOM   3147  CA  HIS B 742     -97.816 -23.986  -2.594  1.00 73.03           C  
ANISOU 3147  CA  HIS B 742     9918   9395   8436  -2063   -750    529       C  
ATOM   3148  C   HIS B 742     -98.511 -25.231  -2.042  1.00 77.71           C  
ANISOU 3148  C   HIS B 742    10570   9944   9012  -2188   -777    556       C  
ATOM   3149  O   HIS B 742     -98.852 -26.135  -2.789  1.00 75.70           O  
ANISOU 3149  O   HIS B 742    10383   9652   8726  -2291   -815    532       O  
ATOM   3150  CB  HIS B 742     -98.780 -22.811  -2.516  1.00 72.74           C  
ANISOU 3150  CB  HIS B 742     9730   9511   8397  -2056   -741    586       C  
ATOM   3151  CG  HIS B 742     -98.118 -21.475  -2.574  1.00 72.37           C  
ANISOU 3151  CG  HIS B 742     9616   9502   8379  -1921   -705    577       C  
ATOM   3152  ND1 HIS B 742     -97.427 -21.030  -3.684  1.00 75.25           N  
ANISOU 3152  ND1 HIS B 742    10000   9854   8738  -1866   -705    530       N  
ATOM   3153  CD2 HIS B 742     -98.064 -20.474  -1.666  1.00 69.77           C  
ANISOU 3153  CD2 HIS B 742     9202   9224   8083  -1835   -666    609       C  
ATOM   3154  CE1 HIS B 742     -96.976 -19.809  -3.451  1.00 76.63           C  
ANISOU 3154  CE1 HIS B 742    10103  10068   8945  -1754   -669    537       C  
ATOM   3155  NE2 HIS B 742     -97.353 -19.450  -2.236  1.00 73.64           N  
ANISOU 3155  NE2 HIS B 742     9663   9727   8592  -1733   -646    583       N  
ATOM   3156  N   ASP B 743     -98.748 -25.240  -0.734  1.00 80.48           N  
ANISOU 3156  N   ASP B 743    10893  10305   9381  -2184   -756    607       N  
ATOM   3157  CA  ASP B 743     -99.502 -26.320  -0.069  1.00 82.38           C  
ANISOU 3157  CA  ASP B 743    11177  10519   9606  -2307   -775    648       C  
ATOM   3158  C   ASP B 743    -100.983 -25.994  -0.054  1.00 82.93           C  
ANISOU 3158  C   ASP B 743    11126  10731   9653  -2406   -784    708       C  
ATOM   3159  O   ASP B 743    -101.341 -24.935   0.435  1.00 84.16           O  
ANISOU 3159  O   ASP B 743    11162  10992   9822  -2349   -752    746       O  
ATOM   3160  CB  ASP B 743     -99.051 -26.499   1.380  1.00 75.71           C  
ANISOU 3160  CB  ASP B 743    10363   9619   8784  -2259   -746    679       C  
ATOM   3161  N   PRO B 750    -106.749 -19.865  -3.012  1.00 74.24           N  
ANISOU 3161  N   PRO B 750     9116  10539   8554  -2399   -832    945       N  
ATOM   3162  CA  PRO B 750    -106.567 -18.461  -2.592  1.00 73.00           C  
ANISOU 3162  CA  PRO B 750     8862  10437   8438  -2256   -782    963       C  
ATOM   3163  C   PRO B 750    -106.378 -17.586  -3.839  1.00 74.28           C  
ANISOU 3163  C   PRO B 750     8991  10636   8594  -2195   -813    953       C  
ATOM   3164  O   PRO B 750    -105.280 -17.511  -4.415  1.00 74.19           O  
ANISOU 3164  O   PRO B 750     9076  10540   8573  -2135   -814    901       O  
ATOM   3165  CB  PRO B 750    -105.350 -18.488  -1.633  1.00 71.07           C  
ANISOU 3165  CB  PRO B 750     8711  10079   8214  -2162   -725    925       C  
ATOM   3166  CG  PRO B 750    -104.904 -19.911  -1.560  1.00 73.07           C  
ANISOU 3166  CG  PRO B 750     9107  10217   8438  -2251   -747    891       C  
ATOM   3167  CD  PRO B 750    -105.684 -20.756  -2.530  1.00 73.17           C  
ANISOU 3167  CD  PRO B 750     9134  10256   8412  -2394   -813    895       C  
ATOM   3168  N   LEU B 751    -107.493 -17.016  -4.300  1.00 71.10           N  
ANISOU 3168  N   LEU B 751     8456  10363   8195  -2223   -844   1006       N  
ATOM   3169  CA  LEU B 751    -107.543 -16.346  -5.592  1.00 70.76           C  
ANISOU 3169  CA  LEU B 751     8381  10369   8136  -2197   -891   1009       C  
ATOM   3170  C   LEU B 751    -106.798 -15.024  -5.507  1.00 69.80           C  
ANISOU 3170  C   LEU B 751     8232  10238   8053  -2036   -844   1004       C  
ATOM   3171  O   LEU B 751    -107.013 -14.245  -4.577  1.00 66.86           O  
ANISOU 3171  O   LEU B 751     7773   9904   7728  -1957   -791   1033       O  
ATOM   3172  CB  LEU B 751    -108.991 -16.111  -6.048  1.00 70.53           C  
ANISOU 3172  CB  LEU B 751     8209  10485   8104  -2271   -943   1075       C  
ATOM   3173  N   LEU B 752    -105.909 -14.789  -6.468  1.00 64.15           N  
ANISOU 3173  N   LEU B 752     7594   9466   7313  -1992   -861    964       N  
ATOM   3174  CA  LEU B 752    -105.136 -13.556  -6.511  1.00 63.99           C  
ANISOU 3174  CA  LEU B 752     7558   9429   7326  -1848   -820    957       C  
ATOM   3175  C   LEU B 752    -105.868 -12.505  -7.349  1.00 64.58           C  
ANISOU 3175  C   LEU B 752     7518   9613   7405  -1818   -856   1011       C  
ATOM   3176  O   LEU B 752    -105.602 -12.327  -8.530  1.00 66.16           O  
ANISOU 3176  O   LEU B 752     7756   9815   7569  -1822   -898   1003       O  
ATOM   3177  CB  LEU B 752    -103.740 -13.829  -7.064  1.00 62.92           C  
ANISOU 3177  CB  LEU B 752     7564   9176   7166  -1813   -812    887       C  
ATOM   3178  CG  LEU B 752    -102.940 -14.862  -6.257  1.00 63.04           C  
ANISOU 3178  CG  LEU B 752     7694   9076   7183  -1831   -780    835       C  
ATOM   3179  CD1 LEU B 752    -101.641 -15.193  -6.966  1.00 64.73           C  
ANISOU 3179  CD1 LEU B 752     8039   9183   7374  -1803   -777    765       C  
ATOM   3180  CD2 LEU B 752    -102.681 -14.394  -4.834  1.00 59.08           C  
ANISOU 3180  CD2 LEU B 752     7156   8555   6735  -1747   -715    844       C  
ATOM   3181  N   ASN B 753    -106.810 -11.819  -6.721  1.00 69.26           N  
ANISOU 3181  N   ASN B 753     7974  10299   8044  -1787   -840   1070       N  
ATOM   3182  CA  ASN B 753    -107.737 -10.913  -7.415  1.00 74.33           C  
ANISOU 3182  CA  ASN B 753     8487  11056   8697  -1767   -881   1134       C  
ATOM   3183  C   ASN B 753    -107.861  -9.548  -6.743  1.00 73.63           C  
ANISOU 3183  C   ASN B 753     8293  11004   8679  -1632   -825   1168       C  
ATOM   3184  O   ASN B 753    -108.775  -8.784  -7.028  1.00 78.86           O  
ANISOU 3184  O   ASN B 753     8829  11766   9368  -1606   -849   1229       O  
ATOM   3185  CB  ASN B 753    -109.125 -11.592  -7.561  1.00 75.22           C  
ANISOU 3185  CB  ASN B 753     8514  11274   8793  -1896   -939   1181       C  
ATOM   3186  CG  ASN B 753    -109.756 -11.999  -6.244  1.00 76.01           C  
ANISOU 3186  CG  ASN B 753     8552  11401   8927  -1929   -892   1197       C  
ATOM   3187  OD1 ASN B 753    -109.299 -11.610  -5.175  1.00 79.31           O  
ANISOU 3187  OD1 ASN B 753     8973  11776   9385  -1844   -816   1182       O  
ATOM   3188  ND2 ASN B 753    -110.801 -12.840  -6.313  1.00 76.35           N  
ANISOU 3188  ND2 ASN B 753     8545  11514   8949  -2062   -937   1227       N  
ATOM   3189  N   ASN B 754    -106.939  -9.245  -5.846  1.00 72.42           N  
ANISOU 3189  N   ASN B 754     8192  10766   8556  -1545   -753   1128       N  
ATOM   3190  CA  ASN B 754    -106.981  -7.991  -5.118  1.00 73.48           C  
ANISOU 3190  CA  ASN B 754     8242  10922   8757  -1418   -694   1150       C  
ATOM   3191  C   ASN B 754    -105.565  -7.577  -4.744  1.00 66.87           C  
ANISOU 3191  C   ASN B 754     7503   9970   7934  -1323   -640   1093       C  
ATOM   3192  O   ASN B 754    -104.646  -8.387  -4.744  1.00 66.13           O  
ANISOU 3192  O   ASN B 754     7532   9786   7809  -1356   -637   1039       O  
ATOM   3193  CB  ASN B 754    -107.884  -8.113  -3.874  1.00 72.15           C  
ANISOU 3193  CB  ASN B 754     7980  10814   8622  -1433   -651   1176       C  
ATOM   3194  CG  ASN B 754    -107.340  -9.093  -2.853  1.00 71.13           C  
ANISOU 3194  CG  ASN B 754     7944  10608   8475  -1477   -610   1129       C  
ATOM   3195  OD1 ASN B 754    -106.527  -8.734  -1.995  1.00 73.08           O  
ANISOU 3195  OD1 ASN B 754     8237  10786   8745  -1396   -549   1094       O  
ATOM   3196  ND2 ASN B 754    -107.769 -10.338  -2.949  1.00 71.54           N  
ANISOU 3196  ND2 ASN B 754     8029  10669   8485  -1608   -647   1130       N  
ATOM   3197  N   ALA B 755    -105.419  -6.316  -4.383  1.00 66.31           N  
ANISOU 3197  N   ALA B 755     7375   9903   7917  -1203   -596   1106       N  
ATOM   3198  CA  ALA B 755    -104.127  -5.734  -4.099  1.00 63.20           C  
ANISOU 3198  CA  ALA B 755     7059   9410   7544  -1108   -549   1059       C  
ATOM   3199  C   ALA B 755    -103.429  -6.394  -2.895  1.00 65.86           C  
ANISOU 3199  C   ALA B 755     7472   9671   7880  -1113   -499   1006       C  
ATOM   3200  O   ALA B 755    -102.233  -6.685  -2.957  1.00 59.37           O  
ANISOU 3200  O   ALA B 755     6759   8754   7046  -1098   -490    954       O  
ATOM   3201  CB  ALA B 755    -104.285  -4.236  -3.880  1.00 61.60           C  
ANISOU 3201  CB  ALA B 755     6769   9232   7402   -987   -513   1088       C  
ATOM   3202  N   ASP B 756    -104.170  -6.636  -1.817  1.00 69.87           N  
ANISOU 3202  N   ASP B 756     7922  10223   8402  -1134   -468   1022       N  
ATOM   3203  CA  ASP B 756    -103.593  -7.245  -0.609  1.00 74.65           C  
ANISOU 3203  CA  ASP B 756     8597  10763   9001  -1140   -423    981       C  
ATOM   3204  C   ASP B 756    -102.986  -8.631  -0.854  1.00 68.56           C  
ANISOU 3204  C   ASP B 756     7948   9921   8181  -1232   -457    945       C  
ATOM   3205  O   ASP B 756    -101.850  -8.916  -0.428  1.00 70.96           O  
ANISOU 3205  O   ASP B 756     8351  10129   8483  -1203   -436    895       O  
ATOM   3206  CB  ASP B 756    -104.635  -7.236   0.548  1.00 83.38           C  
ANISOU 3206  CB  ASP B 756     9612  11945  10124  -1154   -382   1012       C  
ATOM   3207  CG  ASP B 756    -104.617  -5.903   1.294  1.00 89.41           C  
ANISOU 3207  CG  ASP B 756    10310  12722  10941  -1031   -319   1013       C  
ATOM   3208  OD1 ASP B 756    -103.622  -5.695   2.012  1.00 92.04           O  
ANISOU 3208  OD1 ASP B 756    10715  12976  11280   -973   -280    967       O  
ATOM   3209  OD2 ASP B 756    -105.531  -5.051   1.140  1.00 94.31           O  
ANISOU 3209  OD2 ASP B 756    10812  13426  11597   -989   -311   1056       O  
ATOM   3210  N   SER B 757    -103.716  -9.466  -1.584  1.00 66.80           N  
ANISOU 3210  N   SER B 757     7718   9742   7922  -1340   -511    968       N  
ATOM   3211  CA  SER B 757    -103.239 -10.803  -1.934  1.00 63.11           C  
ANISOU 3211  CA  SER B 757     7367   9205   7408  -1433   -547    933       C  
ATOM   3212  C   SER B 757    -101.991 -10.766  -2.846  1.00 56.77           C  
ANISOU 3212  C   SER B 757     6666   8314   6591  -1394   -562    883       C  
ATOM   3213  O   SER B 757    -101.012 -11.512  -2.645  1.00 52.95           O  
ANISOU 3213  O   SER B 757     6294   7731   6094  -1402   -555    833       O  
ATOM   3214  CB  SER B 757    -104.430 -11.550  -2.561  1.00 69.79           C  
ANISOU 3214  CB  SER B 757     8168  10129   8219  -1558   -604    971       C  
ATOM   3215  OG  SER B 757    -104.794 -10.968  -3.815  1.00 72.73           O  
ANISOU 3215  OG  SER B 757     8490  10561   8584  -1553   -650    996       O  
ATOM   3216  N   VAL B 758    -101.974  -9.820  -3.780  1.00 55.33           N  
ANISOU 3216  N   VAL B 758     6441   8165   6416  -1343   -577    898       N  
ATOM   3217  CA  VAL B 758    -100.845  -9.672  -4.693  1.00 52.95           C  
ANISOU 3217  CA  VAL B 758     6225   7792   6100  -1306   -584    856       C  
ATOM   3218  C   VAL B 758     -99.609  -9.213  -3.936  1.00 52.46           C  
ANISOU 3218  C   VAL B 758     6213   7644   6077  -1207   -529    813       C  
ATOM   3219  O   VAL B 758     -98.526  -9.794  -4.087  1.00 54.36           O  
ANISOU 3219  O   VAL B 758     6556   7794   6304  -1206   -524    759       O  
ATOM   3220  CB  VAL B 758    -101.172  -8.688  -5.824  1.00 54.05           C  
ANISOU 3220  CB  VAL B 758     6305   7995   6238  -1274   -612    892       C  
ATOM   3221  CG1 VAL B 758     -99.944  -8.366  -6.650  1.00 50.13           C  
ANISOU 3221  CG1 VAL B 758     5890   7426   5730  -1224   -605    851       C  
ATOM   3222  CG2 VAL B 758    -102.255  -9.277  -6.736  1.00 56.30           C  
ANISOU 3222  CG2 VAL B 758     6557   8359   6475  -1382   -681    929       C  
ATOM   3223  N   GLN B 759     -99.790  -8.173  -3.129  1.00 53.51           N  
ANISOU 3223  N   GLN B 759     6269   7805   6257  -1125   -487    834       N  
ATOM   3224  CA  GLN B 759     -98.732  -7.596  -2.286  1.00 57.91           C  
ANISOU 3224  CA  GLN B 759     6859   8292   6854  -1031   -435    797       C  
ATOM   3225  C   GLN B 759     -98.038  -8.646  -1.436  1.00 58.67           C  
ANISOU 3225  C   GLN B 759     7044   8309   6938  -1059   -423    754       C  
ATOM   3226  O   GLN B 759     -96.803  -8.704  -1.384  1.00 58.67           O  
ANISOU 3226  O   GLN B 759     7120   8223   6948  -1015   -409    706       O  
ATOM   3227  CB  GLN B 759     -99.358  -6.593  -1.292  1.00 60.05           C  
ANISOU 3227  CB  GLN B 759     7032   8617   7169   -965   -393    828       C  
ATOM   3228  CG  GLN B 759     -99.494  -5.187  -1.819  1.00 61.56           C  
ANISOU 3228  CG  GLN B 759     7152   8842   7396   -882   -383    855       C  
ATOM   3229  CD  GLN B 759    -100.443  -4.330  -0.980  1.00 64.33           C  
ANISOU 3229  CD  GLN B 759     7394   9262   7786   -832   -348    892       C  
ATOM   3230  OE1 GLN B 759    -101.438  -3.683  -1.445  1.00 66.89           O  
ANISOU 3230  OE1 GLN B 759     7621   9667   8128   -820   -362    944       O  
ATOM   3231  NE2 GLN B 759    -100.102  -4.289   0.282  1.00 61.62           N  
ANISOU 3231  NE2 GLN B 759     7067   8885   7460   -798   -301    863       N  
ATOM   3232  N   ALA B 760     -98.843  -9.474  -0.771  1.00 54.09           N  
ANISOU 3232  N   ALA B 760     6453   7760   6339  -1132   -430    774       N  
ATOM   3233  CA  ALA B 760     -98.294 -10.538   0.047  1.00 52.25           C  
ANISOU 3233  CA  ALA B 760     6308   7454   6092  -1167   -425    743       C  
ATOM   3234  C   ALA B 760     -97.410 -11.481  -0.766  1.00 51.78           C  
ANISOU 3234  C   ALA B 760     6359   7309   6007  -1203   -456    699       C  
ATOM   3235  O   ALA B 760     -96.360 -11.938  -0.271  1.00 51.10           O  
ANISOU 3235  O   ALA B 760     6354   7132   5928  -1176   -445    657       O  
ATOM   3236  CB  ALA B 760     -99.408 -11.316   0.728  1.00 52.94           C  
ANISOU 3236  CB  ALA B 760     6365   7593   6156  -1256   -431    780       C  
ATOM   3237  N   LYS B 761     -97.820 -11.785  -1.997  1.00 49.10           N  
ANISOU 3237  N   LYS B 761     6023   6998   5637  -1264   -497    706       N  
ATOM   3238  CA  LYS B 761     -97.002 -12.636  -2.855  1.00 49.38           C  
ANISOU 3238  CA  LYS B 761     6164   6955   5645  -1296   -521    657       C  
ATOM   3239  C   LYS B 761     -95.728 -11.978  -3.351  1.00 44.75           C  
ANISOU 3239  C   LYS B 761     5613   6310   5079  -1206   -498    615       C  
ATOM   3240  O   LYS B 761     -94.690 -12.649  -3.484  1.00 44.47           O  
ANISOU 3240  O   LYS B 761     5670   6184   5042  -1198   -495    564       O  
ATOM   3241  CB  LYS B 761     -97.826 -13.214  -4.022  1.00 55.61           C  
ANISOU 3241  CB  LYS B 761     6955   7791   6385  -1397   -573    672       C  
ATOM   3242  CG  LYS B 761     -98.939 -14.134  -3.547  1.00 58.82           C  
ANISOU 3242  CG  LYS B 761     7345   8236   6769  -1504   -599    705       C  
ATOM   3243  CD  LYS B 761     -98.369 -15.281  -2.722  1.00 62.61           C  
ANISOU 3243  CD  LYS B 761     7923   8618   7247  -1533   -591    673       C  
ATOM   3244  CE  LYS B 761     -99.443 -16.204  -2.188  1.00 65.30           C  
ANISOU 3244  CE  LYS B 761     8253   8991   7566  -1645   -612    709       C  
ATOM   3245  NZ  LYS B 761     -99.047 -16.624  -0.818  1.00 66.75           N  
ANISOU 3245  NZ  LYS B 761     8478   9116   7769  -1626   -581    707       N  
ATOM   3246  N   VAL B 762     -95.783 -10.679  -3.609  1.00 43.64           N  
ANISOU 3246  N   VAL B 762     5399   6218   4963  -1136   -480    637       N  
ATOM   3247  CA  VAL B 762     -94.585  -9.955  -4.048  1.00 46.36           C  
ANISOU 3247  CA  VAL B 762     5771   6513   5332  -1053   -454    602       C  
ATOM   3248  C   VAL B 762     -93.551  -9.973  -2.936  1.00 47.33           C  
ANISOU 3248  C   VAL B 762     5930   6558   5494   -989   -419    565       C  
ATOM   3249  O   VAL B 762     -92.364 -10.229  -3.167  1.00 48.12           O  
ANISOU 3249  O   VAL B 762     6098   6581   5604   -958   -408    516       O  
ATOM   3250  CB  VAL B 762     -94.909  -8.498  -4.425  1.00 47.22           C  
ANISOU 3250  CB  VAL B 762     5793   6686   5465   -991   -441    640       C  
ATOM   3251  CG1 VAL B 762     -93.634  -7.717  -4.695  1.00 46.69           C  
ANISOU 3251  CG1 VAL B 762     5752   6561   5428   -907   -408    605       C  
ATOM   3252  CG2 VAL B 762     -95.808  -8.448  -5.664  1.00 45.70           C  
ANISOU 3252  CG2 VAL B 762     5568   6566   5228  -1050   -484    678       C  
ATOM   3253  N   GLU B 763     -94.024  -9.683  -1.734  1.00 48.25           N  
ANISOU 3253  N   GLU B 763     5999   6701   5633   -970   -402    590       N  
ATOM   3254  CA  GLU B 763     -93.198  -9.711  -0.547  1.00 51.31           C  
ANISOU 3254  CA  GLU B 763     6417   7027   6050   -918   -376    562       C  
ATOM   3255  C   GLU B 763     -92.523 -11.057  -0.406  1.00 50.33           C  
ANISOU 3255  C   GLU B 763     6393   6820   5910   -957   -394    525       C  
ATOM   3256  O   GLU B 763     -91.300 -11.168  -0.123  1.00 44.57           O  
ANISOU 3256  O   GLU B 763     5716   6012   5206   -905   -383    483       O  
ATOM   3257  CB  GLU B 763     -94.140  -9.505   0.638  1.00 57.09           C  
ANISOU 3257  CB  GLU B 763     7090   7816   6786   -925   -361    601       C  
ATOM   3258  CG  GLU B 763     -93.581  -9.909   2.001  1.00 67.31           C  
ANISOU 3258  CG  GLU B 763     8428   9057   8089   -905   -346    582       C  
ATOM   3259  CD  GLU B 763     -94.620 -10.114   3.110  1.00 75.54           C  
ANISOU 3259  CD  GLU B 763     9432  10155   9115   -944   -334    620       C  
ATOM   3260  OE1 GLU B 763     -95.687 -10.766   2.914  1.00 79.98           O  
ANISOU 3260  OE1 GLU B 763     9974  10767   9646  -1028   -352    655       O  
ATOM   3261  OE2 GLU B 763     -94.335  -9.639   4.220  1.00 76.26           O  
ANISOU 3261  OE2 GLU B 763     9515  10238   9221   -893   -305    614       O  
ATOM   3262  N   MET B 764     -93.331 -12.090  -0.572  1.00 44.05           N  
ANISOU 3262  N   MET B 764     5621   6040   5077  -1050   -424    543       N  
ATOM   3263  CA  MET B 764     -92.766 -13.397  -0.534  1.00 44.61           C  
ANISOU 3263  CA  MET B 764     5791   6026   5133  -1091   -444    510       C  
ATOM   3264  C   MET B 764     -91.666 -13.560  -1.569  1.00 43.03           C  
ANISOU 3264  C   MET B 764     5652   5760   4937  -1062   -444    457       C  
ATOM   3265  O   MET B 764     -90.572 -14.079  -1.263  1.00 43.67           O  
ANISOU 3265  O   MET B 764     5801   5753   5040  -1026   -438    415       O  
ATOM   3266  CB  MET B 764     -93.837 -14.426  -0.767  1.00 48.72           C  
ANISOU 3266  CB  MET B 764     6329   6572   5610  -1204   -478    535       C  
ATOM   3267  CG  MET B 764     -93.267 -15.823  -0.834  1.00 52.96           C  
ANISOU 3267  CG  MET B 764     6979   7010   6133  -1249   -500    499       C  
ATOM   3268  SD  MET B 764     -94.502 -16.949  -1.491  1.00 74.44           S  
ANISOU 3268  SD  MET B 764     9724   9760   8799  -1393   -545    521       S  
ATOM   3269  CE  MET B 764     -94.281 -16.646  -3.227  1.00 66.79           C  
ANISOU 3269  CE  MET B 764     8765   8807   7806  -1395   -558    487       C  
ATOM   3270  N   LEU B 765     -91.953 -13.174  -2.800  1.00 40.53           N  
ANISOU 3270  N   LEU B 765     5314   5487   4599  -1079   -451    459       N  
ATOM   3271  CA  LEU B 765     -90.958 -13.334  -3.853  1.00 42.30           C  
ANISOU 3271  CA  LEU B 765     5598   5657   4819  -1058   -445    408       C  
ATOM   3272  C   LEU B 765     -89.677 -12.545  -3.568  1.00 39.75           C  
ANISOU 3272  C   LEU B 765     5268   5289   4547   -954   -407    377       C  
ATOM   3273  O   LEU B 765     -88.581 -13.051  -3.830  1.00 40.97           O  
ANISOU 3273  O   LEU B 765     5486   5365   4714   -927   -397    325       O  
ATOM   3274  CB  LEU B 765     -91.497 -12.913  -5.215  1.00 45.03           C  
ANISOU 3274  CB  LEU B 765     5918   6066   5125  -1093   -458    421       C  
ATOM   3275  CG  LEU B 765     -92.557 -13.806  -5.858  1.00 46.30           C  
ANISOU 3275  CG  LEU B 765     6102   6262   5229  -1204   -503    436       C  
ATOM   3276  CD1 LEU B 765     -92.897 -13.261  -7.236  1.00 47.95           C  
ANISOU 3276  CD1 LEU B 765     6289   6533   5397  -1226   -517    447       C  
ATOM   3277  CD2 LEU B 765     -92.064 -15.234  -5.979  1.00 46.97           C  
ANISOU 3277  CD2 LEU B 765     6297   6255   5294  -1253   -516    385       C  
ATOM   3278  N   ASP B 766     -89.804 -11.349  -2.998  1.00 38.54           N  
ANISOU 3278  N   ASP B 766     5037   5181   4425   -896   -386    406       N  
ATOM   3279  CA  ASP B 766     -88.616 -10.568  -2.587  1.00 41.14           C  
ANISOU 3279  CA  ASP B 766     5357   5468   4805   -804   -353    378       C  
ATOM   3280  C   ASP B 766     -87.712 -11.374  -1.641  1.00 41.87           C  
ANISOU 3280  C   ASP B 766     5508   5476   4924   -780   -354    343       C  
ATOM   3281  O   ASP B 766     -86.482 -11.458  -1.844  1.00 39.71           O  
ANISOU 3281  O   ASP B 766     5270   5139   4681   -732   -340    297       O  
ATOM   3282  CB  ASP B 766     -89.006  -9.266  -1.890  1.00 39.37           C  
ANISOU 3282  CB  ASP B 766     5049   5298   4611   -753   -333    413       C  
ATOM   3283  CG  ASP B 766     -89.791  -8.351  -2.781  1.00 40.10           C  
ANISOU 3283  CG  ASP B 766     5079   5467   4689   -760   -332    452       C  
ATOM   3284  OD1 ASP B 766     -89.719  -8.520  -4.046  1.00 41.56           O  
ANISOU 3284  OD1 ASP B 766     5289   5657   4844   -789   -341    444       O  
ATOM   3285  OD2 ASP B 766     -90.474  -7.471  -2.211  1.00 39.75           O  
ANISOU 3285  OD2 ASP B 766     4965   5476   4662   -734   -322    489       O  
ATOM   3286  N   ASN B 767     -88.334 -12.027  -0.665  1.00 40.66           N  
ANISOU 3286  N   ASN B 767     5366   5324   4758   -818   -374    366       N  
ATOM   3287  CA  ASN B 767     -87.580 -12.801   0.301  1.00 42.75           C  
ANISOU 3287  CA  ASN B 767     5688   5513   5043   -799   -382    344       C  
ATOM   3288  C   ASN B 767     -87.018 -14.058  -0.373  1.00 41.15           C  
ANISOU 3288  C   ASN B 767     5573   5232   4830   -828   -399    305       C  
ATOM   3289  O   ASN B 767     -85.876 -14.445  -0.143  1.00 38.26           O  
ANISOU 3289  O   ASN B 767     5250   4788   4497   -779   -397    266       O  
ATOM   3290  CB  ASN B 767     -88.482 -13.057   1.500  1.00 47.55           C  
ANISOU 3290  CB  ASN B 767     6282   6152   5633   -835   -394    388       C  
ATOM   3291  CG  ASN B 767     -87.757 -13.668   2.698  1.00 58.96           C  
ANISOU 3291  CG  ASN B 767     7779   7528   7095   -809   -405    377       C  
ATOM   3292  OD1 ASN B 767     -86.509 -13.602   2.868  1.00 58.74           O  
ANISOU 3292  OD1 ASN B 767     7776   7437   7106   -743   -402    339       O  
ATOM   3293  ND2 ASN B 767     -88.552 -14.282   3.560  1.00 63.16           N  
ANISOU 3293  ND2 ASN B 767     8326   8073   7598   -864   -420    413       N  
ATOM   3294  N   LEU B 768     -87.787 -14.651  -1.267  1.00 42.42           N  
ANISOU 3294  N   LEU B 768     5758   5413   4948   -905   -416    310       N  
ATOM   3295  CA  LEU B 768     -87.304 -15.820  -2.011  1.00 45.37           C  
ANISOU 3295  CA  LEU B 768     6220   5711   5307   -936   -428    266       C  
ATOM   3296  C   LEU B 768     -86.085 -15.482  -2.859  1.00 44.02           C  
ANISOU 3296  C   LEU B 768     6063   5501   5163   -870   -399    212       C  
ATOM   3297  O   LEU B 768     -85.120 -16.244  -2.905  1.00 40.51           O  
ANISOU 3297  O   LEU B 768     5681   4970   4742   -842   -395    166       O  
ATOM   3298  CB  LEU B 768     -88.399 -16.402  -2.900  1.00 47.98           C  
ANISOU 3298  CB  LEU B 768     6571   6078   5580  -1036   -452    279       C  
ATOM   3299  CG  LEU B 768     -89.528 -17.204  -2.246  1.00 50.35           C  
ANISOU 3299  CG  LEU B 768     6885   6395   5851  -1124   -485    321       C  
ATOM   3300  CD1 LEU B 768     -90.422 -17.825  -3.308  1.00 50.94           C  
ANISOU 3300  CD1 LEU B 768     6986   6497   5870  -1225   -512    322       C  
ATOM   3301  CD2 LEU B 768     -88.983 -18.296  -1.347  1.00 51.41           C  
ANISOU 3301  CD2 LEU B 768     7098   6430   6004  -1122   -498    307       C  
ATOM   3302  N   LEU B 769     -86.118 -14.315  -3.479  1.00 44.22           N  
ANISOU 3302  N   LEU B 769     6024   5589   5187   -843   -375    221       N  
ATOM   3303  CA  LEU B 769     -85.005 -13.838  -4.285  1.00 46.74           C  
ANISOU 3303  CA  LEU B 769     6345   5884   5530   -785   -340    177       C  
ATOM   3304  C   LEU B 769     -83.704 -13.797  -3.531  1.00 42.64           C  
ANISOU 3304  C   LEU B 769     5830   5297   5074   -703   -323    144       C  
ATOM   3305  O   LEU B 769     -82.703 -14.367  -3.970  1.00 44.68           O  
ANISOU 3305  O   LEU B 769     6136   5488   5352   -674   -308     92       O  
ATOM   3306  CB  LEU B 769     -85.301 -12.426  -4.758  1.00 51.84           C  
ANISOU 3306  CB  LEU B 769     6913   6609   6173   -763   -320    207       C  
ATOM   3307  CG  LEU B 769     -84.650 -11.856  -6.026  1.00 58.37           C  
ANISOU 3307  CG  LEU B 769     7740   7444   6994   -741   -286    179       C  
ATOM   3308  CD1 LEU B 769     -83.516 -10.877  -5.714  1.00 58.94           C  
ANISOU 3308  CD1 LEU B 769     7769   7498   7127   -654   -249    163       C  
ATOM   3309  CD2 LEU B 769     -84.166 -12.963  -6.957  1.00 61.54           C  
ANISOU 3309  CD2 LEU B 769     8225   7791   7366   -771   -282    124       C  
ATOM   3310  N   ASP B 770     -83.721 -13.140  -2.377  1.00 40.81           N  
ANISOU 3310  N   ASP B 770     5549   5083   4874   -665   -327    173       N  
ATOM   3311  CA  ASP B 770     -82.516 -13.052  -1.558  1.00 39.40           C  
ANISOU 3311  CA  ASP B 770     5368   4847   4754   -590   -320    147       C  
ATOM   3312  C   ASP B 770     -82.111 -14.403  -0.957  1.00 37.99           C  
ANISOU 3312  C   ASP B 770     5263   4585   4585   -594   -348    128       C  
ATOM   3313  O   ASP B 770     -80.909 -14.699  -0.792  1.00 38.37           O  
ANISOU 3313  O   ASP B 770     5331   4567   4681   -535   -343     89       O  
ATOM   3314  CB  ASP B 770     -82.707 -12.017  -0.467  1.00 40.20           C  
ANISOU 3314  CB  ASP B 770     5406   4992   4877   -556   -319    181       C  
ATOM   3315  CG  ASP B 770     -82.451 -10.583  -0.957  1.00 43.40           C  
ANISOU 3315  CG  ASP B 770     5744   5444   5304   -515   -285    182       C  
ATOM   3316  OD1 ASP B 770     -81.542 -10.394  -1.811  1.00 45.80           O  
ANISOU 3316  OD1 ASP B 770     6050   5724   5630   -485   -259    146       O  
ATOM   3317  OD2 ASP B 770     -83.143  -9.650  -0.482  1.00 42.96           O  
ANISOU 3317  OD2 ASP B 770     5633   5446   5245   -512   -281    219       O  
ATOM   3318  N   ILE B 771     -83.089 -15.242  -0.652  1.00 37.31           N  
ANISOU 3318  N   ILE B 771     5217   4500   4459   -663   -378    157       N  
ATOM   3319  CA  ILE B 771     -82.766 -16.620  -0.259  1.00 41.87           C  
ANISOU 3319  CA  ILE B 771     5878   4989   5043   -676   -406    141       C  
ATOM   3320  C   ILE B 771     -82.026 -17.370  -1.397  1.00 43.96           C  
ANISOU 3320  C   ILE B 771     6201   5186   5314   -668   -391     81       C  
ATOM   3321  O   ILE B 771     -81.026 -18.051  -1.140  1.00 42.09           O  
ANISOU 3321  O   ILE B 771     6007   4865   5120   -619   -395     47       O  
ATOM   3322  CB  ILE B 771     -84.019 -17.373   0.221  1.00 43.01           C  
ANISOU 3322  CB  ILE B 771     6055   5147   5139   -763   -439    186       C  
ATOM   3323  CG1 ILE B 771     -84.410 -16.864   1.609  1.00 41.38           C  
ANISOU 3323  CG1 ILE B 771     5806   4981   4935   -753   -449    234       C  
ATOM   3324  CG2 ILE B 771     -83.765 -18.866   0.301  1.00 47.59           C  
ANISOU 3324  CG2 ILE B 771     6733   5628   5719   -790   -465    167       C  
ATOM   3325  CD1 ILE B 771     -85.839 -17.121   1.993  1.00 42.20           C  
ANISOU 3325  CD1 ILE B 771     5904   5141   4989   -840   -465    287       C  
ATOM   3326  N   GLU B 772     -82.495 -17.235  -2.640  1.00 44.66           N  
ANISOU 3326  N   GLU B 772     6292   5314   5361   -712   -373     67       N  
ATOM   3327  CA  GLU B 772     -81.806 -17.847  -3.793  1.00 46.92           C  
ANISOU 3327  CA  GLU B 772     6635   5546   5647   -706   -350      5       C  
ATOM   3328  C   GLU B 772     -80.375 -17.348  -3.898  1.00 45.29           C  
ANISOU 3328  C   GLU B 772     6399   5308   5501   -610   -313    -37       C  
ATOM   3329  O   GLU B 772     -79.446 -18.140  -4.094  1.00 48.77           O  
ANISOU 3329  O   GLU B 772     6890   5667   5975   -571   -302    -88       O  
ATOM   3330  CB  GLU B 772     -82.564 -17.588  -5.093  1.00 48.83           C  
ANISOU 3330  CB  GLU B 772     6876   5851   5825   -770   -338      3       C  
ATOM   3331  CG  GLU B 772     -82.027 -18.269  -6.371  1.00 51.57           C  
ANISOU 3331  CG  GLU B 772     7293   6150   6151   -780   -312    -64       C  
ATOM   3332  CD  GLU B 772     -80.727 -17.665  -6.930  1.00 53.17           C  
ANISOU 3332  CD  GLU B 772     7469   6339   6394   -697   -258   -111       C  
ATOM   3333  OE1 GLU B 772     -80.537 -16.436  -6.882  1.00 51.27           O  
ANISOU 3333  OE1 GLU B 772     7150   6161   6172   -660   -237    -88       O  
ATOM   3334  OE2 GLU B 772     -79.881 -18.430  -7.436  1.00 55.53           O  
ANISOU 3334  OE2 GLU B 772     7825   6564   6708   -670   -233   -174       O  
ATOM   3335  N   VAL B 773     -80.178 -16.054  -3.688  1.00 44.14           N  
ANISOU 3335  N   VAL B 773     6170   5223   5376   -569   -293    -16       N  
ATOM   3336  CA  VAL B 773     -78.825 -15.499  -3.696  1.00 41.12           C  
ANISOU 3336  CA  VAL B 773     5749   4818   5057   -483   -260    -52       C  
ATOM   3337  C   VAL B 773     -77.962 -16.135  -2.621  1.00 39.92           C  
ANISOU 3337  C   VAL B 773     5614   4588   4964   -426   -284    -64       C  
ATOM   3338  O   VAL B 773     -76.821 -16.554  -2.882  1.00 44.27           O  
ANISOU 3338  O   VAL B 773     6180   5077   5562   -370   -264   -114       O  
ATOM   3339  CB  VAL B 773     -78.825 -13.989  -3.480  1.00 43.45           C  
ANISOU 3339  CB  VAL B 773     5956   5186   5368   -456   -242    -22       C  
ATOM   3340  CG1 VAL B 773     -77.408 -13.478  -3.280  1.00 43.39           C  
ANISOU 3340  CG1 VAL B 773     5906   5149   5432   -373   -215    -55       C  
ATOM   3341  CG2 VAL B 773     -79.492 -13.282  -4.651  1.00 45.17           C  
ANISOU 3341  CG2 VAL B 773     6153   5475   5534   -499   -216     -9       C  
ATOM   3342  N   ALA B 774     -78.503 -16.233  -1.413  1.00 38.74           N  
ANISOU 3342  N   ALA B 774     5464   4444   4813   -440   -326    -19       N  
ATOM   3343  CA  ALA B 774     -77.773 -16.850  -0.301  1.00 41.00           C  
ANISOU 3343  CA  ALA B 774     5771   4659   5146   -391   -359    -20       C  
ATOM   3344  C   ALA B 774     -77.441 -18.293  -0.603  1.00 41.87           C  
ANISOU 3344  C   ALA B 774     5969   4675   5264   -394   -372    -53       C  
ATOM   3345  O   ALA B 774     -76.309 -18.740  -0.390  1.00 44.56           O  
ANISOU 3345  O   ALA B 774     6321   4946   5665   -325   -374    -86       O  
ATOM   3346  CB  ALA B 774     -78.580 -16.759   0.988  1.00 39.35           C  
ANISOU 3346  CB  ALA B 774     5558   4479   4915   -420   -400     39       C  
ATOM   3347  N   TYR B 775     -78.424 -19.027  -1.113  1.00 45.40           N  
ANISOU 3347  N   TYR B 775     6478   5117   5655   -473   -381    -46       N  
ATOM   3348  CA  TYR B 775     -78.220 -20.439  -1.399  1.00 50.21           C  
ANISOU 3348  CA  TYR B 775     7181   5628   6268   -484   -394    -79       C  
ATOM   3349  C   TYR B 775     -77.189 -20.660  -2.508  1.00 50.41           C  
ANISOU 3349  C   TYR B 775     7222   5609   6324   -434   -347   -152       C  
ATOM   3350  O   TYR B 775     -76.370 -21.562  -2.391  1.00 53.83           O  
ANISOU 3350  O   TYR B 775     7702   5946   6803   -385   -352   -187       O  
ATOM   3351  CB  TYR B 775     -79.538 -21.142  -1.750  1.00 52.46           C  
ANISOU 3351  CB  TYR B 775     7530   5922   6483   -591   -414    -58       C  
ATOM   3352  CG  TYR B 775     -79.401 -22.632  -1.567  1.00 58.48           C  
ANISOU 3352  CG  TYR B 775     8395   6569   7255   -605   -442    -75       C  
ATOM   3353  CD1 TYR B 775     -79.341 -23.180  -0.292  1.00 59.61           C  
ANISOU 3353  CD1 TYR B 775     8566   6661   7423   -592   -487    -34       C  
ATOM   3354  CD2 TYR B 775     -79.263 -23.490  -2.654  1.00 60.66           C  
ANISOU 3354  CD2 TYR B 775     8745   6783   7518   -626   -424   -133       C  
ATOM   3355  CE1 TYR B 775     -79.188 -24.542  -0.098  1.00 60.43           C  
ANISOU 3355  CE1 TYR B 775     8768   6651   7540   -601   -516    -44       C  
ATOM   3356  CE2 TYR B 775     -79.101 -24.858  -2.467  1.00 60.03           C  
ANISOU 3356  CE2 TYR B 775     8766   6587   7454   -634   -449   -151       C  
ATOM   3357  CZ  TYR B 775     -79.066 -25.376  -1.184  1.00 61.94           C  
ANISOU 3357  CZ  TYR B 775     9034   6777   7725   -620   -496   -103       C  
ATOM   3358  OH  TYR B 775     -78.913 -26.725  -0.947  1.00 61.15           O  
ANISOU 3358  OH  TYR B 775     9036   6553   7643   -626   -525   -113       O  
ATOM   3359  N   SER B 776     -77.240 -19.848  -3.568  1.00 48.01           N  
ANISOU 3359  N   SER B 776     6877   5371   5994   -445   -301   -174       N  
ATOM   3360  CA  SER B 776     -76.255 -19.911  -4.649  1.00 51.20           C  
ANISOU 3360  CA  SER B 776     7286   5746   6421   -399   -246   -243       C  
ATOM   3361  C   SER B 776     -74.847 -19.645  -4.172  1.00 50.74           C  
ANISOU 3361  C   SER B 776     7176   5653   6450   -294   -230   -267       C  
ATOM   3362  O   SER B 776     -73.912 -20.338  -4.561  1.00 54.87           O  
ANISOU 3362  O   SER B 776     7730   6103   7017   -242   -206   -324       O  
ATOM   3363  CB  SER B 776     -76.553 -18.884  -5.724  1.00 55.15           C  
ANISOU 3363  CB  SER B 776     7742   6337   6876   -428   -202   -248       C  
ATOM   3364  OG  SER B 776     -77.706 -19.254  -6.423  1.00 66.27           O  
ANISOU 3364  OG  SER B 776     9203   7773   8204   -521   -214   -239       O  
ATOM   3365  N   LEU B 777     -74.680 -18.623  -3.353  1.00 48.53           N  
ANISOU 3365  N   LEU B 777     6815   5425   6198   -264   -243   -228       N  
ATOM   3366  CA  LEU B 777     -73.360 -18.311  -2.831  1.00 50.34           C  
ANISOU 3366  CA  LEU B 777     6987   5628   6511   -172   -236   -247       C  
ATOM   3367  C   LEU B 777     -72.808 -19.496  -2.060  1.00 50.90           C  
ANISOU 3367  C   LEU B 777     7109   5599   6631   -127   -277   -255       C  
ATOM   3368  O   LEU B 777     -71.656 -19.869  -2.229  1.00 48.82           O  
ANISOU 3368  O   LEU B 777     6836   5279   6434    -53   -258   -301       O  
ATOM   3369  CB  LEU B 777     -73.407 -17.095  -1.912  1.00 49.95           C  
ANISOU 3369  CB  LEU B 777     6855   5646   6476   -159   -255   -200       C  
ATOM   3370  CG  LEU B 777     -73.520 -15.732  -2.601  1.00 50.47           C  
ANISOU 3370  CG  LEU B 777     6852   5800   6525   -172   -209   -196       C  
ATOM   3371  CD1 LEU B 777     -73.623 -14.669  -1.528  1.00 47.75           C  
ANISOU 3371  CD1 LEU B 777     6440   5505   6197   -160   -235   -151       C  
ATOM   3372  CD2 LEU B 777     -72.343 -15.452  -3.537  1.00 47.32           C  
ANISOU 3372  CD2 LEU B 777     6417   5392   6170   -121   -147   -253       C  
ATOM   3373  N   LEU B 778     -73.666 -20.086  -1.235  1.00 53.80           N  
ANISOU 3373  N   LEU B 778     7530   5946   6967   -173   -333   -208       N  
ATOM   3374  CA  LEU B 778     -73.295 -21.176  -0.358  1.00 58.22           C  
ANISOU 3374  CA  LEU B 778     8144   6411   7564   -138   -384   -199       C  
ATOM   3375  C   LEU B 778     -72.923 -22.418  -1.171  1.00 62.90           C  
ANISOU 3375  C   LEU B 778     8819   6907   8174   -124   -364   -256       C  
ATOM   3376  O   LEU B 778     -71.937 -23.090  -0.866  1.00 69.78           O  
ANISOU 3376  O   LEU B 778     9704   7695   9114    -47   -376   -280       O  
ATOM   3377  CB  LEU B 778     -74.458 -21.477   0.595  1.00 57.33           C  
ANISOU 3377  CB  LEU B 778     8075   6309   7399   -209   -439   -132       C  
ATOM   3378  CG  LEU B 778     -74.200 -22.273   1.873  1.00 59.63           C  
ANISOU 3378  CG  LEU B 778     8409   6529   7721   -181   -504    -95       C  
ATOM   3379  CD1 LEU B 778     -73.050 -21.689   2.698  1.00 61.37           C  
ANISOU 3379  CD1 LEU B 778     8557   6753   8010    -89   -523    -91       C  
ATOM   3380  CD2 LEU B 778     -75.474 -22.302   2.694  1.00 59.09           C  
ANISOU 3380  CD2 LEU B 778     8368   6498   7585   -264   -542    -27       C  
ATOM   3381  N   ARG B 779     -73.680 -22.698  -2.223  1.00 62.82           N  
ANISOU 3381  N   ARG B 779     8860   6907   8100   -195   -334   -280       N  
ATOM   3382  CA  ARG B 779     -73.389 -23.862  -3.078  1.00 70.83           C  
ANISOU 3382  CA  ARG B 779     9962   7829   9122   -189   -310   -343       C  
ATOM   3383  C   ARG B 779     -72.141 -23.674  -3.980  1.00 74.79           C  
ANISOU 3383  C   ARG B 779    10425   8316   9676   -107   -242   -417       C  
ATOM   3384  O   ARG B 779     -71.572 -24.667  -4.428  1.00 79.82           O  
ANISOU 3384  O   ARG B 779    11123   8859  10345    -69   -223   -473       O  
ATOM   3385  CB  ARG B 779     -74.616 -24.240  -3.941  1.00 66.22           C  
ANISOU 3385  CB  ARG B 779     9450   7263   8447   -299   -303   -348       C  
ATOM   3386  N   GLY B 780     -71.689 -22.431  -4.203  1.00 71.17           N  
ANISOU 3386  N   GLY B 780     9866   7943   9230    -79   -204   -418       N  
ATOM   3387  CA  GLY B 780     -70.680 -22.129  -5.252  1.00 69.99           C  
ANISOU 3387  CA  GLY B 780     9678   7802   9113    -25   -127   -487       C  
ATOM   3388  C   GLY B 780     -69.215 -21.991  -4.844  1.00 67.02           C  
ANISOU 3388  C   GLY B 780     9228   7394   8841     88   -112   -512       C  
ATOM   3389  O   GLY B 780     -68.840 -22.308  -3.717  1.00 66.40           O  
ANISOU 3389  O   GLY B 780     9138   7270   8820    136   -170   -481       O  
ATOM   3390  N   SER B 786     -59.983 -26.330   1.920  1.00 66.36           N  
ANISOU 3390  N   SER B 786     8844   6737   9631    972   -492   -481       N  
ATOM   3391  CA  SER B 786     -58.785 -26.020   2.706  1.00 69.62           C  
ANISOU 3391  CA  SER B 786     9142   7166  10145   1064   -545   -463       C  
ATOM   3392  C   SER B 786     -58.969 -24.984   3.858  1.00 73.62           C  
ANISOU 3392  C   SER B 786     9588   7764  10618   1020   -622   -392       C  
ATOM   3393  O   SER B 786     -58.407 -25.167   4.942  1.00 76.36           O  
ANISOU 3393  O   SER B 786     9905   8090  11017   1075   -714   -345       O  
ATOM   3394  CB  SER B 786     -57.630 -25.591   1.787  1.00 69.44           C  
ANISOU 3394  CB  SER B 786     9000   7178  10206   1136   -455   -538       C  
ATOM   3395  N   LYS B 787     -59.724 -23.902   3.624  1.00 71.95           N  
ANISOU 3395  N   LYS B 787     9361   7653  10323    924   -586   -385       N  
ATOM   3396  CA  LYS B 787     -60.030 -22.887   4.669  1.00 70.51           C  
ANISOU 3396  CA  LYS B 787     9136   7556  10098    873   -650   -325       C  
ATOM   3397  C   LYS B 787     -61.222 -23.310   5.558  1.00 63.36           C  
ANISOU 3397  C   LYS B 787     8345   6628   9102    802   -722   -255       C  
ATOM   3398  O   LYS B 787     -62.045 -24.110   5.133  1.00 61.74           O  
ANISOU 3398  O   LYS B 787     8247   6365   8846    761   -703   -257       O  
ATOM   3399  CB  LYS B 787     -60.322 -21.519   4.006  1.00 68.59           C  
ANISOU 3399  CB  LYS B 787     8826   7425   9809    806   -576   -349       C  
ATOM   3400  N   ASP B 788     -61.304 -22.787   6.785  1.00 62.17           N  
ANISOU 3400  N   ASP B 788     8171   6520   8929    785   -803   -195       N  
ATOM   3401  CA  ASP B 788     -62.515 -22.941   7.620  1.00 63.96           C  
ANISOU 3401  CA  ASP B 788     8494   6751   9056    703   -857   -129       C  
ATOM   3402  C   ASP B 788     -63.717 -22.489   6.785  1.00 65.43           C  
ANISOU 3402  C   ASP B 788     8720   6988   9151    604   -781   -145       C  
ATOM   3403  O   ASP B 788     -63.664 -21.415   6.177  1.00 64.86           O  
ANISOU 3403  O   ASP B 788     8573   6998   9073    581   -720   -178       O  
ATOM   3404  CB  ASP B 788     -62.418 -22.084   8.900  1.00 62.20           C  
ANISOU 3404  CB  ASP B 788     8222   6599   8813    689   -931    -77       C  
ATOM   3405  CG  ASP B 788     -63.554 -22.362   9.905  1.00 62.73           C  
ANISOU 3405  CG  ASP B 788     8388   6664   8781    615   -991     -5       C  
ATOM   3406  OD1 ASP B 788     -64.620 -22.856   9.494  1.00 60.62           O  
ANISOU 3406  OD1 ASP B 788     8210   6373   8448    550   -959      3       O  
ATOM   3407  OD2 ASP B 788     -63.397 -22.069  11.121  1.00 68.67           O  
ANISOU 3407  OD2 ASP B 788     9129   7443   9518    617  -1070     44       O  
ATOM   3408  N   PRO B 789     -64.791 -23.296   6.737  1.00 63.83           N  
ANISOU 3408  N   PRO B 789     8632   6739   8880    543   -786   -120       N  
ATOM   3409  CA  PRO B 789     -65.962 -22.908   5.942  1.00 61.44           C  
ANISOU 3409  CA  PRO B 789     8364   6488   8492    447   -721   -132       C  
ATOM   3410  C   PRO B 789     -66.572 -21.542   6.300  1.00 61.90           C  
ANISOU 3410  C   PRO B 789     8366   6663   8489    384   -714   -106       C  
ATOM   3411  O   PRO B 789     -67.044 -20.842   5.408  1.00 54.19           O  
ANISOU 3411  O   PRO B 789     7364   5747   7477    337   -646   -135       O  
ATOM   3412  CB  PRO B 789     -66.957 -24.031   6.216  1.00 62.16           C  
ANISOU 3412  CB  PRO B 789     8584   6509   8526    392   -755    -93       C  
ATOM   3413  CG  PRO B 789     -66.093 -25.216   6.484  1.00 63.77           C  
ANISOU 3413  CG  PRO B 789     8827   6596   8807    478   -799    -95       C  
ATOM   3414  CD  PRO B 789     -64.897 -24.684   7.223  1.00 63.94           C  
ANISOU 3414  CD  PRO B 789     8749   6641   8903    563   -844    -87       C  
ATOM   3415  N   ILE B 790     -66.559 -21.168   7.577  1.00 62.05           N  
ANISOU 3415  N   ILE B 790     8369   6711   8495    382   -783    -55       N  
ATOM   3416  CA  ILE B 790     -67.031 -19.846   7.981  1.00 63.34           C  
ANISOU 3416  CA  ILE B 790     8478   6979   8609    333   -775    -37       C  
ATOM   3417  C   ILE B 790     -66.257 -18.767   7.209  1.00 60.16           C  
ANISOU 3417  C   ILE B 790     7967   6633   8257    364   -716    -90       C  
ATOM   3418  O   ILE B 790     -66.860 -17.819   6.712  1.00 58.94           O  
ANISOU 3418  O   ILE B 790     7785   6550   8060    311   -664    -99       O  
ATOM   3419  CB  ILE B 790     -66.902 -19.637   9.501  1.00 69.16           C  
ANISOU 3419  CB  ILE B 790     9213   7733   9332    340   -860     18       C  
ATOM   3420  CG1 ILE B 790     -67.896 -20.532  10.246  1.00 76.63           C  
ANISOU 3420  CG1 ILE B 790    10268   8640  10206    287   -907     78       C  
ATOM   3421  CG2 ILE B 790     -67.195 -18.192   9.882  1.00 71.97           C  
ANISOU 3421  CG2 ILE B 790     9504   8191   9650    301   -847     23       C  
ATOM   3422  CD1 ILE B 790     -67.427 -20.940  11.631  1.00 82.07           C  
ANISOU 3422  CD1 ILE B 790    10981   9299  10902    321  -1003    129       C  
ATOM   3423  N   ASP B 791     -64.935 -18.924   7.105  1.00 56.08           N  
ANISOU 3423  N   ASP B 791     7390   6083   7834    448   -724   -122       N  
ATOM   3424  CA  ASP B 791     -64.091 -17.976   6.375  1.00 54.77           C  
ANISOU 3424  CA  ASP B 791     7119   5967   7726    478   -666   -172       C  
ATOM   3425  C   ASP B 791     -64.375 -17.987   4.872  1.00 52.86           C  
ANISOU 3425  C   ASP B 791     6886   5728   7470    455   -569   -220       C  
ATOM   3426  O   ASP B 791     -64.322 -16.938   4.221  1.00 54.52           O  
ANISOU 3426  O   ASP B 791     7034   6006   7677    433   -510   -244       O  
ATOM   3427  CB  ASP B 791     -62.597 -18.258   6.591  1.00 55.02           C  
ANISOU 3427  CB  ASP B 791     7078   5961   7867    576   -696   -195       C  
ATOM   3428  CG  ASP B 791     -62.092 -17.820   7.961  1.00 56.52           C  
ANISOU 3428  CG  ASP B 791     7224   6176   8076    597   -786   -156       C  
ATOM   3429  OD1 ASP B 791     -60.855 -17.786   8.126  1.00 62.52           O  
ANISOU 3429  OD1 ASP B 791     7902   6927   8927    670   -810   -175       O  
ATOM   3430  OD2 ASP B 791     -62.891 -17.512   8.876  1.00 55.97           O  
ANISOU 3430  OD2 ASP B 791     7196   6137   7932    543   -832   -109       O  
ATOM   3431  N   VAL B 792     -64.678 -19.156   4.316  1.00 50.54           N  
ANISOU 3431  N   VAL B 792     6675   5363   7166    458   -554   -234       N  
ATOM   3432  CA  VAL B 792     -64.986 -19.244   2.895  1.00 48.18           C  
ANISOU 3432  CA  VAL B 792     6396   5065   6843    431   -467   -282       C  
ATOM   3433  C   VAL B 792     -66.254 -18.451   2.608  1.00 48.37           C  
ANISOU 3433  C   VAL B 792     6441   5166   6773    335   -439   -259       C  
ATOM   3434  O   VAL B 792     -66.309 -17.683   1.654  1.00 49.14           O  
ANISOU 3434  O   VAL B 792     6499   5317   6855    311   -371   -288       O  
ATOM   3435  CB  VAL B 792     -65.188 -20.695   2.422  1.00 49.97           C  
ANISOU 3435  CB  VAL B 792     6723   5195   7068    441   -462   -303       C  
ATOM   3436  CG1 VAL B 792     -65.694 -20.743   0.976  1.00 48.80           C  
ANISOU 3436  CG1 VAL B 792     6611   5059   6873    395   -376   -350       C  
ATOM   3437  CG2 VAL B 792     -63.887 -21.474   2.554  1.00 52.08           C  
ANISOU 3437  CG2 VAL B 792     6966   5384   7439    548   -479   -332       C  
ATOM   3438  N   ASN B 793     -67.276 -18.653   3.425  1.00 47.31           N  
ANISOU 3438  N   ASN B 793     6367   5034   6574    280   -492   -205       N  
ATOM   3439  CA  ASN B 793     -68.534 -17.986   3.221  1.00 46.36           C  
ANISOU 3439  CA  ASN B 793     6264   4984   6368    194   -470   -178       C  
ATOM   3440  C   ASN B 793     -68.463 -16.477   3.533  1.00 43.45           C  
ANISOU 3440  C   ASN B 793     5808   4705   5998    184   -460   -166       C  
ATOM   3441  O   ASN B 793     -69.087 -15.685   2.845  1.00 42.77           O  
ANISOU 3441  O   ASN B 793     5703   4679   5869    137   -412   -169       O  
ATOM   3442  CB  ASN B 793     -69.618 -18.677   4.032  1.00 47.55           C  
ANISOU 3442  CB  ASN B 793     6500   5113   6455    139   -525   -124       C  
ATOM   3443  CG  ASN B 793     -69.933 -20.076   3.526  1.00 48.18           C  
ANISOU 3443  CG  ASN B 793     6677   5108   6523    125   -525   -137       C  
ATOM   3444  OD1 ASN B 793     -70.115 -20.302   2.328  1.00 48.48           O  
ANISOU 3444  OD1 ASN B 793     6737   5138   6546    105   -470   -179       O  
ATOM   3445  ND2 ASN B 793     -70.063 -21.013   4.455  1.00 48.06           N  
ANISOU 3445  ND2 ASN B 793     6727   5028   6506    129   -590    -99       N  
ATOM   3446  N   TYR B 794     -67.676 -16.085   4.531  1.00 41.85           N  
ANISOU 3446  N   TYR B 794     5552   4506   5843    231   -507   -154       N  
ATOM   3447  CA  TYR B 794     -67.398 -14.675   4.786  1.00 40.74           C  
ANISOU 3447  CA  TYR B 794     5326   4438   5715    229   -495   -154       C  
ATOM   3448  C   TYR B 794     -66.897 -14.002   3.516  1.00 42.54           C  
ANISOU 3448  C   TYR B 794     5495   4696   5974    237   -415   -200       C  
ATOM   3449  O   TYR B 794     -67.413 -12.966   3.129  1.00 41.18           O  
ANISOU 3449  O   TYR B 794     5294   4585   5767    195   -377   -194       O  
ATOM   3450  CB  TYR B 794     -66.369 -14.516   5.891  1.00 40.07           C  
ANISOU 3450  CB  TYR B 794     5191   4343   5691    285   -558   -147       C  
ATOM   3451  CG  TYR B 794     -65.825 -13.112   6.078  1.00 36.98           C  
ANISOU 3451  CG  TYR B 794     4707   4013   5329    290   -546   -158       C  
ATOM   3452  CD1 TYR B 794     -66.589 -12.127   6.652  1.00 37.60           C  
ANISOU 3452  CD1 TYR B 794     4781   4150   5354    241   -554   -131       C  
ATOM   3453  CD2 TYR B 794     -64.528 -12.786   5.690  1.00 37.57           C  
ANISOU 3453  CD2 TYR B 794     4698   4087   5491    344   -525   -198       C  
ATOM   3454  CE1 TYR B 794     -66.086 -10.834   6.849  1.00 37.75           C  
ANISOU 3454  CE1 TYR B 794     4723   4218   5403    243   -544   -144       C  
ATOM   3455  CE2 TYR B 794     -64.016 -11.503   5.860  1.00 35.66           C  
ANISOU 3455  CE2 TYR B 794     4372   3897   5278    340   -516   -209       C  
ATOM   3456  CZ  TYR B 794     -64.797 -10.523   6.452  1.00 37.03           C  
ANISOU 3456  CZ  TYR B 794     4551   4122   5396    289   -527   -181       C  
ATOM   3457  OH  TYR B 794     -64.312  -9.238   6.659  1.00 33.39           O  
ANISOU 3457  OH  TYR B 794     4016   3705   4964    283   -519   -193       O  
ATOM   3458  N   GLU B 795     -65.915 -14.615   2.865  1.00 44.96           N  
ANISOU 3458  N   GLU B 795     5784   4956   6344    292   -389   -244       N  
ATOM   3459  CA  GLU B 795     -65.293 -14.053   1.652  1.00 48.11           C  
ANISOU 3459  CA  GLU B 795     6124   5380   6775    304   -307   -291       C  
ATOM   3460  C   GLU B 795     -66.274 -13.935   0.517  1.00 45.66           C  
ANISOU 3460  C   GLU B 795     5861   5098   6391    242   -246   -296       C  
ATOM   3461  O   GLU B 795     -66.197 -12.986  -0.266  1.00 45.97           O  
ANISOU 3461  O   GLU B 795     5853   5189   6423    221   -187   -309       O  
ATOM   3462  CB  GLU B 795     -64.070 -14.870   1.208  1.00 50.00           C  
ANISOU 3462  CB  GLU B 795     6340   5562   7096    380   -287   -339       C  
ATOM   3463  CG  GLU B 795     -62.863 -14.657   2.124  1.00 56.36           C  
ANISOU 3463  CG  GLU B 795     7062   6361   7991    447   -336   -340       C  
ATOM   3464  CD  GLU B 795     -61.663 -15.560   1.823  1.00 62.46           C  
ANISOU 3464  CD  GLU B 795     7806   7072   8854    532   -325   -383       C  
ATOM   3465  OE1 GLU B 795     -61.748 -16.478   0.966  1.00 62.43           O  
ANISOU 3465  OE1 GLU B 795     7857   7018   8843    546   -281   -416       O  
ATOM   3466  OE2 GLU B 795     -60.611 -15.350   2.469  1.00 64.72           O  
ANISOU 3466  OE2 GLU B 795     8012   7359   9220    588   -363   -385       O  
ATOM   3467  N   LYS B 796     -67.235 -14.856   0.470  1.00 44.76           N  
ANISOU 3467  N   LYS B 796     5838   4951   6216    205   -265   -280       N  
ATOM   3468  CA  LYS B 796     -68.265 -14.844  -0.544  1.00 45.42           C  
ANISOU 3468  CA  LYS B 796     5972   5062   6223    139   -220   -281       C  
ATOM   3469  C   LYS B 796     -69.206 -13.590  -0.441  1.00 45.53           C  
ANISOU 3469  C   LYS B 796     5958   5159   6181     79   -216   -239       C  
ATOM   3470  O   LYS B 796     -69.781 -13.170  -1.444  1.00 41.61           O  
ANISOU 3470  O   LYS B 796     5470   4705   5637     34   -168   -242       O  
ATOM   3471  CB  LYS B 796     -69.056 -16.184  -0.511  1.00 48.98           C  
ANISOU 3471  CB  LYS B 796     6527   5455   6629    109   -251   -272       C  
ATOM   3472  N   LEU B 797     -69.331 -12.988   0.754  1.00 41.28           N  
ANISOU 3472  N   LEU B 797     5389   4645   5650     81   -265   -201       N  
ATOM   3473  CA  LEU B 797     -70.085 -11.754   0.939  1.00 39.57           C  
ANISOU 3473  CA  LEU B 797     5140   4499   5394     39   -258   -167       C  
ATOM   3474  C   LEU B 797     -69.414 -10.525   0.313  1.00 38.83           C  
ANISOU 3474  C   LEU B 797     4969   4447   5337     52   -205   -187       C  
ATOM   3475  O   LEU B 797     -70.081  -9.540   0.092  1.00 37.12           O  
ANISOU 3475  O   LEU B 797     4735   4284   5086     16   -185   -164       O  
ATOM   3476  CB  LEU B 797     -70.335 -11.464   2.423  1.00 39.81           C  
ANISOU 3476  CB  LEU B 797     5164   4540   5422     41   -321   -129       C  
ATOM   3477  CG  LEU B 797     -71.078 -12.555   3.193  1.00 42.05           C  
ANISOU 3477  CG  LEU B 797     5523   4790   5664     19   -375    -98       C  
ATOM   3478  CD1 LEU B 797     -71.091 -12.230   4.673  1.00 41.03           C  
ANISOU 3478  CD1 LEU B 797     5383   4672   5535     28   -433    -66       C  
ATOM   3479  CD2 LEU B 797     -72.494 -12.745   2.676  1.00 41.96           C  
ANISOU 3479  CD2 LEU B 797     5562   4808   5574    -52   -358    -72       C  
ATOM   3480  N   LYS B 798     -68.115 -10.588   0.060  1.00 38.95           N  
ANISOU 3480  N   LYS B 798     4939   4438   5424    105   -184   -227       N  
ATOM   3481  CA  LYS B 798     -67.344  -9.484  -0.513  1.00 41.82           C  
ANISOU 3481  CA  LYS B 798     5226   4836   5829    116   -132   -247       C  
ATOM   3482  C   LYS B 798     -67.560  -8.196   0.289  1.00 38.50           C  
ANISOU 3482  C   LYS B 798     4759   4458   5412    100   -155   -216       C  
ATOM   3483  O   LYS B 798     -67.825  -7.127  -0.261  1.00 36.75           O  
ANISOU 3483  O   LYS B 798     4510   4279   5174     71   -113   -206       O  
ATOM   3484  CB  LYS B 798     -67.703  -9.293  -1.972  1.00 45.36           C  
ANISOU 3484  CB  LYS B 798     5690   5309   6234     81    -60   -259       C  
ATOM   3485  CG  LYS B 798     -67.264 -10.426  -2.892  1.00 50.82           C  
ANISOU 3485  CG  LYS B 798     6420   5960   6930    101    -22   -305       C  
ATOM   3486  CD  LYS B 798     -67.481 -10.009  -4.352  1.00 58.31           C  
ANISOU 3486  CD  LYS B 798     7376   6945   7834     63     54   -318       C  
ATOM   3487  CE  LYS B 798     -67.464 -11.197  -5.314  1.00 64.71           C  
ANISOU 3487  CE  LYS B 798     8253   7718   8616     63     89   -361       C  
ATOM   3488  NZ  LYS B 798     -67.506 -10.777  -6.749  1.00 65.29           N  
ANISOU 3488  NZ  LYS B 798     8332   7830   8644     30    167   -379       N  
ATOM   3489  N   THR B 799     -67.480  -8.332   1.604  1.00 37.03           N  
ANISOU 3489  N   THR B 799     4571   4257   5240    118   -222   -200       N  
ATOM   3490  CA  THR B 799     -67.803  -7.258   2.517  1.00 37.23           C  
ANISOU 3490  CA  THR B 799     4571   4317   5258    102   -250   -174       C  
ATOM   3491  C   THR B 799     -66.835  -7.349   3.674  1.00 39.20           C  
ANISOU 3491  C   THR B 799     4785   4544   5564    144   -309   -184       C  
ATOM   3492  O   THR B 799     -66.734  -8.390   4.321  1.00 41.22           O  
ANISOU 3492  O   THR B 799     5078   4763   5821    168   -361   -179       O  
ATOM   3493  CB  THR B 799     -69.256  -7.380   3.045  1.00 34.53           C  
ANISOU 3493  CB  THR B 799     4290   3995   4836     59   -278   -132       C  
ATOM   3494  OG1 THR B 799     -70.166  -7.315   1.958  1.00 37.55           O  
ANISOU 3494  OG1 THR B 799     4700   4403   5167     18   -230   -120       O  
ATOM   3495  CG2 THR B 799     -69.603  -6.260   4.012  1.00 34.96           C  
ANISOU 3495  CG2 THR B 799     4319   4084   4881     47   -300   -111       C  
ATOM   3496  N   ASP B 800     -66.154  -6.253   3.973  1.00 38.68           N  
ANISOU 3496  N   ASP B 800     4653   4500   5545    151   -307   -195       N  
ATOM   3497  CA  ASP B 800     -65.330  -6.200   5.162  1.00 38.23           C  
ANISOU 3497  CA  ASP B 800     4562   4431   5534    182   -373   -201       C  
ATOM   3498  C   ASP B 800     -66.226  -5.972   6.383  1.00 36.00           C  
ANISOU 3498  C   ASP B 800     4323   4163   5191    157   -427   -168       C  
ATOM   3499  O   ASP B 800     -66.997  -5.046   6.409  1.00 34.75           O  
ANISOU 3499  O   ASP B 800     4170   4038   4995    122   -405   -154       O  
ATOM   3500  CB  ASP B 800     -64.293  -5.095   5.069  1.00 39.97           C  
ANISOU 3500  CB  ASP B 800     4695   4669   5823    190   -354   -226       C  
ATOM   3501  CG  ASP B 800     -63.297  -5.156   6.216  1.00 41.56           C  
ANISOU 3501  CG  ASP B 800     4854   4858   6077    223   -428   -236       C  
ATOM   3502  OD1 ASP B 800     -62.310  -5.893   6.102  1.00 45.99           O  
ANISOU 3502  OD1 ASP B 800     5381   5394   6700    269   -443   -256       O  
ATOM   3503  OD2 ASP B 800     -63.510  -4.491   7.247  1.00 42.76           O  
ANISOU 3503  OD2 ASP B 800     5009   5027   6210    205   -474   -225       O  
ATOM   3504  N   ILE B 801     -66.135  -6.856   7.372  1.00 36.03           N  
ANISOU 3504  N   ILE B 801     4362   4141   5186    178   -496   -155       N  
ATOM   3505  CA  ILE B 801     -66.931  -6.759   8.585  1.00 35.00           C  
ANISOU 3505  CA  ILE B 801     4279   4026   4994    154   -547   -124       C  
ATOM   3506  C   ILE B 801     -66.036  -6.709   9.813  1.00 35.55           C  
ANISOU 3506  C   ILE B 801     4324   4087   5095    181   -623   -128       C  
ATOM   3507  O   ILE B 801     -65.260  -7.634  10.041  1.00 39.41           O  
ANISOU 3507  O   ILE B 801     4812   4540   5624    222   -668   -131       O  
ATOM   3508  CB  ILE B 801     -67.890  -7.960   8.725  1.00 34.13           C  
ANISOU 3508  CB  ILE B 801     4252   3894   4820    139   -564    -91       C  
ATOM   3509  CG1 ILE B 801     -68.709  -8.148   7.454  1.00 34.27           C  
ANISOU 3509  CG1 ILE B 801     4293   3919   4808    110   -497    -89       C  
ATOM   3510  CG2 ILE B 801     -68.799  -7.749   9.924  1.00 34.94           C  
ANISOU 3510  CG2 ILE B 801     4400   4023   4853    107   -602    -58       C  
ATOM   3511  CD1 ILE B 801     -69.666  -9.328   7.485  1.00 34.62           C  
ANISOU 3511  CD1 ILE B 801     4419   3942   4793     85   -511    -59       C  
ATOM   3512  N   LYS B 802     -66.149  -5.642  10.594  1.00 34.05           N  
ANISOU 3512  N   LYS B 802     4119   3929   4888    160   -640   -130       N  
ATOM   3513  CA  LYS B 802     -65.375  -5.463  11.810  1.00 38.68           C  
ANISOU 3513  CA  LYS B 802     4687   4516   5493    176   -716   -136       C  
ATOM   3514  C   LYS B 802     -66.304  -5.229  12.979  1.00 37.82           C  
ANISOU 3514  C   LYS B 802     4639   4431   5300    144   -750   -111       C  
ATOM   3515  O   LYS B 802     -67.326  -4.568  12.841  1.00 37.17           O  
ANISOU 3515  O   LYS B 802     4578   4377   5168    109   -703   -104       O  
ATOM   3516  CB  LYS B 802     -64.458  -4.239  11.715  1.00 43.32           C  
ANISOU 3516  CB  LYS B 802     5194   5122   6145    176   -706   -172       C  
ATOM   3517  CG  LYS B 802     -63.217  -4.441  10.857  1.00 49.80           C  
ANISOU 3517  CG  LYS B 802     5937   5923   7060    213   -688   -199       C  
ATOM   3518  CD  LYS B 802     -62.403  -3.143  10.823  1.00 56.61           C  
ANISOU 3518  CD  LYS B 802     6721   6808   7981    199   -676   -231       C  
ATOM   3519  CE  LYS B 802     -61.055  -3.299  10.103  1.00 59.21           C  
ANISOU 3519  CE  LYS B 802     6962   7126   8411    234   -661   -259       C  
ATOM   3520  NZ  LYS B 802     -61.179  -3.373   8.615  1.00 57.06           N  
ANISOU 3520  NZ  LYS B 802     6675   6850   8156    234   -566   -268       N  
ATOM   3521  N   VAL B 803     -65.924  -5.750  14.138  1.00 36.35           N  
ANISOU 3521  N   VAL B 803     4478   4236   5099    158   -832    -97       N  
ATOM   3522  CA  VAL B 803     -66.677  -5.552  15.343  1.00 36.27           C  
ANISOU 3522  CA  VAL B 803     4527   4251   5005    128   -867    -77       C  
ATOM   3523  C   VAL B 803     -66.360  -4.172  15.886  1.00 36.26           C  
ANISOU 3523  C   VAL B 803     4488   4280   5010    111   -872   -110       C  
ATOM   3524  O   VAL B 803     -65.210  -3.792  15.948  1.00 35.58           O  
ANISOU 3524  O   VAL B 803     4341   4188   4990    130   -904   -137       O  
ATOM   3525  CB  VAL B 803     -66.314  -6.601  16.408  1.00 37.43           C  
ANISOU 3525  CB  VAL B 803     4718   4375   5127    146   -958    -47       C  
ATOM   3526  CG1 VAL B 803     -67.079  -6.325  17.696  1.00 37.58           C  
ANISOU 3526  CG1 VAL B 803     4801   4427   5051    110   -990    -28       C  
ATOM   3527  CG2 VAL B 803     -66.611  -7.996  15.898  1.00 35.93           C  
ANISOU 3527  CG2 VAL B 803     4573   4144   4935    162   -956    -15       C  
ATOM   3528  N   VAL B 804     -67.388  -3.405  16.229  1.00 37.06           N  
ANISOU 3528  N   VAL B 804     4623   4413   5047     75   -836   -109       N  
ATOM   3529  CA  VAL B 804     -67.195  -2.122  16.900  1.00 39.58           C  
ANISOU 3529  CA  VAL B 804     4923   4754   5360     57   -843   -142       C  
ATOM   3530  C   VAL B 804     -67.127  -2.378  18.422  1.00 43.17           C  
ANISOU 3530  C   VAL B 804     5430   5222   5750     48   -924   -133       C  
ATOM   3531  O   VAL B 804     -68.032  -2.977  19.001  1.00 45.26           O  
ANISOU 3531  O   VAL B 804     5763   5498   5934     33   -929   -100       O  
ATOM   3532  CB  VAL B 804     -68.332  -1.138  16.560  1.00 38.15           C  
ANISOU 3532  CB  VAL B 804     4754   4597   5143     29   -763   -148       C  
ATOM   3533  CG1 VAL B 804     -68.214   0.134  17.395  1.00 36.42           C  
ANISOU 3533  CG1 VAL B 804     4533   4395   4911     11   -772   -185       C  
ATOM   3534  CG2 VAL B 804     -68.332  -0.806  15.063  1.00 36.65           C  
ANISOU 3534  CG2 VAL B 804     4514   4397   5014     35   -690   -154       C  
ATOM   3535  N   ASP B 805     -66.061  -1.910  19.055  1.00 47.49           N  
ANISOU 3535  N   ASP B 805     5943   5769   6330     54   -986   -162       N  
ATOM   3536  CA  ASP B 805     -65.842  -2.094  20.492  1.00 47.88           C  
ANISOU 3536  CA  ASP B 805     6039   5833   6319     44  -1072   -156       C  
ATOM   3537  C   ASP B 805     -67.014  -1.505  21.273  1.00 46.41           C  
ANISOU 3537  C   ASP B 805     5921   5680   6032      6  -1041   -158       C  
ATOM   3538  O   ASP B 805     -67.383  -0.348  21.066  1.00 49.97           O  
ANISOU 3538  O   ASP B 805     6358   6143   6487    -11   -983   -193       O  
ATOM   3539  CB  ASP B 805     -64.529  -1.397  20.888  1.00 53.10           C  
ANISOU 3539  CB  ASP B 805     6641   6496   7040     47  -1134   -196       C  
ATOM   3540  CG  ASP B 805     -64.160  -1.568  22.380  1.00 62.24           C  
ANISOU 3540  CG  ASP B 805     7843   7671   8134     36  -1237   -192       C  
ATOM   3541  OD1 ASP B 805     -63.270  -2.382  22.686  1.00 67.31           O  
ANISOU 3541  OD1 ASP B 805     8467   8300   8807     63  -1320   -171       O  
ATOM   3542  OD2 ASP B 805     -64.735  -0.883  23.255  1.00 65.85           O  
ANISOU 3542  OD2 ASP B 805     8353   8154   8512      0  -1236   -210       O  
ATOM   3543  N   ARG B 806     -67.588  -2.304  22.169  1.00 47.67           N  
ANISOU 3543  N   ARG B 806     6156   5852   6103     -5  -1077   -121       N  
ATOM   3544  CA  ARG B 806     -68.745  -1.911  22.995  1.00 50.49           C  
ANISOU 3544  CA  ARG B 806     6583   6246   6356    -40  -1045   -119       C  
ATOM   3545  C   ARG B 806     -68.532  -0.641  23.807  1.00 53.85           C  
ANISOU 3545  C   ARG B 806     7012   6694   6756    -61  -1055   -172       C  
ATOM   3546  O   ARG B 806     -69.483   0.066  24.091  1.00 50.54           O  
ANISOU 3546  O   ARG B 806     6625   6299   6280    -82   -995   -189       O  
ATOM   3547  CB  ARG B 806     -69.093  -3.041  23.974  1.00 53.38           C  
ANISOU 3547  CB  ARG B 806     7029   6621   6633    -50  -1101    -68       C  
ATOM   3548  N   ASP B 807     -67.278  -0.353  24.162  1.00 58.82           N  
ANISOU 3548  N   ASP B 807     7605   7314   7431    -54  -1130   -201       N  
ATOM   3549  CA  ASP B 807     -66.930   0.824  24.958  1.00 61.55           C  
ANISOU 3549  CA  ASP B 807     7955   7674   7756    -80  -1152   -256       C  
ATOM   3550  C   ASP B 807     -66.564   2.049  24.136  1.00 60.44           C  
ANISOU 3550  C   ASP B 807     7746   7516   7703    -81  -1100   -307       C  
ATOM   3551  O   ASP B 807     -66.266   3.081  24.722  1.00 65.66           O  
ANISOU 3551  O   ASP B 807     8410   8182   8354   -105  -1114   -358       O  
ATOM   3552  CB  ASP B 807     -65.743   0.520  25.869  1.00 67.84           C  
ANISOU 3552  CB  ASP B 807     8751   8475   8552    -81  -1273   -260       C  
ATOM   3553  CG  ASP B 807     -66.009  -0.625  26.821  1.00 71.29           C  
ANISOU 3553  CG  ASP B 807     9264   8927   8896    -83  -1338   -207       C  
ATOM   3554  OD1 ASP B 807     -67.161  -0.799  27.272  1.00 76.55           O  
ANISOU 3554  OD1 ASP B 807    10004   9616   9466   -103  -1293   -187       O  
ATOM   3555  OD2 ASP B 807     -65.051  -1.360  27.121  1.00 76.42           O  
ANISOU 3555  OD2 ASP B 807     9897   9566   9571    -63  -1434   -182       O  
ATOM   3556  N   SER B 808     -66.546   1.950  22.807  1.00 55.01           N  
ANISOU 3556  N   SER B 808     6999   6805   7096    -59  -1042   -295       N  
ATOM   3557  CA  SER B 808     -66.142   3.083  21.967  1.00 53.02           C  
ANISOU 3557  CA  SER B 808     6682   6534   6929    -63   -992   -336       C  
ATOM   3558  C   SER B 808     -67.206   4.151  21.983  1.00 54.09           C  
ANISOU 3558  C   SER B 808     6851   6675   7026    -80   -911   -361       C  
ATOM   3559  O   SER B 808     -68.353   3.895  22.375  1.00 51.54           O  
ANISOU 3559  O   SER B 808     6588   6374   6620    -84   -877   -340       O  
ATOM   3560  CB  SER B 808     -65.901   2.638  20.520  1.00 54.88           C  
ANISOU 3560  CB  SER B 808     6854   6748   7251    -36   -947   -312       C  
ATOM   3561  OG  SER B 808     -67.088   2.127  19.924  1.00 51.45           O  
ANISOU 3561  OG  SER B 808     6452   6318   6779    -28   -879   -274       O  
ATOM   3562  N   GLU B 809     -66.828   5.352  21.552  1.00 56.99           N  
ANISOU 3562  N   GLU B 809     7177   7022   7456    -91   -879   -403       N  
ATOM   3563  CA  GLU B 809     -67.793   6.448  21.434  1.00 58.59           C  
ANISOU 3563  CA  GLU B 809     7405   7219   7638   -100   -797   -427       C  
ATOM   3564  C   GLU B 809     -68.728   6.176  20.250  1.00 50.42           C  
ANISOU 3564  C   GLU B 809     6354   6183   6619    -79   -714   -385       C  
ATOM   3565  O   GLU B 809     -69.908   6.506  20.281  1.00 45.48           O  
ANISOU 3565  O   GLU B 809     5764   5570   5947    -76   -652   -378       O  
ATOM   3566  CB  GLU B 809     -67.082   7.800  21.303  1.00 63.40           C  
ANISOU 3566  CB  GLU B 809     7979   7796   8313   -121   -791   -482       C  
ATOM   3567  CG  GLU B 809     -68.022   9.005  21.327  1.00 69.48           C  
ANISOU 3567  CG  GLU B 809     8784   8553   9065   -126   -714   -511       C  
ATOM   3568  CD  GLU B 809     -67.306  10.346  21.074  1.00 74.53           C  
ANISOU 3568  CD  GLU B 809     9390   9147   9778   -149   -704   -562       C  
ATOM   3569  OE1 GLU B 809     -66.108  10.476  21.443  1.00 74.11           O  
ANISOU 3569  OE1 GLU B 809     9309   9086   9762   -174   -774   -592       O  
ATOM   3570  OE2 GLU B 809     -67.933  11.299  20.547  1.00 74.75           O  
ANISOU 3570  OE2 GLU B 809     9423   9148   9830   -144   -628   -572       O  
ATOM   3571  N   GLU B 810     -68.182   5.536  19.229  1.00 48.20           N  
ANISOU 3571  N   GLU B 810     6020   5890   6403    -64   -714   -357       N  
ATOM   3572  CA  GLU B 810     -68.955   5.086  18.074  1.00 46.45           C  
ANISOU 3572  CA  GLU B 810     5785   5670   6192    -47   -648   -314       C  
ATOM   3573  C   GLU B 810     -70.163   4.245  18.563  1.00 42.96           C  
ANISOU 3573  C   GLU B 810     5405   5260   5658    -45   -638   -277       C  
ATOM   3574  O   GLU B 810     -71.307   4.534  18.231  1.00 36.64           O  
ANISOU 3574  O   GLU B 810     4618   4473   4829    -44   -573   -262       O  
ATOM   3575  CB  GLU B 810     -68.012   4.272  17.179  1.00 47.73           C  
ANISOU 3575  CB  GLU B 810     5893   5818   6423    -31   -669   -296       C  
ATOM   3576  CG  GLU B 810     -68.467   4.003  15.761  1.00 50.17           C  
ANISOU 3576  CG  GLU B 810     6176   6121   6763    -19   -601   -265       C  
ATOM   3577  CD  GLU B 810     -67.348   3.405  14.903  1.00 53.49           C  
ANISOU 3577  CD  GLU B 810     6538   6524   7259     -4   -616   -261       C  
ATOM   3578  OE1 GLU B 810     -66.356   2.877  15.450  1.00 50.38           O  
ANISOU 3578  OE1 GLU B 810     6128   6126   6888      5   -685   -272       O  
ATOM   3579  OE2 GLU B 810     -67.443   3.470  13.658  1.00 62.98           O  
ANISOU 3579  OE2 GLU B 810     7710   7719   8500      1   -557   -249       O  
ATOM   3580  N   ALA B 811     -69.887   3.225  19.378  1.00 41.06           N  
ANISOU 3580  N   ALA B 811     5197   5031   5372    -46   -706   -261       N  
ATOM   3581  CA  ALA B 811     -70.924   2.352  19.878  1.00 39.64           C  
ANISOU 3581  CA  ALA B 811     5076   4880   5107    -51   -702   -222       C  
ATOM   3582  C   ALA B 811     -71.940   3.132  20.724  1.00 40.17           C  
ANISOU 3582  C   ALA B 811     5188   4974   5098    -67   -664   -240       C  
ATOM   3583  O   ALA B 811     -73.126   2.846  20.679  1.00 41.21           O  
ANISOU 3583  O   ALA B 811     5347   5133   5179    -71   -615   -211       O  
ATOM   3584  CB  ALA B 811     -70.317   1.191  20.663  1.00 41.33           C  
ANISOU 3584  CB  ALA B 811     5320   5094   5289    -51   -789   -200       C  
ATOM   3585  N   GLU B 812     -71.462   4.113  21.487  1.00 44.81           N  
ANISOU 3585  N   GLU B 812     5785   5557   5683    -77   -684   -292       N  
ATOM   3586  CA  GLU B 812     -72.302   4.925  22.392  1.00 46.83           C  
ANISOU 3586  CA  GLU B 812     6089   5834   5868    -89   -648   -322       C  
ATOM   3587  C   GLU B 812     -73.325   5.705  21.612  1.00 41.99           C  
ANISOU 3587  C   GLU B 812     5457   5221   5277    -76   -553   -321       C  
ATOM   3588  O   GLU B 812     -74.520   5.741  21.959  1.00 40.01           O  
ANISOU 3588  O   GLU B 812     5237   5001   4963    -76   -502   -310       O  
ATOM   3589  CB  GLU B 812     -71.434   5.938  23.232  1.00 52.49           C  
ANISOU 3589  CB  GLU B 812     6817   6535   6590   -104   -691   -387       C  
ATOM   3590  CG  GLU B 812     -70.889   5.360  24.543  1.00 57.96           C  
ANISOU 3590  CG  GLU B 812     7562   7250   7212   -124   -780   -393       C  
ATOM   3591  CD  GLU B 812     -69.780   6.202  25.177  1.00 65.43           C  
ANISOU 3591  CD  GLU B 812     8504   8177   8179   -143   -841   -454       C  
ATOM   3592  OE1 GLU B 812     -69.563   7.363  24.739  1.00 65.69           O  
ANISOU 3592  OE1 GLU B 812     8506   8180   8274   -145   -804   -498       O  
ATOM   3593  OE2 GLU B 812     -69.124   5.693  26.124  1.00 68.04           O  
ANISOU 3593  OE2 GLU B 812     8865   8523   8464   -159   -930   -455       O  
ATOM   3594  N   ILE B 813     -72.840   6.347  20.555  1.00 40.46           N  
ANISOU 3594  N   ILE B 813     5206   4992   5174    -64   -529   -331       N  
ATOM   3595  CA  ILE B 813     -73.699   7.105  19.641  1.00 37.89           C  
ANISOU 3595  CA  ILE B 813     4856   4660   4882    -48   -445   -323       C  
ATOM   3596  C   ILE B 813     -74.774   6.171  19.102  1.00 36.62           C  
ANISOU 3596  C   ILE B 813     4695   4533   4687    -42   -410   -264       C  
ATOM   3597  O   ILE B 813     -75.975   6.524  19.083  1.00 34.90           O  
ANISOU 3597  O   ILE B 813     4485   4339   4438    -34   -349   -253       O  
ATOM   3598  CB  ILE B 813     -72.871   7.744  18.493  1.00 38.40           C  
ANISOU 3598  CB  ILE B 813     4861   4682   5049    -43   -434   -332       C  
ATOM   3599  CG1 ILE B 813     -71.811   8.707  19.162  1.00 40.68           C  
ANISOU 3599  CG1 ILE B 813     5151   4937   5368    -59   -473   -394       C  
ATOM   3600  CG2 ILE B 813     -73.796   8.417  17.447  1.00 39.08           C  
ANISOU 3600  CG2 ILE B 813     4923   4762   5166    -25   -352   -310       C  
ATOM   3601  CD1 ILE B 813     -71.032   9.686  18.284  1.00 41.73           C  
ANISOU 3601  CD1 ILE B 813     5234   5023   5596    -62   -455   -415       C  
ATOM   3602  N   ILE B 814     -74.356   4.992  18.650  1.00 35.44           N  
ANISOU 3602  N   ILE B 814     4534   4385   4547    -46   -448   -228       N  
ATOM   3603  CA  ILE B 814     -75.286   4.061  18.004  1.00 34.99           C  
ANISOU 3603  CA  ILE B 814     4476   4353   4465    -47   -419   -174       C  
ATOM   3604  C   ILE B 814     -76.326   3.570  18.997  1.00 35.71           C  
ANISOU 3604  C   ILE B 814     4617   4487   4462    -61   -412   -155       C  
ATOM   3605  O   ILE B 814     -77.504   3.486  18.655  1.00 35.95           O  
ANISOU 3605  O   ILE B 814     4644   4549   4468    -63   -358   -125       O  
ATOM   3606  CB  ILE B 814     -74.529   2.903  17.319  1.00 35.57           C  
ANISOU 3606  CB  ILE B 814     4534   4409   4573    -47   -462   -146       C  
ATOM   3607  CG1 ILE B 814     -73.833   3.446  16.068  1.00 35.33           C  
ANISOU 3607  CG1 ILE B 814     4446   4347   4632    -34   -440   -156       C  
ATOM   3608  CG2 ILE B 814     -75.484   1.775  16.938  1.00 35.69           C  
ANISOU 3608  CG2 ILE B 814     4566   4449   4545    -58   -446    -93       C  
ATOM   3609  CD1 ILE B 814     -72.879   2.486  15.387  1.00 36.75           C  
ANISOU 3609  CD1 ILE B 814     4603   4504   4857    -28   -477   -144       C  
ATOM   3610  N   ARG B 815     -75.908   3.271  20.225  1.00 37.02           N  
ANISOU 3610  N   ARG B 815     4830   4661   4575    -74   -464   -172       N  
ATOM   3611  CA  ARG B 815     -76.852   2.853  21.275  1.00 39.51           C  
ANISOU 3611  CA  ARG B 815     5199   5020   4792    -93   -454   -156       C  
ATOM   3612  C   ARG B 815     -77.804   3.972  21.638  1.00 37.16           C  
ANISOU 3612  C   ARG B 815     4904   4746   4468    -85   -383   -185       C  
ATOM   3613  O   ARG B 815     -78.970   3.714  21.901  1.00 35.81           O  
ANISOU 3613  O   ARG B 815     4749   4619   4240    -94   -337   -160       O  
ATOM   3614  CB  ARG B 815     -76.140   2.331  22.538  1.00 42.50           C  
ANISOU 3614  CB  ARG B 815     5634   5402   5113   -110   -531   -166       C  
ATOM   3615  CG  ARG B 815     -75.550   0.931  22.398  1.00 43.77           C  
ANISOU 3615  CG  ARG B 815     5806   5548   5277   -117   -598   -122       C  
ATOM   3616  CD  ARG B 815     -75.093   0.385  23.764  1.00 45.75           C  
ANISOU 3616  CD  ARG B 815     6120   5809   5452   -135   -672   -120       C  
ATOM   3617  NE  ARG B 815     -74.148   1.299  24.386  1.00 45.26           N  
ANISOU 3617  NE  ARG B 815     6058   5735   5405   -131   -713   -177       N  
ATOM   3618  CZ  ARG B 815     -72.825   1.200  24.319  1.00 46.18           C  
ANISOU 3618  CZ  ARG B 815     6150   5819   5578   -120   -787   -191       C  
ATOM   3619  NH1 ARG B 815     -72.092   2.144  24.889  1.00 50.17           N  
ANISOU 3619  NH1 ARG B 815     6652   6317   6093   -124   -818   -246       N  
ATOM   3620  NH2 ARG B 815     -72.222   0.188  23.701  1.00 44.50           N  
ANISOU 3620  NH2 ARG B 815     5914   5581   5415   -106   -830   -154       N  
ATOM   3621  N   LYS B 816     -77.334   5.214  21.607  1.00 37.24           N  
ANISOU 3621  N   LYS B 816     4899   4727   4525    -69   -370   -237       N  
ATOM   3622  CA  LYS B 816     -78.241   6.362  21.846  1.00 41.52           C  
ANISOU 3622  CA  LYS B 816     5441   5280   5055    -52   -296   -268       C  
ATOM   3623  C   LYS B 816     -79.297   6.434  20.748  1.00 38.46           C  
ANISOU 3623  C   LYS B 816     5005   4907   4700    -34   -228   -226       C  
ATOM   3624  O   LYS B 816     -80.480   6.661  21.014  1.00 39.93           O  
ANISOU 3624  O   LYS B 816     5193   5132   4847    -26   -169   -218       O  
ATOM   3625  CB  LYS B 816     -77.495   7.726  21.904  1.00 47.91           C  
ANISOU 3625  CB  LYS B 816     6243   6041   5919    -39   -295   -331       C  
ATOM   3626  CG  LYS B 816     -78.080   8.778  22.880  1.00 55.41           C  
ANISOU 3626  CG  LYS B 816     7232   6998   6824    -30   -249   -386       C  
ATOM   3627  CD  LYS B 816     -77.359  10.137  22.763  1.00 58.72           C  
ANISOU 3627  CD  LYS B 816     7643   7357   7309    -19   -246   -447       C  
ATOM   3628  CE  LYS B 816     -77.490  11.133  23.962  1.00 62.96           C  
ANISOU 3628  CE  LYS B 816     8238   7887   7799    -20   -226   -521       C  
ATOM   3629  NZ  LYS B 816     -78.858  11.597  24.378  1.00 64.17           N  
ANISOU 3629  NZ  LYS B 816     8409   8069   7905      7   -140   -532       N  
ATOM   3630  N   TYR B 817     -78.865   6.252  19.504  1.00 34.22           N  
ANISOU 3630  N   TYR B 817     4423   4343   4235    -28   -238   -200       N  
ATOM   3631  CA  TYR B 817     -79.788   6.344  18.382  1.00 31.30           C  
ANISOU 3631  CA  TYR B 817     4008   3988   3897    -13   -183   -159       C  
ATOM   3632  C   TYR B 817     -80.877   5.297  18.593  1.00 31.03           C  
ANISOU 3632  C   TYR B 817     3984   4010   3795    -33   -168   -111       C  
ATOM   3633  O   TYR B 817     -82.082   5.577  18.414  1.00 28.08           O  
ANISOU 3633  O   TYR B 817     3588   3674   3408    -22   -110    -91       O  
ATOM   3634  CB  TYR B 817     -79.027   6.117  17.078  1.00 28.86           C  
ANISOU 3634  CB  TYR B 817     3660   3645   3661    -12   -204   -139       C  
ATOM   3635  CG  TYR B 817     -79.680   6.562  15.787  1.00 28.32           C  
ANISOU 3635  CG  TYR B 817     3543   3577   3639      5   -154   -107       C  
ATOM   3636  CD1 TYR B 817     -80.959   7.145  15.731  1.00 27.50           C  
ANISOU 3636  CD1 TYR B 817     3423   3503   3522     24    -94    -91       C  
ATOM   3637  CD2 TYR B 817     -79.011   6.342  14.587  1.00 27.26           C  
ANISOU 3637  CD2 TYR B 817     3378   3416   3561      3   -167    -88       C  
ATOM   3638  CE1 TYR B 817     -81.521   7.522  14.510  1.00 27.33           C  
ANISOU 3638  CE1 TYR B 817     3355   3483   3544     40    -58    -55       C  
ATOM   3639  CE2 TYR B 817     -79.554   6.716  13.384  1.00 26.09           C  
ANISOU 3639  CE2 TYR B 817     3193   3271   3449     14   -128    -56       C  
ATOM   3640  CZ  TYR B 817     -80.801   7.295  13.338  1.00 27.32           C  
ANISOU 3640  CZ  TYR B 817     3333   3455   3592     32    -77    -37       C  
ATOM   3641  OH  TYR B 817     -81.285   7.609  12.083  1.00 26.84           O  
ANISOU 3641  OH  TYR B 817     3233   3398   3566     42    -48      2       O  
ATOM   3642  N   VAL B 818     -80.467   4.082  18.960  1.00 31.84           N  
ANISOU 3642  N   VAL B 818     4120   4120   3859    -61   -223    -91       N  
ATOM   3643  CA  VAL B 818     -81.443   2.996  19.181  1.00 32.92           C  
ANISOU 3643  CA  VAL B 818     4273   4306   3931    -89   -213    -42       C  
ATOM   3644  C   VAL B 818     -82.414   3.351  20.324  1.00 34.70           C  
ANISOU 3644  C   VAL B 818     4523   4578   4082    -94   -169    -54       C  
ATOM   3645  O   VAL B 818     -83.626   3.195  20.199  1.00 37.65           O  
ANISOU 3645  O   VAL B 818     4876   5000   4429   -101   -118    -22       O  
ATOM   3646  CB  VAL B 818     -80.748   1.651  19.514  1.00 32.45           C  
ANISOU 3646  CB  VAL B 818     4255   4233   3840   -118   -284    -19       C  
ATOM   3647  CG1 VAL B 818     -81.778   0.624  19.968  1.00 31.76           C  
ANISOU 3647  CG1 VAL B 818     4197   4194   3678   -154   -273     28       C  
ATOM   3648  CG2 VAL B 818     -79.976   1.127  18.304  1.00 31.93           C  
ANISOU 3648  CG2 VAL B 818     4162   4127   3844   -113   -316     -3       C  
ATOM   3649  N   LYS B 819     -81.870   3.834  21.432  1.00 39.33           N  
ANISOU 3649  N   LYS B 819     5153   5155   4635    -91   -187   -102       N  
ATOM   3650  CA  LYS B 819     -82.656   4.112  22.637  1.00 43.66           C  
ANISOU 3650  CA  LYS B 819     5738   5749   5101    -98   -147   -121       C  
ATOM   3651  C   LYS B 819     -83.626   5.270  22.452  1.00 42.46           C  
ANISOU 3651  C   LYS B 819     5547   5615   4972    -63    -61   -143       C  
ATOM   3652  O   LYS B 819     -84.793   5.170  22.796  1.00 40.66           O  
ANISOU 3652  O   LYS B 819     5311   5441   4696    -67     -4   -124       O  
ATOM   3653  CB  LYS B 819     -81.721   4.442  23.782  1.00 49.14           C  
ANISOU 3653  CB  LYS B 819     6491   6424   5757   -103   -192   -174       C  
ATOM   3654  CG  LYS B 819     -82.370   4.542  25.151  1.00 57.46           C  
ANISOU 3654  CG  LYS B 819     7599   7525   6709   -119   -161   -195       C  
ATOM   3655  CD  LYS B 819     -81.560   5.507  26.020  1.00 61.13           C  
ANISOU 3655  CD  LYS B 819     8105   7961   7159   -110   -183   -270       C  
ATOM   3656  CE  LYS B 819     -82.033   5.547  27.478  1.00 62.64           C  
ANISOU 3656  CE  LYS B 819     8366   8200   7235   -131   -162   -298       C  
ATOM   3657  NZ  LYS B 819     -82.216   6.924  28.040  1.00 61.77           N  
ANISOU 3657  NZ  LYS B 819     8272   8082   7118   -105   -107   -375       N  
ATOM   3658  N   ASN B 820     -83.144   6.361  21.874  1.00 40.73           N  
ANISOU 3658  N   ASN B 820     5299   5347   4829    -28    -52   -178       N  
ATOM   3659  CA  ASN B 820     -83.979   7.538  21.715  1.00 40.44           C  
ANISOU 3659  CA  ASN B 820     5229   5314   4821     13     25   -201       C  
ATOM   3660  C   ASN B 820     -85.052   7.471  20.645  1.00 38.87           C  
ANISOU 3660  C   ASN B 820     4964   5145   4660     30     73   -147       C  
ATOM   3661  O   ASN B 820     -86.021   8.195  20.738  1.00 42.05           O  
ANISOU 3661  O   ASN B 820     5340   5571   5067     62    140   -154       O  
ATOM   3662  CB  ASN B 820     -83.124   8.745  21.416  1.00 39.68           C  
ANISOU 3662  CB  ASN B 820     5129   5150   4797     43     18   -252       C  
ATOM   3663  CG  ASN B 820     -82.361   9.217  22.612  1.00 41.00           C  
ANISOU 3663  CG  ASN B 820     5359   5295   4926     34     -9   -320       C  
ATOM   3664  OD1 ASN B 820     -82.577   8.749  23.712  1.00 46.86           O  
ANISOU 3664  OD1 ASN B 820     6150   6076   5581     11    -14   -331       O  
ATOM   3665  ND2 ASN B 820     -81.449  10.133  22.400  1.00 41.52           N  
ANISOU 3665  ND2 ASN B 820     5425   5297   5053     46    -28   -365       N  
ATOM   3666  N   THR B 821     -84.883   6.671  19.609  1.00 35.18           N  
ANISOU 3666  N   THR B 821     4468   4674   4224     11     39    -95       N  
ATOM   3667  CA  THR B 821     -85.823   6.743  18.479  1.00 34.91           C  
ANISOU 3667  CA  THR B 821     4369   4665   4232     26     77    -46       C  
ATOM   3668  C   THR B 821     -86.763   5.552  18.407  1.00 34.39           C  
ANISOU 3668  C   THR B 821     4289   4663   4115    -12     82     12       C  
ATOM   3669  O   THR B 821     -87.350   5.257  17.364  1.00 34.11           O  
ANISOU 3669  O   THR B 821     4205   4648   4108    -16     89     60       O  
ATOM   3670  CB  THR B 821     -85.073   6.940  17.128  1.00 34.59           C  
ANISOU 3670  CB  THR B 821     4298   4573   4271     36     47    -32       C  
ATOM   3671  OG1 THR B 821     -84.348   5.749  16.768  1.00 31.87           O  
ANISOU 3671  OG1 THR B 821     3972   4220   3918     -3    -13     -7       O  
ATOM   3672  CG2 THR B 821     -84.111   8.109  17.238  1.00 33.15           C  
ANISOU 3672  CG2 THR B 821     4129   4325   4139     65     42    -87       C  
ATOM   3673  N   HIS B 822     -86.889   4.831  19.510  1.00 38.72           N  
ANISOU 3673  N   HIS B 822     4884   5244   4585    -46     73      9       N  
ATOM   3674  CA  HIS B 822     -87.895   3.787  19.598  1.00 40.82           C  
ANISOU 3674  CA  HIS B 822     5139   5573   4797    -87     87     62       C  
ATOM   3675  C   HIS B 822     -89.250   4.480  19.730  1.00 41.66           C  
ANISOU 3675  C   HIS B 822     5192   5736   4900    -61    169     67       C  
ATOM   3676  O   HIS B 822     -89.440   5.242  20.641  1.00 42.59           O  
ANISOU 3676  O   HIS B 822     5326   5863   4993    -34    212     23       O  
ATOM   3677  CB  HIS B 822     -87.646   2.892  20.804  1.00 41.68           C  
ANISOU 3677  CB  HIS B 822     5319   5699   4820   -131     59     61       C  
ATOM   3678  CG  HIS B 822     -88.462   1.647  20.770  1.00 42.95           C  
ANISOU 3678  CG  HIS B 822     5477   5909   4932   -185     59    122       C  
ATOM   3679  ND1 HIS B 822     -87.900   0.390  20.781  1.00 44.71           N  
ANISOU 3679  ND1 HIS B 822     5747   6111   5128   -231     -5    152       N  
ATOM   3680  CD2 HIS B 822     -89.797   1.467  20.648  1.00 41.43           C  
ANISOU 3680  CD2 HIS B 822     5237   5783   4720   -202    114    160       C  
ATOM   3681  CE1 HIS B 822     -88.860  -0.512  20.695  1.00 43.48           C  
ANISOU 3681  CE1 HIS B 822     5580   6004   4936   -279     11    206       C  
ATOM   3682  NE2 HIS B 822     -90.016   0.118  20.594  1.00 40.20           N  
ANISOU 3682  NE2 HIS B 822     5104   5646   4525   -264     82    211       N  
ATOM   3683  N   ALA B 823     -90.173   4.234  18.812  1.00 43.68           N  
ANISOU 3683  N   ALA B 823     5383   6031   5182    -66    189    119       N  
ATOM   3684  CA  ALA B 823     -91.451   4.944  18.812  1.00 44.86           C  
ANISOU 3684  CA  ALA B 823     5467   6235   5344    -33    263    128       C  
ATOM   3685  C   ALA B 823     -92.370   4.467  19.955  1.00 51.82           C  
ANISOU 3685  C   ALA B 823     6356   7189   6143    -63    311    134       C  
ATOM   3686  O   ALA B 823     -92.373   3.299  20.306  1.00 49.69           O  
ANISOU 3686  O   ALA B 823     6122   6943   5815   -125    282    164       O  
ATOM   3687  CB  ALA B 823     -92.157   4.751  17.485  1.00 42.61           C  
ANISOU 3687  CB  ALA B 823     5107   5975   5106    -36    261    186       C  
ATOM   3688  N   THR B 824     -93.163   5.390  20.485  1.00 54.81           N  
ANISOU 3688  N   THR B 824     6701   7602   6523    -18    386    108       N  
ATOM   3689  CA  THR B 824     -94.142   5.120  21.542  1.00 58.69           C  
ANISOU 3689  CA  THR B 824     7188   8171   6941    -39    449    110       C  
ATOM   3690  C   THR B 824     -95.146   4.025  21.187  1.00 57.93           C  
ANISOU 3690  C   THR B 824     7042   8148   6820    -98    454    182       C  
ATOM   3691  O   THR B 824     -95.534   3.244  22.043  1.00 57.71           O  
ANISOU 3691  O   THR B 824     7042   8170   6714   -151    471    197       O  
ATOM   3692  CB  THR B 824     -94.916   6.433  21.825  1.00 59.43           C  
ANISOU 3692  CB  THR B 824     7230   8284   7067     36    536     71       C  
ATOM   3693  OG1 THR B 824     -94.103   7.267  22.647  1.00 59.92           O  
ANISOU 3693  OG1 THR B 824     7361   8290   7115     71    543     -6       O  
ATOM   3694  CG2 THR B 824     -96.301   6.240  22.497  1.00 66.38           C  
ANISOU 3694  CG2 THR B 824     8060   9263   7899     26    620     89       C  
ATOM   3695  N   THR B 825     -95.591   4.006  19.938  1.00 55.06           N  
ANISOU 3695  N   THR B 825     6605   7794   6522    -91    440    228       N  
ATOM   3696  CA  THR B 825     -96.617   3.061  19.516  1.00 53.06           C  
ANISOU 3696  CA  THR B 825     6294   7613   6252   -148    444    295       C  
ATOM   3697  C   THR B 825     -96.082   1.679  19.169  1.00 52.19           C  
ANISOU 3697  C   THR B 825     6237   7482   6111   -228    368    334       C  
ATOM   3698  O   THR B 825     -96.850   0.806  18.812  1.00 48.32           O  
ANISOU 3698  O   THR B 825     5710   7043   5605   -287    363    388       O  
ATOM   3699  CB  THR B 825     -97.389   3.563  18.284  1.00 52.56           C  
ANISOU 3699  CB  THR B 825     6128   7575   6267   -114    453    333       C  
ATOM   3700  OG1 THR B 825     -96.490   3.712  17.179  1.00 51.17           O  
ANISOU 3700  OG1 THR B 825     5969   7328   6147    -98    388    335       O  
ATOM   3701  CG2 THR B 825     -98.088   4.893  18.585  1.00 52.80           C  
ANISOU 3701  CG2 THR B 825     6095   7629   6337    -29    532    303       C  
ATOM   3702  N   HIS B 826     -94.772   1.485  19.225  1.00 54.42           N  
ANISOU 3702  N   HIS B 826     6600   7687   6390   -230    308    306       N  
ATOM   3703  CA  HIS B 826     -94.196   0.174  18.933  1.00 53.58           C  
ANISOU 3703  CA  HIS B 826     6549   7552   6259   -297    237    338       C  
ATOM   3704  C   HIS B 826     -93.794  -0.462  20.259  1.00 54.39           C  
ANISOU 3704  C   HIS B 826     6737   7650   6277   -336    229    325       C  
ATOM   3705  O   HIS B 826     -92.615  -0.705  20.530  1.00 47.28           O  
ANISOU 3705  O   HIS B 826     5911   6687   5368   -335    174    300       O  
ATOM   3706  CB  HIS B 826     -93.007   0.324  17.981  1.00 50.17           C  
ANISOU 3706  CB  HIS B 826     6140   7037   5886   -271    174    321       C  
ATOM   3707  CG  HIS B 826     -93.385   0.875  16.644  1.00 52.43           C  
ANISOU 3707  CG  HIS B 826     6350   7326   6243   -241    178    341       C  
ATOM   3708  ND1 HIS B 826     -92.554   1.691  15.904  1.00 51.61           N  
ANISOU 3708  ND1 HIS B 826     6244   7162   6204   -189    158    314       N  
ATOM   3709  CD2 HIS B 826     -94.529   0.754  15.929  1.00 54.00           C  
ANISOU 3709  CD2 HIS B 826     6472   7586   6458   -258    199    388       C  
ATOM   3710  CE1 HIS B 826     -93.162   2.027  14.779  1.00 55.84           C  
ANISOU 3710  CE1 HIS B 826     6710   7719   6787   -174    165    346       C  
ATOM   3711  NE2 HIS B 826     -94.360   1.463  14.765  1.00 54.75           N  
ANISOU 3711  NE2 HIS B 826     6525   7655   6622   -215    186    391       N  
ATOM   3712  N   ASN B 827     -94.804  -0.694  21.091  1.00 55.93           N  
ANISOU 3712  N   ASN B 827     6917   7920   6413   -368    286    343       N  
ATOM   3713  CA  ASN B 827     -94.593  -1.038  22.505  1.00 57.71           C  
ANISOU 3713  CA  ASN B 827     7222   8157   6550   -397    297    327       C  
ATOM   3714  C   ASN B 827     -94.560  -2.546  22.757  1.00 53.48           C  
ANISOU 3714  C   ASN B 827     6743   7622   5953   -484    252    380       C  
ATOM   3715  O   ASN B 827     -94.369  -2.978  23.870  1.00 54.07           O  
ANISOU 3715  O   ASN B 827     6890   7704   5950   -517    251    379       O  
ATOM   3716  CB  ASN B 827     -95.621  -0.313  23.412  1.00 61.00           C  
ANISOU 3716  CB  ASN B 827     7599   8651   6927   -377    395    307       C  
ATOM   3717  CG  ASN B 827     -97.061  -0.496  22.955  1.00 66.07           C  
ANISOU 3717  CG  ASN B 827     8142   9378   7585   -401    452    356       C  
ATOM   3718  OD1 ASN B 827     -97.362  -1.226  21.997  1.00 67.84           O  
ANISOU 3718  OD1 ASN B 827     8329   9607   7839   -443    415    408       O  
ATOM   3719  ND2 ASN B 827     -97.963   0.174  23.647  1.00 66.82           N  
ANISOU 3719  ND2 ASN B 827     8191   9541   7657   -374    542    337       N  
ATOM   3720  N   ALA B 828     -94.722  -3.338  21.705  1.00 54.17           N  
ANISOU 3720  N   ALA B 828     6806   7698   6078   -523    212    427       N  
ATOM   3721  CA  ALA B 828     -94.641  -4.797  21.783  1.00 52.33           C  
ANISOU 3721  CA  ALA B 828     6633   7450   5801   -605    162    477       C  
ATOM   3722  C   ALA B 828     -93.263  -5.322  22.212  1.00 49.99           C  
ANISOU 3722  C   ALA B 828     6440   7070   5482   -605     87    461       C  
ATOM   3723  O   ALA B 828     -93.166  -6.467  22.633  1.00 48.98           O  
ANISOU 3723  O   ALA B 828     6378   6928   5304   -668     52    500       O  
ATOM   3724  CB  ALA B 828     -95.034  -5.405  20.436  1.00 53.69           C  
ANISOU 3724  CB  ALA B 828     6757   7619   6025   -640    133    519       C  
ATOM   3725  N   TYR B 829     -92.204  -4.507  22.112  1.00 46.01           N  
ANISOU 3725  N   TYR B 829     5951   6511   5020   -536     60    408       N  
ATOM   3726  CA  TYR B 829     -90.852  -4.956  22.475  1.00 46.54           C  
ANISOU 3726  CA  TYR B 829     6103   6502   5076   -531    -16    392       C  
ATOM   3727  C   TYR B 829     -89.937  -3.787  22.891  1.00 45.81           C  
ANISOU 3727  C   TYR B 829     6023   6380   5004   -460    -20    324       C  
ATOM   3728  O   TYR B 829     -90.236  -2.653  22.601  1.00 46.03           O  
ANISOU 3728  O   TYR B 829     5992   6426   5073   -412     28    290       O  
ATOM   3729  CB  TYR B 829     -90.242  -5.763  21.312  1.00 44.46           C  
ANISOU 3729  CB  TYR B 829     5847   6175   4872   -542    -82    414       C  
ATOM   3730  CG  TYR B 829     -90.167  -4.986  20.007  1.00 45.73           C  
ANISOU 3730  CG  TYR B 829     5933   6321   5119   -494    -73    392       C  
ATOM   3731  CD1 TYR B 829     -89.136  -4.075  19.777  1.00 45.55           C  
ANISOU 3731  CD1 TYR B 829     5907   6250   5149   -428    -91    340       C  
ATOM   3732  CD2 TYR B 829     -91.130  -5.145  19.006  1.00 45.45           C  
ANISOU 3732  CD2 TYR B 829     5833   6323   5113   -518    -48    425       C  
ATOM   3733  CE1 TYR B 829     -89.066  -3.342  18.596  1.00 46.29           C  
ANISOU 3733  CE1 TYR B 829     5938   6330   5319   -387    -81    324       C  
ATOM   3734  CE2 TYR B 829     -91.074  -4.401  17.826  1.00 46.82           C  
ANISOU 3734  CE2 TYR B 829     5943   6487   5360   -475    -41    409       C  
ATOM   3735  CZ  TYR B 829     -90.029  -3.496  17.629  1.00 45.20           C  
ANISOU 3735  CZ  TYR B 829     5740   6230   5203   -409    -56    360       C  
ATOM   3736  OH  TYR B 829     -89.911  -2.760  16.469  1.00 42.11           O  
ANISOU 3736  OH  TYR B 829     5294   5825   4882   -369    -51    348       O  
ATOM   3737  N   ASP B 830     -88.845  -4.087  23.590  1.00 47.22           N  
ANISOU 3737  N   ASP B 830     6277   6509   5153   -458    -81    308       N  
ATOM   3738  CA  ASP B 830     -87.719  -3.152  23.721  1.00 52.26           C  
ANISOU 3738  CA  ASP B 830     6927   7102   5829   -399   -109    247       C  
ATOM   3739  C   ASP B 830     -86.530  -3.795  22.993  1.00 47.93           C  
ANISOU 3739  C   ASP B 830     6399   6475   5336   -391   -193    254       C  
ATOM   3740  O   ASP B 830     -86.538  -4.994  22.676  1.00 48.35           O  
ANISOU 3740  O   ASP B 830     6478   6510   5383   -431   -230    302       O  
ATOM   3741  CB  ASP B 830     -87.386  -2.672  25.167  1.00 58.24           C  
ANISOU 3741  CB  ASP B 830     7744   7873   6511   -393   -106    208       C  
ATOM   3742  CG  ASP B 830     -87.343  -3.787  26.172  1.00 68.26           C  
ANISOU 3742  CG  ASP B 830     9095   9153   7687   -449   -143    250       C  
ATOM   3743  OD1 ASP B 830     -86.263  -4.414  26.292  1.00 77.26           O  
ANISOU 3743  OD1 ASP B 830    10288  10236   8830   -452   -227    258       O  
ATOM   3744  OD2 ASP B 830     -88.369  -4.004  26.879  1.00 75.33           O  
ANISOU 3744  OD2 ASP B 830    10003  10114   8506   -490    -86    274       O  
ATOM   3745  N   LEU B 831     -85.549  -2.977  22.653  1.00 41.92           N  
ANISOU 3745  N   LEU B 831     5621   5670   4637   -339   -217    205       N  
ATOM   3746  CA  LEU B 831     -84.441  -3.443  21.858  1.00 40.66           C  
ANISOU 3746  CA  LEU B 831     5465   5442   4541   -324   -283    205       C  
ATOM   3747  C   LEU B 831     -83.184  -3.368  22.661  1.00 41.86           C  
ANISOU 3747  C   LEU B 831     5668   5555   4684   -306   -347    174       C  
ATOM   3748  O   LEU B 831     -82.962  -2.430  23.422  1.00 40.48           O  
ANISOU 3748  O   LEU B 831     5501   5392   4488   -285   -336    129       O  
ATOM   3749  CB  LEU B 831     -84.251  -2.600  20.607  1.00 39.04           C  
ANISOU 3749  CB  LEU B 831     5190   5216   4427   -283   -261    179       C  
ATOM   3750  CG  LEU B 831     -85.293  -2.743  19.505  1.00 38.89           C  
ANISOU 3750  CG  LEU B 831     5115   5226   4435   -297   -216    214       C  
ATOM   3751  CD1 LEU B 831     -85.181  -1.642  18.460  1.00 37.51           C  
ANISOU 3751  CD1 LEU B 831     4874   5039   4337   -252   -187    187       C  
ATOM   3752  CD2 LEU B 831     -85.178  -4.121  18.884  1.00 38.34           C  
ANISOU 3752  CD2 LEU B 831     5070   5130   4368   -336   -259    258       C  
ATOM   3753  N   GLU B 832     -82.347  -4.360  22.459  1.00 41.38           N  
ANISOU 3753  N   GLU B 832     5639   5444   4641   -313   -417    196       N  
ATOM   3754  CA  GLU B 832     -81.078  -4.412  23.110  1.00 45.04           C  
ANISOU 3754  CA  GLU B 832     6141   5868   5106   -293   -491    173       C  
ATOM   3755  C   GLU B 832     -80.050  -4.718  22.031  1.00 43.39           C  
ANISOU 3755  C   GLU B 832     5901   5596   4989   -263   -535    167       C  
ATOM   3756  O   GLU B 832     -80.162  -5.712  21.286  1.00 42.54           O  
ANISOU 3756  O   GLU B 832     5795   5463   4903   -278   -547    204       O  
ATOM   3757  CB  GLU B 832     -81.120  -5.513  24.165  1.00 49.69           C  
ANISOU 3757  CB  GLU B 832     6810   6461   5611   -333   -537    218       C  
ATOM   3758  CG  GLU B 832     -79.778  -5.952  24.705  1.00 56.72           C  
ANISOU 3758  CG  GLU B 832     7743   7303   6507   -316   -632    214       C  
ATOM   3759  CD  GLU B 832     -79.885  -6.991  25.832  1.00 62.58           C  
ANISOU 3759  CD  GLU B 832     8572   8051   7156   -356   -679    265       C  
ATOM   3760  OE1 GLU B 832     -80.960  -7.636  26.025  1.00 62.22           O  
ANISOU 3760  OE1 GLU B 832     8555   8036   7050   -404   -641    313       O  
ATOM   3761  OE2 GLU B 832     -78.861  -7.152  26.521  1.00 62.66           O  
ANISOU 3761  OE2 GLU B 832     8618   8033   7155   -341   -757    260       O  
ATOM   3762  N   VAL B 833     -79.036  -3.883  21.964  1.00 40.61           N  
ANISOU 3762  N   VAL B 833     5521   5218   4690   -225   -558    118       N  
ATOM   3763  CA  VAL B 833     -77.987  -4.070  20.988  1.00 40.24           C  
ANISOU 3763  CA  VAL B 833     5439   5117   4732   -194   -593    107       C  
ATOM   3764  C   VAL B 833     -77.050  -5.161  21.473  1.00 40.05           C  
ANISOU 3764  C   VAL B 833     5461   5053   4703   -192   -679    129       C  
ATOM   3765  O   VAL B 833     -76.511  -5.071  22.563  1.00 44.69           O  
ANISOU 3765  O   VAL B 833     6085   5643   5252   -191   -730    119       O  
ATOM   3766  CB  VAL B 833     -77.228  -2.750  20.763  1.00 39.39           C  
ANISOU 3766  CB  VAL B 833     5283   4999   4687   -159   -585     48       C  
ATOM   3767  CG1 VAL B 833     -76.068  -2.955  19.802  1.00 38.76           C  
ANISOU 3767  CG1 VAL B 833     5162   4867   4698   -130   -620     36       C  
ATOM   3768  CG2 VAL B 833     -78.188  -1.680  20.243  1.00 39.19           C  
ANISOU 3768  CG2 VAL B 833     5215   5005   4671   -155   -501     32       C  
ATOM   3769  N   ILE B 834     -76.854  -6.198  20.673  1.00 40.98           N  
ANISOU 3769  N   ILE B 834     5581   5132   4859   -191   -698    158       N  
ATOM   3770  CA  ILE B 834     -75.950  -7.275  21.051  1.00 41.04           C  
ANISOU 3770  CA  ILE B 834     5628   5091   4873   -180   -780    182       C  
ATOM   3771  C   ILE B 834     -74.581  -6.986  20.478  1.00 41.38           C  
ANISOU 3771  C   ILE B 834     5621   5092   5010   -131   -816    144       C  
ATOM   3772  O   ILE B 834     -73.612  -6.933  21.219  1.00 42.63           O  
ANISOU 3772  O   ILE B 834     5787   5237   5175   -111   -882    131       O  
ATOM   3773  CB  ILE B 834     -76.460  -8.635  20.565  1.00 42.89           C  
ANISOU 3773  CB  ILE B 834     5901   5297   5097   -204   -783    233       C  
ATOM   3774  CG1 ILE B 834     -77.764  -8.978  21.261  1.00 45.82           C  
ANISOU 3774  CG1 ILE B 834     6323   5714   5373   -260   -752    275       C  
ATOM   3775  CG2 ILE B 834     -75.456  -9.748  20.851  1.00 42.98           C  
ANISOU 3775  CG2 ILE B 834     5953   5247   5131   -182   -867    256       C  
ATOM   3776  CD1 ILE B 834     -78.461 -10.145  20.605  1.00 48.54           C  
ANISOU 3776  CD1 ILE B 834     6695   6036   5713   -295   -739    321       C  
ATOM   3777  N   ASP B 835     -74.503  -6.851  19.152  1.00 40.28           N  
ANISOU 3777  N   ASP B 835     5428   4935   4941   -115   -774    128       N  
ATOM   3778  CA  ASP B 835     -73.258  -6.566  18.459  1.00 39.60           C  
ANISOU 3778  CA  ASP B 835     5286   4813   4948    -71   -793     92       C  
ATOM   3779  C   ASP B 835     -73.463  -5.429  17.482  1.00 38.43           C  
ANISOU 3779  C   ASP B 835     5074   4683   4843    -66   -722     57       C  
ATOM   3780  O   ASP B 835     -74.524  -5.303  16.860  1.00 40.11           O  
ANISOU 3780  O   ASP B 835     5283   4920   5036    -89   -661     71       O  
ATOM   3781  CB  ASP B 835     -72.749  -7.782  17.678  1.00 42.86           C  
ANISOU 3781  CB  ASP B 835     5704   5171   5410    -51   -817    110       C  
ATOM   3782  CG  ASP B 835     -72.326  -8.944  18.570  1.00 48.85           C  
ANISOU 3782  CG  ASP B 835     6523   5895   6142    -45   -897    146       C  
ATOM   3783  OD1 ASP B 835     -72.736 -10.088  18.260  1.00 54.28           O  
ANISOU 3783  OD1 ASP B 835     7256   6551   6817    -58   -900    182       O  
ATOM   3784  OD2 ASP B 835     -71.568  -8.725  19.551  1.00 53.57           O  
ANISOU 3784  OD2 ASP B 835     7125   6495   6734    -29   -959    139       O  
ATOM   3785  N   ILE B 836     -72.410  -4.637  17.315  1.00 36.26           N  
ANISOU 3785  N   ILE B 836     4747   4396   4634    -37   -734     16       N  
ATOM   3786  CA  ILE B 836     -72.369  -3.584  16.311  1.00 34.05           C  
ANISOU 3786  CA  ILE B 836     4407   4123   4409    -30   -674    -15       C  
ATOM   3787  C   ILE B 836     -71.217  -3.884  15.381  1.00 33.45           C  
ANISOU 3787  C   ILE B 836     4283   4007   4418      1   -685    -32       C  
ATOM   3788  O   ILE B 836     -70.089  -4.036  15.823  1.00 32.79           O  
ANISOU 3788  O   ILE B 836     4183   3902   4373     25   -743    -48       O  
ATOM   3789  CB  ILE B 836     -72.175  -2.206  16.941  1.00 33.41           C  
ANISOU 3789  CB  ILE B 836     4305   4063   4329    -31   -668    -53       C  
ATOM   3790  CG1 ILE B 836     -73.288  -1.921  17.943  1.00 31.90           C  
ANISOU 3790  CG1 ILE B 836     4162   3911   4048    -57   -652    -42       C  
ATOM   3791  CG2 ILE B 836     -72.181  -1.131  15.858  1.00 32.27           C  
ANISOU 3791  CG2 ILE B 836     4103   3918   4242    -24   -604    -77       C  
ATOM   3792  CD1 ILE B 836     -73.046  -0.681  18.778  1.00 33.39           C  
ANISOU 3792  CD1 ILE B 836     4346   4114   4228    -58   -656    -85       C  
ATOM   3793  N   PHE B 837     -71.524  -4.012  14.093  1.00 32.37           N  
ANISOU 3793  N   PHE B 837     4125   3865   4310      1   -631    -27       N  
ATOM   3794  CA  PHE B 837     -70.526  -4.286  13.097  1.00 31.77           C  
ANISOU 3794  CA  PHE B 837     4005   3756   4311     29   -626    -45       C  
ATOM   3795  C   PHE B 837     -70.389  -3.088  12.152  1.00 32.26           C  
ANISOU 3795  C   PHE B 837     4009   3829   4418     28   -564    -71       C  
ATOM   3796  O   PHE B 837     -71.384  -2.466  11.736  1.00 31.43           O  
ANISOU 3796  O   PHE B 837     3907   3751   4284      6   -511    -61       O  
ATOM   3797  CB  PHE B 837     -70.915  -5.504  12.279  1.00 31.84           C  
ANISOU 3797  CB  PHE B 837     4044   3742   4311     26   -611    -21       C  
ATOM   3798  CG  PHE B 837     -71.101  -6.767  13.084  1.00 34.28           C  
ANISOU 3798  CG  PHE B 837     4418   4030   4578     23   -668     10       C  
ATOM   3799  CD1 PHE B 837     -70.007  -7.600  13.384  1.00 34.61           C  
ANISOU 3799  CD1 PHE B 837     4461   4028   4662     61   -728      6       C  
ATOM   3800  CD2 PHE B 837     -72.362  -7.155  13.498  1.00 33.42           C  
ANISOU 3800  CD2 PHE B 837     4366   3943   4391    -16   -660     47       C  
ATOM   3801  CE1 PHE B 837     -70.179  -8.766  14.107  1.00 35.38           C  
ANISOU 3801  CE1 PHE B 837     4623   4098   4722     59   -782     41       C  
ATOM   3802  CE2 PHE B 837     -72.544  -8.338  14.201  1.00 35.90           C  
ANISOU 3802  CE2 PHE B 837     4743   4233   4664    -24   -709     81       C  
ATOM   3803  CZ  PHE B 837     -71.451  -9.137  14.526  1.00 35.17           C  
ANISOU 3803  CZ  PHE B 837     4660   4091   4613     14   -772     80       C  
ATOM   3804  N   LYS B 838     -69.155  -2.777  11.797  1.00 32.81           N  
ANISOU 3804  N   LYS B 838     4024   3879   4562     52   -572   -102       N  
ATOM   3805  CA  LYS B 838     -68.856  -1.790  10.781  1.00 34.58           C  
ANISOU 3805  CA  LYS B 838     4194   4108   4838     50   -514   -123       C  
ATOM   3806  C   LYS B 838     -68.685  -2.549   9.504  1.00 33.31           C  
ANISOU 3806  C   LYS B 838     4023   3930   4702     60   -477   -119       C  
ATOM   3807  O   LYS B 838     -67.883  -3.468   9.448  1.00 39.39           O  
ANISOU 3807  O   LYS B 838     4786   4673   5506     87   -507   -127       O  
ATOM   3808  CB  LYS B 838     -67.581  -1.036  11.133  1.00 38.97           C  
ANISOU 3808  CB  LYS B 838     4693   4655   5460     63   -540   -159       C  
ATOM   3809  CG  LYS B 838     -67.190   0.030  10.132  1.00 44.91           C  
ANISOU 3809  CG  LYS B 838     5388   5407   6267     55   -480   -179       C  
ATOM   3810  CD  LYS B 838     -66.159   0.985  10.722  1.00 52.52           C  
ANISOU 3810  CD  LYS B 838     6304   6366   7285     53   -509   -213       C  
ATOM   3811  CE  LYS B 838     -65.908   2.240   9.867  1.00 58.62           C  
ANISOU 3811  CE  LYS B 838     7029   7137   8105     35   -447   -228       C  
ATOM   3812  NZ  LYS B 838     -65.938   2.039   8.384  1.00 60.59           N  
ANISOU 3812  NZ  LYS B 838     7259   7386   8377     37   -380   -216       N  
ATOM   3813  N   ILE B 839     -69.403  -2.151   8.463  1.00 31.32           N  
ANISOU 3813  N   ILE B 839     3770   3694   4436     41   -414   -108       N  
ATOM   3814  CA  ILE B 839     -69.366  -2.880   7.201  1.00 30.29           C  
ANISOU 3814  CA  ILE B 839     3641   3552   4316     44   -376   -106       C  
ATOM   3815  C   ILE B 839     -68.967  -2.041   6.002  1.00 30.87           C  
ANISOU 3815  C   ILE B 839     3667   3633   4431     39   -313   -120       C  
ATOM   3816  O   ILE B 839     -69.348  -0.857   5.879  1.00 30.56           O  
ANISOU 3816  O   ILE B 839     3610   3613   4388     22   -283   -114       O  
ATOM   3817  CB  ILE B 839     -70.712  -3.547   6.905  1.00 30.22           C  
ANISOU 3817  CB  ILE B 839     3690   3558   4235     17   -362    -72       C  
ATOM   3818  CG1 ILE B 839     -71.858  -2.548   6.926  1.00 30.54           C  
ANISOU 3818  CG1 ILE B 839     3733   3637   4233    -11   -331    -49       C  
ATOM   3819  CG2 ILE B 839     -70.978  -4.653   7.932  1.00 30.47           C  
ANISOU 3819  CG2 ILE B 839     3774   3574   4229     19   -421    -55       C  
ATOM   3820  CD1 ILE B 839     -73.152  -3.159   6.443  1.00 32.76           C  
ANISOU 3820  CD1 ILE B 839     4056   3939   4451    -41   -314    -15       C  
ATOM   3821  N   GLU B 840     -68.180  -2.642   5.117  1.00 29.79           N  
ANISOU 3821  N   GLU B 840     3510   3477   4333     57   -291   -139       N  
ATOM   3822  CA  GLU B 840     -67.755  -1.979   3.874  1.00 32.32           C  
ANISOU 3822  CA  GLU B 840     3789   3805   4687     49   -225   -151       C  
ATOM   3823  C   GLU B 840     -67.931  -2.991   2.773  1.00 31.76           C  
ANISOU 3823  C   GLU B 840     3747   3726   4594     49   -191   -151       C  
ATOM   3824  O   GLU B 840     -67.154  -3.942   2.645  1.00 31.58           O  
ANISOU 3824  O   GLU B 840     3720   3675   4603     79   -201   -175       O  
ATOM   3825  CB  GLU B 840     -66.286  -1.527   3.917  1.00 36.70           C  
ANISOU 3825  CB  GLU B 840     4273   4347   5326     71   -224   -185       C  
ATOM   3826  CG  GLU B 840     -65.960  -0.574   5.058  1.00 41.26           C  
ANISOU 3826  CG  GLU B 840     4821   4927   5927     68   -266   -192       C  
ATOM   3827  CD  GLU B 840     -64.449  -0.347   5.278  1.00 50.28           C  
ANISOU 3827  CD  GLU B 840     5891   6058   7156     88   -283   -227       C  
ATOM   3828  OE1 GLU B 840     -63.586  -0.997   4.601  1.00 50.95           O  
ANISOU 3828  OE1 GLU B 840     5941   6131   7287    113   -262   -246       O  
ATOM   3829  OE2 GLU B 840     -64.132   0.484   6.179  1.00 54.02           O  
ANISOU 3829  OE2 GLU B 840     6341   6534   7650     79   -319   -237       O  
ATOM   3830  N   ARG B 841     -68.971  -2.799   1.980  1.00 31.34           N  
ANISOU 3830  N   ARG B 841     3725   3696   4486     17   -154   -126       N  
ATOM   3831  CA  ARG B 841     -69.157  -3.626   0.803  1.00 31.23           C  
ANISOU 3831  CA  ARG B 841     3742   3679   4445      8   -117   -130       C  
ATOM   3832  C   ARG B 841     -68.136  -3.229  -0.274  1.00 29.82           C  
ANISOU 3832  C   ARG B 841     3517   3500   4314     16    -57   -158       C  
ATOM   3833  O   ARG B 841     -67.972  -2.069  -0.579  1.00 29.10           O  
ANISOU 3833  O   ARG B 841     3388   3428   4241      3    -25   -151       O  
ATOM   3834  CB  ARG B 841     -70.578  -3.481   0.268  1.00 29.84           C  
ANISOU 3834  CB  ARG B 841     3608   3536   4194    -33   -101    -93       C  
ATOM   3835  CG  ARG B 841     -71.692  -3.945   1.197  1.00 31.05           C  
ANISOU 3835  CG  ARG B 841     3805   3696   4296    -48   -149    -63       C  
ATOM   3836  CD  ARG B 841     -72.820  -4.607   0.397  1.00 32.07           C  
ANISOU 3836  CD  ARG B 841     3984   3844   4357    -86   -137    -40       C  
ATOM   3837  NE  ARG B 841     -73.211  -3.716  -0.618  1.00 35.49           N  
ANISOU 3837  NE  ARG B 841     4400   4312   4773   -108    -92    -23       N  
ATOM   3838  CZ  ARG B 841     -73.085  -3.848  -1.930  1.00 33.35           C  
ANISOU 3838  CZ  ARG B 841     4138   4048   4486   -123    -49    -31       C  
ATOM   3839  NH1 ARG B 841     -72.735  -4.960  -2.534  1.00 30.53           N  
ANISOU 3839  NH1 ARG B 841     3815   3667   4120   -124    -40    -59       N  
ATOM   3840  NH2 ARG B 841     -73.417  -2.786  -2.640  1.00 36.21           N  
ANISOU 3840  NH2 ARG B 841     4478   4443   4837   -140    -15     -6       N  
ATOM   3841  N   GLU B 842     -67.518  -4.209  -0.877  1.00 31.00           N  
ANISOU 3841  N   GLU B 842     3673   3626   4478     36    -38   -188       N  
ATOM   3842  CA  GLU B 842     -66.632  -3.976  -2.006  1.00 35.65           C  
ANISOU 3842  CA  GLU B 842     4225   4219   5101     41     29   -216       C  
ATOM   3843  C   GLU B 842     -67.326  -3.224  -3.155  1.00 32.28           C  
ANISOU 3843  C   GLU B 842     3814   3830   4622     -3     86   -191       C  
ATOM   3844  O   GLU B 842     -68.450  -3.553  -3.567  1.00 29.24           O  
ANISOU 3844  O   GLU B 842     3486   3459   4164    -33     83   -166       O  
ATOM   3845  CB  GLU B 842     -66.050  -5.298  -2.503  1.00 39.72           C  
ANISOU 3845  CB  GLU B 842     4759   4702   5629     71     44   -254       C  
ATOM   3846  CG  GLU B 842     -64.956  -5.778  -1.586  1.00 46.03           C  
ANISOU 3846  CG  GLU B 842     5516   5467   6506    125      2   -282       C  
ATOM   3847  CD  GLU B 842     -64.498  -7.193  -1.896  1.00 53.07           C  
ANISOU 3847  CD  GLU B 842     6436   6316   7414    164      6   -316       C  
ATOM   3848  OE1 GLU B 842     -64.714  -7.662  -3.040  1.00 54.97           O  
ANISOU 3848  OE1 GLU B 842     6714   6555   7617    151     61   -334       O  
ATOM   3849  OE2 GLU B 842     -63.910  -7.810  -0.982  1.00 51.68           O  
ANISOU 3849  OE2 GLU B 842     6246   6105   7287    209    -49   -326       O  
ATOM   3850  N   GLY B 843     -66.681  -2.144  -3.569  1.00 31.35           N  
ANISOU 3850  N   GLY B 843     3642   3727   4542    -11    129   -192       N  
ATOM   3851  CA  GLY B 843     -67.176  -1.356  -4.657  1.00 29.90           C  
ANISOU 3851  CA  GLY B 843     3470   3575   4316    -50    182   -165       C  
ATOM   3852  C   GLY B 843     -68.160  -0.285  -4.240  1.00 28.50           C  
ANISOU 3852  C   GLY B 843     3300   3417   4113    -74    159   -117       C  
ATOM   3853  O   GLY B 843     -68.519   0.560  -5.057  1.00 30.47           O  
ANISOU 3853  O   GLY B 843     3551   3689   4336   -103    198    -87       O  
ATOM   3854  N   GLU B 844     -68.669  -0.321  -3.016  1.00 26.10           N  
ANISOU 3854  N   GLU B 844     3004   3105   3809    -63     98   -106       N  
ATOM   3855  CA  GLU B 844     -69.776   0.593  -2.702  1.00 26.39           C  
ANISOU 3855  CA  GLU B 844     3053   3162   3813    -83     83    -62       C  
ATOM   3856  C   GLU B 844     -69.288   2.024  -2.527  1.00 26.37           C  
ANISOU 3856  C   GLU B 844     3004   3154   3860    -85    101    -55       C  
ATOM   3857  O   GLU B 844     -70.029   2.967  -2.876  1.00 26.94           O  
ANISOU 3857  O   GLU B 844     3084   3242   3910   -105    118    -16       O  
ATOM   3858  CB  GLU B 844     -70.541   0.175  -1.462  1.00 27.02           C  
ANISOU 3858  CB  GLU B 844     3157   3238   3870    -73     21    -52       C  
ATOM   3859  CG  GLU B 844     -72.018   0.580  -1.495  1.00 28.07           C  
ANISOU 3859  CG  GLU B 844     3320   3402   3944    -96     13     -5       C  
ATOM   3860  CD  GLU B 844     -72.788   0.111  -0.280  1.00 30.73           C  
ANISOU 3860  CD  GLU B 844     3680   3741   4255    -91    -40      4       C  
ATOM   3861  OE1 GLU B 844     -72.399   0.541   0.831  1.00 32.39           O  
ANISOU 3861  OE1 GLU B 844     3870   3936   4500    -72    -67    -10       O  
ATOM   3862  OE2 GLU B 844     -73.735  -0.718  -0.423  1.00 28.85           O  
ANISOU 3862  OE2 GLU B 844     3481   3520   3959   -109    -55     24       O  
ATOM   3863  N   CYS B 845     -68.083   2.199  -1.969  1.00 25.15           N  
ANISOU 3863  N   CYS B 845     2802   2977   3777    -67     95    -91       N  
ATOM   3864  CA  CYS B 845     -67.521   3.536  -1.786  1.00 28.73           C  
ANISOU 3864  CA  CYS B 845     3211   3421   4283    -76    111    -90       C  
ATOM   3865  C   CYS B 845     -67.404   4.202  -3.161  1.00 27.52           C  
ANISOU 3865  C   CYS B 845     3053   3281   4124   -104    180    -68       C  
ATOM   3866  O   CYS B 845     -67.816   5.332  -3.356  1.00 24.70           O  
ANISOU 3866  O   CYS B 845     2697   2923   3766   -123    197    -35       O  
ATOM   3867  CB  CYS B 845     -66.136   3.522  -1.086  1.00 29.27           C  
ANISOU 3867  CB  CYS B 845     3223   3468   4431    -58     92   -134       C  
ATOM   3868  SG  CYS B 845     -65.318   5.172  -1.028  1.00 35.58           S  
ANISOU 3868  SG  CYS B 845     3965   4253   5302    -83    119   -136       S  
ATOM   3869  N   GLN B 846     -66.839   3.477  -4.103  1.00 29.55           N  
ANISOU 3869  N   GLN B 846     3305   3546   4375   -106    221    -86       N  
ATOM   3870  CA  GLN B 846     -66.677   3.978  -5.458  1.00 32.54           C  
ANISOU 3870  CA  GLN B 846     3685   3942   4738   -135    291    -67       C  
ATOM   3871  C   GLN B 846     -68.054   4.277  -6.094  1.00 29.95           C  
ANISOU 3871  C   GLN B 846     3412   3638   4331   -159    294    -13       C  
ATOM   3872  O   GLN B 846     -68.224   5.294  -6.738  1.00 28.21           O  
ANISOU 3872  O   GLN B 846     3191   3423   4104   -183    327     24       O  
ATOM   3873  CB  GLN B 846     -65.837   2.997  -6.296  1.00 35.86           C  
ANISOU 3873  CB  GLN B 846     4096   4369   5159   -128    336   -105       C  
ATOM   3874  CG  GLN B 846     -65.440   3.485  -7.695  1.00 39.79           C  
ANISOU 3874  CG  GLN B 846     4589   4887   5642   -161    417    -93       C  
ATOM   3875  CD  GLN B 846     -64.499   4.695  -7.675  1.00 44.16           C  
ANISOU 3875  CD  GLN B 846     5081   5430   6266   -179    451    -90       C  
ATOM   3876  OE1 GLN B 846     -63.646   4.847  -6.777  1.00 44.30           O  
ANISOU 3876  OE1 GLN B 846     5042   5428   6362   -161    427   -121       O  
ATOM   3877  NE2 GLN B 846     -64.664   5.576  -8.657  1.00 44.66           N  
ANISOU 3877  NE2 GLN B 846     5157   5508   6303   -218    504    -50       N  
ATOM   3878  N   ARG B 847     -69.022   3.392  -5.893  1.00 28.01           N  
ANISOU 3878  N   ARG B 847     3211   3404   4029   -152    256     -6       N  
ATOM   3879  CA  ARG B 847     -70.359   3.594  -6.430  1.00 28.38           C  
ANISOU 3879  CA  ARG B 847     3302   3479   4004   -173    250     46       C  
ATOM   3880  C   ARG B 847     -71.044   4.800  -5.796  1.00 27.40           C  
ANISOU 3880  C   ARG B 847     3167   3349   3894   -171    227     85       C  
ATOM   3881  O   ARG B 847     -71.718   5.586  -6.481  1.00 27.75           O  
ANISOU 3881  O   ARG B 847     3225   3410   3909   -189    245    135       O  
ATOM   3882  CB  ARG B 847     -71.201   2.320  -6.249  1.00 31.67           C  
ANISOU 3882  CB  ARG B 847     3762   3909   4362   -171    210     41       C  
ATOM   3883  CG  ARG B 847     -72.601   2.368  -6.864  1.00 32.01           C  
ANISOU 3883  CG  ARG B 847     3845   3989   4329   -198    200     92       C  
ATOM   3884  CD  ARG B 847     -73.344   1.080  -6.561  1.00 31.77           C  
ANISOU 3884  CD  ARG B 847     3853   3967   4250   -201    159     83       C  
ATOM   3885  NE  ARG B 847     -73.835   1.062  -5.184  1.00 32.86           N  
ANISOU 3885  NE  ARG B 847     3983   4096   4407   -181    108     86       N  
ATOM   3886  CZ  ARG B 847     -74.686   0.167  -4.695  1.00 32.79           C  
ANISOU 3886  CZ  ARG B 847     4003   4096   4358   -188     67     92       C  
ATOM   3887  NH1 ARG B 847     -75.119  -0.794  -5.452  1.00 33.92           N  
ANISOU 3887  NH1 ARG B 847     4187   4254   4446   -215     66     91       N  
ATOM   3888  NH2 ARG B 847     -75.114   0.247  -3.436  1.00 36.22           N  
ANISOU 3888  NH2 ARG B 847     4429   4526   4807   -172     28     97       N  
ATOM   3889  N   TYR B 848     -70.831   4.989  -4.505  1.00 25.16           N  
ANISOU 3889  N   TYR B 848     2861   3041   3657   -147    190     63       N  
ATOM   3890  CA  TYR B 848     -71.446   6.098  -3.802  1.00 25.67           C  
ANISOU 3890  CA  TYR B 848     2920   3096   3738   -140    172     90       C  
ATOM   3891  C   TYR B 848     -70.813   7.475  -4.080  1.00 27.03           C  
ANISOU 3891  C   TYR B 848     3065   3242   3963   -151    207    101       C  
ATOM   3892  O   TYR B 848     -71.436   8.502  -3.828  1.00 25.19           O  
ANISOU 3892  O   TYR B 848     2836   2998   3738   -148    203    132       O  
ATOM   3893  CB  TYR B 848     -71.379   5.801  -2.311  1.00 25.40           C  
ANISOU 3893  CB  TYR B 848     2878   3045   3728   -116    121     57       C  
ATOM   3894  CG  TYR B 848     -72.063   6.777  -1.399  1.00 24.87           C  
ANISOU 3894  CG  TYR B 848     2811   2967   3671   -104    100     73       C  
ATOM   3895  CD1 TYR B 848     -73.445   6.900  -1.401  1.00 23.93           C  
ANISOU 3895  CD1 TYR B 848     2717   2873   3504   -101     90    115       C  
ATOM   3896  CD2 TYR B 848     -71.333   7.553  -0.506  1.00 24.46           C  
ANISOU 3896  CD2 TYR B 848     2734   2881   3679    -96     89     43       C  
ATOM   3897  CE1 TYR B 848     -74.085   7.756  -0.540  1.00 23.70           C  
ANISOU 3897  CE1 TYR B 848     2686   2833   3485    -84     76    124       C  
ATOM   3898  CE2 TYR B 848     -71.971   8.444   0.350  1.00 23.78           C  
ANISOU 3898  CE2 TYR B 848     2655   2782   3600    -84     74     51       C  
ATOM   3899  CZ  TYR B 848     -73.351   8.541   0.319  1.00 25.03           C  
ANISOU 3899  CZ  TYR B 848     2838   2964   3710    -75     70     91       C  
ATOM   3900  OH  TYR B 848     -74.032   9.427   1.125  1.00 25.94           O  
ANISOU 3900  OH  TYR B 848     2958   3065   3832    -57     63     97       O  
ATOM   3901  N   LYS B 849     -69.589   7.473  -4.603  1.00 30.69           N  
ANISOU 3901  N   LYS B 849     3500   3696   4466   -164    245     75       N  
ATOM   3902  CA  LYS B 849     -68.749   8.664  -4.743  1.00 33.51           C  
ANISOU 3902  CA  LYS B 849     3824   4024   4884   -181    278     77       C  
ATOM   3903  C   LYS B 849     -69.465   9.876  -5.337  1.00 31.91           C  
ANISOU 3903  C   LYS B 849     3643   3815   4668   -197    301    136       C  
ATOM   3904  O   LYS B 849     -69.406  10.949  -4.756  1.00 32.60           O  
ANISOU 3904  O   LYS B 849     3719   3866   4801   -196    294    141       O  
ATOM   3905  CB  LYS B 849     -67.516   8.321  -5.581  1.00 38.99           C  
ANISOU 3905  CB  LYS B 849     4487   4724   5602   -199    328     51       C  
ATOM   3906  CG  LYS B 849     -66.474   9.422  -5.747  1.00 44.64           C  
ANISOU 3906  CG  LYS B 849     5160   5413   6387   -225    367     48       C  
ATOM   3907  CD  LYS B 849     -65.284   8.889  -6.565  1.00 50.66           C  
ANISOU 3907  CD  LYS B 849     5887   6193   7170   -240    421     19       C  
ATOM   3908  CE  LYS B 849     -64.175   9.926  -6.871  1.00 56.22           C  
ANISOU 3908  CE  LYS B 849     6540   6877   7942   -275    470     18       C  
ATOM   3909  NZ  LYS B 849     -63.668   9.916  -8.280  1.00 55.14           N  
ANISOU 3909  NZ  LYS B 849     6400   6765   7784   -307    550     33       N  
ATOM   3910  N   PRO B 850     -70.149   9.712  -6.478  1.00 31.36           N  
ANISOU 3910  N   PRO B 850     3604   3775   4534   -212    324    181       N  
ATOM   3911  CA  PRO B 850     -70.872  10.862  -7.017  1.00 33.76           C  
ANISOU 3911  CA  PRO B 850     3929   4072   4827   -222    338    245       C  
ATOM   3912  C   PRO B 850     -71.892  11.486  -6.056  1.00 35.82           C  
ANISOU 3912  C   PRO B 850     4198   4314   5097   -192    296    264       C  
ATOM   3913  O   PRO B 850     -72.115  12.697  -6.114  1.00 35.13           O  
ANISOU 3913  O   PRO B 850     4115   4194   5038   -192    307    300       O  
ATOM   3914  CB  PRO B 850     -71.604  10.297  -8.243  1.00 33.18           C  
ANISOU 3914  CB  PRO B 850     3891   4045   4669   -238    351    287       C  
ATOM   3915  CG  PRO B 850     -70.894   9.040  -8.574  1.00 32.89           C  
ANISOU 3915  CG  PRO B 850     3851   4032   4612   -246    367    238       C  
ATOM   3916  CD  PRO B 850     -70.381   8.504  -7.274  1.00 31.84           C  
ANISOU 3916  CD  PRO B 850     3690   3878   4529   -219    332    178       C  
ATOM   3917  N   PHE B 851     -72.483  10.677  -5.174  1.00 34.90           N  
ANISOU 3917  N   PHE B 851     4087   4216   4959   -167    252    240       N  
ATOM   3918  CA  PHE B 851     -73.530  11.177  -4.299  1.00 35.27           C  
ANISOU 3918  CA  PHE B 851     4141   4255   5007   -138    219    256       C  
ATOM   3919  C   PHE B 851     -73.014  11.690  -3.010  1.00 35.95           C  
ANISOU 3919  C   PHE B 851     4209   4298   5151   -122    202    211       C  
ATOM   3920  O   PHE B 851     -73.724  12.442  -2.360  1.00 36.55           O  
ANISOU 3920  O   PHE B 851     4293   4355   5240    -99    189    223       O  
ATOM   3921  CB  PHE B 851     -74.572  10.125  -4.032  1.00 35.41           C  
ANISOU 3921  CB  PHE B 851     4174   4317   4964   -125    184    261       C  
ATOM   3922  CG  PHE B 851     -75.381   9.822  -5.224  1.00 38.27           C  
ANISOU 3922  CG  PHE B 851     4556   4722   5263   -141    192    314       C  
ATOM   3923  CD1 PHE B 851     -76.340  10.747  -5.683  1.00 38.70           C  
ANISOU 3923  CD1 PHE B 851     4616   4781   5306   -133    194    378       C  
ATOM   3924  CD2 PHE B 851     -75.101   8.713  -5.973  1.00 38.88           C  
ANISOU 3924  CD2 PHE B 851     4647   4830   5295   -165    199    302       C  
ATOM   3925  CE1 PHE B 851     -77.042  10.512  -6.842  1.00 38.65           C  
ANISOU 3925  CE1 PHE B 851     4627   4818   5239   -151    196    431       C  
ATOM   3926  CE2 PHE B 851     -75.808   8.468  -7.122  1.00 41.22           C  
ANISOU 3926  CE2 PHE B 851     4966   5167   5527   -187    204    349       C  
ATOM   3927  CZ  PHE B 851     -76.778   9.362  -7.561  1.00 41.13           C  
ANISOU 3927  CZ  PHE B 851     4959   5167   5501   -182    200    415       C  
ATOM   3928  N   LYS B 852     -71.752  11.404  -2.707  1.00 39.81           N  
ANISOU 3928  N   LYS B 852     4674   4770   5680   -134    205    160       N  
ATOM   3929  CA  LYS B 852     -71.072  12.023  -1.597  1.00 43.85           C  
ANISOU 3929  CA  LYS B 852     5169   5240   6254   -129    188    116       C  
ATOM   3930  C   LYS B 852     -71.058  13.544  -1.729  1.00 43.57           C  
ANISOU 3930  C   LYS B 852     5136   5156   6263   -137    213    140       C  
ATOM   3931  O   LYS B 852     -70.975  14.226  -0.730  1.00 47.80           O  
ANISOU 3931  O   LYS B 852     5672   5655   6836   -128    194    112       O  
ATOM   3932  CB  LYS B 852     -69.650  11.449  -1.497  1.00 49.68           C  
ANISOU 3932  CB  LYS B 852     5871   5975   7030   -145    188     67       C  
ATOM   3933  CG  LYS B 852     -68.899  11.689  -0.200  1.00 53.12           C  
ANISOU 3933  CG  LYS B 852     6284   6381   7517   -141    152     12       C  
ATOM   3934  CD  LYS B 852     -69.475  10.903   0.952  1.00 53.92           C  
ANISOU 3934  CD  LYS B 852     6404   6500   7584   -113     99    -11       C  
ATOM   3935  CE  LYS B 852     -68.876  11.361   2.280  1.00 59.02           C  
ANISOU 3935  CE  LYS B 852     7038   7116   8272   -111     60    -59       C  
ATOM   3936  NZ  LYS B 852     -69.647  10.828   3.455  1.00 54.19           N  
ANISOU 3936  NZ  LYS B 852     6455   6519   7615    -86     14    -74       N  
ATOM   3937  N   GLN B 853     -71.197  14.074  -2.950  1.00 45.62           N  
ANISOU 3937  N   GLN B 853     5405   5415   6516   -155    253    193       N  
ATOM   3938  CA  GLN B 853     -71.132  15.528  -3.196  1.00 47.75           C  
ANISOU 3938  CA  GLN B 853     5681   5630   6830   -166    279    223       C  
ATOM   3939  C   GLN B 853     -72.466  16.202  -2.857  1.00 45.54           C  
ANISOU 3939  C   GLN B 853     5430   5336   6537   -129    264    260       C  
ATOM   3940  O   GLN B 853     -72.558  17.406  -2.605  1.00 48.17           O  
ANISOU 3940  O   GLN B 853     5775   5612   6915   -122    273    270       O  
ATOM   3941  CB  GLN B 853     -70.772  15.815  -4.699  1.00 52.14           C  
ANISOU 3941  CB  GLN B 853     6241   6192   7377   -202    328    274       C  
ATOM   3942  CG  GLN B 853     -69.856  17.019  -4.883  1.00 58.62           C  
ANISOU 3942  CG  GLN B 853     7053   6953   8266   -236    362    278       C  
ATOM   3943  CD  GLN B 853     -68.528  16.852  -4.174  1.00 62.59           C  
ANISOU 3943  CD  GLN B 853     7514   7441   8827   -259    357    208       C  
ATOM   3944  OE1 GLN B 853     -68.140  15.742  -3.824  1.00 56.45           O  
ANISOU 3944  OE1 GLN B 853     6712   6701   8034   -251    338    164       O  
ATOM   3945  NE2 GLN B 853     -67.814  17.962  -3.972  1.00 67.50           N  
ANISOU 3945  NE2 GLN B 853     8126   8003   9516   -288    373    200       N  
ATOM   3946  N   LEU B 854     -73.512  15.397  -2.830  1.00 44.02           N  
ANISOU 3946  N   LEU B 854     5247   5194   6285   -103    242    277       N  
ATOM   3947  CA  LEU B 854     -74.849  15.866  -2.541  1.00 40.61           C  
ANISOU 3947  CA  LEU B 854     4830   4763   5837    -64    229    313       C  
ATOM   3948  C   LEU B 854     -74.977  16.267  -1.083  1.00 40.35           C  
ANISOU 3948  C   LEU B 854     4799   4697   5836    -36    208    262       C  
ATOM   3949  O   LEU B 854     -74.296  15.746  -0.180  1.00 40.71           O  
ANISOU 3949  O   LEU B 854     4835   4742   5890    -43    188    201       O  
ATOM   3950  CB  LEU B 854     -75.827  14.754  -2.805  1.00 40.80           C  
ANISOU 3950  CB  LEU B 854     4856   4857   5789    -53    208    336       C  
ATOM   3951  CG  LEU B 854     -77.177  15.052  -3.402  1.00 41.01           C  
ANISOU 3951  CG  LEU B 854     4890   4910   5782    -30    205    406       C  
ATOM   3952  CD1 LEU B 854     -77.061  15.922  -4.639  1.00 43.89           C  
ANISOU 3952  CD1 LEU B 854     5267   5253   6157    -45    233    468       C  
ATOM   3953  CD2 LEU B 854     -77.835  13.727  -3.731  1.00 40.21           C  
ANISOU 3953  CD2 LEU B 854     4787   4882   5608    -38    182    417       C  
ATOM   3954  N   HIS B 855     -75.801  17.261  -0.843  1.00 40.24           N  
ANISOU 3954  N   HIS B 855     4798   4650   5841     -2    214    288       N  
ATOM   3955  CA  HIS B 855     -75.998  17.747   0.506  1.00 41.52           C  
ANISOU 3955  CA  HIS B 855     4967   4778   6029     26    202    238       C  
ATOM   3956  C   HIS B 855     -77.019  16.839   1.207  1.00 39.51           C  
ANISOU 3956  C   HIS B 855     4709   4584   5719     56    178    230       C  
ATOM   3957  O   HIS B 855     -77.584  15.951   0.581  1.00 43.02           O  
ANISOU 3957  O   HIS B 855     5144   5088   6112     52    170    266       O  
ATOM   3958  CB  HIS B 855     -76.460  19.204   0.467  1.00 44.36           C  
ANISOU 3958  CB  HIS B 855     5347   5072   6438     54    225    266       C  
ATOM   3959  CG  HIS B 855     -77.746  19.406  -0.263  1.00 49.41           C  
ANISOU 3959  CG  HIS B 855     5985   5736   7053     91    232    341       C  
ATOM   3960  ND1 HIS B 855     -77.882  19.174  -1.619  1.00 52.62           N  
ANISOU 3960  ND1 HIS B 855     6387   6174   7432     72    239    409       N  
ATOM   3961  CD2 HIS B 855     -78.963  19.805   0.178  1.00 50.02           C  
ANISOU 3961  CD2 HIS B 855     6062   5815   7129    145    232    358       C  
ATOM   3962  CE1 HIS B 855     -79.131  19.414  -1.978  1.00 52.09           C  
ANISOU 3962  CE1 HIS B 855     6316   6129   7347    112    235    468       C  
ATOM   3963  NE2 HIS B 855     -79.803  19.805  -0.910  1.00 51.34           N  
ANISOU 3963  NE2 HIS B 855     6220   6016   7272    159    233    439       N  
ATOM   3964  N   ASN B 856     -77.238  17.071   2.498  1.00 37.44           N  
ANISOU 3964  N   ASN B 856     4456   4305   5465     80    168    181       N  
ATOM   3965  CA  ASN B 856     -78.290  16.406   3.260  1.00 36.10           C  
ANISOU 3965  CA  ASN B 856     4284   4187   5246    109    153    174       C  
ATOM   3966  C   ASN B 856     -78.109  14.869   3.234  1.00 35.56           C  
ANISOU 3966  C   ASN B 856     4207   4183   5122     82    125    166       C  
ATOM   3967  O   ASN B 856     -78.977  14.103   2.794  1.00 37.55           O  
ANISOU 3967  O   ASN B 856     4449   4492   5326     85    119    206       O  
ATOM   3968  CB  ASN B 856     -79.644  16.837   2.723  1.00 35.97           C  
ANISOU 3968  CB  ASN B 856     4258   4189   5220    148    170    238       C  
ATOM   3969  CG  ASN B 856     -80.774  16.354   3.564  1.00 36.96           C  
ANISOU 3969  CG  ASN B 856     4374   4365   5304    179    163    231       C  
ATOM   3970  OD1 ASN B 856     -80.599  16.007   4.730  1.00 39.46           O  
ANISOU 3970  OD1 ASN B 856     4702   4686   5605    178    152    174       O  
ATOM   3971  ND2 ASN B 856     -81.963  16.302   2.975  1.00 38.01           N  
ANISOU 3971  ND2 ASN B 856     4485   4540   5416    204    169    292       N  
ATOM   3972  N   ARG B 857     -76.952  14.458   3.718  1.00 33.22           N  
ANISOU 3972  N   ARG B 857     3913   3872   4837     54    106    115       N  
ATOM   3973  CA  ARG B 857     -76.607  13.074   3.890  1.00 31.63           C  
ANISOU 3973  CA  ARG B 857     3708   3714   4595     34     77     97       C  
ATOM   3974  C   ARG B 857     -76.925  12.638   5.298  1.00 30.59           C  
ANISOU 3974  C   ARG B 857     3591   3600   4433     47     51     56       C  
ATOM   3975  O   ARG B 857     -76.507  13.270   6.257  1.00 30.00           O  
ANISOU 3975  O   ARG B 857     3528   3489   4382     52     45     10       O  
ATOM   3976  CB  ARG B 857     -75.137  12.871   3.561  1.00 33.18           C  
ANISOU 3976  CB  ARG B 857     3893   3887   4826      1     71     69       C  
ATOM   3977  CG  ARG B 857     -74.949  12.855   2.071  1.00 34.88           C  
ANISOU 3977  CG  ARG B 857     4097   4109   5046    -17     98    114       C  
ATOM   3978  CD  ARG B 857     -73.581  13.156   1.524  1.00 36.05           C  
ANISOU 3978  CD  ARG B 857     4229   4225   5244    -47    114     97       C  
ATOM   3979  NE  ARG B 857     -72.486  13.124   2.448  1.00 37.45           N  
ANISOU 3979  NE  ARG B 857     4395   4377   5459    -58     90     37       N  
ATOM   3980  CZ  ARG B 857     -71.780  14.177   2.835  1.00 43.50           C  
ANISOU 3980  CZ  ARG B 857     5155   5091   6282    -70     96      9       C  
ATOM   3981  NH1 ARG B 857     -72.061  15.423   2.403  1.00 40.08           N  
ANISOU 3981  NH1 ARG B 857     4733   4616   5881    -69    128     37       N  
ATOM   3982  NH2 ARG B 857     -70.771  13.965   3.692  1.00 47.44           N  
ANISOU 3982  NH2 ARG B 857     5639   5578   6808    -83     64    -46       N  
ATOM   3983  N   ARG B 858     -77.685  11.555   5.419  1.00 28.71           N  
ANISOU 3983  N   ARG B 858     3355   3417   4137     47     36     74       N  
ATOM   3984  CA  ARG B 858     -78.238  11.155   6.701  1.00 29.15           C  
ANISOU 3984  CA  ARG B 858     3426   3496   4153     59     19     48       C  
ATOM   3985  C   ARG B 858     -77.995   9.659   7.007  1.00 28.32           C  
ANISOU 3985  C   ARG B 858     3332   3428   4002     36    -18     40       C  
ATOM   3986  O   ARG B 858     -78.133   8.807   6.101  1.00 28.12           O  
ANISOU 3986  O   ARG B 858     3299   3429   3956     19    -21     73       O  
ATOM   3987  CB  ARG B 858     -79.744  11.421   6.701  1.00 33.12           C  
ANISOU 3987  CB  ARG B 858     3922   4034   4629     86     43     87       C  
ATOM   3988  CG  ARG B 858     -80.231  12.045   7.978  1.00 38.37           C  
ANISOU 3988  CG  ARG B 858     4601   4690   5287    113     54     51       C  
ATOM   3989  CD  ARG B 858     -81.654  12.606   7.920  1.00 39.42           C  
ANISOU 3989  CD  ARG B 858     4716   4848   5413    150     89     87       C  
ATOM   3990  NE  ARG B 858     -81.727  13.934   7.297  1.00 41.57           N  
ANISOU 3990  NE  ARG B 858     4979   5071   5744    179    119    104       N  
ATOM   3991  CZ  ARG B 858     -82.797  14.726   7.310  1.00 40.16           C  
ANISOU 3991  CZ  ARG B 858     4785   4894   5579    223    151    128       C  
ATOM   3992  NH1 ARG B 858     -83.923  14.343   7.914  1.00 40.20           N  
ANISOU 3992  NH1 ARG B 858     4776   4955   5543    243    162    135       N  
ATOM   3993  NH2 ARG B 858     -82.749  15.905   6.698  1.00 38.56           N  
ANISOU 3993  NH2 ARG B 858     4579   4637   5433    249    173    147       N  
ATOM   3994  N   LEU B 859     -77.677   9.368   8.271  1.00 27.26           N  
ANISOU 3994  N   LEU B 859     3218   3291   3850     35    -46     -3       N  
ATOM   3995  CA  LEU B 859     -77.535   8.020   8.779  1.00 28.52           C  
ANISOU 3995  CA  LEU B 859     3394   3478   3964     18    -84     -8       C  
ATOM   3996  C   LEU B 859     -78.893   7.487   9.246  1.00 27.07           C  
ANISOU 3996  C   LEU B 859     3222   3345   3718     20    -78     19       C  
ATOM   3997  O   LEU B 859     -79.456   7.948  10.239  1.00 26.04           O  
ANISOU 3997  O   LEU B 859     3104   3224   3566     34    -68      2       O  
ATOM   3998  CB  LEU B 859     -76.506   7.974   9.907  1.00 30.78           C  
ANISOU 3998  CB  LEU B 859     3698   3740   4258     13   -123    -61       C  
ATOM   3999  CG  LEU B 859     -75.961   6.560  10.194  1.00 32.70           C  
ANISOU 3999  CG  LEU B 859     3954   3995   4473     -3   -170    -64       C  
ATOM   4000  CD1 LEU B 859     -74.984   6.104   9.111  1.00 33.95           C  
ANISOU 4000  CD1 LEU B 859     4089   4136   4675    -11   -175    -60       C  
ATOM   4001  CD2 LEU B 859     -75.284   6.521  11.560  1.00 32.24           C  
ANISOU 4001  CD2 LEU B 859     3920   3926   4405     -4   -214   -108       C  
ATOM   4002  N   LEU B 860     -79.420   6.516   8.505  1.00 26.03           N  
ANISOU 4002  N   LEU B 860     3086   3248   3557      3    -81     59       N  
ATOM   4003  CA  LEU B 860     -80.822   6.070   8.657  1.00 25.53           C  
ANISOU 4003  CA  LEU B 860     3022   3238   3442     -1    -69     95       C  
ATOM   4004  C   LEU B 860     -80.907   4.570   8.739  1.00 24.54           C  
ANISOU 4004  C   LEU B 860     2918   3137   3269    -33   -101    109       C  
ATOM   4005  O   LEU B 860     -80.014   3.865   8.295  1.00 25.75           O  
ANISOU 4005  O   LEU B 860     3083   3268   3435    -47   -126    100       O  
ATOM   4006  CB  LEU B 860     -81.660   6.547   7.451  1.00 25.77           C  
ANISOU 4006  CB  LEU B 860     3019   3289   3485      5    -37    143       C  
ATOM   4007  CG  LEU B 860     -81.787   8.066   7.257  1.00 24.96           C  
ANISOU 4007  CG  LEU B 860     2895   3158   3429     41     -3    142       C  
ATOM   4008  CD1 LEU B 860     -82.417   8.378   5.913  1.00 24.16           C  
ANISOU 4008  CD1 LEU B 860     2765   3075   3339     44     16    196       C  
ATOM   4009  CD2 LEU B 860     -82.594   8.694   8.387  1.00 24.08           C  
ANISOU 4009  CD2 LEU B 860     2784   3060   3305     69     19    127       C  
ATOM   4010  N   TRP B 861     -82.013   4.093   9.285  1.00 25.23           N  
ANISOU 4010  N   TRP B 861     3011   3270   3305    -45    -96    131       N  
ATOM   4011  CA  TRP B 861     -82.215   2.673   9.514  1.00 25.24           C  
ANISOU 4011  CA  TRP B 861     3041   3293   3258    -80   -126    147       C  
ATOM   4012  C   TRP B 861     -82.824   1.971   8.317  1.00 25.54           C  
ANISOU 4012  C   TRP B 861     3066   3356   3283   -108   -125    189       C  
ATOM   4013  O   TRP B 861     -83.646   2.542   7.590  1.00 24.59           O  
ANISOU 4013  O   TRP B 861     2910   3264   3168   -102    -97    220       O  
ATOM   4014  CB  TRP B 861     -83.182   2.466  10.696  1.00 25.50           C  
ANISOU 4014  CB  TRP B 861     3086   3367   3237    -89   -118    155       C  
ATOM   4015  CG  TRP B 861     -82.724   3.055  11.990  1.00 25.07           C  
ANISOU 4015  CG  TRP B 861     3053   3295   3177    -68   -121    112       C  
ATOM   4016  CD1 TRP B 861     -83.192   4.194  12.580  1.00 25.77           C  
ANISOU 4016  CD1 TRP B 861     3128   3393   3270    -39    -84     93       C  
ATOM   4017  CD2 TRP B 861     -81.707   2.541  12.855  1.00 25.16           C  
ANISOU 4017  CD2 TRP B 861     3107   3277   3177    -75   -165     81       C  
ATOM   4018  NE1 TRP B 861     -82.508   4.437  13.751  1.00 24.88           N  
ANISOU 4018  NE1 TRP B 861     3050   3258   3144    -32   -101     48       N  
ATOM   4019  CE2 TRP B 861     -81.606   3.426  13.953  1.00 26.37           C  
ANISOU 4019  CE2 TRP B 861     3272   3426   3321    -55   -154     43       C  
ATOM   4020  CE3 TRP B 861     -80.884   1.416  12.819  1.00 24.36           C  
ANISOU 4020  CE3 TRP B 861     3035   3151   3071    -94   -214     82       C  
ATOM   4021  CZ2 TRP B 861     -80.712   3.208  15.001  1.00 26.47           C  
ANISOU 4021  CZ2 TRP B 861     3324   3416   3316    -59   -197      9       C  
ATOM   4022  CZ3 TRP B 861     -79.996   1.211  13.835  1.00 25.07           C  
ANISOU 4022  CZ3 TRP B 861     3158   3216   3150    -91   -255     51       C  
ATOM   4023  CH2 TRP B 861     -79.913   2.097  14.922  1.00 25.92           C  
ANISOU 4023  CH2 TRP B 861     3277   3326   3244    -76   -249     17       C  
ATOM   4024  N   HIS B 862     -82.448   0.714   8.134  1.00 24.26           N  
ANISOU 4024  N   HIS B 862     2936   3183   3101   -137   -157    192       N  
ATOM   4025  CA  HIS B 862     -83.176  -0.167   7.252  1.00 23.98           C  
ANISOU 4025  CA  HIS B 862     2901   3175   3035   -175   -161    229       C  
ATOM   4026  C   HIS B 862     -83.201  -1.569   7.856  1.00 24.05           C  
ANISOU 4026  C   HIS B 862     2956   3179   3002   -210   -195    232       C  
ATOM   4027  O   HIS B 862     -82.165  -2.196   8.007  1.00 21.34           O  
ANISOU 4027  O   HIS B 862     2647   2790   2672   -207   -224    208       O  
ATOM   4028  CB  HIS B 862     -82.559  -0.218   5.864  1.00 23.23           C  
ANISOU 4028  CB  HIS B 862     2801   3056   2969   -177   -159    227       C  
ATOM   4029  CG  HIS B 862     -83.317  -1.075   4.910  1.00 24.99           C  
ANISOU 4029  CG  HIS B 862     3030   3308   3156   -219   -165    261       C  
ATOM   4030  ND1 HIS B 862     -84.336  -0.598   4.127  1.00 26.89           N  
ANISOU 4030  ND1 HIS B 862     3236   3596   3386   -230   -146    299       N  
ATOM   4031  CD2 HIS B 862     -83.231  -2.394   4.631  1.00 28.11           C  
ANISOU 4031  CD2 HIS B 862     3465   3692   3524   -257   -190    261       C  
ATOM   4032  CE1 HIS B 862     -84.831  -1.572   3.390  1.00 26.17           C  
ANISOU 4032  CE1 HIS B 862     3161   3525   3260   -276   -162    320       C  
ATOM   4033  NE2 HIS B 862     -84.174  -2.673   3.673  1.00 27.50           N  
ANISOU 4033  NE2 HIS B 862     3377   3654   3417   -294   -187    296       N  
ATOM   4034  N   GLY B 863     -84.404  -2.053   8.146  1.00 24.76           N  
ANISOU 4034  N   GLY B 863     3045   3316   3045   -245   -191    267       N  
ATOM   4035  CA  GLY B 863     -84.600  -3.384   8.664  1.00 26.52           C  
ANISOU 4035  CA  GLY B 863     3315   3537   3225   -287   -220    280       C  
ATOM   4036  C   GLY B 863     -85.082  -4.336   7.603  1.00 27.60           C  
ANISOU 4036  C   GLY B 863     3462   3682   3343   -334   -231    306       C  
ATOM   4037  O   GLY B 863     -85.748  -3.936   6.635  1.00 28.63           O  
ANISOU 4037  O   GLY B 863     3554   3848   3476   -344   -213    327       O  
ATOM   4038  N   SER B 864     -84.763  -5.605   7.794  1.00 27.55           N  
ANISOU 4038  N   SER B 864     3511   3641   3316   -365   -264    305       N  
ATOM   4039  CA  SER B 864     -85.136  -6.647   6.832  1.00 28.76           C  
ANISOU 4039  CA  SER B 864     3688   3790   3449   -415   -279    322       C  
ATOM   4040  C   SER B 864     -85.026  -8.007   7.534  1.00 29.99           C  
ANISOU 4040  C   SER B 864     3909   3909   3575   -451   -314    328       C  
ATOM   4041  O   SER B 864     -84.364  -8.110   8.563  1.00 27.38           O  
ANISOU 4041  O   SER B 864     3607   3548   3249   -426   -331    315       O  
ATOM   4042  CB  SER B 864     -84.190  -6.615   5.642  1.00 27.73           C  
ANISOU 4042  CB  SER B 864     3563   3618   3356   -394   -279    293       C  
ATOM   4043  OG  SER B 864     -84.704  -7.329   4.558  1.00 30.70           O  
ANISOU 4043  OG  SER B 864     3953   4002   3708   -441   -285    307       O  
ATOM   4044  N   ARG B 865     -85.667  -9.029   6.972  1.00 30.86           N  
ANISOU 4044  N   ARG B 865     4048   4022   3655   -511   -328    350       N  
ATOM   4045  CA  ARG B 865     -85.573 -10.370   7.501  1.00 32.19           C  
ANISOU 4045  CA  ARG B 865     4286   4146   3799   -549   -362    359       C  
ATOM   4046  C   ARG B 865     -84.153 -10.858   7.415  1.00 30.79           C  
ANISOU 4046  C   ARG B 865     4155   3885   3660   -507   -387    321       C  
ATOM   4047  O   ARG B 865     -83.424 -10.551   6.468  1.00 30.09           O  
ANISOU 4047  O   ARG B 865     4052   3773   3609   -474   -377    289       O  
ATOM   4048  CB  ARG B 865     -86.476 -11.320   6.731  1.00 36.12           C  
ANISOU 4048  CB  ARG B 865     4806   4655   4264   -625   -371    384       C  
ATOM   4049  CG  ARG B 865     -87.965 -11.128   6.992  1.00 40.35           C  
ANISOU 4049  CG  ARG B 865     5299   5274   4759   -679   -353    430       C  
ATOM   4050  CD  ARG B 865     -88.788 -11.865   5.964  1.00 45.89           C  
ANISOU 4050  CD  ARG B 865     6008   5993   5435   -752   -364    448       C  
ATOM   4051  NE  ARG B 865     -90.200 -11.468   6.038  1.00 51.17           N  
ANISOU 4051  NE  ARG B 865     6612   6755   6076   -797   -346    491       N  
ATOM   4052  CZ  ARG B 865     -91.122 -12.071   6.794  1.00 56.43           C  
ANISOU 4052  CZ  ARG B 865     7284   7454   6704   -859   -348    529       C  
ATOM   4053  NH1 ARG B 865     -92.372 -11.622   6.785  1.00 64.81           N  
ANISOU 4053  NH1 ARG B 865     8272   8605   7748   -892   -326    566       N  
ATOM   4054  NH2 ARG B 865     -90.812 -13.107   7.561  1.00 54.88           N  
ANISOU 4054  NH2 ARG B 865     7162   7202   6489   -888   -370    534       N  
ATOM   4055  N   THR B 866     -83.772 -11.621   8.424  1.00 31.44           N  
ANISOU 4055  N   THR B 866     4290   3924   3732   -508   -419    327       N  
ATOM   4056  CA  THR B 866     -82.433 -12.161   8.555  1.00 32.24           C  
ANISOU 4056  CA  THR B 866     4432   3945   3871   -463   -450    297       C  
ATOM   4057  C   THR B 866     -82.011 -12.934   7.318  1.00 31.40           C  
ANISOU 4057  C   THR B 866     4356   3787   3788   -469   -454    273       C  
ATOM   4058  O   THR B 866     -80.859 -12.836   6.889  1.00 31.56           O  
ANISOU 4058  O   THR B 866     4371   3762   3858   -415   -455    234       O  
ATOM   4059  CB  THR B 866     -82.344 -13.002   9.847  1.00 33.00           C  
ANISOU 4059  CB  THR B 866     4589   4008   3940   -476   -491    322       C  
ATOM   4060  OG1 THR B 866     -82.721 -12.166  10.959  1.00 37.33           O  
ANISOU 4060  OG1 THR B 866     5109   4612   4462   -469   -480    338       O  
ATOM   4061  CG2 THR B 866     -80.944 -13.479  10.098  1.00 33.38           C  
ANISOU 4061  CG2 THR B 866     4671   3977   4033   -420   -529    296       C  
ATOM   4062  N   THR B 867     -82.950 -13.650   6.718  1.00 31.52           N  
ANISOU 4062  N   THR B 867     4397   3812   3766   -536   -452    293       N  
ATOM   4063  CA  THR B 867     -82.678 -14.468   5.535  1.00 32.07           C  
ANISOU 4063  CA  THR B 867     4506   3832   3846   -552   -454    267       C  
ATOM   4064  C   THR B 867     -82.413 -13.647   4.261  1.00 34.83           C  
ANISOU 4064  C   THR B 867     4807   4209   4218   -528   -419    236       C  
ATOM   4065  O   THR B 867     -82.054 -14.201   3.226  1.00 36.91           O  
ANISOU 4065  O   THR B 867     5101   4433   4488   -534   -413    206       O  
ATOM   4066  CB  THR B 867     -83.844 -15.443   5.267  1.00 32.71           C  
ANISOU 4066  CB  THR B 867     4631   3920   3877   -642   -466    298       C  
ATOM   4067  OG1 THR B 867     -85.100 -14.747   5.281  1.00 32.86           O  
ANISOU 4067  OG1 THR B 867     4593   4033   3858   -687   -446    334       O  
ATOM   4068  CG2 THR B 867     -83.861 -16.523   6.331  1.00 34.45           C  
ANISOU 4068  CG2 THR B 867     4921   4087   4082   -666   -503    324       C  
ATOM   4069  N   ASN B 868     -82.591 -12.334   4.338  1.00 33.40           N  
ANISOU 4069  N   ASN B 868     4556   4091   4045   -502   -392    243       N  
ATOM   4070  CA  ASN B 868     -82.227 -11.474   3.240  1.00 30.99           C  
ANISOU 4070  CA  ASN B 868     4206   3806   3762   -475   -360    218       C  
ATOM   4071  C   ASN B 868     -80.802 -10.971   3.316  1.00 28.19           C  
ANISOU 4071  C   ASN B 868     3833   3411   3467   -401   -351    178       C  
ATOM   4072  O   ASN B 868     -80.307 -10.454   2.345  1.00 26.91           O  
ANISOU 4072  O   ASN B 868     3646   3251   3327   -379   -323    153       O  
ATOM   4073  CB  ASN B 868     -83.138 -10.263   3.198  1.00 32.38           C  
ANISOU 4073  CB  ASN B 868     4315   4065   3923   -482   -335    248       C  
ATOM   4074  CG  ASN B 868     -84.574 -10.590   2.894  1.00 32.99           C  
ANISOU 4074  CG  ASN B 868     4389   4197   3947   -554   -339    288       C  
ATOM   4075  OD1 ASN B 868     -85.470  -9.923   3.395  1.00 36.51           O  
ANISOU 4075  OD1 ASN B 868     4789   4706   4378   -564   -329    322       O  
ATOM   4076  ND2 ASN B 868     -84.815 -11.570   2.053  1.00 35.23           N  
ANISOU 4076  ND2 ASN B 868     4719   4460   4206   -605   -352    283       N  
ATOM   4077  N   PHE B 869     -80.115 -11.129   4.439  1.00 29.20           N  
ANISOU 4077  N   PHE B 869     3973   3503   3620   -364   -376    172       N  
ATOM   4078  CA  PHE B 869     -78.861 -10.389   4.646  1.00 30.68           C  
ANISOU 4078  CA  PHE B 869     4123   3668   3864   -297   -370    139       C  
ATOM   4079  C   PHE B 869     -77.643 -10.851   3.867  1.00 32.15           C  
ANISOU 4079  C   PHE B 869     4321   3797   4098   -259   -363     95       C  
ATOM   4080  O   PHE B 869     -76.713 -10.060   3.632  1.00 33.60           O  
ANISOU 4080  O   PHE B 869     4457   3978   4330   -214   -343     67       O  
ATOM   4081  CB  PHE B 869     -78.537 -10.241   6.132  1.00 29.11           C  
ANISOU 4081  CB  PHE B 869     3926   3463   3674   -271   -403    148       C  
ATOM   4082  CG  PHE B 869     -79.142  -9.024   6.714  1.00 29.80           C  
ANISOU 4082  CG  PHE B 869     3965   3611   3745   -271   -385    166       C  
ATOM   4083  CD1 PHE B 869     -80.461  -9.028   7.148  1.00 31.05           C  
ANISOU 4083  CD1 PHE B 869     4128   3819   3848   -317   -381    206       C  
ATOM   4084  CD2 PHE B 869     -78.435  -7.849   6.755  1.00 29.56           C  
ANISOU 4084  CD2 PHE B 869     3884   3590   3757   -227   -368    142       C  
ATOM   4085  CE1 PHE B 869     -81.056  -7.891   7.640  1.00 29.89           C  
ANISOU 4085  CE1 PHE B 869     3937   3729   3691   -312   -358    218       C  
ATOM   4086  CE2 PHE B 869     -79.014  -6.711   7.275  1.00 30.57           C  
ANISOU 4086  CE2 PHE B 869     3975   3768   3874   -225   -349    154       C  
ATOM   4087  CZ  PHE B 869     -80.329  -6.728   7.704  1.00 30.36           C  
ANISOU 4087  CZ  PHE B 869     3953   3789   3793   -263   -342    191       C  
ATOM   4088  N   ALA B 870     -77.613 -12.109   3.470  1.00 32.74           N  
ANISOU 4088  N   ALA B 870     4454   3822   4163   -278   -377     86       N  
ATOM   4089  CA  ALA B 870     -76.534 -12.547   2.582  1.00 35.84           C  
ANISOU 4089  CA  ALA B 870     4856   4162   4598   -242   -359     38       C  
ATOM   4090  C   ALA B 870     -76.665 -11.825   1.251  1.00 33.08           C  
ANISOU 4090  C   ALA B 870     4475   3855   4241   -255   -308     23       C  
ATOM   4091  O   ALA B 870     -75.683 -11.399   0.669  1.00 37.28           O  
ANISOU 4091  O   ALA B 870     4973   4374   4815   -214   -277    -12       O  
ATOM   4092  CB  ALA B 870     -76.567 -14.044   2.360  1.00 36.77           C  
ANISOU 4092  CB  ALA B 870     5052   4214   4705   -261   -380     29       C  
ATOM   4093  N   GLY B 871     -77.884 -11.721   0.766  1.00 31.29           N  
ANISOU 4093  N   GLY B 871     4256   3676   3956   -314   -300     52       N  
ATOM   4094  CA  GLY B 871     -78.134 -11.023  -0.463  1.00 31.43           C  
ANISOU 4094  CA  GLY B 871     4247   3738   3956   -331   -259     47       C  
ATOM   4095  C   GLY B 871     -77.804  -9.560  -0.304  1.00 31.14           C  
ANISOU 4095  C   GLY B 871     4139   3742   3951   -295   -235     54       C  
ATOM   4096  O   GLY B 871     -77.154  -8.977  -1.162  1.00 33.24           O  
ANISOU 4096  O   GLY B 871     4378   4013   4240   -275   -197     32       O  
ATOM   4097  N   ILE B 872     -78.264  -8.959   0.796  1.00 29.33           N  
ANISOU 4097  N   ILE B 872     3881   3540   3722   -291   -254     85       N  
ATOM   4098  CA  ILE B 872     -78.005  -7.553   1.024  1.00 27.84           C  
ANISOU 4098  CA  ILE B 872     3631   3384   3565   -258   -234     90       C  
ATOM   4099  C   ILE B 872     -76.499  -7.262   1.133  1.00 29.36           C  
ANISOU 4099  C   ILE B 872     3798   3534   3823   -203   -224     48       C  
ATOM   4100  O   ILE B 872     -76.000  -6.304   0.549  1.00 27.74           O  
ANISOU 4100  O   ILE B 872     3551   3342   3646   -184   -189     37       O  
ATOM   4101  CB  ILE B 872     -78.742  -7.030   2.248  1.00 25.19           C  
ANISOU 4101  CB  ILE B 872     3276   3080   3214   -261   -254    122       C  
ATOM   4102  CG1 ILE B 872     -80.234  -7.016   2.007  1.00 24.03           C  
ANISOU 4102  CG1 ILE B 872     3131   2989   3012   -313   -252    165       C  
ATOM   4103  CG2 ILE B 872     -78.247  -5.641   2.631  1.00 25.87           C  
ANISOU 4103  CG2 ILE B 872     3307   3179   3342   -221   -235    115       C  
ATOM   4104  CD1 ILE B 872     -81.040  -6.876   3.268  1.00 25.39           C  
ANISOU 4104  CD1 ILE B 872     3295   3189   3161   -322   -270    195       C  
ATOM   4105  N   LEU B 873     -75.770  -8.056   1.876  1.00 29.97           N  
ANISOU 4105  N   LEU B 873     3898   3562   3927   -176   -256     28       N  
ATOM   4106  CA  LEU B 873     -74.334  -7.803   1.965  1.00 31.23           C  
ANISOU 4106  CA  LEU B 873     4024   3687   4155   -123   -250    -10       C  
ATOM   4107  C   LEU B 873     -73.620  -8.041   0.646  1.00 31.88           C  
ANISOU 4107  C   LEU B 873     4104   3751   4259   -114   -207    -45       C  
ATOM   4108  O   LEU B 873     -72.775  -7.242   0.249  1.00 33.52           O  
ANISOU 4108  O   LEU B 873     4262   3963   4510    -88   -174    -66       O  
ATOM   4109  CB  LEU B 873     -73.701  -8.612   3.087  1.00 31.41           C  
ANISOU 4109  CB  LEU B 873     4068   3662   4204    -93   -301    -19       C  
ATOM   4110  CG  LEU B 873     -74.230  -8.189   4.462  1.00 33.22           C  
ANISOU 4110  CG  LEU B 873     4296   3915   4412    -99   -338     11       C  
ATOM   4111  CD1 LEU B 873     -73.531  -9.041   5.495  1.00 34.34           C  
ANISOU 4111  CD1 LEU B 873     4464   4008   4576    -70   -393      6       C  
ATOM   4112  CD2 LEU B 873     -73.987  -6.700   4.741  1.00 34.67           C  
ANISOU 4112  CD2 LEU B 873     4419   4134   4622    -83   -320      7       C  
ATOM   4113  N   SER B 874     -73.956  -9.098  -0.072  1.00 30.01           N  
ANISOU 4113  N   SER B 874     3920   3494   3988   -138   -202    -53       N  
ATOM   4114  CA  SER B 874     -73.247  -9.325  -1.321  1.00 31.99           C  
ANISOU 4114  CA  SER B 874     4172   3728   4254   -128   -155    -92       C  
ATOM   4115  C   SER B 874     -73.678  -8.375  -2.432  1.00 30.20           C  
ANISOU 4115  C   SER B 874     3924   3556   3996   -158   -107    -80       C  
ATOM   4116  O   SER B 874     -72.869  -8.028  -3.274  1.00 29.02           O  
ANISOU 4116  O   SER B 874     3750   3405   3872   -141    -60   -108       O  
ATOM   4117  CB  SER B 874     -73.335 -10.759  -1.787  1.00 32.73           C  
ANISOU 4117  CB  SER B 874     4337   3775   4325   -141   -161   -114       C  
ATOM   4118  OG  SER B 874     -74.581 -10.986  -2.311  1.00 36.48           O  
ANISOU 4118  OG  SER B 874     4853   4281   4728   -203   -163    -89       O  
ATOM   4119  N   GLN B 875     -74.934  -7.942  -2.437  1.00 30.10           N  
ANISOU 4119  N   GLN B 875     3916   3591   3929   -202   -118    -35       N  
ATOM   4120  CA  GLN B 875     -75.417  -7.123  -3.557  1.00 32.88           C  
ANISOU 4120  CA  GLN B 875     4254   3993   4247   -232    -79    -17       C  
ATOM   4121  C   GLN B 875     -75.914  -5.743  -3.204  1.00 30.58           C  
ANISOU 4121  C   GLN B 875     3912   3747   3961   -231    -77     23       C  
ATOM   4122  O   GLN B 875     -76.238  -4.988  -4.089  1.00 30.49           O  
ANISOU 4122  O   GLN B 875     3885   3772   3927   -249    -48     43       O  
ATOM   4123  CB  GLN B 875     -76.528  -7.866  -4.255  1.00 36.18           C  
ANISOU 4123  CB  GLN B 875     4724   4431   4591   -289    -89      0       C  
ATOM   4124  CG  GLN B 875     -76.056  -9.258  -4.564  1.00 39.63           C  
ANISOU 4124  CG  GLN B 875     5221   4813   5025   -290    -92    -45       C  
ATOM   4125  CD  GLN B 875     -76.354  -9.593  -5.979  1.00 48.10           C  
ANISOU 4125  CD  GLN B 875     6333   5901   6040   -332    -62    -59       C  
ATOM   4126  OE1 GLN B 875     -77.430 -10.110  -6.285  1.00 49.92           O  
ANISOU 4126  OE1 GLN B 875     6605   6154   6210   -388    -86    -38       O  
ATOM   4127  NE2 GLN B 875     -75.447  -9.204  -6.891  1.00 55.51           N  
ANISOU 4127  NE2 GLN B 875     7257   6840   6996   -311     -8    -91       N  
ATOM   4128  N   GLY B 876     -75.982  -5.429  -1.918  1.00 27.63           N  
ANISOU 4128  N   GLY B 876     3516   3369   3613   -210   -108     35       N  
ATOM   4129  CA  GLY B 876     -76.431  -4.133  -1.463  1.00 26.43           C  
ANISOU 4129  CA  GLY B 876     3320   3251   3470   -204   -105     67       C  
ATOM   4130  C   GLY B 876     -77.937  -4.108  -1.418  1.00 25.13           C  
ANISOU 4130  C   GLY B 876     3166   3133   3248   -242   -121    113       C  
ATOM   4131  O   GLY B 876     -78.599  -4.985  -1.921  1.00 25.38           O  
ANISOU 4131  O   GLY B 876     3235   3176   3232   -280   -132    122       O  
ATOM   4132  N   LEU B 877     -78.472  -3.024  -0.894  1.00 26.27           N  
ANISOU 4132  N   LEU B 877     3273   3307   3401   -232   -120    142       N  
ATOM   4133  CA  LEU B 877     -79.894  -2.758  -0.984  1.00 25.89           C  
ANISOU 4133  CA  LEU B 877     3217   3312   3308   -261   -127    189       C  
ATOM   4134  C   LEU B 877     -80.266  -2.488  -2.422  1.00 26.13           C  
ANISOU 4134  C   LEU B 877     3247   3373   3309   -286   -105    211       C  
ATOM   4135  O   LEU B 877     -79.558  -1.795  -3.153  1.00 24.64           O  
ANISOU 4135  O   LEU B 877     3043   3174   3143   -271    -73    203       O  
ATOM   4136  CB  LEU B 877     -80.281  -1.575  -0.108  1.00 25.91           C  
ANISOU 4136  CB  LEU B 877     3178   3333   3334   -233   -123    209       C  
ATOM   4137  CG  LEU B 877     -80.096  -1.805   1.365  1.00 25.16           C  
ANISOU 4137  CG  LEU B 877     3089   3218   3252   -215   -147    192       C  
ATOM   4138  CD1 LEU B 877     -80.441  -0.564   2.159  1.00 24.77           C  
ANISOU 4138  CD1 LEU B 877     3003   3185   3224   -187   -136    203       C  
ATOM   4139  CD2 LEU B 877     -80.952  -2.984   1.828  1.00 25.84           C  
ANISOU 4139  CD2 LEU B 877     3209   3321   3290   -251   -177    208       C  
ATOM   4140  N   ARG B 878     -81.366  -3.095  -2.835  1.00 29.52           N  
ANISOU 4140  N   ARG B 878     3694   3840   3682   -331   -124    240       N  
ATOM   4141  CA  ARG B 878     -81.830  -3.024  -4.189  1.00 31.00           C  
ANISOU 4141  CA  ARG B 878     3888   4062   3828   -365   -114    263       C  
ATOM   4142  C   ARG B 878     -83.258  -2.540  -4.203  1.00 31.08           C  
ANISOU 4142  C   ARG B 878     3867   4135   3808   -386   -132    320       C  
ATOM   4143  O   ARG B 878     -83.929  -2.484  -3.198  1.00 30.31           O  
ANISOU 4143  O   ARG B 878     3747   4054   3716   -380   -148    337       O  
ATOM   4144  CB  ARG B 878     -81.714  -4.374  -4.879  1.00 34.36           C  
ANISOU 4144  CB  ARG B 878     4372   4472   4212   -407   -124    236       C  
ATOM   4145  CG  ARG B 878     -80.292  -4.711  -5.323  1.00 39.20           C  
ANISOU 4145  CG  ARG B 878     5010   5031   4852   -383    -95    181       C  
ATOM   4146  CD  ARG B 878     -80.008  -6.179  -5.110  1.00 41.35           C  
ANISOU 4146  CD  ARG B 878     5338   5259   5113   -399   -114    142       C  
ATOM   4147  NE  ARG B 878     -80.060  -6.440  -3.670  1.00 46.80           N  
ANISOU 4147  NE  ARG B 878     6021   5927   5833   -379   -143    143       N  
ATOM   4148  CZ  ARG B 878     -80.452  -7.576  -3.098  1.00 47.37           C  
ANISOU 4148  CZ  ARG B 878     6135   5980   5885   -404   -177    140       C  
ATOM   4149  NH1 ARG B 878     -80.834  -8.626  -3.821  1.00 44.84           N  
ANISOU 4149  NH1 ARG B 878     5868   5652   5519   -452   -187    131       N  
ATOM   4150  NH2 ARG B 878     -80.475  -7.647  -1.774  1.00 49.34           N  
ANISOU 4150  NH2 ARG B 878     6376   6215   6157   -385   -201    147       N  
ATOM   4151  N   ILE B 879     -83.703  -2.186  -5.389  1.00 32.19           N  
ANISOU 4151  N   ILE B 879     4003   4313   3915   -409   -127    351       N  
ATOM   4152  CA  ILE B 879     -85.035  -1.717  -5.612  1.00 33.84           C  
ANISOU 4152  CA  ILE B 879     4176   4586   4097   -428   -147    410       C  
ATOM   4153  C   ILE B 879     -85.787  -2.892  -6.226  1.00 34.85           C  
ANISOU 4153  C   ILE B 879     4338   4745   4159   -496   -179    417       C  
ATOM   4154  O   ILE B 879     -85.215  -3.674  -6.966  1.00 31.71           O  
ANISOU 4154  O   ILE B 879     3993   4324   3733   -524   -176    383       O  
ATOM   4155  CB  ILE B 879     -84.966  -0.507  -6.565  1.00 35.64           C  
ANISOU 4155  CB  ILE B 879     4379   4831   4330   -409   -126    444       C  
ATOM   4156  CG1 ILE B 879     -84.341   0.689  -5.823  1.00 35.86           C  
ANISOU 4156  CG1 ILE B 879     4373   4824   4428   -346    -97    439       C  
ATOM   4157  CG2 ILE B 879     -86.328  -0.149  -7.126  1.00 35.50           C  
ANISOU 4157  CG2 ILE B 879     4329   4884   4276   -433   -153    510       C  
ATOM   4158  CD1 ILE B 879     -84.020   1.838  -6.743  1.00 37.45           C  
ANISOU 4158  CD1 ILE B 879     4562   5025   4643   -328    -72    467       C  
ATOM   4159  N   ALA B 880     -87.072  -2.991  -5.949  1.00 35.10           N  
ANISOU 4159  N   ALA B 880     4338   4831   4167   -524   -209    460       N  
ATOM   4160  CA  ALA B 880     -87.896  -3.984  -6.624  1.00 37.60           C  
ANISOU 4160  CA  ALA B 880     4681   5186   4420   -598   -245    473       C  
ATOM   4161  C   ALA B 880     -87.658  -3.962  -8.156  1.00 39.45           C  
ANISOU 4161  C   ALA B 880     4948   5433   4609   -627   -244    474       C  
ATOM   4162  O   ALA B 880     -87.575  -2.898  -8.783  1.00 39.56           O  
ANISOU 4162  O   ALA B 880     4936   5467   4630   -599   -229    504       O  
ATOM   4163  CB  ALA B 880     -89.344  -3.718  -6.316  1.00 37.32           C  
ANISOU 4163  CB  ALA B 880     4584   5222   4372   -618   -272    531       C  
ATOM   4164  N   PRO B 881     -87.524  -5.134  -8.764  1.00 39.37           N  
ANISOU 4164  N   PRO B 881     5002   5409   4550   -683   -258    440       N  
ATOM   4165  CA  PRO B 881     -87.250  -5.168 -10.201  1.00 42.90           C  
ANISOU 4165  CA  PRO B 881     5488   5866   4944   -713   -252    434       C  
ATOM   4166  C   PRO B 881     -88.399  -4.616 -11.069  1.00 45.86           C  
ANISOU 4166  C   PRO B 881     5830   6325   5271   -749   -287    500       C  
ATOM   4167  O   PRO B 881     -89.516  -4.459 -10.585  1.00 45.99           O  
ANISOU 4167  O   PRO B 881     5792   6391   5291   -761   -320    548       O  
ATOM   4168  CB  PRO B 881     -87.020  -6.645 -10.490  1.00 44.10           C  
ANISOU 4168  CB  PRO B 881     5719   5984   5055   -768   -264    380       C  
ATOM   4169  CG  PRO B 881     -87.615  -7.387  -9.352  1.00 44.42           C  
ANISOU 4169  CG  PRO B 881     5751   6015   5111   -786   -292    381       C  
ATOM   4170  CD  PRO B 881     -87.705  -6.462  -8.173  1.00 41.39           C  
ANISOU 4170  CD  PRO B 881     5299   5638   4792   -725   -280    410       C  
ATOM   4171  N   PRO B 882     -88.106  -4.266 -12.331  1.00 47.78           N  
ANISOU 4171  N   PRO B 882     6100   6584   5470   -763   -278    507       N  
ATOM   4172  CA  PRO B 882     -89.098  -3.727 -13.285  1.00 49.24           C  
ANISOU 4172  CA  PRO B 882     6259   6847   5602   -797   -316    574       C  
ATOM   4173  C   PRO B 882     -90.324  -4.637 -13.412  1.00 47.97           C  
ANISOU 4173  C   PRO B 882     6097   6741   5387   -875   -377    592       C  
ATOM   4174  O   PRO B 882     -91.442  -4.152 -13.495  1.00 44.93           O  
ANISOU 4174  O   PRO B 882     5651   6425   4994   -887   -418    659       O  
ATOM   4175  CB  PRO B 882     -88.328  -3.696 -14.609  1.00 50.30           C  
ANISOU 4175  CB  PRO B 882     6457   6974   5682   -816   -292    552       C  
ATOM   4176  CG  PRO B 882     -86.885  -3.622 -14.229  1.00 48.93           C  
ANISOU 4176  CG  PRO B 882     6307   6722   5561   -762   -227    492       C  
ATOM   4177  CD  PRO B 882     -86.730  -4.238 -12.867  1.00 48.92           C  
ANISOU 4177  CD  PRO B 882     6295   6674   5619   -739   -226    455       C  
ATOM   4178  N   GLU B 883     -90.100  -5.948 -13.353  1.00 50.66           N  
ANISOU 4178  N   GLU B 883     6503   7045   5700   -925   -382    534       N  
ATOM   4179  CA  GLU B 883     -91.160  -6.948 -13.483  1.00 51.75           C  
ANISOU 4179  CA  GLU B 883     6653   7223   5785  -1011   -439    542       C  
ATOM   4180  C   GLU B 883     -92.127  -6.967 -12.294  1.00 53.15           C  
ANISOU 4180  C   GLU B 883     6758   7430   6007  -1010   -464    580       C  
ATOM   4181  O   GLU B 883     -93.250  -7.457 -12.417  1.00 55.52           O  
ANISOU 4181  O   GLU B 883     7037   7788   6271  -1079   -515    611       O  
ATOM   4182  CB  GLU B 883     -90.565  -8.339 -13.627  1.00 56.09           C  
ANISOU 4182  CB  GLU B 883     7299   7709   6304  -1058   -431    465       C  
ATOM   4183  CG  GLU B 883     -89.636  -8.512 -14.824  1.00 60.39           C  
ANISOU 4183  CG  GLU B 883     7922   8225   6798  -1067   -401    417       C  
ATOM   4184  CD  GLU B 883     -88.200  -8.034 -14.569  1.00 66.16           C  
ANISOU 4184  CD  GLU B 883     8664   8887   7586   -983   -331    375       C  
ATOM   4185  OE1 GLU B 883     -87.504  -7.659 -15.549  1.00 74.29           O  
ANISOU 4185  OE1 GLU B 883     9726   9915   8584   -974   -297    359       O  
ATOM   4186  OE2 GLU B 883     -87.755  -7.998 -13.398  1.00 61.56           O  
ANISOU 4186  OE2 GLU B 883     8055   8257   7079   -928   -309    360       O  
ATOM   4187  N   ALA B 884     -91.714  -6.437 -11.145  1.00 46.40           N  
ANISOU 4187  N   ALA B 884     5864   6540   5227   -936   -427    577       N  
ATOM   4188  CA  ALA B 884     -92.580  -6.414  -9.968  1.00 46.56           C  
ANISOU 4188  CA  ALA B 884     5818   6589   5285   -931   -441    610       C  
ATOM   4189  C   ALA B 884     -93.688  -5.381 -10.075  1.00 45.23           C  
ANISOU 4189  C   ALA B 884     5554   6506   5126   -915   -465    687       C  
ATOM   4190  O   ALA B 884     -93.488  -4.327 -10.642  1.00 48.54           O  
ANISOU 4190  O   ALA B 884     5949   6938   5555   -869   -453    715       O  
ATOM   4191  CB  ALA B 884     -91.765  -6.128  -8.723  1.00 48.26           C  
ANISOU 4191  CB  ALA B 884     6027   6740   5570   -857   -395    580       C  
ATOM   4192  N   PRO B 885     -94.853  -5.661  -9.490  1.00 45.82           N  
ANISOU 4192  N   PRO B 885     5569   6636   5202   -951   -494    723       N  
ATOM   4193  CA  PRO B 885     -95.911  -4.651  -9.412  1.00 48.98           C  
ANISOU 4193  CA  PRO B 885     5866   7117   5628   -922   -511    796       C  
ATOM   4194  C   PRO B 885     -95.571  -3.545  -8.409  1.00 50.93           C  
ANISOU 4194  C   PRO B 885     6064   7338   5951   -820   -461    802       C  
ATOM   4195  O   PRO B 885     -94.793  -3.780  -7.502  1.00 53.51           O  
ANISOU 4195  O   PRO B 885     6425   7599   6309   -790   -423    754       O  
ATOM   4196  CB  PRO B 885     -97.123  -5.420  -8.900  1.00 47.31           C  
ANISOU 4196  CB  PRO B 885     5609   6964   5402   -991   -546    821       C  
ATOM   4197  CG  PRO B 885     -96.714  -6.830  -8.717  1.00 47.66           C  
ANISOU 4197  CG  PRO B 885     5741   6955   5414  -1060   -551    764       C  
ATOM   4198  CD  PRO B 885     -95.251  -6.966  -8.932  1.00 48.18           C  
ANISOU 4198  CD  PRO B 885     5899   6927   5482  -1024   -514    700       C  
ATOM   4199  N   VAL B 886     -96.203  -2.384  -8.546  1.00 48.98           N  
ANISOU 4199  N   VAL B 886     5736   7142   5734   -770   -464    861       N  
ATOM   4200  CA  VAL B 886     -96.055  -1.268  -7.600  1.00 51.35           C  
ANISOU 4200  CA  VAL B 886     5984   7421   6106   -675   -419    869       C  
ATOM   4201  C   VAL B 886     -96.898  -1.396  -6.309  1.00 52.28           C  
ANISOU 4201  C   VAL B 886     6036   7572   6257   -668   -406    878       C  
ATOM   4202  O   VAL B 886     -96.682  -0.681  -5.317  1.00 48.84           O  
ANISOU 4202  O   VAL B 886     5573   7110   5876   -596   -362    867       O  
ATOM   4203  CB  VAL B 886     -96.424   0.065  -8.309  1.00 53.48           C  
ANISOU 4203  CB  VAL B 886     6197   7726   6399   -620   -427    931       C  
ATOM   4204  CG1 VAL B 886     -97.916   0.134  -8.593  1.00 53.38           C  
ANISOU 4204  CG1 VAL B 886     6095   7813   6374   -648   -476   1000       C  
ATOM   4205  CG2 VAL B 886     -95.992   1.268  -7.483  1.00 52.30           C  
ANISOU 4205  CG2 VAL B 886     6017   7530   6323   -520   -375    926       C  
ATOM   4206  N   THR B 887     -97.901  -2.264  -6.363  1.00 54.21           N  
ANISOU 4206  N   THR B 887     6253   7880   6465   -745   -445    901       N  
ATOM   4207  CA  THR B 887     -98.911  -2.362  -5.318  1.00 56.50           C  
ANISOU 4207  CA  THR B 887     6466   8223   6779   -749   -435    923       C  
ATOM   4208  C   THR B 887     -98.279  -2.516  -3.924  1.00 53.67           C  
ANISOU 4208  C   THR B 887     6138   7804   6450   -714   -382    874       C  
ATOM   4209  O   THR B 887     -97.370  -3.320  -3.700  1.00 51.62           O  
ANISOU 4209  O   THR B 887     5966   7476   6171   -740   -375    821       O  
ATOM   4210  CB  THR B 887     -99.988  -3.453  -5.660  1.00 60.76           C  
ANISOU 4210  CB  THR B 887     6983   8835   7269   -858   -488    951       C  
ATOM   4211  OG1 THR B 887    -100.955  -2.912  -6.599  1.00 66.66           O  
ANISOU 4211  OG1 THR B 887     7652   9667   8008   -866   -534   1017       O  
ATOM   4212  CG2 THR B 887    -100.727  -3.855  -4.430  1.00 59.39           C  
ANISOU 4212  CG2 THR B 887     6757   8695   7113   -876   -466    956       C  
ATOM   4213  N   GLY B 888     -98.768  -1.709  -2.990  1.00 51.38           N  
ANISOU 4213  N   GLY B 888     5775   7538   6207   -652   -345    891       N  
ATOM   4214  CA  GLY B 888     -98.216  -1.664  -1.645  1.00 49.82           C  
ANISOU 4214  CA  GLY B 888     5602   7290   6036   -611   -295    847       C  
ATOM   4215  C   GLY B 888     -97.142  -0.604  -1.442  1.00 48.98           C  
ANISOU 4215  C   GLY B 888     5524   7112   5973   -519   -257    815       C  
ATOM   4216  O   GLY B 888     -96.925  -0.171  -0.327  1.00 47.80           O  
ANISOU 4216  O   GLY B 888     5369   6939   5855   -469   -215    791       O  
ATOM   4217  N   TYR B 889     -96.456  -0.198  -2.511  1.00 48.36           N  
ANISOU 4217  N   TYR B 889     5480   7000   5895   -503   -272    815       N  
ATOM   4218  CA  TYR B 889     -95.435   0.845  -2.404  1.00 45.73           C  
ANISOU 4218  CA  TYR B 889     5171   6599   5606   -424   -237    789       C  
ATOM   4219  C   TYR B 889     -96.053   2.226  -2.320  1.00 44.02           C  
ANISOU 4219  C   TYR B 889     4876   6409   5440   -348   -217    829       C  
ATOM   4220  O   TYR B 889     -96.354   2.825  -3.327  1.00 47.22           O  
ANISOU 4220  O   TYR B 889     5254   6839   5850   -334   -239    874       O  
ATOM   4221  CB  TYR B 889     -94.462   0.777  -3.580  1.00 44.24           C  
ANISOU 4221  CB  TYR B 889     5046   6365   5397   -438   -254    775       C  
ATOM   4222  CG  TYR B 889     -93.446  -0.325  -3.462  1.00 45.01           C  
ANISOU 4222  CG  TYR B 889     5231   6405   5467   -480   -255    716       C  
ATOM   4223  CD1 TYR B 889     -93.624  -1.545  -4.107  1.00 46.37           C  
ANISOU 4223  CD1 TYR B 889     5442   6593   5583   -562   -292    712       C  
ATOM   4224  CD2 TYR B 889     -92.297  -0.153  -2.689  1.00 45.94           C  
ANISOU 4224  CD2 TYR B 889     5389   6448   5617   -438   -222    663       C  
ATOM   4225  CE1 TYR B 889     -92.689  -2.562  -3.977  1.00 47.58           C  
ANISOU 4225  CE1 TYR B 889     5676   6685   5717   -593   -291    658       C  
ATOM   4226  CE2 TYR B 889     -91.335  -1.155  -2.581  1.00 45.28           C  
ANISOU 4226  CE2 TYR B 889     5381   6310   5515   -468   -225    612       C  
ATOM   4227  CZ  TYR B 889     -91.538  -2.363  -3.209  1.00 47.08           C  
ANISOU 4227  CZ  TYR B 889     5648   6549   5691   -543   -258    609       C  
ATOM   4228  OH  TYR B 889     -90.589  -3.360  -3.071  1.00 44.82           O  
ANISOU 4228  OH  TYR B 889     5435   6201   5392   -565   -260    557       O  
ATOM   4229  N   MET B 890     -96.114   2.758  -1.112  1.00 42.68           N  
ANISOU 4229  N   MET B 890     4682   6227   5309   -294   -174    808       N  
ATOM   4230  CA  MET B 890     -96.658   4.067  -0.853  1.00 43.50           C  
ANISOU 4230  CA  MET B 890     4717   6344   5468   -213   -146    836       C  
ATOM   4231  C   MET B 890     -96.017   5.194  -1.651  1.00 44.43           C  
ANISOU 4231  C   MET B 890     4850   6411   5622   -157   -143    848       C  
ATOM   4232  O   MET B 890     -96.723   6.106  -2.105  1.00 45.97           O  
ANISOU 4232  O   MET B 890     4984   6636   5849   -110   -147    901       O  
ATOM   4233  CB  MET B 890     -96.517   4.384   0.634  1.00 47.64           C  
ANISOU 4233  CB  MET B 890     5239   6842   6019   -167    -93    792       C  
ATOM   4234  CG  MET B 890     -97.213   5.664   1.044  1.00 50.67           C  
ANISOU 4234  CG  MET B 890     5551   7242   6460    -83    -57    814       C  
ATOM   4235  SD  MET B 890     -97.417   5.808   2.820  1.00 56.50           S  
ANISOU 4235  SD  MET B 890     6277   7979   7211    -47      5    765       S  
ATOM   4236  CE  MET B 890     -98.325   7.342   2.875  1.00 58.15           C  
ANISOU 4236  CE  MET B 890     6396   8208   7490     55     42    800       C  
ATOM   4237  N   PHE B 891     -94.692   5.152  -1.829  1.00 40.00           N  
ANISOU 4237  N   PHE B 891     4366   5774   5058   -159   -136    804       N  
ATOM   4238  CA  PHE B 891     -94.002   6.175  -2.617  1.00 37.53           C  
ANISOU 4238  CA  PHE B 891     4073   5411   4776   -117   -130    816       C  
ATOM   4239  C   PHE B 891     -93.245   5.598  -3.822  1.00 35.84           C  
ANISOU 4239  C   PHE B 891     3920   5181   4519   -172   -159    815       C  
ATOM   4240  O   PHE B 891     -92.250   6.135  -4.268  1.00 35.96           O  
ANISOU 4240  O   PHE B 891     3976   5137   4550   -152   -144    800       O  
ATOM   4241  CB  PHE B 891     -93.075   6.969  -1.714  1.00 35.88           C  
ANISOU 4241  CB  PHE B 891     3893   5123   4618    -58    -84    764       C  
ATOM   4242  CG  PHE B 891     -93.784   7.664  -0.598  1.00 38.86           C  
ANISOU 4242  CG  PHE B 891     4218   5512   5036      1    -50    761       C  
ATOM   4243  CD1 PHE B 891     -94.621   8.752  -0.855  1.00 39.12           C  
ANISOU 4243  CD1 PHE B 891     4188   5564   5112     61    -42    812       C  
ATOM   4244  CD2 PHE B 891     -93.646   7.226   0.710  1.00 40.20           C  
ANISOU 4244  CD2 PHE B 891     4401   5673   5199     -2    -25    709       C  
ATOM   4245  CE1 PHE B 891     -95.285   9.387   0.178  1.00 40.50           C  
ANISOU 4245  CE1 PHE B 891     4314   5747   5325    121     -4    803       C  
ATOM   4246  CE2 PHE B 891     -94.328   7.846   1.747  1.00 42.08           C  
ANISOU 4246  CE2 PHE B 891     4594   5925   5467     51     13    701       C  
ATOM   4247  CZ  PHE B 891     -95.129   8.940   1.484  1.00 42.00           C  
ANISOU 4247  CZ  PHE B 891     4521   5932   5504    114     27    745       C  
ATOM   4248  N   GLY B 892     -93.764   4.526  -4.385  1.00 36.36           N  
ANISOU 4248  N   GLY B 892     3988   5300   4526   -242   -198    832       N  
ATOM   4249  CA  GLY B 892     -93.134   3.892  -5.527  1.00 33.95           C  
ANISOU 4249  CA  GLY B 892     3743   4985   4172   -298   -223    826       C  
ATOM   4250  C   GLY B 892     -92.049   2.907  -5.151  1.00 32.87           C  
ANISOU 4250  C   GLY B 892     3679   4794   4016   -332   -210    755       C  
ATOM   4251  O   GLY B 892     -91.669   2.772  -3.987  1.00 33.96           O  
ANISOU 4251  O   GLY B 892     3825   4897   4180   -310   -185    712       O  
ATOM   4252  N   LYS B 893     -91.524   2.255  -6.176  1.00 34.33           N  
ANISOU 4252  N   LYS B 893     3918   4972   4155   -382   -228    744       N  
ATOM   4253  CA  LYS B 893     -90.437   1.323  -6.052  1.00 36.89           C  
ANISOU 4253  CA  LYS B 893     4312   5242   4463   -410   -217    680       C  
ATOM   4254  C   LYS B 893     -89.161   2.072  -5.739  1.00 36.34           C  
ANISOU 4254  C   LYS B 893     4265   5100   4444   -355   -175    642       C  
ATOM   4255  O   LYS B 893     -88.696   2.837  -6.556  1.00 37.65           O  
ANISOU 4255  O   LYS B 893     4438   5250   4619   -337   -162    658       O  
ATOM   4256  CB  LYS B 893     -90.212   0.582  -7.360  1.00 39.58           C  
ANISOU 4256  CB  LYS B 893     4705   5593   4742   -471   -240    678       C  
ATOM   4257  CG  LYS B 893     -91.307  -0.384  -7.751  1.00 44.54           C  
ANISOU 4257  CG  LYS B 893     5327   6285   5311   -543   -287    703       C  
ATOM   4258  CD  LYS B 893     -90.962  -0.966  -9.121  1.00 49.59           C  
ANISOU 4258  CD  LYS B 893     6027   6929   5886   -599   -304    694       C  
ATOM   4259  CE  LYS B 893     -92.060  -1.825  -9.702  1.00 48.75           C  
ANISOU 4259  CE  LYS B 893     5918   6889   5716   -679   -358    722       C  
ATOM   4260  NZ  LYS B 893     -91.518  -2.702 -10.786  1.00 51.12           N  
ANISOU 4260  NZ  LYS B 893     6299   7173   5950   -739   -368    686       N  
ATOM   4261  N   GLY B 894     -88.631   1.888  -4.533  1.00 33.37           N  
ANISOU 4261  N   GLY B 894     3897   4681   4100   -331   -156    596       N  
ATOM   4262  CA  GLY B 894     -87.423   2.569  -4.127  1.00 32.08           C  
ANISOU 4262  CA  GLY B 894     3750   4452   3989   -284   -122    557       C  
ATOM   4263  C   GLY B 894     -86.865   1.834  -2.937  1.00 30.66           C  
ANISOU 4263  C   GLY B 894     3595   4235   3819   -283   -119    503       C  
ATOM   4264  O   GLY B 894     -87.347   0.750  -2.592  1.00 29.17           O  
ANISOU 4264  O   GLY B 894     3420   4068   3595   -323   -142    498       O  
ATOM   4265  N   ILE B 895     -85.845   2.411  -2.316  1.00 26.84           N  
ANISOU 4265  N   ILE B 895     3118   3696   3383   -241    -95    465       N  
ATOM   4266  CA  ILE B 895     -85.318   1.860  -1.096  1.00 25.07           C  
ANISOU 4266  CA  ILE B 895     2914   3440   3172   -233    -97    418       C  
ATOM   4267  C   ILE B 895     -85.808   2.762  -0.004  1.00 23.12           C  
ANISOU 4267  C   ILE B 895     2631   3199   2956   -191    -83    424       C  
ATOM   4268  O   ILE B 895     -85.582   3.956  -0.044  1.00 22.93           O  
ANISOU 4268  O   ILE B 895     2585   3154   2973   -150    -60    429       O  
ATOM   4269  CB  ILE B 895     -83.774   1.820  -1.084  1.00 25.82           C  
ANISOU 4269  CB  ILE B 895     3040   3470   3300   -218    -84    367       C  
ATOM   4270  CG1 ILE B 895     -83.246   1.120  -2.315  1.00 25.19           C  
ANISOU 4270  CG1 ILE B 895     2993   3383   3194   -252    -85    359       C  
ATOM   4271  CG2 ILE B 895     -83.257   1.099   0.155  1.00 25.14           C  
ANISOU 4271  CG2 ILE B 895     2977   3354   3220   -214    -98    324       C  
ATOM   4272  CD1 ILE B 895     -81.758   1.344  -2.552  1.00 25.43           C  
ANISOU 4272  CD1 ILE B 895     3037   3359   3265   -231    -62    317       C  
ATOM   4273  N   TYR B 896     -86.402   2.142   1.017  1.00 23.49           N  
ANISOU 4273  N   TYR B 896     2676   3268   2980   -203    -94    419       N  
ATOM   4274  CA  TYR B 896     -87.073   2.807   2.103  1.00 23.64           C  
ANISOU 4274  CA  TYR B 896     2662   3305   3013   -170    -77    424       C  
ATOM   4275  C   TYR B 896     -86.243   2.758   3.395  1.00 22.45           C  
ANISOU 4275  C   TYR B 896     2541   3111   2878   -150    -73    373       C  
ATOM   4276  O   TYR B 896     -85.701   1.724   3.750  1.00 24.07           O  
ANISOU 4276  O   TYR B 896     2785   3296   3062   -177    -94    348       O  
ATOM   4277  CB  TYR B 896     -88.442   2.128   2.325  1.00 24.03           C  
ANISOU 4277  CB  TYR B 896     2687   3423   3020   -205    -89    461       C  
ATOM   4278  CG  TYR B 896     -89.505   2.440   1.289  1.00 25.25           C  
ANISOU 4278  CG  TYR B 896     2795   3634   3165   -216    -95    518       C  
ATOM   4279  CD1 TYR B 896     -89.381   2.013  -0.022  1.00 26.32           C  
ANISOU 4279  CD1 TYR B 896     2947   3777   3278   -252   -117    537       C  
ATOM   4280  CD2 TYR B 896     -90.641   3.162   1.623  1.00 26.40           C  
ANISOU 4280  CD2 TYR B 896     2879   3828   3322   -187    -79    553       C  
ATOM   4281  CE1 TYR B 896     -90.323   2.309  -0.969  1.00 26.58           C  
ANISOU 4281  CE1 TYR B 896     2938   3863   3297   -264   -130    592       C  
ATOM   4282  CE2 TYR B 896     -91.607   3.461   0.657  1.00 28.16           C  
ANISOU 4282  CE2 TYR B 896     3054   4106   3541   -193    -91    611       C  
ATOM   4283  CZ  TYR B 896     -91.438   3.036  -0.626  1.00 26.29           C  
ANISOU 4283  CZ  TYR B 896     2836   3875   3277   -233   -121    631       C  
ATOM   4284  OH  TYR B 896     -92.372   3.306  -1.585  1.00 26.00           O  
ANISOU 4284  OH  TYR B 896     2754   3895   3230   -243   -141    690       O  
ATOM   4285  N   PHE B 897     -86.203   3.870   4.118  1.00 22.81           N  
ANISOU 4285  N   PHE B 897     2567   3140   2958   -103    -48    358       N  
ATOM   4286  CA  PHE B 897     -85.467   4.029   5.388  1.00 21.84           C  
ANISOU 4286  CA  PHE B 897     2470   2981   2849    -83    -45    308       C  
ATOM   4287  C   PHE B 897     -86.289   4.811   6.392  1.00 23.03           C  
ANISOU 4287  C   PHE B 897     2596   3155   3001    -50    -18    307       C  
ATOM   4288  O   PHE B 897     -87.142   5.610   6.011  1.00 21.73           O  
ANISOU 4288  O   PHE B 897     2388   3015   2853    -24      6    339       O  
ATOM   4289  CB  PHE B 897     -84.175   4.836   5.194  1.00 22.64           C  
ANISOU 4289  CB  PHE B 897     2583   3019   3002    -55    -39    273       C  
ATOM   4290  CG  PHE B 897     -83.203   4.232   4.231  1.00 21.85           C  
ANISOU 4290  CG  PHE B 897     2503   2891   2908    -79    -56    266       C  
ATOM   4291  CD1 PHE B 897     -83.299   4.501   2.865  1.00 21.63           C  
ANISOU 4291  CD1 PHE B 897     2460   2870   2887    -86    -46    298       C  
ATOM   4292  CD2 PHE B 897     -82.190   3.443   4.683  1.00 21.93           C  
ANISOU 4292  CD2 PHE B 897     2546   2869   2917    -91    -79    228       C  
ATOM   4293  CE1 PHE B 897     -82.430   3.916   1.971  1.00 21.12           C  
ANISOU 4293  CE1 PHE B 897     2417   2784   2824   -108    -54    287       C  
ATOM   4294  CE2 PHE B 897     -81.273   2.889   3.796  1.00 22.75           C  
ANISOU 4294  CE2 PHE B 897     2664   2947   3032   -106    -88    217       C  
ATOM   4295  CZ  PHE B 897     -81.422   3.103   2.430  1.00 22.32           C  
ANISOU 4295  CZ  PHE B 897     2598   2904   2980   -117    -72    245       C  
ATOM   4296  N   ALA B 898     -86.012   4.583   7.678  1.00 24.41           N  
ANISOU 4296  N   ALA B 898     2798   3319   3158    -48    -20    270       N  
ATOM   4297  CA  ALA B 898     -86.646   5.299   8.764  1.00 24.09           C  
ANISOU 4297  CA  ALA B 898     2744   3295   3113    -17     11    257       C  
ATOM   4298  C   ALA B 898     -85.609   6.070   9.590  1.00 24.99           C  
ANISOU 4298  C   ALA B 898     2888   3352   3254     12     14    199       C  
ATOM   4299  O   ALA B 898     -84.442   5.690   9.623  1.00 23.72           O  
ANISOU 4299  O   ALA B 898     2760   3150   3102     -2    -16    171       O  
ATOM   4300  CB  ALA B 898     -87.326   4.299   9.657  1.00 25.97           C  
ANISOU 4300  CB  ALA B 898     2996   3582   3291    -51      6    264       C  
ATOM   4301  N   ASP B 899     -86.053   7.121  10.283  1.00 26.18           N  
ANISOU 4301  N   ASP B 899     3027   3503   3419     52     51    180       N  
ATOM   4302  CA  ASP B 899     -85.233   7.748  11.310  1.00 27.67           C  
ANISOU 4302  CA  ASP B 899     3250   3646   3619     71     53    121       C  
ATOM   4303  C   ASP B 899     -85.648   7.311  12.716  1.00 28.20           C  
ANISOU 4303  C   ASP B 899     3344   3746   3625     61     59     98       C  
ATOM   4304  O   ASP B 899     -84.997   7.680  13.705  1.00 27.51           O  
ANISOU 4304  O   ASP B 899     3293   3628   3529     69     53     46       O  
ATOM   4305  CB  ASP B 899     -85.209   9.279  11.202  1.00 27.87           C  
ANISOU 4305  CB  ASP B 899     3259   3628   3700    121     88    101       C  
ATOM   4306  CG  ASP B 899     -86.609   9.908  11.235  1.00 29.44           C  
ANISOU 4306  CG  ASP B 899     3417   3868   3903    159    137    128       C  
ATOM   4307  OD1 ASP B 899     -87.576   9.308  11.748  1.00 29.73           O  
ANISOU 4307  OD1 ASP B 899     3438   3965   3891    148    150    145       O  
ATOM   4308  OD2 ASP B 899     -86.726  11.035  10.759  1.00 31.76           O  
ANISOU 4308  OD2 ASP B 899     3690   4128   4250    200    162    132       O  
ATOM   4309  N   MET B 900     -86.671   6.462  12.802  1.00 31.34           N  
ANISOU 4309  N   MET B 900     3727   4207   3975     36     65    136       N  
ATOM   4310  CA  MET B 900     -87.065   5.811  14.087  1.00 31.86           C  
ANISOU 4310  CA  MET B 900     3822   4310   3971     13     69    124       C  
ATOM   4311  C   MET B 900     -86.698   4.341  14.037  1.00 30.07           C  
ANISOU 4311  C   MET B 900     3628   4091   3704    -41     20    146       C  
ATOM   4312  O   MET B 900     -87.216   3.597  13.201  1.00 31.67           O  
ANISOU 4312  O   MET B 900     3809   4323   3903    -70     10    192       O  
ATOM   4313  CB  MET B 900     -88.569   5.946  14.321  1.00 36.15           C  
ANISOU 4313  CB  MET B 900     4322   4924   4492     22    121    153       C  
ATOM   4314  CG  MET B 900     -89.116   7.372  14.333  1.00 37.35           C  
ANISOU 4314  CG  MET B 900     4434   5069   4687     84    176    137       C  
ATOM   4315  SD  MET B 900     -88.670   8.252  15.843  1.00 43.83           S  
ANISOU 4315  SD  MET B 900     5306   5858   5489    116    204     58       S  
ATOM   4316  CE  MET B 900     -89.850   7.592  17.015  1.00 47.08           C  
ANISOU 4316  CE  MET B 900     5716   6354   5816     93    246     67       C  
ATOM   4317  N   VAL B 901     -85.803   3.906  14.927  1.00 32.80           N  
ANISOU 4317  N   VAL B 901     4030   4411   4023    -56    -15    113       N  
ATOM   4318  CA  VAL B 901     -85.300   2.526  14.893  1.00 32.71           C  
ANISOU 4318  CA  VAL B 901     4055   4391   3981   -100    -68    132       C  
ATOM   4319  C   VAL B 901     -86.421   1.476  14.840  1.00 32.31           C  
ANISOU 4319  C   VAL B 901     3999   4397   3881   -145    -60    183       C  
ATOM   4320  O   VAL B 901     -86.320   0.495  14.136  1.00 32.14           O  
ANISOU 4320  O   VAL B 901     3985   4369   3858   -178    -91    213       O  
ATOM   4321  CB  VAL B 901     -84.317   2.234  16.057  1.00 33.39           C  
ANISOU 4321  CB  VAL B 901     4202   4448   4037   -107   -108     95       C  
ATOM   4322  CG1 VAL B 901     -85.002   2.266  17.416  1.00 34.59           C  
ANISOU 4322  CG1 VAL B 901     4381   4643   4118   -116    -83     86       C  
ATOM   4323  CG2 VAL B 901     -83.639   0.880  15.862  1.00 33.14           C  
ANISOU 4323  CG2 VAL B 901     4206   4394   3993   -141   -167    115       C  
ATOM   4324  N   SER B 902     -87.499   1.702  15.580  1.00 34.47           N  
ANISOU 4324  N   SER B 902     4258   4727   4114   -147    -16    192       N  
ATOM   4325  CA  SER B 902     -88.567   0.702  15.695  1.00 34.27           C  
ANISOU 4325  CA  SER B 902     4226   4759   4037   -197     -7    240       C  
ATOM   4326  C   SER B 902     -89.370   0.571  14.415  1.00 33.19           C  
ANISOU 4326  C   SER B 902     4030   4652   3930   -209      3    284       C  
ATOM   4327  O   SER B 902     -89.788  -0.548  14.062  1.00 34.18           O  
ANISOU 4327  O   SER B 902     4161   4798   4028   -263    -18    324       O  
ATOM   4328  CB  SER B 902     -89.484   1.014  16.877  1.00 35.47           C  
ANISOU 4328  CB  SER B 902     4373   4967   4136   -197     45    234       C  
ATOM   4329  OG  SER B 902     -90.090   2.296  16.744  1.00 38.34           O  
ANISOU 4329  OG  SER B 902     4680   5351   4536   -144    102    218       O  
ATOM   4330  N   LYS B 903     -89.551   1.674  13.687  1.00 31.16           N  
ANISOU 4330  N   LYS B 903     3720   4393   3727   -162     30    279       N  
ATOM   4331  CA  LYS B 903     -90.229   1.601  12.374  1.00 30.37           C  
ANISOU 4331  CA  LYS B 903     3565   4319   3655   -173     30    324       C  
ATOM   4332  C   LYS B 903     -89.513   0.638  11.442  1.00 29.51           C  
ANISOU 4332  C   LYS B 903     3488   4174   3551   -210    -22    336       C  
ATOM   4333  O   LYS B 903     -90.149  -0.186  10.776  1.00 30.32           O  
ANISOU 4333  O   LYS B 903     3576   4308   3635   -257    -36    376       O  
ATOM   4334  CB  LYS B 903     -90.340   2.960  11.716  1.00 29.86           C  
ANISOU 4334  CB  LYS B 903     3450   4245   3650   -113     59    319       C  
ATOM   4335  CG  LYS B 903     -91.109   2.919  10.400  1.00 28.90           C  
ANISOU 4335  CG  LYS B 903     3271   4158   3550   -123     55    370       C  
ATOM   4336  CD  LYS B 903     -91.627   4.294  10.016  1.00 31.17           C  
ANISOU 4336  CD  LYS B 903     3500   4455   3890    -60     93    378       C  
ATOM   4337  CE  LYS B 903     -92.496   4.241   8.755  1.00 32.57           C  
ANISOU 4337  CE  LYS B 903     3617   4677   4082    -72     83    436       C  
ATOM   4338  NZ  LYS B 903     -92.865   5.601   8.253  1.00 33.13           N  
ANISOU 4338  NZ  LYS B 903     3635   4743   4209     -5    111    450       N  
ATOM   4339  N   SER B 904     -88.191   0.693  11.452  1.00 29.13           N  
ANISOU 4339  N   SER B 904     3483   4060   3525   -193    -51    299       N  
ATOM   4340  CA  SER B 904     -87.398  -0.227  10.651  1.00 29.33           C  
ANISOU 4340  CA  SER B 904     3541   4045   3558   -221    -95    302       C  
ATOM   4341  C   SER B 904     -87.316  -1.601  11.293  1.00 28.67           C  
ANISOU 4341  C   SER B 904     3513   3957   3424   -270   -128    311       C  
ATOM   4342  O   SER B 904     -87.350  -2.618  10.585  1.00 27.58           O  
ANISOU 4342  O   SER B 904     3392   3811   3276   -311   -155    333       O  
ATOM   4343  CB  SER B 904     -85.983   0.330  10.385  1.00 28.78           C  
ANISOU 4343  CB  SER B 904     3490   3908   3538   -183   -111    261       C  
ATOM   4344  OG  SER B 904     -86.039   1.312   9.380  1.00 29.13           O  
ANISOU 4344  OG  SER B 904     3491   3950   3629   -153    -89    266       O  
ATOM   4345  N   ALA B 905     -87.133  -1.651  12.608  1.00 29.68           N  
ANISOU 4345  N   ALA B 905     3674   4083   3520   -267   -129    293       N  
ATOM   4346  CA  ALA B 905     -87.019  -2.943  13.317  1.00 30.72           C  
ANISOU 4346  CA  ALA B 905     3865   4206   3601   -313   -163    307       C  
ATOM   4347  C   ALA B 905     -88.260  -3.840  13.111  1.00 32.19           C  
ANISOU 4347  C   ALA B 905     4041   4443   3745   -375   -154    357       C  
ATOM   4348  O   ALA B 905     -88.150  -5.059  13.115  1.00 31.08           O  
ANISOU 4348  O   ALA B 905     3948   4282   3579   -421   -189    377       O  
ATOM   4349  CB  ALA B 905     -86.779  -2.717  14.792  1.00 30.07           C  
ANISOU 4349  CB  ALA B 905     3818   4125   3481   -302   -161    284       C  
ATOM   4350  N   ASN B 906     -89.428  -3.237  12.905  1.00 32.49           N  
ANISOU 4350  N   ASN B 906     4017   4546   3783   -375   -110    379       N  
ATOM   4351  CA  ASN B 906     -90.619  -4.019  12.622  1.00 34.59           C  
ANISOU 4351  CA  ASN B 906     4260   4867   4015   -437   -103    427       C  
ATOM   4352  C   ASN B 906     -90.474  -4.873  11.387  1.00 35.82           C  
ANISOU 4352  C   ASN B 906     4428   4997   4184   -475   -141    445       C  
ATOM   4353  O   ASN B 906     -91.081  -5.947  11.306  1.00 38.83           O  
ANISOU 4353  O   ASN B 906     4827   5396   4531   -542   -157    479       O  
ATOM   4354  CB  ASN B 906     -91.842  -3.125  12.468  1.00 35.72           C  
ANISOU 4354  CB  ASN B 906     4319   5085   4168   -421    -51    447       C  
ATOM   4355  CG  ASN B 906     -92.309  -2.547  13.783  1.00 35.11           C  
ANISOU 4355  CG  ASN B 906     4232   5048   4062   -400     -4    435       C  
ATOM   4356  OD1 ASN B 906     -91.957  -3.037  14.860  1.00 36.29           O  
ANISOU 4356  OD1 ASN B 906     4440   5183   4166   -419    -11    424       O  
ATOM   4357  ND2 ASN B 906     -93.076  -1.467  13.703  1.00 33.54           N  
ANISOU 4357  ND2 ASN B 906     3960   4895   3887   -358     46    436       N  
ATOM   4358  N   TYR B 907     -89.670  -4.416  10.427  1.00 32.71           N  
ANISOU 4358  N   TYR B 907     4029   4561   3838   -437   -155    422       N  
ATOM   4359  CA  TYR B 907     -89.465  -5.163   9.183  1.00 30.10           C  
ANISOU 4359  CA  TYR B 907     3713   4205   3517   -470   -186    432       C  
ATOM   4360  C   TYR B 907     -88.451  -6.279   9.324  1.00 30.53           C  
ANISOU 4360  C   TYR B 907     3847   4188   3564   -488   -228    413       C  
ATOM   4361  O   TYR B 907     -88.172  -6.984   8.372  1.00 32.79           O  
ANISOU 4361  O   TYR B 907     4158   4444   3857   -513   -253    413       O  
ATOM   4362  CB  TYR B 907     -89.087  -4.216   8.039  1.00 31.15           C  
ANISOU 4362  CB  TYR B 907     3809   4329   3699   -426   -177    418       C  
ATOM   4363  CG  TYR B 907     -90.238  -3.348   7.643  1.00 31.47           C  
ANISOU 4363  CG  TYR B 907     3772   4438   3746   -417   -145    449       C  
ATOM   4364  CD1 TYR B 907     -91.297  -3.867   6.899  1.00 32.01           C  
ANISOU 4364  CD1 TYR B 907     3811   4560   3793   -472   -154    491       C  
ATOM   4365  CD2 TYR B 907     -90.318  -2.021   8.078  1.00 31.58           C  
ANISOU 4365  CD2 TYR B 907     3743   4466   3789   -356   -109    438       C  
ATOM   4366  CE1 TYR B 907     -92.385  -3.077   6.571  1.00 33.22           C  
ANISOU 4366  CE1 TYR B 907     3885   4781   3955   -460   -129    525       C  
ATOM   4367  CE2 TYR B 907     -91.404  -1.222   7.752  1.00 31.64           C  
ANISOU 4367  CE2 TYR B 907     3678   4535   3809   -340    -80    469       C  
ATOM   4368  CZ  TYR B 907     -92.427  -1.747   7.007  1.00 33.43           C  
ANISOU 4368  CZ  TYR B 907     3868   4817   4016   -389    -91    514       C  
ATOM   4369  OH  TYR B 907     -93.492  -0.967   6.661  1.00 34.77           O  
ANISOU 4369  OH  TYR B 907     3958   5049   4202   -370    -68    548       O  
ATOM   4370  N   CYS B 908     -87.896  -6.468  10.515  1.00 34.04           N  
ANISOU 4370  N   CYS B 908     4334   4605   3995   -475   -239    398       N  
ATOM   4371  CA  CYS B 908     -87.075  -7.655  10.771  1.00 33.90           C  
ANISOU 4371  CA  CYS B 908     4392   4522   3967   -494   -284    391       C  
ATOM   4372  C   CYS B 908     -87.939  -8.918  10.860  1.00 35.58           C  
ANISOU 4372  C   CYS B 908     4639   4748   4133   -572   -298    432       C  
ATOM   4373  O   CYS B 908     -87.455 -10.015  10.577  1.00 33.41           O  
ANISOU 4373  O   CYS B 908     4423   4416   3857   -597   -335    432       O  
ATOM   4374  CB  CYS B 908     -86.273  -7.474  12.039  1.00 34.33           C  
ANISOU 4374  CB  CYS B 908     4480   4548   4015   -459   -298    370       C  
ATOM   4375  SG  CYS B 908     -85.055  -6.143  11.977  1.00 36.08           S  
ANISOU 4375  SG  CYS B 908     4672   4740   4297   -377   -292    317       S  
ATOM   4376  N   HIS B 909     -89.214  -8.735  11.231  1.00 36.61           N  
ANISOU 4376  N   HIS B 909     4729   4953   4227   -609   -267    467       N  
ATOM   4377  CA  HIS B 909     -90.178  -9.824  11.418  1.00 41.21           C  
ANISOU 4377  CA  HIS B 909     5334   5560   4763   -692   -274    510       C  
ATOM   4378  C   HIS B 909     -89.663 -10.832  12.421  1.00 38.71           C  
ANISOU 4378  C   HIS B 909     5103   5191   4414   -715   -307    518       C  
ATOM   4379  O   HIS B 909     -89.670 -12.021  12.179  1.00 36.33           O  
ANISOU 4379  O   HIS B 909     4857   4848   4099   -768   -339    536       O  
ATOM   4380  CB  HIS B 909     -90.601 -10.465  10.081  1.00 42.69           C  
ANISOU 4380  CB  HIS B 909     5516   5745   4957   -742   -292    524       C  
ATOM   4381  CG  HIS B 909     -91.439  -9.547   9.241  1.00 47.23           C  
ANISOU 4381  CG  HIS B 909     6004   6392   5549   -735   -262    534       C  
ATOM   4382  ND1 HIS B 909     -91.006  -9.017   8.035  1.00 49.37           N  
ANISOU 4382  ND1 HIS B 909     6251   6649   5859   -701   -266    513       N  
ATOM   4383  CD2 HIS B 909     -92.657  -9.005   9.473  1.00 48.20           C  
ANISOU 4383  CD2 HIS B 909     6054   6603   5658   -752   -227    566       C  
ATOM   4384  CE1 HIS B 909     -91.941  -8.215   7.551  1.00 49.90           C  
ANISOU 4384  CE1 HIS B 909     6238   6789   5931   -698   -241    535       C  
ATOM   4385  NE2 HIS B 909     -92.948  -8.183   8.408  1.00 51.50           N  
ANISOU 4385  NE2 HIS B 909     6406   7055   6107   -726   -217    566       N  
ATOM   4386  N   THR B 910     -89.169 -10.325  13.540  1.00 38.59           N  
ANISOU 4386  N   THR B 910     5102   5173   4388   -673   -301    503       N  
ATOM   4387  CA  THR B 910     -88.742 -11.194  14.608  1.00 38.55           C  
ANISOU 4387  CA  THR B 910     5176   5126   4344   -694   -333    517       C  
ATOM   4388  C   THR B 910     -89.960 -11.621  15.390  1.00 39.24           C  
ANISOU 4388  C   THR B 910     5266   5275   4369   -765   -307    565       C  
ATOM   4389  O   THR B 910     -91.035 -11.082  15.204  1.00 43.90           O  
ANISOU 4389  O   THR B 910     5786   5943   4950   -784   -260    579       O  
ATOM   4390  CB  THR B 910     -87.719 -10.515  15.521  1.00 34.65           C  
ANISOU 4390  CB  THR B 910     4700   4609   3857   -627   -344    483       C  
ATOM   4391  OG1 THR B 910     -88.205  -9.253  15.953  1.00 32.24           O  
ANISOU 4391  OG1 THR B 910     4335   4371   3545   -597   -293    468       O  
ATOM   4392  CG2 THR B 910     -86.430 -10.364  14.790  1.00 37.39           C  
ANISOU 4392  CG2 THR B 910     5052   4887   4267   -569   -377    442       C  
ATOM   4393  N   SER B 911     -89.786 -12.585  16.275  1.00 41.89           N  
ANISOU 4393  N   SER B 911     5680   5577   4661   -803   -336    592       N  
ATOM   4394  CA  SER B 911     -90.897 -13.093  17.107  1.00 45.44           C  
ANISOU 4394  CA  SER B 911     6141   6082   5042   -879   -309    642       C  
ATOM   4395  C   SER B 911     -90.337 -13.646  18.409  1.00 44.26           C  
ANISOU 4395  C   SER B 911     6078   5895   4842   -886   -339    659       C  
ATOM   4396  O   SER B 911     -89.113 -13.683  18.595  1.00 47.96           O  
ANISOU 4396  O   SER B 911     6594   6295   5333   -831   -386    633       O  
ATOM   4397  CB  SER B 911     -91.674 -14.160  16.347  1.00 42.92           C  
ANISOU 4397  CB  SER B 911     5831   5758   4719   -965   -320    681       C  
ATOM   4398  OG  SER B 911     -90.790 -15.201  15.957  1.00 44.59           O  
ANISOU 4398  OG  SER B 911     6124   5867   4952   -970   -380    678       O  
ATOM   4399  N   GLN B 912     -91.219 -14.030  19.328  1.00 49.27           N  
ANISOU 4399  N   GLN B 912     6732   6580   5407   -951   -311    704       N  
ATOM   4400  CA  GLN B 912     -90.782 -14.555  20.639  1.00 46.91           C  
ANISOU 4400  CA  GLN B 912     6522   6256   5048   -965   -338    728       C  
ATOM   4401  C   GLN B 912     -89.942 -15.811  20.426  1.00 45.07           C  
ANISOU 4401  C   GLN B 912     6380   5913   4830   -979   -414    748       C  
ATOM   4402  O   GLN B 912     -88.939 -16.020  21.112  1.00 46.62           O  
ANISOU 4402  O   GLN B 912     6642   6053   5017   -941   -463    745       O  
ATOM   4403  CB  GLN B 912     -91.966 -14.797  21.589  1.00 47.57           C  
ANISOU 4403  CB  GLN B 912     6608   6416   5048  -1043   -287    778       C  
ATOM   4404  N   GLY B 913     -90.318 -16.615  19.435  1.00 46.49           N  
ANISOU 4404  N   GLY B 913     6562   6061   5040  -1028   -426    765       N  
ATOM   4405  CA  GLY B 913     -89.585 -17.821  19.082  1.00 48.39           C  
ANISOU 4405  CA  GLY B 913     6889   6192   5306  -1039   -492    778       C  
ATOM   4406  C   GLY B 913     -88.270 -17.601  18.384  1.00 53.12           C  
ANISOU 4406  C   GLY B 913     7488   6716   5977   -950   -534    725       C  
ATOM   4407  O   GLY B 913     -87.399 -18.479  18.456  1.00 54.03           O  
ANISOU 4407  O   GLY B 913     7680   6737   6110   -934   -593    732       O  
ATOM   4408  N   ASP B 914     -88.132 -16.467  17.676  1.00 55.62           N  
ANISOU 4408  N   ASP B 914     7720   7074   6340   -892   -504    675       N  
ATOM   4409  CA  ASP B 914     -86.854 -16.036  17.076  1.00 59.50           C  
ANISOU 4409  CA  ASP B 914     8199   7509   6899   -804   -533    621       C  
ATOM   4410  C   ASP B 914     -86.640 -14.514  17.258  1.00 55.46           C  
ANISOU 4410  C   ASP B 914     7611   7058   6402   -738   -497    578       C  
ATOM   4411  O   ASP B 914     -86.940 -13.707  16.357  1.00 53.13           O  
ANISOU 4411  O   ASP B 914     7241   6801   6143   -718   -460    550       O  
ATOM   4412  CB  ASP B 914     -86.780 -16.424  15.589  1.00 67.08           C  
ANISOU 4412  CB  ASP B 914     9145   8428   7915   -808   -537    599       C  
ATOM   4413  CG  ASP B 914     -85.338 -16.377  15.038  1.00 75.05           C  
ANISOU 4413  CG  ASP B 914    10164   9358   8992   -726   -574    551       C  
ATOM   4414  OD1 ASP B 914     -85.089 -16.962  13.954  1.00 84.95           O  
ANISOU 4414  OD1 ASP B 914    11432  10559  10285   -729   -586    534       O  
ATOM   4415  OD2 ASP B 914     -84.447 -15.782  15.705  1.00 74.49           O  
ANISOU 4415  OD2 ASP B 914    10088   9280   8934   -662   -591    530       O  
ATOM   4416  N   PRO B 915     -86.124 -14.120  18.428  1.00 47.75           N  
ANISOU 4416  N   PRO B 915     6658   6088   5396   -705   -511    574       N  
ATOM   4417  CA  PRO B 915     -86.116 -12.731  18.853  1.00 48.03           C  
ANISOU 4417  CA  PRO B 915     6635   6186   5429   -659   -473    539       C  
ATOM   4418  C   PRO B 915     -84.831 -11.935  18.511  1.00 45.45           C  
ANISOU 4418  C   PRO B 915     6280   5820   5168   -574   -497    482       C  
ATOM   4419  O   PRO B 915     -84.647 -10.832  18.997  1.00 43.27           O  
ANISOU 4419  O   PRO B 915     5971   5580   4889   -535   -476    450       O  
ATOM   4420  CB  PRO B 915     -86.278 -12.873  20.370  1.00 48.17           C  
ANISOU 4420  CB  PRO B 915     6707   6229   5367   -683   -479    567       C  
ATOM   4421  CG  PRO B 915     -85.473 -14.099  20.694  1.00 46.96           C  
ANISOU 4421  CG  PRO B 915     6643   5990   5209   -691   -553    596       C  
ATOM   4422  CD  PRO B 915     -85.598 -15.005  19.482  1.00 49.02           C  
ANISOU 4422  CD  PRO B 915     6910   6199   5518   -718   -566    607       C  
ATOM   4423  N   ILE B 916     -83.948 -12.522  17.713  1.00 44.95           N  
ANISOU 4423  N   ILE B 916     6234   5682   5162   -549   -539    469       N  
ATOM   4424  CA  ILE B 916     -82.735 -11.874  17.289  1.00 42.75           C  
ANISOU 4424  CA  ILE B 916     5925   5368   4951   -476   -559    418       C  
ATOM   4425  C   ILE B 916     -82.901 -11.421  15.828  1.00 41.32           C  
ANISOU 4425  C   ILE B 916     5680   5193   4826   -464   -521    392       C  
ATOM   4426  O   ILE B 916     -83.175 -12.240  14.935  1.00 39.16           O  
ANISOU 4426  O   ILE B 916     5421   4893   4566   -494   -524    406       O  
ATOM   4427  CB  ILE B 916     -81.525 -12.821  17.393  1.00 44.53           C  
ANISOU 4427  CB  ILE B 916     6206   5504   5207   -447   -629    419       C  
ATOM   4428  CG1 ILE B 916     -81.444 -13.436  18.813  1.00 46.90           C  
ANISOU 4428  CG1 ILE B 916     6581   5796   5445   -468   -674    458       C  
ATOM   4429  CG2 ILE B 916     -80.270 -12.092  16.924  1.00 45.06           C  
ANISOU 4429  CG2 ILE B 916     6228   5544   5350   -373   -644    365       C  
ATOM   4430  CD1 ILE B 916     -81.172 -12.463  19.935  1.00 46.61           C  
ANISOU 4430  CD1 ILE B 916     6534   5804   5373   -443   -677    441       C  
ATOM   4431  N   GLY B 917     -82.727 -10.114  15.610  1.00 37.40           N  
ANISOU 4431  N   GLY B 917     5119   4731   4359   -421   -489    355       N  
ATOM   4432  CA  GLY B 917     -82.801  -9.533  14.286  1.00 37.61           C  
ANISOU 4432  CA  GLY B 917     5087   4766   4437   -404   -455    332       C  
ATOM   4433  C   GLY B 917     -81.561  -8.758  13.859  1.00 35.53           C  
ANISOU 4433  C   GLY B 917     4790   4469   4240   -339   -463    284       C  
ATOM   4434  O   GLY B 917     -80.683  -8.445  14.680  1.00 33.34           O  
ANISOU 4434  O   GLY B 917     4523   4173   3972   -304   -493    263       O  
ATOM   4435  N   LEU B 918     -81.513  -8.457  12.559  1.00 33.75           N  
ANISOU 4435  N   LEU B 918     4524   4241   4059   -329   -438    268       N  
ATOM   4436  CA  LEU B 918     -80.467  -7.653  11.965  1.00 32.13           C  
ANISOU 4436  CA  LEU B 918     4278   4011   3917   -276   -433    225       C  
ATOM   4437  C   LEU B 918     -81.044  -6.376  11.353  1.00 31.82           C  
ANISOU 4437  C   LEU B 918     4176   4021   3892   -267   -380    218       C  
ATOM   4438  O   LEU B 918     -82.080  -6.401  10.674  1.00 32.59           O  
ANISOU 4438  O   LEU B 918     4256   4157   3971   -299   -350    243       O  
ATOM   4439  CB  LEU B 918     -79.753  -8.446  10.896  1.00 32.59           C  
ANISOU 4439  CB  LEU B 918     4350   4015   4017   -268   -447    212       C  
ATOM   4440  CG  LEU B 918     -78.966  -9.686  11.343  1.00 31.25           C  
ANISOU 4440  CG  LEU B 918     4239   3781   3853   -261   -502    214       C  
ATOM   4441  CD1 LEU B 918     -78.398 -10.425  10.130  1.00 32.15           C  
ANISOU 4441  CD1 LEU B 918     4363   3844   4009   -252   -502    196       C  
ATOM   4442  CD2 LEU B 918     -77.865  -9.290  12.300  1.00 30.36           C  
ANISOU 4442  CD2 LEU B 918     4122   3647   3766   -214   -538    193       C  
ATOM   4443  N   ILE B 919     -80.359  -5.262  11.610  1.00 29.42           N  
ANISOU 4443  N   ILE B 919     3840   3714   3624   -224   -372    185       N  
ATOM   4444  CA  ILE B 919     -80.770  -3.969  11.106  1.00 27.58           C  
ANISOU 4444  CA  ILE B 919     3552   3516   3412   -208   -324    177       C  
ATOM   4445  C   ILE B 919     -79.544  -3.166  10.608  1.00 28.79           C  
ANISOU 4445  C   ILE B 919     3675   3633   3633   -166   -323    137       C  
ATOM   4446  O   ILE B 919     -78.449  -3.225  11.195  1.00 32.28           O  
ANISOU 4446  O   ILE B 919     4128   4039   4099   -143   -358    110       O  
ATOM   4447  CB  ILE B 919     -81.548  -3.217  12.195  1.00 27.66           C  
ANISOU 4447  CB  ILE B 919     3555   3570   3384   -208   -303    181       C  
ATOM   4448  CG1 ILE B 919     -82.245  -2.010  11.628  1.00 28.87           C  
ANISOU 4448  CG1 ILE B 919     3653   3759   3556   -193   -252    183       C  
ATOM   4449  CG2 ILE B 919     -80.618  -2.755  13.302  1.00 28.47           C  
ANISOU 4449  CG2 ILE B 919     3674   3650   3494   -180   -329    146       C  
ATOM   4450  CD1 ILE B 919     -83.329  -1.509  12.543  1.00 30.05           C  
ANISOU 4450  CD1 ILE B 919     3795   3961   3662   -198   -221    194       C  
ATOM   4451  N   LEU B 920     -79.725  -2.435   9.515  1.00 27.11           N  
ANISOU 4451  N   LEU B 920     3421   3430   3449   -158   -285    137       N  
ATOM   4452  CA  LEU B 920     -78.652  -1.640   8.918  1.00 25.73           C  
ANISOU 4452  CA  LEU B 920     3214   3224   3337   -126   -275    106       C  
ATOM   4453  C   LEU B 920     -78.716  -0.166   9.300  1.00 25.28           C  
ANISOU 4453  C   LEU B 920     3126   3179   3302   -103   -249     90       C  
ATOM   4454  O   LEU B 920     -79.800   0.389   9.499  1.00 25.81           O  
ANISOU 4454  O   LEU B 920     3181   3284   3342   -107   -221    110       O  
ATOM   4455  CB  LEU B 920     -78.734  -1.714   7.420  1.00 25.40           C  
ANISOU 4455  CB  LEU B 920     3155   3183   3313   -135   -249    117       C  
ATOM   4456  CG  LEU B 920     -78.500  -3.087   6.830  1.00 26.98           C  
ANISOU 4456  CG  LEU B 920     3388   3361   3501   -155   -269    121       C  
ATOM   4457  CD1 LEU B 920     -79.004  -3.144   5.414  1.00 27.86           C  
ANISOU 4457  CD1 LEU B 920     3490   3491   3606   -177   -240    139       C  
ATOM   4458  CD2 LEU B 920     -77.038  -3.425   6.871  1.00 28.40           C  
ANISOU 4458  CD2 LEU B 920     3572   3490   3730   -127   -292     84       C  
ATOM   4459  N   LEU B 921     -77.552   0.452   9.429  1.00 24.41           N  
ANISOU 4459  N   LEU B 921     3000   3034   3242    -78   -258     54       N  
ATOM   4460  CA  LEU B 921     -77.476   1.911   9.360  1.00 26.29           C  
ANISOU 4460  CA  LEU B 921     3205   3269   3515    -59   -226     38       C  
ATOM   4461  C   LEU B 921     -76.809   2.241   8.053  1.00 24.58           C  
ANISOU 4461  C   LEU B 921     2959   3031   3351    -54   -204     35       C  
ATOM   4462  O   LEU B 921     -75.702   1.796   7.796  1.00 23.66           O  
ANISOU 4462  O   LEU B 921     2838   2885   3267    -50   -223     14       O  
ATOM   4463  CB  LEU B 921     -76.684   2.495  10.511  1.00 27.10           C  
ANISOU 4463  CB  LEU B 921     3314   3350   3635    -44   -251     -3       C  
ATOM   4464  CG  LEU B 921     -77.444   2.573  11.833  1.00 27.69           C  
ANISOU 4464  CG  LEU B 921     3417   3450   3653    -47   -258     -4       C  
ATOM   4465  CD1 LEU B 921     -76.451   2.825  12.954  1.00 26.86           C  
ANISOU 4465  CD1 LEU B 921     3328   3321   3556    -39   -300    -46       C  
ATOM   4466  CD2 LEU B 921     -78.489   3.685  11.814  1.00 28.67           C  
ANISOU 4466  CD2 LEU B 921     3524   3598   3771    -37   -207      3       C  
ATOM   4467  N   GLY B 922     -77.520   2.984   7.221  1.00 23.55           N  
ANISOU 4467  N   GLY B 922     2806   2917   3224    -54   -163     60       N  
ATOM   4468  CA  GLY B 922     -76.994   3.426   5.948  1.00 22.98           C  
ANISOU 4468  CA  GLY B 922     2710   2830   3194    -53   -136     63       C  
ATOM   4469  C   GLY B 922     -76.804   4.945   5.898  1.00 23.09           C  
ANISOU 4469  C   GLY B 922     2697   2824   3251    -36   -107     55       C  
ATOM   4470  O   GLY B 922     -77.596   5.709   6.457  1.00 23.22           O  
ANISOU 4470  O   GLY B 922     2713   2852   3258    -23    -94     62       O  
ATOM   4471  N   GLU B 923     -75.724   5.387   5.265  1.00 22.00           N  
ANISOU 4471  N   GLU B 923     2540   2655   3166    -35    -95     37       N  
ATOM   4472  CA  GLU B 923     -75.584   6.814   4.932  1.00 22.60           C  
ANISOU 4472  CA  GLU B 923     2594   2707   3285    -26    -62     39       C  
ATOM   4473  C   GLU B 923     -76.373   6.973   3.638  1.00 21.85           C  
ANISOU 4473  C   GLU B 923     2493   2635   3174    -33    -29     89       C  
ATOM   4474  O   GLU B 923     -76.068   6.316   2.645  1.00 22.05           O  
ANISOU 4474  O   GLU B 923     2519   2669   3191    -49    -22    100       O  
ATOM   4475  CB  GLU B 923     -74.128   7.199   4.731  1.00 23.93           C  
ANISOU 4475  CB  GLU B 923     2741   2837   3515    -31    -61      5       C  
ATOM   4476  CG  GLU B 923     -73.944   8.690   4.476  1.00 25.94           C  
ANISOU 4476  CG  GLU B 923     2980   3059   3817    -28    -29      6       C  
ATOM   4477  CD  GLU B 923     -72.519   9.069   4.084  1.00 25.88           C  
ANISOU 4477  CD  GLU B 923     2945   3018   3872    -42    -21    -21       C  
ATOM   4478  OE1 GLU B 923     -71.586   8.431   4.629  1.00 26.08           O  
ANISOU 4478  OE1 GLU B 923     2959   3037   3913    -45    -54    -57       O  
ATOM   4479  OE2 GLU B 923     -72.351  10.000   3.234  1.00 26.08           O  
ANISOU 4479  OE2 GLU B 923     2957   3022   3930    -51     17     -2       O  
ATOM   4480  N   VAL B 924     -77.416   7.786   3.671  1.00 21.28           N  
ANISOU 4480  N   VAL B 924     2417   2575   3092    -19    -11    118       N  
ATOM   4481  CA  VAL B 924     -78.268   7.994   2.502  1.00 22.26           C  
ANISOU 4481  CA  VAL B 924     2533   2725   3198    -23     13    172       C  
ATOM   4482  C   VAL B 924     -78.112   9.433   2.006  1.00 22.87           C  
ANISOU 4482  C   VAL B 924     2597   2768   3324     -9     44    188       C  
ATOM   4483  O   VAL B 924     -78.266  10.391   2.769  1.00 25.63           O  
ANISOU 4483  O   VAL B 924     2945   3091   3702     15     52    173       O  
ATOM   4484  CB  VAL B 924     -79.740   7.731   2.858  1.00 22.88           C  
ANISOU 4484  CB  VAL B 924     2611   2851   3230    -16      7    204       C  
ATOM   4485  CG1 VAL B 924     -80.622   7.836   1.641  1.00 23.28           C  
ANISOU 4485  CG1 VAL B 924     2650   2936   3259    -23     20    262       C  
ATOM   4486  CG2 VAL B 924     -79.900   6.367   3.508  1.00 23.69           C  
ANISOU 4486  CG2 VAL B 924     2734   2981   3288    -34    -25    189       C  
ATOM   4487  N   ALA B 925     -77.798   9.596   0.738  1.00 24.03           N  
ANISOU 4487  N   ALA B 925     2740   2913   3478    -25     64    216       N  
ATOM   4488  CA  ALA B 925     -77.610  10.938   0.174  1.00 25.37           C  
ANISOU 4488  CA  ALA B 925     2901   3045   3693    -17     94    239       C  
ATOM   4489  C   ALA B 925     -78.966  11.460  -0.312  1.00 25.82           C  
ANISOU 4489  C   ALA B 925     2954   3128   3729      2    102    300       C  
ATOM   4490  O   ALA B 925     -79.398  11.173  -1.423  1.00 25.56           O  
ANISOU 4490  O   ALA B 925     2921   3128   3663    -13    105    347       O  
ATOM   4491  CB  ALA B 925     -76.619  10.896  -0.970  1.00 25.14           C  
ANISOU 4491  CB  ALA B 925     2871   3004   3677    -46    116    245       C  
ATOM   4492  N   LEU B 926     -79.639  12.221   0.543  1.00 26.72           N  
ANISOU 4492  N   LEU B 926     3063   3228   3862     37    105    298       N  
ATOM   4493  CA  LEU B 926     -81.022  12.589   0.274  1.00 28.08           C  
ANISOU 4493  CA  LEU B 926     3221   3432   4017     64    108    353       C  
ATOM   4494  C   LEU B 926     -81.147  13.816  -0.616  1.00 29.60           C  
ANISOU 4494  C   LEU B 926     3410   3590   4246     80    131    402       C  
ATOM   4495  O   LEU B 926     -82.163  13.993  -1.286  1.00 32.78           O  
ANISOU 4495  O   LEU B 926     3799   4026   4631     94    128    463       O  
ATOM   4496  CB  LEU B 926     -81.759  12.839   1.597  1.00 26.82           C  
ANISOU 4496  CB  LEU B 926     3055   3275   3861    100    107    327       C  
ATOM   4497  CG  LEU B 926     -81.831  11.641   2.522  1.00 26.56           C  
ANISOU 4497  CG  LEU B 926     3029   3281   3784     84     84    290       C  
ATOM   4498  CD1 LEU B 926     -82.267  12.086   3.890  1.00 27.56           C  
ANISOU 4498  CD1 LEU B 926     3156   3398   3917    117     92    254       C  
ATOM   4499  CD2 LEU B 926     -82.783  10.610   1.987  1.00 27.18           C  
ANISOU 4499  CD2 LEU B 926     3094   3428   3805     65     68    332       C  
ATOM   4500  N   GLY B 927     -80.164  14.708  -0.532  1.00 30.35           N  
ANISOU 4500  N   GLY B 927     3518   3619   4396     79    150    378       N  
ATOM   4501  CA  GLY B 927     -80.229  15.947  -1.247  1.00 32.10           C  
ANISOU 4501  CA  GLY B 927     3743   3794   4657     94    172    424       C  
ATOM   4502  C   GLY B 927     -81.520  16.693  -0.924  1.00 32.35           C  
ANISOU 4502  C   GLY B 927     3763   3827   4703    149    175    459       C  
ATOM   4503  O   GLY B 927     -81.907  16.800   0.224  1.00 33.68           O  
ANISOU 4503  O   GLY B 927     3927   3989   4880    179    175    419       O  
ATOM   4504  N   ASN B 928     -82.109  17.295  -1.936  1.00 33.03           N  
ANISOU 4504  N   ASN B 928     3844   3912   4793    163    180    532       N  
ATOM   4505  CA  ASN B 928     -83.378  18.019  -1.841  1.00 35.87           C  
ANISOU 4505  CA  ASN B 928     4184   4274   5170    221    181    578       C  
ATOM   4506  C   ASN B 928     -84.533  17.025  -1.861  1.00 32.46           C  
ANISOU 4506  C   ASN B 928     3719   3934   4680    226    157    604       C  
ATOM   4507  O   ASN B 928     -84.787  16.325  -2.844  1.00 31.72           O  
ANISOU 4507  O   ASN B 928     3618   3897   4536    194    136    649       O  
ATOM   4508  CB  ASN B 928     -83.469  18.990  -3.030  1.00 39.82           C  
ANISOU 4508  CB  ASN B 928     4693   4739   5695    230    189    655       C  
ATOM   4509  CG  ASN B 928     -84.507  20.059  -2.872  1.00 46.77           C  
ANISOU 4509  CG  ASN B 928     5559   5590   6620    300    195    698       C  
ATOM   4510  OD1 ASN B 928     -85.315  20.093  -1.919  1.00 45.58           O  
ANISOU 4510  OD1 ASN B 928     5385   5454   6481    347    198    673       O  
ATOM   4511  ND2 ASN B 928     -84.544  20.933  -3.886  1.00 48.83           N  
ANISOU 4511  ND2 ASN B 928     5834   5814   6906    308    198    769       N  
ATOM   4512  N   MET B 929     -85.210  16.968  -0.735  1.00 34.08           N  
ANISOU 4512  N   MET B 929     3905   4154   4890    262    161    571       N  
ATOM   4513  CA  MET B 929     -86.252  15.993  -0.489  1.00 34.03           C  
ANISOU 4513  CA  MET B 929     3864   4233   4832    261    142    583       C  
ATOM   4514  C   MET B 929     -87.600  16.507  -0.984  1.00 33.90           C  
ANISOU 4514  C   MET B 929     3805   4251   4825    307    137    657       C  
ATOM   4515  O   MET B 929     -87.951  17.646  -0.752  1.00 32.70           O  
ANISOU 4515  O   MET B 929     3645   4052   4728    366    158    670       O  
ATOM   4516  CB  MET B 929     -86.348  15.728   1.013  1.00 34.98           C  
ANISOU 4516  CB  MET B 929     3983   4356   4951    277    154    513       C  
ATOM   4517  CG  MET B 929     -85.095  15.100   1.602  1.00 33.42           C  
ANISOU 4517  CG  MET B 929     3823   4135   4740    233    148    443       C  
ATOM   4518  SD  MET B 929     -85.122  14.886   3.395  1.00 33.05           S  
ANISOU 4518  SD  MET B 929     3786   4085   4685    249    158    363       S  
ATOM   4519  CE  MET B 929     -85.460  16.544   3.946  1.00 36.85           C  
ANISOU 4519  CE  MET B 929     4269   4497   5235    318    197    351       C  
ATOM   4520  N   TYR B 930     -88.306  15.651  -1.702  1.00 34.49           N  
ANISOU 4520  N   TYR B 930     3852   4406   4846    280    107    705       N  
ATOM   4521  CA  TYR B 930     -89.640  15.893  -2.110  1.00 36.39           C  
ANISOU 4521  CA  TYR B 930     4041   4699   5087    316     92    774       C  
ATOM   4522  C   TYR B 930     -90.475  15.442  -0.924  1.00 37.99           C  
ANISOU 4522  C   TYR B 930     4205   4948   5282    337    103    740       C  
ATOM   4523  O   TYR B 930     -90.616  14.252  -0.672  1.00 35.43           O  
ANISOU 4523  O   TYR B 930     3876   4683   4903    290     87    721       O  
ATOM   4524  CB  TYR B 930     -89.928  15.070  -3.368  1.00 38.84           C  
ANISOU 4524  CB  TYR B 930     4344   5078   5336    262     51    833       C  
ATOM   4525  CG  TYR B 930     -91.248  15.315  -4.081  1.00 43.32           C  
ANISOU 4525  CG  TYR B 930     4855   5705   5898    290     22    919       C  
ATOM   4526  CD1 TYR B 930     -91.919  16.521  -4.002  1.00 50.79           C  
ANISOU 4526  CD1 TYR B 930     5768   6622   6906    367     34    961       C  
ATOM   4527  CD2 TYR B 930     -91.769  14.345  -4.914  1.00 49.24           C  
ANISOU 4527  CD2 TYR B 930     5590   6538   6583    236    -20    960       C  
ATOM   4528  CE1 TYR B 930     -93.103  16.740  -4.703  1.00 56.78           C  
ANISOU 4528  CE1 TYR B 930     6471   7439   7665    394      2   1045       C  
ATOM   4529  CE2 TYR B 930     -92.949  14.546  -5.614  1.00 54.43           C  
ANISOU 4529  CE2 TYR B 930     6192   7255   7232    255    -55   1042       C  
ATOM   4530  CZ  TYR B 930     -93.614  15.745  -5.507  1.00 55.87           C  
ANISOU 4530  CZ  TYR B 930     6335   7413   7481    336    -45   1087       C  
ATOM   4531  OH  TYR B 930     -94.801  15.920  -6.181  1.00 59.87           O  
ANISOU 4531  OH  TYR B 930     6779   7985   7984    359    -85   1171       O  
ATOM   4532  N   GLU B 931     -91.038  16.397  -0.205  1.00 39.84           N  
ANISOU 4532  N   GLU B 931     4414   5153   5569    408    133    734       N  
ATOM   4533  CA  GLU B 931     -91.762  16.098   1.023  1.00 42.30           C  
ANISOU 4533  CA  GLU B 931     4694   5504   5875    432    156    694       C  
ATOM   4534  C   GLU B 931     -93.231  15.808   0.729  1.00 43.25           C  
ANISOU 4534  C   GLU B 931     4737   5715   5982    451    141    757       C  
ATOM   4535  O   GLU B 931     -93.907  16.622   0.148  1.00 50.85           O  
ANISOU 4535  O   GLU B 931     5660   6675   6984    503    137    818       O  
ATOM   4536  CB  GLU B 931     -91.629  17.263   1.982  1.00 41.67           C  
ANISOU 4536  CB  GLU B 931     4628   5348   5857    500    202    647       C  
ATOM   4537  CG  GLU B 931     -90.182  17.647   2.195  1.00 44.06           C  
ANISOU 4537  CG  GLU B 931     5002   5560   6178    477    212    590       C  
ATOM   4538  CD  GLU B 931     -89.953  18.504   3.423  1.00 48.94           C  
ANISOU 4538  CD  GLU B 931     5645   6110   6839    524    254    519       C  
ATOM   4539  OE1 GLU B 931     -90.934  19.031   3.983  1.00 55.43           O  
ANISOU 4539  OE1 GLU B 931     6432   6943   7688    588    284    520       O  
ATOM   4540  OE2 GLU B 931     -88.783  18.634   3.830  1.00 53.03           O  
ANISOU 4540  OE2 GLU B 931     6218   6568   7365    496    258    461       O  
ATOM   4541  N   LEU B 932     -93.713  14.641   1.118  1.00 41.58           N  
ANISOU 4541  N   LEU B 932     4501   5583   5715    406    129    747       N  
ATOM   4542  CA  LEU B 932     -95.067  14.213   0.792  1.00 43.10           C  
ANISOU 4542  CA  LEU B 932     4615   5870   5889    407    109    807       C  
ATOM   4543  C   LEU B 932     -95.772  13.739   2.058  1.00 45.04           C  
ANISOU 4543  C   LEU B 932     4825   6168   6121    413    142    768       C  
ATOM   4544  O   LEU B 932     -95.140  13.148   2.951  1.00 41.76           O  
ANISOU 4544  O   LEU B 932     4457   5738   5674    379    157    702       O  
ATOM   4545  CB  LEU B 932     -95.047  13.075  -0.234  1.00 41.93           C  
ANISOU 4545  CB  LEU B 932     4472   5781   5676    324     55    845       C  
ATOM   4546  CG  LEU B 932     -94.466  13.464  -1.598  1.00 45.08           C  
ANISOU 4546  CG  LEU B 932     4905   6147   6078    311     23    891       C  
ATOM   4547  CD1 LEU B 932     -94.340  12.260  -2.512  1.00 42.44           C  
ANISOU 4547  CD1 LEU B 932     4589   5865   5670    224    -24    912       C  
ATOM   4548  CD2 LEU B 932     -95.323  14.541  -2.259  1.00 47.00           C  
ANISOU 4548  CD2 LEU B 932     5094   6395   6368    377     14    968       C  
ATOM   4549  N   LYS B 933     -97.075  14.011   2.125  1.00 45.87           N  
ANISOU 4549  N   LYS B 933     4846   6336   6248    458    151    811       N  
ATOM   4550  CA  LYS B 933     -97.901  13.634   3.273  1.00 47.52           C  
ANISOU 4550  CA  LYS B 933     5006   6604   6444    467    190    783       C  
ATOM   4551  C   LYS B 933     -98.766  12.417   2.947  1.00 49.53           C  
ANISOU 4551  C   LYS B 933     5206   6968   6645    399    154    826       C  
ATOM   4552  O   LYS B 933     -99.243  11.750   3.860  1.00 53.59           O  
ANISOU 4552  O   LYS B 933     5698   7535   7128    374    179    800       O  
ATOM   4553  CB  LYS B 933     -98.752  14.829   3.731  1.00 46.58           C  
ANISOU 4553  CB  LYS B 933     4825   6477   6395    571    238    792       C  
ATOM   4554  N   HIS B 934     -98.921  12.075   1.666  1.00 50.16           N  
ANISOU 4554  N   HIS B 934     5272   7080   6707    359     95    890       N  
ATOM   4555  CA  HIS B 934     -99.766  10.949   1.269  1.00 52.51           C  
ANISOU 4555  CA  HIS B 934     5518   7479   6954    288     55    932       C  
ATOM   4556  C   HIS B 934     -99.147  10.172   0.121  1.00 50.69           C  
ANISOU 4556  C   HIS B 934     5341   7246   6671    208     -7    953       C  
ATOM   4557  O   HIS B 934     -98.252  10.652  -0.531  1.00 51.29           O  
ANISOU 4557  O   HIS B 934     5475   7255   6758    218    -18    952       O  
ATOM   4558  CB  HIS B 934    -101.169  11.441   0.871  1.00 54.66           C  
ANISOU 4558  CB  HIS B 934     5676   7828   7266    336     45   1005       C  
ATOM   4559  CG  HIS B 934    -101.773  12.376   1.866  1.00 60.57           C  
ANISOU 4559  CG  HIS B 934     6368   8570   8076    431    111    987       C  
ATOM   4560  ND1 HIS B 934    -102.309  11.945   3.066  1.00 62.25           N  
ANISOU 4560  ND1 HIS B 934     6547   8830   8274    425    162    947       N  
ATOM   4561  CD2 HIS B 934    -101.882  13.725   1.865  1.00 61.49           C  
ANISOU 4561  CD2 HIS B 934     6464   8632   8267    534    140    997       C  
ATOM   4562  CE1 HIS B 934    -102.728  12.991   3.754  1.00 64.96           C  
ANISOU 4562  CE1 HIS B 934     6850   9153   8680    523    221    930       C  
ATOM   4563  NE2 HIS B 934    -102.484  14.081   3.047  1.00 64.40           N  
ANISOU 4563  NE2 HIS B 934     6786   9017   8665    592    208    959       N  
ATOM   4564  N   ALA B 935     -99.657   8.970  -0.108  1.00 50.69           N  
ANISOU 4564  N   ALA B 935     5321   7321   6615    126    -42    971       N  
ATOM   4565  CA  ALA B 935     -99.153   8.076  -1.127  1.00 55.04           C  
ANISOU 4565  CA  ALA B 935     5927   7877   7109     43    -97    983       C  
ATOM   4566  C   ALA B 935     -99.043   8.719  -2.503  1.00 60.44           C  
ANISOU 4566  C   ALA B 935     6612   8549   7803     59   -138   1040       C  
ATOM   4567  O   ALA B 935     -99.886   9.521  -2.910  1.00 66.22           O  
ANISOU 4567  O   ALA B 935     7272   9315   8574    112   -149   1100       O  
ATOM   4568  CB  ALA B 935    -100.051   6.852  -1.225  1.00 56.96           C  
ANISOU 4568  CB  ALA B 935     6129   8214   7301    -40   -132   1007       C  
ATOM   4569  N   SER B 936     -98.004   8.360  -3.243  1.00 69.17           N  
ANISOU 4569  N   SER B 936     7801   9608   8872     13   -160   1022       N  
ATOM   4570  CA  SER B 936     -97.957   8.767  -4.652  1.00 72.28           C  
ANISOU 4570  CA  SER B 936     8203  10006   9255      9   -203   1081       C  
ATOM   4571  C   SER B 936     -97.312   7.724  -5.539  1.00 74.25           C  
ANISOU 4571  C   SER B 936     8523  10257   9431    -82   -241   1069       C  
ATOM   4572  O   SER B 936     -97.892   7.375  -6.561  1.00 81.05           O  
ANISOU 4572  O   SER B 936     9366  11180  10250   -127   -294   1121       O  
ATOM   4573  CB  SER B 936     -97.273  10.117  -4.832  1.00 72.35           C  
ANISOU 4573  CB  SER B 936     8238   9932   9320     85   -176   1087       C  
ATOM   4574  OG  SER B 936     -97.544  10.634  -6.141  1.00 73.39           O  
ANISOU 4574  OG  SER B 936     8358  10082   9445     90   -220   1163       O  
ATOM   4575  N   SER B 939     -93.165   8.072 -10.494  1.00 88.69           N  
ANISOU 4575  N   SER B 939    10667  11926  11107   -205   -277   1084       N  
ATOM   4576  CA  SER B 939     -92.390   7.494 -11.598  1.00 85.64           C  
ANISOU 4576  CA  SER B 939    10354  11536  10651   -269   -284   1070       C  
ATOM   4577  C   SER B 939     -91.093   8.250 -11.899  1.00 80.19           C  
ANISOU 4577  C   SER B 939     9717  10767   9986   -245   -236   1052       C  
ATOM   4578  O   SER B 939     -90.114   7.642 -12.303  1.00 85.45           O  
ANISOU 4578  O   SER B 939    10445  11408  10615   -288   -216   1004       O  
ATOM   4579  CB  SER B 939     -93.255   7.387 -12.848  1.00 84.68           C  
ANISOU 4579  CB  SER B 939    10222  11489  10462   -311   -344   1144       C  
ATOM   4580  OG  SER B 939     -94.350   6.534 -12.582  1.00 87.28           O  
ANISOU 4580  OG  SER B 939    10505  11893  10765   -348   -388   1152       O  
ATOM   4581  N   LYS B 940     -91.086   9.565 -11.706  1.00 71.43           N  
ANISOU 4581  N   LYS B 940     8582   9617   8942   -177   -217   1089       N  
ATOM   4582  CA  LYS B 940     -89.883  10.355 -11.842  1.00 61.15           C  
ANISOU 4582  CA  LYS B 940     7323   8235   7674   -155   -169   1072       C  
ATOM   4583  C   LYS B 940     -89.954  11.478 -10.835  1.00 56.58           C  
ANISOU 4583  C   LYS B 940     6707   7602   7189    -76   -141   1072       C  
ATOM   4584  O   LYS B 940     -90.982  12.133 -10.718  1.00 57.08           O  
ANISOU 4584  O   LYS B 940     6717   7688   7283    -29   -163   1130       O  
ATOM   4585  CB  LYS B 940     -89.812  10.938 -13.260  1.00 59.41           C  
ANISOU 4585  CB  LYS B 940     7134   8026   7413   -173   -185   1143       C  
ATOM   4586  N   LEU B 941     -88.856  11.727 -10.133  1.00 49.39           N  
ANISOU 4586  N   LEU B 941     5824   6617   6325    -60    -93   1009       N  
ATOM   4587  CA  LEU B 941     -88.814  12.835  -9.207  1.00 45.16           C  
ANISOU 4587  CA  LEU B 941     5264   6020   5875     10    -63   1002       C  
ATOM   4588  C   LEU B 941     -88.882  14.177  -9.963  1.00 43.80           C  
ANISOU 4588  C   LEU B 941     5095   5811   5735     47    -61   1076       C  
ATOM   4589  O   LEU B 941     -88.436  14.268 -11.072  1.00 41.81           O  
ANISOU 4589  O   LEU B 941     4882   5560   5445     11    -65   1111       O  
ATOM   4590  CB  LEU B 941     -87.529  12.777  -8.369  1.00 44.84           C  
ANISOU 4590  CB  LEU B 941     5256   5909   5872      9    -19    916       C  
ATOM   4591  CG  LEU B 941     -87.454  11.665  -7.320  1.00 45.43           C  
ANISOU 4591  CG  LEU B 941     5325   6002   5933     -9    -19    843       C  
ATOM   4592  CD1 LEU B 941     -86.080  11.607  -6.694  1.00 45.82           C  
ANISOU 4592  CD1 LEU B 941     5409   5986   6014    -15     17    767       C  
ATOM   4593  CD2 LEU B 941     -88.502  11.905  -6.258  1.00 45.42           C  
ANISOU 4593  CD2 LEU B 941     5273   6021   5966     40    -24    846       C  
ATOM   4594  N   PRO B 942     -89.421  15.226  -9.341  1.00 42.27           N  
ANISOU 4594  N   PRO B 942     4866   5582   5613    119    -52   1099       N  
ATOM   4595  CA  PRO B 942     -89.268  16.560  -9.902  1.00 44.65           C  
ANISOU 4595  CA  PRO B 942     5182   5823   5958    157    -42   1160       C  
ATOM   4596  C   PRO B 942     -87.777  16.910 -10.080  1.00 45.40           C  
ANISOU 4596  C   PRO B 942     5338   5841   6069    128      1   1121       C  
ATOM   4597  O   PRO B 942     -86.972  16.513  -9.233  1.00 46.07           O  
ANISOU 4597  O   PRO B 942     5436   5895   6172    115     31   1036       O  
ATOM   4598  CB  PRO B 942     -89.921  17.466  -8.845  1.00 45.42           C  
ANISOU 4598  CB  PRO B 942     5236   5881   6139    242    -27   1157       C  
ATOM   4599  CG  PRO B 942     -90.870  16.585  -8.084  1.00 45.46           C  
ANISOU 4599  CG  PRO B 942     5186   5961   6125    247    -45   1131       C  
ATOM   4600  CD  PRO B 942     -90.264  15.208  -8.129  1.00 45.56           C  
ANISOU 4600  CD  PRO B 942     5228   6014   6069    168    -50   1074       C  
ATOM   4601  N   LYS B 943     -87.427  17.638 -11.150  1.00 42.14           N  
ANISOU 4601  N   LYS B 943     4961   5400   5651    116      4   1184       N  
ATOM   4602  CA  LYS B 943     -86.066  18.122 -11.365  1.00 42.26           C  
ANISOU 4602  CA  LYS B 943     5027   5341   5689     89     49   1157       C  
ATOM   4603  C   LYS B 943     -85.630  18.872 -10.130  1.00 39.99           C  
ANISOU 4603  C   LYS B 943     4734   4969   5492    135     84   1100       C  
ATOM   4604  O   LYS B 943     -86.375  19.690  -9.604  1.00 40.91           O  
ANISOU 4604  O   LYS B 943     4824   5054   5665    201     79   1124       O  
ATOM   4605  CB  LYS B 943     -85.963  19.101 -12.565  1.00 45.41           C  
ANISOU 4605  CB  LYS B 943     5460   5710   6083     84     47   1250       C  
ATOM   4606  CG  LYS B 943     -85.905  18.454 -13.934  1.00 48.51           C  
ANISOU 4606  CG  LYS B 943     5883   6171   6377     19     27   1296       C  
ATOM   4607  CD  LYS B 943     -84.504  17.948 -14.244  1.00 52.03           C  
ANISOU 4607  CD  LYS B 943     6374   6601   6794    -48     73   1236       C  
ATOM   4608  CE  LYS B 943     -84.308  17.286 -15.588  1.00 55.92           C  
ANISOU 4608  CE  LYS B 943     6906   7157   7184   -116     66   1267       C  
ATOM   4609  NZ  LYS B 943     -85.540  16.629 -16.067  1.00 55.71           N  
ANISOU 4609  NZ  LYS B 943     6859   7220   7087   -121      4   1313       N  
ATOM   4610  N   GLY B 944     -84.428  18.591  -9.661  1.00 38.16           N  
ANISOU 4610  N   GLY B 944     4524   4699   5274    101    119   1022       N  
ATOM   4611  CA  GLY B 944     -83.927  19.234  -8.471  1.00 36.47           C  
ANISOU 4611  CA  GLY B 944     4310   4409   5139    135    148    960       C  
ATOM   4612  C   GLY B 944     -84.199  18.489  -7.172  1.00 33.50           C  
ANISOU 4612  C   GLY B 944     3904   4058   4766    153    143    883       C  
ATOM   4613  O   GLY B 944     -83.681  18.904  -6.139  1.00 32.93           O  
ANISOU 4613  O   GLY B 944     3836   3927   4748    172    165    821       O  
ATOM   4614  N   LYS B 945     -85.018  17.437  -7.226  1.00 32.09           N  
ANISOU 4614  N   LYS B 945     3699   3965   4528    143    111    890       N  
ATOM   4615  CA  LYS B 945     -85.265  16.571  -6.076  1.00 31.57           C  
ANISOU 4615  CA  LYS B 945     3611   3933   4453    149    105    823       C  
ATOM   4616  C   LYS B 945     -84.556  15.245  -6.173  1.00 28.64           C  
ANISOU 4616  C   LYS B 945     3255   3599   4026     87    100    773       C  
ATOM   4617  O   LYS B 945     -84.464  14.695  -7.238  1.00 27.73           O  
ANISOU 4617  O   LYS B 945     3156   3524   3858     45     88    804       O  
ATOM   4618  CB  LYS B 945     -86.745  16.286  -5.939  1.00 32.13           C  
ANISOU 4618  CB  LYS B 945     3634   4071   4501    180     76    863       C  
ATOM   4619  CG  LYS B 945     -87.579  17.547  -5.804  1.00 33.56           C  
ANISOU 4619  CG  LYS B 945     3790   4220   4742    253     80    914       C  
ATOM   4620  CD  LYS B 945     -87.382  18.185  -4.447  1.00 32.85           C  
ANISOU 4620  CD  LYS B 945     3700   4066   4717    300    113    849       C  
ATOM   4621  CE  LYS B 945     -88.412  19.275  -4.224  1.00 34.22           C  
ANISOU 4621  CE  LYS B 945     3840   4216   4946    381    119    894       C  
ATOM   4622  NZ  LYS B 945     -88.202  19.900  -2.888  1.00 34.37           N  
ANISOU 4622  NZ  LYS B 945     3867   4170   5023    425    156    822       N  
ATOM   4623  N   HIS B 946     -83.996  14.763  -5.067  1.00 29.03           N  
ANISOU 4623  N   HIS B 946     3307   3632   4090     84    110    695       N  
ATOM   4624  CA  HIS B 946     -83.210  13.526  -5.103  1.00 29.94           C  
ANISOU 4624  CA  HIS B 946     3441   3771   4164     33    105    645       C  
ATOM   4625  C   HIS B 946     -83.757  12.392  -4.290  1.00 30.49           C  
ANISOU 4625  C   HIS B 946     3497   3891   4199     27     83    610       C  
ATOM   4626  O   HIS B 946     -83.237  11.275  -4.346  1.00 32.94           O  
ANISOU 4626  O   HIS B 946     3823   4221   4472    -12     74    574       O  
ATOM   4627  CB  HIS B 946     -81.814  13.846  -4.652  1.00 30.05           C  
ANISOU 4627  CB  HIS B 946     3474   3719   4224     24    133    585       C  
ATOM   4628  CG  HIS B 946     -81.298  15.055  -5.332  1.00 33.91           C  
ANISOU 4628  CG  HIS B 946     3978   4152   4756     27    158    619       C  
ATOM   4629  ND1 HIS B 946     -81.303  16.295  -4.739  1.00 36.88           N  
ANISOU 4629  ND1 HIS B 946     4353   4463   5198     66    174    618       N  
ATOM   4630  CD2 HIS B 946     -80.885  15.242  -6.598  1.00 34.79           C  
ANISOU 4630  CD2 HIS B 946     4108   4264   4848     -6    171    663       C  
ATOM   4631  CE1 HIS B 946     -80.846  17.189  -5.592  1.00 38.44           C  
ANISOU 4631  CE1 HIS B 946     4568   4617   5420     56    195    660       C  
ATOM   4632  NE2 HIS B 946     -80.585  16.574  -6.728  1.00 40.58           N  
ANISOU 4632  NE2 HIS B 946     4851   4931   5639     12    194    689       N  
ATOM   4633  N   SER B 947     -84.763  12.695  -3.500  1.00 29.23           N  
ANISOU 4633  N   SER B 947     3307   3746   4053     68     77    619       N  
ATOM   4634  CA  SER B 947     -85.354  11.705  -2.648  1.00 30.65           C  
ANISOU 4634  CA  SER B 947     3472   3973   4200     61     59    591       C  
ATOM   4635  C   SER B 947     -86.763  12.135  -2.253  1.00 30.45           C  
ANISOU 4635  C   SER B 947     3403   3985   4183    104     55    630       C  
ATOM   4636  O   SER B 947     -87.165  13.273  -2.473  1.00 33.48           O  
ANISOU 4636  O   SER B 947     3769   4344   4607    149     67    669       O  
ATOM   4637  CB  SER B 947     -84.495  11.534  -1.392  1.00 29.76           C  
ANISOU 4637  CB  SER B 947     3378   3819   4112     65     71    513       C  
ATOM   4638  OG  SER B 947     -84.440  12.738  -0.661  1.00 27.15           O  
ANISOU 4638  OG  SER B 947     3042   3435   3839    113     95    497       O  
ATOM   4639  N   VAL B 948     -87.504  11.203  -1.693  1.00 32.19           N  
ANISOU 4639  N   VAL B 948     3603   4262   4364     90     39    621       N  
ATOM   4640  CA  VAL B 948     -88.782  11.512  -1.089  1.00 32.48           C  
ANISOU 4640  CA  VAL B 948     3592   4339   4412    130     43    645       C  
ATOM   4641  C   VAL B 948     -88.638  11.378   0.416  1.00 31.38           C  
ANISOU 4641  C   VAL B 948     3457   4183   4282    147     63    581       C  
ATOM   4642  O   VAL B 948     -87.981  10.456   0.920  1.00 29.75           O  
ANISOU 4642  O   VAL B 948     3283   3974   4046    109     55    533       O  
ATOM   4643  CB  VAL B 948     -89.899  10.575  -1.597  1.00 35.03           C  
ANISOU 4643  CB  VAL B 948     3879   4751   4679     96     10    692       C  
ATOM   4644  CG1 VAL B 948     -91.144  10.682  -0.717  1.00 34.40           C  
ANISOU 4644  CG1 VAL B 948     3742   4719   4608    131     19    703       C  
ATOM   4645  CG2 VAL B 948     -90.263  10.906  -3.036  1.00 34.64           C  
ANISOU 4645  CG2 VAL B 948     3818   4725   4619     88    -14    765       C  
ATOM   4646  N   LYS B 949     -89.241  12.322   1.125  1.00 31.22           N  
ANISOU 4646  N   LYS B 949     3410   4149   4302    206     90    579       N  
ATOM   4647  CA  LYS B 949     -89.457  12.197   2.566  1.00 32.35           C  
ANISOU 4647  CA  LYS B 949     3552   4297   4444    224    112    527       C  
ATOM   4648  C   LYS B 949     -90.961  12.148   2.825  1.00 33.83           C  
ANISOU 4648  C   LYS B 949     3677   4557   4622    250    120    565       C  
ATOM   4649  O   LYS B 949     -91.670  13.095   2.520  1.00 30.52           O  
ANISOU 4649  O   LYS B 949     3217   4136   4243    304    134    604       O  
ATOM   4650  CB  LYS B 949     -88.888  13.367   3.309  1.00 32.40           C  
ANISOU 4650  CB  LYS B 949     3580   4225   4504    273    146    481       C  
ATOM   4651  CG  LYS B 949     -89.127  13.277   4.798  1.00 34.14           C  
ANISOU 4651  CG  LYS B 949     3804   4453   4713    291    170    424       C  
ATOM   4652  CD  LYS B 949     -88.534  14.462   5.522  1.00 36.91           C  
ANISOU 4652  CD  LYS B 949     4186   4723   5116    335    201    372       C  
ATOM   4653  CE  LYS B 949     -88.778  14.347   7.007  1.00 40.33           C  
ANISOU 4653  CE  LYS B 949     4629   5168   5527    348    226    313       C  
ATOM   4654  NZ  LYS B 949     -88.374  15.593   7.706  1.00 43.90           N  
ANISOU 4654  NZ  LYS B 949     5110   5543   6027    395    259    261       N  
ATOM   4655  N   GLY B 950     -91.426  11.017   3.342  1.00 34.29           N  
ANISOU 4655  N   GLY B 950     3725   4677   4628    210    110    556       N  
ATOM   4656  CA  GLY B 950     -92.783  10.904   3.819  1.00 36.93           C  
ANISOU 4656  CA  GLY B 950     3997   5082   4953    228    125    581       C  
ATOM   4657  C   GLY B 950     -92.843  11.532   5.192  1.00 38.43           C  
ANISOU 4657  C   GLY B 950     4192   5247   5164    277    173    527       C  
ATOM   4658  O   GLY B 950     -92.090  11.132   6.076  1.00 38.14           O  
ANISOU 4658  O   GLY B 950     4205   5183   5103    254    178    468       O  
ATOM   4659  N   LEU B 951     -93.712  12.526   5.365  1.00 38.33           N  
ANISOU 4659  N   LEU B 951     4128   5240   5195    346    207    545       N  
ATOM   4660  CA  LEU B 951     -93.715  13.345   6.585  1.00 40.43           C  
ANISOU 4660  CA  LEU B 951     4405   5468   5488    403    260    488       C  
ATOM   4661  C   LEU B 951     -94.529  12.726   7.701  1.00 42.59           C  
ANISOU 4661  C   LEU B 951     4652   5811   5719    394    290    466       C  
ATOM   4662  O   LEU B 951     -95.736  12.579   7.561  1.00 45.89           O  
ANISOU 4662  O   LEU B 951     4997   6303   6137    407    300    512       O  
ATOM   4663  CB  LEU B 951     -94.286  14.720   6.285  1.00 41.46           C  
ANISOU 4663  CB  LEU B 951     4496   5566   5690    488    289    514       C  
ATOM   4664  CG  LEU B 951     -93.475  15.527   5.269  1.00 43.40           C  
ANISOU 4664  CG  LEU B 951     4775   5732   5983    502    267    536       C  
ATOM   4665  CD1 LEU B 951     -94.126  16.880   5.013  1.00 42.00           C  
ANISOU 4665  CD1 LEU B 951     4560   5518   5879    591    295    568       C  
ATOM   4666  CD2 LEU B 951     -92.048  15.716   5.765  1.00 43.69           C  
ANISOU 4666  CD2 LEU B 951     4893   5685   6022    480    270    465       C  
ATOM   4667  N   GLY B 952     -93.871  12.327   8.786  1.00 41.62           N  
ANISOU 4667  N   GLY B 952     4586   5668   5558    367    301    401       N  
ATOM   4668  CA  GLY B 952     -94.584  11.759   9.950  1.00 42.36           C  
ANISOU 4668  CA  GLY B 952     4665   5826   5603    355    335    378       C  
ATOM   4669  C   GLY B 952     -95.146  12.804  10.896  1.00 40.30           C  
ANISOU 4669  C   GLY B 952     4386   5556   5372    430    402    340       C  
ATOM   4670  O   GLY B 952     -94.729  13.956  10.847  1.00 42.04           O  
ANISOU 4670  O   GLY B 952     4626   5700   5646    487    420    314       O  
ATOM   4671  N   LYS B 953     -96.079  12.392  11.757  1.00 39.14           N  
ANISOU 4671  N   LYS B 953     4204   5483   5187    427    443    334       N  
ATOM   4672  CA  LYS B 953     -96.576  13.245  12.869  1.00 41.55           C  
ANISOU 4672  CA  LYS B 953     4500   5784   5503    492    517    283       C  
ATOM   4673  C   LYS B 953     -95.527  13.415  13.976  1.00 40.36           C  
ANISOU 4673  C   LYS B 953     4446   5572   5319    482    529    198       C  
ATOM   4674  O   LYS B 953     -95.521  14.401  14.696  1.00 36.19           O  
ANISOU 4674  O   LYS B 953     3937   5001   4813    540    579    143       O  
ATOM   4675  CB  LYS B 953     -97.893  12.709  13.461  1.00 42.28           C  
ANISOU 4675  CB  LYS B 953     4523   5983   5560    486    563    304       C  
ATOM   4676  N   THR B 954     -94.636  12.438  14.097  1.00 39.51           N  
ANISOU 4676  N   THR B 954     4398   5458   5158    407    478    188       N  
ATOM   4677  CA  THR B 954     -93.559  12.475  15.082  1.00 40.93           C  
ANISOU 4677  CA  THR B 954     4666   5584   5301    388    472    114       C  
ATOM   4678  C   THR B 954     -92.222  12.428  14.320  1.00 41.29           C  
ANISOU 4678  C   THR B 954     4760   5556   5374    360    407    113       C  
ATOM   4679  O   THR B 954     -92.067  11.671  13.356  1.00 40.33           O  
ANISOU 4679  O   THR B 954     4621   5450   5251    319    360    164       O  
ATOM   4680  CB  THR B 954     -93.696  11.279  16.038  1.00 41.25           C  
ANISOU 4680  CB  THR B 954     4734   5688   5251    324    470    105       C  
ATOM   4681  OG1 THR B 954     -94.963  11.360  16.704  1.00 42.41           O  
ANISOU 4681  OG1 THR B 954     4831   5908   5375    349    539    108       O  
ATOM   4682  CG2 THR B 954     -92.567  11.211  17.053  1.00 42.58           C  
ANISOU 4682  CG2 THR B 954     4995   5807   5375    300    452     36       C  
ATOM   4683  N   THR B 955     -91.277  13.231  14.775  1.00 41.89           N  
ANISOU 4683  N   THR B 955     4893   5553   5471    380    409     51       N  
ATOM   4684  CA  THR B 955     -89.955  13.312  14.195  1.00 42.19           C  
ANISOU 4684  CA  THR B 955     4973   5519   5537    356    356     40       C  
ATOM   4685  C   THR B 955     -88.920  13.345  15.312  1.00 41.53           C  
ANISOU 4685  C   THR B 955     4965   5394   5420    334    342    -35       C  
ATOM   4686  O   THR B 955     -89.224  13.838  16.384  1.00 44.68           O  
ANISOU 4686  O   THR B 955     5387   5794   5796    359    384    -86       O  
ATOM   4687  CB  THR B 955     -89.833  14.576  13.309  1.00 42.24           C  
ANISOU 4687  CB  THR B 955     4961   5458   5631    410    368     52       C  
ATOM   4688  OG1 THR B 955     -88.594  14.537  12.605  1.00 43.86           O  
ANISOU 4688  OG1 THR B 955     5197   5605   5862    377    318     52       O  
ATOM   4689  CG2 THR B 955     -89.911  15.869  14.122  1.00 41.31           C  
ANISOU 4689  CG2 THR B 955     4867   5284   5544    470    419    -10       C  
ATOM   4690  N   PRO B 956     -87.695  12.835  15.076  1.00 43.50           N  
ANISOU 4690  N   PRO B 956     5253   5609   5667    288    283    -44       N  
ATOM   4691  CA  PRO B 956     -86.638  13.046  16.073  1.00 46.50           C  
ANISOU 4691  CA  PRO B 956     5699   5943   6026    272    263   -115       C  
ATOM   4692  C   PRO B 956     -86.363  14.518  16.289  1.00 44.35           C  
ANISOU 4692  C   PRO B 956     5446   5597   5809    318    294   -167       C  
ATOM   4693  O   PRO B 956     -86.354  15.288  15.340  1.00 47.20           O  
ANISOU 4693  O   PRO B 956     5779   5913   6240    347    304   -143       O  
ATOM   4694  CB  PRO B 956     -85.413  12.355  15.449  1.00 47.94           C  
ANISOU 4694  CB  PRO B 956     5896   6098   6219    224    196   -103       C  
ATOM   4695  CG  PRO B 956     -86.014  11.328  14.556  1.00 49.67           C  
ANISOU 4695  CG  PRO B 956     6075   6374   6425    202    183    -31       C  
ATOM   4696  CD  PRO B 956     -87.182  12.051  13.943  1.00 48.84           C  
ANISOU 4696  CD  PRO B 956     5914   6287   6356    249    232      6       C  
ATOM   4697  N   ASP B 957     -86.172  14.893  17.541  1.00 45.24           N  
ANISOU 4697  N   ASP B 957     5609   5696   5885    321    310   -237       N  
ATOM   4698  CA  ASP B 957     -85.958  16.272  17.923  1.00 44.36           C  
ANISOU 4698  CA  ASP B 957     5527   5511   5817    361    343   -298       C  
ATOM   4699  C   ASP B 957     -84.749  16.836  17.186  1.00 42.82           C  
ANISOU 4699  C   ASP B 957     5344   5233   5691    347    302   -305       C  
ATOM   4700  O   ASP B 957     -83.625  16.456  17.465  1.00 37.73           O  
ANISOU 4700  O   ASP B 957     4734   4571   5032    300    249   -332       O  
ATOM   4701  CB  ASP B 957     -85.739  16.340  19.436  1.00 45.53           C  
ANISOU 4701  CB  ASP B 957     5740   5664   5896    348    351   -376       C  
ATOM   4702  CG  ASP B 957     -85.673  17.757  19.969  1.00 47.78           C  
ANISOU 4702  CG  ASP B 957     6062   5876   6215    390    394   -449       C  
ATOM   4703  OD1 ASP B 957     -85.487  18.716  19.173  1.00 50.58           O  
ANISOU 4703  OD1 ASP B 957     6403   6160   6657    422    404   -443       O  
ATOM   4704  OD2 ASP B 957     -85.768  17.895  21.210  1.00 46.13           O  
ANISOU 4704  OD2 ASP B 957     5905   5679   5944    388    416   -515       O  
ATOM   4705  N   PRO B 958     -84.980  17.793  16.272  1.00 47.38           N  
ANISOU 4705  N   PRO B 958     5894   5761   6348    389    329   -280       N  
ATOM   4706  CA  PRO B 958     -83.883  18.416  15.509  1.00 46.52           C  
ANISOU 4706  CA  PRO B 958     5795   5572   6309    373    299   -281       C  
ATOM   4707  C   PRO B 958     -82.766  19.027  16.343  1.00 43.31           C  
ANISOU 4707  C   PRO B 958     5450   5099   5909    347    277   -363       C  
ATOM   4708  O   PRO B 958     -81.633  19.079  15.882  1.00 42.71           O  
ANISOU 4708  O   PRO B 958     5379   4980   5869    309    235   -366       O  
ATOM   4709  CB  PRO B 958     -84.584  19.526  14.718  1.00 48.36           C  
ANISOU 4709  CB  PRO B 958     6000   5759   6616    433    345   -249       C  
ATOM   4710  CG  PRO B 958     -86.019  19.154  14.694  1.00 46.93           C  
ANISOU 4710  CG  PRO B 958     5772   5653   6408    474    384   -205       C  
ATOM   4711  CD  PRO B 958     -86.288  18.405  15.957  1.00 46.70           C  
ANISOU 4711  CD  PRO B 958     5765   5687   6292    455    391   -248       C  
ATOM   4712  N   SER B 959     -83.070  19.486  17.553  1.00 41.12           N  
ANISOU 4712  N   SER B 959     5215   4814   5595    365    307   -432       N  
ATOM   4713  CA  SER B 959     -82.063  20.115  18.400  1.00 41.92           C  
ANISOU 4713  CA  SER B 959     5379   4852   5696    338    284   -515       C  
ATOM   4714  C   SER B 959     -81.050  19.099  18.931  1.00 41.65           C  
ANISOU 4714  C   SER B 959     5366   4854   5605    272    213   -533       C  
ATOM   4715  O   SER B 959     -79.949  19.470  19.346  1.00 45.39           O  
ANISOU 4715  O   SER B 959     5876   5278   6090    235    173   -587       O  
ATOM   4716  CB  SER B 959     -82.745  20.845  19.582  1.00 42.70           C  
ANISOU 4716  CB  SER B 959     5525   4939   5760    376    340   -588       C  
ATOM   4717  N   ALA B 960     -81.419  17.822  18.922  1.00 40.05           N  
ANISOU 4717  N   ALA B 960     5139   4735   5344    256    195   -487       N  
ATOM   4718  CA  ALA B 960     -80.502  16.753  19.318  1.00 40.73           C  
ANISOU 4718  CA  ALA B 960     5240   4854   5382    199    124   -490       C  
ATOM   4719  C   ALA B 960     -79.759  16.070  18.129  1.00 37.90           C  
ANISOU 4719  C   ALA B 960     4837   4495   5069    172     78   -432       C  
ATOM   4720  O   ALA B 960     -78.957  15.166  18.338  1.00 38.17           O  
ANISOU 4720  O   ALA B 960     4876   4551   5075    132     19   -430       O  
ATOM   4721  CB  ALA B 960     -81.240  15.709  20.135  1.00 38.21           C  
ANISOU 4721  CB  ALA B 960     4934   4619   4967    192    128   -479       C  
ATOM   4722  N   ASN B 961     -79.999  16.512  16.902  1.00 37.93           N  
ANISOU 4722  N   ASN B 961     4798   4473   5141    195    105   -385       N  
ATOM   4723  CA  ASN B 961     -79.250  15.998  15.756  1.00 39.06           C  
ANISOU 4723  CA  ASN B 961     4905   4611   5327    168     70   -338       C  
ATOM   4724  C   ASN B 961     -77.768  16.278  15.920  1.00 37.52           C  
ANISOU 4724  C   ASN B 961     4725   4365   5167    129     22   -382       C  
ATOM   4725  O   ASN B 961     -77.401  17.311  16.461  1.00 36.43           O  
ANISOU 4725  O   ASN B 961     4618   4170   5054    129     28   -438       O  
ATOM   4726  CB  ASN B 961     -79.751  16.629  14.458  1.00 40.39           C  
ANISOU 4726  CB  ASN B 961     5034   4754   5559    199    110   -284       C  
ATOM   4727  CG  ASN B 961     -79.033  16.070  13.250  1.00 42.90           C  
ANISOU 4727  CG  ASN B 961     5317   5073   5909    170     81   -236       C  
ATOM   4728  OD1 ASN B 961     -79.262  14.928  12.845  1.00 43.38           O  
ANISOU 4728  OD1 ASN B 961     5357   5191   5936    157     64   -193       O  
ATOM   4729  ND2 ASN B 961     -78.089  16.826  12.737  1.00 42.29           N  
ANISOU 4729  ND2 ASN B 961     5239   4932   5898    154     75   -248       N  
ATOM   4730  N   ILE B 962     -76.925  15.326  15.521  1.00 37.31           N  
ANISOU 4730  N   ILE B 962     4677   4359   5141     95    -28   -360       N  
ATOM   4731  CA  ILE B 962     -75.487  15.569  15.526  1.00 36.61           C  
ANISOU 4731  CA  ILE B 962     4585   4227   5097     58    -73   -395       C  
ATOM   4732  C   ILE B 962     -74.946  15.310  14.143  1.00 35.67           C  
ANISOU 4732  C   ILE B 962     4418   4100   5035     47    -74   -346       C  
ATOM   4733  O   ILE B 962     -75.522  14.538  13.389  1.00 34.21           O  
ANISOU 4733  O   ILE B 962     4209   3956   4833     58    -61   -290       O  
ATOM   4734  CB  ILE B 962     -74.726  14.722  16.546  1.00 39.19           C  
ANISOU 4734  CB  ILE B 962     4933   4583   5376     27   -139   -429       C  
ATOM   4735  CG1 ILE B 962     -74.792  13.229  16.215  1.00 38.05           C  
ANISOU 4735  CG1 ILE B 962     4767   4497   5194     22   -167   -379       C  
ATOM   4736  CG2 ILE B 962     -75.234  15.025  17.955  1.00 40.22           C  
ANISOU 4736  CG2 ILE B 962     5120   4723   5439     33   -137   -482       C  
ATOM   4737  CD1 ILE B 962     -73.820  12.403  17.024  1.00 40.93           C  
ANISOU 4737  CD1 ILE B 962     5144   4878   5528     -7   -241   -404       C  
ATOM   4738  N   SER B 963     -73.855  15.984  13.820  1.00 36.22           N  
ANISOU 4738  N   SER B 963     4476   4116   5170     21    -87   -369       N  
ATOM   4739  CA  SER B 963     -73.194  15.824  12.546  1.00 37.49           C  
ANISOU 4739  CA  SER B 963     4591   4267   5385      5    -84   -329       C  
ATOM   4740  C   SER B 963     -71.850  15.140  12.752  1.00 37.81           C  
ANISOU 4740  C   SER B 963     4609   4316   5440    -32   -142   -353       C  
ATOM   4741  O   SER B 963     -71.001  15.603  13.506  1.00 38.93           O  
ANISOU 4741  O   SER B 963     4760   4430   5602    -57   -176   -406       O  
ATOM   4742  CB  SER B 963     -73.056  17.167  11.832  1.00 35.10           C  
ANISOU 4742  CB  SER B 963     4285   3898   5155      4    -43   -324       C  
ATOM   4743  OG  SER B 963     -72.176  17.059  10.735  1.00 36.94           O  
ANISOU 4743  OG  SER B 963     4476   4120   5438    -23    -42   -296       O  
ATOM   4744  N   LEU B 964     -71.697  14.009  12.076  1.00 38.98           N  
ANISOU 4744  N   LEU B 964     4727   4505   5577    -32   -153   -313       N  
ATOM   4745  CA  LEU B 964     -70.513  13.163  12.190  1.00 39.58           C  
ANISOU 4745  CA  LEU B 964     4776   4597   5667    -55   -206   -327       C  
ATOM   4746  C   LEU B 964     -69.912  12.962  10.808  1.00 36.19           C  
ANISOU 4746  C   LEU B 964     4297   4162   5290    -66   -183   -293       C  
ATOM   4747  O   LEU B 964     -70.511  12.303   9.956  1.00 34.53           O  
ANISOU 4747  O   LEU B 964     4081   3981   5059    -51   -156   -246       O  
ATOM   4748  CB  LEU B 964     -70.874  11.802  12.760  1.00 37.79           C  
ANISOU 4748  CB  LEU B 964     4565   4422   5372    -43   -243   -315       C  
ATOM   4749  CG  LEU B 964     -71.073  11.669  14.272  1.00 40.55           C  
ANISOU 4749  CG  LEU B 964     4960   4786   5661    -44   -285   -353       C  
ATOM   4750  CD1 LEU B 964     -71.108  10.168  14.578  1.00 39.08           C  
ANISOU 4750  CD1 LEU B 964     4780   4645   5423    -40   -327   -330       C  
ATOM   4751  CD2 LEU B 964     -69.971  12.340  15.079  1.00 40.37           C  
ANISOU 4751  CD2 LEU B 964     4938   4732   5670    -71   -330   -412       C  
ATOM   4752  N   ASP B 965     -68.726  13.507  10.601  1.00 35.75           N  
ANISOU 4752  N   ASP B 965     4209   4075   5302    -94   -192   -318       N  
ATOM   4753  CA  ASP B 965     -68.025  13.344   9.330  1.00 37.18           C  
ANISOU 4753  CA  ASP B 965     4341   4253   5533   -108   -165   -290       C  
ATOM   4754  C   ASP B 965     -68.897  13.827   8.153  1.00 35.86           C  
ANISOU 4754  C   ASP B 965     4182   4078   5366    -97    -99   -238       C  
ATOM   4755  O   ASP B 965     -68.976  13.172   7.101  1.00 34.44           O  
ANISOU 4755  O   ASP B 965     3983   3924   5180    -93    -74   -199       O  
ATOM   4756  CB  ASP B 965     -67.602  11.841   9.122  1.00 38.03           C  
ANISOU 4756  CB  ASP B 965     4422   4405   5622    -99   -195   -278       C  
ATOM   4757  CG  ASP B 965     -66.538  11.661   7.996  1.00 43.90           C  
ANISOU 4757  CG  ASP B 965     5108   5147   6427   -116   -172   -269       C  
ATOM   4758  OD1 ASP B 965     -66.196  10.501   7.694  1.00 50.18           O  
ANISOU 4758  OD1 ASP B 965     5881   5970   7213   -104   -186   -260       O  
ATOM   4759  OD2 ASP B 965     -66.023  12.650   7.410  1.00 44.75           O  
ANISOU 4759  OD2 ASP B 965     5190   5221   6590   -142   -138   -270       O  
ATOM   4760  N   GLY B 966     -69.611  14.919   8.369  1.00 33.36           N  
ANISOU 4760  N   GLY B 966     3898   3728   5052    -89    -73   -238       N  
ATOM   4761  CA  GLY B 966     -70.469  15.482   7.346  1.00 33.75           C  
ANISOU 4761  CA  GLY B 966     3955   3765   5103    -75    -18   -186       C  
ATOM   4762  C   GLY B 966     -71.833  14.788   7.219  1.00 32.09           C  
ANISOU 4762  C   GLY B 966     3764   3602   4826    -39     -7   -146       C  
ATOM   4763  O   GLY B 966     -72.577  15.126   6.336  1.00 32.71           O  
ANISOU 4763  O   GLY B 966     3846   3681   4903    -25     31    -98       O  
ATOM   4764  N   VAL B 967     -72.168  13.831   8.092  1.00 31.36           N  
ANISOU 4764  N   VAL B 967     3686   3550   4679    -26    -43   -163       N  
ATOM   4765  CA  VAL B 967     -73.456  13.122   8.048  1.00 29.58           C  
ANISOU 4765  CA  VAL B 967     3476   3373   4390      0    -34   -126       C  
ATOM   4766  C   VAL B 967     -74.298  13.402   9.283  1.00 29.99           C  
ANISOU 4766  C   VAL B 967     3561   3430   4402     22    -40   -152       C  
ATOM   4767  O   VAL B 967     -73.827  13.302  10.398  1.00 30.58           O  
ANISOU 4767  O   VAL B 967     3653   3500   4465     13    -76   -200       O  
ATOM   4768  CB  VAL B 967     -73.234  11.595   7.945  1.00 27.77           C  
ANISOU 4768  CB  VAL B 967     3238   3191   4123     -8    -66   -117       C  
ATOM   4769  CG1 VAL B 967     -74.549  10.832   7.791  1.00 28.21           C  
ANISOU 4769  CG1 VAL B 967     3308   3296   4115      8    -57    -76       C  
ATOM   4770  CG2 VAL B 967     -72.280  11.276   6.795  1.00 27.51           C  
ANISOU 4770  CG2 VAL B 967     3171   3152   4128    -28    -56   -104       C  
ATOM   4771  N   ASP B 968     -75.562  13.742   9.081  1.00 29.94           N  
ANISOU 4771  N   ASP B 968     3564   3438   4375     50     -5   -118       N  
ATOM   4772  CA  ASP B 968     -76.480  13.891  10.202  1.00 30.27           C  
ANISOU 4772  CA  ASP B 968     3633   3495   4374     74     -1   -139       C  
ATOM   4773  C   ASP B 968     -76.942  12.553  10.778  1.00 29.59           C  
ANISOU 4773  C   ASP B 968     3555   3471   4217     70    -28   -132       C  
ATOM   4774  O   ASP B 968     -77.263  11.616  10.049  1.00 27.60           O  
ANISOU 4774  O   ASP B 968     3287   3258   3942     64    -31    -89       O  
ATOM   4775  CB  ASP B 968     -77.668  14.703   9.771  1.00 30.72           C  
ANISOU 4775  CB  ASP B 968     3686   3547   4440    111     47   -104       C  
ATOM   4776  CG  ASP B 968     -77.311  16.142   9.453  1.00 35.13           C  
ANISOU 4776  CG  ASP B 968     4250   4033   5067    119     74   -115       C  
ATOM   4777  OD1 ASP B 968     -76.348  16.707  10.030  1.00 37.95           O  
ANISOU 4777  OD1 ASP B 968     4623   4341   5455     99     59   -169       O  
ATOM   4778  OD2 ASP B 968     -78.011  16.748   8.628  1.00 42.40           O  
ANISOU 4778  OD2 ASP B 968     5158   4941   6010    144    109    -68       O  
ATOM   4779  N   VAL B 969     -76.934  12.466  12.101  1.00 30.24           N  
ANISOU 4779  N   VAL B 969     3668   3560   4262     70    -49   -177       N  
ATOM   4780  CA  VAL B 969     -77.512  11.347  12.816  1.00 30.66           C  
ANISOU 4780  CA  VAL B 969     3739   3669   4242     66    -69   -169       C  
ATOM   4781  C   VAL B 969     -78.664  11.922  13.643  1.00 32.23           C  
ANISOU 4781  C   VAL B 969     3958   3885   4405     93    -31   -182       C  
ATOM   4782  O   VAL B 969     -78.420  12.636  14.625  1.00 31.40           O  
ANISOU 4782  O   VAL B 969     3882   3752   4295     97    -32   -236       O  
ATOM   4783  CB  VAL B 969     -76.499  10.698  13.752  1.00 30.05           C  
ANISOU 4783  CB  VAL B 969     3684   3591   4143     41   -127   -209       C  
ATOM   4784  CG1 VAL B 969     -77.096   9.443  14.353  1.00 31.00           C  
ANISOU 4784  CG1 VAL B 969     3825   3765   4187     33   -148   -189       C  
ATOM   4785  CG2 VAL B 969     -75.209  10.388  13.008  1.00 30.63           C  
ANISOU 4785  CG2 VAL B 969     3730   3639   4268     21   -159   -208       C  
ATOM   4786  N   PRO B 970     -79.917  11.667  13.228  1.00 31.32           N  
ANISOU 4786  N   PRO B 970     3823   3812   4264    111      3   -134       N  
ATOM   4787  CA  PRO B 970     -81.059  12.249  13.891  1.00 30.76           C  
ANISOU 4787  CA  PRO B 970     3760   3760   4168    142     48   -143       C  
ATOM   4788  C   PRO B 970     -81.449  11.423  15.090  1.00 34.33           C  
ANISOU 4788  C   PRO B 970     4241   4261   4540    128     35   -159       C  
ATOM   4789  O   PRO B 970     -82.526  10.804  15.113  1.00 34.92           O  
ANISOU 4789  O   PRO B 970     4303   4395   4572    130     56   -122       O  
ATOM   4790  CB  PRO B 970     -82.148  12.199  12.821  1.00 31.08           C  
ANISOU 4790  CB  PRO B 970     3756   3832   4220    162     82    -77       C  
ATOM   4791  CG  PRO B 970     -81.826  10.971  12.048  1.00 31.30           C  
ANISOU 4791  CG  PRO B 970     3772   3889   4233    126     45    -37       C  
ATOM   4792  CD  PRO B 970     -80.311  10.842  12.075  1.00 31.70           C  
ANISOU 4792  CD  PRO B 970     3840   3894   4310    101      3    -72       C  
ATOM   4793  N   LEU B 971     -80.610  11.451  16.110  1.00 36.14           N  
ANISOU 4793  N   LEU B 971     4512   4470   4748    110      2   -213       N  
ATOM   4794  CA  LEU B 971     -80.811  10.591  17.264  1.00 41.35           C  
ANISOU 4794  CA  LEU B 971     5209   5175   5326     90    -19   -226       C  
ATOM   4795  C   LEU B 971     -81.630  11.233  18.412  1.00 39.78           C  
ANISOU 4795  C   LEU B 971     5040   4994   5079    110     26   -265       C  
ATOM   4796  O   LEU B 971     -81.696  10.690  19.503  1.00 41.25           O  
ANISOU 4796  O   LEU B 971     5268   5214   5192     91     11   -284       O  
ATOM   4797  CB  LEU B 971     -79.466  10.023  17.772  1.00 41.63           C  
ANISOU 4797  CB  LEU B 971     5274   5191   5351     56    -91   -254       C  
ATOM   4798  CG  LEU B 971     -78.301  10.976  17.958  1.00 42.34           C  
ANISOU 4798  CG  LEU B 971     5375   5220   5493     53   -115   -310       C  
ATOM   4799  CD1 LEU B 971     -78.651  12.025  18.987  1.00 42.28           C  
ANISOU 4799  CD1 LEU B 971     5405   5197   5461     68    -84   -368       C  
ATOM   4800  CD2 LEU B 971     -77.081  10.168  18.371  1.00 45.73           C  
ANISOU 4800  CD2 LEU B 971     5819   5645   5910     21   -193   -323       C  
ATOM   4801  N   GLY B 972     -82.283  12.349  18.152  1.00 40.16           N  
ANISOU 4801  N   GLY B 972     5070   5022   5168    151     84   -275       N  
ATOM   4802  CA  GLY B 972     -83.184  12.940  19.141  1.00 42.89           C  
ANISOU 4802  CA  GLY B 972     5438   5387   5472    179    140   -311       C  
ATOM   4803  C   GLY B 972     -84.391  12.076  19.456  1.00 44.10           C  
ANISOU 4803  C   GLY B 972     5577   5623   5558    176    170   -271       C  
ATOM   4804  O   GLY B 972     -84.828  11.300  18.605  1.00 44.04           O  
ANISOU 4804  O   GLY B 972     5526   5650   5557    165    163   -207       O  
ATOM   4805  N   THR B 973     -84.926  12.196  20.672  1.00 44.27           N  
ANISOU 4805  N   THR B 973     5633   5676   5512    180    204   -311       N  
ATOM   4806  CA  THR B 973     -86.199  11.534  21.009  1.00 46.57           C  
ANISOU 4806  CA  THR B 973     5904   6048   5743    179    249   -275       C  
ATOM   4807  C   THR B 973     -87.333  12.096  20.160  1.00 48.88           C  
ANISOU 4807  C   THR B 973     6125   6355   6091    228    311   -237       C  
ATOM   4808  O   THR B 973     -87.300  13.252  19.774  1.00 49.48           O  
ANISOU 4808  O   THR B 973     6189   6378   6235    275    338   -260       O  
ATOM   4809  CB  THR B 973     -86.579  11.634  22.514  1.00 47.39           C  
ANISOU 4809  CB  THR B 973     6061   6186   5759    175    285   -328       C  
ATOM   4810  OG1 THR B 973     -86.564  12.992  22.916  1.00 50.10           O  
ANISOU 4810  OG1 THR B 973     6424   6481   6131    220    329   -396       O  
ATOM   4811  CG2 THR B 973     -85.598  10.859  23.396  1.00 49.54           C  
ANISOU 4811  CG2 THR B 973     6403   6460   5961    121    216   -349       C  
ATOM   4812  N   GLY B 974     -88.336  11.269  19.892  1.00 50.47           N  
ANISOU 4812  N   GLY B 974     6283   6630   6265    216    330   -178       N  
ATOM   4813  CA  GLY B 974     -89.478  11.666  19.078  1.00 52.56           C  
ANISOU 4813  CA  GLY B 974     6471   6922   6577    258    380   -133       C  
ATOM   4814  C   GLY B 974     -90.354  12.745  19.688  1.00 52.51           C  
ANISOU 4814  C   GLY B 974     6450   6921   6581    320    461   -172       C  
ATOM   4815  O   GLY B 974     -90.825  12.618  20.813  1.00 53.94           O  
ANISOU 4815  O   GLY B 974     6656   7145   6694    316    503   -205       O  
ATOM   4816  N   ILE B 975     -90.550  13.818  18.926  1.00 52.21           N  
ANISOU 4816  N   ILE B 975     6374   6836   6627    379    486   -167       N  
ATOM   4817  CA  ILE B 975     -91.438  14.911  19.297  1.00 50.79           C  
ANISOU 4817  CA  ILE B 975     6171   6652   6476    451    566   -198       C  
ATOM   4818  C   ILE B 975     -92.398  15.174  18.148  1.00 51.10           C  
ANISOU 4818  C   ILE B 975     6119   6713   6584    496    586   -127       C  
ATOM   4819  O   ILE B 975     -92.229  14.642  17.046  1.00 49.18           O  
ANISOU 4819  O   ILE B 975     5843   6477   6365    468    536    -63       O  
ATOM   4820  CB  ILE B 975     -90.667  16.221  19.603  1.00 47.92           C  
ANISOU 4820  CB  ILE B 975     5862   6188   6158    490    576   -272       C  
ATOM   4821  CG1 ILE B 975     -90.026  16.787  18.333  1.00 46.23           C  
ANISOU 4821  CG1 ILE B 975     5632   5899   6036    504    536   -240       C  
ATOM   4822  CG2 ILE B 975     -89.633  15.995  20.692  1.00 45.09           C  
ANISOU 4822  CG2 ILE B 975     5592   5806   5733    441    543   -341       C  
ATOM   4823  CD1 ILE B 975     -89.442  18.172  18.506  1.00 46.96           C  
ANISOU 4823  CD1 ILE B 975     5768   5888   6186    545    554   -303       C  
ATOM   4824  N   SER B 976     -93.368  16.043  18.401  1.00 51.77           N  
ANISOU 4824  N   SER B 976     6165   6806   6700    567    660   -141       N  
ATOM   4825  CA  SER B 976     -94.347  16.402  17.406  1.00 53.37           C  
ANISOU 4825  CA  SER B 976     6277   7030   6970    620    680    -75       C  
ATOM   4826  C   SER B 976     -93.687  17.201  16.298  1.00 49.75           C  
ANISOU 4826  C   SER B 976     5823   6482   6598    646    643    -54       C  
ATOM   4827  O   SER B 976     -92.915  18.104  16.566  1.00 48.83           O  
ANISOU 4827  O   SER B 976     5765   6275   6512    669    646   -112       O  
ATOM   4828  CB  SER B 976     -95.460  17.238  18.036  1.00 54.60           C  
ANISOU 4828  CB  SER B 976     6392   7205   7146    700    772   -104       C  
ATOM   4829  OG  SER B 976     -96.469  17.474  17.071  1.00 56.13           O  
ANISOU 4829  OG  SER B 976     6488   7433   7405    750    785    -31       O  
ATOM   4830  N   SER B 977     -93.987  16.847  15.056  1.00 49.47           N  
ANISOU 4830  N   SER B 977     5727   6473   6595    638    605     28       N  
ATOM   4831  CA  SER B 977     -93.423  17.542  13.900  1.00 49.69           C  
ANISOU 4831  CA  SER B 977     5758   6425   6698    658    570     61       C  
ATOM   4832  C   SER B 977     -94.255  18.757  13.552  1.00 53.41           C  
ANISOU 4832  C   SER B 977     6180   6865   7249    752    617     79       C  
ATOM   4833  O   SER B 977     -93.822  19.601  12.780  1.00 58.80           O  
ANISOU 4833  O   SER B 977     6875   7469   7999    782    601     96       O  
ATOM   4834  CB  SER B 977     -93.392  16.618  12.683  1.00 46.94           C  
ANISOU 4834  CB  SER B 977     5371   6120   6342    605    509    142       C  
ATOM   4835  OG  SER B 977     -94.696  16.151  12.367  1.00 44.25           O  
ANISOU 4835  OG  SER B 977     4946   5874   5994    617    523    203       O  
ATOM   4836  N   GLY B 978     -95.473  18.815  14.075  1.00 56.46           N  
ANISOU 4836  N   GLY B 978     6508   7316   7629    799    675     81       N  
ATOM   4837  CA  GLY B 978     -96.401  19.880  13.724  1.00 59.15           C  
ANISOU 4837  CA  GLY B 978     6788   7637   8050    897    721    107       C  
ATOM   4838  C   GLY B 978     -97.138  19.625  12.423  1.00 59.88           C  
ANISOU 4838  C   GLY B 978     6791   7783   8179    906    684    212       C  
ATOM   4839  O   GLY B 978     -97.881  20.477  11.967  1.00 61.72           O  
ANISOU 4839  O   GLY B 978     6968   8000   8484    988    708    248       O  
ATOM   4840  N   VAL B 979     -96.938  18.468  11.806  1.00 59.30           N  
ANISOU 4840  N   VAL B 979     6706   7769   8057    824    624    262       N  
ATOM   4841  CA  VAL B 979     -97.617  18.179  10.544  1.00 62.91           C  
ANISOU 4841  CA  VAL B 979     7084   8279   8539    823    583    360       C  
ATOM   4842  C   VAL B 979     -98.996  17.569  10.774  1.00 67.35           C  
ANISOU 4842  C   VAL B 979     7549   8962   9080    828    610    397       C  
ATOM   4843  O   VAL B 979     -99.116  16.486  11.361  1.00 68.77           O  
ANISOU 4843  O   VAL B 979     7730   9213   9185    761    611    383       O  
ATOM   4844  CB  VAL B 979     -96.713  17.316   9.629  1.00 60.83           C  
ANISOU 4844  CB  VAL B 979     6859   8014   8240    734    505    395       C  
ATOM   4845  CG1 VAL B 979     -97.502  16.754   8.460  1.00 58.13           C  
ANISOU 4845  CG1 VAL B 979     6439   7749   7898    714    461    490       C  
ATOM   4846  CG2 VAL B 979     -95.534  18.151   9.133  1.00 61.33           C  
ANISOU 4846  CG2 VAL B 979     6993   7962   8348    743    483    377       C  
ATOM   4847  N   ASN B 980    -100.040  18.259  10.297  1.00 69.77           N  
ANISOU 4847  N   ASN B 980     7768   9290   9452    907    630    448       N  
ATOM   4848  CA  ASN B 980    -101.395  17.845  10.574  1.00 73.64           C  
ANISOU 4848  CA  ASN B 980     8153   9893   9934    924    665    480       C  
ATOM   4849  C   ASN B 980    -101.899  16.737   9.661  1.00 72.66           C  
ANISOU 4849  C   ASN B 980     7965   9867   9777    851    601    564       C  
ATOM   4850  O   ASN B 980    -102.223  15.623  10.124  1.00 76.53           O  
ANISOU 4850  O   ASN B 980     8438  10442  10199    779    603    561       O  
ATOM   4851  CB  ASN B 980    -102.328  19.070  10.466  1.00 74.90           C  
ANISOU 4851  CB  ASN B 980     8236  10035  10185   1047    713    501       C  
ATOM   4852  N   ASP B 981    -101.941  17.024   8.372  1.00 66.98           N  
ANISOU 4852  N   ASP B 981     7218   9133   9100    863    543    637       N  
ATOM   4853  CA  ASP B 981    -102.741  16.223   7.470  1.00 69.96           C  
ANISOU 4853  CA  ASP B 981     7512   9611   9461    817    490    722       C  
ATOM   4854  C   ASP B 981    -101.810  15.224   6.842  1.00 69.88           C  
ANISOU 4854  C   ASP B 981     7572   9593   9386    710    420    731       C  
ATOM   4855  O   ASP B 981    -101.389  15.434   5.720  1.00 74.36           O  
ANISOU 4855  O   ASP B 981     8159  10124   9971    703    364    777       O  
ATOM   4856  CB  ASP B 981    -103.446  17.085   6.401  1.00 70.65           C  
ANISOU 4856  CB  ASP B 981     7519   9697   9625    894    463    803       C  
ATOM   4857  N   THR B 982    -101.451  14.157   7.559  1.00 67.14           N  
ANISOU 4857  N   THR B 982     7270   9276   8965    629    424    688       N  
ATOM   4858  CA  THR B 982    -100.553  13.145   6.986  1.00 64.60           C  
ANISOU 4858  CA  THR B 982     7017   8944   8584    531    360    693       C  
ATOM   4859  C   THR B 982    -101.054  11.728   7.218  1.00 59.13           C  
ANISOU 4859  C   THR B 982     6300   8346   7822    439    343    707       C  
ATOM   4860  O   THR B 982    -101.655  11.436   8.230  1.00 53.51           O  
ANISOU 4860  O   THR B 982     5558   7687   7087    436    393    683       O  
ATOM   4861  CB  THR B 982     -99.094  13.262   7.514  1.00 61.65           C  
ANISOU 4861  CB  THR B 982     6761   8470   8192    515    365    618       C  
ATOM   4862  OG1 THR B 982     -98.317  12.160   7.028  1.00 59.14           O  
ANISOU 4862  OG1 THR B 982     6499   8153   7818    422    308    622       O  
ATOM   4863  CG2 THR B 982     -99.054  13.227   9.040  1.00 61.63           C  
ANISOU 4863  CG2 THR B 982     6788   8468   8162    524    427    542       C  
ATOM   4864  N   SER B 983    -100.732  10.849   6.280  1.00 59.59           N  
ANISOU 4864  N   SER B 983     6380   8420   7843    361    276    744       N  
ATOM   4865  CA  SER B 983    -101.012   9.422   6.404  1.00 59.35           C  
ANISOU 4865  CA  SER B 983     6348   8461   7743    262    251    754       C  
ATOM   4866  C   SER B 983    -100.031   8.682   7.339  1.00 56.67           C  
ANISOU 4866  C   SER B 983     6107   8080   7348    209    261    687       C  
ATOM   4867  O   SER B 983    -100.225   7.508   7.588  1.00 51.76           O  
ANISOU 4867  O   SER B 983     5492   7505   6668    130    245    692       O  
ATOM   4868  CB  SER B 983    -100.942   8.767   5.012  1.00 58.29           C  
ANISOU 4868  CB  SER B 983     6214   8347   7588    198    173    811       C  
ATOM   4869  OG  SER B 983    -101.736   9.481   4.067  1.00 67.59           O  
ANISOU 4869  OG  SER B 983     7309   9558   8815    246    152    878       O  
ATOM   4870  N   LEU B 984     -98.978   9.343   7.831  1.00 51.72           N  
ANISOU 4870  N   LEU B 984     5554   7362   6736    249    281    628       N  
ATOM   4871  CA  LEU B 984     -97.866   8.629   8.464  1.00 48.90           C  
ANISOU 4871  CA  LEU B 984     5294   6958   6329    197    270    573       C  
ATOM   4872  C   LEU B 984     -97.654   9.045   9.907  1.00 46.55           C  
ANISOU 4872  C   LEU B 984     5030   6636   6022    231    329    506       C  
ATOM   4873  O   LEU B 984     -97.648  10.241  10.211  1.00 44.95           O  
ANISOU 4873  O   LEU B 984     4819   6392   5867    310    370    479       O  
ATOM   4874  CB  LEU B 984     -96.569   8.891   7.687  1.00 46.96           C  
ANISOU 4874  CB  LEU B 984     5117   6624   6102    196    230    559       C  
ATOM   4875  CG  LEU B 984     -96.409   8.326   6.269  1.00 45.91           C  
ANISOU 4875  CG  LEU B 984     4983   6499   5961    147    168    610       C  
ATOM   4876  CD1 LEU B 984     -95.159   8.892   5.626  1.00 44.10           C  
ANISOU 4876  CD1 LEU B 984     4814   6181   5761    164    148    591       C  
ATOM   4877  CD2 LEU B 984     -96.339   6.800   6.272  1.00 44.04           C  
ANISOU 4877  CD2 LEU B 984     4775   6300   5657     53    132    614       C  
ATOM   4878  N   LEU B 985     -97.479   8.059  10.792  1.00 45.61           N  
ANISOU 4878  N   LEU B 985     4954   6538   5837    171    331    480       N  
ATOM   4879  CA  LEU B 985     -97.107   8.351  12.182  1.00 48.08           C  
ANISOU 4879  CA  LEU B 985     5318   6826   6125    192    378    413       C  
ATOM   4880  C   LEU B 985     -95.655   8.847  12.265  1.00 45.31           C  
ANISOU 4880  C   LEU B 985     5052   6372   5790    210    356    358       C  
ATOM   4881  O   LEU B 985     -95.349   9.762  13.011  1.00 45.88           O  
ANISOU 4881  O   LEU B 985     5152   6401   5880    262    395    305       O  
ATOM   4882  CB  LEU B 985     -97.291   7.118  13.073  1.00 50.33           C  
ANISOU 4882  CB  LEU B 985     5630   7161   6330    118    380    407       C  
ATOM   4883  CG  LEU B 985     -98.728   6.585  13.268  1.00 52.91           C  
ANISOU 4883  CG  LEU B 985     5874   7595   6633     90    413    453       C  
ATOM   4884  CD1 LEU B 985     -98.727   5.316  14.121  1.00 53.22           C  
ANISOU 4884  CD1 LEU B 985     5959   7670   6591      6    409    450       C  
ATOM   4885  CD2 LEU B 985     -99.632   7.633  13.901  1.00 54.27           C  
ANISOU 4885  CD2 LEU B 985     5980   7802   6837    168    493    437       C  
ATOM   4886  N   TYR B 986     -94.776   8.253  11.462  1.00 42.45           N  
ANISOU 4886  N   TYR B 986     4732   5974   5424    165    295    372       N  
ATOM   4887  CA  TYR B 986     -93.355   8.582  11.492  1.00 40.08           C  
ANISOU 4887  CA  TYR B 986     4506   5585   5140    171    270    324       C  
ATOM   4888  C   TYR B 986     -92.807   8.821  10.074  1.00 34.99           C  
ANISOU 4888  C   TYR B 986     3856   4898   4540    173    229    356       C  
ATOM   4889  O   TYR B 986     -93.388   8.374   9.078  1.00 33.04           O  
ANISOU 4889  O   TYR B 986     3567   4695   4293    149    205    414       O  
ATOM   4890  CB  TYR B 986     -92.587   7.461  12.203  1.00 39.43           C  
ANISOU 4890  CB  TYR B 986     4493   5495   4995    108    239    296       C  
ATOM   4891  CG  TYR B 986     -93.270   7.044  13.480  1.00 43.23           C  
ANISOU 4891  CG  TYR B 986     4977   6031   5418     93    276    281       C  
ATOM   4892  CD1 TYR B 986     -93.215   7.843  14.608  1.00 43.52           C  
ANISOU 4892  CD1 TYR B 986     5036   6051   5449    135    322    226       C  
ATOM   4893  CD2 TYR B 986     -94.035   5.881  13.540  1.00 43.89           C  
ANISOU 4893  CD2 TYR B 986     5040   6185   5451     32    268    323       C  
ATOM   4894  CE1 TYR B 986     -93.867   7.485  15.774  1.00 44.29           C  
ANISOU 4894  CE1 TYR B 986     5137   6204   5486    119    363    212       C  
ATOM   4895  CE2 TYR B 986     -94.698   5.528  14.700  1.00 43.89           C  
ANISOU 4895  CE2 TYR B 986     5040   6239   5396     14    308    313       C  
ATOM   4896  CZ  TYR B 986     -94.613   6.328  15.818  1.00 44.89           C  
ANISOU 4896  CZ  TYR B 986     5191   6353   5513     59    358    258       C  
ATOM   4897  OH  TYR B 986     -95.289   5.974  16.982  1.00 43.33           O  
ANISOU 4897  OH  TYR B 986     4997   6214   5251     38    404    248       O  
ATOM   4898  N   ASN B 987     -91.706   9.553  10.003  1.00 32.22           N  
ANISOU 4898  N   ASN B 987     3550   4467   4226    199    223    318       N  
ATOM   4899  CA  ASN B 987     -91.052   9.830   8.734  1.00 33.20           C  
ANISOU 4899  CA  ASN B 987     3678   4547   4389    198    191    342       C  
ATOM   4900  C   ASN B 987     -90.610   8.546   8.044  1.00 33.01           C  
ANISOU 4900  C   ASN B 987     3676   4539   4327    129    141    365       C  
ATOM   4901  O   ASN B 987     -90.441   7.496   8.681  1.00 31.44           O  
ANISOU 4901  O   ASN B 987     3507   4360   4077     83    125    348       O  
ATOM   4902  CB  ASN B 987     -89.795  10.677   8.922  1.00 32.71           C  
ANISOU 4902  CB  ASN B 987     3667   4396   4367    222    192    291       C  
ATOM   4903  CG  ASN B 987     -90.083  12.023   9.544  1.00 32.89           C  
ANISOU 4903  CG  ASN B 987     3682   4383   4433    290    240    261       C  
ATOM   4904  OD1 ASN B 987     -91.093  12.633   9.254  1.00 34.76           O  
ANISOU 4904  OD1 ASN B 987     3866   4644   4698    335    268    295       O  
ATOM   4905  ND2 ASN B 987     -89.198  12.486  10.401  1.00 33.92           N  
ANISOU 4905  ND2 ASN B 987     3864   4455   4569    298    247    195       N  
ATOM   4906  N   GLU B 988     -90.502   8.624   6.729  1.00 30.62           N  
ANISOU 4906  N   GLU B 988     3358   4230   4046    122    118    406       N  
ATOM   4907  CA  GLU B 988     -89.733   7.667   5.999  1.00 30.57           C  
ANISOU 4907  CA  GLU B 988     3387   4213   4016     67     76    410       C  
ATOM   4908  C   GLU B 988     -89.056   8.376   4.837  1.00 30.31           C  
ANISOU 4908  C   GLU B 988     3359   4133   4026     82     68    425       C  
ATOM   4909  O   GLU B 988     -89.452   9.475   4.447  1.00 31.70           O  
ANISOU 4909  O   GLU B 988     3504   4298   4244    129     88    450       O  
ATOM   4910  CB  GLU B 988     -90.556   6.471   5.542  1.00 31.41           C  
ANISOU 4910  CB  GLU B 988     3473   4388   4073     12     51    453       C  
ATOM   4911  CG  GLU B 988     -91.852   6.770   4.829  1.00 33.58           C  
ANISOU 4911  CG  GLU B 988     3679   4726   4355     23     54    515       C  
ATOM   4912  CD  GLU B 988     -92.699   5.517   4.686  1.00 35.98           C  
ANISOU 4912  CD  GLU B 988     3964   5101   4605    -41     30    548       C  
ATOM   4913  OE1 GLU B 988     -92.818   4.996   3.557  1.00 39.39           O  
ANISOU 4913  OE1 GLU B 988     4393   5554   5020    -81     -4    584       O  
ATOM   4914  OE2 GLU B 988     -93.252   5.049   5.710  1.00 39.49           O  
ANISOU 4914  OE2 GLU B 988     4400   5582   5022    -55     47    538       O  
ATOM   4915  N   TYR B 989     -88.005   7.751   4.334  1.00 28.02           N  
ANISOU 4915  N   TYR B 989     3110   3812   3726     45     42    409       N  
ATOM   4916  CA  TYR B 989     -87.164   8.355   3.348  1.00 27.01           C  
ANISOU 4916  CA  TYR B 989     2994   3635   3633     52     40    414       C  
ATOM   4917  C   TYR B 989     -86.950   7.345   2.258  1.00 26.26           C  
ANISOU 4917  C   TYR B 989     2914   3562   3503      0     11    437       C  
ATOM   4918  O   TYR B 989     -86.671   6.169   2.533  1.00 24.85           O  
ANISOU 4918  O   TYR B 989     2762   3393   3287    -40    -10    416       O  
ATOM   4919  CB  TYR B 989     -85.832   8.723   3.968  1.00 28.17           C  
ANISOU 4919  CB  TYR B 989     3180   3713   3810     62     46    354       C  
ATOM   4920  CG  TYR B 989     -85.913   9.659   5.132  1.00 26.49           C  
ANISOU 4920  CG  TYR B 989     2966   3472   3626    106     73    318       C  
ATOM   4921  CD1 TYR B 989     -86.110   9.179   6.412  1.00 28.02           C  
ANISOU 4921  CD1 TYR B 989     3173   3684   3788    103     74    283       C  
ATOM   4922  CD2 TYR B 989     -85.784  11.019   4.960  1.00 27.86           C  
ANISOU 4922  CD2 TYR B 989     3132   3598   3854    150     98    319       C  
ATOM   4923  CE1 TYR B 989     -86.179  10.023   7.495  1.00 26.94           C  
ANISOU 4923  CE1 TYR B 989     3043   3525   3669    141    101    244       C  
ATOM   4924  CE2 TYR B 989     -85.847  11.874   6.035  1.00 27.02           C  
ANISOU 4924  CE2 TYR B 989     3033   3462   3774    189    125    278       C  
ATOM   4925  CZ  TYR B 989     -86.030  11.359   7.300  1.00 27.25           C  
ANISOU 4925  CZ  TYR B 989     3075   3513   3764    184    126    238       C  
ATOM   4926  OH  TYR B 989     -86.099  12.176   8.389  1.00 27.54           O  
ANISOU 4926  OH  TYR B 989     3124   3522   3816    220    154    193       O  
ATOM   4927  N   ILE B 990     -87.109   7.781   1.013  1.00 24.91           N  
ANISOU 4927  N   ILE B 990     2728   3396   3340      0      9    482       N  
ATOM   4928  CA  ILE B 990     -86.997   6.889  -0.126  1.00 24.67           C  
ANISOU 4928  CA  ILE B 990     2714   3390   3269    -50    -16    505       C  
ATOM   4929  C   ILE B 990     -86.043   7.470  -1.153  1.00 25.97           C  
ANISOU 4929  C   ILE B 990     2898   3511   3457    -49     -7    509       C  
ATOM   4930  O   ILE B 990     -86.154   8.658  -1.550  1.00 25.17           O  
ANISOU 4930  O   ILE B 990     2779   3390   3393    -14      9    539       O  
ATOM   4931  CB  ILE B 990     -88.373   6.640  -0.795  1.00 26.99           C  
ANISOU 4931  CB  ILE B 990     2968   3757   3528    -67    -36    567       C  
ATOM   4932  CG1 ILE B 990     -89.377   6.108   0.227  1.00 28.00           C  
ANISOU 4932  CG1 ILE B 990     3068   3934   3635    -72    -39    567       C  
ATOM   4933  CG2 ILE B 990     -88.274   5.619  -1.896  1.00 27.05           C  
ANISOU 4933  CG2 ILE B 990     3002   3791   3485   -127    -65    582       C  
ATOM   4934  CD1 ILE B 990     -90.113   7.202   0.983  1.00 28.05           C  
ANISOU 4934  CD1 ILE B 990     3028   3948   3682    -11    -10    578       C  
ATOM   4935  N   VAL B 991     -85.107   6.627  -1.612  1.00 25.41           N  
ANISOU 4935  N   VAL B 991     2865   3423   3365    -87    -15    480       N  
ATOM   4936  CA  VAL B 991     -84.286   6.966  -2.786  1.00 24.50           C  
ANISOU 4936  CA  VAL B 991     2768   3282   3257    -98     -4    489       C  
ATOM   4937  C   VAL B 991     -84.543   5.988  -3.924  1.00 25.71           C  
ANISOU 4937  C   VAL B 991     2941   3477   3350   -149    -23    511       C  
ATOM   4938  O   VAL B 991     -84.978   4.864  -3.686  1.00 26.68           O  
ANISOU 4938  O   VAL B 991     3073   3632   3432   -180    -47    501       O  
ATOM   4939  CB  VAL B 991     -82.791   7.011  -2.439  1.00 24.93           C  
ANISOU 4939  CB  VAL B 991     2848   3275   3349    -94     14    430       C  
ATOM   4940  CG1 VAL B 991     -82.511   8.119  -1.442  1.00 24.68           C  
ANISOU 4940  CG1 VAL B 991     2801   3199   3376    -50     32    409       C  
ATOM   4941  CG2 VAL B 991     -82.272   5.679  -1.908  1.00 25.06           C  
ANISOU 4941  CG2 VAL B 991     2890   3290   3343   -120     -3    382       C  
ATOM   4942  N   TYR B 992     -84.292   6.435  -5.153  1.00 26.99           N  
ANISOU 4942  N   TYR B 992     3113   3640   3504   -160    -14    542       N  
ATOM   4943  CA  TYR B 992     -84.688   5.731  -6.379  1.00 27.80           C  
ANISOU 4943  CA  TYR B 992     3234   3788   3541   -208    -33    572       C  
ATOM   4944  C   TYR B 992     -83.501   5.281  -7.196  1.00 28.38           C  
ANISOU 4944  C   TYR B 992     3350   3834   3597   -236    -12    539       C  
ATOM   4945  O   TYR B 992     -83.663   4.873  -8.313  1.00 29.67           O  
ANISOU 4945  O   TYR B 992     3538   4029   3708   -275    -20    560       O  
ATOM   4946  CB  TYR B 992     -85.664   6.610  -7.209  1.00 26.87           C  
ANISOU 4946  CB  TYR B 992     3089   3709   3411   -199    -45    650       C  
ATOM   4947  CG  TYR B 992     -86.873   6.916  -6.373  1.00 27.55           C  
ANISOU 4947  CG  TYR B 992     3126   3827   3516   -168    -63    678       C  
ATOM   4948  CD1 TYR B 992     -86.913   8.025  -5.548  1.00 28.62           C  
ANISOU 4948  CD1 TYR B 992     3233   3928   3715   -109    -41    679       C  
ATOM   4949  CD2 TYR B 992     -87.948   6.038  -6.328  1.00 27.89           C  
ANISOU 4949  CD2 TYR B 992     3150   3933   3512   -200    -97    697       C  
ATOM   4950  CE1 TYR B 992     -88.009   8.289  -4.720  1.00 29.23           C  
ANISOU 4950  CE1 TYR B 992     3262   4034   3809    -76    -48    698       C  
ATOM   4951  CE2 TYR B 992     -89.040   6.299  -5.530  1.00 28.19           C  
ANISOU 4951  CE2 TYR B 992     3136   4005   3569   -172   -107    721       C  
ATOM   4952  CZ  TYR B 992     -89.071   7.415  -4.720  1.00 27.52           C  
ANISOU 4952  CZ  TYR B 992     3021   3887   3547   -107    -80    720       C  
ATOM   4953  OH  TYR B 992     -90.154   7.661  -3.869  1.00 27.80           O  
ANISOU 4953  OH  TYR B 992     3004   3958   3602    -75    -80    738       O  
ATOM   4954  N   ASP B 993     -82.302   5.375  -6.630  1.00 30.23           N  
ANISOU 4954  N   ASP B 993     3594   4014   3880   -218     14    485       N  
ATOM   4955  CA  ASP B 993     -81.073   4.960  -7.294  1.00 29.16           C  
ANISOU 4955  CA  ASP B 993     3488   3851   3739   -239     41    447       C  
ATOM   4956  C   ASP B 993     -80.247   4.258  -6.233  1.00 28.11           C  
ANISOU 4956  C   ASP B 993     3360   3680   3639   -226     41    380       C  
ATOM   4957  O   ASP B 993     -79.960   4.831  -5.205  1.00 27.07           O  
ANISOU 4957  O   ASP B 993     3206   3517   3560   -193     43    363       O  
ATOM   4958  CB  ASP B 993     -80.359   6.193  -7.827  1.00 31.51           C  
ANISOU 4958  CB  ASP B 993     3779   4118   4076   -224     79    464       C  
ATOM   4959  CG  ASP B 993     -79.038   5.880  -8.541  1.00 33.65           C  
ANISOU 4959  CG  ASP B 993     4073   4365   4348   -244    117    426       C  
ATOM   4960  OD1 ASP B 993     -78.420   4.798  -8.364  1.00 32.02           O  
ANISOU 4960  OD1 ASP B 993     3883   4149   4133   -255    118    371       O  
ATOM   4961  OD2 ASP B 993     -78.600   6.761  -9.311  1.00 37.72           O  
ANISOU 4961  OD2 ASP B 993     4590   4869   4874   -249    149    452       O  
ATOM   4962  N   ILE B 994     -79.874   3.018  -6.483  1.00 27.78           N  
ANISOU 4962  N   ILE B 994     3350   3639   3566   -252     35    344       N  
ATOM   4963  CA  ILE B 994     -79.159   2.209  -5.493  1.00 27.82           C  
ANISOU 4963  CA  ILE B 994     3362   3609   3599   -239     26    287       C  
ATOM   4964  C   ILE B 994     -77.796   2.766  -5.097  1.00 26.71           C  
ANISOU 4964  C   ILE B 994     3203   3419   3525   -210     54    247       C  
ATOM   4965  O   ILE B 994     -77.267   2.431  -4.025  1.00 28.25           O  
ANISOU 4965  O   ILE B 994     3393   3585   3756   -189     38    209       O  
ATOM   4966  CB  ILE B 994     -78.970   0.757  -5.978  1.00 28.56           C  
ANISOU 4966  CB  ILE B 994     3499   3704   3649   -271     18    256       C  
ATOM   4967  CG1 ILE B 994     -78.095   0.717  -7.234  1.00 31.11           C  
ANISOU 4967  CG1 ILE B 994     3841   4020   3961   -285     59    238       C  
ATOM   4968  CG2 ILE B 994     -80.308   0.131  -6.237  1.00 26.98           C  
ANISOU 4968  CG2 ILE B 994     3316   3551   3384   -308    -15    290       C  
ATOM   4969  CD1 ILE B 994     -77.853  -0.680  -7.784  1.00 33.38           C  
ANISOU 4969  CD1 ILE B 994     4175   4301   4206   -312     58    200       C  
ATOM   4970  N   ALA B 995     -77.231   3.612  -5.939  1.00 25.86           N  
ANISOU 4970  N   ALA B 995     3087   3304   3436   -212     91    259       N  
ATOM   4971  CA  ALA B 995     -75.939   4.232  -5.666  1.00 24.91           C  
ANISOU 4971  CA  ALA B 995     2942   3140   3382   -192    120    226       C  
ATOM   4972  C   ALA B 995     -76.021   5.345  -4.627  1.00 25.58           C  
ANISOU 4972  C   ALA B 995     2998   3202   3520   -163    111    232       C  
ATOM   4973  O   ALA B 995     -74.988   5.802  -4.170  1.00 25.12           O  
ANISOU 4973  O   ALA B 995     2918   3106   3519   -149    124    200       O  
ATOM   4974  CB  ALA B 995     -75.333   4.761  -6.953  1.00 25.60           C  
ANISOU 4974  CB  ALA B 995     3032   3229   3467   -211    167    240       C  
ATOM   4975  N   GLN B 996     -77.232   5.781  -4.252  1.00 26.38           N  
ANISOU 4975  N   GLN B 996     3095   3324   3603   -153     90    272       N  
ATOM   4976  CA  GLN B 996     -77.403   6.803  -3.225  1.00 26.67           C  
ANISOU 4976  CA  GLN B 996     3110   3337   3686   -123     84    273       C  
ATOM   4977  C   GLN B 996     -77.270   6.305  -1.777  1.00 27.29           C  
ANISOU 4977  C   GLN B 996     3188   3403   3779   -105     54    229       C  
ATOM   4978  O   GLN B 996     -77.477   7.083  -0.835  1.00 24.95           O  
ANISOU 4978  O   GLN B 996     2878   3089   3511    -81     49    224       O  
ATOM   4979  CB  GLN B 996     -78.762   7.514  -3.370  1.00 27.36           C  
ANISOU 4979  CB  GLN B 996     3190   3452   3753   -112     78    331       C  
ATOM   4980  CG  GLN B 996     -78.781   8.641  -4.368  1.00 28.36           C  
ANISOU 4980  CG  GLN B 996     3313   3570   3894   -112    106    377       C  
ATOM   4981  CD  GLN B 996     -80.178   9.176  -4.605  1.00 27.94           C  
ANISOU 4981  CD  GLN B 996     3249   3549   3818    -98     93    440       C  
ATOM   4982  OE1 GLN B 996     -80.841   8.749  -5.534  1.00 28.21           O  
ANISOU 4982  OE1 GLN B 996     3291   3628   3799   -120     83    481       O  
ATOM   4983  NE2 GLN B 996     -80.586  10.172  -3.836  1.00 28.23           N  
ANISOU 4983  NE2 GLN B 996     3267   3562   3897    -60     96    448       N  
ATOM   4984  N   VAL B 997     -76.905   5.043  -1.601  1.00 25.54           N  
ANISOU 4984  N   VAL B 997     2981   3185   3536   -117     35    198       N  
ATOM   4985  CA  VAL B 997     -76.808   4.461  -0.289  1.00 25.09           C  
ANISOU 4985  CA  VAL B 997     2930   3119   3484   -104      2    165       C  
ATOM   4986  C   VAL B 997     -75.411   3.928  -0.067  1.00 25.72           C  
ANISOU 4986  C   VAL B 997     3007   3164   3600   -100     -2    115       C  
ATOM   4987  O   VAL B 997     -74.897   3.159  -0.897  1.00 26.63           O  
ANISOU 4987  O   VAL B 997     3132   3278   3706   -113      9    104       O  
ATOM   4988  CB  VAL B 997     -77.756   3.257  -0.165  1.00 25.23           C  
ANISOU 4988  CB  VAL B 997     2973   3171   3442   -122    -25    179       C  
ATOM   4989  CG1 VAL B 997     -77.616   2.625   1.214  1.00 26.48           C  
ANISOU 4989  CG1 VAL B 997     3144   3318   3601   -111    -60    149       C  
ATOM   4990  CG2 VAL B 997     -79.189   3.698  -0.384  1.00 26.00           C  
ANISOU 4990  CG2 VAL B 997     3063   3311   3504   -127    -24    230       C  
ATOM   4991  N   ASN B 998     -74.836   4.231   1.102  1.00 23.75           N  
ANISOU 4991  N   ASN B 998     2746   2888   3389    -80    -23     82       N  
ATOM   4992  CA  ASN B 998     -73.594   3.615   1.517  1.00 23.84           C  
ANISOU 4992  CA  ASN B 998     2750   2872   3435    -72    -41     37       C  
ATOM   4993  C   ASN B 998     -73.822   3.008   2.891  1.00 25.16           C  
ANISOU 4993  C   ASN B 998     2936   3039   3585    -61    -89     22       C  
ATOM   4994  O   ASN B 998     -73.974   3.724   3.911  1.00 25.14           O  
ANISOU 4994  O   ASN B 998     2930   3031   3592    -51   -104     14       O  
ATOM   4995  CB  ASN B 998     -72.496   4.671   1.503  1.00 26.10           C  
ANISOU 4995  CB  ASN B 998     3000   3128   3788    -66    -21     14       C  
ATOM   4996  CG  ASN B 998     -71.099   4.119   1.709  1.00 25.11           C  
ANISOU 4996  CG  ASN B 998     2851   2979   3709    -58    -35    -29       C  
ATOM   4997  OD1 ASN B 998     -70.197   4.859   2.099  1.00 27.48           O  
ANISOU 4997  OD1 ASN B 998     3119   3257   4065    -55    -36    -54       O  
ATOM   4998  ND2 ASN B 998     -70.887   2.881   1.380  1.00 25.23           N  
ANISOU 4998  ND2 ASN B 998     2881   2999   3707    -55    -43    -39       N  
ATOM   4999  N   LEU B 999     -73.882   1.682   2.917  1.00 25.84           N  
ANISOU 4999  N   LEU B 999     3049   3129   3641    -66   -113     19       N  
ATOM   5000  CA  LEU B 999     -74.085   0.958   4.162  1.00 27.28           C  
ANISOU 5000  CA  LEU B 999     3256   3309   3800    -60   -160     11       C  
ATOM   5001  C   LEU B 999     -72.881   1.119   5.106  1.00 26.02           C  
ANISOU 5001  C   LEU B 999     3078   3118   3689    -39   -192    -28       C  
ATOM   5002  O   LEU B 999     -71.745   1.049   4.678  1.00 27.39           O  
ANISOU 5002  O   LEU B 999     3225   3270   3912    -28   -186    -53       O  
ATOM   5003  CB  LEU B 999     -74.317  -0.516   3.868  1.00 27.14           C  
ANISOU 5003  CB  LEU B 999     3274   3291   3745    -72   -178     18       C  
ATOM   5004  CG  LEU B 999     -75.569  -0.785   3.048  1.00 25.81           C  
ANISOU 5004  CG  LEU B 999     3126   3157   3522   -101   -158     56       C  
ATOM   5005  CD1 LEU B 999     -75.707  -2.287   2.861  1.00 27.51           C  
ANISOU 5005  CD1 LEU B 999     3384   3363   3705   -117   -180     56       C  
ATOM   5006  CD2 LEU B 999     -76.810  -0.215   3.693  1.00 25.79           C  
ANISOU 5006  CD2 LEU B 999     3125   3191   3485   -110   -160     87       C  
ATOM   5007  N   LYS B1000     -73.148   1.442   6.358  1.00 26.50           N  
ANISOU 5007  N   LYS B1000     3150   3184   3736    -34   -222    -33       N  
ATOM   5008  CA  LYS B1000     -72.090   1.727   7.326  1.00 27.65           C  
ANISOU 5008  CA  LYS B1000     3279   3305   3921    -18   -258    -68       C  
ATOM   5009  C   LYS B1000     -72.036   0.713   8.448  1.00 27.98           C  
ANISOU 5009  C   LYS B1000     3355   3345   3932    -13   -316    -72       C  
ATOM   5010  O   LYS B1000     -70.954   0.280   8.830  1.00 27.80           O  
ANISOU 5010  O   LYS B1000     3320   3298   3944      2   -355    -95       O  
ATOM   5011  CB  LYS B1000     -72.269   3.115   7.968  1.00 28.94           C  
ANISOU 5011  CB  LYS B1000     3432   3470   4096    -19   -249    -80       C  
ATOM   5012  CG  LYS B1000     -72.392   4.294   7.004  1.00 29.76           C  
ANISOU 5012  CG  LYS B1000     3508   3570   4231    -23   -194    -71       C  
ATOM   5013  CD  LYS B1000     -71.382   4.299   5.895  1.00 30.68           C  
ANISOU 5013  CD  LYS B1000     3589   3669   4400    -26   -170    -80       C  
ATOM   5014  CE  LYS B1000     -70.021   4.744   6.350  1.00 34.62           C  
ANISOU 5014  CE  LYS B1000     4052   4141   4963    -22   -191   -120       C  
ATOM   5015  NZ  LYS B1000     -69.168   5.005   5.156  1.00 36.26           N  
ANISOU 5015  NZ  LYS B1000     4218   4336   5222    -30   -150   -124       N  
ATOM   5016  N   TYR B1001     -73.181   0.427   9.063  1.00 27.71           N  
ANISOU 5016  N   TYR B1001     3360   3335   3833    -25   -324    -47       N  
ATOM   5017  CA  TYR B1001     -73.203  -0.466  10.240  1.00 28.77           C  
ANISOU 5017  CA  TYR B1001     3534   3468   3929    -25   -378    -44       C  
ATOM   5018  C   TYR B1001     -74.288  -1.522  10.094  1.00 28.54           C  
ANISOU 5018  C   TYR B1001     3547   3456   3839    -46   -376     -6       C  
ATOM   5019  O   TYR B1001     -75.294  -1.311   9.392  1.00 26.26           O  
ANISOU 5019  O   TYR B1001     3256   3194   3527    -63   -334     18       O  
ATOM   5020  CB  TYR B1001     -73.416   0.293  11.552  1.00 28.17           C  
ANISOU 5020  CB  TYR B1001     3472   3406   3827    -26   -397    -57       C  
ATOM   5021  CG  TYR B1001     -72.386   1.338  11.822  1.00 31.94           C  
ANISOU 5021  CG  TYR B1001     3914   3864   4359    -14   -406    -97       C  
ATOM   5022  CD1 TYR B1001     -71.134   1.005  12.373  1.00 32.54           C  
ANISOU 5022  CD1 TYR B1001     3978   3916   4469     -2   -463   -122       C  
ATOM   5023  CD2 TYR B1001     -72.651   2.684  11.529  1.00 34.20           C  
ANISOU 5023  CD2 TYR B1001     4176   4153   4667    -16   -361   -109       C  
ATOM   5024  CE1 TYR B1001     -70.195   1.974  12.612  1.00 33.87           C  
ANISOU 5024  CE1 TYR B1001     4109   4069   4689      2   -474   -159       C  
ATOM   5025  CE2 TYR B1001     -71.719   3.672  11.771  1.00 32.93           C  
ANISOU 5025  CE2 TYR B1001     3986   3969   4558    -12   -369   -146       C  
ATOM   5026  CZ  TYR B1001     -70.499   3.304  12.306  1.00 35.68           C  
ANISOU 5026  CZ  TYR B1001     4320   4299   4937     -7   -425   -172       C  
ATOM   5027  OH  TYR B1001     -69.559   4.255  12.521  1.00 40.23           O  
ANISOU 5027  OH  TYR B1001     4863   4856   5567    -10   -436   -209       O  
ATOM   5028  N   LEU B1002     -74.027  -2.666  10.731  1.00 27.35           N  
ANISOU 5028  N   LEU B1002     3434   3288   3668    -46   -425      0       N  
ATOM   5029  CA  LEU B1002     -74.979  -3.731  10.838  1.00 27.49           C  
ANISOU 5029  CA  LEU B1002     3500   3318   3628    -72   -433     36       C  
ATOM   5030  C   LEU B1002     -75.106  -4.054  12.298  1.00 26.97           C  
ANISOU 5030  C   LEU B1002     3474   3257   3517    -77   -479     45       C  
ATOM   5031  O   LEU B1002     -74.129  -4.291  12.953  1.00 26.19           O  
ANISOU 5031  O   LEU B1002     3381   3132   3438    -57   -528     29       O  
ATOM   5032  CB  LEU B1002     -74.496  -4.924  10.067  1.00 30.03           C  
ANISOU 5032  CB  LEU B1002     3837   3602   3971    -67   -446     38       C  
ATOM   5033  CG  LEU B1002     -75.362  -6.192  10.075  1.00 32.40           C  
ANISOU 5033  CG  LEU B1002     4194   3899   4217    -99   -459     73       C  
ATOM   5034  CD1 LEU B1002     -76.702  -5.922   9.464  1.00 35.95           C  
ANISOU 5034  CD1 LEU B1002     4641   4394   4625   -137   -413     99       C  
ATOM   5035  CD2 LEU B1002     -74.701  -7.271   9.265  1.00 34.32           C  
ANISOU 5035  CD2 LEU B1002     4453   4093   4492    -88   -469     63       C  
ATOM   5036  N   LEU B1003     -76.322  -3.997  12.834  1.00 28.71           N  
ANISOU 5036  N   LEU B1003     3720   3517   3673   -106   -462     71       N  
ATOM   5037  CA  LEU B1003     -76.543  -4.273  14.244  1.00 29.39           C  
ANISOU 5037  CA  LEU B1003     3849   3615   3703   -117   -498     82       C  
ATOM   5038  C   LEU B1003     -77.267  -5.594  14.400  1.00 30.04           C  
ANISOU 5038  C   LEU B1003     3985   3698   3733   -151   -514    125       C  
ATOM   5039  O   LEU B1003     -78.241  -5.880  13.683  1.00 28.91           O  
ANISOU 5039  O   LEU B1003     3840   3576   3570   -180   -477    150       O  
ATOM   5040  CB  LEU B1003     -77.364  -3.180  14.891  1.00 29.92           C  
ANISOU 5040  CB  LEU B1003     3907   3729   3732   -125   -461     76       C  
ATOM   5041  CG  LEU B1003     -76.680  -1.889  15.318  1.00 31.01           C  
ANISOU 5041  CG  LEU B1003     4016   3863   3903    -99   -460     32       C  
ATOM   5042  CD1 LEU B1003     -76.141  -1.140  14.120  1.00 30.11           C  
ANISOU 5042  CD1 LEU B1003     3846   3729   3863    -78   -430     10       C  
ATOM   5043  CD2 LEU B1003     -77.676  -1.026  16.082  1.00 31.71           C  
ANISOU 5043  CD2 LEU B1003     4111   3996   3941   -108   -422     28       C  
ATOM   5044  N   LYS B1004     -76.787  -6.390  15.341  1.00 31.16           N  
ANISOU 5044  N   LYS B1004     4173   3815   3850   -151   -571    136       N  
ATOM   5045  CA  LYS B1004     -77.525  -7.560  15.802  1.00 33.86           C  
ANISOU 5045  CA  LYS B1004     4577   4158   4132   -189   -589    182       C  
ATOM   5046  C   LYS B1004     -78.303  -7.117  17.022  1.00 32.77           C  
ANISOU 5046  C   LYS B1004     4460   4070   3919   -214   -580    195       C  
ATOM   5047  O   LYS B1004     -77.716  -6.694  17.999  1.00 30.55           O  
ANISOU 5047  O   LYS B1004     4191   3791   3626   -197   -612    177       O  
ATOM   5048  CB  LYS B1004     -76.549  -8.672  16.143  1.00 38.04           C  
ANISOU 5048  CB  LYS B1004     5149   4628   4678   -172   -659    191       C  
ATOM   5049  CG  LYS B1004     -77.164 -10.001  16.521  1.00 40.46           C  
ANISOU 5049  CG  LYS B1004     5525   4916   4930   -212   -683    241       C  
ATOM   5050  CD  LYS B1004     -76.067 -11.057  16.557  1.00 44.50           C  
ANISOU 5050  CD  LYS B1004     6072   5355   5483   -180   -749    245       C  
ATOM   5051  CE  LYS B1004     -76.386 -12.189  17.519  1.00 51.80           C  
ANISOU 5051  CE  LYS B1004     7078   6257   6346   -211   -797    297       C  
ATOM   5052  NZ  LYS B1004     -75.288 -13.203  17.510  1.00 53.48           N  
ANISOU 5052  NZ  LYS B1004     7322   6391   6608   -171   -863    303       N  
ATOM   5053  N   LEU B1005     -79.625  -7.189  16.928  1.00 35.19           N  
ANISOU 5053  N   LEU B1005     4771   4422   4179   -255   -533    224       N  
ATOM   5054  CA  LEU B1005     -80.528  -6.747  17.974  1.00 36.55           C  
ANISOU 5054  CA  LEU B1005     4958   4651   4280   -280   -507    235       C  
ATOM   5055  C   LEU B1005     -81.344  -7.890  18.583  1.00 37.52           C  
ANISOU 5055  C   LEU B1005     5139   4787   4330   -334   -517    288       C  
ATOM   5056  O   LEU B1005     -81.822  -8.777  17.873  1.00 35.97           O  
ANISOU 5056  O   LEU B1005     4953   4577   4137   -366   -513    319       O  
ATOM   5057  CB  LEU B1005     -81.526  -5.756  17.393  1.00 39.96           C  
ANISOU 5057  CB  LEU B1005     5330   5134   4717   -282   -434    228       C  
ATOM   5058  CG  LEU B1005     -81.040  -4.441  16.797  1.00 39.91           C  
ANISOU 5058  CG  LEU B1005     5266   5125   4775   -237   -407    182       C  
ATOM   5059  CD1 LEU B1005     -82.237  -3.659  16.326  1.00 41.63           C  
ANISOU 5059  CD1 LEU B1005     5435   5395   4987   -243   -339    190       C  
ATOM   5060  CD2 LEU B1005     -80.292  -3.645  17.827  1.00 42.45           C  
ANISOU 5060  CD2 LEU B1005     5597   5440   5091   -209   -428    143       C  
ATOM   5061  N   LYS B1006     -81.488  -7.865  19.906  1.00 40.40           N  
ANISOU 5061  N   LYS B1006     5547   5177   4627   -349   -530    298       N  
ATOM   5062  CA  LYS B1006     -82.366  -8.757  20.611  1.00 39.07           C  
ANISOU 5062  CA  LYS B1006     5432   5032   4380   -406   -527    349       C  
ATOM   5063  C   LYS B1006     -83.616  -7.949  20.829  1.00 38.48           C  
ANISOU 5063  C   LYS B1006     5319   5036   4265   -427   -450    348       C  
ATOM   5064  O   LYS B1006     -83.553  -6.846  21.362  1.00 36.72           O  
ANISOU 5064  O   LYS B1006     5076   4845   4033   -399   -425    310       O  
ATOM   5065  CB  LYS B1006     -81.791  -9.154  21.995  1.00 42.65           C  
ANISOU 5065  CB  LYS B1006     5958   5473   4774   -411   -584    363       C  
ATOM   5066  N   PHE B1007     -84.747  -8.519  20.416  1.00 37.96           N  
ANISOU 5066  N   PHE B1007     5244   5001   4177   -477   -414    389       N  
ATOM   5067  CA  PHE B1007     -86.064  -7.974  20.676  1.00 39.37           C  
ANISOU 5067  CA  PHE B1007     5385   5260   4313   -505   -341    400       C  
ATOM   5068  C   PHE B1007     -86.597  -8.633  21.960  1.00 43.76           C  
ANISOU 5068  C   PHE B1007     6005   5848   4775   -558   -340    439       C  
ATOM   5069  O   PHE B1007     -86.751  -9.847  21.992  1.00 41.79           O  
ANISOU 5069  O   PHE B1007     5805   5575   4500   -608   -371    487       O  
ATOM   5070  CB  PHE B1007     -87.003  -8.326  19.515  1.00 39.62           C  
ANISOU 5070  CB  PHE B1007     5369   5312   4372   -538   -309    428       C  
ATOM   5071  CG  PHE B1007     -86.716  -7.594  18.231  1.00 37.70           C  
ANISOU 5071  CG  PHE B1007     5060   5054   4209   -493   -298    396       C  
ATOM   5072  CD1 PHE B1007     -85.540  -7.813  17.525  1.00 36.54           C  
ANISOU 5072  CD1 PHE B1007     4926   4836   4122   -460   -346    373       C  
ATOM   5073  CD2 PHE B1007     -87.667  -6.725  17.694  1.00 37.99           C  
ANISOU 5073  CD2 PHE B1007     5021   5150   4263   -486   -237    393       C  
ATOM   5074  CE1 PHE B1007     -85.293  -7.140  16.336  1.00 37.52           C  
ANISOU 5074  CE1 PHE B1007     4993   4950   4313   -424   -331    347       C  
ATOM   5075  CE2 PHE B1007     -87.423  -6.045  16.508  1.00 37.12           C  
ANISOU 5075  CE2 PHE B1007     4857   5026   4222   -447   -228    370       C  
ATOM   5076  CZ  PHE B1007     -86.233  -6.255  15.828  1.00 35.06           C  
ANISOU 5076  CZ  PHE B1007     4614   4695   4012   -419   -274    347       C  
ATOM   5077  N   ASN B1008     -86.837  -7.849  23.018  1.00 45.86           N  
ANISOU 5077  N   ASN B1008     6276   6164   4987   -548   -305    418       N  
ATOM   5078  CA  ASN B1008     -87.407  -8.366  24.265  1.00 46.81           C  
ANISOU 5078  CA  ASN B1008     6454   6324   5006   -601   -293    453       C  
ATOM   5079  C   ASN B1008     -88.882  -8.055  24.293  1.00 47.09           C  
ANISOU 5079  C   ASN B1008     6437   6446   5010   -636   -204    470       C  
ATOM   5080  O   ASN B1008     -89.283  -6.933  24.609  1.00 44.48           O  
ANISOU 5080  O   ASN B1008     6063   6166   4672   -604   -144    431       O  
ATOM   5081  CB  ASN B1008     -86.712  -7.750  25.485  1.00 49.67           C  
ANISOU 5081  CB  ASN B1008     6863   6690   5317   -573   -312    417       C  
ATOM   5082  CG  ASN B1008     -85.265  -8.210  25.624  1.00 49.47           C  
ANISOU 5082  CG  ASN B1008     6894   6587   5315   -546   -409    411       C  
ATOM   5083  OD1 ASN B1008     -84.970  -9.396  25.509  1.00 49.56           O  
ANISOU 5083  OD1 ASN B1008     6953   6552   5325   -573   -464    458       O  
ATOM   5084  ND2 ASN B1008     -84.364  -7.268  25.808  1.00 48.75           N  
ANISOU 5084  ND2 ASN B1008     6790   6479   5253   -491   -431    354       N  
ATOM   5085  N   PHE B1009     -89.683  -9.044  23.921  1.00 49.11           N  
ANISOU 5085  N   PHE B1009     6692   6714   5252   -700   -196    526       N  
ATOM   5086  CA  PHE B1009     -91.131  -8.854  23.813  1.00 52.89           C  
ANISOU 5086  CA  PHE B1009     7106   7277   5711   -739   -115    549       C  
ATOM   5087  C   PHE B1009     -91.763  -8.683  25.205  1.00 58.80           C  
ANISOU 5087  C   PHE B1009     7884   8096   6362   -769    -61    557       C  
ATOM   5088  O   PHE B1009     -91.372  -9.350  26.158  1.00 56.56           O  
ANISOU 5088  O   PHE B1009     7688   7793   6008   -802    -96    581       O  
ATOM   5089  CB  PHE B1009     -91.732  -9.992  23.002  1.00 51.67           C  
ANISOU 5089  CB  PHE B1009     6946   7114   5572   -807   -130    605       C  
ATOM   5090  CG  PHE B1009     -91.365  -9.926  21.539  1.00 54.36           C  
ANISOU 5090  CG  PHE B1009     7241   7408   6004   -776   -159    588       C  
ATOM   5091  CD1 PHE B1009     -90.249 -10.586  21.054  1.00 55.49           C  
ANISOU 5091  CD1 PHE B1009     7437   7459   6185   -761   -235    583       C  
ATOM   5092  CD2 PHE B1009     -92.118  -9.160  20.650  1.00 55.42           C  
ANISOU 5092  CD2 PHE B1009     7278   7593   6187   -757   -110    576       C  
ATOM   5093  CE1 PHE B1009     -89.902 -10.513  19.702  1.00 57.48           C  
ANISOU 5093  CE1 PHE B1009     7651   7673   6516   -733   -255    565       C  
ATOM   5094  CE2 PHE B1009     -91.776  -9.080  19.299  1.00 58.00           C  
ANISOU 5094  CE2 PHE B1009     7568   7880   6589   -732   -137    562       C  
ATOM   5095  CZ  PHE B1009     -90.659  -9.757  18.821  1.00 57.35           C  
ANISOU 5095  CZ  PHE B1009     7544   7709   6539   -721   -207    554       C  
ATOM   5096  N   LYS B1010     -92.700  -7.746  25.317  1.00 62.00           N  
ANISOU 5096  N   LYS B1010     8215   8579   6763   -753     24    536       N  
ATOM   5097  CA  LYS B1010     -93.217  -7.301  26.617  1.00 63.75           C  
ANISOU 5097  CA  LYS B1010     8456   8869   6897   -762     88    524       C  
ATOM   5098  C   LYS B1010     -94.647  -7.809  26.803  1.00 64.29           C  
ANISOU 5098  C   LYS B1010     8486   9022   6921   -836    159    577       C  
ATOM   5099  O   LYS B1010     -95.151  -8.524  25.940  1.00 58.31           O  
ANISOU 5099  O   LYS B1010     7692   8264   6201   -881    147    622       O  
ATOM   5100  CB  LYS B1010     -93.139  -5.771  26.722  1.00 61.39           C  
ANISOU 5100  CB  LYS B1010     8107   8592   6628   -680    139    451       C  
TER    5101      LYS B1010                                                      
ATOM   5102  N   LYS C 662     -99.899  44.477 -47.591  1.00 70.03           N  
ANISOU 5102  N   LYS C 662     7775  11209   7625   1641    308   1168       N  
ATOM   5103  CA  LYS C 662     -99.204  45.194 -46.461  1.00 72.25           C  
ANISOU 5103  CA  LYS C 662     8178  11279   7995   1639    372   1190       C  
ATOM   5104  C   LYS C 662     -99.310  44.419 -45.145  1.00 71.43           C  
ANISOU 5104  C   LYS C 662     8068  11112   7962   1514    346   1122       C  
ATOM   5105  O   LYS C 662    -100.357  43.840 -44.844  1.00 74.87           O  
ANISOU 5105  O   LYS C 662     8404  11675   8367   1487    308   1097       O  
ATOM   5106  CB  LYS C 662     -99.753  46.614 -46.264  1.00 75.55           C  
ANISOU 5106  CB  LYS C 662     8632  11691   8382   1801    451   1292       C  
ATOM   5107  N   SER C 663     -98.226  44.397 -44.371  1.00 66.58           N  
ANISOU 5107  N   SER C 663     7555  10306   7437   1437    366   1092       N  
ATOM   5108  CA  SER C 663     -98.185  43.594 -43.140  1.00 64.21           C  
ANISOU 5108  CA  SER C 663     7257   9936   7204   1316    341   1025       C  
ATOM   5109  C   SER C 663     -98.924  44.283 -42.007  1.00 61.97           C  
ANISOU 5109  C   SER C 663     6983   9630   6932   1372    385   1064       C  
ATOM   5110  O   SER C 663     -98.885  45.511 -41.882  1.00 58.79           O  
ANISOU 5110  O   SER C 663     6646   9167   6526   1483    452   1134       O  
ATOM   5111  CB  SER C 663     -96.745  43.309 -42.701  1.00 66.67           C  
ANISOU 5111  CB  SER C 663     7669  10063   7602   1219    345    979       C  
ATOM   5112  N   LYS C 664     -99.578  43.485 -41.171  1.00 58.00           N  
ANISOU 5112  N   LYS C 664     6421   9172   6445   1295    352   1018       N  
ATOM   5113  CA  LYS C 664    -100.159  43.996 -39.945  1.00 61.65           C  
ANISOU 5113  CA  LYS C 664     6900   9596   6929   1329    391   1043       C  
ATOM   5114  C   LYS C 664     -99.140  44.082 -38.792  1.00 59.28           C  
ANISOU 5114  C   LYS C 664     6711   9094   6720   1261    417   1014       C  
ATOM   5115  O   LYS C 664     -99.511  44.505 -37.703  1.00 59.73           O  
ANISOU 5115  O   LYS C 664     6792   9103   6798   1284    451   1029       O  
ATOM   5116  CB  LYS C 664    -101.369  43.136 -39.530  1.00 68.78           C  
ANISOU 5116  CB  LYS C 664     7685  10643   7805   1279    348   1011       C  
ATOM   5117  N   LEU C 665     -97.887  43.662 -39.016  1.00 53.79           N  
ANISOU 5117  N   LEU C 665     6077   8289   6072   1180    401    970       N  
ATOM   5118  CA  LEU C 665     -96.841  43.720 -37.986  1.00 47.92           C  
ANISOU 5118  CA  LEU C 665     5433   7365   5409   1115    422    938       C  
ATOM   5119  C   LEU C 665     -96.329  45.134 -37.772  1.00 47.89           C  
ANISOU 5119  C   LEU C 665     5530   7241   5423   1205    496    994       C  
ATOM   5120  O   LEU C 665     -96.189  45.899 -38.720  1.00 49.82           O  
ANISOU 5120  O   LEU C 665     5796   7499   5634   1290    527   1045       O  
ATOM   5121  CB  LEU C 665     -95.637  42.862 -38.375  1.00 45.87           C  
ANISOU 5121  CB  LEU C 665     5203   7037   5188   1009    382    877       C  
ATOM   5122  CG  LEU C 665     -95.862  41.361 -38.564  1.00 44.35           C  
ANISOU 5122  CG  LEU C 665     4935   6925   4991    900    312    810       C  
ATOM   5123  CD1 LEU C 665     -94.654  40.725 -39.234  1.00 43.70           C  
ANISOU 5123  CD1 LEU C 665     4887   6783   4932    829    283    765       C  
ATOM   5124  CD2 LEU C 665     -96.164  40.683 -37.250  1.00 44.52           C  
ANISOU 5124  CD2 LEU C 665     4949   6913   5053    823    300    769       C  
ATOM   5125  N   PRO C 666     -96.009  45.477 -36.527  1.00 46.70           N  
ANISOU 5125  N   PRO C 666     5450   6969   5327   1183    528    982       N  
ATOM   5126  CA  PRO C 666     -95.372  46.757 -36.246  1.00 47.56           C  
ANISOU 5126  CA  PRO C 666     5666   6942   5462   1246    600   1020       C  
ATOM   5127  C   PRO C 666     -94.077  46.951 -37.045  1.00 51.01           C  
ANISOU 5127  C   PRO C 666     6165   7293   5923   1221    609   1013       C  
ATOM   5128  O   PRO C 666     -93.384  45.977 -37.362  1.00 53.48           O  
ANISOU 5128  O   PRO C 666     6459   7604   6256   1126    556    959       O  
ATOM   5129  CB  PRO C 666     -95.048  46.669 -34.749  1.00 46.09           C  
ANISOU 5129  CB  PRO C 666     5531   6645   5335   1182    609    977       C  
ATOM   5130  CG  PRO C 666     -95.946  45.606 -34.208  1.00 44.93           C  
ANISOU 5130  CG  PRO C 666     5295   6599   5176   1129    558    945       C  
ATOM   5131  CD  PRO C 666     -96.166  44.642 -35.322  1.00 44.62           C  
ANISOU 5131  CD  PRO C 666     5169   6683   5101   1092    499    927       C  
ATOM   5132  N   LYS C 667     -93.759  48.197 -37.369  1.00 53.09           N  
ANISOU 5132  N   LYS C 667     6504   7484   6184   1307    678   1068       N  
ATOM   5133  CA  LYS C 667     -92.574  48.496 -38.171  1.00 55.34           C  
ANISOU 5133  CA  LYS C 667     6848   7690   6488   1291    696   1070       C  
ATOM   5134  C   LYS C 667     -91.305  47.855 -37.566  1.00 53.55           C  
ANISOU 5134  C   LYS C 667     6663   7351   6332   1160    668    994       C  
ATOM   5135  O   LYS C 667     -90.564  47.193 -38.279  1.00 52.98           O  
ANISOU 5135  O   LYS C 667     6575   7289   6266   1102    630    964       O  
ATOM   5136  CB  LYS C 667     -92.385  50.017 -38.331  1.00 52.16           C  
ANISOU 5136  CB  LYS C 667     6538   7195   6084   1393    790   1138       C  
ATOM   5137  N   PRO C 668     -91.067  48.053 -36.257  1.00 48.75           N  
ANISOU 5137  N   PRO C 668     6106   6645   5772   1120    686    963       N  
ATOM   5138  CA  PRO C 668     -89.884  47.489 -35.622  1.00 45.58           C  
ANISOU 5138  CA  PRO C 668     5741   6147   5431   1006    661    893       C  
ATOM   5139  C   PRO C 668     -89.730  46.000 -35.863  1.00 39.82           C  
ANISOU 5139  C   PRO C 668     4941   5489   4702    916    580    839       C  
ATOM   5140  O   PRO C 668     -88.627  45.523 -36.073  1.00 38.91           O  
ANISOU 5140  O   PRO C 668     4844   5323   4616    844    557    798       O  
ATOM   5141  CB  PRO C 668     -90.120  47.769 -34.142  1.00 50.31           C  
ANISOU 5141  CB  PRO C 668     6376   6680   6060    993    681    872       C  
ATOM   5142  CG  PRO C 668     -91.013  48.998 -34.122  1.00 49.58           C  
ANISOU 5142  CG  PRO C 668     6312   6590   5936   1114    750    942       C  
ATOM   5143  CD  PRO C 668     -91.915  48.798 -35.298  1.00 50.66           C  
ANISOU 5143  CD  PRO C 668     6371   6869   6009   1185    731    991       C  
ATOM   5144  N   VAL C 669     -90.833  45.285 -35.866  1.00 38.09           N  
ANISOU 5144  N   VAL C 669     4639   5387   4446    923    540    838       N  
ATOM   5145  CA  VAL C 669     -90.811  43.852 -36.079  1.00 37.25           C  
ANISOU 5145  CA  VAL C 669     4468   5348   4337    837    469    786       C  
ATOM   5146  C   VAL C 669     -90.459  43.563 -37.527  1.00 39.98           C  
ANISOU 5146  C   VAL C 669     4786   5751   4652    842    446    792       C  
ATOM   5147  O   VAL C 669     -89.652  42.678 -37.831  1.00 41.69           O  
ANISOU 5147  O   VAL C 669     5000   5953   4888    765    406    745       O  
ATOM   5148  CB  VAL C 669     -92.164  43.203 -35.685  1.00 35.53           C  
ANISOU 5148  CB  VAL C 669     4167   5244   4087    838    438    783       C  
ATOM   5149  CG1 VAL C 669     -92.160  41.713 -35.942  1.00 33.71           C  
ANISOU 5149  CG1 VAL C 669     3877   5076   3856    744    371    726       C  
ATOM   5150  CG2 VAL C 669     -92.469  43.461 -34.218  1.00 34.42           C  
ANISOU 5150  CG2 VAL C 669     4057   5044   3977    832    461    776       C  
ATOM   5151  N   GLN C 670     -91.089  44.299 -38.427  1.00 42.66           N  
ANISOU 5151  N   GLN C 670     5105   6162   4940    940    473    854       N  
ATOM   5152  CA  GLN C 670     -90.819  44.168 -39.845  1.00 42.15           C  
ANISOU 5152  CA  GLN C 670     5016   6160   4838    962    458    869       C  
ATOM   5153  C   GLN C 670     -89.348  44.390 -40.118  1.00 39.64           C  
ANISOU 5153  C   GLN C 670     4772   5726   4562    924    477    854       C  
ATOM   5154  O   GLN C 670     -88.728  43.613 -40.835  1.00 40.04           O  
ANISOU 5154  O   GLN C 670     4804   5798   4610    873    438    821       O  
ATOM   5155  CB  GLN C 670     -91.684  45.154 -40.659  1.00 46.79           C  
ANISOU 5155  CB  GLN C 670     5585   6831   5362   1092    498    949       C  
ATOM   5156  CG  GLN C 670     -93.163  44.757 -40.754  1.00 47.43           C  
ANISOU 5156  CG  GLN C 670     5566   7072   5384   1130    466    961       C  
ATOM   5157  CD  GLN C 670     -94.057  45.696 -41.566  1.00 51.20           C  
ANISOU 5157  CD  GLN C 670     6015   7649   5788   1269    503   1043       C  
ATOM   5158  OE1 GLN C 670     -95.286  45.724 -41.373  1.00 52.10           O  
ANISOU 5158  OE1 GLN C 670     6062   7875   5858   1321    497   1066       O  
ATOM   5159  NE2 GLN C 670     -93.465  46.459 -42.467  1.00 52.97           N  
ANISOU 5159  NE2 GLN C 670     6290   7840   5998   1334    544   1089       N  
ATOM   5160  N   ASP C 671     -88.790  45.439 -39.537  1.00 38.68           N  
ANISOU 5160  N   ASP C 671     4733   5485   4480    947    538    876       N  
ATOM   5161  CA  ASP C 671     -87.359  45.715 -39.666  1.00 39.21           C  
ANISOU 5161  CA  ASP C 671     4869   5437   4591    903    561    859       C  
ATOM   5162  C   ASP C 671     -86.469  44.585 -39.111  1.00 38.54           C  
ANISOU 5162  C   ASP C 671     4780   5311   4551    785    508    780       C  
ATOM   5163  O   ASP C 671     -85.443  44.268 -39.719  1.00 34.57           O  
ANISOU 5163  O   ASP C 671     4291   4782   4062    744    497    760       O  
ATOM   5164  CB  ASP C 671     -87.005  47.051 -39.005  1.00 44.70           C  
ANISOU 5164  CB  ASP C 671     5653   6008   5321    939    639    888       C  
ATOM   5165  CG  ASP C 671     -87.520  48.275 -39.809  1.00 53.02           C  
ANISOU 5165  CG  ASP C 671     6734   7077   6334   1061    706    973       C  
ATOM   5166  OD1 ASP C 671     -88.082  48.087 -40.918  1.00 53.98           O  
ANISOU 5166  OD1 ASP C 671     6801   7311   6397   1119    689   1010       O  
ATOM   5167  OD2 ASP C 671     -87.391  49.422 -39.312  1.00 59.22           O  
ANISOU 5167  OD2 ASP C 671     7596   7763   7142   1102    778   1003       O  
ATOM   5168  N   LEU C 672     -86.880  43.964 -37.995  1.00 35.39           N  
ANISOU 5168  N   LEU C 672     4363   4913   4172    737    479    741       N  
ATOM   5169  CA  LEU C 672     -86.161  42.833 -37.450  1.00 33.81           C  
ANISOU 5169  CA  LEU C 672     4157   4683   4006    637    430    673       C  
ATOM   5170  C   LEU C 672     -86.164  41.666 -38.430  1.00 34.56           C  
ANISOU 5170  C   LEU C 672     4194   4865   4072    603    374    648       C  
ATOM   5171  O   LEU C 672     -85.134  41.030 -38.653  1.00 32.86           O  
ANISOU 5171  O   LEU C 672     3992   4616   3878    544    350    609       O  
ATOM   5172  CB  LEU C 672     -86.768  42.412 -36.107  1.00 33.51           C  
ANISOU 5172  CB  LEU C 672     4107   4638   3985    605    414    645       C  
ATOM   5173  CG  LEU C 672     -86.190  41.178 -35.415  1.00 32.33           C  
ANISOU 5173  CG  LEU C 672     3952   4465   3867    511    367    580       C  
ATOM   5174  CD1 LEU C 672     -84.767  41.442 -34.953  1.00 33.08           C  
ANISOU 5174  CD1 LEU C 672     4110   4450   4008    468    382    551       C  
ATOM   5175  CD2 LEU C 672     -87.052  40.776 -34.239  1.00 32.66           C  
ANISOU 5175  CD2 LEU C 672     3973   4522   3913    494    356    565       C  
ATOM   5176  N   ILE C 673     -87.323  41.370 -39.006  1.00 36.86           N  
ANISOU 5176  N   ILE C 673     4420   5273   4313    639    352    667       N  
ATOM   5177  CA  ILE C 673     -87.433  40.267 -39.962  1.00 37.40           C  
ANISOU 5177  CA  ILE C 673     4431   5432   4348    605    299    638       C  
ATOM   5178  C   ILE C 673     -86.526  40.477 -41.162  1.00 36.92           C  
ANISOU 5178  C   ILE C 673     4390   5364   4275    622    306    650       C  
ATOM   5179  O   ILE C 673     -85.879  39.548 -41.643  1.00 36.57           O  
ANISOU 5179  O   ILE C 673     4336   5325   4232    566    269    607       O  
ATOM   5180  CB  ILE C 673     -88.896  40.067 -40.443  1.00 39.70           C  
ANISOU 5180  CB  ILE C 673     4641   5863   4579    647    278    658       C  
ATOM   5181  CG1 ILE C 673     -89.817  39.760 -39.267  1.00 40.69           C  
ANISOU 5181  CG1 ILE C 673     4739   6004   4716    623    270    644       C  
ATOM   5182  CG2 ILE C 673     -88.988  38.937 -41.463  1.00 38.79           C  
ANISOU 5182  CG2 ILE C 673     4468   5842   4427    605    224    620       C  
ATOM   5183  CD1 ILE C 673     -89.259  38.732 -38.312  1.00 43.20           C  
ANISOU 5183  CD1 ILE C 673     5077   6254   5083    523    242    581       C  
ATOM   5184  N   LYS C 674     -86.490  41.693 -41.675  1.00 40.08           N  
ANISOU 5184  N   LYS C 674     4819   5750   4660    704    358    711       N  
ATOM   5185  CA  LYS C 674     -85.616  41.998 -42.826  1.00 40.60           C  
ANISOU 5185  CA  LYS C 674     4908   5805   4713    726    374    730       C  
ATOM   5186  C   LYS C 674     -84.148  41.805 -42.469  1.00 38.72           C  
ANISOU 5186  C   LYS C 674     4724   5455   4531    655    379    691       C  
ATOM   5187  O   LYS C 674     -83.360  41.209 -43.217  1.00 39.13           O  
ANISOU 5187  O   LYS C 674     4773   5517   4580    623    356    667       O  
ATOM   5188  CB  LYS C 674     -85.823  43.439 -43.287  1.00 42.08           C  
ANISOU 5188  CB  LYS C 674     5130   5979   4879    828    442    808       C  
ATOM   5189  CG  LYS C 674     -87.146  43.682 -43.986  1.00 48.49           C  
ANISOU 5189  CG  LYS C 674     5883   6922   5620    918    440    857       C  
ATOM   5190  CD  LYS C 674     -87.257  45.145 -44.420  1.00 52.85           C  
ANISOU 5190  CD  LYS C 674     6483   7447   6153   1028    516    941       C  
ATOM   5191  CE  LYS C 674     -88.680  45.500 -44.786  1.00 56.99           C  
ANISOU 5191  CE  LYS C 674     6951   8096   6608   1128    521    994       C  
ATOM   5192  NZ  LYS C 674     -88.895  46.975 -44.816  1.00 61.11           N  
ANISOU 5192  NZ  LYS C 674     7531   8567   7119   1238    605   1076       N  
ATOM   5193  N   MET C 675     -83.803  42.344 -41.319  1.00 35.66           N  
ANISOU 5193  N   MET C 675     4386   4969   4194    635    409    685       N  
ATOM   5194  CA  MET C 675     -82.476  42.248 -40.782  1.00 37.32           C  
ANISOU 5194  CA  MET C 675     4643   5079   4457    569    415    646       C  
ATOM   5195  C   MET C 675     -82.002  40.781 -40.681  1.00 35.98           C  
ANISOU 5195  C   MET C 675     4445   4931   4296    489    352    581       C  
ATOM   5196  O   MET C 675     -80.890  40.435 -41.135  1.00 33.52           O  
ANISOU 5196  O   MET C 675     4147   4592   3997    454    344    559       O  
ATOM   5197  CB  MET C 675     -82.505  42.899 -39.417  1.00 38.34           C  
ANISOU 5197  CB  MET C 675     4815   5125   4628    559    447    642       C  
ATOM   5198  CG  MET C 675     -81.176  43.220 -38.830  1.00 42.44           C  
ANISOU 5198  CG  MET C 675     5389   5538   5198    505    469    612       C  
ATOM   5199  SD  MET C 675     -81.527  43.961 -37.223  1.00 45.31           S  
ANISOU 5199  SD  MET C 675     5795   5825   5597    503    502    605       S  
ATOM   5200  CE  MET C 675     -79.868  43.990 -36.601  1.00 40.42           C  
ANISOU 5200  CE  MET C 675     5219   5107   5030    422    509    552       C  
ATOM   5201  N   ILE C 676     -82.860  39.911 -40.146  1.00 34.06           N  
ANISOU 5201  N   ILE C 676     4161   4736   4043    463    311    554       N  
ATOM   5202  CA  ILE C 676     -82.423  38.533 -39.877  1.00 33.51           C  
ANISOU 5202  CA  ILE C 676     4076   4668   3986    388    260    492       C  
ATOM   5203  C   ILE C 676     -82.476  37.622 -41.086  1.00 32.36           C  
ANISOU 5203  C   ILE C 676     3891   4602   3801    378    222    476       C  
ATOM   5204  O   ILE C 676     -81.727  36.640 -41.158  1.00 30.71           O  
ANISOU 5204  O   ILE C 676     3687   4377   3604    325    192    430       O  
ATOM   5205  CB  ILE C 676     -83.072  37.907 -38.640  1.00 34.69           C  
ANISOU 5205  CB  ILE C 676     4214   4813   4153    349    239    463       C  
ATOM   5206  CG1 ILE C 676     -84.534  37.612 -38.816  1.00 37.10           C  
ANISOU 5206  CG1 ILE C 676     4463   5215   4420    370    221    475       C  
ATOM   5207  CG2 ILE C 676     -82.875  38.807 -37.425  1.00 36.12           C  
ANISOU 5207  CG2 ILE C 676     4440   4912   4372    356    277    473       C  
ATOM   5208  CD1 ILE C 676     -85.102  37.101 -37.510  1.00 37.59           C  
ANISOU 5208  CD1 ILE C 676     4519   5262   4503    331    209    450       C  
ATOM   5209  N   PHE C 677     -83.299  37.970 -42.077  1.00 32.46           N  
ANISOU 5209  N   PHE C 677     3868   4702   3765    436    225    512       N  
ATOM   5210  CA  PHE C 677     -83.352  37.200 -43.333  1.00 31.12           C  
ANISOU 5210  CA  PHE C 677     3659   4615   3549    432    190    496       C  
ATOM   5211  C   PHE C 677     -82.590  37.857 -44.506  1.00 32.32           C  
ANISOU 5211  C   PHE C 677     3830   4768   3681    480    216    531       C  
ATOM   5212  O   PHE C 677     -82.780  37.494 -45.650  1.00 32.42           O  
ANISOU 5212  O   PHE C 677     3811   4862   3646    500    196    531       O  
ATOM   5213  CB  PHE C 677     -84.791  36.921 -43.715  1.00 30.49           C  
ANISOU 5213  CB  PHE C 677     3513   4654   3417    455    165    502       C  
ATOM   5214  CG  PHE C 677     -85.422  35.795 -42.938  1.00 29.65           C  
ANISOU 5214  CG  PHE C 677     3378   4567   3321    386    126    450       C  
ATOM   5215  CD1 PHE C 677     -85.008  34.480 -43.127  1.00 29.86           C  
ANISOU 5215  CD1 PHE C 677     3401   4593   3351    314     87    389       C  
ATOM   5216  CD2 PHE C 677     -86.446  36.047 -42.057  1.00 28.45           C  
ANISOU 5216  CD2 PHE C 677     3203   4433   3173    395    133    465       C  
ATOM   5217  CE1 PHE C 677     -85.592  33.433 -42.422  1.00 30.50           C  
ANISOU 5217  CE1 PHE C 677     3462   4685   3443    248     58    344       C  
ATOM   5218  CE2 PHE C 677     -87.044  35.011 -41.355  1.00 29.92           C  
ANISOU 5218  CE2 PHE C 677     3363   4637   3369    328    103    420       C  
ATOM   5219  CZ  PHE C 677     -86.629  33.696 -41.547  1.00 29.52           C  
ANISOU 5219  CZ  PHE C 677     3311   4581   3323    253     66    359       C  
ATOM   5220  N   ASP C 678     -81.652  38.744 -44.195  1.00 34.68           N  
ANISOU 5220  N   ASP C 678     4184   4974   4020    491    262    555       N  
ATOM   5221  CA  ASP C 678     -80.882  39.466 -45.202  1.00 34.22           C  
ANISOU 5221  CA  ASP C 678     4149   4902   3949    533    298    593       C  
ATOM   5222  C   ASP C 678     -79.861  38.577 -45.902  1.00 32.27           C  
ANISOU 5222  C   ASP C 678     3902   4660   3699    492    270    554       C  
ATOM   5223  O   ASP C 678     -78.795  38.247 -45.352  1.00 32.52           O  
ANISOU 5223  O   ASP C 678     3963   4620   3775    437    268    519       O  
ATOM   5224  CB  ASP C 678     -80.196  40.663 -44.547  1.00 38.79           C  
ANISOU 5224  CB  ASP C 678     4788   5374   4575    543    359    622       C  
ATOM   5225  CG  ASP C 678     -79.663  41.640 -45.570  1.00 43.92           C  
ANISOU 5225  CG  ASP C 678     5465   6011   5210    598    411    677       C  
ATOM   5226  OD1 ASP C 678     -79.145  41.229 -46.625  1.00 44.57           O  
ANISOU 5226  OD1 ASP C 678     5534   6134   5266    601    398    674       O  
ATOM   5227  OD2 ASP C 678     -79.734  42.841 -45.309  1.00 52.79           O  
ANISOU 5227  OD2 ASP C 678     6629   7080   6349    639    470    723       O  
ATOM   5228  N   VAL C 679     -80.172  38.213 -47.140  1.00 31.77           N  
ANISOU 5228  N   VAL C 679     3804   4688   3579    522    250    560       N  
ATOM   5229  CA  VAL C 679     -79.343  37.287 -47.958  1.00 31.66           C  
ANISOU 5229  CA  VAL C 679     3786   4695   3550    492    220    522       C  
ATOM   5230  C   VAL C 679     -77.979  37.879 -48.279  1.00 31.93           C  
ANISOU 5230  C   VAL C 679     3862   4659   3609    497    262    543       C  
ATOM   5231  O   VAL C 679     -76.947  37.190 -48.275  1.00 31.83           O  
ANISOU 5231  O   VAL C 679     3862   4614   3617    451    247    503       O  
ATOM   5232  CB  VAL C 679     -80.080  36.937 -49.257  1.00 32.11           C  
ANISOU 5232  CB  VAL C 679     3795   4872   3532    533    194    529       C  
ATOM   5233  CG1 VAL C 679     -79.202  36.160 -50.219  1.00 32.66           C  
ANISOU 5233  CG1 VAL C 679     3867   4962   3580    515    174    497       C  
ATOM   5234  CG2 VAL C 679     -81.332  36.152 -48.922  1.00 32.06           C  
ANISOU 5234  CG2 VAL C 679     3741   4938   3503    508    148    493       C  
ATOM   5235  N   GLU C 680     -77.952  39.173 -48.505  1.00 31.12           N  
ANISOU 5235  N   GLU C 680     3784   4532   3508    553    318    605       N  
ATOM   5236  CA  GLU C 680     -76.682  39.843 -48.745  1.00 33.22           C  
ANISOU 5236  CA  GLU C 680     4091   4727   3803    552    366    627       C  
ATOM   5237  C   GLU C 680     -75.749  39.771 -47.514  1.00 28.44           C  
ANISOU 5237  C   GLU C 680     3517   4023   3267    480    372    588       C  
ATOM   5238  O   GLU C 680     -74.552  39.615 -47.658  1.00 27.67           O  
ANISOU 5238  O   GLU C 680     3433   3889   3190    448    380    570       O  
ATOM   5239  CB  GLU C 680     -76.949  41.314 -49.120  1.00 32.72           C  
ANISOU 5239  CB  GLU C 680     4055   4645   3731    625    435    704       C  
ATOM   5240  CG  GLU C 680     -75.662  42.098 -49.360  1.00 37.37           C  
ANISOU 5240  CG  GLU C 680     4690   5156   4353    617    495    729       C  
ATOM   5241  CD  GLU C 680     -75.858  43.505 -49.930  1.00 42.43           C  
ANISOU 5241  CD  GLU C 680     5366   5776   4981    693    571    810       C  
ATOM   5242  OE1 GLU C 680     -76.803  43.730 -50.708  1.00 44.17           O  
ANISOU 5242  OE1 GLU C 680     5567   6074   5143    771    574    855       O  
ATOM   5243  OE2 GLU C 680     -75.042  44.387 -49.603  1.00 44.51           O  
ANISOU 5243  OE2 GLU C 680     5678   5944   5290    674    632    828       O  
ATOM   5244  N   SER C 681     -76.307  39.942 -46.319  1.00 28.61           N  
ANISOU 5244  N   SER C 681     3545   4006   3318    461    369    576       N  
ATOM   5245  CA  SER C 681     -75.534  39.769 -45.097  1.00 29.65           C  
ANISOU 5245  CA  SER C 681     3700   4060   3506    396    366    534       C  
ATOM   5246  C   SER C 681     -74.986  38.352 -44.969  1.00 27.43           C  
ANISOU 5246  C   SER C 681     3399   3796   3226    342    311    473       C  
ATOM   5247  O   SER C 681     -73.854  38.174 -44.519  1.00 29.37           O  
ANISOU 5247  O   SER C 681     3661   3993   3505    300    314    445       O  
ATOM   5248  CB  SER C 681     -76.345  40.076 -43.853  1.00 31.31           C  
ANISOU 5248  CB  SER C 681     3918   4239   3740    389    368    530       C  
ATOM   5249  OG  SER C 681     -76.591  41.465 -43.775  1.00 33.36           O  
ANISOU 5249  OG  SER C 681     4210   4456   4009    433    429    582       O  
ATOM   5250  N   MET C 682     -75.777  37.360 -45.377  1.00 25.57           N  
ANISOU 5250  N   MET C 682     3131   3633   2953    345    264    452       N  
ATOM   5251  CA  MET C 682     -75.308  35.966 -45.408  1.00 25.12           C  
ANISOU 5251  CA  MET C 682     3063   3591   2892    301    217    396       C  
ATOM   5252  C   MET C 682     -74.072  35.809 -46.304  1.00 24.27           C  
ANISOU 5252  C   MET C 682     2963   3483   2777    302    226    393       C  
ATOM   5253  O   MET C 682     -73.049  35.272 -45.888  1.00 22.35           O  
ANISOU 5253  O   MET C 682     2732   3203   2558    265    218    359       O  
ATOM   5254  CB  MET C 682     -76.423  35.023 -45.861  1.00 24.04           C  
ANISOU 5254  CB  MET C 682     2890   3533   2710    302    173    375       C  
ATOM   5255  CG  MET C 682     -77.615  34.967 -44.915  1.00 25.49           C  
ANISOU 5255  CG  MET C 682     3060   3724   2903    291    160    370       C  
ATOM   5256  SD  MET C 682     -78.932  33.975 -45.658  1.00 28.91           S  
ANISOU 5256  SD  MET C 682     3442   4265   3278    290    114    346       S  
ATOM   5257  CE  MET C 682     -80.394  34.713 -44.905  1.00 29.72           C  
ANISOU 5257  CE  MET C 682     3520   4394   3379    315    125    380       C  
ATOM   5258  N   LYS C 683     -74.162  36.318 -47.525  1.00 25.11           N  
ANISOU 5258  N   LYS C 683     3061   3635   2845    351    247    433       N  
ATOM   5259  CA  LYS C 683     -73.031  36.267 -48.454  1.00 26.75           C  
ANISOU 5259  CA  LYS C 683     3275   3847   3042    359    261    437       C  
ATOM   5260  C   LYS C 683     -71.814  37.046 -47.962  1.00 25.34           C  
ANISOU 5260  C   LYS C 683     3123   3593   2912    338    305    449       C  
ATOM   5261  O   LYS C 683     -70.674  36.594 -48.093  1.00 24.59           O  
ANISOU 5261  O   LYS C 683     3030   3485   2826    314    303    425       O  
ATOM   5262  CB  LYS C 683     -73.452  36.772 -49.814  1.00 28.39           C  
ANISOU 5262  CB  LYS C 683     3470   4120   3197    423    280    484       C  
ATOM   5263  CG  LYS C 683     -74.389  35.839 -50.545  1.00 30.61           C  
ANISOU 5263  CG  LYS C 683     3716   4492   3420    437    231    461       C  
ATOM   5264  CD  LYS C 683     -74.850  36.549 -51.831  1.00 37.00           C  
ANISOU 5264  CD  LYS C 683     4513   5373   4173    511    255    516       C  
ATOM   5265  CE  LYS C 683     -76.047  35.884 -52.488  1.00 40.92           C  
ANISOU 5265  CE  LYS C 683     4966   5975   4606    532    209    499       C  
ATOM   5266  NZ  LYS C 683     -76.495  36.691 -53.653  1.00 46.16           N  
ANISOU 5266  NZ  LYS C 683     5615   6712   5212    614    235    559       N  
ATOM   5267  N   LYS C 684     -72.046  38.229 -47.429  1.00 25.49           N  
ANISOU 5267  N   LYS C 684     3162   3564   2959    347    349    484       N  
ATOM   5268  CA  LYS C 684     -70.937  39.029 -46.903  1.00 28.35           C  
ANISOU 5268  CA  LYS C 684     3550   3853   3369    317    393    489       C  
ATOM   5269  C   LYS C 684     -70.190  38.267 -45.816  1.00 26.54           C  
ANISOU 5269  C   LYS C 684     3318   3591   3174    256    362    431       C  
ATOM   5270  O   LYS C 684     -68.958  38.250 -45.770  1.00 25.17           O  
ANISOU 5270  O   LYS C 684     3147   3397   3021    226    374    415       O  
ATOM   5271  CB  LYS C 684     -71.437  40.388 -46.425  1.00 31.24           C  
ANISOU 5271  CB  LYS C 684     3945   4166   3758    335    446    531       C  
ATOM   5272  CG  LYS C 684     -71.520  41.378 -47.562  1.00 35.63           C  
ANISOU 5272  CG  LYS C 684     4516   4732   4290    393    501    596       C  
ATOM   5273  CD  LYS C 684     -71.882  42.754 -47.011  1.00 42.65           C  
ANISOU 5273  CD  LYS C 684     5445   5552   5208    409    563    637       C  
ATOM   5274  CE  LYS C 684     -71.995  43.790 -48.125  1.00 47.66           C  
ANISOU 5274  CE  LYS C 684     6104   6189   5818    474    628    709       C  
ATOM   5275  NZ  LYS C 684     -72.152  45.182 -47.605  1.00 50.75           N  
ANISOU 5275  NZ  LYS C 684     6547   6495   6242    486    701    748       N  
ATOM   5276  N   ALA C 685     -70.946  37.636 -44.925  1.00 26.75           N  
ANISOU 5276  N   ALA C 685     3339   3619   3205    240    323    401       N  
ATOM   5277  CA  ALA C 685     -70.343  36.829 -43.855  1.00 26.45           C  
ANISOU 5277  CA  ALA C 685     3301   3556   3194    191    292    348       C  
ATOM   5278  C   ALA C 685     -69.461  35.759 -44.445  1.00 26.01           C  
ANISOU 5278  C   ALA C 685     3232   3532   3119    183    265    320       C  
ATOM   5279  O   ALA C 685     -68.315  35.594 -44.015  1.00 26.83           O  
ANISOU 5279  O   ALA C 685     3336   3614   3244    155    267    296       O  
ATOM   5280  CB  ALA C 685     -71.414  36.202 -43.019  1.00 28.16           C  
ANISOU 5280  CB  ALA C 685     3513   3778   3408    183    256    327       C  
ATOM   5281  N   MET C 686     -69.944  35.099 -45.500  1.00 25.43           N  
ANISOU 5281  N   MET C 686     3146   3514   3003    211    243    322       N  
ATOM   5282  CA  MET C 686     -69.135  34.075 -46.167  1.00 26.01           C  
ANISOU 5282  CA  MET C 686     3212   3616   3053    210    221    295       C  
ATOM   5283  C   MET C 686     -67.884  34.651 -46.819  1.00 25.13           C  
ANISOU 5283  C   MET C 686     3099   3502   2946    217    258    315       C  
ATOM   5284  O   MET C 686     -66.790  34.022 -46.825  1.00 23.55           O  
ANISOU 5284  O   MET C 686     2895   3305   2748    204    250    289       O  
ATOM   5285  CB  MET C 686     -69.979  33.297 -47.194  1.00 27.04           C  
ANISOU 5285  CB  MET C 686     3332   3810   3133    236    192    290       C  
ATOM   5286  CG  MET C 686     -71.072  32.465 -46.537  1.00 28.79           C  
ANISOU 5286  CG  MET C 686     3551   4038   3350    216    153    258       C  
ATOM   5287  SD  MET C 686     -72.256  31.652 -47.669  1.00 31.74           S  
ANISOU 5287  SD  MET C 686     3904   4491   3663    234    119    245       S  
ATOM   5288  CE  MET C 686     -71.144  30.419 -48.310  1.00 29.13           C  
ANISOU 5288  CE  MET C 686     3587   4168   3312    227    101    202       C  
ATOM   5289  N   VAL C 687     -68.016  35.836 -47.404  1.00 26.36           N  
ANISOU 5289  N   VAL C 687     3259   3654   3102    241    302    364       N  
ATOM   5290  CA  VAL C 687     -66.849  36.493 -47.983  1.00 26.81           C  
ANISOU 5290  CA  VAL C 687     3316   3703   3168    242    346    387       C  
ATOM   5291  C   VAL C 687     -65.849  36.781 -46.875  1.00 26.19           C  
ANISOU 5291  C   VAL C 687     3239   3574   3137    191    359    362       C  
ATOM   5292  O   VAL C 687     -64.686  36.493 -47.031  1.00 24.80           O  
ANISOU 5292  O   VAL C 687     3050   3408   2965    176    363    346       O  
ATOM   5293  CB  VAL C 687     -67.224  37.772 -48.745  1.00 27.70           C  
ANISOU 5293  CB  VAL C 687     3441   3811   3273    278    400    449       C  
ATOM   5294  CG1 VAL C 687     -65.994  38.617 -49.054  1.00 26.91           C  
ANISOU 5294  CG1 VAL C 687     3346   3682   3196    263    456    471       C  
ATOM   5295  CG2 VAL C 687     -67.947  37.409 -50.039  1.00 29.74           C  
ANISOU 5295  CG2 VAL C 687     3690   4139   3472    334    386    471       C  
ATOM   5296  N   GLU C 688     -66.310  37.312 -45.753  1.00 28.13           N  
ANISOU 5296  N   GLU C 688     3498   3774   3416    167    364    357       N  
ATOM   5297  CA  GLU C 688     -65.417  37.608 -44.637  1.00 33.41           C  
ANISOU 5297  CA  GLU C 688     4166   4401   4126    117    374    328       C  
ATOM   5298  C   GLU C 688     -64.697  36.363 -44.095  1.00 32.86           C  
ANISOU 5298  C   GLU C 688     4077   4355   4052     98    328    278       C  
ATOM   5299  O   GLU C 688     -63.585  36.475 -43.589  1.00 29.41           O  
ANISOU 5299  O   GLU C 688     3627   3912   3636     66    337    256       O  
ATOM   5300  CB  GLU C 688     -66.141  38.352 -43.506  1.00 36.94           C  
ANISOU 5300  CB  GLU C 688     4634   4798   4605     99    386    327       C  
ATOM   5301  CG  GLU C 688     -66.298  39.832 -43.788  1.00 44.26           C  
ANISOU 5301  CG  GLU C 688     5585   5681   5549    104    450    372       C  
ATOM   5302  CD  GLU C 688     -67.285  40.545 -42.873  1.00 49.12           C  
ANISOU 5302  CD  GLU C 688     6228   6250   6185    104    463    379       C  
ATOM   5303  OE1 GLU C 688     -67.811  39.969 -41.900  1.00 51.63           O  
ANISOU 5303  OE1 GLU C 688     6543   6568   6506     93    423    348       O  
ATOM   5304  OE2 GLU C 688     -67.558  41.713 -43.189  1.00 53.13           O  
ANISOU 5304  OE2 GLU C 688     6763   6720   6702    120    519    421       O  
ATOM   5305  N   TYR C 689     -65.316  35.192 -44.224  1.00 31.04           N  
ANISOU 5305  N   TYR C 689     3847   4154   3793    119    283    260       N  
ATOM   5306  CA  TYR C 689     -64.646  33.945 -43.842  1.00 31.35           C  
ANISOU 5306  CA  TYR C 689     3876   4211   3822    113    246    219       C  
ATOM   5307  C   TYR C 689     -63.733  33.413 -44.911  1.00 33.49           C  
ANISOU 5307  C   TYR C 689     4134   4524   4066    134    248    218       C  
ATOM   5308  O   TYR C 689     -63.107  32.370 -44.711  1.00 33.81           O  
ANISOU 5308  O   TYR C 689     4170   4581   4094    138    222    188       O  
ATOM   5309  CB  TYR C 689     -65.660  32.868 -43.495  1.00 29.45           C  
ANISOU 5309  CB  TYR C 689     3649   3975   3565    121    203    197       C  
ATOM   5310  CG  TYR C 689     -66.374  33.098 -42.193  1.00 28.16           C  
ANISOU 5310  CG  TYR C 689     3497   3776   3428     99    195    187       C  
ATOM   5311  CD1 TYR C 689     -65.669  33.263 -40.990  1.00 29.07           C  
ANISOU 5311  CD1 TYR C 689     3609   3866   3570     71    196    165       C  
ATOM   5312  CD2 TYR C 689     -67.735  33.105 -42.158  1.00 26.82           C  
ANISOU 5312  CD2 TYR C 689     3335   3604   3251    107    185    198       C  
ATOM   5313  CE1 TYR C 689     -66.335  33.456 -39.802  1.00 28.93           C  
ANISOU 5313  CE1 TYR C 689     3602   3817   3572     55    188    156       C  
ATOM   5314  CE2 TYR C 689     -68.403  33.303 -41.006  1.00 28.37           C  
ANISOU 5314  CE2 TYR C 689     3541   3771   3469     91    179    192       C  
ATOM   5315  CZ  TYR C 689     -67.713  33.470 -39.827  1.00 28.86           C  
ANISOU 5315  CZ  TYR C 689     3605   3803   3557     65    181    171       C  
ATOM   5316  OH  TYR C 689     -68.449  33.672 -38.684  1.00 29.87           O  
ANISOU 5316  OH  TYR C 689     3744   3904   3702     53    177    165       O  
ATOM   5317  N   GLU C 690     -63.661  34.117 -46.045  1.00 34.04           N  
ANISOU 5317  N   GLU C 690     4200   4609   4124    153    281    255       N  
ATOM   5318  CA  GLU C 690     -62.797  33.749 -47.160  1.00 33.80           C  
ANISOU 5318  CA  GLU C 690     4156   4620   4065    177    290    261       C  
ATOM   5319  C   GLU C 690     -63.251  32.477 -47.825  1.00 34.85           C  
ANISOU 5319  C   GLU C 690     4298   4789   4155    209    251    242       C  
ATOM   5320  O   GLU C 690     -62.460  31.761 -48.440  1.00 34.43           O  
ANISOU 5320  O   GLU C 690     4238   4768   4076    228    246    230       O  
ATOM   5321  CB  GLU C 690     -61.340  33.656 -46.732  1.00 39.36           C  
ANISOU 5321  CB  GLU C 690     4838   5331   4785    154    299    241       C  
ATOM   5322  CG  GLU C 690     -60.758  35.010 -46.352  1.00 44.59           C  
ANISOU 5322  CG  GLU C 690     5490   5965   5488    115    346    259       C  
ATOM   5323  CD  GLU C 690     -59.256  34.968 -46.069  1.00 52.44           C  
ANISOU 5323  CD  GLU C 690     6449   6982   6492     90    357    238       C  
ATOM   5324  OE1 GLU C 690     -58.653  33.865 -45.913  1.00 54.69           O  
ANISOU 5324  OE1 GLU C 690     6719   7302   6757    106    325    209       O  
ATOM   5325  OE2 GLU C 690     -58.671  36.069 -46.009  1.00 58.40           O  
ANISOU 5325  OE2 GLU C 690     7192   7720   7276     54    402    252       O  
ATOM   5326  N   ILE C 691     -64.540  32.189 -47.692  1.00 34.54           N  
ANISOU 5326  N   ILE C 691     4273   4746   4105    213    226    238       N  
ATOM   5327  CA  ILE C 691     -65.132  31.067 -48.372  1.00 35.11           C  
ANISOU 5327  CA  ILE C 691     4354   4852   4135    235    193    216       C  
ATOM   5328  C   ILE C 691     -65.216  31.350 -49.869  1.00 38.49           C  
ANISOU 5328  C   ILE C 691     4775   5327   4523    273    209    245       C  
ATOM   5329  O   ILE C 691     -65.499  32.461 -50.269  1.00 43.19           O  
ANISOU 5329  O   ILE C 691     5364   5924   5120    286    241    288       O  
ATOM   5330  CB  ILE C 691     -66.489  30.758 -47.765  1.00 34.80           C  
ANISOU 5330  CB  ILE C 691     4325   4800   4098    221    165    202       C  
ATOM   5331  CG1 ILE C 691     -66.191  30.152 -46.395  1.00 34.85           C  
ANISOU 5331  CG1 ILE C 691     4342   4766   4135    191    147    169       C  
ATOM   5332  CG2 ILE C 691     -67.304  29.805 -48.633  1.00 33.51           C  
ANISOU 5332  CG2 ILE C 691     4166   4677   3888    237    135    181       C  
ATOM   5333  CD1 ILE C 691     -67.343  29.699 -45.575  1.00 38.42           C  
ANISOU 5333  CD1 ILE C 691     4805   5197   4594    171    121    150       C  
ATOM   5334  N   ASP C 692     -64.953  30.343 -50.683  1.00 39.28           N  
ANISOU 5334  N   ASP C 692     4879   5463   4582    294    191    221       N  
ATOM   5335  CA  ASP C 692     -65.042  30.472 -52.121  1.00 37.38           C  
ANISOU 5335  CA  ASP C 692     4632   5275   4294    334    201    242       C  
ATOM   5336  C   ASP C 692     -66.489  30.331 -52.573  1.00 36.11           C  
ANISOU 5336  C   ASP C 692     4472   5148   4100    345    177    240       C  
ATOM   5337  O   ASP C 692     -66.998  29.221 -52.690  1.00 33.08           O  
ANISOU 5337  O   ASP C 692     4098   4780   3690    337    140    196       O  
ATOM   5338  CB  ASP C 692     -64.187  29.394 -52.780  1.00 42.22           C  
ANISOU 5338  CB  ASP C 692     5253   5915   4874    353    190    211       C  
ATOM   5339  CG  ASP C 692     -64.008  29.569 -54.316  1.00 45.17           C  
ANISOU 5339  CG  ASP C 692     5618   6347   5196    399    208    235       C  
ATOM   5340  OD1 ASP C 692     -64.957  29.477 -55.146  1.00 50.02           O  
ANISOU 5340  OD1 ASP C 692     6232   7005   5766    421    193    237       O  
ATOM   5341  OD2 ASP C 692     -62.840  29.704 -54.690  1.00 49.87           O  
ANISOU 5341  OD2 ASP C 692     6206   6951   5790    414    234    248       O  
ATOM   5342  N   LEU C 693     -67.152  31.468 -52.797  1.00 36.65           N  
ANISOU 5342  N   LEU C 693     4529   5226   4169    361    200    287       N  
ATOM   5343  CA  LEU C 693     -68.569  31.496 -53.174  1.00 37.41           C  
ANISOU 5343  CA  LEU C 693     4617   5365   4232    376    179    292       C  
ATOM   5344  C   LEU C 693     -68.823  30.986 -54.580  1.00 36.55           C  
ANISOU 5344  C   LEU C 693     4499   5332   4055    413    164    284       C  
ATOM   5345  O   LEU C 693     -69.939  30.629 -54.930  1.00 35.38           O  
ANISOU 5345  O   LEU C 693     4339   5234   3870    418    135    268       O  
ATOM   5346  CB  LEU C 693     -69.138  32.901 -53.028  1.00 37.77           C  
ANISOU 5346  CB  LEU C 693     4656   5402   4294    395    214    350       C  
ATOM   5347  CG  LEU C 693     -69.403  33.426 -51.621  1.00 39.65           C  
ANISOU 5347  CG  LEU C 693     4901   5574   4589    360    222    353       C  
ATOM   5348  CD1 LEU C 693     -70.041  34.805 -51.688  1.00 39.57           C  
ANISOU 5348  CD1 LEU C 693     4891   5560   4584    391    261    413       C  
ATOM   5349  CD2 LEU C 693     -70.344  32.485 -50.882  1.00 40.18           C  
ANISOU 5349  CD2 LEU C 693     4966   5644   4658    328    174    307       C  
ATOM   5350  N   GLN C 694     -67.784  30.956 -55.391  1.00 42.21           N  
ANISOU 5350  N   GLN C 694     5220   6065   4754    439    185    294       N  
ATOM   5351  CA  GLN C 694     -67.863  30.341 -56.706  1.00 46.60           C  
ANISOU 5351  CA  GLN C 694     5771   6692   5242    474    170    279       C  
ATOM   5352  C   GLN C 694     -68.018  28.835 -56.584  1.00 44.29           C  
ANISOU 5352  C   GLN C 694     5493   6402   4932    444    124    205       C  
ATOM   5353  O   GLN C 694     -68.892  28.261 -57.212  1.00 46.25           O  
ANISOU 5353  O   GLN C 694     5736   6706   5131    449     94    175       O  
ATOM   5354  CB  GLN C 694     -66.619  30.678 -57.543  1.00 52.91           C  
ANISOU 5354  CB  GLN C 694     6572   7503   6027    509    209    309       C  
ATOM   5355  CG  GLN C 694     -66.795  30.497 -59.052  1.00 56.45           C  
ANISOU 5355  CG  GLN C 694     7014   8035   6400    562    206    316       C  
ATOM   5356  CD  GLN C 694     -66.554  29.114 -59.592  1.00 54.68           C  
ANISOU 5356  CD  GLN C 694     6802   7841   6133    561    172    252       C  
ATOM   5357  OE1 GLN C 694     -65.419  28.672 -59.656  1.00 57.08           O  
ANISOU 5357  OE1 GLN C 694     7119   8125   6445    563    184    239       O  
ATOM   5358  NE2 GLN C 694     -67.605  28.468 -60.072  1.00 58.20           N  
ANISOU 5358  NE2 GLN C 694     7244   8341   6530    561    132    213       N  
ATOM   5359  N   LYS C 695     -67.207  28.196 -55.734  1.00 44.34           N  
ANISOU 5359  N   LYS C 695     5520   6349   4978    414    121    174       N  
ATOM   5360  CA  LYS C 695     -67.294  26.718 -55.554  1.00 42.79           C  
ANISOU 5360  CA  LYS C 695     5350   6141   4769    388     86    105       C  
ATOM   5361  C   LYS C 695     -68.373  26.293 -54.536  1.00 42.68           C  
ANISOU 5361  C   LYS C 695     5341   6097   4780    340     57     75       C  
ATOM   5362  O   LYS C 695     -68.942  25.216 -54.643  1.00 40.29           O  
ANISOU 5362  O   LYS C 695     5054   5801   4453    316     28     21       O  
ATOM   5363  CB  LYS C 695     -65.914  26.115 -55.223  1.00 43.41           C  
ANISOU 5363  CB  LYS C 695     5450   6178   4866    391     98     89       C  
ATOM   5364  N   MET C 696     -68.673  27.150 -53.563  1.00 41.29           N  
ANISOU 5364  N   MET C 696     5152   5886   4651    323     68    107       N  
ATOM   5365  CA  MET C 696     -69.718  26.858 -52.593  1.00 40.45           C  
ANISOU 5365  CA  MET C 696     5046   5755   4567    281     45     85       C  
ATOM   5366  C   MET C 696     -70.652  28.041 -52.336  1.00 39.00           C  
ANISOU 5366  C   MET C 696     4835   5588   4397    287     54    131       C  
ATOM   5367  O   MET C 696     -70.500  28.742 -51.354  1.00 38.62           O  
ANISOU 5367  O   MET C 696     4787   5491   4395    276     72    157       O  
ATOM   5368  CB  MET C 696     -69.124  26.423 -51.265  1.00 40.86           C  
ANISOU 5368  CB  MET C 696     5122   5731   4670    250     46     67       C  
ATOM   5369  CG  MET C 696     -70.175  25.848 -50.315  1.00 41.95           C  
ANISOU 5369  CG  MET C 696     5269   5844   4827    206     23     37       C  
ATOM   5370  SD  MET C 696     -69.451  25.122 -48.849  1.00 50.16           S  
ANISOU 5370  SD  MET C 696     6343   6801   5914    179     24     14       S  
ATOM   5371  CE  MET C 696     -69.031  26.567 -47.879  1.00 53.91           C  
ANISOU 5371  CE  MET C 696     6798   7247   6440    183     50     65       C  
ATOM   5372  N   PRO C 697     -71.638  28.247 -53.207  1.00 36.85           N  
ANISOU 5372  N   PRO C 697     4537   5386   4076    307     43    138       N  
ATOM   5373  CA  PRO C 697     -72.585  29.342 -52.966  1.00 36.53           C  
ANISOU 5373  CA  PRO C 697     4470   5366   4042    322     53    184       C  
ATOM   5374  C   PRO C 697     -73.483  29.094 -51.749  1.00 33.73           C  
ANISOU 5374  C   PRO C 697     4114   4981   3722    277     35    164       C  
ATOM   5375  O   PRO C 697     -73.580  27.974 -51.296  1.00 34.14           O  
ANISOU 5375  O   PRO C 697     4180   5010   3781    233     10    111       O  
ATOM   5376  CB  PRO C 697     -73.433  29.363 -54.236  1.00 35.43           C  
ANISOU 5376  CB  PRO C 697     4301   5326   3833    356     38    188       C  
ATOM   5377  CG  PRO C 697     -73.299  28.009 -54.810  1.00 38.36           C  
ANISOU 5377  CG  PRO C 697     4684   5722   4169    332      6    122       C  
ATOM   5378  CD  PRO C 697     -71.904  27.551 -54.476  1.00 38.41           C  
ANISOU 5378  CD  PRO C 697     4728   5656   4208    322     21    108       C  
ATOM   5379  N   LEU C 698     -74.168  30.137 -51.301  1.00 33.81           N  
ANISOU 5379  N   LEU C 698     4106   4993   3748    292     51    208       N  
ATOM   5380  CA  LEU C 698     -75.180  30.057 -50.260  1.00 33.98           C  
ANISOU 5380  CA  LEU C 698     4117   5000   3793    259     37    198       C  
ATOM   5381  C   LEU C 698     -76.093  28.855 -50.441  1.00 34.11           C  
ANISOU 5381  C   LEU C 698     4118   5062   3778    221     -5    141       C  
ATOM   5382  O   LEU C 698     -76.374  28.124 -49.490  1.00 34.61           O  
ANISOU 5382  O   LEU C 698     4194   5085   3870    171    -19    105       O  
ATOM   5383  CB  LEU C 698     -76.008  31.339 -50.245  1.00 33.93           C  
ANISOU 5383  CB  LEU C 698     4087   5023   3782    300     59    256       C  
ATOM   5384  CG  LEU C 698     -76.706  31.740 -48.960  1.00 36.96           C  
ANISOU 5384  CG  LEU C 698     4469   5369   4206    281     64    267       C  
ATOM   5385  CD1 LEU C 698     -75.860  31.663 -47.704  1.00 36.18           C  
ANISOU 5385  CD1 LEU C 698     4405   5173   4169    244     76    254       C  
ATOM   5386  CD2 LEU C 698     -77.283  33.143 -49.120  1.00 39.54           C  
ANISOU 5386  CD2 LEU C 698     4781   5718   4524    338     97    333       C  
ATOM   5387  N   GLY C 699     -76.577  28.650 -51.651  1.00 35.83           N  
ANISOU 5387  N   GLY C 699     4311   5368   3936    241    -22    131       N  
ATOM   5388  CA  GLY C 699     -77.537  27.556 -51.919  1.00 39.84           C  
ANISOU 5388  CA  GLY C 699     4798   5931   4408    198    -61     71       C  
ATOM   5389  C   GLY C 699     -76.958  26.153 -51.776  1.00 40.39           C  
ANISOU 5389  C   GLY C 699     4908   5950   4487    146    -77      4       C  
ATOM   5390  O   GLY C 699     -77.710  25.193 -51.658  1.00 46.06           O  
ANISOU 5390  O   GLY C 699     5621   6684   5193     93   -102    -49       O  
ATOM   5391  N   LYS C 700     -75.637  26.025 -51.797  1.00 37.99           N  
ANISOU 5391  N   LYS C 700     4644   5587   4202    161    -59      8       N  
ATOM   5392  CA  LYS C 700     -74.985  24.717 -51.801  1.00 39.11           C  
ANISOU 5392  CA  LYS C 700     4830   5686   4346    128    -68    -50       C  
ATOM   5393  C   LYS C 700     -74.568  24.251 -50.407  1.00 39.24           C  
ANISOU 5393  C   LYS C 700     4883   5605   4420     93    -59    -62       C  
ATOM   5394  O   LYS C 700     -74.227  23.099 -50.220  1.00 38.60           O  
ANISOU 5394  O   LYS C 700     4841   5481   4342     64    -65   -109       O  
ATOM   5395  CB  LYS C 700     -73.755  24.754 -52.726  1.00 40.67           C  
ANISOU 5395  CB  LYS C 700     5046   5886   4521    173    -54    -41       C  
ATOM   5396  N   LEU C 701     -74.543  25.165 -49.438  1.00 43.51           N  
ANISOU 5396  N   LEU C 701     5415   6111   5005    101    -43    -17       N  
ATOM   5397  CA  LEU C 701     -74.286  24.809 -48.033  1.00 41.83           C  
ANISOU 5397  CA  LEU C 701     5232   5818   4844     71    -36    -25       C  
ATOM   5398  C   LEU C 701     -75.165  23.669 -47.577  1.00 38.59           C  
ANISOU 5398  C   LEU C 701     4835   5396   4434     14    -54    -75       C  
ATOM   5399  O   LEU C 701     -76.380  23.754 -47.710  1.00 36.62           O  
ANISOU 5399  O   LEU C 701     4550   5196   4167     -8    -68    -81       O  
ATOM   5400  CB  LEU C 701     -74.569  26.016 -47.122  1.00 43.04           C  
ANISOU 5400  CB  LEU C 701     5365   5955   5035     81    -20     24       C  
ATOM   5401  CG  LEU C 701     -73.537  27.147 -47.138  1.00 46.02           C  
ANISOU 5401  CG  LEU C 701     5742   6313   5431    123      8     72       C  
ATOM   5402  CD1 LEU C 701     -73.944  28.237 -46.151  1.00 48.43           C  
ANISOU 5402  CD1 LEU C 701     6034   6593   5772    125     25    111       C  
ATOM   5403  CD2 LEU C 701     -72.162  26.612 -46.788  1.00 46.12           C  
ANISOU 5403  CD2 LEU C 701     5788   6272   5463    123     16     56       C  
ATOM   5404  N   SER C 702     -74.570  22.622 -47.007  1.00 37.96           N  
ANISOU 5404  N   SER C 702     4802   5248   4371     -7    -50   -108       N  
ATOM   5405  CA  SER C 702     -75.350  21.452 -46.581  1.00 38.43           C  
ANISOU 5405  CA  SER C 702     4885   5284   4432    -65    -59   -157       C  
ATOM   5406  C   SER C 702     -75.041  21.043 -45.139  1.00 37.03           C  
ANISOU 5406  C   SER C 702     4746   5023   4300    -81    -44   -154       C  
ATOM   5407  O   SER C 702     -73.917  21.103 -44.691  1.00 34.28           O  
ANISOU 5407  O   SER C 702     4424   4630   3971    -49    -31   -138       O  
ATOM   5408  CB  SER C 702     -75.094  20.285 -47.539  1.00 39.57           C  
ANISOU 5408  CB  SER C 702     5063   5432   4539    -79    -66   -212       C  
ATOM   5409  OG  SER C 702     -74.254  19.299 -46.978  1.00 41.53           O  
ANISOU 5409  OG  SER C 702     5375   5599   4805    -81    -50   -234       O  
ATOM   5410  N   LYS C 703     -76.062  20.593 -44.432  1.00 39.89           N  
ANISOU 5410  N   LYS C 703     5109   5372   4676   -130    -47   -171       N  
ATOM   5411  CA  LYS C 703     -75.925  20.141 -43.050  1.00 38.42           C  
ANISOU 5411  CA  LYS C 703     4959   5111   4528   -146    -31   -168       C  
ATOM   5412  C   LYS C 703     -74.944  18.991 -42.917  1.00 35.52           C  
ANISOU 5412  C   LYS C 703     4658   4676   4160   -139    -17   -196       C  
ATOM   5413  O   LYS C 703     -74.175  18.938 -41.963  1.00 32.43           O  
ANISOU 5413  O   LYS C 703     4296   4232   3794   -114     -2   -177       O  
ATOM   5414  CB  LYS C 703     -77.278  19.712 -42.506  1.00 45.07           C  
ANISOU 5414  CB  LYS C 703     5790   5955   5378   -206    -33   -187       C  
ATOM   5415  CG  LYS C 703     -78.237  20.857 -42.235  1.00 50.83           C  
ANISOU 5415  CG  LYS C 703     6458   6741   6114   -205    -41   -151       C  
ATOM   5416  CD  LYS C 703     -79.507  20.402 -41.543  1.00 58.20           C  
ANISOU 5416  CD  LYS C 703     7378   7676   7058   -264    -39   -167       C  
ATOM   5417  CE  LYS C 703     -80.442  19.629 -42.463  1.00 64.21           C  
ANISOU 5417  CE  LYS C 703     8120   8489   7785   -320    -54   -218       C  
ATOM   5418  NZ  LYS C 703     -80.874  20.454 -43.632  1.00 69.45           N  
ANISOU 5418  NZ  LYS C 703     8721   9256   8410   -296    -77   -209       N  
ATOM   5419  N   ARG C 704     -74.952  18.083 -43.891  1.00 34.05           N  
ANISOU 5419  N   ARG C 704     4498   4497   3944   -156    -20   -241       N  
ATOM   5420  CA  ARG C 704     -74.112  16.893 -43.820  1.00 32.66           C  
ANISOU 5420  CA  ARG C 704     4394   4253   3764   -147     -2   -270       C  
ATOM   5421  C   ARG C 704     -72.643  17.230 -44.135  1.00 32.32           C  
ANISOU 5421  C   ARG C 704     4359   4208   3712    -77      3   -245       C  
ATOM   5422  O   ARG C 704     -71.734  16.647 -43.543  1.00 32.09           O  
ANISOU 5422  O   ARG C 704     4377   4122   3693    -47     22   -243       O  
ATOM   5423  CB  ARG C 704     -74.683  15.743 -44.678  1.00 31.68           C  
ANISOU 5423  CB  ARG C 704     4302   4126   3609   -196     -3   -333       C  
ATOM   5424  N   GLN C 705     -72.397  18.178 -45.037  1.00 31.16           N  
ANISOU 5424  N   GLN C 705     4165   4127   3548    -48    -10   -225       N  
ATOM   5425  CA  GLN C 705     -71.048  18.634 -45.286  1.00 31.88           C  
ANISOU 5425  CA  GLN C 705     4254   4224   3636     12     -2   -198       C  
ATOM   5426  C   GLN C 705     -70.474  19.335 -44.046  1.00 28.35           C  
ANISOU 5426  C   GLN C 705     3794   3749   3226     34      7   -156       C  
ATOM   5427  O   GLN C 705     -69.323  19.119 -43.670  1.00 27.30           O  
ANISOU 5427  O   GLN C 705     3684   3591   3098     73     19   -148       O  
ATOM   5428  CB  GLN C 705     -70.969  19.556 -46.522  1.00 36.33           C  
ANISOU 5428  CB  GLN C 705     4769   4862   4172     36    -13   -181       C  
ATOM   5429  CG  GLN C 705     -71.229  18.850 -47.870  1.00 46.16           C  
ANISOU 5429  CG  GLN C 705     6027   6143   5370     28    -22   -225       C  
ATOM   5430  CD  GLN C 705     -70.329  17.614 -48.154  1.00 49.19           C  
ANISOU 5430  CD  GLN C 705     6475   6481   5734     48     -9   -262       C  
ATOM   5431  OE1 GLN C 705     -70.682  16.452 -47.852  1.00 50.37           O  
ANISOU 5431  OE1 GLN C 705     6677   6578   5883     14     -2   -304       O  
ATOM   5432  NE2 GLN C 705     -69.158  17.877 -48.709  1.00 52.75           N  
ANISOU 5432  NE2 GLN C 705     6924   6949   6170    103      0   -243       N  
ATOM   5433  N   ILE C 706     -71.269  20.168 -43.413  1.00 25.70           N  
ANISOU 5433  N   ILE C 706     3424   3426   2915     12      1   -133       N  
ATOM   5434  CA  ILE C 706     -70.803  20.915 -42.239  1.00 24.64           C  
ANISOU 5434  CA  ILE C 706     3276   3270   2814     28      9    -98       C  
ATOM   5435  C   ILE C 706     -70.492  19.957 -41.106  1.00 25.39           C  
ANISOU 5435  C   ILE C 706     3420   3303   2923     28     20   -109       C  
ATOM   5436  O   ILE C 706     -69.470  20.085 -40.463  1.00 25.52           O  
ANISOU 5436  O   ILE C 706     3443   3305   2950     62     28    -94       O  
ATOM   5437  CB  ILE C 706     -71.813  22.013 -41.838  1.00 24.06           C  
ANISOU 5437  CB  ILE C 706     3159   3221   2760      7      4    -71       C  
ATOM   5438  CG1 ILE C 706     -71.769  23.148 -42.888  1.00 23.91           C  
ANISOU 5438  CG1 ILE C 706     3097   3261   2728     29      1    -46       C  
ATOM   5439  CG2 ILE C 706     -71.490  22.594 -40.464  1.00 24.29           C  
ANISOU 5439  CG2 ILE C 706     3187   3219   2824     15     13    -46       C  
ATOM   5440  CD1 ILE C 706     -72.964  24.077 -42.869  1.00 24.31           C  
ANISOU 5440  CD1 ILE C 706     3108   3346   2784     14     -3    -23       C  
ATOM   5441  N   GLN C 707     -71.362  18.969 -40.901  1.00 26.66           N  
ANISOU 5441  N   GLN C 707     3615   3432   3082    -10     23   -138       N  
ATOM   5442  CA  GLN C 707     -71.133  17.954 -39.916  1.00 28.58           C  
ANISOU 5442  CA  GLN C 707     3913   3611   3335     -8     40   -147       C  
ATOM   5443  C   GLN C 707     -69.823  17.232 -40.163  1.00 26.00           C  
ANISOU 5443  C   GLN C 707     3627   3262   2988     42     52   -155       C  
ATOM   5444  O   GLN C 707     -69.061  16.981 -39.221  1.00 26.76           O  
ANISOU 5444  O   GLN C 707     3747   3328   3092     78     65   -140       O  
ATOM   5445  CB  GLN C 707     -72.292  16.984 -39.903  1.00 32.28           C  
ANISOU 5445  CB  GLN C 707     4413   4049   3801    -65     46   -181       C  
ATOM   5446  CG  GLN C 707     -72.134  15.774 -38.991  1.00 37.04           C  
ANISOU 5446  CG  GLN C 707     5087   4575   4411    -65     72   -191       C  
ATOM   5447  CD  GLN C 707     -73.161  14.681 -39.291  1.00 44.92           C  
ANISOU 5447  CD  GLN C 707     6124   5538   5403   -129     84   -234       C  
ATOM   5448  OE1 GLN C 707     -73.182  14.116 -40.386  1.00 49.46           O  
ANISOU 5448  OE1 GLN C 707     6719   6121   5955   -144     83   -272       O  
ATOM   5449  NE2 GLN C 707     -73.988  14.369 -38.329  1.00 48.18           N  
ANISOU 5449  NE2 GLN C 707     6552   5916   5838   -168     99   -231       N  
ATOM   5450  N   ALA C 708     -69.543  16.916 -41.416  1.00 24.35           N  
ANISOU 5450  N   ALA C 708     3426   3075   2752     51     49   -177       N  
ATOM   5451  CA  ALA C 708     -68.305  16.229 -41.772  1.00 24.85           C  
ANISOU 5451  CA  ALA C 708     3527   3122   2792    105     63   -185       C  
ATOM   5452  C   ALA C 708     -67.097  17.140 -41.523  1.00 24.21           C  
ANISOU 5452  C   ALA C 708     3405   3079   2717    157     61   -149       C  
ATOM   5453  O   ALA C 708     -66.017  16.684 -41.144  1.00 24.68           O  
ANISOU 5453  O   ALA C 708     3487   3123   2766    207     74   -142       O  
ATOM   5454  CB  ALA C 708     -68.327  15.758 -43.238  1.00 24.34           C  
ANISOU 5454  CB  ALA C 708     3476   3079   2693    102     60   -219       C  
ATOM   5455  N   ALA C 709     -67.280  18.417 -41.779  1.00 23.37           N  
ANISOU 5455  N   ALA C 709     3236   3021   2622    144     46   -126       N  
ATOM   5456  CA  ALA C 709     -66.232  19.400 -41.520  1.00 23.20           C  
ANISOU 5456  CA  ALA C 709     3172   3033   2610    178     47    -95       C  
ATOM   5457  C   ALA C 709     -65.908  19.479 -40.010  1.00 22.78           C  
ANISOU 5457  C   ALA C 709     3121   2954   2578    188     51    -80       C  
ATOM   5458  O   ALA C 709     -64.744  19.587 -39.626  1.00 21.64           O  
ANISOU 5458  O   ALA C 709     2967   2826   2431    229     56    -68       O  
ATOM   5459  CB  ALA C 709     -66.647  20.772 -42.066  1.00 22.33           C  
ANISOU 5459  CB  ALA C 709     3004   2969   2510    158     38    -74       C  
ATOM   5460  N   TYR C 710     -66.936  19.449 -39.168  1.00 22.29           N  
ANISOU 5460  N   TYR C 710     3069   2862   2537    152     49    -80       N  
ATOM   5461  CA  TYR C 710     -66.717  19.399 -37.719  1.00 21.63           C  
ANISOU 5461  CA  TYR C 710     2995   2755   2469    164     54    -67       C  
ATOM   5462  C   TYR C 710     -65.855  18.217 -37.345  1.00 23.22           C  
ANISOU 5462  C   TYR C 710     3246   2928   2650    212     68    -74       C  
ATOM   5463  O   TYR C 710     -64.867  18.351 -36.596  1.00 23.83           O  
ANISOU 5463  O   TYR C 710     3312   3021   2723    253     71    -60       O  
ATOM   5464  CB  TYR C 710     -68.029  19.297 -36.973  1.00 21.86           C  
ANISOU 5464  CB  TYR C 710     3037   2751   2517    120     54    -68       C  
ATOM   5465  CG  TYR C 710     -68.762  20.597 -36.727  1.00 20.88           C  
ANISOU 5465  CG  TYR C 710     2864   2653   2418     88     43    -50       C  
ATOM   5466  CD1 TYR C 710     -68.156  21.652 -36.034  1.00 20.47           C  
ANISOU 5466  CD1 TYR C 710     2776   2621   2381    103     41    -30       C  
ATOM   5467  CD2 TYR C 710     -70.078  20.747 -37.122  1.00 20.72           C  
ANISOU 5467  CD2 TYR C 710     2833   2636   2403     45     38    -55       C  
ATOM   5468  CE1 TYR C 710     -68.854  22.810 -35.776  1.00 20.44           C  
ANISOU 5468  CE1 TYR C 710     2737   2631   2398     77     37    -14       C  
ATOM   5469  CE2 TYR C 710     -70.775  21.926 -36.905  1.00 20.64           C  
ANISOU 5469  CE2 TYR C 710     2780   2649   2411     25     32    -35       C  
ATOM   5470  CZ  TYR C 710     -70.166  22.947 -36.241  1.00 21.13           C  
ANISOU 5470  CZ  TYR C 710     2818   2722   2490     43     34    -14       C  
ATOM   5471  OH  TYR C 710     -70.896  24.080 -35.978  1.00 23.62           O  
ANISOU 5471  OH  TYR C 710     3100   3051   2823     26     33      5       O  
ATOM   5472  N   SER C 711     -66.192  17.052 -37.876  1.00 24.07           N  
ANISOU 5472  N   SER C 711     3410   2997   2741    209     80    -97       N  
ATOM   5473  CA  SER C 711     -65.418  15.850 -37.593  1.00 26.29           C  
ANISOU 5473  CA  SER C 711     3750   3242   2999    261    101   -102       C  
ATOM   5474  C   SER C 711     -63.979  15.966 -37.980  1.00 25.42           C  
ANISOU 5474  C   SER C 711     3619   3175   2865    324    102    -94       C  
ATOM   5475  O   SER C 711     -63.115  15.578 -37.211  1.00 30.00           O  
ANISOU 5475  O   SER C 711     4212   3754   3431    378    113    -80       O  
ATOM   5476  CB  SER C 711     -65.989  14.620 -38.306  1.00 27.28           C  
ANISOU 5476  CB  SER C 711     3943   3314   3109    243    119   -135       C  
ATOM   5477  OG  SER C 711     -67.267  14.362 -37.814  1.00 30.93           O  
ANISOU 5477  OG  SER C 711     4426   3736   3592    184    123   -144       O  
ATOM   5478  N   ILE C 712     -63.721  16.478 -39.160  1.00 24.32           N  
ANISOU 5478  N   ILE C 712     3446   3078   2718    319     93    -99       N  
ATOM   5479  CA  ILE C 712     -62.352  16.635 -39.606  1.00 25.47           C  
ANISOU 5479  CA  ILE C 712     3566   3272   2841    376     96    -90       C  
ATOM   5480  C   ILE C 712     -61.592  17.556 -38.666  1.00 24.54           C  
ANISOU 5480  C   ILE C 712     3391   3198   2735    392     87    -66       C  
ATOM   5481  O   ILE C 712     -60.464  17.280 -38.330  1.00 22.83           O  
ANISOU 5481  O   ILE C 712     3169   3009   2499    448     94    -57       O  
ATOM   5482  CB  ILE C 712     -62.293  17.183 -41.056  1.00 26.37           C  
ANISOU 5482  CB  ILE C 712     3648   3428   2946    362     89    -97       C  
ATOM   5483  CG1 ILE C 712     -62.752  16.126 -42.052  1.00 28.13           C  
ANISOU 5483  CG1 ILE C 712     3928   3616   3143    360     98   -128       C  
ATOM   5484  CG2 ILE C 712     -60.904  17.655 -41.419  1.00 26.17           C  
ANISOU 5484  CG2 ILE C 712     3577   3462   2903    410     92    -81       C  
ATOM   5485  CD1 ILE C 712     -61.940  14.845 -42.142  1.00 29.63           C  
ANISOU 5485  CD1 ILE C 712     4180   3777   3300    421    121   -140       C  
ATOM   5486  N   LEU C 713     -62.218  18.659 -38.257  1.00 24.52           N  
ANISOU 5486  N   LEU C 713     3345   3206   2764    342     73    -56       N  
ATOM   5487  CA  LEU C 713     -61.589  19.550 -37.296  1.00 24.08           C  
ANISOU 5487  CA  LEU C 713     3241   3188   2722    347     66    -40       C  
ATOM   5488  C   LEU C 713     -61.254  18.827 -35.983  1.00 25.33           C  
ANISOU 5488  C   LEU C 713     3427   3330   2869    386     71    -36       C  
ATOM   5489  O   LEU C 713     -60.231  19.117 -35.351  1.00 23.86           O  
ANISOU 5489  O   LEU C 713     3205   3190   2672    420     68    -29       O  
ATOM   5490  CB  LEU C 713     -62.452  20.798 -37.059  1.00 22.93           C  
ANISOU 5490  CB  LEU C 713     3058   3044   2611    288     56    -33       C  
ATOM   5491  CG  LEU C 713     -62.557  21.794 -38.203  1.00 22.39           C  
ANISOU 5491  CG  LEU C 713     2950   3005   2552    260     55    -27       C  
ATOM   5492  CD1 LEU C 713     -63.454  22.989 -37.840  1.00 24.04           C  
ANISOU 5492  CD1 LEU C 713     3131   3208   2794    211     50    -16       C  
ATOM   5493  CD2 LEU C 713     -61.194  22.259 -38.597  1.00 22.86           C  
ANISOU 5493  CD2 LEU C 713     2967   3118   2600    287     60    -21       C  
ATOM   5494  N   SER C 714     -62.122  17.898 -35.577  1.00 26.21           N  
ANISOU 5494  N   SER C 714     3599   3378   2980    381     81    -41       N  
ATOM   5495  CA  SER C 714     -61.882  17.099 -34.375  1.00 26.95           C  
ANISOU 5495  CA  SER C 714     3731   3449   3060    424     92    -33       C  
ATOM   5496  C   SER C 714     -60.702  16.160 -34.583  1.00 28.66           C  
ANISOU 5496  C   SER C 714     3974   3680   3237    503    107    -30       C  
ATOM   5497  O   SER C 714     -59.877  16.010 -33.678  1.00 30.73           O  
ANISOU 5497  O   SER C 714     4225   3973   3478    558    109    -16       O  
ATOM   5498  CB  SER C 714     -63.104  16.258 -33.982  1.00 26.36           C  
ANISOU 5498  CB  SER C 714     3723   3297   2995    396    107    -37       C  
ATOM   5499  OG  SER C 714     -64.038  17.069 -33.343  1.00 25.89           O  
ANISOU 5499  OG  SER C 714     3638   3234   2967    343     94    -32       O  
ATOM   5500  N   GLU C 715     -60.620  15.542 -35.751  1.00 26.94           N  
ANISOU 5500  N   GLU C 715     3788   3445   3004    513    119    -43       N  
ATOM   5501  CA  GLU C 715     -59.492  14.696 -36.070  1.00 30.21           C  
ANISOU 5501  CA  GLU C 715     4227   3874   3379    593    136    -40       C  
ATOM   5502  C   GLU C 715     -58.196  15.492 -36.100  1.00 29.04           C  
ANISOU 5502  C   GLU C 715     3999   3818   3215    628    123    -29       C  
ATOM   5503  O   GLU C 715     -57.180  15.022 -35.649  1.00 28.51           O  
ANISOU 5503  O   GLU C 715     3930   3786   3115    702    132    -17       O  
ATOM   5504  CB  GLU C 715     -59.682  13.967 -37.399  1.00 32.80           C  
ANISOU 5504  CB  GLU C 715     4604   4168   3693    593    151    -61       C  
ATOM   5505  CG  GLU C 715     -60.809  12.943 -37.369  1.00 38.69           C  
ANISOU 5505  CG  GLU C 715     5436   4820   4445    563    171    -79       C  
ATOM   5506  CD  GLU C 715     -60.872  12.119 -38.663  1.00 43.06           C  
ANISOU 5506  CD  GLU C 715     6043   5341   4978    567    188   -107       C  
ATOM   5507  OE1 GLU C 715     -61.978  11.986 -39.257  1.00 49.07           O  
ANISOU 5507  OE1 GLU C 715     6827   6063   5754    499    186   -134       O  
ATOM   5508  OE2 GLU C 715     -59.790  11.652 -39.102  1.00 45.08           O  
ANISOU 5508  OE2 GLU C 715     6310   5618   5199    639    202   -103       O  
ATOM   5509  N   VAL C 716     -58.239  16.693 -36.637  1.00 29.09           N  
ANISOU 5509  N   VAL C 716     3939   3867   3245    576    104    -32       N  
ATOM   5510  CA  VAL C 716     -57.078  17.558 -36.617  1.00 32.62           C  
ANISOU 5510  CA  VAL C 716     4308   4401   3686    593     94    -24       C  
ATOM   5511  C   VAL C 716     -56.586  17.763 -35.184  1.00 32.86           C  
ANISOU 5511  C   VAL C 716     4309   4468   3710    616     86    -15       C  
ATOM   5512  O   VAL C 716     -55.392  17.639 -34.910  1.00 33.66           O  
ANISOU 5512  O   VAL C 716     4375   4636   3780    674     87     -9       O  
ATOM   5513  CB  VAL C 716     -57.380  18.943 -37.256  1.00 33.17           C  
ANISOU 5513  CB  VAL C 716     4318   4496   3789    521     82    -26       C  
ATOM   5514  CG1 VAL C 716     -56.283  19.938 -36.952  1.00 35.55           C  
ANISOU 5514  CG1 VAL C 716     4538   4879   4091    521     75    -21       C  
ATOM   5515  CG2 VAL C 716     -57.562  18.790 -38.750  1.00 35.08           C  
ANISOU 5515  CG2 VAL C 716     4576   4729   4025    514     90    -33       C  
ATOM   5516  N   GLN C 717     -57.502  18.130 -34.292  1.00 35.51           N  
ANISOU 5516  N   GLN C 717     4652   4767   4072    572     77    -15       N  
ATOM   5517  CA  GLN C 717     -57.162  18.429 -32.882  1.00 35.71           C  
ANISOU 5517  CA  GLN C 717     4649   4828   4091    587     66    -10       C  
ATOM   5518  C   GLN C 717     -56.566  17.189 -32.256  1.00 35.63           C  
ANISOU 5518  C   GLN C 717     4681   4820   4036    677     80      3       C  
ATOM   5519  O   GLN C 717     -55.545  17.266 -31.594  1.00 39.18           O  
ANISOU 5519  O   GLN C 717     5088   5343   4456    726     74      8       O  
ATOM   5520  CB  GLN C 717     -58.400  18.899 -32.125  1.00 40.58           C  
ANISOU 5520  CB  GLN C 717     5281   5395   4743    527     59    -11       C  
ATOM   5521  CG  GLN C 717     -58.184  19.240 -30.651  1.00 50.34           C  
ANISOU 5521  CG  GLN C 717     6491   6664   5971    539     47     -8       C  
ATOM   5522  CD  GLN C 717     -59.417  18.926 -29.760  1.00 57.40           C  
ANISOU 5522  CD  GLN C 717     7438   7489   6880    518     52     -2       C  
ATOM   5523  OE1 GLN C 717     -60.200  17.975 -30.011  1.00 54.62           O  
ANISOU 5523  OE1 GLN C 717     7156   7066   6531    522     70      4       O  
ATOM   5524  NE2 GLN C 717     -59.608  19.751 -28.722  1.00 61.85           N  
ANISOU 5524  NE2 GLN C 717     7969   8075   7455    492     39     -5       N  
ATOM   5525  N   GLN C 718     -57.143  16.032 -32.530  1.00 36.67           N  
ANISOU 5525  N   GLN C 718     4897   4875   4160    701    103      7       N  
ATOM   5526  CA  GLN C 718     -56.560  14.766 -32.061  1.00 39.60           C  
ANISOU 5526  CA  GLN C 718     5323   5236   4486    796    126     23       C  
ATOM   5527  C   GLN C 718     -55.166  14.477 -32.597  1.00 42.00           C  
ANISOU 5527  C   GLN C 718     5598   5613   4749    873    132     29       C  
ATOM   5528  O   GLN C 718     -54.288  14.048 -31.848  1.00 39.16           O  
ANISOU 5528  O   GLN C 718     5228   5304   4346    955    137     45       O  
ATOM   5529  CB  GLN C 718     -57.455  13.578 -32.373  1.00 42.28           C  
ANISOU 5529  CB  GLN C 718     5767   5469   4829    798    157     23       C  
ATOM   5530  CG  GLN C 718     -58.706  13.557 -31.545  1.00 47.58           C  
ANISOU 5530  CG  GLN C 718     6475   6073   5529    746    160     25       C  
ATOM   5531  CD  GLN C 718     -59.659  12.508 -32.076  1.00 54.04           C  
ANISOU 5531  CD  GLN C 718     7387   6788   6357    725    190     15       C  
ATOM   5532  OE1 GLN C 718     -60.845  12.793 -32.280  1.00 54.63           O  
ANISOU 5532  OE1 GLN C 718     7471   6818   6469    642    184      1       O  
ATOM   5533  NE2 GLN C 718     -59.141  11.291 -32.336  1.00 51.26           N  
ANISOU 5533  NE2 GLN C 718     7105   6400   5970    798    224     21       N  
ATOM   5534  N   ALA C 719     -54.981  14.659 -33.899  1.00 41.72           N  
ANISOU 5534  N   ALA C 719     5548   5584   4719    853    133     17       N  
ATOM   5535  CA  ALA C 719     -53.684  14.430 -34.509  1.00 43.07           C  
ANISOU 5535  CA  ALA C 719     5686   5826   4850    923    140     22       C  
ATOM   5536  C   ALA C 719     -52.634  15.357 -33.945  1.00 41.37           C  
ANISOU 5536  C   ALA C 719     5368   5728   4624    931    118     25       C  
ATOM   5537  O   ALA C 719     -51.517  14.952 -33.677  1.00 45.95           O  
ANISOU 5537  O   ALA C 719     5921   6380   5158   1015    123     37       O  
ATOM   5538  CB  ALA C 719     -53.760  14.612 -36.009  1.00 44.82           C  
ANISOU 5538  CB  ALA C 719     5907   6039   5085    889    144      8       C  
ATOM   5539  N   VAL C 720     -52.979  16.604 -33.765  1.00 44.35           N  
ANISOU 5539  N   VAL C 720     5685   6126   5040    846     94     13       N  
ATOM   5540  CA  VAL C 720     -52.040  17.493 -33.160  1.00 47.76           C  
ANISOU 5540  CA  VAL C 720     6022   6662   5463    842     75      8       C  
ATOM   5541  C   VAL C 720     -51.668  16.931 -31.768  1.00 52.68           C  
ANISOU 5541  C   VAL C 720     6650   7319   6047    912     71     20       C  
ATOM   5542  O   VAL C 720     -50.488  16.705 -31.494  1.00 53.32           O  
ANISOU 5542  O   VAL C 720     6684   7494   6082    984     70     26       O  
ATOM   5543  CB  VAL C 720     -52.604  18.909 -33.047  1.00 46.57           C  
ANISOU 5543  CB  VAL C 720     5821   6509   5362    736     56     -8       C  
ATOM   5544  CG1 VAL C 720     -51.722  19.757 -32.140  1.00 48.55           C  
ANISOU 5544  CG1 VAL C 720     5983   6861   5602    727     37    -20       C  
ATOM   5545  CG2 VAL C 720     -52.706  19.533 -34.427  1.00 48.48           C  
ANISOU 5545  CG2 VAL C 720     6045   6742   5632    683     62    -14       C  
ATOM   5546  N   SER C 721     -52.670  16.685 -30.912  1.00 50.78           N  
ANISOU 5546  N   SER C 721     6465   7007   5821    896     71     24       N  
ATOM   5547  CA  SER C 721     -52.432  16.159 -29.553  1.00 47.54           C  
ANISOU 5547  CA  SER C 721     6067   6624   5373    964     71     39       C  
ATOM   5548  C   SER C 721     -51.683  14.820 -29.526  1.00 50.08           C  
ANISOU 5548  C   SER C 721     6435   6959   5636   1087     97     64       C  
ATOM   5549  O   SER C 721     -50.818  14.620 -28.699  1.00 48.37           O  
ANISOU 5549  O   SER C 721     6182   6827   5370   1163     91     76       O  
ATOM   5550  CB  SER C 721     -53.755  16.013 -28.807  1.00 47.99           C  
ANISOU 5550  CB  SER C 721     6189   6587   5458    925     75     43       C  
ATOM   5551  OG  SER C 721     -54.316  17.309 -28.576  1.00 53.14           O  
ANISOU 5551  OG  SER C 721     6791   7244   6155    827     50     22       O  
ATOM   5552  N   GLN C 722     -52.009  13.926 -30.454  1.00 51.53           N  
ANISOU 5552  N   GLN C 722     6697   7061   5820   1110    126     72       N  
ATOM   5553  CA  GLN C 722     -51.454  12.582 -30.510  1.00 54.05           C  
ANISOU 5553  CA  GLN C 722     7081   7366   6087   1226    160     96       C  
ATOM   5554  C   GLN C 722     -50.006  12.646 -30.956  1.00 58.14           C  
ANISOU 5554  C   GLN C 722     7527   8002   6561   1296    156    100       C  
ATOM   5555  O   GLN C 722     -49.265  11.696 -30.754  1.00 55.23           O  
ANISOU 5555  O   GLN C 722     7187   7661   6137   1411    179    125       O  
ATOM   5556  CB  GLN C 722     -52.267  11.737 -31.492  1.00 53.59           C  
ANISOU 5556  CB  GLN C 722     7126   7184   6050   1211    192     92       C  
ATOM   5557  CG  GLN C 722     -51.763  10.311 -31.757  1.00 58.03           C  
ANISOU 5557  CG  GLN C 722     7774   7711   6563   1326    236    114       C  
ATOM   5558  CD  GLN C 722     -52.062   9.306 -30.640  1.00 62.10           C  
ANISOU 5558  CD  GLN C 722     8375   8168   7053   1397    267    143       C  
ATOM   5559  OE1 GLN C 722     -52.839   9.557 -29.708  1.00 61.24           O  
ANISOU 5559  OE1 GLN C 722     8276   8026   6966   1352    259    146       O  
ATOM   5560  NE2 GLN C 722     -51.434   8.146 -30.745  1.00 62.46           N  
ANISOU 5560  NE2 GLN C 722     8488   8197   7048   1512    308    166       N  
ATOM   5561  N   GLY C 723     -49.621  13.764 -31.576  1.00 63.96           N  
ANISOU 5561  N   GLY C 723     8172   8808   7323   1227    130     78       N  
ATOM   5562  CA  GLY C 723     -48.269  13.963 -32.108  1.00 65.57           C  
ANISOU 5562  CA  GLY C 723     8294   9130   7490   1275    127     79       C  
ATOM   5563  C   GLY C 723     -48.072  13.195 -33.394  1.00 67.18           C  
ANISOU 5563  C   GLY C 723     8551   9293   7680   1319    157     85       C  
ATOM   5564  O   GLY C 723     -47.096  12.470 -33.560  1.00 63.79           O  
ANISOU 5564  O   GLY C 723     8121   8920   7197   1425    176    103       O  
ATOM   5565  N   SER C 724     -49.026  13.341 -34.306  1.00 74.30           N  
ANISOU 5565  N   SER C 724     9501  10099   8629   1241    162     69       N  
ATOM   5566  CA  SER C 724     -48.970  12.648 -35.590  1.00 68.92           C  
ANISOU 5566  CA  SER C 724     8876   9373   7938   1271    189     68       C  
ATOM   5567  C   SER C 724     -48.016  13.377 -36.523  1.00 64.05           C  
ANISOU 5567  C   SER C 724     8167   8854   7314   1262    182     61       C  
ATOM   5568  O   SER C 724     -47.629  14.535 -36.281  1.00 56.55           O  
ANISOU 5568  O   SER C 724     7116   7986   6382   1205    156     53       O  
ATOM   5569  CB  SER C 724     -50.365  12.585 -36.217  1.00 66.39           C  
ANISOU 5569  CB  SER C 724     8631   8928   7665   1186    194     49       C  
ATOM   5570  OG  SER C 724     -51.245  11.840 -35.400  1.00 65.96           O  
ANISOU 5570  OG  SER C 724     8664   8780   7617   1193    208     55       O  
ATOM   5571  N   SER C 725     -47.650  12.686 -37.592  1.00 62.45           N  
ANISOU 5571  N   SER C 725     8004   8639   7086   1316    208     64       N  
ATOM   5572  CA  SER C 725     -46.778  13.243 -38.610  1.00 65.82           C  
ANISOU 5572  CA  SER C 725     8355   9151   7503   1315    208     62       C  
ATOM   5573  C   SER C 725     -47.284  14.612 -39.072  1.00 66.76           C  
ANISOU 5573  C   SER C 725     8413   9274   7679   1188    185     44       C  
ATOM   5574  O   SER C 725     -48.485  14.889 -39.022  1.00 66.97           O  
ANISOU 5574  O   SER C 725     8482   9212   7750   1110    175     32       O  
ATOM   5575  CB  SER C 725     -46.710  12.284 -39.800  1.00 67.95           C  
ANISOU 5575  CB  SER C 725     8700   9371   7746   1373    241     61       C  
ATOM   5576  OG  SER C 725     -48.013  11.887 -40.220  1.00 65.14           O  
ANISOU 5576  OG  SER C 725     8443   8885   7421   1319    248     43       O  
ATOM   5577  N   ASP C 726     -46.366  15.464 -39.515  1.00 64.13           N  
ANISOU 5577  N   ASP C 726     7980   9043   7343   1171    179     45       N  
ATOM   5578  CA  ASP C 726     -46.748  16.700 -40.199  1.00 65.19           C  
ANISOU 5578  CA  ASP C 726     8067   9176   7526   1064    169     33       C  
ATOM   5579  C   ASP C 726     -47.472  16.383 -41.489  1.00 57.06           C  
ANISOU 5579  C   ASP C 726     7107   8068   6507   1047    185     28       C  
ATOM   5580  O   ASP C 726     -48.315  17.133 -41.930  1.00 58.52           O  
ANISOU 5580  O   ASP C 726     7294   8206   6734    962    177     19       O  
ATOM   5581  CB  ASP C 726     -45.528  17.573 -40.450  1.00 68.49           C  
ANISOU 5581  CB  ASP C 726     8369   9720   7935   1054    170     36       C  
ATOM   5582  CG  ASP C 726     -44.972  18.135 -39.158  1.00 72.88           C  
ANISOU 5582  CG  ASP C 726     8846  10357   8489   1040    148     31       C  
ATOM   5583  OD1 ASP C 726     -45.275  17.559 -38.090  1.00 78.36           O  
ANISOU 5583  OD1 ASP C 726     9579  11026   9170   1076    137     32       O  
ATOM   5584  OD2 ASP C 726     -44.241  19.141 -39.201  1.00 79.18           O  
ANISOU 5584  OD2 ASP C 726     9544  11243   9297    991    144     24       O  
ATOM   5585  N   SER C 727     -47.155  15.238 -42.053  1.00 57.14           N  
ANISOU 5585  N   SER C 727     7176   8061   6473   1135    208     32       N  
ATOM   5586  CA  SER C 727     -47.826  14.719 -43.220  1.00 57.17           C  
ANISOU 5586  CA  SER C 727     7257   7988   6476   1131    223     21       C  
ATOM   5587  C   SER C 727     -49.296  14.368 -42.947  1.00 52.88           C  
ANISOU 5587  C   SER C 727     6802   7325   5964   1078    216      4       C  
ATOM   5588  O   SER C 727     -50.152  14.589 -43.799  1.00 55.67           O  
ANISOU 5588  O   SER C 727     7184   7628   6340   1020    213    -10       O  
ATOM   5589  CB  SER C 727     -47.064  13.470 -43.710  1.00 58.87           C  
ANISOU 5589  CB  SER C 727     7523   8213   6632   1247    254     27       C  
ATOM   5590  OG  SER C 727     -47.833  12.744 -44.651  1.00 59.24           O  
ANISOU 5590  OG  SER C 727     7665   8168   6674   1246    270      8       O  
ATOM   5591  N   GLN C 728     -49.595  13.773 -41.799  1.00 49.91           N  
ANISOU 5591  N   GLN C 728     6469   6907   5587   1102    214      7       N  
ATOM   5592  CA  GLN C 728     -50.988  13.394 -41.529  1.00 48.30           C  
ANISOU 5592  CA  GLN C 728     6347   6591   5412   1050    211     -8       C  
ATOM   5593  C   GLN C 728     -51.847  14.617 -41.271  1.00 45.90           C  
ANISOU 5593  C   GLN C 728     5996   6280   5162    941    183    -14       C  
ATOM   5594  O   GLN C 728     -52.978  14.705 -41.768  1.00 42.64           O  
ANISOU 5594  O   GLN C 728     5623   5802   4777    877    178    -30       O  
ATOM   5595  CB  GLN C 728     -51.137  12.413 -40.365  1.00 46.12           C  
ANISOU 5595  CB  GLN C 728     6137   6265   5121   1104    223      0       C  
ATOM   5596  N   ILE C 729     -51.316  15.578 -40.538  1.00 43.04           N  
ANISOU 5596  N   ILE C 729     5550   5990   4814    920    165     -3       N  
ATOM   5597  CA  ILE C 729     -52.137  16.705 -40.231  1.00 45.07           C  
ANISOU 5597  CA  ILE C 729     5772   6231   5121    824    144     -8       C  
ATOM   5598  C   ILE C 729     -52.252  17.639 -41.437  1.00 43.79           C  
ANISOU 5598  C   ILE C 729     5569   6089   4978    768    143    -10       C  
ATOM   5599  O   ILE C 729     -53.254  18.315 -41.595  1.00 39.49           O  
ANISOU 5599  O   ILE C 729     5029   5505   4472    695    133    -16       O  
ATOM   5600  CB  ILE C 729     -51.725  17.469 -38.958  1.00 47.88           C  
ANISOU 5600  CB  ILE C 729     6061   6643   5490    807    126     -2       C  
ATOM   5601  CG1 ILE C 729     -50.896  18.659 -39.317  1.00 49.74           C  
ANISOU 5601  CG1 ILE C 729     6199   6964   5734    773    121      0       C  
ATOM   5602  CG2 ILE C 729     -51.002  16.633 -37.894  1.00 50.51           C  
ANISOU 5602  CG2 ILE C 729     6403   7007   5783    892    129      8       C  
ATOM   5603  CD1 ILE C 729     -50.659  19.522 -38.120  1.00 56.12           C  
ANISOU 5603  CD1 ILE C 729     6944   7818   6560    735    103     -4       C  
ATOM   5604  N   LEU C 730     -51.242  17.667 -42.299  1.00 46.60           N  
ANISOU 5604  N   LEU C 730     5889   6510   5308    808    157     -4       N  
ATOM   5605  CA  LEU C 730     -51.392  18.354 -43.568  1.00 44.57           C  
ANISOU 5605  CA  LEU C 730     5611   6264   5062    768    163     -3       C  
ATOM   5606  C   LEU C 730     -52.568  17.780 -44.352  1.00 39.96           C  
ANISOU 5606  C   LEU C 730     5105   5599   4478    750    164    -18       C  
ATOM   5607  O   LEU C 730     -53.346  18.527 -44.912  1.00 38.95           O  
ANISOU 5607  O   LEU C 730     4969   5453   4376    688    158    -19       O  
ATOM   5608  CB  LEU C 730     -50.133  18.239 -44.400  1.00 46.45           C  
ANISOU 5608  CB  LEU C 730     5808   6578   5262    825    182      7       C  
ATOM   5609  CG  LEU C 730     -50.336  18.751 -45.833  1.00 50.33           C  
ANISOU 5609  CG  LEU C 730     6292   7075   5757    797    194     10       C  
ATOM   5610  CD1 LEU C 730     -50.514  20.270 -45.859  1.00 51.25           C  
ANISOU 5610  CD1 LEU C 730     6342   7215   5917    714    190     22       C  
ATOM   5611  CD2 LEU C 730     -49.184  18.294 -46.724  1.00 52.98           C  
ANISOU 5611  CD2 LEU C 730     6610   7475   6046    870    217     18       C  
ATOM   5612  N   ASP C 731     -52.647  16.457 -44.456  1.00 39.05           N  
ANISOU 5612  N   ASP C 731     5066   5439   4331    807    176    -31       N  
ATOM   5613  CA  ASP C 731     -53.740  15.834 -45.219  1.00 37.41           C  
ANISOU 5613  CA  ASP C 731     4935   5158   4121    785    178    -54       C  
ATOM   5614  C   ASP C 731     -55.100  16.182 -44.628  1.00 35.22           C  
ANISOU 5614  C   ASP C 731     4676   4821   3885    708    159    -62       C  
ATOM   5615  O   ASP C 731     -56.052  16.361 -45.360  1.00 35.66           O  
ANISOU 5615  O   ASP C 731     4750   4850   3951    660    152    -76       O  
ATOM   5616  CB  ASP C 731     -53.606  14.298 -45.259  1.00 37.58           C  
ANISOU 5616  CB  ASP C 731     5046   5130   4105    855    199    -70       C  
ATOM   5617  N   LEU C 732     -55.193  16.235 -43.290  1.00 36.33           N  
ANISOU 5617  N   LEU C 732     4812   4947   4046    701    151    -54       N  
ATOM   5618  CA  LEU C 732     -56.455  16.548 -42.635  1.00 34.36           C  
ANISOU 5618  CA  LEU C 732     4578   4643   3834    633    135    -60       C  
ATOM   5619  C   LEU C 732     -56.822  18.003 -42.895  1.00 32.22           C  
ANISOU 5619  C   LEU C 732     4240   4405   3597    567    120    -50       C  
ATOM   5620  O   LEU C 732     -57.958  18.299 -43.233  1.00 31.66           O  
ANISOU 5620  O   LEU C 732     4182   4301   3544    513    111    -58       O  
ATOM   5621  CB  LEU C 732     -56.375  16.263 -41.142  1.00 34.23           C  
ANISOU 5621  CB  LEU C 732     4571   4609   3824    650    133    -52       C  
ATOM   5622  CG  LEU C 732     -56.290  14.784 -40.779  1.00 34.79           C  
ANISOU 5622  CG  LEU C 732     4726   4627   3866    712    153    -59       C  
ATOM   5623  CD1 LEU C 732     -55.935  14.648 -39.315  1.00 34.62           C  
ANISOU 5623  CD1 LEU C 732     4698   4612   3843    745    153    -41       C  
ATOM   5624  CD2 LEU C 732     -57.590  14.030 -41.099  1.00 34.60           C  
ANISOU 5624  CD2 LEU C 732     4782   4514   3852    671    160    -83       C  
ATOM   5625  N   SER C 733     -55.838  18.892 -42.808  1.00 30.77           N  
ANISOU 5625  N   SER C 733     3985   4289   3417    573    121    -32       N  
ATOM   5626  CA  SER C 733     -56.016  20.287 -43.161  1.00 31.34           C  
ANISOU 5626  CA  SER C 733     3999   4390   3518    516    117    -20       C  
ATOM   5627  C   SER C 733     -56.607  20.435 -44.558  1.00 32.39           C  
ANISOU 5627  C   SER C 733     4146   4516   3644    499    121    -22       C  
ATOM   5628  O   SER C 733     -57.598  21.166 -44.782  1.00 32.52           O  
ANISOU 5628  O   SER C 733     4157   4514   3685    446    114    -18       O  
ATOM   5629  CB  SER C 733     -54.687  21.016 -43.104  1.00 32.79           C  
ANISOU 5629  CB  SER C 733     4109   4649   3699    530    126     -6       C  
ATOM   5630  OG  SER C 733     -54.822  22.259 -42.496  1.00 33.41           O  
ANISOU 5630  OG  SER C 733     4140   4739   3816    472    121      2       O  
ATOM   5631  N   ASN C 734     -56.028  19.715 -45.508  1.00 34.80           N  
ANISOU 5631  N   ASN C 734     4470   4840   3911    548    134    -28       N  
ATOM   5632  CA  ASN C 734     -56.496  19.748 -46.892  1.00 35.68           C  
ANISOU 5632  CA  ASN C 734     4596   4956   4006    542    138    -33       C  
ATOM   5633  C   ASN C 734     -57.852  19.125 -47.048  1.00 36.77           C  
ANISOU 5633  C   ASN C 734     4793   5034   4143    512    125    -58       C  
ATOM   5634  O   ASN C 734     -58.650  19.593 -47.881  1.00 38.18           O  
ANISOU 5634  O   ASN C 734     4967   5218   4322    480    120    -59       O  
ATOM   5635  CB  ASN C 734     -55.501  19.057 -47.830  1.00 36.81           C  
ANISOU 5635  CB  ASN C 734     4749   5134   4103    607    156    -37       C  
ATOM   5636  CG  ASN C 734     -54.186  19.831 -47.944  1.00 39.73           C  
ANISOU 5636  CG  ASN C 734     5046   5578   4471    628    171    -10       C  
ATOM   5637  OD1 ASN C 734     -54.144  21.043 -47.729  1.00 39.07           O  
ANISOU 5637  OD1 ASN C 734     4907   5519   4420    582    172     10       O  
ATOM   5638  ND2 ASN C 734     -53.105  19.124 -48.234  1.00 40.54           N  
ANISOU 5638  ND2 ASN C 734     5149   5717   4536    695    187    -11       N  
ATOM   5639  N   ARG C 735     -58.140  18.077 -46.278  1.00 36.07           N  
ANISOU 5639  N   ARG C 735     4760   4893   4052    524    123    -78       N  
ATOM   5640  CA  ARG C 735     -59.461  17.472 -46.357  1.00 38.92           C  
ANISOU 5640  CA  ARG C 735     5175   5197   4416    485    114   -105       C  
ATOM   5641  C   ARG C 735     -60.512  18.523 -45.938  1.00 34.60           C  
ANISOU 5641  C   ARG C 735     4593   4646   3907    419     96    -93       C  
ATOM   5642  O   ARG C 735     -61.590  18.638 -46.533  1.00 34.41           O  
ANISOU 5642  O   ARG C 735     4576   4615   3882    380     86   -105       O  
ATOM   5643  CB  ARG C 735     -59.543  16.194 -45.528  1.00 46.99           C  
ANISOU 5643  CB  ARG C 735     6266   6156   5432    507    122   -124       C  
ATOM   5644  CG  ARG C 735     -60.563  15.171 -46.027  1.00 58.45           C  
ANISOU 5644  CG  ARG C 735     7789   7551   6869    481    124   -164       C  
ATOM   5645  CD  ARG C 735     -60.551  13.875 -45.197  1.00 62.27           C  
ANISOU 5645  CD  ARG C 735     8350   7962   7347    506    143   -179       C  
ATOM   5646  NE  ARG C 735     -59.359  13.080 -45.453  1.00 64.85           N  
ANISOU 5646  NE  ARG C 735     8710   8293   7637    588    167   -178       N  
ATOM   5647  CZ  ARG C 735     -59.192  12.287 -46.512  1.00 71.39           C  
ANISOU 5647  CZ  ARG C 735     9587   9109   8429    614    183   -207       C  
ATOM   5648  NH1 ARG C 735     -60.147  12.166 -47.432  1.00 73.62           N  
ANISOU 5648  NH1 ARG C 735     9890   9379   8705    562    174   -242       N  
ATOM   5649  NH2 ARG C 735     -58.055  11.612 -46.666  1.00 71.83           N  
ANISOU 5649  NH2 ARG C 735     9671   9172   8450    697    207   -201       N  
ATOM   5650  N   PHE C 736     -60.189  19.304 -44.925  1.00 30.84           N  
ANISOU 5650  N   PHE C 736     4076   4180   3462    409     94    -69       N  
ATOM   5651  CA  PHE C 736     -61.111  20.339 -44.459  1.00 30.17           C  
ANISOU 5651  CA  PHE C 736     3962   4090   3413    354     82    -56       C  
ATOM   5652  C   PHE C 736     -61.381  21.390 -45.541  1.00 28.43           C  
ANISOU 5652  C   PHE C 736     3702   3909   3193    334     83    -39       C  
ATOM   5653  O   PHE C 736     -62.531  21.708 -45.834  1.00 29.65           O  
ANISOU 5653  O   PHE C 736     3857   4056   3354    299     74    -41       O  
ATOM   5654  CB  PHE C 736     -60.577  21.026 -43.209  1.00 28.79           C  
ANISOU 5654  CB  PHE C 736     3751   3922   3267    349     82    -37       C  
ATOM   5655  CG  PHE C 736     -61.450  22.131 -42.739  1.00 27.16           C  
ANISOU 5655  CG  PHE C 736     3517   3707   3096    298     74    -23       C  
ATOM   5656  CD1 PHE C 736     -62.540  21.849 -41.950  1.00 26.12           C  
ANISOU 5656  CD1 PHE C 736     3413   3532   2981    268     64    -32       C  
ATOM   5657  CD2 PHE C 736     -61.229  23.460 -43.136  1.00 27.31           C  
ANISOU 5657  CD2 PHE C 736     3486   3760   3131    279     83      0       C  
ATOM   5658  CE1 PHE C 736     -63.391  22.854 -41.551  1.00 24.79           C  
ANISOU 5658  CE1 PHE C 736     3221   3357   2842    227     59    -18       C  
ATOM   5659  CE2 PHE C 736     -62.094  24.478 -42.745  1.00 25.83           C  
ANISOU 5659  CE2 PHE C 736     3282   3559   2974    238     81     14       C  
ATOM   5660  CZ  PHE C 736     -63.166  24.171 -41.943  1.00 25.23           C  
ANISOU 5660  CZ  PHE C 736     3231   3443   2912    214     68      5       C  
ATOM   5661  N   TYR C 737     -60.323  21.892 -46.146  1.00 27.65           N  
ANISOU 5661  N   TYR C 737     3567   3855   3083    361     97    -22       N  
ATOM   5662  CA  TYR C 737     -60.448  22.881 -47.218  1.00 31.13           C  
ANISOU 5662  CA  TYR C 737     3975   4334   3520    352    106      0       C  
ATOM   5663  C   TYR C 737     -61.129  22.368 -48.475  1.00 34.04           C  
ANISOU 5663  C   TYR C 737     4369   4713   3852    360    101    -16       C  
ATOM   5664  O   TYR C 737     -61.676  23.143 -49.245  1.00 38.15           O  
ANISOU 5664  O   TYR C 737     4869   5259   4368    347    103      1       O  
ATOM   5665  CB  TYR C 737     -59.086  23.471 -47.554  1.00 29.39           C  
ANISOU 5665  CB  TYR C 737     3711   4160   3296    377    128     22       C  
ATOM   5666  CG  TYR C 737     -58.566  24.348 -46.441  1.00 29.05           C  
ANISOU 5666  CG  TYR C 737     3628   4118   3291    353    134     37       C  
ATOM   5667  CD1 TYR C 737     -59.285  25.466 -45.997  1.00 29.71           C  
ANISOU 5667  CD1 TYR C 737     3694   4184   3410    307    135     54       C  
ATOM   5668  CD2 TYR C 737     -57.374  24.085 -45.832  1.00 29.76           C  
ANISOU 5668  CD2 TYR C 737     3698   4231   3378    377    139     33       C  
ATOM   5669  CE1 TYR C 737     -58.821  26.288 -44.971  1.00 28.50           C  
ANISOU 5669  CE1 TYR C 737     3509   4030   3291    280    142     61       C  
ATOM   5670  CE2 TYR C 737     -56.907  24.913 -44.817  1.00 28.99           C  
ANISOU 5670  CE2 TYR C 737     3560   4143   3312    349    142     41       C  
ATOM   5671  CZ  TYR C 737     -57.626  26.021 -44.410  1.00 28.42           C  
ANISOU 5671  CZ  TYR C 737     3475   4047   3276    297    144     53       C  
ATOM   5672  OH  TYR C 737     -57.129  26.852 -43.430  1.00 30.50           O  
ANISOU 5672  OH  TYR C 737     3701   4317   3568    266    149     54       O  
ATOM   5673  N   THR C 738     -61.133  21.055 -48.667  1.00 36.69           N  
ANISOU 5673  N   THR C 738     4754   5028   4159    381     95    -50       N  
ATOM   5674  CA  THR C 738     -61.888  20.437 -49.737  1.00 37.93           C  
ANISOU 5674  CA  THR C 738     4941   5189   4280    379     87    -78       C  
ATOM   5675  C   THR C 738     -63.363  20.414 -49.420  1.00 38.74           C  
ANISOU 5675  C   THR C 738     5056   5268   4397    327     67    -93       C  
ATOM   5676  O   THR C 738     -64.171  20.612 -50.317  1.00 43.54           O  
ANISOU 5676  O   THR C 738     5656   5905   4983    313     58   -100       O  
ATOM   5677  CB  THR C 738     -61.378  19.000 -49.975  1.00 42.98           C  
ANISOU 5677  CB  THR C 738     5637   5806   4887    415     93   -114       C  
ATOM   5678  OG1 THR C 738     -60.025  19.068 -50.454  1.00 41.81           O  
ANISOU 5678  OG1 THR C 738     5472   5696   4719    469    112    -97       O  
ATOM   5679  CG2 THR C 738     -62.222  18.257 -50.984  1.00 44.64           C  
ANISOU 5679  CG2 THR C 738     5887   6016   5060    403     84   -154       C  
ATOM   5680  N   LEU C 739     -63.734  20.153 -48.161  1.00 36.68           N  
ANISOU 5680  N   LEU C 739     4810   4958   4168    301     62    -99       N  
ATOM   5681  CA  LEU C 739     -65.149  20.185 -47.777  1.00 33.69           C  
ANISOU 5681  CA  LEU C 739     4437   4560   3805    250     45   -110       C  
ATOM   5682  C   LEU C 739     -65.653  21.599 -47.787  1.00 32.61           C  
ANISOU 5682  C   LEU C 739     4246   4455   3688    232     42    -73       C  
ATOM   5683  O   LEU C 739     -66.788  21.827 -48.133  1.00 35.73           O  
ANISOU 5683  O   LEU C 739     4631   4868   4078    205     30    -78       O  
ATOM   5684  CB  LEU C 739     -65.389  19.690 -46.361  1.00 35.02           C  
ANISOU 5684  CB  LEU C 739     4631   4670   4004    230     44   -118       C  
ATOM   5685  CG  LEU C 739     -65.644  18.243 -45.944  1.00 37.82           C  
ANISOU 5685  CG  LEU C 739     5052   4967   4350    223     48   -156       C  
ATOM   5686  CD1 LEU C 739     -65.938  17.385 -47.155  1.00 37.83           C  
ANISOU 5686  CD1 LEU C 739     5088   4976   4312    221     47   -196       C  
ATOM   5687  CD2 LEU C 739     -64.442  17.691 -45.195  1.00 41.40           C  
ANISOU 5687  CD2 LEU C 739     5531   5393   4806    271     64   -149       C  
ATOM   5688  N   ILE C 740     -64.837  22.524 -47.305  1.00 29.13           N  
ANISOU 5688  N   ILE C 740     3774   4021   3273    246     56    -39       N  
ATOM   5689  CA  ILE C 740     -65.253  23.898 -47.208  1.00 29.69           C  
ANISOU 5689  CA  ILE C 740     3804   4110   3368    230     61     -2       C  
ATOM   5690  C   ILE C 740     -64.250  24.742 -48.010  1.00 31.33           C  
ANISOU 5690  C   ILE C 740     3981   4357   3567    259     82     28       C  
ATOM   5691  O   ILE C 740     -63.220  25.161 -47.494  1.00 30.09           O  
ANISOU 5691  O   ILE C 740     3807   4196   3430    266     98     43       O  
ATOM   5692  CB  ILE C 740     -65.300  24.356 -45.757  1.00 31.02           C  
ANISOU 5692  CB  ILE C 740     3966   4242   3580    207     62      9       C  
ATOM   5693  CG1 ILE C 740     -66.026  23.333 -44.870  1.00 30.12           C  
ANISOU 5693  CG1 ILE C 740     3888   4085   3472    185     46    -21       C  
ATOM   5694  CG2 ILE C 740     -65.969  25.711 -45.685  1.00 32.56           C  
ANISOU 5694  CG2 ILE C 740     4128   4446   3795    189     69     42       C  
ATOM   5695  CD1 ILE C 740     -67.517  23.268 -45.090  1.00 30.06           C  
ANISOU 5695  CD1 ILE C 740     3882   4080   3459    152     32    -30       C  
ATOM   5696  N   PRO C 741     -64.530  24.935 -49.299  1.00 31.74           N  
ANISOU 5696  N   PRO C 741     4025   4450   3585    275     85     36       N  
ATOM   5697  CA  PRO C 741     -63.571  25.567 -50.161  1.00 33.34           C  
ANISOU 5697  CA  PRO C 741     4203   4689   3774    306    110     64       C  
ATOM   5698  C   PRO C 741     -63.357  27.011 -49.769  1.00 33.63           C  
ANISOU 5698  C   PRO C 741     4208   4723   3848    293    134    107       C  
ATOM   5699  O   PRO C 741     -64.327  27.746 -49.551  1.00 34.90           O  
ANISOU 5699  O   PRO C 741     4361   4875   4024    274    134    126       O  
ATOM   5700  CB  PRO C 741     -64.184  25.453 -51.561  1.00 34.75           C  
ANISOU 5700  CB  PRO C 741     4384   4915   3905    325    104     62       C  
ATOM   5701  CG  PRO C 741     -65.458  24.692 -51.415  1.00 36.12           C  
ANISOU 5701  CG  PRO C 741     4579   5079   4066    299     74     26       C  
ATOM   5702  CD  PRO C 741     -65.762  24.499 -49.987  1.00 33.35           C  
ANISOU 5702  CD  PRO C 741     4239   4674   3758    265     65     15       C  
ATOM   5703  N   HIS C 742     -62.095  27.393 -49.685  1.00 32.85           N  
ANISOU 5703  N   HIS C 742     4089   4630   3761    302    158    122       N  
ATOM   5704  CA  HIS C 742     -61.703  28.744 -49.346  1.00 35.12           C  
ANISOU 5704  CA  HIS C 742     4348   4910   4084    284    188    157       C  
ATOM   5705  C   HIS C 742     -60.965  29.374 -50.517  1.00 34.77           C  
ANISOU 5705  C   HIS C 742     4284   4905   4021    308    222    190       C  
ATOM   5706  O   HIS C 742     -60.551  28.706 -51.444  1.00 35.86           O  
ANISOU 5706  O   HIS C 742     4426   5078   4120    342    220    182       O  
ATOM   5707  CB  HIS C 742     -60.783  28.741 -48.140  1.00 33.45           C  
ANISOU 5707  CB  HIS C 742     4125   4680   3906    263    190    144       C  
ATOM   5708  CG  HIS C 742     -61.488  28.556 -46.839  1.00 35.60           C  
ANISOU 5708  CG  HIS C 742     4411   4909   4205    235    167    125       C  
ATOM   5709  ND1 HIS C 742     -62.188  27.406 -46.522  1.00 35.48           N  
ANISOU 5709  ND1 HIS C 742     4428   4877   4175    240    136     95       N  
ATOM   5710  CD2 HIS C 742     -61.568  29.360 -45.755  1.00 35.11           C  
ANISOU 5710  CD2 HIS C 742     4339   4819   4183    202    174    131       C  
ATOM   5711  CE1 HIS C 742     -62.665  27.517 -45.298  1.00 33.33           C  
ANISOU 5711  CE1 HIS C 742     4162   4570   3933    213    125     88       C  
ATOM   5712  NE2 HIS C 742     -62.323  28.703 -44.823  1.00 33.59           N  
ANISOU 5712  NE2 HIS C 742     4169   4596   3997    191    146    108       N  
ATOM   5713  N   ASP C 743     -60.822  30.678 -50.449  1.00 40.42           N  
ANISOU 5713  N   ASP C 743     4981   5610   4765    290    257    227       N  
ATOM   5714  CA  ASP C 743     -60.274  31.483 -51.505  1.00 46.51           C  
ANISOU 5714  CA  ASP C 743     5736   6410   5525    308    299    266       C  
ATOM   5715  C   ASP C 743     -59.124  32.235 -50.894  1.00 51.26           C  
ANISOU 5715  C   ASP C 743     6312   6999   6167    275    332    275       C  
ATOM   5716  O   ASP C 743     -59.236  33.325 -50.313  1.00 48.59           O  
ANISOU 5716  O   ASP C 743     5969   6624   5867    239    358    293       O  
ATOM   5717  CB  ASP C 743     -61.365  32.381 -52.059  1.00 54.88           C  
ANISOU 5717  CB  ASP C 743     6806   7465   6579    318    316    305       C  
ATOM   5718  CG  ASP C 743     -61.187  32.677 -53.519  1.00 65.56           C  
ANISOU 5718  CG  ASP C 743     8155   8864   7891    360    344    341       C  
ATOM   5719  OD1 ASP C 743     -60.022  32.899 -53.965  1.00 62.53           O  
ANISOU 5719  OD1 ASP C 743     7754   8498   7507    366    376    355       O  
ATOM   5720  OD2 ASP C 743     -62.244  32.663 -54.209  1.00 72.32           O  
ANISOU 5720  OD2 ASP C 743     9022   9744   8713    390    332    354       O  
ATOM   5721  N   PHE C 744     -57.995  31.562 -50.950  1.00 64.78           N  
ANISOU 5721  N   PHE C 744     8005   8742   7866    286    329    255       N  
ATOM   5722  CA  PHE C 744     -56.722  32.205 -50.749  1.00 72.06           C  
ANISOU 5722  CA  PHE C 744     8890   9677   8811    261    364    264       C  
ATOM   5723  C   PHE C 744     -56.612  33.368 -51.758  1.00 71.32           C  
ANISOU 5723  C   PHE C 744     8790   9589   8720    261    419    315       C  
ATOM   5724  O   PHE C 744     -57.090  33.261 -52.904  1.00 73.15           O  
ANISOU 5724  O   PHE C 744     9038   9843   8914    304    425    339       O  
ATOM   5725  CB  PHE C 744     -55.617  31.170 -50.988  1.00 76.94           C  
ANISOU 5725  CB  PHE C 744     9489  10346   9400    292    353    242       C  
ATOM   5726  CG  PHE C 744     -55.544  30.659 -52.411  1.00 82.79           C  
ANISOU 5726  CG  PHE C 744    10239  11127  10090    346    360    256       C  
ATOM   5727  CD1 PHE C 744     -54.664  31.238 -53.328  1.00 85.58           C  
ANISOU 5727  CD1 PHE C 744    10565  11519  10433    357    405    288       C  
ATOM   5728  CD2 PHE C 744     -56.343  29.601 -52.836  1.00 88.40           C  
ANISOU 5728  CD2 PHE C 744    10986  11839  10761    384    323    234       C  
ATOM   5729  CE1 PHE C 744     -54.585  30.776 -54.630  1.00 88.75           C  
ANISOU 5729  CE1 PHE C 744    10975  11961  10783    410    412    301       C  
ATOM   5730  CE2 PHE C 744     -56.266  29.133 -54.140  1.00 93.36           C  
ANISOU 5730  CE2 PHE C 744    11626  12508  11340    432    329    241       C  
ATOM   5731  CZ  PHE C 744     -55.383  29.718 -55.036  1.00 94.66           C  
ANISOU 5731  CZ  PHE C 744    11761  12713  11491    448    372    276       C  
ATOM   5732  N   GLY C 745     -56.018  34.478 -51.334  1.00 64.20           N  
ANISOU 5732  N   GLY C 745     7868   8667   7860    214    461    330       N  
ATOM   5733  CA  GLY C 745     -55.527  35.459 -52.297  1.00 63.18           C  
ANISOU 5733  CA  GLY C 745     7728   8547   7731    213    523    377       C  
ATOM   5734  C   GLY C 745     -54.037  35.233 -52.503  1.00 61.50           C  
ANISOU 5734  C   GLY C 745     7469   8385   7513    205    542    368       C  
ATOM   5735  O   GLY C 745     -53.621  34.313 -53.201  1.00 60.60           O  
ANISOU 5735  O   GLY C 745     7346   8323   7356    253    526    362       O  
ATOM   5736  N   MET C 746     -53.244  36.045 -51.826  1.00 62.35           N  
ANISOU 5736  N   MET C 746     7546   8481   7663    143    574    363       N  
ATOM   5737  CA  MET C 746     -51.781  36.035 -51.926  1.00 64.90           C  
ANISOU 5737  CA  MET C 746     7814   8858   7987    123    599    355       C  
ATOM   5738  C   MET C 746     -51.128  34.875 -51.154  1.00 65.87           C  
ANISOU 5738  C   MET C 746     7905   9029   8094    136    547    305       C  
ATOM   5739  O   MET C 746     -50.218  34.223 -51.668  1.00 67.59           O  
ANISOU 5739  O   MET C 746     8090   9312   8280    170    547    302       O  
ATOM   5740  CB  MET C 746     -51.248  37.360 -51.370  1.00 62.07           C  
ANISOU 5740  CB  MET C 746     7433   8468   7681     41    652    359       C  
ATOM   5741  CG  MET C 746     -50.070  37.885 -52.127  1.00 63.33           C  
ANISOU 5741  CG  MET C 746     7552   8670   7842     21    712    383       C  
ATOM   5742  SD  MET C 746     -49.669  39.588 -51.724  1.00 66.34           S  
ANISOU 5742  SD  MET C 746     7925   8994   8287    -81    790    396       S  
ATOM   5743  CE  MET C 746     -51.249  40.390 -51.982  1.00 62.27           C  
ANISOU 5743  CE  MET C 746     7494   8381   7785    -61    811    440       C  
ATOM   5744  N   LYS C 747     -51.588  34.667 -49.914  1.00 67.15           N  
ANISOU 5744  N   LYS C 747     8077   9161   8278    112    507    270       N  
ATOM   5745  CA  LYS C 747     -51.200  33.536 -49.044  1.00 69.67           C  
ANISOU 5745  CA  LYS C 747     8378   9514   8579    133    455    225       C  
ATOM   5746  C   LYS C 747     -52.014  32.294 -49.379  1.00 66.70           C  
ANISOU 5746  C   LYS C 747     8048   9131   8164    200    411    219       C  
ATOM   5747  O   LYS C 747     -53.202  32.409 -49.638  1.00 63.65           O  
ANISOU 5747  O   LYS C 747     7708   8698   7779    208    403    232       O  
ATOM   5748  CB  LYS C 747     -51.466  33.888 -47.565  1.00 67.06           C  
ANISOU 5748  CB  LYS C 747     8045   9147   8286     80    435    193       C  
ATOM   5749  N   LYS C 748     -51.388  31.117 -49.375  1.00 68.57           N  
ANISOU 5749  N   LYS C 748     8273   9416   8365    248    385    197       N  
ATOM   5750  CA  LYS C 748     -52.147  29.849 -49.382  1.00 66.74           C  
ANISOU 5750  CA  LYS C 748     8090   9166   8101    301    341    179       C  
ATOM   5751  C   LYS C 748     -52.922  29.758 -48.057  1.00 62.20           C  
ANISOU 5751  C   LYS C 748     7538   8541   7553    273    307    154       C  
ATOM   5752  O   LYS C 748     -52.556  30.406 -47.074  1.00 55.20           O  
ANISOU 5752  O   LYS C 748     6621   7653   6699    226    312    143       O  
ATOM   5753  CB  LYS C 748     -51.229  28.638 -49.548  1.00 66.89           C  
ANISOU 5753  CB  LYS C 748     8098   9240   8077    361    327    161       C  
ATOM   5754  N   PRO C 749     -54.014  28.972 -48.023  1.00 63.99           N  
ANISOU 5754  N   PRO C 749     7818   8730   7766    297    276    143       N  
ATOM   5755  CA  PRO C 749     -54.779  28.923 -46.765  1.00 61.16           C  
ANISOU 5755  CA  PRO C 749     7480   8325   7434    269    248    123       C  
ATOM   5756  C   PRO C 749     -53.944  28.367 -45.596  1.00 50.94           C  
ANISOU 5756  C   PRO C 749     6161   7054   6138    275    230     95       C  
ATOM   5757  O   PRO C 749     -53.086  27.521 -45.817  1.00 55.90           O  
ANISOU 5757  O   PRO C 749     6779   7728   6734    322    226     87       O  
ATOM   5758  CB  PRO C 749     -55.953  27.999 -47.076  1.00 62.83           C  
ANISOU 5758  CB  PRO C 749     7748   8502   7624    298    221    114       C  
ATOM   5759  CG  PRO C 749     -55.941  27.764 -48.557  1.00 63.71           C  
ANISOU 5759  CG  PRO C 749     7868   8638   7699    334    234    129       C  
ATOM   5760  CD  PRO C 749     -54.563  28.082 -49.062  1.00 64.72           C  
ANISOU 5760  CD  PRO C 749     7952   8823   7818    346    264    143       C  
ATOM   5761  N   PRO C 750     -54.172  28.872 -44.376  1.00 45.60           N  
ANISOU 5761  N   PRO C 750     5477   6354   5494    233    220     82       N  
ATOM   5762  CA  PRO C 750     -53.445  28.446 -43.168  1.00 46.12           C  
ANISOU 5762  CA  PRO C 750     5517   6449   5555    239    201     56       C  
ATOM   5763  C   PRO C 750     -53.447  26.943 -42.891  1.00 44.27           C  
ANISOU 5763  C   PRO C 750     5316   6218   5285    302    173     41       C  
ATOM   5764  O   PRO C 750     -54.498  26.302 -43.012  1.00 44.11           O  
ANISOU 5764  O   PRO C 750     5353   6147   5260    317    158     40       O  
ATOM   5765  CB  PRO C 750     -54.230  29.105 -42.024  1.00 47.78           C  
ANISOU 5765  CB  PRO C 750     5739   6613   5802    189    190     46       C  
ATOM   5766  CG  PRO C 750     -55.239  30.015 -42.629  1.00 45.53           C  
ANISOU 5766  CG  PRO C 750     5479   6277   5544    156    209     69       C  
ATOM   5767  CD  PRO C 750     -55.210  29.894 -44.106  1.00 44.28           C  
ANISOU 5767  CD  PRO C 750     5328   6133   5364    184    228     93       C  
ATOM   5768  N   LEU C 751     -52.309  26.406 -42.471  1.00 39.93           N  
ANISOU 5768  N   LEU C 751     4733   5728   4711    338    169     30       N  
ATOM   5769  CA  LEU C 751     -52.248  25.037 -41.992  1.00 42.49           C  
ANISOU 5769  CA  LEU C 751     5093   6052   5001    402    148     18       C  
ATOM   5770  C   LEU C 751     -53.020  24.946 -40.672  1.00 40.11           C  
ANISOU 5770  C   LEU C 751     4817   5705   4717    382    126      5       C  
ATOM   5771  O   LEU C 751     -52.806  25.765 -39.779  1.00 37.63           O  
ANISOU 5771  O   LEU C 751     4464   5407   4425    340    122     -4       O  
ATOM   5772  CB  LEU C 751     -50.792  24.608 -41.763  1.00 45.31           C  
ANISOU 5772  CB  LEU C 751     5398   6494   5325    450    151     14       C  
ATOM   5773  CG  LEU C 751     -50.569  23.110 -41.512  1.00 47.66           C  
ANISOU 5773  CG  LEU C 751     5737   6794   5578    536    141      9       C  
ATOM   5774  CD1 LEU C 751     -51.108  22.278 -42.671  1.00 48.15           C  
ANISOU 5774  CD1 LEU C 751     5864   6810   5620    573    149     15       C  
ATOM   5775  CD2 LEU C 751     -49.082  22.850 -41.322  1.00 50.23           C  
ANISOU 5775  CD2 LEU C 751     6000   7217   5867    587    146      9       C  
ATOM   5776  N   LEU C 752     -53.897  23.947 -40.565  1.00 35.23           N  
ANISOU 5776  N   LEU C 752     4266   5031   4088    411    113      2       N  
ATOM   5777  CA  LEU C 752     -54.672  23.736 -39.355  1.00 36.00           C  
ANISOU 5777  CA  LEU C 752     4394   5083   4199    399     95     -8       C  
ATOM   5778  C   LEU C 752     -53.941  22.803 -38.368  1.00 40.25           C  
ANISOU 5778  C   LEU C 752     4934   5653   4705    458     86    -15       C  
ATOM   5779  O   LEU C 752     -54.179  21.604 -38.339  1.00 42.24           O  
ANISOU 5779  O   LEU C 752     5242   5873   4932    509     85    -15       O  
ATOM   5780  CB  LEU C 752     -56.049  23.190 -39.698  1.00 33.61           C  
ANISOU 5780  CB  LEU C 752     4161   4706   3904    391     90     -7       C  
ATOM   5781  CG  LEU C 752     -56.839  24.108 -40.640  1.00 32.33           C  
ANISOU 5781  CG  LEU C 752     3996   4523   3767    341     98      3       C  
ATOM   5782  CD1 LEU C 752     -58.109  23.442 -41.053  1.00 31.23           C  
ANISOU 5782  CD1 LEU C 752     3915   4326   3624    338     91     -1       C  
ATOM   5783  CD2 LEU C 752     -57.111  25.468 -40.003  1.00 31.75           C  
ANISOU 5783  CD2 LEU C 752     3887   4445   3732    282    100      8       C  
ATOM   5784  N   ASN C 753     -53.015  23.374 -37.606  1.00 39.41           N  
ANISOU 5784  N   ASN C 753     4765   5613   4598    452     81    -22       N  
ATOM   5785  CA  ASN C 753     -52.088  22.602 -36.804  1.00 43.76           C  
ANISOU 5785  CA  ASN C 753     5300   6220   5109    517     74    -26       C  
ATOM   5786  C   ASN C 753     -51.985  23.121 -35.365  1.00 42.22           C  
ANISOU 5786  C   ASN C 753     5070   6051   4920    493     56    -40       C  
ATOM   5787  O   ASN C 753     -51.069  22.772 -34.651  1.00 44.31           O  
ANISOU 5787  O   ASN C 753     5299   6386   5150    540     48    -45       O  
ATOM   5788  CB  ASN C 753     -50.697  22.565 -37.466  1.00 46.10           C  
ANISOU 5788  CB  ASN C 753     5537   6605   5374    555     85    -22       C  
ATOM   5789  CG  ASN C 753     -49.960  23.891 -37.403  1.00 49.16           C  
ANISOU 5789  CG  ASN C 753     5837   7061   5783    492     89    -32       C  
ATOM   5790  OD1 ASN C 753     -50.551  24.950 -37.214  1.00 43.46           O  
ANISOU 5790  OD1 ASN C 753     5106   6304   5103    415     89    -39       O  
ATOM   5791  ND2 ASN C 753     -48.638  23.826 -37.575  1.00 51.69           N  
ANISOU 5791  ND2 ASN C 753     6092   7478   6072    526     95    -34       N  
ATOM   5792  N   ASN C 754     -52.919  23.967 -34.968  1.00 38.31           N  
ANISOU 5792  N   ASN C 754     4585   5506   4466    424     51    -46       N  
ATOM   5793  CA  ASN C 754     -52.893  24.558 -33.647  1.00 40.22           C  
ANISOU 5793  CA  ASN C 754     4797   5769   4715    395     36    -63       C  
ATOM   5794  C   ASN C 754     -54.326  24.882 -33.215  1.00 39.46           C  
ANISOU 5794  C   ASN C 754     4751   5585   4654    350     32    -62       C  
ATOM   5795  O   ASN C 754     -55.242  24.942 -34.032  1.00 39.57           O  
ANISOU 5795  O   ASN C 754     4806   5536   4692    327     42    -50       O  
ATOM   5796  CB  ASN C 754     -52.013  25.815 -33.621  1.00 39.80           C  
ANISOU 5796  CB  ASN C 754     4662   5785   4677    337     40    -82       C  
ATOM   5797  CG  ASN C 754     -52.565  26.920 -34.475  1.00 39.56           C  
ANISOU 5797  CG  ASN C 754     4632   5706   4693    264     60    -77       C  
ATOM   5798  OD1 ASN C 754     -53.391  27.724 -34.028  1.00 39.25           O  
ANISOU 5798  OD1 ASN C 754     4609   5616   4689    208     61    -83       O  
ATOM   5799  ND2 ASN C 754     -52.127  26.968 -35.725  1.00 41.83           N  
ANISOU 5799  ND2 ASN C 754     4906   6009   4980    268     79    -63       N  
ATOM   5800  N   ALA C 755     -54.492  25.087 -31.927  1.00 35.71           N  
ANISOU 5800  N   ALA C 755     4271   5118   4179    341     18    -75       N  
ATOM   5801  CA  ALA C 755     -55.790  25.250 -31.343  1.00 33.33           C  
ANISOU 5801  CA  ALA C 755     4018   4743   3904    311     15    -72       C  
ATOM   5802  C   ALA C 755     -56.502  26.517 -31.857  1.00 34.36           C  
ANISOU 5802  C   ALA C 755     4143   4831   4082    234     27    -73       C  
ATOM   5803  O   ALA C 755     -57.689  26.481 -32.143  1.00 31.38           O  
ANISOU 5803  O   ALA C 755     3811   4385   3726    218     31    -60       O  
ATOM   5804  CB  ALA C 755     -55.654  25.271 -29.818  1.00 31.83           C  
ANISOU 5804  CB  ALA C 755     3816   4582   3697    322     -1    -87       C  
ATOM   5805  N   ASP C 756     -55.782  27.626 -31.954  1.00 35.37           N  
ANISOU 5805  N   ASP C 756     4215   5001   4225    189     34    -88       N  
ATOM   5806  CA  ASP C 756     -56.361  28.903 -32.406  1.00 35.52           C  
ANISOU 5806  CA  ASP C 756     4231   4977   4287    120     53    -87       C  
ATOM   5807  C   ASP C 756     -56.932  28.818 -33.837  1.00 33.23           C  
ANISOU 5807  C   ASP C 756     3970   4645   4010    122     69    -59       C  
ATOM   5808  O   ASP C 756     -58.070  29.264 -34.082  1.00 32.67           O  
ANISOU 5808  O   ASP C 756     3933   4515   3964     96     78    -46       O  
ATOM   5809  CB  ASP C 756     -55.302  30.050 -32.289  1.00 39.31           C  
ANISOU 5809  CB  ASP C 756     4646   5511   4778     68     65   -111       C  
ATOM   5810  CG  ASP C 756     -55.190  30.629 -30.866  1.00 45.93           C  
ANISOU 5810  CG  ASP C 756     5465   6369   5619     37     53   -144       C  
ATOM   5811  OD1 ASP C 756     -54.433  31.611 -30.727  1.00 51.88           O  
ANISOU 5811  OD1 ASP C 756     6169   7160   6385    -17     65   -170       O  
ATOM   5812  OD2 ASP C 756     -55.838  30.147 -29.895  1.00 49.28           O  
ANISOU 5812  OD2 ASP C 756     5921   6772   6032     61     34   -146       O  
ATOM   5813  N   SER C 757     -56.186  28.203 -34.754  1.00 30.34           N  
ANISOU 5813  N   SER C 757     3591   4315   3620    158     74    -51       N  
ATOM   5814  CA  SER C 757     -56.678  28.034 -36.131  1.00 30.98           C  
ANISOU 5814  CA  SER C 757     3699   4367   3705    166     87    -28       C  
ATOM   5815  C   SER C 757     -57.886  27.088 -36.200  1.00 28.94           C  
ANISOU 5815  C   SER C 757     3504   4051   3440    191     75    -19       C  
ATOM   5816  O   SER C 757     -58.822  27.352 -36.932  1.00 28.18           O  
ANISOU 5816  O   SER C 757     3433   3916   3360    173     83     -5       O  
ATOM   5817  CB  SER C 757     -55.604  27.504 -37.032  1.00 32.54           C  
ANISOU 5817  CB  SER C 757     3872   4617   3874    204     94    -24       C  
ATOM   5818  OG  SER C 757     -54.467  28.341 -36.982  1.00 36.73           O  
ANISOU 5818  OG  SER C 757     4339   5207   4410    176    107    -34       O  
ATOM   5819  N   VAL C 758     -57.900  26.062 -35.360  1.00 27.59           N  
ANISOU 5819  N   VAL C 758     3358   3878   3248    230     59    -27       N  
ATOM   5820  CA  VAL C 758     -59.009  25.110 -35.325  1.00 28.60           C  
ANISOU 5820  CA  VAL C 758     3546   3949   3370    247     52    -22       C  
ATOM   5821  C   VAL C 758     -60.258  25.796 -34.810  1.00 27.58           C  
ANISOU 5821  C   VAL C 758     3432   3773   3273    201     50    -19       C  
ATOM   5822  O   VAL C 758     -61.332  25.724 -35.433  1.00 27.69           O  
ANISOU 5822  O   VAL C 758     3475   3748   3297    186     53     -9       O  
ATOM   5823  CB  VAL C 758     -58.677  23.873 -34.478  1.00 27.82           C  
ANISOU 5823  CB  VAL C 758     3475   3854   3241    301     43    -27       C  
ATOM   5824  CG1 VAL C 758     -59.898  23.011 -34.276  1.00 28.44           C  
ANISOU 5824  CG1 VAL C 758     3617   3866   3321    305     42    -24       C  
ATOM   5825  CG2 VAL C 758     -57.591  23.055 -35.183  1.00 29.52           C  
ANISOU 5825  CG2 VAL C 758     3686   4110   3421    358     49    -26       C  
ATOM   5826  N   GLN C 759     -60.098  26.497 -33.700  1.00 27.15           N  
ANISOU 5826  N   GLN C 759     3355   3729   3231    180     46    -28       N  
ATOM   5827  CA  GLN C 759     -61.186  27.238 -33.063  1.00 27.54           C  
ANISOU 5827  CA  GLN C 759     3417   3738   3308    141     47    -26       C  
ATOM   5828  C   GLN C 759     -61.839  28.249 -34.019  1.00 23.99           C  
ANISOU 5828  C   GLN C 759     2964   3267   2886    104     64    -11       C  
ATOM   5829  O   GLN C 759     -63.043  28.314 -34.108  1.00 23.58           O  
ANISOU 5829  O   GLN C 759     2937   3176   2846     92     64      0       O  
ATOM   5830  CB  GLN C 759     -60.634  27.986 -31.841  1.00 31.66           C  
ANISOU 5830  CB  GLN C 759     3909   4286   3837    123     43    -44       C  
ATOM   5831  CG  GLN C 759     -61.662  28.488 -30.849  1.00 34.16           C  
ANISOU 5831  CG  GLN C 759     4244   4563   4172     97     42    -46       C  
ATOM   5832  CD  GLN C 759     -60.989  29.251 -29.713  1.00 37.73           C  
ANISOU 5832  CD  GLN C 759     4664   5047   4624     78     38    -71       C  
ATOM   5833  OE1 GLN C 759     -59.840  28.919 -29.337  1.00 40.48           O  
ANISOU 5833  OE1 GLN C 759     4981   5453   4947     99     28    -87       O  
ATOM   5834  NE2 GLN C 759     -61.666  30.292 -29.170  1.00 34.86           N  
ANISOU 5834  NE2 GLN C 759     4305   4652   4286     38     48    -76       N  
ATOM   5835  N   ALA C 760     -61.030  28.991 -34.756  1.00 23.85           N  
ANISOU 5835  N   ALA C 760     2911   3276   2873     90     79     -9       N  
ATOM   5836  CA  ALA C 760     -61.555  29.938 -35.753  1.00 25.22           C  
ANISOU 5836  CA  ALA C 760     3084   3431   3068     64    100     12       C  
ATOM   5837  C   ALA C 760     -62.404  29.234 -36.829  1.00 25.36           C  
ANISOU 5837  C   ALA C 760     3130   3433   3071     86     96     28       C  
ATOM   5838  O   ALA C 760     -63.447  29.747 -37.211  1.00 25.55           O  
ANISOU 5838  O   ALA C 760     3167   3433   3108     72    104     45       O  
ATOM   5839  CB  ALA C 760     -60.432  30.693 -36.429  1.00 25.05           C  
ANISOU 5839  CB  ALA C 760     3024   3443   3051     50    122     13       C  
ATOM   5840  N   LYS C 761     -61.984  28.046 -37.252  1.00 24.87           N  
ANISOU 5840  N   LYS C 761     3079   3389   2981    121     84     21       N  
ATOM   5841  CA  LYS C 761     -62.804  27.261 -38.176  1.00 25.13           C  
ANISOU 5841  CA  LYS C 761     3142   3408   2998    136     78     27       C  
ATOM   5842  C   LYS C 761     -64.092  26.711 -37.582  1.00 23.02           C  
ANISOU 5842  C   LYS C 761     2910   3103   2735    127     65     23       C  
ATOM   5843  O   LYS C 761     -65.114  26.677 -38.269  1.00 21.60           O  
ANISOU 5843  O   LYS C 761     2743   2913   2553    118     64     30       O  
ATOM   5844  CB  LYS C 761     -61.989  26.161 -38.842  1.00 25.84           C  
ANISOU 5844  CB  LYS C 761     3241   3521   3055    176     75     17       C  
ATOM   5845  CG  LYS C 761     -60.855  26.731 -39.684  1.00 28.62           C  
ANISOU 5845  CG  LYS C 761     3556   3917   3402    184     91     26       C  
ATOM   5846  CD  LYS C 761     -61.381  27.694 -40.726  1.00 30.36           C  
ANISOU 5846  CD  LYS C 761     3767   4137   3633    163    107     48       C  
ATOM   5847  CE  LYS C 761     -60.287  28.167 -41.631  1.00 35.86           C  
ANISOU 5847  CE  LYS C 761     4430   4874   4321    172    128     59       C  
ATOM   5848  NZ  LYS C 761     -60.490  29.601 -41.896  1.00 41.59           N  
ANISOU 5848  NZ  LYS C 761     5137   5593   5074    139    154     82       N  
ATOM   5849  N   VAL C 762     -64.060  26.283 -36.324  1.00 24.34           N  
ANISOU 5849  N   VAL C 762     3089   3254   2904    131     56     12       N  
ATOM   5850  CA  VAL C 762     -65.279  25.775 -35.656  1.00 23.85           C  
ANISOU 5850  CA  VAL C 762     3060   3156   2848    120     49     10       C  
ATOM   5851  C   VAL C 762     -66.322  26.890 -35.538  1.00 26.36           C  
ANISOU 5851  C   VAL C 762     3365   3460   3190     87     54     24       C  
ATOM   5852  O   VAL C 762     -67.503  26.718 -35.871  1.00 30.27           O  
ANISOU 5852  O   VAL C 762     3873   3943   3686     74     52     30       O  
ATOM   5853  CB  VAL C 762     -64.973  25.228 -34.258  1.00 23.62           C  
ANISOU 5853  CB  VAL C 762     3045   3115   2815    134     42      0       C  
ATOM   5854  CG1 VAL C 762     -66.269  24.871 -33.538  1.00 24.13           C  
ANISOU 5854  CG1 VAL C 762     3139   3142   2889    118     40      2       C  
ATOM   5855  CG2 VAL C 762     -64.085  24.014 -34.315  1.00 23.57           C  
ANISOU 5855  CG2 VAL C 762     3058   3117   2779    177     40    -10       C  
ATOM   5856  N   GLU C 763     -65.878  28.043 -35.084  1.00 28.66           N  
ANISOU 5856  N   GLU C 763     3631   3759   3500     74     64     29       N  
ATOM   5857  CA  GLU C 763     -66.731  29.217 -35.005  1.00 31.01           C  
ANISOU 5857  CA  GLU C 763     3921   4041   3820     50     77     45       C  
ATOM   5858  C   GLU C 763     -67.300  29.591 -36.361  1.00 26.25           C  
ANISOU 5858  C   GLU C 763     3312   3448   3213     51     86     66       C  
ATOM   5859  O   GLU C 763     -68.502  29.888 -36.489  1.00 25.89           O  
ANISOU 5859  O   GLU C 763     3271   3394   3171     45     89     80       O  
ATOM   5860  CB  GLU C 763     -65.875  30.405 -34.508  1.00 38.99           C  
ANISOU 5860  CB  GLU C 763     4908   5056   4849     34     93     42       C  
ATOM   5861  CG  GLU C 763     -66.439  31.795 -34.847  1.00 53.47           C  
ANISOU 5861  CG  GLU C 763     6737   6873   6706     15    119     63       C  
ATOM   5862  CD  GLU C 763     -65.662  32.964 -34.193  1.00 64.04           C  
ANISOU 5862  CD  GLU C 763     8062   8205   8067    -11    139     53       C  
ATOM   5863  OE1 GLU C 763     -64.518  33.316 -34.602  1.00 68.38           O  
ANISOU 5863  OE1 GLU C 763     8589   8774   8618    -21    151     46       O  
ATOM   5864  OE2 GLU C 763     -66.229  33.553 -33.241  1.00 73.77           O  
ANISOU 5864  OE2 GLU C 763     9306   9410   9314    -25    145     49       O  
ATOM   5865  N   MET C 764     -66.460  29.568 -37.386  1.00 22.80           N  
ANISOU 5865  N   MET C 764     2864   3036   2765     63     92     68       N  
ATOM   5866  CA  MET C 764     -66.993  29.752 -38.727  1.00 23.95           C  
ANISOU 5866  CA  MET C 764     3005   3198   2897     72     99     87       C  
ATOM   5867  C   MET C 764     -68.084  28.732 -39.059  1.00 23.06           C  
ANISOU 5867  C   MET C 764     2910   3087   2764     75     79     79       C  
ATOM   5868  O   MET C 764     -69.175  29.102 -39.542  1.00 22.63           O  
ANISOU 5868  O   MET C 764     2851   3042   2705     72     80     95       O  
ATOM   5869  CB  MET C 764     -65.920  29.615 -39.758  1.00 27.10           C  
ANISOU 5869  CB  MET C 764     3392   3626   3279     89    106     88       C  
ATOM   5870  CG  MET C 764     -66.460  29.713 -41.167  1.00 30.02           C  
ANISOU 5870  CG  MET C 764     3760   4020   3628    103    111    106       C  
ATOM   5871  SD  MET C 764     -65.235  29.193 -42.348  1.00 40.99           S  
ANISOU 5871  SD  MET C 764     5140   5444   4989    129    116    102       S  
ATOM   5872  CE  MET C 764     -65.439  27.428 -42.224  1.00 37.79           C  
ANISOU 5872  CE  MET C 764     4766   5034   4558    141     85     66       C  
ATOM   5873  N   LEU C 765     -67.821  27.464 -38.801  1.00 21.80           N  
ANISOU 5873  N   LEU C 765     2772   2921   2591     81     63     55       N  
ATOM   5874  CA  LEU C 765     -68.841  26.437 -39.098  1.00 22.33           C  
ANISOU 5874  CA  LEU C 765     2860   2984   2641     73     48     40       C  
ATOM   5875  C   LEU C 765     -70.134  26.672 -38.324  1.00 22.74           C  
ANISOU 5875  C   LEU C 765     2912   3020   2707     50     45     47       C  
ATOM   5876  O   LEU C 765     -71.204  26.468 -38.880  1.00 22.07           O  
ANISOU 5876  O   LEU C 765     2823   2951   2611     38     38     46       O  
ATOM   5877  CB  LEU C 765     -68.314  25.046 -38.809  1.00 21.89           C  
ANISOU 5877  CB  LEU C 765     2836   2910   2570     84     40     14       C  
ATOM   5878  CG  LEU C 765     -67.226  24.489 -39.724  1.00 23.33           C  
ANISOU 5878  CG  LEU C 765     3024   3110   2728    112     42      4       C  
ATOM   5879  CD1 LEU C 765     -66.881  23.042 -39.327  1.00 23.19           C  
ANISOU 5879  CD1 LEU C 765     3050   3066   2696    128     39    -20       C  
ATOM   5880  CD2 LEU C 765     -67.675  24.539 -41.167  1.00 24.03           C  
ANISOU 5880  CD2 LEU C 765     3105   3230   2795    112     40      5       C  
ATOM   5881  N   ASP C 766     -70.039  27.097 -37.058  1.00 23.04           N  
ANISOU 5881  N   ASP C 766     2952   3035   2769     45     50     51       N  
ATOM   5882  CA  ASP C 766     -71.245  27.384 -36.273  1.00 25.57           C  
ANISOU 5882  CA  ASP C 766     3272   3342   3103     27     50     59       C  
ATOM   5883  C   ASP C 766     -72.095  28.454 -36.968  1.00 27.40           C  
ANISOU 5883  C   ASP C 766     3478   3598   3335     27     59     85       C  
ATOM   5884  O   ASP C 766     -73.317  28.306 -37.112  1.00 28.17           O  
ANISOU 5884  O   ASP C 766     3568   3709   3425     16     54     89       O  
ATOM   5885  CB  ASP C 766     -70.912  27.886 -34.863  1.00 26.22           C  
ANISOU 5885  CB  ASP C 766     3358   3399   3206     25     57     61       C  
ATOM   5886  CG  ASP C 766     -70.190  26.846 -34.015  1.00 31.11           C  
ANISOU 5886  CG  ASP C 766     4000   4000   3819     34     49     40       C  
ATOM   5887  OD1 ASP C 766     -70.201  25.621 -34.349  1.00 34.05           O  
ANISOU 5887  OD1 ASP C 766     4396   4366   4174     38     42     26       O  
ATOM   5888  OD2 ASP C 766     -69.513  27.271 -33.056  1.00 31.08           O  
ANISOU 5888  OD2 ASP C 766     3994   3991   3825     40     52     38       O  
ATOM   5889  N   ASN C 767     -71.434  29.506 -37.444  1.00 25.16           N  
ANISOU 5889  N   ASN C 767     3180   3321   3057     40     76    103       N  
ATOM   5890  CA  ASN C 767     -72.141  30.574 -38.141  1.00 24.87           C  
ANISOU 5890  CA  ASN C 767     3125   3305   3018     51     91    134       C  
ATOM   5891  C   ASN C 767     -72.693  30.085 -39.493  1.00 23.70           C  
ANISOU 5891  C   ASN C 767     2966   3202   2839     61     79    136       C  
ATOM   5892  O   ASN C 767     -73.823  30.410 -39.881  1.00 21.51           O  
ANISOU 5892  O   ASN C 767     2672   2954   2548     67     79    153       O  
ATOM   5893  CB  ASN C 767     -71.210  31.779 -38.261  1.00 26.29           C  
ANISOU 5893  CB  ASN C 767     3302   3473   3216     60    119    152       C  
ATOM   5894  CG  ASN C 767     -71.901  33.053 -38.788  1.00 31.56           C  
ANISOU 5894  CG  ASN C 767     3960   4147   3885     78    146    191       C  
ATOM   5895  OD1 ASN C 767     -73.151  33.257 -38.688  1.00 31.75           O  
ANISOU 5895  OD1 ASN C 767     3979   4182   3902     86    145    207       O  
ATOM   5896  ND2 ASN C 767     -71.073  33.961 -39.298  1.00 33.07           N  
ANISOU 5896  ND2 ASN C 767     4151   4330   4085     85    174    209       N  
ATOM   5897  N   LEU C 768     -71.918  29.262 -40.193  1.00 23.89           N  
ANISOU 5897  N   LEU C 768     2996   3236   2845     64     69    116       N  
ATOM   5898  CA  LEU C 768     -72.395  28.691 -41.469  1.00 26.86           C  
ANISOU 5898  CA  LEU C 768     3363   3656   3185     71     56    109       C  
ATOM   5899  C   LEU C 768     -73.648  27.861 -41.260  1.00 27.96           C  
ANISOU 5899  C   LEU C 768     3503   3808   3313     46     36     89       C  
ATOM   5900  O   LEU C 768     -74.586  27.916 -42.049  1.00 29.94           O  
ANISOU 5900  O   LEU C 768     3731   4107   3539     48     28     93       O  
ATOM   5901  CB  LEU C 768     -71.320  27.824 -42.119  1.00 27.40           C  
ANISOU 5901  CB  LEU C 768     3447   3727   3236     79     49     85       C  
ATOM   5902  CG  LEU C 768     -70.165  28.534 -42.800  1.00 28.21           C  
ANISOU 5902  CG  LEU C 768     3541   3841   3337    104     68    105       C  
ATOM   5903  CD1 LEU C 768     -69.259  27.541 -43.508  1.00 30.76           C  
ANISOU 5903  CD1 LEU C 768     3876   4174   3636    116     60     80       C  
ATOM   5904  CD2 LEU C 768     -70.642  29.571 -43.772  1.00 29.33           C  
ANISOU 5904  CD2 LEU C 768     3661   4019   3465    125     84    141       C  
ATOM   5905  N   LEU C 769     -73.672  27.104 -40.181  1.00 29.91           N  
ANISOU 5905  N   LEU C 769     3771   4015   3576     23     29     67       N  
ATOM   5906  CA  LEU C 769     -74.802  26.250 -39.870  1.00 32.70           C  
ANISOU 5906  CA  LEU C 769     4128   4372   3924     -9     16     46       C  
ATOM   5907  C   LEU C 769     -76.099  27.049 -39.769  1.00 31.83           C  
ANISOU 5907  C   LEU C 769     3984   4296   3813    -11     18     70       C  
ATOM   5908  O   LEU C 769     -77.104  26.709 -40.370  1.00 32.20           O  
ANISOU 5908  O   LEU C 769     4009   4389   3837    -27      5     60       O  
ATOM   5909  CB  LEU C 769     -74.532  25.580 -38.535  1.00 36.03           C  
ANISOU 5909  CB  LEU C 769     4582   4739   4369    -25     19     31       C  
ATOM   5910  CG  LEU C 769     -75.205  24.278 -38.117  1.00 41.75           C  
ANISOU 5910  CG  LEU C 769     5331   5443   5090    -61     13      1       C  
ATOM   5911  CD1 LEU C 769     -76.369  24.517 -37.136  1.00 46.02           C  
ANISOU 5911  CD1 LEU C 769     5858   5981   5647    -83     16     13       C  
ATOM   5912  CD2 LEU C 769     -75.672  23.495 -39.327  1.00 42.38           C  
ANISOU 5912  CD2 LEU C 769     5408   5556   5140    -81      0    -27       C  
ATOM   5913  N   ASP C 770     -76.074  28.112 -38.977  1.00 32.10           N  
ANISOU 5913  N   ASP C 770     4013   4311   3872      4     35    100       N  
ATOM   5914  CA  ASP C 770     -77.259  28.939 -38.782  1.00 29.78           C  
ANISOU 5914  CA  ASP C 770     3690   4045   3578     12     42    127       C  
ATOM   5915  C   ASP C 770     -77.608  29.739 -40.016  1.00 29.16           C  
ANISOU 5915  C   ASP C 770     3583   4024   3473     44     46    154       C  
ATOM   5916  O   ASP C 770     -78.803  29.995 -40.296  1.00 28.90           O  
ANISOU 5916  O   ASP C 770     3517   4043   3420     51     43    168       O  
ATOM   5917  CB  ASP C 770     -77.052  29.871 -37.592  1.00 34.92           C  
ANISOU 5917  CB  ASP C 770     4353   4653   4261     23     62    148       C  
ATOM   5918  CG  ASP C 770     -77.365  29.192 -36.228  1.00 38.82           C  
ANISOU 5918  CG  ASP C 770     4865   5112   4774     -5     58    130       C  
ATOM   5919  OD1 ASP C 770     -78.290  28.341 -36.170  1.00 40.60           O  
ANISOU 5919  OD1 ASP C 770     5082   5357   4989    -32     46    115       O  
ATOM   5920  OD2 ASP C 770     -76.683  29.521 -35.237  1.00 38.48           O  
ANISOU 5920  OD2 ASP C 770     4843   5025   4753     -1     68    131       O  
ATOM   5921  N   ILE C 771     -76.594  30.090 -40.811  1.00 27.24           N  
ANISOU 5921  N   ILE C 771     3348   3779   3224     67     55    163       N  
ATOM   5922  CA  ILE C 771     -76.877  30.660 -42.123  1.00 27.87           C  
ANISOU 5922  CA  ILE C 771     3402   3917   3270    101     59    188       C  
ATOM   5923  C   ILE C 771     -77.648  29.664 -43.032  1.00 27.29           C  
ANISOU 5923  C   ILE C 771     3306   3909   3155     85     29    159       C  
ATOM   5924  O   ILE C 771     -78.639  30.039 -43.671  1.00 28.15           O  
ANISOU 5924  O   ILE C 771     3378   4085   3232    105     25    177       O  
ATOM   5925  CB  ILE C 771     -75.600  31.190 -42.796  1.00 27.54           C  
ANISOU 5925  CB  ILE C 771     3374   3859   3230    126     78    203       C  
ATOM   5926  CG1 ILE C 771     -75.188  32.492 -42.123  1.00 27.40           C  
ANISOU 5926  CG1 ILE C 771     3370   3796   3246    142    113    238       C  
ATOM   5927  CG2 ILE C 771     -75.836  31.445 -44.271  1.00 27.60           C  
ANISOU 5927  CG2 ILE C 771     3360   3933   3195    161     78    222       C  
ATOM   5928  CD1 ILE C 771     -73.746  32.860 -42.324  1.00 27.77           C  
ANISOU 5928  CD1 ILE C 771     3433   3809   3309    146    134    241       C  
ATOM   5929  N   GLU C 772     -77.211  28.416 -43.078  1.00 29.20           N  
ANISOU 5929  N   GLU C 772     3568   4133   3394     52     11    114       N  
ATOM   5930  CA  GLU C 772     -77.933  27.377 -43.851  1.00 30.64           C  
ANISOU 5930  CA  GLU C 772     3735   4368   3539     24    -16     75       C  
ATOM   5931  C   GLU C 772     -79.394  27.295 -43.364  1.00 30.70           C  
ANISOU 5931  C   GLU C 772     3710   4412   3542     -2    -25     72       C  
ATOM   5932  O   GLU C 772     -80.320  27.202 -44.181  1.00 30.74           O  
ANISOU 5932  O   GLU C 772     3675   4497   3508     -4    -41     65       O  
ATOM   5933  CB  GLU C 772     -77.239  26.025 -43.728  1.00 32.09           C  
ANISOU 5933  CB  GLU C 772     3958   4506   3727    -10    -26     26       C  
ATOM   5934  CG  GLU C 772     -77.787  24.854 -44.575  1.00 34.66           C  
ANISOU 5934  CG  GLU C 772     4281   4873   4015    -45    -48    -24       C  
ATOM   5935  CD  GLU C 772     -79.149  24.296 -44.120  1.00 35.82           C  
ANISOU 5935  CD  GLU C 772     4407   5043   4159    -97    -60    -48       C  
ATOM   5936  OE1 GLU C 772     -79.404  24.186 -42.896  1.00 35.34           O  
ANISOU 5936  OE1 GLU C 772     4360   4935   4135   -119    -51    -44       O  
ATOM   5937  OE2 GLU C 772     -79.959  23.945 -45.007  1.00 39.67           O  
ANISOU 5937  OE2 GLU C 772     4863   5602   4608   -117    -79    -75       O  
ATOM   5938  N   VAL C 773     -79.609  27.354 -42.052  1.00 27.89           N  
ANISOU 5938  N   VAL C 773     3367   4008   3223    -20    -15     78       N  
ATOM   5939  CA  VAL C 773     -80.973  27.297 -41.525  1.00 27.84           C  
ANISOU 5939  CA  VAL C 773     3328   4037   3215    -44    -21     78       C  
ATOM   5940  C   VAL C 773     -81.810  28.459 -42.030  1.00 29.17           C  
ANISOU 5940  C   VAL C 773     3447   4278   3357      2    -15    122       C  
ATOM   5941  O   VAL C 773     -82.951  28.284 -42.472  1.00 31.26           O  
ANISOU 5941  O   VAL C 773     3665   4623   3590     -9    -30    114       O  
ATOM   5942  CB  VAL C 773     -80.989  27.302 -39.990  1.00 28.11           C  
ANISOU 5942  CB  VAL C 773     3386   4004   3291    -60     -6     85       C  
ATOM   5943  CG1 VAL C 773     -82.411  27.478 -39.466  1.00 25.71           C  
ANISOU 5943  CG1 VAL C 773     3042   3744   2984    -74     -6     95       C  
ATOM   5944  CG2 VAL C 773     -80.359  26.013 -39.449  1.00 27.27           C  
ANISOU 5944  CG2 VAL C 773     3327   3834   3203   -103    -10     43       C  
ATOM   5945  N   ALA C 774     -81.241  29.652 -41.971  1.00 30.13           N  
ANISOU 5945  N   ALA C 774     3580   4374   3492     54      9    167       N  
ATOM   5946  CA  ALA C 774     -81.921  30.834 -42.411  1.00 29.06           C  
ANISOU 5946  CA  ALA C 774     3411   4296   3335    108     24    215       C  
ATOM   5947  C   ALA C 774     -82.245  30.727 -43.899  1.00 32.36           C  
ANISOU 5947  C   ALA C 774     3793   4804   3697    130      7    214       C  
ATOM   5948  O   ALA C 774     -83.358  31.040 -44.328  1.00 30.98           O  
ANISOU 5948  O   ALA C 774     3568   4716   3485    154      0    231       O  
ATOM   5949  CB  ALA C 774     -81.062  32.065 -42.140  1.00 29.47           C  
ANISOU 5949  CB  ALA C 774     3496   4288   3414    153     60    259       C  
ATOM   5950  N   TYR C 775     -81.258  30.305 -44.682  1.00 33.86           N  
ANISOU 5950  N   TYR C 775     4006   4981   3878    128      0    195       N  
ATOM   5951  CA  TYR C 775     -81.430  30.215 -46.109  1.00 35.27           C  
ANISOU 5951  CA  TYR C 775     4156   5245   4002    153    -14    192       C  
ATOM   5952  C   TYR C 775     -82.489  29.184 -46.487  1.00 35.50           C  
ANISOU 5952  C   TYR C 775     4143   5352   3993    108    -51    144       C  
ATOM   5953  O   TYR C 775     -83.292  29.441 -47.389  1.00 34.09           O  
ANISOU 5953  O   TYR C 775     3915   5276   3762    136    -63    154       O  
ATOM   5954  CB  TYR C 775     -80.115  29.895 -46.820  1.00 33.51           C  
ANISOU 5954  CB  TYR C 775     3968   4988   3777    157    -12    178       C  
ATOM   5955  CG  TYR C 775     -80.212  30.205 -48.257  1.00 34.71           C  
ANISOU 5955  CG  TYR C 775     4093   5223   3871    204    -17    194       C  
ATOM   5956  CD1 TYR C 775     -80.271  31.510 -48.667  1.00 36.11           C  
ANISOU 5956  CD1 TYR C 775     4260   5425   4036    272     13    258       C  
ATOM   5957  CD2 TYR C 775     -80.311  29.190 -49.224  1.00 37.60           C  
ANISOU 5957  CD2 TYR C 775     4446   5648   4193    181    -48    145       C  
ATOM   5958  CE1 TYR C 775     -80.416  31.845 -50.001  1.00 38.12           C  
ANISOU 5958  CE1 TYR C 775     4489   5763   4232    324     12    280       C  
ATOM   5959  CE2 TYR C 775     -80.448  29.514 -50.576  1.00 40.92           C  
ANISOU 5959  CE2 TYR C 775     4838   6156   4553    229    -53    161       C  
ATOM   5960  CZ  TYR C 775     -80.481  30.856 -50.947  1.00 39.49           C  
ANISOU 5960  CZ  TYR C 775     4646   6001   4359    304    -22    232       C  
ATOM   5961  OH  TYR C 775     -80.566  31.216 -52.257  1.00 44.55           O  
ANISOU 5961  OH  TYR C 775     5262   6727   4938    360    -22    255       O  
ATOM   5962  N   SER C 776     -82.473  28.029 -45.828  1.00 34.17           N  
ANISOU 5962  N   SER C 776     3996   5139   3849     38    -65     91       N  
ATOM   5963  CA  SER C 776     -83.508  26.996 -46.055  1.00 37.08           C  
ANISOU 5963  CA  SER C 776     4329   5571   4189    -21    -94     39       C  
ATOM   5964  C   SER C 776     -84.915  27.476 -45.741  1.00 35.65           C  
ANISOU 5964  C   SER C 776     4086   5467   3991    -16    -97     60       C  
ATOM   5965  O   SER C 776     -85.847  27.215 -46.480  1.00 38.24           O  
ANISOU 5965  O   SER C 776     4358   5900   4270    -28   -121     38       O  
ATOM   5966  CB  SER C 776     -83.247  25.788 -45.190  1.00 39.03           C  
ANISOU 5966  CB  SER C 776     4619   5736   4473    -93    -96    -11       C  
ATOM   5967  OG  SER C 776     -82.118  25.131 -45.674  1.00 43.20           O  
ANISOU 5967  OG  SER C 776     5196   6216   5003    -99    -98    -40       O  
ATOM   5968  N   LEU C 777     -85.070  28.179 -44.633  1.00 35.82           N  
ANISOU 5968  N   LEU C 777     4116   5442   4052      2    -74    100       N  
ATOM   5969  CA  LEU C 777     -86.380  28.694 -44.271  1.00 37.07           C  
ANISOU 5969  CA  LEU C 777     4216   5672   4195     15    -73    125       C  
ATOM   5970  C   LEU C 777     -86.889  29.613 -45.353  1.00 37.63           C  
ANISOU 5970  C   LEU C 777     4237   5851   4210     88    -75    166       C  
ATOM   5971  O   LEU C 777     -88.050  29.540 -45.748  1.00 41.81           O  
ANISOU 5971  O   LEU C 777     4699   6493   4695     87    -93    160       O  
ATOM   5972  CB  LEU C 777     -86.332  29.423 -42.943  1.00 34.92           C  
ANISOU 5972  CB  LEU C 777     3970   5326   3972     35    -43    165       C  
ATOM   5973  CG  LEU C 777     -86.262  28.555 -41.679  1.00 35.70           C  
ANISOU 5973  CG  LEU C 777     4102   5344   4117    -32    -40    132       C  
ATOM   5974  CD1 LEU C 777     -86.147  29.471 -40.461  1.00 33.41           C  
ANISOU 5974  CD1 LEU C 777     3837   4989   3868      2    -10    176       C  
ATOM   5975  CD2 LEU C 777     -87.475  27.640 -41.541  1.00 35.96           C  
ANISOU 5975  CD2 LEU C 777     4087   5441   4134    -97    -59     93       C  
ATOM   5976  N   LEU C 778     -86.007  30.486 -45.800  1.00 39.42           N  
ANISOU 5976  N   LEU C 778     4496   6044   4438    153    -53    208       N  
ATOM   5977  CA  LEU C 778     -86.341  31.500 -46.766  1.00 42.22           C  
ANISOU 5977  CA  LEU C 778     4816   6483   4743    236    -44    260       C  
ATOM   5978  C   LEU C 778     -86.727  30.857 -48.109  1.00 44.51           C  
ANISOU 5978  C   LEU C 778     5058   6888   4964    229    -80    224       C  
ATOM   5979  O   LEU C 778     -87.686  31.280 -48.752  1.00 44.65           O  
ANISOU 5979  O   LEU C 778     5012   7026   4924    274    -89    247       O  
ATOM   5980  CB  LEU C 778     -85.153  32.436 -46.923  1.00 43.31           C  
ANISOU 5980  CB  LEU C 778     5011   6542   4905    292     -7    307       C  
ATOM   5981  CG  LEU C 778     -85.370  33.818 -47.528  1.00 48.62           C  
ANISOU 5981  CG  LEU C 778     5671   7257   5545    391     25    381       C  
ATOM   5982  CD1 LEU C 778     -86.487  34.618 -46.863  1.00 47.77           C  
ANISOU 5982  CD1 LEU C 778     5533   7184   5433    433     44    425       C  
ATOM   5983  CD2 LEU C 778     -84.050  34.579 -47.431  1.00 50.45           C  
ANISOU 5983  CD2 LEU C 778     5970   7382   5818    419     66    415       C  
ATOM   5984  N   ARG C 779     -85.997  29.826 -48.505  1.00 43.49           N  
ANISOU 5984  N   ARG C 779     4958   6726   4839    174   -100    167       N  
ATOM   5985  CA  ARG C 779     -86.271  29.120 -49.747  1.00 47.45           C  
ANISOU 5985  CA  ARG C 779     5424   7329   5277    158   -134    122       C  
ATOM   5986  C   ARG C 779     -87.518  28.198 -49.674  1.00 50.81           C  
ANISOU 5986  C   ARG C 779     5789   7842   5676     87   -169     63       C  
ATOM   5987  O   ARG C 779     -88.148  27.958 -50.701  1.00 51.72           O  
ANISOU 5987  O   ARG C 779     5848   8081   5725     89   -197     38       O  
ATOM   5988  CB  ARG C 779     -85.020  28.330 -50.215  1.00 45.35           C  
ANISOU 5988  CB  ARG C 779     5216   6993   5023    128   -139     80       C  
ATOM   5989  N   GLY C 780     -87.866  27.679 -48.493  1.00 53.42           N  
ANISOU 5989  N   GLY C 780     6128   8113   6055     21   -165     40       N  
ATOM   5990  CA  GLY C 780     -89.145  26.955 -48.272  1.00 56.35           C  
ANISOU 5990  CA  GLY C 780     6438   8566   6407    -49   -189     -6       C  
ATOM   5991  C   GLY C 780     -90.404  27.808 -48.485  1.00 62.07           C  
ANISOU 5991  C   GLY C 780     7074   9428   7082      5   -195     36       C  
ATOM   5992  O   GLY C 780     -90.388  29.014 -48.239  1.00 68.02           O  
ANISOU 5992  O   GLY C 780     7829  10175   7841     92   -168    111       O  
ATOM   5993  N   GLY C 781     -91.502  27.183 -48.926  1.00 70.39           N  
ANISOU 5993  N   GLY C 781     8051  10607   8086    -45   -227    -13       N  
ATOM   5994  CA  GLY C 781     -92.653  27.900 -49.530  1.00 71.98           C  
ANISOU 5994  CA  GLY C 781     8156  10977   8218     16   -241     20       C  
ATOM   5995  C   GLY C 781     -93.911  28.038 -48.686  1.00 71.85           C  
ANISOU 5995  C   GLY C 781     8072  11024   8204     -3   -238     31       C  
ATOM   5996  O   GLY C 781     -93.862  28.031 -47.452  1.00 75.82           O  
ANISOU 5996  O   GLY C 781     8611  11427   8771    -30   -213     45       O  
ATOM   5997  N   SER C 785     -98.886  33.443 -52.387  1.00 62.28           N  
ANISOU 5997  N   SER C 785     6393  10737   6535    628   -248    369       N  
ATOM   5998  CA  SER C 785     -99.689  33.541 -51.176  1.00 68.32           C  
ANISOU 5998  CA  SER C 785     7127  11494   7337    604   -232    381       C  
ATOM   5999  C   SER C 785    -100.236  34.961 -50.989  1.00 69.73           C  
ANISOU 5999  C   SER C 785     7289  11722   7485    759   -189    490       C  
ATOM   6000  O   SER C 785     -99.667  35.934 -51.494  1.00 74.42           O  
ANISOU 6000  O   SER C 785     7936  12279   8062    874   -154    563       O  
ATOM   6001  CB  SER C 785     -98.869  33.131 -49.943  1.00 69.30           C  
ANISOU 6001  CB  SER C 785     7353  11403   7575    515   -207    358       C  
ATOM   6002  OG  SER C 785     -99.468  33.591 -48.728  1.00 68.70           O  
ANISOU 6002  OG  SER C 785     7270  11296   7538    531   -176    398       O  
ATOM   6003  N   SER C 786    -101.328  35.062 -50.233  1.00 69.37           N  
ANISOU 6003  N   SER C 786     7172  11751   7433    758   -185    502       N  
ATOM   6004  CA  SER C 786    -102.013  36.348 -49.955  1.00 67.79           C  
ANISOU 6004  CA  SER C 786     6948  11609   7200    905   -142    603       C  
ATOM   6005  C   SER C 786    -101.119  37.343 -49.205  1.00 64.67           C  
ANISOU 6005  C   SER C 786     6682  11013   6879    973    -76    675       C  
ATOM   6006  O   SER C 786    -101.244  38.553 -49.395  1.00 60.07           O  
ANISOU 6006  O   SER C 786     6116  10444   6262   1117    -31    766       O  
ATOM   6007  CB  SER C 786    -103.275  36.096 -49.129  1.00 63.58           C  
ANISOU 6007  CB  SER C 786     6320  11177   6660    868   -151    590       C  
ATOM   6008  N   LYS C 787    -100.215  36.823 -48.364  1.00 64.84           N  
ANISOU 6008  N   LYS C 787     6793  10847   6996    871    -67    633       N  
ATOM   6009  CA  LYS C 787     -99.567  37.648 -47.344  1.00 58.89           C  
ANISOU 6009  CA  LYS C 787     6145   9912   6318    911     -8    686       C  
ATOM   6010  C   LYS C 787     -98.335  38.368 -47.872  1.00 53.12           C  
ANISOU 6010  C   LYS C 787     5516   9061   5605    975     27    729       C  
ATOM   6011  O   LYS C 787     -97.627  37.902 -48.780  1.00 51.62           O  
ANISOU 6011  O   LYS C 787     5343   8869   5402    944      2    696       O  
ATOM   6012  CB  LYS C 787     -99.253  36.832 -46.066  1.00 58.97           C  
ANISOU 6012  CB  LYS C 787     6198   9788   6419    781    -12    627       C  
ATOM   6013  N   ASP C 788     -98.133  39.555 -47.324  1.00 50.38           N  
ANISOU 6013  N   ASP C 788     5237   8620   5285   1069     89    806       N  
ATOM   6014  CA  ASP C 788     -96.872  40.275 -47.463  1.00 55.88           C  
ANISOU 6014  CA  ASP C 788     6048   9162   6024   1109    135    843       C  
ATOM   6015  C   ASP C 788     -95.711  39.305 -47.142  1.00 55.69           C  
ANISOU 6015  C   ASP C 788     6084   9001   6074    975    110    766       C  
ATOM   6016  O   ASP C 788     -95.811  38.521 -46.198  1.00 54.77           O  
ANISOU 6016  O   ASP C 788     5964   8839   6007    875     89    711       O  
ATOM   6017  CB  ASP C 788     -96.892  41.441 -46.477  1.00 58.43           C  
ANISOU 6017  CB  ASP C 788     6437   9377   6386   1184    203    911       C  
ATOM   6018  CG  ASP C 788     -95.694  42.383 -46.622  1.00 61.32           C  
ANISOU 6018  CG  ASP C 788     6919   9589   6791   1235    261    958       C  
ATOM   6019  OD1 ASP C 788     -95.799  43.567 -46.230  1.00 64.24           O  
ANISOU 6019  OD1 ASP C 788     7340   9900   7167   1332    326   1029       O  
ATOM   6020  OD2 ASP C 788     -94.637  41.926 -47.081  1.00 61.67           O  
ANISOU 6020  OD2 ASP C 788     7004   9565   6861   1175    246    921       O  
ATOM   6021  N   PRO C 789     -94.632  39.312 -47.952  1.00 58.31           N  
ANISOU 6021  N   PRO C 789     6469   9276   6409    975    113    763       N  
ATOM   6022  CA  PRO C 789     -93.503  38.397 -47.688  1.00 56.13           C  
ANISOU 6022  CA  PRO C 789     6250   8879   6200    859     91    694       C  
ATOM   6023  C   PRO C 789     -92.885  38.514 -46.290  1.00 53.63           C  
ANISOU 6023  C   PRO C 789     6011   8394   5974    808    121    685       C  
ATOM   6024  O   PRO C 789     -92.446  37.509 -45.735  1.00 49.86           O  
ANISOU 6024  O   PRO C 789     5549   7852   5544    700     92    619       O  
ATOM   6025  CB  PRO C 789     -92.480  38.780 -48.766  1.00 56.43           C  
ANISOU 6025  CB  PRO C 789     6337   8883   6221    904    107    718       C  
ATOM   6026  CG  PRO C 789     -93.312  39.263 -49.899  1.00 57.03           C  
ANISOU 6026  CG  PRO C 789     6344   9123   6201   1008    104    765       C  
ATOM   6027  CD  PRO C 789     -94.489  39.969 -49.269  1.00 59.21           C  
ANISOU 6027  CD  PRO C 789     6579   9462   6456   1078    127    816       C  
ATOM   6028  N   ILE C 790     -92.845  39.722 -45.742  1.00 52.89           N  
ANISOU 6028  N   ILE C 790     5967   8229   5901    887    179    751       N  
ATOM   6029  CA  ILE C 790     -92.363  39.910 -44.386  1.00 55.09           C  
ANISOU 6029  CA  ILE C 790     6313   8361   6257    846    207    743       C  
ATOM   6030  C   ILE C 790     -93.180  39.031 -43.427  1.00 54.71           C  
ANISOU 6030  C   ILE C 790     6214   8349   6225    770    173    695       C  
ATOM   6031  O   ILE C 790     -92.609  38.368 -42.567  1.00 50.74           O  
ANISOU 6031  O   ILE C 790     5749   7748   5782    680    163    646       O  
ATOM   6032  CB  ILE C 790     -92.430  41.392 -43.968  1.00 56.33           C  
ANISOU 6032  CB  ILE C 790     6524   8456   6423    949    277    821       C  
ATOM   6033  CG1 ILE C 790     -91.388  42.212 -44.736  1.00 58.69           C  
ANISOU 6033  CG1 ILE C 790     6893   8680   6726   1002    319    862       C  
ATOM   6034  CG2 ILE C 790     -92.151  41.549 -42.487  1.00 57.26           C  
ANISOU 6034  CG2 ILE C 790     6698   8444   6612    905    301    806       C  
ATOM   6035  CD1 ILE C 790     -91.785  43.664 -44.946  1.00 63.21           C  
ANISOU 6035  CD1 ILE C 790     7495   9253   7268   1134    387    952       C  
ATOM   6036  N   ASP C 791     -94.503  39.012 -43.600  1.00 54.53           N  
ANISOU 6036  N   ASP C 791     6104   8470   6146    806    159    710       N  
ATOM   6037  CA  ASP C 791     -95.387  38.178 -42.777  1.00 52.29           C  
ANISOU 6037  CA  ASP C 791     5761   8237   5871    734    130    668       C  
ATOM   6038  C   ASP C 791     -95.138  36.681 -43.003  1.00 47.45           C  
ANISOU 6038  C   ASP C 791     5122   7637   5268    608     74    582       C  
ATOM   6039  O   ASP C 791     -95.248  35.880 -42.073  1.00 43.28           O  
ANISOU 6039  O   ASP C 791     4596   7067   4783    519     61    536       O  
ATOM   6040  CB  ASP C 791     -96.876  38.491 -43.031  1.00 56.86           C  
ANISOU 6040  CB  ASP C 791     6240   8986   6378    802    126    703       C  
ATOM   6041  CG  ASP C 791     -97.339  39.816 -42.407  1.00 62.92           C  
ANISOU 6041  CG  ASP C 791     7031   9731   7143    916    184    782       C  
ATOM   6042  OD1 ASP C 791     -98.571  40.045 -42.378  1.00 65.65           O  
ANISOU 6042  OD1 ASP C 791     7297  10209   7438    970    184    811       O  
ATOM   6043  OD2 ASP C 791     -96.507  40.642 -41.983  1.00 64.32           O  
ANISOU 6043  OD2 ASP C 791     7305   9768   7365    953    232    815       O  
ATOM   6044  N   VAL C 792     -94.824  36.292 -44.232  1.00 44.98           N  
ANISOU 6044  N   VAL C 792     4790   7384   4916    602     45    560       N  
ATOM   6045  CA  VAL C 792     -94.585  34.872 -44.523  1.00 46.46           C  
ANISOU 6045  CA  VAL C 792     4960   7583   5110    485     -4    476       C  
ATOM   6046  C   VAL C 792     -93.345  34.410 -43.769  1.00 46.43           C  
ANISOU 6046  C   VAL C 792     5050   7407   5185    415      5    442       C  
ATOM   6047  O   VAL C 792     -93.338  33.351 -43.166  1.00 44.65           O  
ANISOU 6047  O   VAL C 792     4826   7146   4992    316    -15    384       O  
ATOM   6048  CB  VAL C 792     -94.407  34.612 -46.028  1.00 50.56           C  
ANISOU 6048  CB  VAL C 792     5448   8196   5568    501    -34    460       C  
ATOM   6049  CG1 VAL C 792     -93.957  33.177 -46.305  1.00 49.27           C  
ANISOU 6049  CG1 VAL C 792     5288   8014   5417    382    -77    370       C  
ATOM   6050  CG2 VAL C 792     -95.709  34.914 -46.770  1.00 55.50           C  
ANISOU 6050  CG2 VAL C 792     5967   9014   6105    564    -51    484       C  
ATOM   6051  N   ASN C 793     -92.293  35.213 -43.831  1.00 45.19           N  
ANISOU 6051  N   ASN C 793     4969   7148   5055    466     38    480       N  
ATOM   6052  CA  ASN C 793     -91.035  34.849 -43.197  1.00 46.14           C  
ANISOU 6052  CA  ASN C 793     5171   7116   5242    408     47    450       C  
ATOM   6053  C   ASN C 793     -91.123  34.952 -41.657  1.00 41.60           C  
ANISOU 6053  C   ASN C 793     4629   6452   4725    382     69    452       C  
ATOM   6054  O   ASN C 793     -90.542  34.138 -40.973  1.00 37.09           O  
ANISOU 6054  O   ASN C 793     4096   5798   4200    305     59    407       O  
ATOM   6055  CB  ASN C 793     -89.901  35.709 -43.760  1.00 44.52           C  
ANISOU 6055  CB  ASN C 793     5029   6839   5046    467     77    489       C  
ATOM   6056  CG  ASN C 793     -89.558  35.371 -45.201  1.00 46.08           C  
ANISOU 6056  CG  ASN C 793     5208   7105   5196    476     52    475       C  
ATOM   6057  OD1 ASN C 793     -89.442  34.192 -45.581  1.00 49.47           O  
ANISOU 6057  OD1 ASN C 793     5619   7561   5617    403     12    412       O  
ATOM   6058  ND2 ASN C 793     -89.392  36.402 -46.019  1.00 45.61           N  
ANISOU 6058  ND2 ASN C 793     5157   7070   5103    569     81    534       N  
ATOM   6059  N   TYR C 794     -91.886  35.917 -41.145  1.00 39.75           N  
ANISOU 6059  N   TYR C 794     4380   6242   4482    450    100    505       N  
ATOM   6060  CA  TYR C 794     -92.190  35.994 -39.717  1.00 40.26           C  
ANISOU 6060  CA  TYR C 794     4463   6244   4588    429    119    507       C  
ATOM   6061  C   TYR C 794     -92.755  34.688 -39.219  1.00 40.90           C  
ANISOU 6061  C   TYR C 794     4502   6359   4677    333     85    449       C  
ATOM   6062  O   TYR C 794     -92.246  34.121 -38.259  1.00 41.41           O  
ANISOU 6062  O   TYR C 794     4612   6328   4792    271     86    418       O  
ATOM   6063  CB  TYR C 794     -93.173  37.099 -39.426  1.00 41.04           C  
ANISOU 6063  CB  TYR C 794     4535   6398   4662    521    153    569       C  
ATOM   6064  CG  TYR C 794     -93.738  37.095 -38.012  1.00 41.23           C  
ANISOU 6064  CG  TYR C 794     4561   6388   4716    502    170    569       C  
ATOM   6065  CD1 TYR C 794     -92.982  37.515 -36.958  1.00 39.95           C  
ANISOU 6065  CD1 TYR C 794     4478   6092   4609    497    200    572       C  
ATOM   6066  CD2 TYR C 794     -95.049  36.724 -37.764  1.00 40.67           C  
ANISOU 6066  CD2 TYR C 794     4410   6429   4616    493    156    567       C  
ATOM   6067  CE1 TYR C 794     -93.505  37.553 -35.692  1.00 40.44           C  
ANISOU 6067  CE1 TYR C 794     4543   6129   4695    488    216    574       C  
ATOM   6068  CE2 TYR C 794     -95.582  36.745 -36.497  1.00 40.23           C  
ANISOU 6068  CE2 TYR C 794     4354   6346   4584    481    174    571       C  
ATOM   6069  CZ  TYR C 794     -94.803  37.159 -35.457  1.00 41.49           C  
ANISOU 6069  CZ  TYR C 794     4598   6368   4798    480    205    575       C  
ATOM   6070  OH  TYR C 794     -95.310  37.185 -34.167  1.00 40.89           O  
ANISOU 6070  OH  TYR C 794     4527   6266   4745    472    224    579       O  
ATOM   6071  N   GLU C 795     -93.745  34.172 -39.919  1.00 41.03           N  
ANISOU 6071  N   GLU C 795     4436   6511   4644    318     55    433       N  
ATOM   6072  CA  GLU C 795     -94.395  32.915 -39.543  1.00 42.44           C  
ANISOU 6072  CA  GLU C 795     4569   6731   4827    219     26    376       C  
ATOM   6073  C   GLU C 795     -93.431  31.756 -39.550  1.00 41.41           C  
ANISOU 6073  C   GLU C 795     4489   6513   4731    127      6    313       C  
ATOM   6074  O   GLU C 795     -93.572  30.822 -38.756  1.00 39.42           O  
ANISOU 6074  O   GLU C 795     4244   6222   4511     45      1    273       O  
ATOM   6075  CB  GLU C 795     -95.622  32.622 -40.451  1.00 46.42           C  
ANISOU 6075  CB  GLU C 795     4965   7410   5261    218     -3    365       C  
ATOM   6076  CG  GLU C 795     -96.805  33.554 -40.156  1.00 50.27           C  
ANISOU 6076  CG  GLU C 795     5390   7996   5714    299     18    423       C  
ATOM   6077  CD  GLU C 795     -97.969  33.475 -41.146  1.00 57.54           C  
ANISOU 6077  CD  GLU C 795     6198   9108   6556    320    -10    422       C  
ATOM   6078  OE1 GLU C 795     -97.925  32.703 -42.131  1.00 64.64           O  
ANISOU 6078  OE1 GLU C 795     7062  10075   7423    269    -49    372       O  
ATOM   6079  OE2 GLU C 795     -98.971  34.190 -40.925  1.00 60.61           O  
ANISOU 6079  OE2 GLU C 795     6529   9590   6912    390      6    470       O  
ATOM   6080  N   LYS C 796     -92.455  31.786 -40.456  1.00 41.81           N  
ANISOU 6080  N   LYS C 796     4576   6534   4776    141     -3    306       N  
ATOM   6081  CA  LYS C 796     -91.454  30.706 -40.527  1.00 40.37           C  
ANISOU 6081  CA  LYS C 796     4446   6268   4624     64    -20    249       C  
ATOM   6082  C   LYS C 796     -90.562  30.596 -39.294  1.00 35.97           C  
ANISOU 6082  C   LYS C 796     3968   5568   4132     40      2    246       C  
ATOM   6083  O   LYS C 796     -90.020  29.528 -39.023  1.00 34.48           O  
ANISOU 6083  O   LYS C 796     3815   5316   3970    -31     -9    198       O  
ATOM   6084  CB  LYS C 796     -90.563  30.886 -41.742  1.00 44.62           C  
ANISOU 6084  CB  LYS C 796     5006   6806   5139     97    -30    249       C  
ATOM   6085  CG  LYS C 796     -91.243  30.566 -43.062  1.00 48.81           C  
ANISOU 6085  CG  LYS C 796     5466   7475   5603     97    -62    229       C  
ATOM   6086  CD  LYS C 796     -90.365  31.019 -44.213  1.00 50.88           C  
ANISOU 6086  CD  LYS C 796     5754   7739   5840    152    -63    246       C  
ATOM   6087  CE  LYS C 796     -91.012  30.775 -45.577  1.00 52.39           C  
ANISOU 6087  CE  LYS C 796     5874   8075   5956    163    -95    228       C  
ATOM   6088  NZ  LYS C 796     -90.189  31.395 -46.667  1.00 51.93           N  
ANISOU 6088  NZ  LYS C 796     5840   8020   5869    233    -88    258       N  
ATOM   6089  N   LEU C 797     -90.412  31.693 -38.559  1.00 33.57           N  
ANISOU 6089  N   LEU C 797     3693   5213   3850    101     34    296       N  
ATOM   6090  CA  LEU C 797     -89.655  31.690 -37.304  1.00 33.28           C  
ANISOU 6090  CA  LEU C 797     3722   5053   3868     84     55    294       C  
ATOM   6091  C   LEU C 797     -90.365  30.946 -36.192  1.00 32.61           C  
ANISOU 6091  C   LEU C 797     3625   4962   3803     26     56    273       C  
ATOM   6092  O   LEU C 797     -89.722  30.527 -35.255  1.00 32.68           O  
ANISOU 6092  O   LEU C 797     3687   4878   3852     -6     64    256       O  
ATOM   6093  CB  LEU C 797     -89.356  33.111 -36.824  1.00 31.50           C  
ANISOU 6093  CB  LEU C 797     3531   4779   3658    162     92    348       C  
ATOM   6094  CG  LEU C 797     -88.570  33.984 -37.792  1.00 32.80           C  
ANISOU 6094  CG  LEU C 797     3720   4933   3811    221    104    377       C  
ATOM   6095  CD1 LEU C 797     -88.516  35.412 -37.277  1.00 33.76           C  
ANISOU 6095  CD1 LEU C 797     3873   5010   3945    294    148    430       C  
ATOM   6096  CD2 LEU C 797     -87.169  33.454 -38.025  1.00 33.43           C  
ANISOU 6096  CD2 LEU C 797     3853   4933   3917    183     93    343       C  
ATOM   6097  N   LYS C 798     -91.680  30.770 -36.305  1.00 34.60           N  
ANISOU 6097  N   LYS C 798     3804   5317   4024     15     48    274       N  
ATOM   6098  CA  LYS C 798     -92.455  30.001 -35.342  1.00 34.68           C  
ANISOU 6098  CA  LYS C 798     3794   5332   4049    -46     51    253       C  
ATOM   6099  C   LYS C 798     -92.226  30.621 -33.946  1.00 34.65           C  
ANISOU 6099  C   LYS C 798     3839   5244   4084    -15     84    284       C  
ATOM   6100  O   LYS C 798     -92.032  29.933 -32.929  1.00 33.84           O  
ANISOU 6100  O   LYS C 798     3771   5073   4014    -64     92    264       O  
ATOM   6101  CB  LYS C 798     -92.064  28.500 -35.429  1.00 35.47           C  
ANISOU 6101  CB  LYS C 798     3918   5393   4165   -143     32    191       C  
ATOM   6102  N   THR C 799     -92.274  31.942 -33.907  1.00 33.52           N  
ANISOU 6102  N   THR C 799     3698   5106   3932     71    106    335       N  
ATOM   6103  CA  THR C 799     -91.970  32.693 -32.706  1.00 34.36           C  
ANISOU 6103  CA  THR C 799     3855   5131   4069    108    138    362       C  
ATOM   6104  C   THR C 799     -92.903  33.887 -32.661  1.00 36.53           C  
ANISOU 6104  C   THR C 799     4093   5470   4318    190    163    415       C  
ATOM   6105  O   THR C 799     -92.970  34.673 -33.610  1.00 37.05           O  
ANISOU 6105  O   THR C 799     4141   5581   4353    252    166    445       O  
ATOM   6106  CB  THR C 799     -90.501  33.193 -32.735  1.00 33.36           C  
ANISOU 6106  CB  THR C 799     3804   4900   3970    130    146    362       C  
ATOM   6107  OG1 THR C 799     -89.612  32.068 -32.804  1.00 37.44           O  
ANISOU 6107  OG1 THR C 799     4354   5363   4508     63    124    315       O  
ATOM   6108  CG2 THR C 799     -90.157  33.984 -31.499  1.00 34.81           C  
ANISOU 6108  CG2 THR C 799     4040   5003   4184    163    178    382       C  
ATOM   6109  N   ASP C 800     -93.602  34.053 -31.550  1.00 37.83           N  
ANISOU 6109  N   ASP C 800     4249   5633   4490    198    184    431       N  
ATOM   6110  CA  ASP C 800     -94.411  35.249 -31.363  1.00 39.16           C  
ANISOU 6110  CA  ASP C 800     4394   5848   4635    286    215    484       C  
ATOM   6111  C   ASP C 800     -93.492  36.405 -30.961  1.00 36.86           C  
ANISOU 6111  C   ASP C 800     4184   5453   4368    346    248    509       C  
ATOM   6112  O   ASP C 800     -92.726  36.273 -30.020  1.00 36.23           O  
ANISOU 6112  O   ASP C 800     4164   5274   4326    317    256    488       O  
ATOM   6113  CB  ASP C 800     -95.486  35.031 -30.302  1.00 40.77           C  
ANISOU 6113  CB  ASP C 800     4562   6091   4838    275    229    492       C  
ATOM   6114  CG  ASP C 800     -96.436  36.212 -30.206  1.00 41.90           C  
ANISOU 6114  CG  ASP C 800     4673   6300   4949    373    261    549       C  
ATOM   6115  OD1 ASP C 800     -97.407  36.233 -30.975  1.00 47.09           O  
ANISOU 6115  OD1 ASP C 800     5249   7082   5561    396    250    566       O  
ATOM   6116  OD2 ASP C 800     -96.194  37.132 -29.396  1.00 39.84           O  
ANISOU 6116  OD2 ASP C 800     4467   5966   4703    428    297    575       O  
ATOM   6117  N   ILE C 801     -93.554  37.516 -31.696  1.00 34.70           N  
ANISOU 6117  N   ILE C 801     3912   5202   4070    428    269    552       N  
ATOM   6118  CA  ILE C 801     -92.713  38.679 -31.422  1.00 34.62           C  
ANISOU 6118  CA  ILE C 801     3980   5092   4082    482    307    575       C  
ATOM   6119  C   ILE C 801     -93.584  39.917 -31.212  1.00 37.50           C  
ANISOU 6119  C   ILE C 801     4340   5487   4422    581    351    632       C  
ATOM   6120  O   ILE C 801     -94.323  40.303 -32.117  1.00 35.15           O  
ANISOU 6120  O   ILE C 801     3993   5284   4080    641    355    670       O  
ATOM   6121  CB  ILE C 801     -91.714  38.952 -32.572  1.00 34.80           C  
ANISOU 6121  CB  ILE C 801     4032   5086   4104    491    302    575       C  
ATOM   6122  CG1 ILE C 801     -90.922  37.683 -32.915  1.00 35.34           C  
ANISOU 6122  CG1 ILE C 801     4099   5137   4190    402    257    520       C  
ATOM   6123  CG2 ILE C 801     -90.767  40.077 -32.182  1.00 33.72           C  
ANISOU 6123  CG2 ILE C 801     3979   4835   3997    528    344    590       C  
ATOM   6124  CD1 ILE C 801     -89.931  37.847 -34.050  1.00 36.76           C  
ANISOU 6124  CD1 ILE C 801     4303   5296   4368    407    251    518       C  
ATOM   6125  N   LYS C 802     -93.465  40.541 -30.032  1.00 37.08           N  
ANISOU 6125  N   LYS C 802     4340   5354   4393    602    387    638       N  
ATOM   6126  CA  LYS C 802     -94.178  41.749 -29.703  1.00 38.34           C  
ANISOU 6126  CA  LYS C 802     4512   5522   4533    698    436    690       C  
ATOM   6127  C   LYS C 802     -93.201  42.839 -29.296  1.00 38.43           C  
ANISOU 6127  C   LYS C 802     4622   5404   4575    728    480    695       C  
ATOM   6128  O   LYS C 802     -92.199  42.580 -28.652  1.00 37.39           O  
ANISOU 6128  O   LYS C 802     4543   5180   4484    668    473    652       O  
ATOM   6129  CB  LYS C 802     -95.125  41.513 -28.532  1.00 42.18           C  
ANISOU 6129  CB  LYS C 802     4972   6040   5016    697    444    691       C  
ATOM   6130  CG  LYS C 802     -96.378  40.728 -28.867  1.00 46.35           C  
ANISOU 6130  CG  LYS C 802     5395   6710   5506    685    416    698       C  
ATOM   6131  CD  LYS C 802     -97.217  40.539 -27.604  1.00 50.20           C  
ANISOU 6131  CD  LYS C 802     5862   7216   5995    681    430    700       C  
ATOM   6132  CE  LYS C 802     -98.579  39.887 -27.875  1.00 54.52           C  
ANISOU 6132  CE  LYS C 802     6299   7913   6502    673    411    711       C  
ATOM   6133  NZ  LYS C 802     -98.495  38.416 -28.135  1.00 55.79           N  
ANISOU 6133  NZ  LYS C 802     6415   8108   6675    560    361    659       N  
ATOM   6134  N   VAL C 803     -93.523  44.074 -29.650  1.00 38.21           N  
ANISOU 6134  N   VAL C 803     4620   5373   4526    824    530    747       N  
ATOM   6135  CA  VAL C 803     -92.736  45.209 -29.265  1.00 37.98           C  
ANISOU 6135  CA  VAL C 803     4686   5220   4524    855    581    754       C  
ATOM   6136  C   VAL C 803     -93.073  45.554 -27.833  1.00 40.37           C  
ANISOU 6136  C   VAL C 803     5024   5476   4840    866    609    746       C  
ATOM   6137  O   VAL C 803     -94.233  45.614 -27.474  1.00 42.83           O  
ANISOU 6137  O   VAL C 803     5293   5860   5122    916    620    774       O  
ATOM   6138  CB  VAL C 803     -93.051  46.423 -30.155  1.00 39.49           C  
ANISOU 6138  CB  VAL C 803     4898   5421   4684    961    633    818       C  
ATOM   6139  CG1 VAL C 803     -92.279  47.651 -29.690  1.00 40.30           C  
ANISOU 6139  CG1 VAL C 803     5109   5386   4818    989    697    823       C  
ATOM   6140  CG2 VAL C 803     -92.719  46.097 -31.606  1.00 38.53           C  
ANISOU 6140  CG2 VAL C 803     4743   5353   4544    956    606    829       C  
ATOM   6141  N   VAL C 804     -92.055  45.781 -27.019  1.00 40.13           N  
ANISOU 6141  N   VAL C 804     5067   5331   4851    821    621    705       N  
ATOM   6142  CA  VAL C 804     -92.258  46.281 -25.682  1.00 39.01           C  
ANISOU 6142  CA  VAL C 804     4971   5133   4719    838    654    695       C  
ATOM   6143  C   VAL C 804     -92.281  47.813 -25.727  1.00 42.09           C  
ANISOU 6143  C   VAL C 804     5435   5453   5104    924    727    733       C  
ATOM   6144  O   VAL C 804     -91.355  48.452 -26.232  1.00 40.34           O  
ANISOU 6144  O   VAL C 804     5272   5152   4902    919    752    729       O  
ATOM   6145  CB  VAL C 804     -91.156  45.791 -24.746  1.00 37.48           C  
ANISOU 6145  CB  VAL C 804     4818   4856   4565    749    631    629       C  
ATOM   6146  CG1 VAL C 804     -91.282  46.452 -23.391  1.00 37.21           C  
ANISOU 6146  CG1 VAL C 804     4841   4760   4538    772    670    617       C  
ATOM   6147  CG2 VAL C 804     -91.203  44.266 -24.611  1.00 38.42           C  
ANISOU 6147  CG2 VAL C 804     4873   5038   4687    673    568    597       C  
ATOM   6148  N   ASP C 805     -93.354  48.397 -25.206  1.00 46.36           N  
ANISOU 6148  N   ASP C 805     5974   6022   5617   1005    766    770       N  
ATOM   6149  CA  ASP C 805     -93.540  49.843 -25.231  1.00 48.72           C  
ANISOU 6149  CA  ASP C 805     6346   6258   5906   1100    843    812       C  
ATOM   6150  C   ASP C 805     -92.370  50.524 -24.527  1.00 44.18           C  
ANISOU 6150  C   ASP C 805     5876   5535   5374   1057    876    765       C  
ATOM   6151  O   ASP C 805     -92.039  50.183 -23.389  1.00 41.51           O  
ANISOU 6151  O   ASP C 805     5556   5159   5057   1000    860    713       O  
ATOM   6152  CB  ASP C 805     -94.867  50.179 -24.531  1.00 55.82           C  
ANISOU 6152  CB  ASP C 805     7225   7214   6770   1184    873    850       C  
ATOM   6153  CG  ASP C 805     -95.255  51.633 -24.681  1.00 63.99           C  
ANISOU 6153  CG  ASP C 805     8329   8200   7784   1301    957    904       C  
ATOM   6154  OD1 ASP C 805     -95.244  52.373 -23.667  1.00 67.30           O  
ANISOU 6154  OD1 ASP C 805     8823   8536   8214   1327   1005    892       O  
ATOM   6155  OD2 ASP C 805     -95.592  52.030 -25.821  1.00 67.01           O  
ANISOU 6155  OD2 ASP C 805     8693   8630   8138   1372    975    961       O  
ATOM   6156  N   ARG C 806     -91.759  51.493 -25.200  1.00 45.76           N  
ANISOU 6156  N   ARG C 806     6144   5657   5586   1084    925    783       N  
ATOM   6157  CA  ARG C 806     -90.601  52.234 -24.679  1.00 46.89           C  
ANISOU 6157  CA  ARG C 806     6387   5660   5770   1038    963    736       C  
ATOM   6158  C   ARG C 806     -90.838  52.886 -23.314  1.00 50.93           C  
ANISOU 6158  C   ARG C 806     6962   6103   6285   1058   1005    713       C  
ATOM   6159  O   ARG C 806     -89.898  53.071 -22.551  1.00 54.00           O  
ANISOU 6159  O   ARG C 806     7409   6402   6707    990   1010    650       O  
ATOM   6160  CB  ARG C 806     -90.145  53.285 -25.701  1.00 49.68           C  
ANISOU 6160  CB  ARG C 806     6803   5945   6129   1081   1024    774       C  
ATOM   6161  N   ASP C 807     -92.090  53.223 -23.011  1.00 56.41           N  
ANISOU 6161  N   ASP C 807     7642   6847   6942   1153   1036    760       N  
ATOM   6162  CA  ASP C 807     -92.459  53.871 -21.751  1.00 60.34           C  
ANISOU 6162  CA  ASP C 807     8200   7289   7436   1188   1081    745       C  
ATOM   6163  C   ASP C 807     -92.873  52.918 -20.642  1.00 57.84           C  
ANISOU 6163  C   ASP C 807     7829   7035   7113   1149   1030    710       C  
ATOM   6164  O   ASP C 807     -93.185  53.379 -19.554  1.00 59.48           O  
ANISOU 6164  O   ASP C 807     8081   7204   7314   1177   1063    695       O  
ATOM   6165  CB  ASP C 807     -93.633  54.837 -21.968  1.00 65.68           C  
ANISOU 6165  CB  ASP C 807     8897   7985   8072   1327   1150    820       C  
ATOM   6166  CG  ASP C 807     -93.326  55.934 -22.971  1.00 70.23           C  
ANISOU 6166  CG  ASP C 807     9545   8490   8651   1386   1218    864       C  
ATOM   6167  OD1 ASP C 807     -92.162  56.386 -23.042  1.00 71.64           O  
ANISOU 6167  OD1 ASP C 807     9799   8553   8869   1322   1240    823       O  
ATOM   6168  OD2 ASP C 807     -94.266  56.352 -23.679  1.00 74.53           O  
ANISOU 6168  OD2 ASP C 807    10068   9096   9153   1498   1252    942       O  
ATOM   6169  N   SER C 808     -92.903  51.615 -20.899  1.00 53.43           N  
ANISOU 6169  N   SER C 808     7178   6569   6554   1088    955    699       N  
ATOM   6170  CA  SER C 808     -93.327  50.661 -19.881  1.00 48.96           C  
ANISOU 6170  CA  SER C 808     6561   6061   5982   1052    912    672       C  
ATOM   6171  C   SER C 808     -92.270  50.541 -18.808  1.00 50.63           C  
ANISOU 6171  C   SER C 808     6827   6186   6223    971    898    597       C  
ATOM   6172  O   SER C 808     -91.106  50.930 -19.017  1.00 52.65           O  
ANISOU 6172  O   SER C 808     7140   6356   6509    921    905    559       O  
ATOM   6173  CB  SER C 808     -93.576  49.287 -20.513  1.00 50.41           C  
ANISOU 6173  CB  SER C 808     6640   6356   6160   1001    840    678       C  
ATOM   6174  OG  SER C 808     -92.389  48.744 -21.089  1.00 50.06           O  
ANISOU 6174  OG  SER C 808     6596   6278   6145    915    799    639       O  
ATOM   6175  N   GLU C 809     -92.657  49.967 -17.673  1.00 49.89           N  
ANISOU 6175  N   GLU C 809     6712   6124   6119    956    879    575       N  
ATOM   6176  CA  GLU C 809     -91.701  49.694 -16.616  1.00 52.76           C  
ANISOU 6176  CA  GLU C 809     7115   6428   6504    881    858    504       C  
ATOM   6177  C   GLU C 809     -90.777  48.542 -17.054  1.00 46.11           C  
ANISOU 6177  C   GLU C 809     6228   5608   5685    786    790    470       C  
ATOM   6178  O   GLU C 809     -89.608  48.509 -16.702  1.00 43.26           O  
ANISOU 6178  O   GLU C 809     5905   5185   5346    721    774    413       O  
ATOM   6179  CB  GLU C 809     -92.392  49.349 -15.276  1.00 57.57           C  
ANISOU 6179  CB  GLU C 809     7713   7070   7090    897    856    494       C  
ATOM   6180  CG  GLU C 809     -91.390  49.143 -14.125  1.00 62.60           C  
ANISOU 6180  CG  GLU C 809     8394   7649   7740    830    837    420       C  
ATOM   6181  CD  GLU C 809     -91.803  48.233 -12.971  1.00 69.81           C  
ANISOU 6181  CD  GLU C 809     9272   8616   8635    815    809    406       C  
ATOM   6182  OE1 GLU C 809     -92.525  47.228 -13.179  1.00 80.07           O  
ANISOU 6182  OE1 GLU C 809    10494  10004   9925    811    778    440       O  
ATOM   6183  OE2 GLU C 809     -91.295  48.467 -11.853  1.00 65.09           O  
ANISOU 6183  OE2 GLU C 809     8726   7971   8035    798    816    356       O  
ATOM   6184  N   GLU C 810     -91.334  47.604 -17.809  1.00 43.21           N  
ANISOU 6184  N   GLU C 810     5779   5331   5308    779    751    504       N  
ATOM   6185  CA  GLU C 810     -90.593  46.502 -18.400  1.00 41.51           C  
ANISOU 6185  CA  GLU C 810     5520   5141   5111    700    692    480       C  
ATOM   6186  C   GLU C 810     -89.369  47.058 -19.169  1.00 38.76           C  
ANISOU 6186  C   GLU C 810     5218   4720   4789    669    698    458       C  
ATOM   6187  O   GLU C 810     -88.239  46.662 -18.919  1.00 33.07           O  
ANISOU 6187  O   GLU C 810     4513   3961   4090    599    669    407       O  
ATOM   6188  CB  GLU C 810     -91.550  45.734 -19.316  1.00 45.39           C  
ANISOU 6188  CB  GLU C 810     5924   5738   5583    715    666    527       C  
ATOM   6189  CG  GLU C 810     -91.123  44.346 -19.766  1.00 51.35           C  
ANISOU 6189  CG  GLU C 810     6624   6537   6349    637    604    505       C  
ATOM   6190  CD  GLU C 810     -92.253  43.594 -20.490  1.00 53.64           C  
ANISOU 6190  CD  GLU C 810     6827   6937   6616    649    582    545       C  
ATOM   6191  OE1 GLU C 810     -93.225  44.226 -20.946  1.00 55.35           O  
ANISOU 6191  OE1 GLU C 810     7020   7203   6807    721    611    594       O  
ATOM   6192  OE2 GLU C 810     -92.195  42.353 -20.570  1.00 58.74           O  
ANISOU 6192  OE2 GLU C 810     7428   7625   7267    587    537    527       O  
ATOM   6193  N   ALA C 811     -89.609  48.016 -20.062  1.00 37.36           N  
ANISOU 6193  N   ALA C 811     5063   4524   4608    726    741    499       N  
ATOM   6194  CA  ALA C 811     -88.547  48.593 -20.868  1.00 37.40           C  
ANISOU 6194  CA  ALA C 811     5111   4461   4637    700    756    486       C  
ATOM   6195  C   ALA C 811     -87.535  49.325 -20.005  1.00 38.46           C  
ANISOU 6195  C   ALA C 811     5326   4491   4795    663    783    429       C  
ATOM   6196  O   ALA C 811     -86.328  49.248 -20.252  1.00 39.24           O  
ANISOU 6196  O   ALA C 811     5443   4548   4920    596    767    388       O  
ATOM   6197  CB  ALA C 811     -89.118  49.522 -21.909  1.00 40.41           C  
ANISOU 6197  CB  ALA C 811     5507   4844   5005    781    806    549       C  
ATOM   6198  N   GLU C 812     -88.013  49.978 -18.951  1.00 37.81           N  
ANISOU 6198  N   GLU C 812     5289   4375   4702    701    822    421       N  
ATOM   6199  CA  GLU C 812     -87.130  50.731 -18.051  1.00 36.88           C  
ANISOU 6199  CA  GLU C 812     5250   4161   4601    665    850    360       C  
ATOM   6200  C   GLU C 812     -86.169  49.824 -17.295  1.00 33.81           C  
ANISOU 6200  C   GLU C 812     4842   3782   4224    577    792    293       C  
ATOM   6201  O   GLU C 812     -84.980  50.127 -17.190  1.00 34.71           O  
ANISOU 6201  O   GLU C 812     4992   3836   4359    515    792    239       O  
ATOM   6202  CB  GLU C 812     -87.917  51.618 -17.074  1.00 35.44           C  
ANISOU 6202  CB  GLU C 812     5124   3944   4400    731    906    365       C  
ATOM   6203  N   ILE C 813     -86.688  48.711 -16.803  1.00 31.27           N  
ANISOU 6203  N   ILE C 813     4461   3537   3885    573    745    298       N  
ATOM   6204  CA  ILE C 813     -85.882  47.678 -16.184  1.00 31.77           C  
ANISOU 6204  CA  ILE C 813     4497   3622   3952    502    688    247       C  
ATOM   6205  C   ILE C 813     -84.791  47.213 -17.174  1.00 30.50           C  
ANISOU 6205  C   ILE C 813     4313   3459   3815    440    654    231       C  
ATOM   6206  O   ILE C 813     -83.624  47.114 -16.818  1.00 30.15           O  
ANISOU 6206  O   ILE C 813     4285   3386   3783    380    634    175       O  
ATOM   6207  CB  ILE C 813     -86.738  46.438 -15.801  1.00 32.59           C  
ANISOU 6207  CB  ILE C 813     4535   3812   4035    511    648    271       C  
ATOM   6208  CG1 ILE C 813     -87.834  46.767 -14.780  1.00 35.89           C  
ANISOU 6208  CG1 ILE C 813     4966   4245   4427    570    680    289       C  
ATOM   6209  CG2 ILE C 813     -85.903  45.291 -15.230  1.00 31.62           C  
ANISOU 6209  CG2 ILE C 813     4388   3712   3915    445    593    227       C  
ATOM   6210  CD1 ILE C 813     -87.294  47.223 -13.468  1.00 38.59           C  
ANISOU 6210  CD1 ILE C 813     5364   4536   4762    556    693    232       C  
ATOM   6211  N   ILE C 814     -85.192  46.917 -18.401  1.00 30.05           N  
ANISOU 6211  N   ILE C 814     4217   3442   3760    459    646    280       N  
ATOM   6212  CA  ILE C 814     -84.270  46.369 -19.387  1.00 31.85           C  
ANISOU 6212  CA  ILE C 814     4417   3679   4006    408    612    271       C  
ATOM   6213  C   ILE C 814     -83.194  47.396 -19.743  1.00 31.51           C  
ANISOU 6213  C   ILE C 814     4430   3556   3987    381    646    243       C  
ATOM   6214  O   ILE C 814     -82.029  47.033 -19.839  1.00 31.99           O  
ANISOU 6214  O   ILE C 814     4484   3606   4063    318    617    201       O  
ATOM   6215  CB  ILE C 814     -85.018  45.847 -20.620  1.00 32.08           C  
ANISOU 6215  CB  ILE C 814     4391   3773   4026    437    597    328       C  
ATOM   6216  CG1 ILE C 814     -85.762  44.551 -20.235  1.00 35.40           C  
ANISOU 6216  CG1 ILE C 814     4750   4272   4428    430    553    336       C  
ATOM   6217  CG2 ILE C 814     -84.054  45.588 -21.749  1.00 32.62           C  
ANISOU 6217  CG2 ILE C 814     4445   3837   4110    395    577    321       C  
ATOM   6218  CD1 ILE C 814     -86.723  44.024 -21.288  1.00 35.98           C  
ANISOU 6218  CD1 ILE C 814     4762   4422   4485    458    539    387       C  
ATOM   6219  N   ARG C 815     -83.572  48.669 -19.878  1.00 31.14           N  
ANISOU 6219  N   ARG C 815     4437   3452   3942    427    710    265       N  
ATOM   6220  CA  ARG C 815     -82.595  49.735 -20.144  1.00 33.38           C  
ANISOU 6220  CA  ARG C 815     4784   3648   4251    397    754    238       C  
ATOM   6221  C   ARG C 815     -81.650  49.926 -18.965  1.00 32.64           C  
ANISOU 6221  C   ARG C 815     4725   3511   4167    335    749    159       C  
ATOM   6222  O   ARG C 815     -80.471  50.176 -19.175  1.00 30.13           O  
ANISOU 6222  O   ARG C 815     4423   3153   3870    272    749    116       O  
ATOM   6223  CB  ARG C 815     -83.251  51.073 -20.508  1.00 36.37           C  
ANISOU 6223  CB  ARG C 815     5224   3967   4629    467    833    281       C  
ATOM   6224  CG  ARG C 815     -83.836  51.138 -21.917  1.00 38.70           C  
ANISOU 6224  CG  ARG C 815     5494   4295   4916    524    847    356       C  
ATOM   6225  CD  ARG C 815     -84.257  52.575 -22.293  1.00 40.74           C  
ANISOU 6225  CD  ARG C 815     5827   4479   5174    593    935    397       C  
ATOM   6226  NE  ARG C 815     -85.188  53.103 -21.309  1.00 42.23           N  
ANISOU 6226  NE  ARG C 815     6051   4652   5343    653    970    404       N  
ATOM   6227  CZ  ARG C 815     -86.520  53.098 -21.408  1.00 43.59           C  
ANISOU 6227  CZ  ARG C 815     6196   4882   5483    744    982    466       C  
ATOM   6228  NH1 ARG C 815     -87.241  53.550 -20.397  1.00 43.54           N  
ANISOU 6228  NH1 ARG C 815     6225   4860   5460    791   1013    464       N  
ATOM   6229  NH2 ARG C 815     -87.138  52.654 -22.496  1.00 45.25           N  
ANISOU 6229  NH2 ARG C 815     6346   5173   5674    788    963    527       N  
ATOM   6230  N   LYS C 816     -82.144  49.745 -17.741  1.00 32.21           N  
ANISOU 6230  N   LYS C 816     4675   3471   4092    350    740    138       N  
ATOM   6231  CA  LYS C 816     -81.261  49.805 -16.577  1.00 33.68           C  
ANISOU 6231  CA  LYS C 816     4886   3633   4279    293    726     60       C  
ATOM   6232  C   LYS C 816     -80.259  48.649 -16.634  1.00 32.96           C  
ANISOU 6232  C   LYS C 816     4737   3594   4190    228    658     26       C  
ATOM   6233  O   LYS C 816     -79.075  48.847 -16.370  1.00 35.37           O  
ANISOU 6233  O   LYS C 816     5055   3876   4507    164    650    -34       O  
ATOM   6234  CB  LYS C 816     -82.030  49.713 -15.259  1.00 36.91           C  
ANISOU 6234  CB  LYS C 816     5306   4059   4659    329    726     49       C  
ATOM   6235  CG  LYS C 816     -81.457  50.492 -14.094  1.00 41.96           C  
ANISOU 6235  CG  LYS C 816     6005   4643   5294    298    750    -24       C  
ATOM   6236  CD  LYS C 816     -82.206  50.206 -12.779  1.00 47.40           C  
ANISOU 6236  CD  LYS C 816     6695   5365   5949    336    742    -33       C  
ATOM   6237  CE  LYS C 816     -81.765  51.199 -11.714  1.00 55.09           C  
ANISOU 6237  CE  LYS C 816     7740   6275   6916    316    777   -104       C  
ATOM   6238  NZ  LYS C 816     -82.426  51.137 -10.374  1.00 57.26           N  
ANISOU 6238  NZ  LYS C 816     8030   6571   7155    355    779   -120       N  
ATOM   6239  N   TYR C 817     -80.729  47.446 -16.961  1.00 29.51           N  
ANISOU 6239  N   TYR C 817     4239   3232   3743    244    611     63       N  
ATOM   6240  CA  TYR C 817     -79.847  46.287 -17.015  1.00 27.15           C  
ANISOU 6240  CA  TYR C 817     3890   2981   3443    193    551     37       C  
ATOM   6241  C   TYR C 817     -78.715  46.574 -18.019  1.00 26.48           C  
ANISOU 6241  C   TYR C 817     3806   2870   3384    145    553     21       C  
ATOM   6242  O   TYR C 817     -77.551  46.342 -17.730  1.00 26.03           O  
ANISOU 6242  O   TYR C 817     3740   2819   3332     89    527    -31       O  
ATOM   6243  CB  TYR C 817     -80.647  45.057 -17.421  1.00 24.91           C  
ANISOU 6243  CB  TYR C 817     3550   2767   3147    219    513     85       C  
ATOM   6244  CG  TYR C 817     -80.058  43.695 -17.139  1.00 23.01           C  
ANISOU 6244  CG  TYR C 817     3267   2579   2898    184    455     64       C  
ATOM   6245  CD1 TYR C 817     -78.809  43.518 -16.545  1.00 22.85           C  
ANISOU 6245  CD1 TYR C 817     3251   2557   2876    137    431      6       C  
ATOM   6246  CD2 TYR C 817     -80.763  42.556 -17.520  1.00 22.05           C  
ANISOU 6246  CD2 TYR C 817     3099   2512   2766    200    426    104       C  
ATOM   6247  CE1 TYR C 817     -78.295  42.228 -16.324  1.00 21.89           C  
ANISOU 6247  CE1 TYR C 817     3091   2484   2741    117    381     -6       C  
ATOM   6248  CE2 TYR C 817     -80.273  41.281 -17.280  1.00 21.95           C  
ANISOU 6248  CE2 TYR C 817     3056   2538   2745    173    380     88       C  
ATOM   6249  CZ  TYR C 817     -79.065  41.117 -16.678  1.00 21.85           C  
ANISOU 6249  CZ  TYR C 817     3051   2522   2729    138    358     37       C  
ATOM   6250  OH  TYR C 817     -78.634  39.836 -16.539  1.00 22.88           O  
ANISOU 6250  OH  TYR C 817     3154   2691   2848    123    317     31       O  
ATOM   6251  N   VAL C 818     -79.063  47.116 -19.173  1.00 27.32           N  
ANISOU 6251  N   VAL C 818     3922   2954   3505    170    586     68       N  
ATOM   6252  CA  VAL C 818     -78.064  47.443 -20.174  1.00 29.13           C  
ANISOU 6252  CA  VAL C 818     4153   3157   3758    130    596     61       C  
ATOM   6253  C   VAL C 818     -77.074  48.504 -19.673  1.00 30.25           C  
ANISOU 6253  C   VAL C 818     4347   3230   3918     78    633      1       C  
ATOM   6254  O   VAL C 818     -75.860  48.362 -19.819  1.00 30.35           O  
ANISOU 6254  O   VAL C 818     4344   3246   3943     15    614    -42       O  
ATOM   6255  CB  VAL C 818     -78.710  47.968 -21.470  1.00 30.49           C  
ANISOU 6255  CB  VAL C 818     4334   3314   3938    178    635    127       C  
ATOM   6256  CG1 VAL C 818     -77.633  48.518 -22.414  1.00 29.51           C  
ANISOU 6256  CG1 VAL C 818     4224   3149   3839    136    659    118       C  
ATOM   6257  CG2 VAL C 818     -79.508  46.873 -22.158  1.00 29.53           C  
ANISOU 6257  CG2 VAL C 818     4152   3270   3799    213    594    178       C  
ATOM   6258  N   LYS C 819     -77.599  49.554 -19.064  1.00 31.73           N  
ANISOU 6258  N   LYS C 819     4594   3357   4104    103    685     -5       N  
ATOM   6259  CA  LYS C 819     -76.778  50.652 -18.629  1.00 34.80           C  
ANISOU 6259  CA  LYS C 819     5039   3671   4510     52    729    -64       C  
ATOM   6260  C   LYS C 819     -75.850  50.283 -17.490  1.00 33.38           C  
ANISOU 6260  C   LYS C 819     4844   3519   4321    -11    688   -145       C  
ATOM   6261  O   LYS C 819     -74.673  50.625 -17.500  1.00 36.68           O  
ANISOU 6261  O   LYS C 819     5266   3917   4754    -83    691   -201       O  
ATOM   6262  CB  LYS C 819     -77.646  51.827 -18.198  1.00 40.52           C  
ANISOU 6262  CB  LYS C 819     5839   4323   5234    101    799    -51       C  
ATOM   6263  CG  LYS C 819     -76.820  53.122 -18.147  1.00 45.53           C  
ANISOU 6263  CG  LYS C 819     6545   4860   5894     46    862   -101       C  
ATOM   6264  CD  LYS C 819     -77.032  53.958 -16.906  1.00 52.99           C  
ANISOU 6264  CD  LYS C 819     7556   5748   6829     45    900   -153       C  
ATOM   6265  CE  LYS C 819     -76.509  55.389 -17.134  1.00 57.55           C  
ANISOU 6265  CE  LYS C 819     8219   6210   7437      5    984   -182       C  
ATOM   6266  NZ  LYS C 819     -75.604  55.907 -16.065  1.00 61.47           N  
ANISOU 6266  NZ  LYS C 819     8750   6671   7936    -79    991   -285       N  
ATOM   6267  N   ASN C 820     -76.381  49.614 -16.492  1.00 31.66           N  
ANISOU 6267  N   ASN C 820     4607   3349   4074     16    652   -153       N  
ATOM   6268  CA  ASN C 820     -75.594  49.295 -15.331  1.00 31.39           C  
ANISOU 6268  CA  ASN C 820     4560   3346   4021    -30    615   -227       C  
ATOM   6269  C   ASN C 820     -74.578  48.198 -15.501  1.00 30.27           C  
ANISOU 6269  C   ASN C 820     4352   3276   3873    -73    552   -248       C  
ATOM   6270  O   ASN C 820     -73.625  48.167 -14.750  1.00 32.77           O  
ANISOU 6270  O   ASN C 820     4658   3614   4178   -123    529   -316       O  
ATOM   6271  CB  ASN C 820     -76.502  48.885 -14.198  1.00 33.89           C  
ANISOU 6271  CB  ASN C 820     4878   3694   4304     19    599   -223       C  
ATOM   6272  CG  ASN C 820     -77.251  50.044 -13.603  1.00 36.15           C  
ANISOU 6272  CG  ASN C 820     5236   3913   4587     52    660   -229       C  
ATOM   6273  OD1 ASN C 820     -76.976  51.194 -13.897  1.00 37.84           O  
ANISOU 6273  OD1 ASN C 820     5504   4049   4823     30    715   -247       O  
ATOM   6274  ND2 ASN C 820     -78.194  49.737 -12.737  1.00 38.30           N  
ANISOU 6274  ND2 ASN C 820     5510   4212   4830    106    654   -213       N  
ATOM   6275  N   THR C 821     -74.761  47.277 -16.443  1.00 28.18           N  
ANISOU 6275  N   THR C 821     4041   3052   3612    -52    522   -194       N  
ATOM   6276  CA  THR C 821     -73.868  46.115 -16.510  1.00 28.97           C  
ANISOU 6276  CA  THR C 821     4082   3223   3702    -80    462   -212       C  
ATOM   6277  C   THR C 821     -72.900  46.170 -17.693  1.00 29.88           C  
ANISOU 6277  C   THR C 821     4175   3335   3842   -123    462   -211       C  
ATOM   6278  O   THR C 821     -72.310  45.164 -18.074  1.00 29.50           O  
ANISOU 6278  O   THR C 821     4079   3344   3788   -133    418   -208       O  
ATOM   6279  CB  THR C 821     -74.647  44.771 -16.478  1.00 25.92           C  
ANISOU 6279  CB  THR C 821     3657   2897   3295    -31    419   -164       C  
ATOM   6280  OG1 THR C 821     -75.345  44.604 -17.707  1.00 25.93           O  
ANISOU 6280  OG1 THR C 821     3648   2892   3312     -1    430    -99       O  
ATOM   6281  CG2 THR C 821     -75.619  44.767 -15.334  1.00 25.13           C  
ANISOU 6281  CG2 THR C 821     3579   2800   3171     10    425   -161       C  
ATOM   6282  N   HIS C 822     -72.699  47.361 -18.243  1.00 32.20           N  
ANISOU 6282  N   HIS C 822     4509   3561   4164   -147    517   -216       N  
ATOM   6283  CA  HIS C 822     -71.639  47.556 -19.223  1.00 32.07           C  
ANISOU 6283  CA  HIS C 822     4476   3538   4171   -197    525   -225       C  
ATOM   6284  C   HIS C 822     -70.299  47.550 -18.511  1.00 31.43           C  
ANISOU 6284  C   HIS C 822     4371   3488   4083   -268    501   -305       C  
ATOM   6285  O   HIS C 822     -70.090  48.347 -17.648  1.00 34.00           O  
ANISOU 6285  O   HIS C 822     4730   3782   4407   -301    524   -360       O  
ATOM   6286  CB  HIS C 822     -71.828  48.861 -19.969  1.00 32.99           C  
ANISOU 6286  CB  HIS C 822     4649   3568   4319   -202    598   -204       C  
ATOM   6287  CG  HIS C 822     -70.985  48.951 -21.193  1.00 34.59           C  
ANISOU 6287  CG  HIS C 822     4832   3767   4545   -238    610   -191       C  
ATOM   6288  ND1 HIS C 822     -71.509  49.168 -22.439  1.00 32.89           N  
ANISOU 6288  ND1 HIS C 822     4629   3526   4344   -198    642   -122       N  
ATOM   6289  CD2 HIS C 822     -69.647  48.799 -21.363  1.00 35.12           C  
ANISOU 6289  CD2 HIS C 822     4863   3863   4620   -306    592   -236       C  
ATOM   6290  CE1 HIS C 822     -70.531  49.159 -23.327  1.00 33.34           C  
ANISOU 6290  CE1 HIS C 822     4662   3589   4417   -240    645   -125       C  
ATOM   6291  NE2 HIS C 822     -69.394  48.938 -22.700  1.00 33.17           N  
ANISOU 6291  NE2 HIS C 822     4610   3600   4393   -307    616   -193       N  
ATOM   6292  N   ALA C 823     -69.403  46.622 -18.839  1.00 32.79           N  
ANISOU 6292  N   ALA C 823     4484   3729   4247   -289    453   -314       N  
ATOM   6293  CA  ALA C 823     -68.141  46.490 -18.109  1.00 33.31           C  
ANISOU 6293  CA  ALA C 823     4514   3845   4296   -348    423   -389       C  
ATOM   6294  C   ALA C 823     -67.163  47.621 -18.415  1.00 36.24           C  
ANISOU 6294  C   ALA C 823     4900   4176   4696   -428    466   -438       C  
ATOM   6295  O   ALA C 823     -67.129  48.116 -19.532  1.00 34.97           O  
ANISOU 6295  O   ALA C 823     4754   3966   4566   -438    506   -403       O  
ATOM   6296  CB  ALA C 823     -67.484  45.167 -18.441  1.00 34.42           C  
ANISOU 6296  CB  ALA C 823     4588   4071   4417   -337    364   -378       C  
ATOM   6297  N   THR C 824     -66.374  48.023 -17.411  1.00 42.32           N  
ANISOU 6297  N   THR C 824     5662   4966   5451   -485    459   -520       N  
ATOM   6298  CA  THR C 824     -65.387  49.130 -17.567  1.00 46.94           C  
ANISOU 6298  CA  THR C 824     6259   5514   6062   -577    502   -580       C  
ATOM   6299  C   THR C 824     -64.338  48.833 -18.628  1.00 46.62           C  
ANISOU 6299  C   THR C 824     6164   5511   6037   -616    495   -572       C  
ATOM   6300  O   THR C 824     -63.904  49.748 -19.310  1.00 51.07           O  
ANISOU 6300  O   THR C 824     6751   6016   6636   -672    549   -580       O  
ATOM   6301  CB  THR C 824     -64.580  49.480 -16.297  1.00 47.13           C  
ANISOU 6301  CB  THR C 824     6268   5577   6061   -642    486   -681       C  
ATOM   6302  OG1 THR C 824     -63.806  48.343 -15.895  1.00 45.08           O  
ANISOU 6302  OG1 THR C 824     5929   5438   5762   -636    413   -703       O  
ATOM   6303  CG2 THR C 824     -65.499  49.936 -15.177  1.00 46.46           C  
ANISOU 6303  CG2 THR C 824     6241   5451   5959   -613    500   -701       C  
ATOM   6304  N   THR C 825     -63.943  47.574 -18.777  1.00 43.54           N  
ANISOU 6304  N   THR C 825     5708   5214   5622   -585    433   -554       N  
ATOM   6305  CA  THR C 825     -62.916  47.220 -19.755  1.00 42.83           C  
ANISOU 6305  CA  THR C 825     5563   5169   5541   -616    423   -547       C  
ATOM   6306  C   THR C 825     -63.417  47.067 -21.179  1.00 42.05           C  
ANISOU 6306  C   THR C 825     5479   5029   5469   -575    447   -465       C  
ATOM   6307  O   THR C 825     -62.629  46.773 -22.075  1.00 43.68           O  
ANISOU 6307  O   THR C 825     5644   5269   5683   -594    443   -453       O  
ATOM   6308  CB  THR C 825     -62.202  45.903 -19.396  1.00 42.45           C  
ANISOU 6308  CB  THR C 825     5439   5239   5451   -593    350   -561       C  
ATOM   6309  OG1 THR C 825     -63.143  44.825 -19.398  1.00 37.92           O  
ANISOU 6309  OG1 THR C 825     4870   4681   4858   -505    315   -500       O  
ATOM   6310  CG2 THR C 825     -61.534  46.020 -18.018  1.00 43.65           C  
ANISOU 6310  CG2 THR C 825     5563   5453   5567   -633    321   -646       C  
ATOM   6311  N   HIS C 826     -64.713  47.197 -21.398  1.00 41.39           N  
ANISOU 6311  N   HIS C 826     5447   4884   5394   -515    469   -408       N  
ATOM   6312  CA  HIS C 826     -65.265  47.086 -22.755  1.00 40.28           C  
ANISOU 6312  CA  HIS C 826     5319   4712   5272   -472    492   -330       C  
ATOM   6313  C   HIS C 826     -65.600  48.485 -23.232  1.00 41.32           C  
ANISOU 6313  C   HIS C 826     5518   4742   5440   -493    572   -315       C  
ATOM   6314  O   HIS C 826     -66.755  48.840 -23.467  1.00 37.19           O  
ANISOU 6314  O   HIS C 826     5044   4163   4923   -438    603   -264       O  
ATOM   6315  CB  HIS C 826     -66.497  46.163 -22.752  1.00 37.34           C  
ANISOU 6315  CB  HIS C 826     4951   4357   4880   -386    459   -272       C  
ATOM   6316  CG  HIS C 826     -66.182  44.749 -22.364  1.00 34.79           C  
ANISOU 6316  CG  HIS C 826     4572   4123   4523   -362    389   -279       C  
ATOM   6317  ND1 HIS C 826     -67.060  43.949 -21.661  1.00 32.38           N  
ANISOU 6317  ND1 HIS C 826     4269   3841   4192   -308    354   -262       N  
ATOM   6318  CD2 HIS C 826     -65.061  44.008 -22.549  1.00 32.43           C  
ANISOU 6318  CD2 HIS C 826     4216   3895   4210   -383    351   -301       C  
ATOM   6319  CE1 HIS C 826     -66.494  42.775 -21.431  1.00 31.37           C  
ANISOU 6319  CE1 HIS C 826     4094   3787   4037   -296    301   -273       C  
ATOM   6320  NE2 HIS C 826     -65.286  42.786 -21.963  1.00 32.62           N  
ANISOU 6320  NE2 HIS C 826     4215   3977   4201   -337    298   -296       N  
ATOM   6321  N   ASN C 827     -64.547  49.278 -23.351  1.00 45.97           N  
ANISOU 6321  N   ASN C 827     6106   5310   6051   -574    607   -362       N  
ATOM   6322  CA  ASN C 827     -64.674  50.727 -23.554  1.00 50.55           C  
ANISOU 6322  CA  ASN C 827     6757   5783   6666   -612    692   -367       C  
ATOM   6323  C   ASN C 827     -64.655  51.154 -25.033  1.00 46.89           C  
ANISOU 6323  C   ASN C 827     6313   5273   6231   -603    746   -303       C  
ATOM   6324  O   ASN C 827     -64.792  52.325 -25.334  1.00 49.76           O  
ANISOU 6324  O   ASN C 827     6742   5542   6623   -624    823   -294       O  
ATOM   6325  CB  ASN C 827     -63.605  51.479 -22.735  1.00 54.67           C  
ANISOU 6325  CB  ASN C 827     7278   6298   7198   -716    711   -463       C  
ATOM   6326  CG  ASN C 827     -62.191  50.968 -22.988  1.00 56.59           C  
ANISOU 6326  CG  ASN C 827     7439   6628   7436   -779    676   -502       C  
ATOM   6327  OD1 ASN C 827     -61.942  50.093 -23.828  1.00 59.55           O  
ANISOU 6327  OD1 ASN C 827     7763   7062   7803   -746    643   -458       O  
ATOM   6328  ND2 ASN C 827     -61.259  51.504 -22.232  1.00 58.62           N  
ANISOU 6328  ND2 ASN C 827     7680   6899   7694   -871    682   -590       N  
ATOM   6329  N   ALA C 828     -64.550  50.193 -25.944  1.00 44.14           N  
ANISOU 6329  N   ALA C 828     5914   4988   5871   -563    707   -255       N  
ATOM   6330  CA  ALA C 828     -64.622  50.458 -27.371  1.00 44.52           C  
ANISOU 6330  CA  ALA C 828     5975   5004   5936   -540    751   -188       C  
ATOM   6331  C   ALA C 828     -65.969  51.041 -27.864  1.00 48.42           C  
ANISOU 6331  C   ALA C 828     6538   5425   6435   -464    800   -115       C  
ATOM   6332  O   ALA C 828     -66.022  51.592 -28.968  1.00 49.22           O  
ANISOU 6332  O   ALA C 828     6667   5483   6552   -448    854    -63       O  
ATOM   6333  CB  ALA C 828     -64.294  49.185 -28.138  1.00 45.73           C  
ANISOU 6333  CB  ALA C 828     6059   5249   6068   -507    691   -158       C  
ATOM   6334  N   TYR C 829     -67.049  50.899 -27.082  1.00 44.99           N  
ANISOU 6334  N   TYR C 829     6127   4983   5983   -411    781   -109       N  
ATOM   6335  CA  TYR C 829     -68.361  51.355 -27.525  1.00 41.94           C  
ANISOU 6335  CA  TYR C 829     5794   4545   5594   -330    822    -38       C  
ATOM   6336  C   TYR C 829     -69.291  51.621 -26.346  1.00 41.29           C  
ANISOU 6336  C   TYR C 829     5752   4435   5502   -300    822    -56       C  
ATOM   6337  O   TYR C 829     -69.003  51.233 -25.225  1.00 40.33           O  
ANISOU 6337  O   TYR C 829     5609   4347   5369   -333    779   -116       O  
ATOM   6338  CB  TYR C 829     -68.993  50.321 -28.466  1.00 39.39           C  
ANISOU 6338  CB  TYR C 829     5428   4290   5247   -255    777     29       C  
ATOM   6339  CG  TYR C 829     -69.142  48.925 -27.843  1.00 40.09           C  
ANISOU 6339  CG  TYR C 829     5456   4468   5307   -240    689      8       C  
ATOM   6340  CD1 TYR C 829     -70.201  48.637 -26.980  1.00 37.90           C  
ANISOU 6340  CD1 TYR C 829     5189   4199   5011   -195    665     11       C  
ATOM   6341  CD2 TYR C 829     -68.207  47.918 -28.080  1.00 38.32           C  
ANISOU 6341  CD2 TYR C 829     5169   4318   5074   -270    634    -15       C  
ATOM   6342  CE1 TYR C 829     -70.327  47.389 -26.382  1.00 37.34           C  
ANISOU 6342  CE1 TYR C 829     5070   4202   4916   -183    593     -6       C  
ATOM   6343  CE2 TYR C 829     -68.322  46.677 -27.481  1.00 36.83           C  
ANISOU 6343  CE2 TYR C 829     4935   4201   4860   -254    563    -32       C  
ATOM   6344  CZ  TYR C 829     -69.400  46.411 -26.642  1.00 38.05           C  
ANISOU 6344  CZ  TYR C 829     5103   4357   4997   -211    543    -26       C  
ATOM   6345  OH  TYR C 829     -69.575  45.180 -26.051  1.00 34.73           O  
ANISOU 6345  OH  TYR C 829     4644   4000   4551   -193    479    -38       O  
ATOM   6346  N   ASP C 830     -70.368  52.345 -26.618  1.00 41.43           N  
ANISOU 6346  N   ASP C 830     5829   4392   5521   -235    876     -1       N  
ATOM   6347  CA  ASP C 830     -71.510  52.431 -25.731  1.00 44.72           C  
ANISOU 6347  CA  ASP C 830     6275   4796   5919   -180    873      6       C  
ATOM   6348  C   ASP C 830     -72.653  51.806 -26.410  1.00 37.15           C  
ANISOU 6348  C   ASP C 830     5293   3886   4937    -88    850     82       C  
ATOM   6349  O   ASP C 830     -72.663  51.729 -27.605  1.00 38.48           O  
ANISOU 6349  O   ASP C 830     5448   4066   5105    -61    862    135       O  
ATOM   6350  CB  ASP C 830     -71.973  53.877 -25.567  1.00 51.80           C  
ANISOU 6350  CB  ASP C 830     7266   5583   6834   -164    965     16       C  
ATOM   6351  CG  ASP C 830     -70.929  54.758 -24.975  1.00 60.45           C  
ANISOU 6351  CG  ASP C 830     8402   6609   7957   -261   1008    -61       C  
ATOM   6352  OD1 ASP C 830     -70.007  54.241 -24.301  1.00 70.26           O  
ANISOU 6352  OD1 ASP C 830     9597   7901   9198   -334    957   -133       O  
ATOM   6353  OD2 ASP C 830     -71.042  55.979 -25.193  1.00 66.17           O  
ANISOU 6353  OD2 ASP C 830     9207   7230   8703   -261   1096    -48       O  
ATOM   6354  N   LEU C 831     -73.668  51.470 -25.642  1.00 36.05           N  
ANISOU 6354  N   LEU C 831     5152   3770   4775    -38    825     90       N  
ATOM   6355  CA  LEU C 831     -74.812  50.808 -26.196  1.00 34.78           C  
ANISOU 6355  CA  LEU C 831     4960   3667   4588     43    799    156       C  
ATOM   6356  C   LEU C 831     -76.019  51.646 -26.053  1.00 32.88           C  
ANISOU 6356  C   LEU C 831     4772   3382   4338    118    853    201       C  
ATOM   6357  O   LEU C 831     -76.217  52.299 -25.043  1.00 31.57           O  
ANISOU 6357  O   LEU C 831     4656   3164   4177    114    882    170       O  
ATOM   6358  CB  LEU C 831     -75.082  49.489 -25.476  1.00 34.86           C  
ANISOU 6358  CB  LEU C 831     4910   3760   4575     44    718    134       C  
ATOM   6359  CG  LEU C 831     -74.069  48.380 -25.749  1.00 34.40           C  
ANISOU 6359  CG  LEU C 831     4790   3764   4516     -7    656    105       C  
ATOM   6360  CD1 LEU C 831     -74.244  47.211 -24.800  1.00 34.59           C  
ANISOU 6360  CD1 LEU C 831     4771   3852   4519    -11    589     76       C  
ATOM   6361  CD2 LEU C 831     -74.170  47.934 -27.193  1.00 34.80           C  
ANISOU 6361  CD2 LEU C 831     4809   3853   4561     22    648    159       C  
ATOM   6362  N   GLU C 832     -76.851  51.584 -27.066  1.00 33.47           N  
ANISOU 6362  N   GLU C 832     4835   3485   4396    191    863    275       N  
ATOM   6363  CA  GLU C 832     -78.116  52.272 -27.041  1.00 39.17           C  
ANISOU 6363  CA  GLU C 832     5596   4185   5100    279    910    329       C  
ATOM   6364  C   GLU C 832     -79.194  51.299 -27.480  1.00 36.57           C  
ANISOU 6364  C   GLU C 832     5200   3957   4736    343    859    379       C  
ATOM   6365  O   GLU C 832     -79.085  50.676 -28.548  1.00 37.07           O  
ANISOU 6365  O   GLU C 832     5217   4079   4790    349    830    408       O  
ATOM   6366  CB  GLU C 832     -78.018  53.467 -28.005  1.00 45.52           C  
ANISOU 6366  CB  GLU C 832     6463   4916   5917    311    995    377       C  
ATOM   6367  CG  GLU C 832     -79.325  54.112 -28.390  1.00 52.61           C  
ANISOU 6367  CG  GLU C 832     7393   5808   6789    423   1046    454       C  
ATOM   6368  CD  GLU C 832     -79.144  55.344 -29.287  1.00 58.69           C  
ANISOU 6368  CD  GLU C 832     8235   6493   7570    457   1139    503       C  
ATOM   6369  OE1 GLU C 832     -78.041  55.585 -29.854  1.00 55.19           O  
ANISOU 6369  OE1 GLU C 832     7807   6008   7154    395   1161    487       O  
ATOM   6370  OE2 GLU C 832     -80.144  56.079 -29.411  1.00 64.69           O  
ANISOU 6370  OE2 GLU C 832     9039   7230   8310    551   1195    562       O  
ATOM   6371  N   VAL C 833     -80.233  51.175 -26.670  1.00 35.28           N  
ANISOU 6371  N   VAL C 833     5033   3819   4553    387    850    386       N  
ATOM   6372  CA  VAL C 833     -81.318  50.267 -26.977  1.00 33.05           C  
ANISOU 6372  CA  VAL C 833     4684   3634   4237    440    804    428       C  
ATOM   6373  C   VAL C 833     -82.226  50.907 -27.996  1.00 34.51           C  
ANISOU 6373  C   VAL C 833     4878   3833   4399    532    850    507       C  
ATOM   6374  O   VAL C 833     -82.701  52.000 -27.788  1.00 38.06           O  
ANISOU 6374  O   VAL C 833     5389   4225   4847    587    917    534       O  
ATOM   6375  CB  VAL C 833     -82.097  49.911 -25.708  1.00 32.78           C  
ANISOU 6375  CB  VAL C 833     4640   3625   4190    453    782    408       C  
ATOM   6376  CG1 VAL C 833     -83.281  49.007 -26.045  1.00 32.30           C  
ANISOU 6376  CG1 VAL C 833     4508   3668   4095    502    740    452       C  
ATOM   6377  CG2 VAL C 833     -81.181  49.219 -24.700  1.00 33.51           C  
ANISOU 6377  CG2 VAL C 833     4721   3713   4298    369    735    333       C  
ATOM   6378  N   ILE C 834     -82.412  50.263 -29.131  1.00 35.69           N  
ANISOU 6378  N   ILE C 834     4972   4058   4529    551    818    543       N  
ATOM   6379  CA  ILE C 834     -83.257  50.802 -30.175  1.00 35.82           C  
ANISOU 6379  CA  ILE C 834     4988   4105   4516    643    856    619       C  
ATOM   6380  C   ILE C 834     -84.644  50.249 -30.006  1.00 37.80           C  
ANISOU 6380  C   ILE C 834     5181   4452   4727    703    825    650       C  
ATOM   6381  O   ILE C 834     -85.592  51.011 -29.845  1.00 41.33           O  
ANISOU 6381  O   ILE C 834     5653   4897   5154    785    872    695       O  
ATOM   6382  CB  ILE C 834     -82.731  50.459 -31.584  1.00 38.33           C  
ANISOU 6382  CB  ILE C 834     5274   4461   4826    636    840    643       C  
ATOM   6383  CG1 ILE C 834     -81.406  51.153 -31.820  1.00 39.56           C  
ANISOU 6383  CG1 ILE C 834     5489   4521   5020    583    884    621       C  
ATOM   6384  CG2 ILE C 834     -83.707  50.925 -32.669  1.00 38.84           C  
ANISOU 6384  CG2 ILE C 834     5329   4579   4850    741    873    725       C  
ATOM   6385  CD1 ILE C 834     -80.715  50.637 -33.054  1.00 42.78           C  
ANISOU 6385  CD1 ILE C 834     5861   4969   5424    561    859    631       C  
ATOM   6386  N   ASP C 835     -84.765  48.925 -30.030  1.00 37.21           N  
ANISOU 6386  N   ASP C 835     5031   4464   4643    661    749    626       N  
ATOM   6387  CA  ASP C 835     -86.051  48.235 -29.810  1.00 37.61           C  
ANISOU 6387  CA  ASP C 835     5017   4613   4660    699    714    646       C  
ATOM   6388  C   ASP C 835     -85.908  47.087 -28.826  1.00 36.28           C  
ANISOU 6388  C   ASP C 835     4814   4467   4505    625    654    589       C  
ATOM   6389  O   ASP C 835     -84.851  46.429 -28.766  1.00 32.22           O  
ANISOU 6389  O   ASP C 835     4297   3931   4014    549    618    541       O  
ATOM   6390  CB  ASP C 835     -86.561  47.631 -31.125  1.00 41.77           C  
ANISOU 6390  CB  ASP C 835     5475   5245   5151    729    682    684       C  
ATOM   6391  CG  ASP C 835     -86.909  48.692 -32.164  1.00 46.52           C  
ANISOU 6391  CG  ASP C 835     6101   5848   5727    820    739    753       C  
ATOM   6392  OD1 ASP C 835     -86.495  48.506 -33.334  1.00 51.27           O  
ANISOU 6392  OD1 ASP C 835     6683   6479   6317    819    729    769       O  
ATOM   6393  OD2 ASP C 835     -87.628  49.667 -31.811  1.00 46.10           O  
ANISOU 6393  OD2 ASP C 835     6084   5771   5660    897    796    793       O  
ATOM   6394  N   ILE C 836     -86.980  46.838 -28.087  1.00 33.81           N  
ANISOU 6394  N   ILE C 836     4473   4201   4173    654    646    598       N  
ATOM   6395  CA  ILE C 836     -87.063  45.729 -27.175  1.00 31.65           C  
ANISOU 6395  CA  ILE C 836     4164   3958   3905    597    596    555       C  
ATOM   6396  C   ILE C 836     -88.227  44.883 -27.608  1.00 32.94           C  
ANISOU 6396  C   ILE C 836     4247   4235   4034    618    561    582       C  
ATOM   6397  O   ILE C 836     -89.358  45.383 -27.700  1.00 36.85           O  
ANISOU 6397  O   ILE C 836     4723   4779   4500    691    588    629       O  
ATOM   6398  CB  ILE C 836     -87.282  46.193 -25.739  1.00 32.73           C  
ANISOU 6398  CB  ILE C 836     4343   4044   4050    604    622    536       C  
ATOM   6399  CG1 ILE C 836     -86.154  47.126 -25.305  1.00 32.19           C  
ANISOU 6399  CG1 ILE C 836     4355   3863   4013    580    660    503       C  
ATOM   6400  CG2 ILE C 836     -87.320  44.993 -24.806  1.00 31.94           C  
ANISOU 6400  CG2 ILE C 836     4207   3975   3954    547    571    495       C  
ATOM   6401  CD1 ILE C 836     -86.396  47.810 -23.974  1.00 31.92           C  
ANISOU 6401  CD1 ILE C 836     4373   3774   3983    597    696    485       C  
ATOM   6402  N   PHE C 837     -87.955  43.616 -27.901  1.00 30.40           N  
ANISOU 6402  N   PHE C 837     3878   3959   3715    555    504    553       N  
ATOM   6403  CA  PHE C 837     -88.982  42.689 -28.308  1.00 30.68           C  
ANISOU 6403  CA  PHE C 837     3835   4102   3721    555    468    567       C  
ATOM   6404  C   PHE C 837     -89.184  41.601 -27.250  1.00 29.87           C  
ANISOU 6404  C   PHE C 837     3710   4011   3627    497    435    529       C  
ATOM   6405  O   PHE C 837     -88.226  41.093 -26.681  1.00 28.48           O  
ANISOU 6405  O   PHE C 837     3563   3779   3478    439    416    486       O  
ATOM   6406  CB  PHE C 837     -88.603  42.017 -29.618  1.00 31.86           C  
ANISOU 6406  CB  PHE C 837     3948   4297   3861    528    433    562       C  
ATOM   6407  CG  PHE C 837     -88.346  42.963 -30.763  1.00 33.08           C  
ANISOU 6407  CG  PHE C 837     4122   4446   4003    583    464    601       C  
ATOM   6408  CD1 PHE C 837     -89.389  43.415 -31.538  1.00 34.22           C  
ANISOU 6408  CD1 PHE C 837     4227   4670   4105    658    480    654       C  
ATOM   6409  CD2 PHE C 837     -87.066  43.391 -31.062  1.00 33.29           C  
ANISOU 6409  CD2 PHE C 837     4202   4390   4057    561    479    586       C  
ATOM   6410  CE1 PHE C 837     -89.172  44.291 -32.580  1.00 35.07           C  
ANISOU 6410  CE1 PHE C 837     4356   4772   4197    717    513    696       C  
ATOM   6411  CE2 PHE C 837     -86.837  44.267 -32.111  1.00 34.36           C  
ANISOU 6411  CE2 PHE C 837     4359   4516   4181    611    513    626       C  
ATOM   6412  CZ  PHE C 837     -87.898  44.729 -32.864  1.00 34.05           C  
ANISOU 6412  CZ  PHE C 837     4287   4552   4098    693    532    683       C  
ATOM   6413  N   LYS C 838     -90.443  41.250 -27.004  1.00 31.90           N  
ANISOU 6413  N   LYS C 838     3913   4347   3859    517    430    550       N  
ATOM   6414  CA  LYS C 838     -90.790  40.124 -26.168  1.00 34.11           C  
ANISOU 6414  CA  LYS C 838     4164   4652   4144    462    402    522       C  
ATOM   6415  C   LYS C 838     -90.990  38.969 -27.099  1.00 31.67           C  
ANISOU 6415  C   LYS C 838     3795   4416   3823    414    358    509       C  
ATOM   6416  O   LYS C 838     -91.769  39.066 -28.036  1.00 29.84           O  
ANISOU 6416  O   LYS C 838     3510   4267   3560    446    355    538       O  
ATOM   6417  CB  LYS C 838     -92.084  40.375 -25.385  1.00 40.56           C  
ANISOU 6417  CB  LYS C 838     4952   5518   4940    506    425    550       C  
ATOM   6418  CG  LYS C 838     -92.584  39.152 -24.575  1.00 47.35           C  
ANISOU 6418  CG  LYS C 838     5775   6413   5803    447    400    527       C  
ATOM   6419  CD  LYS C 838     -92.613  39.306 -23.057  1.00 59.95           C  
ANISOU 6419  CD  LYS C 838     7410   7958   7410    451    422    517       C  
ATOM   6420  CE  LYS C 838     -93.388  38.176 -22.319  1.00 65.48           C  
ANISOU 6420  CE  LYS C 838     8066   8708   8106    407    408    509       C  
ATOM   6421  NZ  LYS C 838     -93.363  36.796 -22.920  1.00 65.63           N  
ANISOU 6421  NZ  LYS C 838     8041   8767   8128    330    368    485       N  
ATOM   6422  N   ILE C 839     -90.315  37.853 -26.827  1.00 29.17           N  
ANISOU 6422  N   ILE C 839     3486   4071   3527    340    326    466       N  
ATOM   6423  CA  ILE C 839     -90.390  36.691 -27.729  1.00 28.67           C  
ANISOU 6423  CA  ILE C 839     3376   4063   3454    287    286    446       C  
ATOM   6424  C   ILE C 839     -90.863  35.399 -27.051  1.00 28.83           C  
ANISOU 6424  C   ILE C 839     3370   4105   3478    224    267    421       C  
ATOM   6425  O   ILE C 839     -90.506  35.122 -25.904  1.00 29.60           O  
ANISOU 6425  O   ILE C 839     3505   4145   3597    203    273    404       O  
ATOM   6426  CB  ILE C 839     -89.029  36.453 -28.424  1.00 28.08           C  
ANISOU 6426  CB  ILE C 839     3337   3936   3397    257    267    419       C  
ATOM   6427  CG1 ILE C 839     -87.899  36.306 -27.426  1.00 27.70           C  
ANISOU 6427  CG1 ILE C 839     3350   3795   3381    227    268    388       C  
ATOM   6428  CG2 ILE C 839     -88.719  37.602 -29.357  1.00 28.34           C  
ANISOU 6428  CG2 ILE C 839     3384   3964   3421    314    287    449       C  
ATOM   6429  CD1 ILE C 839     -86.604  35.864 -28.064  1.00 27.59           C  
ANISOU 6429  CD1 ILE C 839     3360   3742   3381    192    246    358       C  
ATOM   6430  N   GLU C 840     -91.677  34.625 -27.757  1.00 29.86           N  
ANISOU 6430  N   GLU C 840     3437   4321   3588    194    246    417       N  
ATOM   6431  CA  GLU C 840     -92.150  33.324 -27.288  1.00 29.49           C  
ANISOU 6431  CA  GLU C 840     3365   4295   3546    124    231    391       C  
ATOM   6432  C   GLU C 840     -91.977  32.346 -28.412  1.00 28.96           C  
ANISOU 6432  C   GLU C 840     3272   4262   3471     68    198    360       C  
ATOM   6433  O   GLU C 840     -92.701  32.390 -29.404  1.00 29.47           O  
ANISOU 6433  O   GLU C 840     3276   4417   3505     76    186    368       O  
ATOM   6434  CB  GLU C 840     -93.619  33.359 -26.889  1.00 32.11           C  
ANISOU 6434  CB  GLU C 840     3633   4710   3855    135    245    415       C  
ATOM   6435  CG  GLU C 840     -93.957  34.405 -25.828  1.00 35.36           C  
ANISOU 6435  CG  GLU C 840     4067   5099   4268    200    282    449       C  
ATOM   6436  CD  GLU C 840     -95.468  34.654 -25.642  1.00 39.37           C  
ANISOU 6436  CD  GLU C 840     4503   5709   4746    231    299    482       C  
ATOM   6437  OE1 GLU C 840     -96.318  34.042 -26.343  1.00 42.00           O  
ANISOU 6437  OE1 GLU C 840     4762   6140   5056    199    281    478       O  
ATOM   6438  OE2 GLU C 840     -95.799  35.495 -24.776  1.00 43.47           O  
ANISOU 6438  OE2 GLU C 840     5041   6212   5264    289    332    510       O  
ATOM   6439  N   ARG C 841     -90.952  31.508 -28.310  1.00 28.84           N  
ANISOU 6439  N   ARG C 841     3303   4176   3478     19    183    325       N  
ATOM   6440  CA  ARG C 841     -90.752  30.457 -29.301  1.00 29.25           C  
ANISOU 6440  CA  ARG C 841     3340   4251   3524    -37    155    290       C  
ATOM   6441  C   ARG C 841     -91.778  29.346 -29.097  1.00 29.28           C  
ANISOU 6441  C   ARG C 841     3300   4304   3521   -104    151    270       C  
ATOM   6442  O   ARG C 841     -91.980  28.876 -27.995  1.00 30.84           O  
ANISOU 6442  O   ARG C 841     3516   4466   3735   -130    168    268       O  
ATOM   6443  CB  ARG C 841     -89.338  29.859 -29.205  1.00 27.75           C  
ANISOU 6443  CB  ARG C 841     3217   3970   3359    -64    145    259       C  
ATOM   6444  CG  ARG C 841     -88.182  30.803 -29.520  1.00 27.49           C  
ANISOU 6444  CG  ARG C 841     3224   3887   3333    -15    147    270       C  
ATOM   6445  CD  ARG C 841     -87.079  30.056 -30.256  1.00 28.60           C  
ANISOU 6445  CD  ARG C 841     3394   3994   3480    -46    125    237       C  
ATOM   6446  NE  ARG C 841     -86.747  28.924 -29.496  1.00 30.49           N  
ANISOU 6446  NE  ARG C 841     3665   4183   3735    -93    123    209       N  
ATOM   6447  CZ  ARG C 841     -86.878  27.651 -29.826  1.00 30.21           C  
ANISOU 6447  CZ  ARG C 841     3629   4153   3697   -150    111    178       C  
ATOM   6448  NH1 ARG C 841     -87.229  27.211 -31.016  1.00 29.70           N  
ANISOU 6448  NH1 ARG C 841     3530   4142   3612   -176     93    160       N  
ATOM   6449  NH2 ARG C 841     -86.571  26.791 -28.892  1.00 34.60           N  
ANISOU 6449  NH2 ARG C 841     4225   4651   4269   -179    120    164       N  
ATOM   6450  N   GLU C 842     -92.375  28.898 -30.171  1.00 32.24           N  
ANISOU 6450  N   GLU C 842     3619   4760   3869   -135    130    254       N  
ATOM   6451  CA  GLU C 842     -93.309  27.793 -30.103  1.00 35.46           C  
ANISOU 6451  CA  GLU C 842     3985   5217   4272   -212    127    226       C  
ATOM   6452  C   GLU C 842     -92.681  26.557 -29.504  1.00 32.75           C  
ANISOU 6452  C   GLU C 842     3702   4784   3959   -279    133    191       C  
ATOM   6453  O   GLU C 842     -91.563  26.147 -29.877  1.00 32.46           O  
ANISOU 6453  O   GLU C 842     3719   4681   3934   -288    121    168       O  
ATOM   6454  CB  GLU C 842     -93.906  27.524 -31.482  1.00 39.38           C  
ANISOU 6454  CB  GLU C 842     4413   5817   4731   -237    100    205       C  
ATOM   6455  CG  GLU C 842     -94.972  28.561 -31.801  1.00 46.59           C  
ANISOU 6455  CG  GLU C 842     5250   6845   5608   -176    102    245       C  
ATOM   6456  CD  GLU C 842     -95.452  28.520 -33.235  1.00 52.77           C  
ANISOU 6456  CD  GLU C 842     5964   7741   6346   -180     73    230       C  
ATOM   6457  OE1 GLU C 842     -95.328  27.449 -33.882  1.00 51.22           O  
ANISOU 6457  OE1 GLU C 842     5764   7554   6145   -256     51    179       O  
ATOM   6458  OE2 GLU C 842     -95.940  29.582 -33.686  1.00 56.88           O  
ANISOU 6458  OE2 GLU C 842     6439   8340   6832   -101     74    272       O  
ATOM   6459  N   GLY C 843     -93.369  26.012 -28.508  1.00 29.10           N  
ANISOU 6459  N   GLY C 843     3233   4315   3508   -319    155    192       N  
ATOM   6460  CA  GLY C 843     -92.933  24.795 -27.860  1.00 29.16           C  
ANISOU 6460  CA  GLY C 843     3298   4240   3542   -380    169    165       C  
ATOM   6461  C   GLY C 843     -91.971  24.992 -26.708  1.00 27.98           C  
ANISOU 6461  C   GLY C 843     3225   3990   3418   -340    186    183       C  
ATOM   6462  O   GLY C 843     -91.681  24.038 -25.983  1.00 30.13           O  
ANISOU 6462  O   GLY C 843     3545   4195   3707   -378    204    170       O  
ATOM   6463  N   GLU C 844     -91.407  26.189 -26.560  1.00 26.30           N  
ANISOU 6463  N   GLU C 844     3026   3763   3204   -263    183    210       N  
ATOM   6464  CA  GLU C 844     -90.330  26.357 -25.588  1.00 24.70           C  
ANISOU 6464  CA  GLU C 844     2894   3470   3021   -229    194    217       C  
ATOM   6465  C   GLU C 844     -90.843  26.370 -24.164  1.00 25.90           C  
ANISOU 6465  C   GLU C 844     3056   3604   3180   -222    224    239       C  
ATOM   6466  O   GLU C 844     -90.169  25.853 -23.274  1.00 24.92           O  
ANISOU 6466  O   GLU C 844     2989   3410   3069   -225    236    234       O  
ATOM   6467  CB  GLU C 844     -89.539  27.626 -25.841  1.00 25.00           C  
ANISOU 6467  CB  GLU C 844     2947   3494   3057   -160    185    233       C  
ATOM   6468  CG  GLU C 844     -88.082  27.501 -25.425  1.00 24.92           C  
ANISOU 6468  CG  GLU C 844     3006   3400   3064   -145    181    220       C  
ATOM   6469  CD  GLU C 844     -87.287  28.764 -25.742  1.00 27.30           C  
ANISOU 6469  CD  GLU C 844     3319   3688   3365    -88    176    232       C  
ATOM   6470  OE1 GLU C 844     -87.639  29.816 -25.148  1.00 26.76           O  
ANISOU 6470  OE1 GLU C 844     3245   3626   3295    -45    192    257       O  
ATOM   6471  OE2 GLU C 844     -86.295  28.697 -26.529  1.00 25.00           O  
ANISOU 6471  OE2 GLU C 844     3047   3376   3076    -88    158    215       O  
ATOM   6472  N   CYS C 845     -92.052  26.907 -23.941  1.00 27.37           N  
ANISOU 6472  N   CYS C 845     3186   3860   3354   -210    237    264       N  
ATOM   6473  CA  CYS C 845     -92.675  26.874 -22.597  1.00 29.42           C  
ANISOU 6473  CA  CYS C 845     3449   4112   3617   -204    268    286       C  
ATOM   6474  C   CYS C 845     -92.835  25.450 -22.119  1.00 28.63           C  
ANISOU 6474  C   CYS C 845     3371   3978   3529   -275    285    268       C  
ATOM   6475  O   CYS C 845     -92.457  25.106 -21.022  1.00 26.83           O  
ANISOU 6475  O   CYS C 845     3194   3690   3311   -269    306    275       O  
ATOM   6476  CB  CYS C 845     -94.041  27.604 -22.563  1.00 30.47           C  
ANISOU 6476  CB  CYS C 845     3508   4338   3731   -181    281    315       C  
ATOM   6477  SG  CYS C 845     -94.920  27.471 -20.992  1.00 35.68           S  
ANISOU 6477  SG  CYS C 845     4165   5000   4392   -179    323    343       S  
ATOM   6478  N   GLN C 846     -93.397  24.627 -22.981  1.00 31.94           N  
ANISOU 6478  N   GLN C 846     3753   4438   3945   -344    277    244       N  
ATOM   6479  CA  GLN C 846     -93.631  23.215 -22.676  1.00 33.54           C  
ANISOU 6479  CA  GLN C 846     3978   4606   4160   -423    299    223       C  
ATOM   6480  C   GLN C 846     -92.292  22.505 -22.467  1.00 31.86           C  
ANISOU 6480  C   GLN C 846     3853   4289   3962   -422    298    206       C  
ATOM   6481  O   GLN C 846     -92.143  21.761 -21.512  1.00 35.47           O  
ANISOU 6481  O   GLN C 846     4360   4686   4430   -437    328    212       O  
ATOM   6482  CB  GLN C 846     -94.451  22.541 -23.784  1.00 34.17           C  
ANISOU 6482  CB  GLN C 846     3998   4753   4231   -501    288    191       C  
ATOM   6483  CG  GLN C 846     -94.904  21.127 -23.445  1.00 38.58           C  
ANISOU 6483  CG  GLN C 846     4575   5280   4804   -594    319    168       C  
ATOM   6484  CD  GLN C 846     -95.914  21.051 -22.271  1.00 42.30           C  
ANISOU 6484  CD  GLN C 846     5021   5771   5279   -608    360    198       C  
ATOM   6485  OE1 GLN C 846     -96.751  21.943 -22.083  1.00 44.82           O  
ANISOU 6485  OE1 GLN C 846     5275   6173   5584   -574    359    226       O  
ATOM   6486  NE2 GLN C 846     -95.822  19.991 -21.486  1.00 39.63           N  
ANISOU 6486  NE2 GLN C 846     4740   5358   4959   -654    398    196       N  
ATOM   6487  N   ARG C 847     -91.310  22.772 -23.311  1.00 28.23           N  
ANISOU 6487  N   ARG C 847     3414   3811   3501   -397    268    189       N  
ATOM   6488  CA  ARG C 847     -89.964  22.201 -23.118  1.00 29.16           C  
ANISOU 6488  CA  ARG C 847     3611   3840   3628   -383    266    176       C  
ATOM   6489  C   ARG C 847     -89.296  22.673 -21.784  1.00 27.31           C  
ANISOU 6489  C   ARG C 847     3424   3556   3397   -320    280    203       C  
ATOM   6490  O   ARG C 847     -88.652  21.889 -21.100  1.00 27.61           O  
ANISOU 6490  O   ARG C 847     3523   3528   3441   -320    297    201       O  
ATOM   6491  CB  ARG C 847     -89.070  22.536 -24.310  1.00 29.22           C  
ANISOU 6491  CB  ARG C 847     3621   3849   3630   -363    231    155       C  
ATOM   6492  CG  ARG C 847     -87.702  21.887 -24.305  1.00 30.00           C  
ANISOU 6492  CG  ARG C 847     3792   3870   3735   -352    227    138       C  
ATOM   6493  CD  ARG C 847     -86.893  22.375 -25.526  1.00 31.19           C  
ANISOU 6493  CD  ARG C 847     3935   4036   3879   -329    193    122       C  
ATOM   6494  NE  ARG C 847     -86.369  23.735 -25.345  1.00 30.39           N  
ANISOU 6494  NE  ARG C 847     3824   3947   3776   -262    181    144       N  
ATOM   6495  CZ  ARG C 847     -85.506  24.327 -26.176  1.00 34.53           C  
ANISOU 6495  CZ  ARG C 847     4348   4474   4296   -232    158    137       C  
ATOM   6496  NH1 ARG C 847     -85.053  23.679 -27.234  1.00 33.73           N  
ANISOU 6496  NH1 ARG C 847     4256   4369   4190   -256    143    111       N  
ATOM   6497  NH2 ARG C 847     -85.039  25.558 -25.929  1.00 34.91           N  
ANISOU 6497  NH2 ARG C 847     4393   4525   4346   -178    154    156       N  
ATOM   6498  N   TYR C 848     -89.484  23.935 -21.423  1.00 24.41           N  
ANISOU 6498  N   TYR C 848     3029   3223   3024   -266    276    226       N  
ATOM   6499  CA  TYR C 848     -88.875  24.484 -20.234  1.00 23.76           C  
ANISOU 6499  CA  TYR C 848     2985   3102   2940   -209    286    244       C  
ATOM   6500  C   TYR C 848     -89.555  24.057 -18.942  1.00 25.47           C  
ANISOU 6500  C   TYR C 848     3214   3309   3155   -215    322    266       C  
ATOM   6501  O   TYR C 848     -88.956  24.148 -17.881  1.00 23.00           O  
ANISOU 6501  O   TYR C 848     2945   2957   2838   -175    332    276       O  
ATOM   6502  CB  TYR C 848     -88.910  26.009 -20.335  1.00 23.04           C  
ANISOU 6502  CB  TYR C 848     2865   3047   2842   -153    274    258       C  
ATOM   6503  CG  TYR C 848     -88.248  26.767 -19.246  1.00 22.30           C  
ANISOU 6503  CG  TYR C 848     2808   2920   2745    -96    280    268       C  
ATOM   6504  CD1 TYR C 848     -86.876  26.755 -19.119  1.00 22.26           C  
ANISOU 6504  CD1 TYR C 848     2849   2866   2741    -75    265    251       C  
ATOM   6505  CD2 TYR C 848     -88.980  27.558 -18.369  1.00 24.46           C  
ANISOU 6505  CD2 TYR C 848     3066   3217   3011    -62    301    292       C  
ATOM   6506  CE1 TYR C 848     -86.236  27.489 -18.152  1.00 22.48           C  
ANISOU 6506  CE1 TYR C 848     2906   2872   2763    -28    268    253       C  
ATOM   6507  CE2 TYR C 848     -88.348  28.304 -17.365  1.00 24.13           C  
ANISOU 6507  CE2 TYR C 848     3060   3145   2963    -12    306    294       C  
ATOM   6508  CZ  TYR C 848     -86.965  28.273 -17.283  1.00 24.08           C  
ANISOU 6508  CZ  TYR C 848     3097   3093   2958      2    288    272       C  
ATOM   6509  OH  TYR C 848     -86.283  28.933 -16.282  1.00 24.26           O  
ANISOU 6509  OH  TYR C 848     3153   3093   2972     45    291    267       O  
ATOM   6510  N   LYS C 849     -90.809  23.590 -19.044  1.00 29.07           N  
ANISOU 6510  N   LYS C 849     3626   3806   3612   -266    341    272       N  
ATOM   6511  CA  LYS C 849     -91.685  23.316 -17.872  1.00 32.46           C  
ANISOU 6511  CA  LYS C 849     4053   4242   4040   -273    380    298       C  
ATOM   6512  C   LYS C 849     -91.011  22.535 -16.738  1.00 33.35           C  
ANISOU 6512  C   LYS C 849     4239   4280   4153   -261    406    306       C  
ATOM   6513  O   LYS C 849     -91.065  22.989 -15.594  1.00 32.02           O  
ANISOU 6513  O   LYS C 849     4084   4107   3974   -215    423    330       O  
ATOM   6514  CB  LYS C 849     -92.999  22.605 -18.256  1.00 35.38           C  
ANISOU 6514  CB  LYS C 849     4368   4660   4413   -350    399    296       C  
ATOM   6515  N   PRO C 850     -90.344  21.403 -17.054  1.00 31.80           N  
ANISOU 6515  N   PRO C 850     4092   4027   3965   -295    409    287       N  
ATOM   6516  CA  PRO C 850     -89.684  20.679 -15.949  1.00 32.90           C  
ANISOU 6516  CA  PRO C 850     4304   4099   4099   -270    436    301       C  
ATOM   6517  C   PRO C 850     -88.655  21.528 -15.196  1.00 31.01           C  
ANISOU 6517  C   PRO C 850     4093   3847   3843   -187    418    309       C  
ATOM   6518  O   PRO C 850     -88.468  21.340 -14.006  1.00 30.44           O  
ANISOU 6518  O   PRO C 850     4057   3750   3757   -151    442    330       O  
ATOM   6519  CB  PRO C 850     -88.974  19.511 -16.646  1.00 33.71           C  
ANISOU 6519  CB  PRO C 850     4455   4144   4210   -306    436    277       C  
ATOM   6520  CG  PRO C 850     -89.631  19.389 -17.982  1.00 31.99           C  
ANISOU 6520  CG  PRO C 850     4185   3965   4003   -373    420    249       C  
ATOM   6521  CD  PRO C 850     -90.092  20.768 -18.356  1.00 30.95           C  
ANISOU 6521  CD  PRO C 850     3983   3912   3867   -345    389    254       C  
ATOM   6522  N   PHE C 851     -88.040  22.506 -15.864  1.00 32.31           N  
ANISOU 6522  N   PHE C 851     4237   4033   4007   -157    379    292       N  
ATOM   6523  CA  PHE C 851     -86.983  23.298 -15.212  1.00 29.83           C  
ANISOU 6523  CA  PHE C 851     3949   3707   3679    -89    362    291       C  
ATOM   6524  C   PHE C 851     -87.484  24.488 -14.511  1.00 29.79           C  
ANISOU 6524  C   PHE C 851     3917   3737   3664    -50    365    305       C  
ATOM   6525  O   PHE C 851     -86.750  25.075 -13.737  1.00 30.48           O  
ANISOU 6525  O   PHE C 851     4030   3815   3737      0    359    303       O  
ATOM   6526  CB  PHE C 851     -85.925  23.653 -16.200  1.00 30.40           C  
ANISOU 6526  CB  PHE C 851     4023   3773   3755    -79    324    264       C  
ATOM   6527  CG  PHE C 851     -85.153  22.469 -16.634  1.00 31.21           C  
ANISOU 6527  CG  PHE C 851     4167   3832   3859    -98    323    250       C  
ATOM   6528  CD1 PHE C 851     -84.225  21.906 -15.779  1.00 35.46           C  
ANISOU 6528  CD1 PHE C 851     4759   4332   4382    -60    332    255       C  
ATOM   6529  CD2 PHE C 851     -85.375  21.896 -17.851  1.00 32.77           C  
ANISOU 6529  CD2 PHE C 851     4351   4029   4071   -149    315    233       C  
ATOM   6530  CE1 PHE C 851     -83.500  20.788 -16.154  1.00 36.16           C  
ANISOU 6530  CE1 PHE C 851     4893   4378   4470    -67    336    245       C  
ATOM   6531  CE2 PHE C 851     -84.664  20.782 -18.243  1.00 34.42           C  
ANISOU 6531  CE2 PHE C 851     4605   4192   4280   -163    318    219       C  
ATOM   6532  CZ  PHE C 851     -83.728  20.228 -17.396  1.00 35.52           C  
ANISOU 6532  CZ  PHE C 851     4803   4289   4405   -120    330    227       C  
ATOM   6533  N   LYS C 852     -88.741  24.853 -14.751  1.00 31.01           N  
ANISOU 6533  N   LYS C 852     4021   3937   3824    -72    377    319       N  
ATOM   6534  CA  LYS C 852     -89.333  25.952 -14.016  1.00 36.64           C  
ANISOU 6534  CA  LYS C 852     4712   4684   4526    -30    388    337       C  
ATOM   6535  C   LYS C 852     -89.349  25.619 -12.525  1.00 39.67           C  
ANISOU 6535  C   LYS C 852     5133   5047   4892     -2    418    356       C  
ATOM   6536  O   LYS C 852     -89.448  26.518 -11.727  1.00 45.17           O  
ANISOU 6536  O   LYS C 852     5831   5757   5574     45    424    364       O  
ATOM   6537  CB  LYS C 852     -90.706  26.412 -14.594  1.00 38.61           C  
ANISOU 6537  CB  LYS C 852     4894   4995   4780    -51    397    352       C  
ATOM   6538  N   GLN C 853     -89.218  24.336 -12.151  1.00 42.74           N  
ANISOU 6538  N   GLN C 853     5559   5401   5281    -27    439    363       N  
ATOM   6539  CA  GLN C 853     -89.202  23.942 -10.720  1.00 44.35           C  
ANISOU 6539  CA  GLN C 853     5802   5585   5464      6    471    386       C  
ATOM   6540  C   GLN C 853     -87.921  24.236 -10.021  1.00 41.03           C  
ANISOU 6540  C   GLN C 853     5427   5141   5020     65    453    374       C  
ATOM   6541  O   GLN C 853     -87.811  24.225  -8.807  1.00 38.21           O  
ANISOU 6541  O   GLN C 853     5099   4782   4638    108    472    389       O  
ATOM   6542  CB  GLN C 853     -89.315  22.431 -10.551  1.00 49.31           C  
ANISOU 6542  CB  GLN C 853     6466   6172   6097    -34    504    400       C  
ATOM   6543  CG  GLN C 853     -90.658  21.902 -10.942  1.00 54.79           C  
ANISOU 6543  CG  GLN C 853     7120   6888   6809   -103    533    413       C  
ATOM   6544  CD  GLN C 853     -91.706  22.720 -10.239  1.00 57.45           C  
ANISOU 6544  CD  GLN C 853     7414   7278   7135    -81    552    437       C  
ATOM   6545  OE1 GLN C 853     -92.349  23.577 -10.843  1.00 52.09           O  
ANISOU 6545  OE1 GLN C 853     6676   6652   6463    -87    536    433       O  
ATOM   6546  NE2 GLN C 853     -91.790  22.546  -8.918  1.00 59.74           N  
ANISOU 6546  NE2 GLN C 853     7738   7557   7405    -44    586    464       N  
ATOM   6547  N   LEU C 854     -86.907  24.359 -10.823  1.00 38.12           N  
ANISOU 6547  N   LEU C 854     5066   4758   4659     65    418    345       N  
ATOM   6548  CA  LEU C 854     -85.612  24.585 -10.286  1.00 35.70           C  
ANISOU 6548  CA  LEU C 854     4795   4438   4330    115    397    328       C  
ATOM   6549  C   LEU C 854     -85.556  26.004  -9.696  1.00 34.78           C  
ANISOU 6549  C   LEU C 854     4664   4352   4200    157    386    317       C  
ATOM   6550  O   LEU C 854     -86.221  26.944 -10.152  1.00 30.72           O  
ANISOU 6550  O   LEU C 854     4113   3861   3700    148    383    315       O  
ATOM   6551  CB  LEU C 854     -84.646  24.440 -11.422  1.00 35.12           C  
ANISOU 6551  CB  LEU C 854     4723   4350   4271     99    364    301       C  
ATOM   6552  CG  LEU C 854     -83.435  23.592 -11.247  1.00 37.24           C  
ANISOU 6552  CG  LEU C 854     5036   4590   4523    122    356    294       C  
ATOM   6553  CD1 LEU C 854     -83.791  22.227 -10.664  1.00 38.15           C  
ANISOU 6553  CD1 LEU C 854     5193   4673   4631    116    397    323       C  
ATOM   6554  CD2 LEU C 854     -82.769  23.459 -12.595  1.00 33.90           C  
ANISOU 6554  CD2 LEU C 854     4604   4157   4120     95    328    269       C  
ATOM   6555  N   HIS C 855     -84.834  26.138  -8.619  1.00 33.24           N  
ANISOU 6555  N   HIS C 855     4500   4157   3974    205    384    311       N  
ATOM   6556  CA AHIS C 855     -84.595  27.429  -7.992  0.50 33.04           C  
ANISOU 6556  CA AHIS C 855     4470   4153   3930    243    373    290       C  
ATOM   6557  CA BHIS C 855     -84.650  27.463  -8.039  0.50 36.64           C  
ANISOU 6557  CA BHIS C 855     4924   4610   4388    241    373    290       C  
ATOM   6558  C   HIS C 855     -83.530  28.172  -8.807  1.00 36.03           C  
ANISOU 6558  C   HIS C 855     4840   4529   4320    238    334    250       C  
ATOM   6559  O   HIS C 855     -82.956  27.608  -9.759  1.00 35.47           O  
ANISOU 6559  O   HIS C 855     4767   4444   4266    212    316    242       O  
ATOM   6560  CB AHIS C 855     -84.134  27.220  -6.538  0.50 32.22           C  
ANISOU 6560  CB AHIS C 855     4402   4058   3783    295    383    293       C  
ATOM   6561  CB BHIS C 855     -84.431  27.376  -6.538  0.50 40.58           C  
ANISOU 6561  CB BHIS C 855     5454   5119   4844    292    388    296       C  
ATOM   6562  CG AHIS C 855     -82.873  26.415  -6.407  0.50 29.34           C  
ANISOU 6562  CG AHIS C 855     4066   3684   3397    314    365    282       C  
ATOM   6563  CG BHIS C 855     -85.580  26.720  -5.827  0.50 44.27           C  
ANISOU 6563  CG BHIS C 855     5926   5589   5304    293    431    340       C  
ATOM   6564  ND1AHIS C 855     -82.786  25.094  -6.789  0.50 28.82           N  
ANISOU 6564  ND1AHIS C 855     4020   3591   3339    297    377    304       N  
ATOM   6565  ND1BHIS C 855     -86.865  26.735  -6.340  0.50 44.17           N  
ANISOU 6565  ND1BHIS C 855     5880   5583   5319    256    454    363       N  
ATOM   6566  CD2AHIS C 855     -81.648  26.748  -5.944  0.50 27.91           C  
ANISOU 6566  CD2AHIS C 855     3896   3521   3185    350    337    250       C  
ATOM   6567  CD2BHIS C 855     -85.647  26.040  -4.657  0.50 43.91           C  
ANISOU 6567  CD2BHIS C 855     5913   5544   5225    327    459    365       C  
ATOM   6568  CE1AHIS C 855     -81.568  24.648  -6.569  0.50 27.42           C  
ANISOU 6568  CE1AHIS C 855     3868   3416   3136    330    359    292       C  
ATOM   6569  CE1BHIS C 855     -87.667  26.081  -5.521  0.50 45.74           C  
ANISOU 6569  CE1BHIS C 855     6088   5785   5504    261    494    400       C  
ATOM   6570  NE2AHIS C 855     -80.857  25.635  -6.059  0.50 26.69           N  
ANISOU 6570  NE2AHIS C 855     3765   3356   3019    361    333    258       N  
ATOM   6571  NE2BHIS C 855     -86.955  25.658  -4.488  0.50 45.62           N  
ANISOU 6571  NE2BHIS C 855     6117   5764   5454    306    499    403       N  
ATOM   6572  N   ASN C 856     -83.255  29.412  -8.434  1.00 36.07           N  
ANISOU 6572  N   ASN C 856     4843   4547   4316    260    325    224       N  
ATOM   6573  CA  ASN C 856     -82.154  30.177  -9.014  1.00 32.34           C  
ANISOU 6573  CA  ASN C 856     4367   4071   3851    254    294    184       C  
ATOM   6574  C   ASN C 856     -82.293  30.330 -10.545  1.00 32.07           C  
ANISOU 6574  C   ASN C 856     4306   4025   3854    215    284    185       C  
ATOM   6575  O   ASN C 856     -81.420  29.941 -11.335  1.00 29.68           O  
ANISOU 6575  O   ASN C 856     4002   3715   3562    197    261    170       O  
ATOM   6576  CB  ASN C 856     -80.840  29.529  -8.606  1.00 33.00           C  
ANISOU 6576  CB  ASN C 856     4470   4160   3908    272    272    164       C  
ATOM   6577  CG  ASN C 856     -79.661  30.379  -8.936  1.00 36.07           C  
ANISOU 6577  CG  ASN C 856     4851   4556   4297    267    243    117       C  
ATOM   6578  OD1 ASN C 856     -79.789  31.566  -9.151  1.00 39.94           O  
ANISOU 6578  OD1 ASN C 856     5333   5042   4801    257    244     97       O  
ATOM   6579  ND2 ASN C 856     -78.495  29.760  -9.035  1.00 40.38           N  
ANISOU 6579  ND2 ASN C 856     5401   5113   4828    273    220    102       N  
ATOM   6580  N   ARG C 857     -83.436  30.870 -10.934  1.00 28.21           N  
ANISOU 6580  N   ARG C 857     3795   3540   3383    207    302    205       N  
ATOM   6581  CA  ARG C 857     -83.724  31.175 -12.290  1.00 27.31           C  
ANISOU 6581  CA  ARG C 857     3652   3425   3297    179    295    210       C  
ATOM   6582  C   ARG C 857     -83.355  32.612 -12.549  1.00 28.30           C  
ANISOU 6582  C   ARG C 857     3779   3544   3430    191    292    187       C  
ATOM   6583  O   ARG C 857     -83.747  33.506 -11.809  1.00 27.42           O  
ANISOU 6583  O   ARG C 857     3679   3433   3308    218    311    185       O  
ATOM   6584  CB  ARG C 857     -85.187  30.920 -12.552  1.00 29.72           C  
ANISOU 6584  CB  ARG C 857     3930   3751   3612    167    318    246       C  
ATOM   6585  CG  ARG C 857     -85.419  29.448 -12.749  1.00 31.55           C  
ANISOU 6585  CG  ARG C 857     4160   3981   3847    135    320    262       C  
ATOM   6586  CD  ARG C 857     -86.812  28.925 -12.544  1.00 35.35           C  
ANISOU 6586  CD  ARG C 857     4618   4485   4330    119    349    295       C  
ATOM   6587  NE  ARG C 857     -87.872  29.898 -12.511  1.00 37.47           N  
ANISOU 6587  NE  ARG C 857     4855   4785   4597    137    366    312       N  
ATOM   6588  CZ  ARG C 857     -88.618  30.186 -11.454  1.00 45.29           C  
ANISOU 6588  CZ  ARG C 857     5847   5791   5572    165    394    331       C  
ATOM   6589  NH1 ARG C 857     -88.406  29.597 -10.272  1.00 45.86           N  
ANISOU 6589  NH1 ARG C 857     5951   5849   5624    180    408    336       N  
ATOM   6590  NH2 ARG C 857     -89.596  31.088 -11.596  1.00 49.83           N  
ANISOU 6590  NH2 ARG C 857     6388   6398   6145    185    410    348       N  
ATOM   6591  N   ARG C 858     -82.550  32.835 -13.586  1.00 27.90           N  
ANISOU 6591  N   ARG C 858     3721   3482   3396    172    272    169       N  
ATOM   6592  CA  ARG C 858     -81.944  34.143 -13.808  1.00 26.67           C  
ANISOU 6592  CA  ARG C 858     3574   3310   3247    177    272    143       C  
ATOM   6593  C   ARG C 858     -82.128  34.620 -15.226  1.00 24.61           C  
ANISOU 6593  C   ARG C 858     3294   3046   3012    163    272    154       C  
ATOM   6594  O   ARG C 858     -81.979  33.826 -16.169  1.00 22.40           O  
ANISOU 6594  O   ARG C 858     2995   2774   2742    139    255    162       O  
ATOM   6595  CB  ARG C 858     -80.479  34.144 -13.532  1.00 28.00           C  
ANISOU 6595  CB  ARG C 858     3759   3472   3408    170    249    102       C  
ATOM   6596  CG  ARG C 858     -80.083  34.922 -12.334  1.00 31.94           C  
ANISOU 6596  CG  ARG C 858     4282   3968   3886    189    256     70       C  
ATOM   6597  CD  ARG C 858     -78.591  35.004 -12.040  1.00 33.52           C  
ANISOU 6597  CD  ARG C 858     4488   4174   4073    178    231     23       C  
ATOM   6598  NE  ARG C 858     -78.530  34.275 -10.786  1.00 35.58           N  
ANISOU 6598  NE  ARG C 858     4761   4459   4298    204    226     21       N  
ATOM   6599  CZ  ARG C 858     -77.483  34.192  -9.983  1.00 39.48           C  
ANISOU 6599  CZ  ARG C 858     5262   4977   4762    212    207    -15       C  
ATOM   6600  NH1 ARG C 858     -76.354  34.826 -10.275  1.00 40.72           N  
ANISOU 6600  NH1 ARG C 858     5411   5138   4923    189    190    -60       N  
ATOM   6601  NH2 ARG C 858     -77.582  33.454  -8.888  1.00 38.82           N  
ANISOU 6601  NH2 ARG C 858     5189   4918   4642    245    206     -7       N  
ATOM   6602  N   LEU C 859     -82.372  35.930 -15.351  1.00 21.42           N  
ANISOU 6602  N   LEU C 859     2897   2627   2615    179    293    153       N  
ATOM   6603  CA  LEU C 859     -82.449  36.608 -16.634  1.00 20.02           C  
ANISOU 6603  CA  LEU C 859     2707   2443   2457    176    300    165       C  
ATOM   6604  C   LEU C 859     -81.070  37.104 -17.066  1.00 19.47           C  
ANISOU 6604  C   LEU C 859     2652   2346   2398    155    288    130       C  
ATOM   6605  O   LEU C 859     -80.495  38.011 -16.473  1.00 19.56           O  
ANISOU 6605  O   LEU C 859     2691   2331   2409    157    300    101       O  
ATOM   6606  CB  LEU C 859     -83.453  37.754 -16.575  1.00 19.95           C  
ANISOU 6606  CB  LEU C 859     2704   2429   2447    212    336    189       C  
ATOM   6607  CG  LEU C 859     -83.927  38.230 -17.938  1.00 19.79           C  
ANISOU 6607  CG  LEU C 859     2663   2418   2440    221    346    219       C  
ATOM   6608  CD1 LEU C 859     -84.920  37.269 -18.532  1.00 20.29           C  
ANISOU 6608  CD1 LEU C 859     2680   2533   2498    216    334    252       C  
ATOM   6609  CD2 LEU C 859     -84.575  39.617 -17.808  1.00 21.58           C  
ANISOU 6609  CD2 LEU C 859     2910   2625   2664    266    388    236       C  
ATOM   6610  N   LEU C 860     -80.545  36.474 -18.109  1.00 19.40           N  
ANISOU 6610  N   LEU C 860     2624   2347   2400    132    266    132       N  
ATOM   6611  CA  LEU C 860     -79.133  36.596 -18.489  1.00 20.39           C  
ANISOU 6611  CA  LEU C 860     2756   2458   2533    107    250     99       C  
ATOM   6612  C   LEU C 860     -78.997  36.877 -19.983  1.00 19.77           C  
ANISOU 6612  C   LEU C 860     2662   2377   2471     98    252    114       C  
ATOM   6613  O   LEU C 860     -79.889  36.557 -20.760  1.00 18.93           O  
ANISOU 6613  O   LEU C 860     2534   2292   2366    106    253    148       O  
ATOM   6614  CB  LEU C 860     -78.368  35.326 -18.155  1.00 19.96           C  
ANISOU 6614  CB  LEU C 860     2695   2422   2465     94    219     82       C  
ATOM   6615  CG  LEU C 860     -78.289  34.970 -16.674  1.00 22.81           C  
ANISOU 6615  CG  LEU C 860     3074   2791   2804    107    215     66       C  
ATOM   6616  CD1 LEU C 860     -77.694  33.568 -16.498  1.00 23.72           C  
ANISOU 6616  CD1 LEU C 860     3185   2924   2904    104    190     62       C  
ATOM   6617  CD2 LEU C 860     -77.463  35.995 -15.890  1.00 22.61           C  
ANISOU 6617  CD2 LEU C 860     3067   2753   2772    105    220     24       C  
ATOM   6618  N   TRP C 861     -77.863  37.476 -20.353  1.00 19.27           N  
ANISOU 6618  N   TRP C 861     2608   2295   2420     79    252     89       N  
ATOM   6619  CA  TRP C 861     -77.610  37.875 -21.722  1.00 18.40           C  
ANISOU 6619  CA  TRP C 861     2488   2180   2325     73    259    103       C  
ATOM   6620  C   TRP C 861     -77.007  36.758 -22.545  1.00 18.54           C  
ANISOU 6620  C   TRP C 861     2481   2223   2340     55    227    101       C  
ATOM   6621  O   TRP C 861     -76.253  35.902 -22.047  1.00 17.82           O  
ANISOU 6621  O   TRP C 861     2388   2144   2239     42    202     77       O  
ATOM   6622  CB  TRP C 861     -76.619  39.026 -21.748  1.00 19.43           C  
ANISOU 6622  CB  TRP C 861     2639   2274   2469     55    279     75       C  
ATOM   6623  CG  TRP C 861     -77.047  40.244 -21.012  1.00 19.16           C  
ANISOU 6623  CG  TRP C 861     2639   2202   2439     69    317     70       C  
ATOM   6624  CD1 TRP C 861     -76.574  40.681 -19.813  1.00 19.31           C  
ANISOU 6624  CD1 TRP C 861     2681   2204   2452     56    322     28       C  
ATOM   6625  CD2 TRP C 861     -78.002  41.204 -21.434  1.00 19.28           C  
ANISOU 6625  CD2 TRP C 861     2671   2194   2460    101    357    105       C  
ATOM   6626  NE1 TRP C 861     -77.222  41.819 -19.433  1.00 19.00           N  
ANISOU 6626  NE1 TRP C 861     2676   2126   2418     76    363     34       N  
ATOM   6627  CE2 TRP C 861     -78.086  42.183 -20.429  1.00 20.55           C  
ANISOU 6627  CE2 TRP C 861     2871   2316   2622    107    387     83       C  
ATOM   6628  CE3 TRP C 861     -78.774  41.350 -22.559  1.00 20.30           C  
ANISOU 6628  CE3 TRP C 861     2787   2335   2592    129    370    153       C  
ATOM   6629  CZ2 TRP C 861     -78.929  43.310 -20.536  1.00 20.84           C  
ANISOU 6629  CZ2 TRP C 861     2939   2317   2664    144    436    111       C  
ATOM   6630  CZ3 TRP C 861     -79.628  42.453 -22.653  1.00 20.80           C  
ANISOU 6630  CZ3 TRP C 861     2875   2372   2656    169    416    184       C  
ATOM   6631  CH2 TRP C 861     -79.688  43.408 -21.660  1.00 21.18           C  
ANISOU 6631  CH2 TRP C 861     2966   2374   2707    178    450    164       C  
ATOM   6632  N   HIS C 862     -77.350  36.750 -23.824  1.00 19.22           N  
ANISOU 6632  N   HIS C 862     2551   2320   2431     59    230    128       N  
ATOM   6633  CA  HIS C 862     -76.620  35.932 -24.797  1.00 18.98           C  
ANISOU 6633  CA  HIS C 862     2503   2309   2399     43    206    123       C  
ATOM   6634  C   HIS C 862     -76.536  36.680 -26.104  1.00 18.35           C  
ANISOU 6634  C   HIS C 862     2417   2227   2329     48    223    144       C  
ATOM   6635  O   HIS C 862     -77.556  36.976 -26.729  1.00 17.45           O  
ANISOU 6635  O   HIS C 862     2294   2127   2211     70    236    177       O  
ATOM   6636  CB  HIS C 862     -77.287  34.587 -25.042  1.00 18.84           C  
ANISOU 6636  CB  HIS C 862     2468   2321   2369     42    183    135       C  
ATOM   6637  CG  HIS C 862     -76.533  33.710 -25.998  1.00 20.10           C  
ANISOU 6637  CG  HIS C 862     2616   2496   2524     28    160    127       C  
ATOM   6638  ND1 HIS C 862     -75.564  32.813 -25.588  1.00 21.39           N  
ANISOU 6638  ND1 HIS C 862     2787   2658   2680     18    140    101       N  
ATOM   6639  CD2 HIS C 862     -76.612  33.581 -27.338  1.00 20.96           C  
ANISOU 6639  CD2 HIS C 862     2708   2623   2631     27    156    140       C  
ATOM   6640  CE1 HIS C 862     -75.091  32.163 -26.635  1.00 21.19           C  
ANISOU 6640  CE1 HIS C 862     2753   2647   2652     12    126    100       C  
ATOM   6641  NE2 HIS C 862     -75.682  32.638 -27.713  1.00 21.79           N  
ANISOU 6641  NE2 HIS C 862     2814   2735   2731     15    135    121       N  
ATOM   6642  N   GLY C 863     -75.314  36.983 -26.507  1.00 19.00           N  
ANISOU 6642  N   GLY C 863     2502   2297   2419     30    224    124       N  
ATOM   6643  CA  GLY C 863     -75.069  37.683 -27.780  1.00 20.67           C  
ANISOU 6643  CA  GLY C 863     2710   2504   2639     34    244    145       C  
ATOM   6644  C   GLY C 863     -74.590  36.735 -28.859  1.00 20.80           C  
ANISOU 6644  C   GLY C 863     2705   2553   2647     28    218    146       C  
ATOM   6645  O   GLY C 863     -73.980  35.706 -28.561  1.00 20.62           O  
ANISOU 6645  O   GLY C 863     2674   2544   2616     13    190    122       O  
ATOM   6646  N   SER C 864     -74.903  37.072 -30.097  1.00 21.30           N  
ANISOU 6646  N   SER C 864     2758   2629   2706     44    231    176       N  
ATOM   6647  CA  SER C 864     -74.548  36.258 -31.237  1.00 22.90           C  
ANISOU 6647  CA  SER C 864     2941   2864   2896     42    210    179       C  
ATOM   6648  C   SER C 864     -74.596  37.149 -32.488  1.00 22.94           C  
ANISOU 6648  C   SER C 864     2944   2872   2900     62    238    212       C  
ATOM   6649  O   SER C 864     -75.207  38.193 -32.468  1.00 22.43           O  
ANISOU 6649  O   SER C 864     2892   2789   2841     84    271    238       O  
ATOM   6650  CB  SER C 864     -75.533  35.105 -31.372  1.00 22.78           C  
ANISOU 6650  CB  SER C 864     2909   2884   2861     47    182    183       C  
ATOM   6651  OG  SER C 864     -75.022  34.106 -32.238  1.00 24.46           O  
ANISOU 6651  OG  SER C 864     3110   3122   3061     38    158    172       O  
ATOM   6652  N   ARG C 865     -73.946  36.719 -33.556  1.00 23.97           N  
ANISOU 6652  N   ARG C 865     3062   3026   3022     60    228    212       N  
ATOM   6653  CA  ARG C 865     -73.978  37.427 -34.822  1.00 27.02           C  
ANISOU 6653  CA  ARG C 865     3445   3422   3401     83    253    246       C  
ATOM   6654  C   ARG C 865     -75.394  37.467 -35.350  1.00 26.02           C  
ANISOU 6654  C   ARG C 865     3304   3331   3251    120    254    280       C  
ATOM   6655  O   ARG C 865     -76.155  36.508 -35.203  1.00 24.98           O  
ANISOU 6655  O   ARG C 865     3154   3235   3104    116    222    271       O  
ATOM   6656  CB  ARG C 865     -73.077  36.760 -35.868  1.00 28.86           C  
ANISOU 6656  CB  ARG C 865     3662   3682   3621     77    237    237       C  
ATOM   6657  CG  ARG C 865     -71.595  36.881 -35.604  1.00 32.14           C  
ANISOU 6657  CG  ARG C 865     4082   4074   4054     47    243    210       C  
ATOM   6658  CD  ARG C 865     -70.820  35.899 -36.486  1.00 35.58           C  
ANISOU 6658  CD  ARG C 865     4501   4547   4473     45    219    198       C  
ATOM   6659  NE  ARG C 865     -69.442  35.744 -36.001  1.00 39.16           N  
ANISOU 6659  NE  ARG C 865     4950   4990   4938     18    216    166       N  
ATOM   6660  CZ  ARG C 865     -68.424  36.498 -36.389  1.00 42.41           C  
ANISOU 6660  CZ  ARG C 865     5358   5393   5362      5    244    168       C  
ATOM   6661  NH1 ARG C 865     -67.222  36.286 -35.884  1.00 47.10           N  
ANISOU 6661  NH1 ARG C 865     5940   5992   5963    -21    237    136       N  
ATOM   6662  NH2 ARG C 865     -68.596  37.472 -37.276  1.00 46.01           N  
ANISOU 6662  NH2 ARG C 865     5821   5838   5822     17    282    204       N  
ATOM   6663  N   THR C 866     -75.723  38.583 -35.976  1.00 26.83           N  
ANISOU 6663  N   THR C 866     3415   3428   3350    154    292    320       N  
ATOM   6664  CA  THR C 866     -77.046  38.815 -36.541  1.00 27.42           C  
ANISOU 6664  CA  THR C 866     3474   3547   3398    200    298    360       C  
ATOM   6665  C   THR C 866     -77.486  37.732 -37.498  1.00 26.35           C  
ANISOU 6665  C   THR C 866     3300   3482   3228    203    259    356       C  
ATOM   6666  O   THR C 866     -78.661  37.304 -37.466  1.00 25.86           O  
ANISOU 6666  O   THR C 866     3212   3469   3145    216    240    363       O  
ATOM   6667  CB  THR C 866     -77.084  40.200 -37.202  1.00 28.02           C  
ANISOU 6667  CB  THR C 866     3572   3602   3474    243    352    407       C  
ATOM   6668  OG1 THR C 866     -76.702  41.170 -36.210  1.00 26.96           O  
ANISOU 6668  OG1 THR C 866     3477   3393   3373    231    390    402       O  
ATOM   6669  CG2 THR C 866     -78.484  40.551 -37.668  1.00 27.43           C  
ANISOU 6669  CG2 THR C 866     3478   3577   3366    302    362    453       C  
ATOM   6670  N   THR C 867     -76.542  37.221 -38.283  1.00 26.21           N  
ANISOU 6670  N   THR C 867     3279   3474   3205    188    246    341       N  
ATOM   6671  CA  THR C 867     -76.825  36.142 -39.243  1.00 25.21           C  
ANISOU 6671  CA  THR C 867     3122   3411   3045    187    209    330       C  
ATOM   6672  C   THR C 867     -77.186  34.805 -38.595  1.00 25.27           C  
ANISOU 6672  C   THR C 867     3118   3431   3051    149    168    289       C  
ATOM   6673  O   THR C 867     -77.552  33.853 -39.300  1.00 24.66           O  
ANISOU 6673  O   THR C 867     3020   3403   2946    141    139    273       O  
ATOM   6674  CB  THR C 867     -75.646  35.940 -40.230  1.00 25.19           C  
ANISOU 6674  CB  THR C 867     3123   3412   3036    184    210    324       C  
ATOM   6675  OG1 THR C 867     -74.410  35.833 -39.528  1.00 23.23           O  
ANISOU 6675  OG1 THR C 867     2895   3111   2819    150    212    295       O  
ATOM   6676  CG2 THR C 867     -75.563  37.141 -41.189  1.00 26.34           C  
ANISOU 6676  CG2 THR C 867     3274   3562   3171    229    252    373       C  
ATOM   6677  N   ASN C 868     -77.065  34.711 -37.267  1.00 23.91           N  
ANISOU 6677  N   ASN C 868     2964   3213   2907    125    167    270       N  
ATOM   6678  CA  ASN C 868     -77.465  33.516 -36.571  1.00 24.22           C  
ANISOU 6678  CA  ASN C 868     2999   3258   2946     93    137    238       C  
ATOM   6679  C   ASN C 868     -78.897  33.553 -36.076  1.00 24.90           C  
ANISOU 6679  C   ASN C 868     3066   3371   3024     98    136    251       C  
ATOM   6680  O   ASN C 868     -79.420  32.527 -35.701  1.00 25.63           O  
ANISOU 6680  O   ASN C 868     3149   3477   3111     70    113    228       O  
ATOM   6681  CB  ASN C 868     -76.576  33.257 -35.358  1.00 23.52           C  
ANISOU 6681  CB  ASN C 868     2937   3114   2884     67    136    210       C  
ATOM   6682  CG  ASN C 868     -75.131  32.920 -35.695  1.00 22.89           C  
ANISOU 6682  CG  ASN C 868     2870   3017   2809     57    130    190       C  
ATOM   6683  OD1 ASN C 868     -74.248  33.303 -34.963  1.00 26.06           O  
ANISOU 6683  OD1 ASN C 868     3287   3383   3232     48    141    179       O  
ATOM   6684  ND2 ASN C 868     -74.893  32.231 -36.743  1.00 23.16           N  
ANISOU 6684  ND2 ASN C 868     2895   3081   2823     57    115    182       N  
ATOM   6685  N   PHE C 869     -79.541  34.710 -36.079  1.00 27.02           N  
ANISOU 6685  N   PHE C 869     3329   3648   3291    136    163    288       N  
ATOM   6686  CA  PHE C 869     -80.801  34.858 -35.344  1.00 28.93           C  
ANISOU 6686  CA  PHE C 869     3555   3909   3529    145    167    302       C  
ATOM   6687  C   PHE C 869     -82.049  34.195 -35.916  1.00 31.01           C  
ANISOU 6687  C   PHE C 869     3771   4252   3758    143    145    304       C  
ATOM   6688  O   PHE C 869     -82.975  33.869 -35.180  1.00 30.79           O  
ANISOU 6688  O   PHE C 869     3727   4242   3730    131    140    301       O  
ATOM   6689  CB  PHE C 869     -81.067  36.305 -35.015  1.00 28.62           C  
ANISOU 6689  CB  PHE C 869     3531   3845   3497    189    208    340       C  
ATOM   6690  CG  PHE C 869     -80.470  36.701 -33.701  1.00 28.85           C  
ANISOU 6690  CG  PHE C 869     3598   3802   3560    174    224    325       C  
ATOM   6691  CD1 PHE C 869     -79.157  37.073 -33.626  1.00 29.58           C  
ANISOU 6691  CD1 PHE C 869     3723   3842   3675    159    236    310       C  
ATOM   6692  CD2 PHE C 869     -81.208  36.612 -32.538  1.00 27.54           C  
ANISOU 6692  CD2 PHE C 869     3433   3630   3400    170    226    321       C  
ATOM   6693  CE1 PHE C 869     -78.589  37.436 -32.422  1.00 29.71           C  
ANISOU 6693  CE1 PHE C 869     3769   3801   3717    141    249    289       C  
ATOM   6694  CE2 PHE C 869     -80.644  36.932 -31.336  1.00 28.15           C  
ANISOU 6694  CE2 PHE C 869     3545   3648   3503    156    238    302       C  
ATOM   6695  CZ  PHE C 869     -79.323  37.354 -31.277  1.00 29.16           C  
ANISOU 6695  CZ  PHE C 869     3703   3725   3651    141    248    285       C  
ATOM   6696  N   ALA C 870     -82.062  33.937 -37.211  1.00 32.45           N  
ANISOU 6696  N   ALA C 870     3931   4488   3912    151    131    305       N  
ATOM   6697  CA  ALA C 870     -83.141  33.159 -37.773  1.00 30.63           C  
ANISOU 6697  CA  ALA C 870     3653   4338   3648    137    104    294       C  
ATOM   6698  C   ALA C 870     -83.059  31.761 -37.250  1.00 28.87           C  
ANISOU 6698  C   ALA C 870     3436   4096   3435     73     78    246       C  
ATOM   6699  O   ALA C 870     -84.062  31.160 -36.918  1.00 31.61           O  
ANISOU 6699  O   ALA C 870     3755   4481   3775     46     67    234       O  
ATOM   6700  CB  ALA C 870     -83.072  33.142 -39.293  1.00 34.07           C  
ANISOU 6700  CB  ALA C 870     4064   4836   4044    159     93    300       C  
ATOM   6701  N   GLY C 871     -81.856  31.214 -37.207  1.00 27.27           N  
ANISOU 6701  N   GLY C 871     3272   3839   3252     50     72    219       N  
ATOM   6702  CA  GLY C 871     -81.646  29.891 -36.659  1.00 24.29           C  
ANISOU 6702  CA  GLY C 871     2914   3431   2886     -2     55    177       C  
ATOM   6703  C   GLY C 871     -81.979  29.852 -35.184  1.00 23.63           C  
ANISOU 6703  C   GLY C 871     2845   3307   2828    -16     66    178       C  
ATOM   6704  O   GLY C 871     -82.687  28.949 -34.738  1.00 24.43           O  
ANISOU 6704  O   GLY C 871     2938   3417   2928    -55     58    159       O  
ATOM   6705  N   ILE C 872     -81.498  30.846 -34.425  1.00 22.42           N  
ANISOU 6705  N   ILE C 872     2713   3109   2696     13     88    200       N  
ATOM   6706  CA  ILE C 872     -81.793  30.904 -32.996  1.00 21.74           C  
ANISOU 6706  CA  ILE C 872     2642   2987   2630      6     99    202       C  
ATOM   6707  C   ILE C 872     -83.289  31.038 -32.710  1.00 23.35           C  
ANISOU 6707  C   ILE C 872     2809   3240   2823      8    105    220       C  
ATOM   6708  O   ILE C 872     -83.836  30.329 -31.869  1.00 22.39           O  
ANISOU 6708  O   ILE C 872     2687   3113   2708    -22    103    208       O  
ATOM   6709  CB  ILE C 872     -81.067  32.037 -32.324  1.00 21.26           C  
ANISOU 6709  CB  ILE C 872     2609   2878   2591     35    122    218       C  
ATOM   6710  CG1 ILE C 872     -79.568  31.734 -32.319  1.00 19.97           C  
ANISOU 6710  CG1 ILE C 872     2477   2669   2440     24    116    194       C  
ATOM   6711  CG2 ILE C 872     -81.573  32.266 -30.896  1.00 20.80           C  
ANISOU 6711  CG2 ILE C 872     2562   2794   2546     37    136    223       C  
ATOM   6712  CD1 ILE C 872     -78.748  32.951 -32.011  1.00 20.14           C  
ANISOU 6712  CD1 ILE C 872     2520   2654   2480     47    138    205       C  
ATOM   6713  N   LEU C 873     -83.983  31.894 -33.436  1.00 26.16           N  
ANISOU 6713  N   LEU C 873     3130   3650   3158     45    112    250       N  
ATOM   6714  CA  LEU C 873     -85.425  31.996 -33.220  1.00 27.42           C  
ANISOU 6714  CA  LEU C 873     3246   3871   3301     51    116    268       C  
ATOM   6715  C   LEU C 873     -86.181  30.747 -33.639  1.00 26.31           C  
ANISOU 6715  C   LEU C 873     3068   3786   3142     -1     92    239       C  
ATOM   6716  O   LEU C 873     -87.044  30.268 -32.925  1.00 26.14           O  
ANISOU 6716  O   LEU C 873     3029   3782   3123    -29     94    234       O  
ATOM   6717  CB  LEU C 873     -86.003  33.241 -33.883  1.00 26.91           C  
ANISOU 6717  CB  LEU C 873     3154   3856   3214    114    134    312       C  
ATOM   6718  CG  LEU C 873     -85.474  34.519 -33.266  1.00 27.32           C  
ANISOU 6718  CG  LEU C 873     3247   3846   3287    160    168    340       C  
ATOM   6719  CD1 LEU C 873     -86.120  35.704 -33.968  1.00 28.89           C  
ANISOU 6719  CD1 LEU C 873     3424   4091   3460    229    192    388       C  
ATOM   6720  CD2 LEU C 873     -85.743  34.603 -31.773  1.00 27.52           C  
ANISOU 6720  CD2 LEU C 873     3293   3829   3335    153    183    338       C  
ATOM   6721  N   SER C 874     -85.840  30.178 -34.768  1.00 26.92           N  
ANISOU 6721  N   SER C 874     3138   3889   3202    -19     70    217       N  
ATOM   6722  CA  SER C 874     -86.517  28.987 -35.219  1.00 25.70           C  
ANISOU 6722  CA  SER C 874     2951   3783   3028    -76     48    182       C  
ATOM   6723  C   SER C 874     -86.176  27.739 -34.383  1.00 26.47           C  
ANISOU 6723  C   SER C 874     3090   3817   3152   -136     47    145       C  
ATOM   6724  O   SER C 874     -87.017  26.890 -34.174  1.00 27.43           O  
ANISOU 6724  O   SER C 874     3190   3964   3269   -187     44    123       O  
ATOM   6725  CB  SER C 874     -86.098  28.803 -36.675  1.00 26.53           C  
ANISOU 6725  CB  SER C 874     3046   3927   3105    -72     28    166       C  
ATOM   6726  OG  SER C 874     -85.684  27.521 -37.039  1.00 31.21           O  
ANISOU 6726  OG  SER C 874     3660   4502   3698   -128     11    118       O  
ATOM   6727  N   GLN C 875     -84.934  27.601 -33.936  1.00 26.59           N  
ANISOU 6727  N   GLN C 875     3163   3749   3191   -130     53    137       N  
ATOM   6728  CA  GLN C 875     -84.513  26.366 -33.286  1.00 27.62           C  
ANISOU 6728  CA  GLN C 875     3336   3820   3340   -177     53    105       C  
ATOM   6729  C   GLN C 875     -84.070  26.534 -31.830  1.00 25.74           C  
ANISOU 6729  C   GLN C 875     3137   3513   3128   -163     72    119       C  
ATOM   6730  O   GLN C 875     -83.776  25.549 -31.182  1.00 24.69           O  
ANISOU 6730  O   GLN C 875     3042   3333   3007   -192     77     99       O  
ATOM   6731  CB  GLN C 875     -83.353  25.714 -34.052  1.00 30.26           C  
ANISOU 6731  CB  GLN C 875     3706   4121   3670   -183     41     77       C  
ATOM   6732  CG  GLN C 875     -83.602  25.438 -35.517  1.00 37.16           C  
ANISOU 6732  CG  GLN C 875     4550   5056   4513   -197     21     57       C  
ATOM   6733  CD  GLN C 875     -82.591  24.470 -36.143  1.00 44.53           C  
ANISOU 6733  CD  GLN C 875     5525   5951   5442   -214     12     21       C  
ATOM   6734  OE1 GLN C 875     -81.533  24.200 -35.580  1.00 47.39           O  
ANISOU 6734  OE1 GLN C 875     5937   6247   5824   -202     20     19       O  
ATOM   6735  NE2 GLN C 875     -82.881  24.023 -37.354  1.00 48.70           N  
ANISOU 6735  NE2 GLN C 875     6032   6532   5941   -235     -5     -5       N  
ATOM   6736  N   GLY C 876     -83.965  27.767 -31.349  1.00 24.99           N  
ANISOU 6736  N   GLY C 876     3040   3415   3042   -116     84    150       N  
ATOM   6737  CA  GLY C 876     -83.532  28.026 -29.991  1.00 24.85           C  
ANISOU 6737  CA  GLY C 876     3056   3341   3045   -101    100    159       C  
ATOM   6738  C   GLY C 876     -82.034  27.969 -29.888  1.00 24.87           C  
ANISOU 6738  C   GLY C 876     3103   3289   3058    -87     96    146       C  
ATOM   6739  O   GLY C 876     -81.346  27.606 -30.847  1.00 24.65           O  
ANISOU 6739  O   GLY C 876     3081   3262   3023    -92     83    130       O  
ATOM   6740  N   LEU C 877     -81.518  28.344 -28.729  1.00 23.74           N  
ANISOU 6740  N   LEU C 877     2987   3105   2929    -69    108    151       N  
ATOM   6741  CA  LEU C 877     -80.091  28.212 -28.468  1.00 23.29           C  
ANISOU 6741  CA  LEU C 877     2966   3005   2879    -58    103    135       C  
ATOM   6742  C   LEU C 877     -79.738  26.755 -28.377  1.00 22.50           C  
ANISOU 6742  C   LEU C 877     2894   2882   2775    -82     96    113       C  
ATOM   6743  O   LEU C 877     -80.491  25.952 -27.828  1.00 23.44           O  
ANISOU 6743  O   LEU C 877     3020   2994   2894   -106    104    111       O  
ATOM   6744  CB  LEU C 877     -79.708  28.920 -27.176  1.00 21.98           C  
ANISOU 6744  CB  LEU C 877     2818   2810   2723    -35    116    141       C  
ATOM   6745  CG  LEU C 877     -79.853  30.425 -27.236  1.00 22.50           C  
ANISOU 6745  CG  LEU C 877     2870   2884   2795     -8    129    160       C  
ATOM   6746  CD1 LEU C 877     -79.506  31.026 -25.889  1.00 23.13           C  
ANISOU 6746  CD1 LEU C 877     2972   2934   2882      7    141    157       C  
ATOM   6747  CD2 LEU C 877     -78.981  31.015 -28.313  1.00 22.18           C  
ANISOU 6747  CD2 LEU C 877     2826   2846   2756      1    125    158       C  
ATOM   6748  N   ARG C 878     -78.616  26.408 -28.964  1.00 24.04           N  
ANISOU 6748  N   ARG C 878     3105   3063   2966    -76     86     97       N  
ATOM   6749  CA  ARG C 878     -78.202  25.022 -29.071  1.00 26.56           C  
ANISOU 6749  CA  ARG C 878     3457   3357   3278    -92     82     76       C  
ATOM   6750  C   ARG C 878     -76.792  24.888 -28.591  1.00 24.76           C  
ANISOU 6750  C   ARG C 878     3259   3102   3049    -63     80     69       C  
ATOM   6751  O   ARG C 878     -76.104  25.865 -28.402  1.00 24.89           O  
ANISOU 6751  O   ARG C 878     3264   3124   3070    -39     78     74       O  
ATOM   6752  CB  ARG C 878     -78.321  24.518 -30.524  1.00 28.23           C  
ANISOU 6752  CB  ARG C 878     3657   3591   3477   -112     71     60       C  
ATOM   6753  CG  ARG C 878     -79.731  24.152 -30.953  1.00 31.86           C  
ANISOU 6753  CG  ARG C 878     4092   4084   3932   -152     71     57       C  
ATOM   6754  CD  ARG C 878     -79.965  24.572 -32.411  1.00 35.20           C  
ANISOU 6754  CD  ARG C 878     4478   4559   4339   -154     56     53       C  
ATOM   6755  NE  ARG C 878     -79.883  26.041 -32.508  1.00 37.87           N  
ANISOU 6755  NE  ARG C 878     4788   4922   4681   -116     57     82       N  
ATOM   6756  CZ  ARG C 878     -79.469  26.740 -33.558  1.00 36.16           C  
ANISOU 6756  CZ  ARG C 878     4553   4733   4454    -93     51     90       C  
ATOM   6757  NH1 ARG C 878     -79.087  26.153 -34.682  1.00 38.25           N  
ANISOU 6757  NH1 ARG C 878     4819   5013   4701   -100     38     70       N  
ATOM   6758  NH2 ARG C 878     -79.420  28.053 -33.455  1.00 37.38           N  
ANISOU 6758  NH2 ARG C 878     4692   4896   4615    -60     61    118       N  
ATOM   6759  N   ILE C 879     -76.373  23.645 -28.405  1.00 26.46           N  
ANISOU 6759  N   ILE C 879     3512   3287   3256    -64     84     56       N  
ATOM   6760  CA  ILE C 879     -75.067  23.313 -27.924  1.00 26.42           C  
ANISOU 6760  CA  ILE C 879     3534   3263   3243    -30     83     50       C  
ATOM   6761  C   ILE C 879     -74.291  22.795 -29.148  1.00 29.55           C  
ANISOU 6761  C   ILE C 879     3937   3664   3628    -25     74     34       C  
ATOM   6762  O   ILE C 879     -74.822  22.082 -29.979  1.00 25.61           O  
ANISOU 6762  O   ILE C 879     3447   3161   3125    -51     75     22       O  
ATOM   6763  CB  ILE C 879     -75.181  22.256 -26.833  1.00 28.33           C  
ANISOU 6763  CB  ILE C 879     3818   3468   3478    -24     99     53       C  
ATOM   6764  CG1 ILE C 879     -75.821  22.868 -25.570  1.00 27.84           C  
ANISOU 6764  CG1 ILE C 879     3747   3407   3423    -21    108     70       C  
ATOM   6765  CG2 ILE C 879     -73.833  21.608 -26.475  1.00 29.79           C  
ANISOU 6765  CG2 ILE C 879     4036   3638   3645     19    100     48       C  
ATOM   6766  CD1 ILE C 879     -76.202  21.814 -24.537  1.00 27.54           C  
ANISOU 6766  CD1 ILE C 879     3751   3333   3378    -20    131     79       C  
ATOM   6767  N   ALA C 880     -73.000  23.085 -29.184  1.00 29.16           N  
ANISOU 6767  N   ALA C 880     3885   3624   3572      8     67     30       N  
ATOM   6768  CA  ALA C 880     -72.140  22.509 -30.178  1.00 28.63           C  
ANISOU 6768  CA  ALA C 880     3828   3559   3490     22     62     17       C  
ATOM   6769  C   ALA C 880     -72.362  20.990 -30.321  1.00 24.56           C  
ANISOU 6769  C   ALA C 880     3363   3007   2963     16     73      5       C  
ATOM   6770  O   ALA C 880     -72.460  20.256 -29.348  1.00 25.96           O  
ANISOU 6770  O   ALA C 880     3575   3151   3136     25     88     10       O  
ATOM   6771  CB  ALA C 880     -70.688  22.808 -29.838  1.00 29.04           C  
ANISOU 6771  CB  ALA C 880     3874   3627   3534     62     56     16       C  
ATOM   6772  N   PRO C 881     -72.405  20.505 -31.550  1.00 23.41           N  
ANISOU 6772  N   PRO C 881     3223   2864   2809      2     70    -11       N  
ATOM   6773  CA  PRO C 881     -72.655  19.068 -31.761  1.00 23.70           C  
ANISOU 6773  CA  PRO C 881     3312   2858   2834    -10     86    -29       C  
ATOM   6774  C   PRO C 881     -71.518  18.173 -31.294  1.00 24.87           C  
ANISOU 6774  C   PRO C 881     3509   2975   2966     40    100    -28       C  
ATOM   6775  O   PRO C 881     -70.398  18.641 -31.100  1.00 25.30           O  
ANISOU 6775  O   PRO C 881     3547   3055   3012     85     91    -20       O  
ATOM   6776  CB  PRO C 881     -72.845  18.957 -33.278  1.00 23.90           C  
ANISOU 6776  CB  PRO C 881     3326   2905   2850    -33     76    -50       C  
ATOM   6777  CG  PRO C 881     -72.235  20.176 -33.877  1.00 23.56           C  
ANISOU 6777  CG  PRO C 881     3233   2912   2807    -12     58    -39       C  
ATOM   6778  CD  PRO C 881     -72.198  21.246 -32.814  1.00 23.05           C  
ANISOU 6778  CD  PRO C 881     3140   2860   2760     -1     56    -15       C  
ATOM   6779  N   PRO C 882     -71.807  16.903 -31.035  1.00 26.36           N  
ANISOU 6779  N   PRO C 882     3759   3110   3149     34    124    -36       N  
ATOM   6780  CA  PRO C 882     -70.802  15.892 -30.623  1.00 28.37           C  
ANISOU 6780  CA  PRO C 882     4070   3328   3382     90    145    -32       C  
ATOM   6781  C   PRO C 882     -69.536  15.877 -31.524  1.00 31.32           C  
ANISOU 6781  C   PRO C 882     4438   3728   3734    136    134    -41       C  
ATOM   6782  O   PRO C 882     -68.427  15.721 -31.031  1.00 28.53           O  
ANISOU 6782  O   PRO C 882     4094   3385   3363    198    138    -28       O  
ATOM   6783  CB  PRO C 882     -71.550  14.562 -30.788  1.00 29.65           C  
ANISOU 6783  CB  PRO C 882     4300   3423   3543     56    176    -49       C  
ATOM   6784  CG  PRO C 882     -72.997  14.920 -30.710  1.00 29.97           C  
ANISOU 6784  CG  PRO C 882     4312   3467   3607    -17    173    -53       C  
ATOM   6785  CD  PRO C 882     -73.162  16.348 -31.165  1.00 28.24           C  
ANISOU 6785  CD  PRO C 882     4013   3319   3397    -29    138    -49       C  
ATOM   6786  N   GLU C 883     -69.733  16.088 -32.829  1.00 31.88           N  
ANISOU 6786  N   GLU C 883     4487   3820   3804    106    121    -61       N  
ATOM   6787  CA  GLU C 883     -68.660  16.071 -33.809  1.00 33.87           C  
ANISOU 6787  CA  GLU C 883     4732   4100   4036    144    114    -70       C  
ATOM   6788  C   GLU C 883     -67.694  17.249 -33.664  1.00 33.44           C  
ANISOU 6788  C   GLU C 883     4617   4106   3982    177     93    -52       C  
ATOM   6789  O   GLU C 883     -66.573  17.187 -34.151  1.00 33.87           O  
ANISOU 6789  O   GLU C 883     4665   4186   4017    221     92    -53       O  
ATOM   6790  CB  GLU C 883     -69.230  16.083 -35.242  1.00 37.06           C  
ANISOU 6790  CB  GLU C 883     5125   4517   4437    101    104    -96       C  
ATOM   6791  CG  GLU C 883     -70.129  14.898 -35.588  1.00 40.41           C  
ANISOU 6791  CG  GLU C 883     5608   4888   4858     58    123   -125       C  
ATOM   6792  CD  GLU C 883     -71.596  15.094 -35.213  1.00 42.62           C  
ANISOU 6792  CD  GLU C 883     5871   5161   5161    -11    122   -129       C  
ATOM   6793  OE1 GLU C 883     -72.328  14.088 -35.238  1.00 46.04           O  
ANISOU 6793  OE1 GLU C 883     6353   5546   5595    -52    143   -152       O  
ATOM   6794  OE2 GLU C 883     -72.037  16.229 -34.937  1.00 42.16           O  
ANISOU 6794  OE2 GLU C 883     5754   5147   5119    -26    103   -110       O  
ATOM   6795  N   ALA C 884     -68.140  18.336 -33.053  1.00 29.45           N  
ANISOU 6795  N   ALA C 884     4066   3624   3498    153     80    -38       N  
ATOM   6796  CA  ALA C 884     -67.290  19.511 -32.887  1.00 28.29           C  
ANISOU 6796  CA  ALA C 884     3864   3530   3356    173     65    -27       C  
ATOM   6797  C   ALA C 884     -66.207  19.270 -31.849  1.00 26.97           C  
ANISOU 6797  C   ALA C 884     3703   3373   3172    227     69    -18       C  
ATOM   6798  O   ALA C 884     -66.440  18.611 -30.856  1.00 25.21           O  
ANISOU 6798  O   ALA C 884     3516   3118   2943    242     81    -11       O  
ATOM   6799  CB  ALA C 884     -68.121  20.707 -32.470  1.00 28.31           C  
ANISOU 6799  CB  ALA C 884     3825   3546   3384    133     56    -17       C  
ATOM   6800  N   PRO C 885     -65.008  19.787 -32.089  1.00 26.99           N  
ANISOU 6800  N   PRO C 885     3667   3425   3163    257     60    -17       N  
ATOM   6801  CA  PRO C 885     -64.004  19.803 -31.018  1.00 27.34           C  
ANISOU 6801  CA  PRO C 885     3699   3499   3190    304     58    -10       C  
ATOM   6802  C   PRO C 885     -64.386  20.682 -29.817  1.00 27.89           C  
ANISOU 6802  C   PRO C 885     3742   3579   3275    282     50     -5       C  
ATOM   6803  O   PRO C 885     -65.157  21.639 -29.946  1.00 33.23           O  
ANISOU 6803  O   PRO C 885     4395   4253   3980    233     44     -6       O  
ATOM   6804  CB  PRO C 885     -62.778  20.419 -31.690  1.00 25.34           C  
ANISOU 6804  CB  PRO C 885     3395   3307   2927    322     50    -15       C  
ATOM   6805  CG  PRO C 885     -63.165  20.760 -33.065  1.00 26.06           C  
ANISOU 6805  CG  PRO C 885     3476   3394   3031    287     49    -20       C  
ATOM   6806  CD  PRO C 885     -64.609  20.560 -33.269  1.00 25.12           C  
ANISOU 6806  CD  PRO C 885     3389   3226   2931    243     52    -22       C  
ATOM   6807  N   VAL C 886     -63.767  20.430 -28.689  1.00 30.66           N  
ANISOU 6807  N   VAL C 886     4095   3949   3605    325     50      0       N  
ATOM   6808  CA  VAL C 886     -63.982  21.223 -27.455  1.00 32.21           C  
ANISOU 6808  CA  VAL C 886     4267   4162   3809    312     41      1       C  
ATOM   6809  C   VAL C 886     -63.163  22.533 -27.395  1.00 33.02           C  
ANISOU 6809  C   VAL C 886     4303   4326   3917    295     25    -14       C  
ATOM   6810  O   VAL C 886     -63.398  23.405 -26.528  1.00 32.21           O  
ANISOU 6810  O   VAL C 886     4177   4235   3825    271     18    -20       O  
ATOM   6811  CB  VAL C 886     -63.663  20.346 -26.243  1.00 34.83           C  
ANISOU 6811  CB  VAL C 886     4631   4495   4109    369     49     12       C  
ATOM   6812  CG1 VAL C 886     -62.164  20.098 -26.156  1.00 40.00           C  
ANISOU 6812  CG1 VAL C 886     5260   5212   4725    431     42      9       C  
ATOM   6813  CG2 VAL C 886     -64.151  20.962 -24.948  1.00 39.23           C  
ANISOU 6813  CG2 VAL C 886     5177   5057   4670    356     43     13       C  
ATOM   6814  N   THR C 887     -62.157  22.630 -28.255  1.00 32.34           N  
ANISOU 6814  N   THR C 887     4187   4279   3822    308     22    -20       N  
ATOM   6815  CA  THR C 887     -61.166  23.718 -28.202  1.00 33.39           C  
ANISOU 6815  CA  THR C 887     4256   4476   3956    293     11    -36       C  
ATOM   6816  C   THR C 887     -61.734  25.121 -28.025  1.00 30.05           C  
ANISOU 6816  C   THR C 887     3806   4044   3568    230     10    -45       C  
ATOM   6817  O   THR C 887     -62.611  25.552 -28.782  1.00 28.84           O  
ANISOU 6817  O   THR C 887     3663   3851   3443    193     18    -37       O  
ATOM   6818  CB  THR C 887     -60.350  23.750 -29.540  1.00 37.92           C  
ANISOU 6818  CB  THR C 887     4804   5077   4526    297     14    -38       C  
ATOM   6819  OG1 THR C 887     -60.028  22.428 -29.952  1.00 41.72           O  
ANISOU 6819  OG1 THR C 887     5322   5551   4978    354     21    -29       O  
ATOM   6820  CG2 THR C 887     -59.081  24.587 -29.442  1.00 39.76           C  
ANISOU 6820  CG2 THR C 887     4970   5385   4751    291      7    -54       C  
ATOM   6821  N   GLY C 888     -61.222  25.833 -27.033  1.00 28.84           N  
ANISOU 6821  N   GLY C 888     3619   3930   3410    222      1    -62       N  
ATOM   6822  CA  GLY C 888     -61.714  27.143 -26.757  1.00 27.43           C  
ANISOU 6822  CA  GLY C 888     3422   3737   3262    166      5    -73       C  
ATOM   6823  C   GLY C 888     -62.871  27.171 -25.772  1.00 27.26           C  
ANISOU 6823  C   GLY C 888     3435   3675   3249    160      6    -67       C  
ATOM   6824  O   GLY C 888     -63.092  28.206 -25.168  1.00 29.00           O  
ANISOU 6824  O   GLY C 888     3641   3894   3484    126      8    -82       O  
ATOM   6825  N   TYR C 889     -63.600  26.071 -25.596  1.00 25.21           N  
ANISOU 6825  N   TYR C 889     3221   3380   2979    189      9    -48       N  
ATOM   6826  CA  TYR C 889     -64.626  26.019 -24.560  1.00 26.46           C  
ANISOU 6826  CA  TYR C 889     3408   3505   3140    187     12    -40       C  
ATOM   6827  C   TYR C 889     -64.005  25.852 -23.175  1.00 27.35           C  
ANISOU 6827  C   TYR C 889     3513   3659   3219    222      2    -52       C  
ATOM   6828  O   TYR C 889     -63.728  24.746 -22.728  1.00 31.84           O  
ANISOU 6828  O   TYR C 889     4106   4236   3757    274      2    -40       O  
ATOM   6829  CB  TYR C 889     -65.611  24.892 -24.813  1.00 24.74           C  
ANISOU 6829  CB  TYR C 889     3241   3237   2924    199     23    -17       C  
ATOM   6830  CG  TYR C 889     -66.608  25.182 -25.891  1.00 24.48           C  
ANISOU 6830  CG  TYR C 889     3214   3167   2922    159     31     -7       C  
ATOM   6831  CD1 TYR C 889     -66.423  24.731 -27.192  1.00 23.52           C  
ANISOU 6831  CD1 TYR C 889     3095   3040   2801    158     32     -5       C  
ATOM   6832  CD2 TYR C 889     -67.781  25.895 -25.596  1.00 23.15           C  
ANISOU 6832  CD2 TYR C 889     3047   2972   2776    125     38      0       C  
ATOM   6833  CE1 TYR C 889     -67.374  24.995 -28.170  1.00 24.27           C  
ANISOU 6833  CE1 TYR C 889     3192   3111   2917    124     38      3       C  
ATOM   6834  CE2 TYR C 889     -68.737  26.137 -26.563  1.00 25.26           C  
ANISOU 6834  CE2 TYR C 889     3315   3216   3065     95     44     10       C  
ATOM   6835  CZ  TYR C 889     -68.526  25.714 -27.844  1.00 24.58           C  
ANISOU 6835  CZ  TYR C 889     3229   3132   2978     94     43     11       C  
ATOM   6836  OH  TYR C 889     -69.503  25.968 -28.778  1.00 28.35           O  
ANISOU 6836  OH  TYR C 889     3703   3597   3471     67     48     21       O  
ATOM   6837  N   MET C 890     -63.967  26.936 -22.450  1.00 26.46           N  
ANISOU 6837  N   MET C 890     3375   3566   3114    194     -3    -73       N  
ATOM   6838  CA  MET C 890     -63.490  26.959 -21.091  1.00 28.34           C  
ANISOU 6838  CA  MET C 890     3601   3848   3318    220    -14    -89       C  
ATOM   6839  C   MET C 890     -64.183  25.996 -20.101  1.00 25.91           C  
ANISOU 6839  C   MET C 890     3339   3519   2988    265     -9    -66       C  
ATOM   6840  O   MET C 890     -63.511  25.406 -19.243  1.00 25.85           O  
ANISOU 6840  O   MET C 890     3329   3556   2936    317    -17    -67       O  
ATOM   6841  CB  MET C 890     -63.593  28.380 -20.572  1.00 30.76           C  
ANISOU 6841  CB  MET C 890     3882   4162   3642    171    -15   -119       C  
ATOM   6842  CG  MET C 890     -62.929  28.553 -19.228  1.00 39.31           C  
ANISOU 6842  CG  MET C 890     4942   5306   4686    191    -31   -147       C  
ATOM   6843  SD  MET C 890     -62.642  30.295 -18.859  1.00 47.62           S  
ANISOU 6843  SD  MET C 890     5958   6377   5758    122    -31   -197       S  
ATOM   6844  CE  MET C 890     -61.830  30.131 -17.333  1.00 48.39           C  
ANISOU 6844  CE  MET C 890     6028   6560   5796    158    -55   -230       C  
ATOM   6845  N   PHE C 891     -65.491  25.831 -20.224  1.00 21.97           N  
ANISOU 6845  N   PHE C 891     2879   2956   2514    246      8    -43       N  
ATOM   6846  CA  PHE C 891     -66.235  24.938 -19.330  1.00 22.37           C  
ANISOU 6846  CA  PHE C 891     2974   2979   2547    280     20    -19       C  
ATOM   6847  C   PHE C 891     -66.998  23.858 -20.099  1.00 21.80           C  
ANISOU 6847  C   PHE C 891     2947   2848   2490    281     38     10       C  
ATOM   6848  O   PHE C 891     -68.064  23.387 -19.697  1.00 21.76           O  
ANISOU 6848  O   PHE C 891     2978   2800   2491    277     56     30       O  
ATOM   6849  CB  PHE C 891     -67.189  25.770 -18.461  1.00 22.73           C  
ANISOU 6849  CB  PHE C 891     3023   3008   2606    253     25    -22       C  
ATOM   6850  CG  PHE C 891     -66.479  26.785 -17.604  1.00 23.07           C  
ANISOU 6850  CG  PHE C 891     3029   3106   2632    249      9    -57       C  
ATOM   6851  CD1 PHE C 891     -65.689  26.371 -16.551  1.00 24.55           C  
ANISOU 6851  CD1 PHE C 891     3210   3348   2771    299     -3    -66       C  
ATOM   6852  CD2 PHE C 891     -66.541  28.144 -17.901  1.00 22.64           C  
ANISOU 6852  CD2 PHE C 891     2947   3048   2607    196      8    -83       C  
ATOM   6853  CE1 PHE C 891     -65.014  27.296 -15.785  1.00 24.15           C  
ANISOU 6853  CE1 PHE C 891     3121   3355   2700    289    -19   -105       C  
ATOM   6854  CE2 PHE C 891     -65.887  29.078 -17.129  1.00 22.16           C  
ANISOU 6854  CE2 PHE C 891     2857   3033   2531    184     -3   -122       C  
ATOM   6855  CZ  PHE C 891     -65.133  28.652 -16.058  1.00 23.85           C  
ANISOU 6855  CZ  PHE C 891     3059   3307   2695    227    -19   -136       C  
ATOM   6856  N   GLY C 892     -66.443  23.448 -21.225  1.00 23.20           N  
ANISOU 6856  N   GLY C 892     3119   3025   2669    284     36      9       N  
ATOM   6857  CA  GLY C 892     -67.094  22.451 -22.067  1.00 21.83           C  
ANISOU 6857  CA  GLY C 892     2988   2798   2508    278     53     27       C  
ATOM   6858  C   GLY C 892     -68.149  23.011 -23.016  1.00 22.54           C  
ANISOU 6858  C   GLY C 892     3070   2855   2638    218     56     27       C  
ATOM   6859  O   GLY C 892     -68.517  24.190 -22.981  1.00 22.07           O  
ANISOU 6859  O   GLY C 892     2980   2805   2599    184     50     19       O  
ATOM   6860  N   LYS C 893     -68.662  22.117 -23.838  1.00 24.14           N  
ANISOU 6860  N   LYS C 893     3305   3020   2848    208     68     36       N  
ATOM   6861  CA  LYS C 893     -69.719  22.407 -24.770  1.00 23.95           C  
ANISOU 6861  CA  LYS C 893     3276   2972   2854    158     71     37       C  
ATOM   6862  C   LYS C 893     -71.002  22.646 -24.002  1.00 22.21           C  
ANISOU 6862  C   LYS C 893     3063   2730   2647    132     82     49       C  
ATOM   6863  O   LYS C 893     -71.508  21.756 -23.365  1.00 26.39           O  
ANISOU 6863  O   LYS C 893     3630   3230   3169    140     99     61       O  
ATOM   6864  CB  LYS C 893     -69.934  21.236 -25.701  1.00 23.41           C  
ANISOU 6864  CB  LYS C 893     3244   2871   2782    153     82     37       C  
ATOM   6865  CG  LYS C 893     -68.804  20.968 -26.686  1.00 25.68           C  
ANISOU 6865  CG  LYS C 893     3525   3177   3055    177     74     26       C  
ATOM   6866  CD  LYS C 893     -69.118  19.678 -27.456  1.00 25.48           C  
ANISOU 6866  CD  LYS C 893     3548   3109   3024    174     90     23       C  
ATOM   6867  CE  LYS C 893     -67.990  19.246 -28.317  1.00 26.40           C  
ANISOU 6867  CE  LYS C 893     3668   3241   3121    208     86     13       C  
ATOM   6868  NZ  LYS C 893     -68.462  18.268 -29.345  1.00 27.81           N  
ANISOU 6868  NZ  LYS C 893     3887   3380   3299    190     99      2       N  
ATOM   6869  N   GLY C 894     -71.545  23.845 -24.087  1.00 21.38           N  
ANISOU 6869  N   GLY C 894     2923   2638   2562    103     76     47       N  
ATOM   6870  CA  GLY C 894     -72.793  24.187 -23.390  1.00 20.61           C  
ANISOU 6870  CA  GLY C 894     2827   2528   2477     82     88     60       C  
ATOM   6871  C   GLY C 894     -73.306  25.489 -23.958  1.00 20.14           C  
ANISOU 6871  C   GLY C 894     2731   2483   2439     55     84     59       C  
ATOM   6872  O   GLY C 894     -72.772  25.972 -24.948  1.00 20.86           O  
ANISOU 6872  O   GLY C 894     2801   2589   2536     49     75     51       O  
ATOM   6873  N   ILE C 895     -74.361  26.046 -23.369  1.00 19.75           N  
ANISOU 6873  N   ILE C 895     2675   2430   2399     42     94     71       N  
ATOM   6874  CA  ILE C 895     -74.834  27.364 -23.766  1.00 18.65           C  
ANISOU 6874  CA  ILE C 895     2506   2302   2277     28     95     75       C  
ATOM   6875  C   ILE C 895     -74.317  28.331 -22.705  1.00 18.32           C  
ANISOU 6875  C   ILE C 895     2461   2266   2232     43     97     65       C  
ATOM   6876  O   ILE C 895     -74.563  28.129 -21.518  1.00 17.27           O  
ANISOU 6876  O   ILE C 895     2343   2129   2089     57    102     67       O  
ATOM   6877  CB  ILE C 895     -76.341  27.420 -23.839  1.00 20.13           C  
ANISOU 6877  CB  ILE C 895     2686   2489   2474      9    108     94       C  
ATOM   6878  CG1 ILE C 895     -76.886  26.305 -24.724  1.00 22.09           C  
ANISOU 6878  CG1 ILE C 895     2938   2734   2721    -15    106     96       C  
ATOM   6879  CG2 ILE C 895     -76.798  28.754 -24.418  1.00 19.50           C  
ANISOU 6879  CG2 ILE C 895     2577   2423   2407      4    112    102       C  
ATOM   6880  CD1 ILE C 895     -78.371  26.083 -24.570  1.00 22.77           C  
ANISOU 6880  CD1 ILE C 895     3014   2825   2811    -38    119    111       C  
ATOM   6881  N   TYR C 896     -73.639  29.370 -23.164  1.00 17.23           N  
ANISOU 6881  N   TYR C 896     2304   2138   2104     39     94     53       N  
ATOM   6882  CA  TYR C 896     -72.948  30.334 -22.336  1.00 17.43           C  
ANISOU 6882  CA  TYR C 896     2326   2170   2128     43     95     33       C  
ATOM   6883  C   TYR C 896     -73.738  31.655 -22.276  1.00 17.32           C  
ANISOU 6883  C   TYR C 896     2307   2142   2132     33    114     40       C  
ATOM   6884  O   TYR C 896     -74.259  32.131 -23.298  1.00 16.64           O  
ANISOU 6884  O   TYR C 896     2211   2051   2060     24    123     57       O  
ATOM   6885  CB  TYR C 896     -71.548  30.601 -22.911  1.00 17.73           C  
ANISOU 6885  CB  TYR C 896     2347   2226   2164     39     84     11       C  
ATOM   6886  CG  TYR C 896     -70.543  29.483 -22.663  1.00 17.45           C  
ANISOU 6886  CG  TYR C 896     2315   2212   2104     61     67      0       C  
ATOM   6887  CD1 TYR C 896     -70.690  28.271 -23.272  1.00 17.46           C  
ANISOU 6887  CD1 TYR C 896     2330   2206   2099     71     63     14       C  
ATOM   6888  CD2 TYR C 896     -69.432  29.671 -21.851  1.00 17.88           C  
ANISOU 6888  CD2 TYR C 896     2359   2297   2140     73     56    -26       C  
ATOM   6889  CE1 TYR C 896     -69.792  27.241 -23.027  1.00 18.25           C  
ANISOU 6889  CE1 TYR C 896     2439   2321   2173    101     53      8       C  
ATOM   6890  CE2 TYR C 896     -68.497  28.648 -21.644  1.00 18.86           C  
ANISOU 6890  CE2 TYR C 896     2483   2448   2236    104     42    -32       C  
ATOM   6891  CZ  TYR C 896     -68.699  27.439 -22.242  1.00 18.14           C  
ANISOU 6891  CZ  TYR C 896     2413   2342   2139    121     42    -12       C  
ATOM   6892  OH  TYR C 896     -67.799  26.417 -22.075  1.00 21.03           O  
ANISOU 6892  OH  TYR C 896     2786   2730   2475    160     34    -14       O  
ATOM   6893  N   PHE C 897     -73.821  32.226 -21.070  1.00 17.18           N  
ANISOU 6893  N   PHE C 897     2299   2120   2107     40    121     28       N  
ATOM   6894  CA  PHE C 897     -74.518  33.478 -20.799  1.00 17.30           C  
ANISOU 6894  CA  PHE C 897     2320   2118   2136     37    144     32       C  
ATOM   6895  C   PHE C 897     -73.672  34.349 -19.898  1.00 18.11           C  
ANISOU 6895  C   PHE C 897     2428   2219   2233     32    147     -4       C  
ATOM   6896  O   PHE C 897     -72.890  33.848 -19.128  1.00 18.22           O  
ANISOU 6896  O   PHE C 897     2441   2255   2226     38    129    -28       O  
ATOM   6897  CB  PHE C 897     -75.849  33.234 -20.070  1.00 17.44           C  
ANISOU 6897  CB  PHE C 897     2348   2132   2148     53    155     55       C  
ATOM   6898  CG  PHE C 897     -76.818  32.402 -20.816  1.00 17.09           C  
ANISOU 6898  CG  PHE C 897     2294   2094   2107     50    155     86       C  
ATOM   6899  CD1 PHE C 897     -76.776  31.009 -20.727  1.00 17.25           C  
ANISOU 6899  CD1 PHE C 897     2319   2120   2115     49    142     89       C  
ATOM   6900  CD2 PHE C 897     -77.810  32.982 -21.556  1.00 17.40           C  
ANISOU 6900  CD2 PHE C 897     2320   2134   2159     50    170    110       C  
ATOM   6901  CE1 PHE C 897     -77.666  30.235 -21.427  1.00 16.05           C  
ANISOU 6901  CE1 PHE C 897     2158   1972   1966     37    143    110       C  
ATOM   6902  CE2 PHE C 897     -78.739  32.193 -22.232  1.00 17.40           C  
ANISOU 6902  CE2 PHE C 897     2304   2150   2157     43    167    133       C  
ATOM   6903  CZ  PHE C 897     -78.651  30.819 -22.169  1.00 16.07           C  
ANISOU 6903  CZ  PHE C 897     2140   1985   1980     31    153    130       C  
ATOM   6904  N   ALA C 898     -73.911  35.660 -19.961  1.00 19.91           N  
ANISOU 6904  N   ALA C 898     2665   2423   2478     22    171     -9       N  
ATOM   6905  CA  ALA C 898     -73.283  36.639 -19.091  1.00 20.46           C  
ANISOU 6905  CA  ALA C 898     2745   2484   2544      9    181    -49       C  
ATOM   6906  C   ALA C 898     -74.333  37.384 -18.251  1.00 21.99           C  
ANISOU 6906  C   ALA C 898     2965   2653   2737     25    206    -42       C  
ATOM   6907  O   ALA C 898     -75.482  37.503 -18.659  1.00 21.39           O  
ANISOU 6907  O   ALA C 898     2893   2563   2670     43    224     -4       O  
ATOM   6908  CB  ALA C 898     -72.559  37.648 -19.943  1.00 21.70           C  
ANISOU 6908  CB  ALA C 898     2899   2622   2724    -21    197    -63       C  
ATOM   6909  N   ASP C 899     -73.895  37.947 -17.119  1.00 22.51           N  
ANISOU 6909  N   ASP C 899     3045   2719   2790     19    209    -82       N  
ATOM   6910  CA  ASP C 899     -74.688  38.935 -16.416  1.00 22.58           C  
ANISOU 6910  CA  ASP C 899     3084   2697   2800     31    240    -85       C  
ATOM   6911  C   ASP C 899     -74.230  40.380 -16.696  1.00 23.80           C  
ANISOU 6911  C   ASP C 899     3258   2809   2975      2    272   -114       C  
ATOM   6912  O   ASP C 899     -74.858  41.314 -16.202  1.00 22.45           O  
ANISOU 6912  O   ASP C 899     3120   2602   2807     12    305   -117       O  
ATOM   6913  CB  ASP C 899     -74.757  38.654 -14.900  1.00 22.71           C  
ANISOU 6913  CB  ASP C 899     3110   2736   2783     48    230   -109       C  
ATOM   6914  CG  ASP C 899     -73.413  38.568 -14.231  1.00 21.65           C  
ANISOU 6914  CG  ASP C 899     2964   2634   2627     27    205   -164       C  
ATOM   6915  OD1 ASP C 899     -72.408  39.098 -14.738  1.00 22.94           O  
ANISOU 6915  OD1 ASP C 899     3116   2796   2803    -11    203   -196       O  
ATOM   6916  OD2 ASP C 899     -73.351  37.918 -13.177  1.00 22.60           O  
ANISOU 6916  OD2 ASP C 899     3083   2791   2714     49    186   -174       O  
ATOM   6917  N   MET C 900     -73.167  40.542 -17.482  1.00 24.19           N  
ANISOU 6917  N   MET C 900     3292   2860   3039    -34    267   -132       N  
ATOM   6918  CA  MET C 900     -72.693  41.867 -17.916  1.00 24.86           C  
ANISOU 6918  CA  MET C 900     3398   2898   3149    -68    303   -155       C  
ATOM   6919  C   MET C 900     -73.002  42.025 -19.409  1.00 24.13           C  
ANISOU 6919  C   MET C 900     3302   2784   3082    -62    322   -106       C  
ATOM   6920  O   MET C 900     -72.510  41.247 -20.231  1.00 23.46           O  
ANISOU 6920  O   MET C 900     3185   2730   2999    -68    297    -93       O  
ATOM   6921  CB  MET C 900     -71.206  42.031 -17.705  1.00 26.13           C  
ANISOU 6921  CB  MET C 900     3540   3082   3307   -119    288   -213       C  
ATOM   6922  CG  MET C 900     -70.703  41.851 -16.292  1.00 28.14           C  
ANISOU 6922  CG  MET C 900     3789   3374   3529   -127    264   -267       C  
ATOM   6923  SD  MET C 900     -71.120  43.265 -15.235  1.00 32.46           S  
ANISOU 6923  SD  MET C 900     4388   3868   4076   -140    306   -309       S  
ATOM   6924  CE  MET C 900     -69.881  44.446 -15.712  1.00 31.75           C  
ANISOU 6924  CE  MET C 900     4303   3747   4013   -218    334   -365       C  
ATOM   6925  N   VAL C 901     -73.854  42.992 -19.750  1.00 23.33           N  
ANISOU 6925  N   VAL C 901     3234   2633   2996    -43    367    -78       N  
ATOM   6926  CA  VAL C 901     -74.343  43.144 -21.117  1.00 24.71           C  
ANISOU 6926  CA  VAL C 901     3406   2794   3187    -22    387    -25       C  
ATOM   6927  C   VAL C 901     -73.204  43.198 -22.145  1.00 24.07           C  
ANISOU 6927  C   VAL C 901     3307   2715   3122    -60    386    -34       C  
ATOM   6928  O   VAL C 901     -73.296  42.584 -23.207  1.00 23.80           O  
ANISOU 6928  O   VAL C 901     3248   2707   3089    -46    371      2       O  
ATOM   6929  CB  VAL C 901     -75.287  44.358 -21.289  1.00 25.77           C  
ANISOU 6929  CB  VAL C 901     3584   2873   3332      9    444      6       C  
ATOM   6930  CG1 VAL C 901     -74.557  45.681 -21.076  1.00 27.04           C  
ANISOU 6930  CG1 VAL C 901     3790   2971   3514    -28    490    -33       C  
ATOM   6931  CG2 VAL C 901     -75.931  44.350 -22.664  1.00 25.35           C  
ANISOU 6931  CG2 VAL C 901     3521   2826   3286     44    457     67       C  
ATOM   6932  N   SER C 902     -72.123  43.873 -21.815  1.00 25.33           N  
ANISOU 6932  N   SER C 902     3478   2855   3294   -109    399    -84       N  
ATOM   6933  CA  SER C 902     -71.018  44.045 -22.766  1.00 25.58           C  
ANISOU 6933  CA  SER C 902     3491   2886   3341   -149    405    -93       C  
ATOM   6934  C   SER C 902     -70.278  42.734 -23.048  1.00 24.95           C  
ANISOU 6934  C   SER C 902     3358   2874   3245   -155    351    -99       C  
ATOM   6935  O   SER C 902     -69.836  42.511 -24.163  1.00 26.10           O  
ANISOU 6935  O   SER C 902     3484   3032   3399   -160    350    -78       O  
ATOM   6936  CB  SER C 902     -70.079  45.129 -22.276  1.00 28.16           C  
ANISOU 6936  CB  SER C 902     3840   3176   3684   -208    437   -149       C  
ATOM   6937  OG  SER C 902     -69.503  44.815 -21.016  1.00 31.43           O  
ANISOU 6937  OG  SER C 902     4238   3626   4077   -234    404   -209       O  
ATOM   6938  N   LYS C 903     -70.164  41.847 -22.049  1.00 24.62           N  
ANISOU 6938  N   LYS C 903     3298   2877   3179   -148    309   -124       N  
ATOM   6939  CA  LYS C 903     -69.511  40.570 -22.252  1.00 22.53           C  
ANISOU 6939  CA  LYS C 903     2992   2673   2897   -144    263   -127       C  
ATOM   6940  C   LYS C 903     -70.224  39.800 -23.362  1.00 21.63           C  
ANISOU 6940  C   LYS C 903     2869   2568   2784   -108    254    -71       C  
ATOM   6941  O   LYS C 903     -69.577  39.204 -24.211  1.00 20.36           O  
ANISOU 6941  O   LYS C 903     2681   2433   2620   -113    238    -65       O  
ATOM   6942  CB  LYS C 903     -69.453  39.740 -20.976  1.00 23.02           C  
ANISOU 6942  CB  LYS C 903     3043   2775   2927   -129    226   -152       C  
ATOM   6943  CG  LYS C 903     -68.715  38.398 -21.139  1.00 22.42           C  
ANISOU 6943  CG  LYS C 903     2930   2758   2829   -117    183   -153       C  
ATOM   6944  CD  LYS C 903     -68.247  37.829 -19.811  1.00 22.54           C  
ANISOU 6944  CD  LYS C 903     2935   2818   2811   -108    153   -189       C  
ATOM   6945  CE  LYS C 903     -67.418  36.557 -19.973  1.00 22.50           C  
ANISOU 6945  CE  LYS C 903     2897   2870   2781    -89    117   -188       C  
ATOM   6946  NZ  LYS C 903     -67.104  35.891 -18.674  1.00 23.11           N  
ANISOU 6946  NZ  LYS C 903     2968   2994   2820    -64     90   -212       N  
ATOM   6947  N   SER C 904     -71.555  39.828 -23.329  1.00 21.71           N  
ANISOU 6947  N   SER C 904     2898   2558   2792    -74    265    -35       N  
ATOM   6948  CA  SER C 904     -72.362  39.177 -24.350  1.00 21.20           C  
ANISOU 6948  CA  SER C 904     2822   2507   2726    -44    258     13       C  
ATOM   6949  C   SER C 904     -72.424  39.977 -25.635  1.00 22.39           C  
ANISOU 6949  C   SER C 904     2978   2634   2894    -43    291     43       C  
ATOM   6950  O   SER C 904     -72.305  39.406 -26.702  1.00 24.07           O  
ANISOU 6950  O   SER C 904     3171   2871   3103    -36    278     64       O  
ATOM   6951  CB  SER C 904     -73.771  38.897 -23.836  1.00 21.02           C  
ANISOU 6951  CB  SER C 904     2809   2484   2693    -10    258     40       C  
ATOM   6952  OG  SER C 904     -73.783  37.764 -22.969  1.00 19.94           O  
ANISOU 6952  OG  SER C 904     2663   2377   2537     -5    224     26       O  
ATOM   6953  N   ALA C 905     -72.548  41.302 -25.534  1.00 22.97           N  
ANISOU 6953  N   ALA C 905     3084   2660   2985    -48    336     43       N  
ATOM   6954  CA  ALA C 905     -72.561  42.159 -26.700  1.00 24.62           C  
ANISOU 6954  CA  ALA C 905     3305   2840   3208    -42    375     75       C  
ATOM   6955  C   ALA C 905     -71.295  42.032 -27.567  1.00 24.78           C  
ANISOU 6955  C   ALA C 905     3303   2874   3236    -75    371     63       C  
ATOM   6956  O   ALA C 905     -71.370  42.199 -28.784  1.00 24.82           O  
ANISOU 6956  O   ALA C 905     3305   2880   3244    -60    388     99       O  
ATOM   6957  CB  ALA C 905     -72.756  43.621 -26.296  1.00 24.76           C  
ANISOU 6957  CB  ALA C 905     3370   2793   3244    -46    431     72       C  
ATOM   6958  N   ASN C 906     -70.155  41.712 -26.959  1.00 23.99           N  
ANISOU 6958  N   ASN C 906     3185   2793   3136   -116    349     14       N  
ATOM   6959  CA  ASN C 906     -68.949  41.476 -27.732  1.00 23.94           C  
ANISOU 6959  CA  ASN C 906     3151   2811   3133   -144    342      2       C  
ATOM   6960  C   ASN C 906     -69.114  40.374 -28.746  1.00 24.31           C  
ANISOU 6960  C   ASN C 906     3172   2902   3165   -113    312     34       C  
ATOM   6961  O   ASN C 906     -68.491  40.404 -29.810  1.00 25.66           O  
ANISOU 6961  O   ASN C 906     3328   3083   3339   -120    321     47       O  
ATOM   6962  CB  ASN C 906     -67.762  41.176 -26.844  1.00 23.46           C  
ANISOU 6962  CB  ASN C 906     3067   2782   3067   -184    316    -55       C  
ATOM   6963  CG  ASN C 906     -67.273  42.390 -26.100  1.00 24.95           C  
ANISOU 6963  CG  ASN C 906     3276   2932   3273   -231    350    -97       C  
ATOM   6964  OD1 ASN C 906     -67.577  43.544 -26.466  1.00 26.17           O  
ANISOU 6964  OD1 ASN C 906     3467   3027   3450   -241    403    -82       O  
ATOM   6965  ND2 ASN C 906     -66.534  42.153 -25.035  1.00 24.65           N  
ANISOU 6965  ND2 ASN C 906     3218   2927   3222   -259    324   -151       N  
ATOM   6966  N   TYR C 907     -69.961  39.401 -28.441  1.00 25.17           N  
ANISOU 6966  N   TYR C 907     3275   3034   3255    -82    279     46       N  
ATOM   6967  CA  TYR C 907     -70.170  38.253 -29.345  1.00 23.82           C  
ANISOU 6967  CA  TYR C 907     3082   2902   3066    -58    250     69       C  
ATOM   6968  C   TYR C 907     -71.151  38.562 -30.469  1.00 23.95           C  
ANISOU 6968  C   TYR C 907     3104   2914   3081    -28    269    117       C  
ATOM   6969  O   TYR C 907     -71.435  37.702 -31.296  1.00 22.52           O  
ANISOU 6969  O   TYR C 907     2907   2767   2884    -10    247    134       O  
ATOM   6970  CB  TYR C 907     -70.605  37.021 -28.549  1.00 23.33           C  
ANISOU 6970  CB  TYR C 907     3015   2865   2985    -44    210     58       C  
ATOM   6971  CG  TYR C 907     -69.478  36.478 -27.691  1.00 22.50           C  
ANISOU 6971  CG  TYR C 907     2897   2781   2871    -62    186     17       C  
ATOM   6972  CD1 TYR C 907     -68.429  35.768 -28.273  1.00 22.57           C  
ANISOU 6972  CD1 TYR C 907     2883   2824   2870    -65    168      6       C  
ATOM   6973  CD2 TYR C 907     -69.448  36.700 -26.337  1.00 22.95           C  
ANISOU 6973  CD2 TYR C 907     2964   2832   2926    -70    183    -11       C  
ATOM   6974  CE1 TYR C 907     -67.375  35.307 -27.528  1.00 22.73           C  
ANISOU 6974  CE1 TYR C 907     2886   2873   2877    -74    147    -28       C  
ATOM   6975  CE2 TYR C 907     -68.404  36.237 -25.578  1.00 23.63           C  
ANISOU 6975  CE2 TYR C 907     3033   2947   2996    -80    160    -47       C  
ATOM   6976  CZ  TYR C 907     -67.376  35.540 -26.184  1.00 23.88           C  
ANISOU 6976  CZ  TYR C 907     3040   3017   3018    -80    142    -55       C  
ATOM   6977  OH  TYR C 907     -66.334  35.091 -25.451  1.00 25.23           O  
ANISOU 6977  OH  TYR C 907     3189   3227   3169    -83    121    -88       O  
ATOM   6978  N   CYS C 908     -71.659  39.785 -30.521  1.00 24.99           N  
ANISOU 6978  N   CYS C 908     3262   3008   3227    -20    312    138       N  
ATOM   6979  CA  CYS C 908     -72.436  40.211 -31.673  1.00 27.14           C  
ANISOU 6979  CA  CYS C 908     3537   3282   3493     16    335    187       C  
ATOM   6980  C   CYS C 908     -71.534  40.439 -32.886  1.00 28.93           C  
ANISOU 6980  C   CYS C 908     3755   3514   3723      8    352    198       C  
ATOM   6981  O   CYS C 908     -71.994  40.329 -34.017  1.00 33.47           O  
ANISOU 6981  O   CYS C 908     4322   4114   4282     40    355    235       O  
ATOM   6982  CB  CYS C 908     -73.218  41.485 -31.357  1.00 27.85           C  
ANISOU 6982  CB  CYS C 908     3662   3327   3595     37    383    211       C  
ATOM   6983  SG  CYS C 908     -74.485  41.307 -30.087  1.00 31.58           S  
ANISOU 6983  SG  CYS C 908     4143   3799   4059     58    371    209       S  
ATOM   6984  N   HIS C 909     -70.263  40.746 -32.631  1.00 31.36           N  
ANISOU 6984  N   HIS C 909     4062   3805   4047    -34    361    166       N  
ATOM   6985  CA  HIS C 909     -69.257  41.037 -33.660  1.00 33.71           C  
ANISOU 6985  CA  HIS C 909     4351   4107   4351    -49    382    173       C  
ATOM   6986  C   HIS C 909     -69.740  42.178 -34.556  1.00 33.70           C  
ANISOU 6986  C   HIS C 909     4377   4070   4356    -23    438    222       C  
ATOM   6987  O   HIS C 909     -69.682  42.088 -35.752  1.00 31.36           O  
ANISOU 6987  O   HIS C 909     4072   3798   4048      0    446    254       O  
ATOM   6988  CB  HIS C 909     -68.863  39.775 -34.451  1.00 31.96           C  
ANISOU 6988  CB  HIS C 909     4094   3942   4106    -38    341    172       C  
ATOM   6989  CG  HIS C 909     -68.133  38.768 -33.623  1.00 35.70           C  
ANISOU 6989  CG  HIS C 909     4547   4444   4574    -61    297    127       C  
ATOM   6990  ND1 HIS C 909     -66.840  38.961 -33.198  1.00 37.77           N  
ANISOU 6990  ND1 HIS C 909     4796   4710   4847   -100    301     91       N  
ATOM   6991  CD2 HIS C 909     -68.528  37.573 -33.100  1.00 35.56           C  
ANISOU 6991  CD2 HIS C 909     4520   4453   4538    -47    253    113       C  
ATOM   6992  CE1 HIS C 909     -66.452  37.920 -32.477  1.00 39.12           C  
ANISOU 6992  CE1 HIS C 909     4948   4913   5003   -102    258     59       C  
ATOM   6993  NE2 HIS C 909     -67.462  37.068 -32.395  1.00 37.27           N  
ANISOU 6993  NE2 HIS C 909     4721   4688   4752    -70    232     73       N  
ATOM   6994  N   THR C 910     -70.236  43.247 -33.938  1.00 34.36           N  
ANISOU 6994  N   THR C 910     4499   4099   4456    -21    479    228       N  
ATOM   6995  CA  THR C 910     -70.625  44.412 -34.672  1.00 32.70           C  
ANISOU 6995  CA  THR C 910     4324   3847   4253      7    541    275       C  
ATOM   6996  C   THR C 910     -69.392  45.221 -34.968  1.00 35.73           C  
ANISOU 6996  C   THR C 910     4722   4190   4662    -41    587    263       C  
ATOM   6997  O   THR C 910     -68.327  44.947 -34.435  1.00 34.85           O  
ANISOU 6997  O   THR C 910     4591   4087   4565    -98    569    212       O  
ATOM   6998  CB  THR C 910     -71.647  45.272 -33.916  1.00 31.30           C  
ANISOU 6998  CB  THR C 910     4190   3621   4083     33    574    290       C  
ATOM   6999  OG1 THR C 910     -71.170  45.546 -32.603  1.00 32.30           O  
ANISOU 6999  OG1 THR C 910     4331   3710   4230    -17    575    235       O  
ATOM   7000  CG2 THR C 910     -72.962  44.571 -33.867  1.00 29.97           C  
ANISOU 7000  CG2 THR C 910     4002   3500   3886     86    538    314       C  
ATOM   7001  N   SER C 911     -69.542  46.207 -35.848  1.00 40.52           N  
ANISOU 7001  N   SER C 911     5362   4759   5275    -16    649    311       N  
ATOM   7002  CA  SER C 911     -68.417  47.039 -36.276  1.00 44.50           C  
ANISOU 7002  CA  SER C 911     5883   5219   5805    -63    704    306       C  
ATOM   7003  C   SER C 911     -68.957  48.396 -36.733  1.00 46.57           C  
ANISOU 7003  C   SER C 911     6209   5409   6079    -29    787    359       C  
ATOM   7004  O   SER C 911     -70.161  48.625 -36.740  1.00 42.27           O  
ANISOU 7004  O   SER C 911     5686   4857   5516     36    797    399       O  
ATOM   7005  CB  SER C 911     -67.671  46.356 -37.407  1.00 41.90           C  
ANISOU 7005  CB  SER C 911     5512   4946   5460    -62    685    319       C  
ATOM   7006  OG  SER C 911     -68.571  46.084 -38.476  1.00 46.25           O  
ANISOU 7006  OG  SER C 911     6060   5534   5979     12    680    378       O  
ATOM   7007  N   GLN C 912     -68.057  49.312 -37.069  1.00 52.72           N  
ANISOU 7007  N   GLN C 912     7015   6131   6884    -73    852    359       N  
ATOM   7008  CA  GLN C 912     -68.462  50.666 -37.475  1.00 52.60           C  
ANISOU 7008  CA  GLN C 912     7071   6032   6883    -43    943    409       C  
ATOM   7009  C   GLN C 912     -69.296  50.616 -38.753  1.00 50.08           C  
ANISOU 7009  C   GLN C 912     6754   5747   6527     51    956    491       C  
ATOM   7010  O   GLN C 912     -70.253  51.352 -38.891  1.00 49.98           O  
ANISOU 7010  O   GLN C 912     6788   5696   6505    116   1002    542       O  
ATOM   7011  CB  GLN C 912     -67.254  51.564 -37.623  1.00 53.99           C  
ANISOU 7011  CB  GLN C 912     7275   6143   7097   -119   1011    390       C  
ATOM   7012  CG  GLN C 912     -66.799  52.182 -36.307  1.00 60.46           C  
ANISOU 7012  CG  GLN C 912     8122   6897   7951   -199   1031    320       C  
ATOM   7013  CD  GLN C 912     -65.386  52.723 -36.371  1.00 67.31           C  
ANISOU 7013  CD  GLN C 912     8990   7731   8855   -298   1075    279       C  
ATOM   7014  OE1 GLN C 912     -64.467  52.257 -35.664  1.00 70.85           O  
ANISOU 7014  OE1 GLN C 912     9389   8217   9312   -374   1031    207       O  
ATOM   7015  NE2 GLN C 912     -65.203  53.716 -37.232  1.00 67.13           N  
ANISOU 7015  NE2 GLN C 912     9018   7640   8848   -295   1164    327       N  
ATOM   7016  N   GLY C 913     -68.972  49.680 -39.626  1.00 52.17           N  
ANISOU 7016  N   GLY C 913     6963   6091   6767     63    910    501       N  
ATOM   7017  CA  GLY C 913     -69.726  49.455 -40.846  1.00 52.15           C  
ANISOU 7017  CA  GLY C 913     6950   6141   6722    150    908    569       C  
ATOM   7018  C   GLY C 913     -71.072  48.794 -40.678  1.00 58.34           C  
ANISOU 7018  C   GLY C 913     7712   6986   7470    216    854    584       C  
ATOM   7019  O   GLY C 913     -71.937  48.978 -41.542  1.00 57.56           O  
ANISOU 7019  O   GLY C 913     7618   6917   7335    297    870    647       O  
ATOM   7020  N   ASP C 914     -71.220  47.972 -39.623  1.00 58.72           N  
ANISOU 7020  N   ASP C 914     7730   7059   7523    182    789    529       N  
ATOM   7021  CA  ASP C 914     -72.515  47.368 -39.252  1.00 56.08           C  
ANISOU 7021  CA  ASP C 914     7375   6775   7160    232    741    536       C  
ATOM   7022  C   ASP C 914     -72.696  47.435 -37.716  1.00 53.67           C  
ANISOU 7022  C   ASP C 914     7084   6429   6879    194    728    487       C  
ATOM   7023  O   ASP C 914     -72.402  46.461 -37.000  1.00 49.49           O  
ANISOU 7023  O   ASP C 914     6519   5932   6353    151    666    434       O  
ATOM   7024  CB  ASP C 914     -72.582  45.926 -39.771  1.00 63.08           C  
ANISOU 7024  CB  ASP C 914     8198   7757   8014    236    664    521       C  
ATOM   7025  CG  ASP C 914     -73.958  45.300 -39.648  1.00 69.83           C  
ANISOU 7025  CG  ASP C 914     9026   8673   8835    287    620    535       C  
ATOM   7026  OD1 ASP C 914     -74.881  45.783 -40.325  1.00 72.49           O  
ANISOU 7026  OD1 ASP C 914     9369   9032   9142    357    646    591       O  
ATOM   7027  OD2 ASP C 914     -74.096  44.298 -38.895  1.00 76.31           O  
ANISOU 7027  OD2 ASP C 914     9816   9523   9655    256    560    490       O  
ATOM   7028  N   PRO C 915     -73.114  48.610 -37.202  1.00 47.06           N  
ANISOU 7028  N   PRO C 915     6305   5518   6059    211    790    504       N  
ATOM   7029  CA  PRO C 915     -73.111  48.891 -35.767  1.00 46.45           C  
ANISOU 7029  CA  PRO C 915     6252   5389   6007    170    790    454       C  
ATOM   7030  C   PRO C 915     -74.409  48.527 -35.026  1.00 41.67           C  
ANISOU 7030  C   PRO C 915     5637   4815   5381    216    758    459       C  
ATOM   7031  O   PRO C 915     -74.586  48.892 -33.865  1.00 40.05           O  
ANISOU 7031  O   PRO C 915     5460   4566   5192    197    767    428       O  
ATOM   7032  CB  PRO C 915     -72.898  50.405 -35.740  1.00 45.68           C  
ANISOU 7032  CB  PRO C 915     6230   5188   5936    168    884    474       C  
ATOM   7033  CG  PRO C 915     -73.670  50.879 -36.931  1.00 45.56           C  
ANISOU 7033  CG  PRO C 915     6232   5185   5893    257    927    557       C  
ATOM   7034  CD  PRO C 915     -73.594  49.776 -37.963  1.00 45.94           C  
ANISOU 7034  CD  PRO C 915     6214   5331   5910    274    868    572       C  
ATOM   7035  N   ILE C 916     -75.299  47.820 -35.695  1.00 38.81           N  
ANISOU 7035  N   ILE C 916     5234   4532   4982    272    721    496       N  
ATOM   7036  CA  ILE C 916     -76.527  47.382 -35.109  1.00 39.57           C  
ANISOU 7036  CA  ILE C 916     5309   4669   5055    312    688    503       C  
ATOM   7037  C   ILE C 916     -76.409  45.885 -34.835  1.00 37.90           C  
ANISOU 7037  C   ILE C 916     5038   4527   4833    273    606    460       C  
ATOM   7038  O   ILE C 916     -76.163  45.080 -35.755  1.00 39.32           O  
ANISOU 7038  O   ILE C 916     5178   4765   4995    272    571    464       O  
ATOM   7039  CB  ILE C 916     -77.719  47.648 -36.049  1.00 41.88           C  
ANISOU 7039  CB  ILE C 916     5594   5011   5308    404    706    574       C  
ATOM   7040  CG1 ILE C 916     -77.747  49.132 -36.496  1.00 45.70           C  
ANISOU 7040  CG1 ILE C 916     6143   5422   5798    452    797    626       C  
ATOM   7041  CG2 ILE C 916     -79.004  47.148 -35.393  1.00 41.23           C  
ANISOU 7041  CG2 ILE C 916     5481   4983   5203    439    671    577       C  
ATOM   7042  CD1 ILE C 916     -77.984  50.146 -35.395  1.00 48.63           C  
ANISOU 7042  CD1 ILE C 916     6578   5705   6194    455    850    618       C  
ATOM   7043  N   GLY C 917     -76.604  45.521 -33.575  1.00 33.29           N  
ANISOU 7043  N   GLY C 917     4453   3937   4260    246    579    419       N  
ATOM   7044  CA  GLY C 917     -76.585  44.112 -33.154  1.00 32.85           C  
ANISOU 7044  CA  GLY C 917     4349   3938   4195    214    508    381       C  
ATOM   7045  C   GLY C 917     -77.842  43.645 -32.438  1.00 30.44           C  
ANISOU 7045  C   GLY C 917     4026   3669   3872    242    483    386       C  
ATOM   7046  O   GLY C 917     -78.720  44.455 -32.067  1.00 28.75           O  
ANISOU 7046  O   GLY C 917     3836   3435   3654    285    519    414       O  
ATOM   7047  N   LEU C 918     -77.931  42.329 -32.308  1.00 27.99           N  
ANISOU 7047  N   LEU C 918     3674   3411   3550    218    425    362       N  
ATOM   7048  CA  LEU C 918     -79.018  41.666 -31.630  1.00 27.34           C  
ANISOU 7048  CA  LEU C 918     3568   3368   3452    230    397    361       C  
ATOM   7049  C   LEU C 918     -78.481  40.874 -30.440  1.00 26.87           C  
ANISOU 7049  C   LEU C 918     3508   3294   3406    180    364    309       C  
ATOM   7050  O   LEU C 918     -77.472  40.153 -30.540  1.00 26.26           O  
ANISOU 7050  O   LEU C 918     3422   3219   3335    141    336    277       O  
ATOM   7051  CB  LEU C 918     -79.758  40.733 -32.574  1.00 27.85           C  
ANISOU 7051  CB  LEU C 918     3584   3513   3486    247    362    380       C  
ATOM   7052  CG  LEU C 918     -80.488  41.355 -33.758  1.00 29.79           C  
ANISOU 7052  CG  LEU C 918     3817   3797   3705    306    387    434       C  
ATOM   7053  CD1 LEU C 918     -81.074  40.287 -34.655  1.00 30.59           C  
ANISOU 7053  CD1 LEU C 918     3865   3985   3774    308    343    438       C  
ATOM   7054  CD2 LEU C 918     -81.566  42.305 -33.272  1.00 32.44           C  
ANISOU 7054  CD2 LEU C 918     4166   4125   4033    361    425    470       C  
ATOM   7055  N   ILE C 919     -79.179  41.019 -29.327  1.00 25.92           N  
ANISOU 7055  N   ILE C 919     3398   3163   3286    190    370    305       N  
ATOM   7056  CA  ILE C 919     -78.827  40.347 -28.101  1.00 27.20           C  
ANISOU 7056  CA  ILE C 919     3564   3316   3456    154    344    263       C  
ATOM   7057  C   ILE C 919     -80.100  39.798 -27.394  1.00 25.22           C  
ANISOU 7057  C   ILE C 919     3294   3099   3189    173    331    274       C  
ATOM   7058  O   ILE C 919     -81.157  40.417 -27.396  1.00 27.43           O  
ANISOU 7058  O   ILE C 919     3574   3390   3459    215    356    308       O  
ATOM   7059  CB  ILE C 919     -78.036  41.303 -27.206  1.00 27.35           C  
ANISOU 7059  CB  ILE C 919     3626   3272   3496    136    373    234       C  
ATOM   7060  CG1 ILE C 919     -77.383  40.538 -26.081  1.00 30.86           C  
ANISOU 7060  CG1 ILE C 919     4068   3716   3942     99    340    186       C  
ATOM   7061  CG2 ILE C 919     -78.932  42.358 -26.638  1.00 28.30           C  
ANISOU 7061  CG2 ILE C 919     3776   3362   3616    175    415    255       C  
ATOM   7062  CD1 ILE C 919     -76.286  41.338 -25.445  1.00 34.95           C  
ANISOU 7062  CD1 ILE C 919     4616   4186   4476     67    359    146       C  
ATOM   7063  N   LEU C 920     -79.978  38.620 -26.842  1.00 22.81           N  
ANISOU 7063  N   LEU C 920     2973   2814   2880    144    294    249       N  
ATOM   7064  CA  LEU C 920     -81.069  37.974 -26.146  1.00 21.53           C  
ANISOU 7064  CA  LEU C 920     2793   2682   2704    151    283    256       C  
ATOM   7065  C   LEU C 920     -81.016  38.173 -24.644  1.00 21.09           C  
ANISOU 7065  C   LEU C 920     2765   2596   2654    148    292    235       C  
ATOM   7066  O   LEU C 920     -79.945  38.226 -24.049  1.00 19.08           O  
ANISOU 7066  O   LEU C 920     2533   2308   2409    125    286    200       O  
ATOM   7067  CB  LEU C 920     -81.013  36.486 -26.403  1.00 20.73           C  
ANISOU 7067  CB  LEU C 920     2666   2616   2595    120    243    242       C  
ATOM   7068  CG  LEU C 920     -81.216  36.071 -27.837  1.00 21.24           C  
ANISOU 7068  CG  LEU C 920     2699   2722   2648    119    229    257       C  
ATOM   7069  CD1 LEU C 920     -80.771  34.664 -28.055  1.00 21.13           C  
ANISOU 7069  CD1 LEU C 920     2675   2721   2631     82    195    232       C  
ATOM   7070  CD2 LEU C 920     -82.684  36.195 -28.187  1.00 23.80           C  
ANISOU 7070  CD2 LEU C 920     2990   3098   2954    146    237    291       C  
ATOM   7071  N   LEU C 921     -82.196  38.255 -24.027  1.00 22.16           N  
ANISOU 7071  N   LEU C 921     2893   2749   2779    174    304    256       N  
ATOM   7072  CA  LEU C 921     -82.326  37.974 -22.578  1.00 21.32           C  
ANISOU 7072  CA  LEU C 921     2802   2631   2669    169    303    237       C  
ATOM   7073  C   LEU C 921     -83.047  36.663 -22.431  1.00 21.71           C  
ANISOU 7073  C   LEU C 921     2820   2724   2707    154    279    244       C  
ATOM   7074  O   LEU C 921     -84.152  36.481 -22.949  1.00 22.16           O  
ANISOU 7074  O   LEU C 921     2843   2825   2754    167    282    274       O  
ATOM   7075  CB  LEU C 921     -83.088  39.064 -21.861  1.00 20.12           C  
ANISOU 7075  CB  LEU C 921     2671   2463   2513    209    341    253       C  
ATOM   7076  CG  LEU C 921     -82.285  40.327 -21.606  1.00 20.31           C  
ANISOU 7076  CG  LEU C 921     2741   2427   2550    214    370    233       C  
ATOM   7077  CD1 LEU C 921     -83.231  41.444 -21.238  1.00 20.75           C  
ANISOU 7077  CD1 LEU C 921     2819   2467   2600    265    415    259       C  
ATOM   7078  CD2 LEU C 921     -81.251  40.130 -20.507  1.00 20.52           C  
ANISOU 7078  CD2 LEU C 921     2792   2425   2580    182    356    183       C  
ATOM   7079  N   GLY C 922     -82.403  35.726 -21.756  1.00 22.22           N  
ANISOU 7079  N   GLY C 922     2894   2778   2771    126    258    217       N  
ATOM   7080  CA  GLY C 922     -82.985  34.401 -21.511  1.00 21.17           C  
ANISOU 7080  CA  GLY C 922     2742   2673   2629    107    242    221       C  
ATOM   7081  C   GLY C 922     -83.211  34.175 -20.034  1.00 21.66           C  
ANISOU 7081  C   GLY C 922     2822   2724   2682    114    250    215       C  
ATOM   7082  O   GLY C 922     -82.410  34.592 -19.193  1.00 20.23           O  
ANISOU 7082  O   GLY C 922     2672   2515   2501    121    253    192       O  
ATOM   7083  N   GLU C 923     -84.305  33.499 -19.716  1.00 20.84           N  
ANISOU 7083  N   GLU C 923     2699   2650   2571    110    256    235       N  
ATOM   7084  CA  GLU C 923     -84.504  32.990 -18.376  1.00 21.00           C  
ANISOU 7084  CA  GLU C 923     2735   2663   2581    113    264    233       C  
ATOM   7085  C   GLU C 923     -83.773  31.663 -18.365  1.00 20.09           C  
ANISOU 7085  C   GLU C 923     2632   2535   2465     83    243    216       C  
ATOM   7086  O   GLU C 923     -84.101  30.757 -19.141  1.00 19.87           O  
ANISOU 7086  O   GLU C 923     2586   2523   2441     53    234    222       O  
ATOM   7087  CB  GLU C 923     -85.999  32.776 -18.050  1.00 20.27           C  
ANISOU 7087  CB  GLU C 923     2614   2607   2480    118    284    264       C  
ATOM   7088  CG  GLU C 923     -86.227  32.332 -16.607  1.00 21.58           C  
ANISOU 7088  CG  GLU C 923     2801   2765   2634    126    298    266       C  
ATOM   7089  CD  GLU C 923     -87.674  31.954 -16.307  1.00 22.14           C  
ANISOU 7089  CD  GLU C 923     2839   2876   2698    123    320    296       C  
ATOM   7090  OE1 GLU C 923     -88.571  32.566 -16.877  1.00 22.35           O  
ANISOU 7090  OE1 GLU C 923     2830   2940   2723    137    330    317       O  
ATOM   7091  OE2 GLU C 923     -87.913  31.008 -15.523  1.00 24.28           O  
ANISOU 7091  OE2 GLU C 923     3118   3145   2962    108    328    301       O  
ATOM   7092  N   VAL C 924     -82.758  31.553 -17.519  1.00 19.57           N  
ANISOU 7092  N   VAL C 924     2600   2445   2392     92    236    194       N  
ATOM   7093  CA  VAL C 924     -81.952  30.347 -17.439  1.00 17.83           C  
ANISOU 7093  CA  VAL C 924     2397   2213   2167     77    220    181       C  
ATOM   7094  C   VAL C 924     -82.179  29.698 -16.087  1.00 18.67           C  
ANISOU 7094  C   VAL C 924     2524   2314   2254     90    233    188       C  
ATOM   7095  O   VAL C 924     -82.005  30.324 -15.040  1.00 18.13           O  
ANISOU 7095  O   VAL C 924     2472   2244   2173    118    241    181       O  
ATOM   7096  CB  VAL C 924     -80.465  30.708 -17.601  1.00 18.05           C  
ANISOU 7096  CB  VAL C 924     2438   2227   2194     82    200    150       C  
ATOM   7097  CG1 VAL C 924     -79.597  29.454 -17.616  1.00 18.19           C  
ANISOU 7097  CG1 VAL C 924     2473   2237   2202     76    185    140       C  
ATOM   7098  CG2 VAL C 924     -80.256  31.504 -18.875  1.00 19.06           C  
ANISOU 7098  CG2 VAL C 924     2547   2356   2339     72    194    147       C  
ATOM   7099  N   ALA C 925     -82.519  28.422 -16.080  1.00 19.53           N  
ANISOU 7099  N   ALA C 925     2640   2419   2362     71    239    201       N  
ATOM   7100  CA  ALA C 925     -82.759  27.711 -14.833  1.00 19.88           C  
ANISOU 7100  CA  ALA C 925     2710   2456   2388     85    258    214       C  
ATOM   7101  C   ALA C 925     -81.460  27.130 -14.350  1.00 20.45           C  
ANISOU 7101  C   ALA C 925     2816   2513   2443    107    245    198       C  
ATOM   7102  O   ALA C 925     -81.061  26.024 -14.733  1.00 21.14           O  
ANISOU 7102  O   ALA C 925     2920   2582   2529     95    242    199       O  
ATOM   7103  CB  ALA C 925     -83.785  26.601 -15.061  1.00 21.18           C  
ANISOU 7103  CB  ALA C 925     2868   2619   2560     50    277    237       C  
ATOM   7104  N   LEU C 926     -80.767  27.864 -13.500  1.00 22.10           N  
ANISOU 7104  N   LEU C 926     3035   2730   2633    141    237    181       N  
ATOM   7105  CA  LEU C 926     -79.423  27.512 -13.110  1.00 21.36           C  
ANISOU 7105  CA  LEU C 926     2962   2637   2518    165    219    160       C  
ATOM   7106  C   LEU C 926     -79.373  26.521 -11.981  1.00 24.61           C  
ANISOU 7106  C   LEU C 926     3406   3046   2900    196    235    178       C  
ATOM   7107  O   LEU C 926     -78.386  25.771 -11.846  1.00 21.97           O  
ANISOU 7107  O   LEU C 926     3092   2711   2546    218    225    172       O  
ATOM   7108  CB  LEU C 926     -78.654  28.759 -12.663  1.00 21.01           C  
ANISOU 7108  CB  LEU C 926     2911   2611   2463    183    203    127       C  
ATOM   7109  CG  LEU C 926     -78.522  29.817 -13.726  1.00 19.97           C  
ANISOU 7109  CG  LEU C 926     2754   2476   2358    158    193    110       C  
ATOM   7110  CD1 LEU C 926     -78.077  31.119 -13.102  1.00 21.49           C  
ANISOU 7110  CD1 LEU C 926     2947   2676   2542    169    191     79       C  
ATOM   7111  CD2 LEU C 926     -77.540  29.380 -14.787  1.00 20.58           C  
ANISOU 7111  CD2 LEU C 926     2824   2551   2444    142    171     97       C  
ATOM   7112  N   GLY C 927     -80.378  26.560 -11.094  1.00 27.11           N  
ANISOU 7112  N   GLY C 927     3728   3364   3208    205    261    200       N  
ATOM   7113  CA  GLY C 927     -80.395  25.687  -9.922  1.00 26.20           C  
ANISOU 7113  CA  GLY C 927     3647   3247   3061    240    282    222       C  
ATOM   7114  C   GLY C 927     -79.153  25.858  -9.083  1.00 25.88           C  
ANISOU 7114  C   GLY C 927     3621   3232   2981    288    263    200       C  
ATOM   7115  O   GLY C 927     -78.689  26.951  -8.887  1.00 29.50           O  
ANISOU 7115  O   GLY C 927     4062   3715   3433    295    243    167       O  
ATOM   7116  N   ASN C 928     -78.636  24.762  -8.584  1.00 27.53           N  
ANISOU 7116  N   ASN C 928     3862   3437   3162    322    271    216       N  
ATOM   7117  CA  ASN C 928     -77.375  24.702  -7.877  1.00 31.59           C  
ANISOU 7117  CA  ASN C 928     4385   3986   3632    374    251    198       C  
ATOM   7118  C   ASN C 928     -76.182  24.778  -8.853  1.00 26.81           C  
ANISOU 7118  C   ASN C 928     3761   3390   3034    364    217    167       C  
ATOM   7119  O   ASN C 928     -75.932  23.871  -9.649  1.00 25.11           O  
ANISOU 7119  O   ASN C 928     3560   3149   2832    356    220    180       O  
ATOM   7120  CB  ASN C 928     -77.342  23.389  -7.070  1.00 36.97           C  
ANISOU 7120  CB  ASN C 928     5111   4656   4278    420    280    237       C  
ATOM   7121  CG  ASN C 928     -76.318  23.376  -5.966  1.00 44.97           C  
ANISOU 7121  CG  ASN C 928     6134   5721   5233    489    266    227       C  
ATOM   7122  OD1 ASN C 928     -75.504  24.293  -5.792  1.00 44.95           O  
ANISOU 7122  OD1 ASN C 928     6102   5766   5212    499    231    184       O  
ATOM   7123  ND2 ASN C 928     -76.337  22.269  -5.212  1.00 47.81           N  
ANISOU 7123  ND2 ASN C 928     6537   6071   5557    539    297    267       N  
ATOM   7124  N   MET C 929     -75.448  25.870  -8.733  1.00 24.64           N  
ANISOU 7124  N   MET C 929     3458   3153   2750    365    187    126       N  
ATOM   7125  CA  MET C 929     -74.369  26.184  -9.617  1.00 25.17           C  
ANISOU 7125  CA  MET C 929     3500   3237   2827    350    157     93       C  
ATOM   7126  C   MET C 929     -73.076  25.557  -9.142  1.00 24.23           C  
ANISOU 7126  C   MET C 929     3385   3161   2661    402    139     85       C  
ATOM   7127  O   MET C 929     -72.717  25.652  -7.974  1.00 23.55           O  
ANISOU 7127  O   MET C 929     3302   3118   2529    445    135     76       O  
ATOM   7128  CB  MET C 929     -74.193  27.707  -9.694  1.00 25.30           C  
ANISOU 7128  CB  MET C 929     3484   3271   2857    320    139     50       C  
ATOM   7129  CG  MET C 929     -75.381  28.399 -10.281  1.00 25.33           C  
ANISOU 7129  CG  MET C 929     3483   3238   2904    278    156     61       C  
ATOM   7130  SD  MET C 929     -75.281  30.212 -10.299  1.00 27.61           S  
ANISOU 7130  SD  MET C 929     3750   3534   3208    250    149     16       S  
ATOM   7131  CE  MET C 929     -75.001  30.535  -8.560  1.00 29.84           C  
ANISOU 7131  CE  MET C 929     4045   3857   3437    292    147     -8       C  
ATOM   7132  N   TYR C 930     -72.383  24.913 -10.061  1.00 24.61           N  
ANISOU 7132  N   TYR C 930     3431   3202   2717    401    130     87       N  
ATOM   7133  CA  TYR C 930     -71.010  24.434  -9.838  1.00 25.44           C  
ANISOU 7133  CA  TYR C 930     3529   3358   2779    451    110     75       C  
ATOM   7134  C   TYR C 930     -70.096  25.616 -10.106  1.00 25.71           C  
ANISOU 7134  C   TYR C 930     3513   3441   2815    425     75     22       C  
ATOM   7135  O   TYR C 930     -69.953  26.049 -11.249  1.00 24.56           O  
ANISOU 7135  O   TYR C 930     3346   3278   2709    378     66      7       O  
ATOM   7136  CB  TYR C 930     -70.745  23.277 -10.791  1.00 25.25           C  
ANISOU 7136  CB  TYR C 930     3527   3300   2766    459    120    100       C  
ATOM   7137  CG  TYR C 930     -69.465  22.481 -10.606  1.00 26.36           C  
ANISOU 7137  CG  TYR C 930     3671   3484   2859    525    109    103       C  
ATOM   7138  CD1 TYR C 930     -68.820  22.405  -9.389  1.00 27.95           C  
ANISOU 7138  CD1 TYR C 930     3869   3750   3001    589    101    100       C  
ATOM   7139  CD2 TYR C 930     -68.931  21.774 -11.673  1.00 26.06           C  
ANISOU 7139  CD2 TYR C 930     3641   3428   2833    528    109    110       C  
ATOM   7140  CE1 TYR C 930     -67.654  21.664  -9.235  1.00 29.45           C  
ANISOU 7140  CE1 TYR C 930     4059   3990   3142    658     92    107       C  
ATOM   7141  CE2 TYR C 930     -67.787  21.047 -11.531  1.00 27.09           C  
ANISOU 7141  CE2 TYR C 930     3774   3600   2918    594    103    116       C  
ATOM   7142  CZ  TYR C 930     -67.167  20.967 -10.307  1.00 29.36           C  
ANISOU 7142  CZ  TYR C 930     4057   3955   3145    662     95    117       C  
ATOM   7143  OH  TYR C 930     -66.019  20.230 -10.199  1.00 32.13           O  
ANISOU 7143  OH  TYR C 930     4406   4355   3446    737     89    126       O  
ATOM   7144  N   GLU C 931     -69.549  26.201  -9.056  1.00 28.13           N  
ANISOU 7144  N   GLU C 931     3800   3808   3080    448     58     -8       N  
ATOM   7145  CA  GLU C 931     -68.807  27.468  -9.186  1.00 30.47           C  
ANISOU 7145  CA  GLU C 931     4051   4147   3381    410     31    -66       C  
ATOM   7146  C   GLU C 931     -67.339  27.197  -9.450  1.00 31.34           C  
ANISOU 7146  C   GLU C 931     4126   4322   3462    432      4    -89       C  
ATOM   7147  O   GLU C 931     -66.711  26.501  -8.693  1.00 33.97           O  
ANISOU 7147  O   GLU C 931     4459   4711   3739    495     -5    -82       O  
ATOM   7148  CB  GLU C 931     -68.951  28.296  -7.932  1.00 33.24           C  
ANISOU 7148  CB  GLU C 931     4396   4533   3700    416     27    -97       C  
ATOM   7149  CG  GLU C 931     -70.402  28.523  -7.560  1.00 35.44           C  
ANISOU 7149  CG  GLU C 931     4709   4755   4002    405     57    -70       C  
ATOM   7150  CD  GLU C 931     -70.617  29.661  -6.584  1.00 37.75           C  
ANISOU 7150  CD  GLU C 931     4997   5070   4277    395     55   -110       C  
ATOM   7151  OE1 GLU C 931     -69.658  30.114  -5.937  1.00 42.54           O  
ANISOU 7151  OE1 GLU C 931     5578   5743   4843    404     30   -158       O  
ATOM   7152  OE2 GLU C 931     -71.765  30.082  -6.433  1.00 42.38           O  
ANISOU 7152  OE2 GLU C 931     5605   5611   4887    379     79    -94       O  
ATOM   7153  N   LEU C 932     -66.805  27.716 -10.551  1.00 29.56           N  
ANISOU 7153  N   LEU C 932     3868   4093   3270    384     -8   -113       N  
ATOM   7154  CA  LEU C 932     -65.441  27.380 -10.965  1.00 29.26           C  
ANISOU 7154  CA  LEU C 932     3793   4116   3207    404    -31   -129       C  
ATOM   7155  C   LEU C 932     -64.688  28.642 -11.303  1.00 29.65           C  
ANISOU 7155  C   LEU C 932     3792   4202   3272    344    -50   -187       C  
ATOM   7156  O   LEU C 932     -65.271  29.636 -11.740  1.00 29.25           O  
ANISOU 7156  O   LEU C 932     3743   4102   3267    283    -39   -202       O  
ATOM   7157  CB  LEU C 932     -65.471  26.471 -12.194  1.00 26.82           C  
ANISOU 7157  CB  LEU C 932     3503   3762   2926    409    -20    -92       C  
ATOM   7158  CG  LEU C 932     -66.109  25.104 -11.987  1.00 26.27           C  
ANISOU 7158  CG  LEU C 932     3488   3649   2843    462      5    -37       C  
ATOM   7159  CD1 LEU C 932     -66.207  24.342 -13.293  1.00 25.50           C  
ANISOU 7159  CD1 LEU C 932     3410   3499   2778    453     17    -11       C  
ATOM   7160  CD2 LEU C 932     -65.312  24.287 -10.965  1.00 27.47           C  
ANISOU 7160  CD2 LEU C 932     3644   3869   2926    547     -2    -27       C  
ATOM   7161  N   LYS C 933     -63.402  28.621 -11.024  1.00 32.89           N  
ANISOU 7161  N   LYS C 933     4155   4701   3639    365    -76   -219       N  
ATOM   7162  CA  LYS C 933     -62.546  29.794 -11.250  1.00 33.81           C  
ANISOU 7162  CA  LYS C 933     4218   4864   3765    303    -93   -281       C  
ATOM   7163  C   LYS C 933     -61.643  29.617 -12.431  1.00 32.20           C  
ANISOU 7163  C   LYS C 933     3979   4679   3577    288   -100   -282       C  
ATOM   7164  O   LYS C 933     -61.071  30.583 -12.892  1.00 36.10           O  
ANISOU 7164  O   LYS C 933     4433   5189   4093    226   -105   -324       O  
ATOM   7165  CB  LYS C 933     -61.672  30.060 -10.007  1.00 36.29           C  
ANISOU 7165  CB  LYS C 933     4490   5284   4013    325   -120   -329       C  
ATOM   7166  CG  LYS C 933     -62.439  30.460  -8.760  1.00 38.11           C  
ANISOU 7166  CG  LYS C 933     4749   5508   4222    333   -115   -342       C  
ATOM   7167  CD  LYS C 933     -61.544  30.459  -7.540  1.00 44.57           C  
ANISOU 7167  CD  LYS C 933     5527   6445   4963    372   -145   -383       C  
ATOM   7168  CE  LYS C 933     -62.202  29.720  -6.362  1.00 52.09           C  
ANISOU 7168  CE  LYS C 933     6521   7405   5867    451   -138   -347       C  
ATOM   7169  NZ  LYS C 933     -61.645  30.208  -5.075  1.00 56.09           N  
ANISOU 7169  NZ  LYS C 933     6993   8013   6306    465   -164   -403       N  
ATOM   7170  N   HIS C 934     -61.471  28.383 -12.888  1.00 29.68           N  
ANISOU 7170  N   HIS C 934     3675   4358   3244    347    -98   -237       N  
ATOM   7171  CA AHIS C 934     -60.573  28.091 -13.986  0.50 28.43           C  
ANISOU 7171  CA AHIS C 934     3485   4224   3094    345   -103   -235       C  
ATOM   7172  CA BHIS C 934     -60.581  28.112 -13.997  0.50 29.90           C  
ANISOU 7172  CA BHIS C 934     3670   4409   3280    343   -103   -235       C  
ATOM   7173  C   HIS C 934     -61.170  27.021 -14.890  1.00 28.07           C  
ANISOU 7173  C   HIS C 934     3489   4105   3072    375    -83   -178       C  
ATOM   7174  O   HIS C 934     -62.128  26.345 -14.511  1.00 25.22           O  
ANISOU 7174  O   HIS C 934     3182   3689   2710    406    -66   -141       O  
ATOM   7175  CB AHIS C 934     -59.215  27.610 -13.462  0.50 29.00           C  
ANISOU 7175  CB AHIS C 934     3506   4415   3100    402   -129   -252       C  
ATOM   7176  CB BHIS C 934     -59.129  27.843 -13.529  0.50 32.53           C  
ANISOU 7176  CB BHIS C 934     3943   4865   3551    387   -131   -262       C  
ATOM   7177  CG AHIS C 934     -58.645  28.479 -12.386  0.50 28.96           C  
ANISOU 7177  CG AHIS C 934     3451   4496   3057    381   -152   -311       C  
ATOM   7178  CG BHIS C 934     -58.877  26.493 -12.931  0.50 34.59           C  
ANISOU 7178  CG BHIS C 934     4224   5166   3752    491   -134   -223       C  
ATOM   7179  ND1AHIS C 934     -58.049  29.697 -12.644  0.50 29.14           N  
ANISOU 7179  ND1AHIS C 934     3421   4551   3101    299   -162   -370       N  
ATOM   7180  ND1BHIS C 934     -58.582  25.381 -13.690  0.50 35.98           N  
ANISOU 7180  ND1BHIS C 934     4420   5329   3923    545   -123   -180       N  
ATOM   7181  CD2AHIS C 934     -58.619  28.323 -11.045  0.50 28.38           C  
ANISOU 7181  CD2AHIS C 934     3376   4480   2926    428   -166   -322       C  
ATOM   7182  CD2BHIS C 934     -58.780  26.100 -11.641  0.50 37.06           C  
ANISOU 7182  CD2BHIS C 934     4541   5537   4004    555   -143   -220       C  
ATOM   7183  CE1AHIS C 934     -57.667  30.242 -11.505  0.50 27.85           C  
ANISOU 7183  CE1AHIS C 934     3224   4463   2894    292   -182   -420       C  
ATOM   7184  CE1BHIS C 934     -58.351  24.357 -12.893  0.50 36.97           C  
ANISOU 7184  CE1BHIS C 934     4565   5495   3988    639   -123   -151       C  
ATOM   7185  NE2AHIS C 934     -58.001  29.428 -10.523  0.50 27.71           N  
ANISOU 7185  NE2AHIS C 934     3236   4466   2827    372   -187   -391       N  
ATOM   7186  NE2BHIS C 934     -58.471  24.763 -11.643  0.50 36.68           N  
ANISOU 7186  NE2BHIS C 934     4518   5504   3916    648   -135   -172       N  
ATOM   7187  N   ALA C 935     -60.592  26.887 -16.073  1.00 26.09           N  
ANISOU 7187  N   ALA C 935     3218   3855   2840    362    -83   -175       N  
ATOM   7188  CA  ALA C 935     -61.091  26.002 -17.110  1.00 28.48           C  
ANISOU 7188  CA  ALA C 935     3564   4089   3168    378    -64   -132       C  
ATOM   7189  C   ALA C 935     -61.231  24.541 -16.642  1.00 31.66           C  
ANISOU 7189  C   ALA C 935     4015   4483   3532    462    -54    -90       C  
ATOM   7190  O   ALA C 935     -60.426  24.045 -15.863  1.00 28.74           O  
ANISOU 7190  O   ALA C 935     3630   4185   3106    526    -65    -91       O  
ATOM   7191  CB  ALA C 935     -60.170  26.042 -18.291  1.00 28.37           C  
ANISOU 7191  CB  ALA C 935     3513   4102   3163    366    -68   -140       C  
ATOM   7192  N   SER C 936     -62.319  23.911 -17.019  1.00 32.46           N  
ANISOU 7192  N   SER C 936     4175   4497   3660    459    -30    -55       N  
ATOM   7193  CA  SER C 936     -62.557  22.600 -16.478  1.00 36.26           C  
ANISOU 7193  CA  SER C 936     4711   4957   4109    530    -12    -16       C  
ATOM   7194  C   SER C 936     -63.207  21.692 -17.492  1.00 35.27           C  
ANISOU 7194  C   SER C 936     4639   4748   4013    526     13     15       C  
ATOM   7195  O   SER C 936     -64.063  22.104 -18.276  1.00 32.54           O  
ANISOU 7195  O   SER C 936     4302   4346   3717    462     20     13       O  
ATOM   7196  CB  SER C 936     -63.355  22.710 -15.166  1.00 41.57           C  
ANISOU 7196  CB  SER C 936     5408   5618   4767    540     -5     -8       C  
ATOM   7197  OG  SER C 936     -63.491  21.438 -14.560  1.00 53.79           O  
ANISOU 7197  OG  SER C 936     7010   7150   6279    614     17     32       O  
ATOM   7198  N   HIS C 937     -62.723  20.464 -17.550  1.00 35.51           N  
ANISOU 7198  N   HIS C 937     4705   4778   4011    595     28     41       N  
ATOM   7199  CA  HIS C 937     -63.457  19.423 -18.255  1.00 37.65           C  
ANISOU 7199  CA  HIS C 937     5042   4960   4303    595     59     69       C  
ATOM   7200  C   HIS C 937     -64.750  19.049 -17.543  1.00 40.80           C  
ANISOU 7200  C   HIS C 937     5496   5292   4714    583     85     94       C  
ATOM   7201  O   HIS C 937     -64.713  18.494 -16.451  1.00 41.63           O  
ANISOU 7201  O   HIS C 937     5630   5406   4782    641     99    116       O  
ATOM   7202  CB  HIS C 937     -62.572  18.203 -18.397  1.00 38.89           C  
ANISOU 7202  CB  HIS C 937     5232   5129   4418    679     74     91       C  
ATOM   7203  CG  HIS C 937     -63.307  17.018 -18.888  1.00 39.65           C  
ANISOU 7203  CG  HIS C 937     5409   5130   4528    685    112    119       C  
ATOM   7204  ND1 HIS C 937     -63.765  16.942 -20.174  1.00 42.71           N  
ANISOU 7204  ND1 HIS C 937     5809   5462   4957    629    118    109       N  
ATOM   7205  CD2 HIS C 937     -63.752  15.910 -18.260  1.00 42.13           C  
ANISOU 7205  CD2 HIS C 937     5795   5388   4822    731    150    154       C  
ATOM   7206  CE1 HIS C 937     -64.427  15.814 -20.338  1.00 45.12           C  
ANISOU 7206  CE1 HIS C 937     6191   5686   5268    637    156    131       C  
ATOM   7207  NE2 HIS C 937     -64.428  15.164 -19.193  1.00 44.76           N  
ANISOU 7207  NE2 HIS C 937     6186   5634   5188    698    178    160       N  
ATOM   7208  N   ILE C 938     -65.878  19.445 -18.138  1.00 50.39           N  
ANISOU 7208  N   ILE C 938     6717   6448   5979    508     91     89       N  
ATOM   7209  CA  ILE C 938     -67.190  18.951 -17.759  1.00 54.88           C  
ANISOU 7209  CA  ILE C 938     7337   6948   6567    486    121    113       C  
ATOM   7210  C   ILE C 938     -67.793  17.932 -18.749  1.00 60.02           C  
ANISOU 7210  C   ILE C 938     8041   7522   7242    463    149    126       C  
ATOM   7211  O   ILE C 938     -68.121  18.276 -19.905  1.00 58.51           O  
ANISOU 7211  O   ILE C 938     7831   7314   7085    407    140    109       O  
ATOM   7212  CB  ILE C 938     -68.257  20.088 -17.603  1.00 57.13           C  
ANISOU 7212  CB  ILE C 938     7593   7225   6890    416    113    101       C  
ATOM   7213  CG1 ILE C 938     -67.781  21.226 -16.676  1.00 51.80           C  
ANISOU 7213  CG1 ILE C 938     6869   6616   6196    424     87     80       C  
ATOM   7214  CG2 ILE C 938     -69.558  19.478 -17.050  1.00 58.61           C  
ANISOU 7214  CG2 ILE C 938     7829   7351   7088    402    146    129       C  
ATOM   7215  CD1 ILE C 938     -67.300  20.734 -15.326  1.00 49.86           C  
ANISOU 7215  CD1 ILE C 938     6640   6406   5897    496     92     94       C  
ATOM   7216  N   SER C 939     -67.931  16.693 -18.287  1.00 60.62           N  
ANISOU 7216  N   SER C 939     8183   7553   7296    507    185    155       N  
ATOM   7217  CA  SER C 939     -68.804  15.671 -18.948  1.00 66.91           C  
ANISOU 7217  CA  SER C 939     9042   8262   8117    472    222    165       C  
ATOM   7218  C   SER C 939     -70.171  15.583 -18.251  1.00 68.64           C  
ANISOU 7218  C   SER C 939     9286   8436   8357    430    248    182       C  
ATOM   7219  O   SER C 939     -71.176  16.069 -18.780  1.00 67.88           O  
ANISOU 7219  O   SER C 939     9168   8323   8300    355    243    169       O  
ATOM   7220  CB  SER C 939     -68.174  14.259 -18.952  1.00 61.55           C  
ANISOU 7220  CB  SER C 939     8435   7545   7406    542    257    187       C  
ATOM   7221  N   LYS C 940     -70.177  14.956 -17.068  1.00 62.00           N  
ANISOU 7221  N   LYS C 940     8490   7583   7486    485    277    214       N  
ATOM   7222  CA  LYS C 940     -71.326  14.948 -16.167  1.00 59.12           C  
ANISOU 7222  CA  LYS C 940     8143   7189   7132    458    303    234       C  
ATOM   7223  C   LYS C 940     -71.110  16.049 -15.130  1.00 54.79           C  
ANISOU 7223  C   LYS C 940     7542   6712   6563    482    273    231       C  
ATOM   7224  O   LYS C 940     -70.054  16.092 -14.493  1.00 60.81           O  
ANISOU 7224  O   LYS C 940     8296   7529   7282    555    259    235       O  
ATOM   7225  CB  LYS C 940     -71.461  13.577 -15.438  1.00 57.62           C  
ANISOU 7225  CB  LYS C 940     8039   6936   6917    507    360    275       C  
ATOM   7226  N   LEU C 941     -72.092  16.936 -14.946  1.00 43.30           N  
ANISOU 7226  N   LEU C 941     6052   5264   5137    424    264    223       N  
ATOM   7227  CA  LEU C 941     -72.080  17.808 -13.774  1.00 38.37           C  
ANISOU 7227  CA  LEU C 941     5396   4692   4491    449    249    223       C  
ATOM   7228  C   LEU C 941     -72.105  16.951 -12.521  1.00 35.93           C  
ANISOU 7228  C   LEU C 941     5140   4370   4141    513    285    261       C  
ATOM   7229  O   LEU C 941     -72.653  15.863 -12.538  1.00 34.91           O  
ANISOU 7229  O   LEU C 941     5070   4175   4018    511    330    290       O  
ATOM   7230  CB  LEU C 941     -73.307  18.711 -13.770  1.00 35.78           C  
ANISOU 7230  CB  LEU C 941     5037   4359   4200    381    246    215       C  
ATOM   7231  CG  LEU C 941     -73.275  19.888 -14.750  1.00 34.13           C  
ANISOU 7231  CG  LEU C 941     4768   4176   4023    329    209    180       C  
ATOM   7232  CD1 LEU C 941     -74.609  20.587 -14.761  1.00 32.01           C  
ANISOU 7232  CD1 LEU C 941     4478   3896   3788    272    216    181       C  
ATOM   7233  CD2 LEU C 941     -72.191  20.867 -14.346  1.00 34.77           C  
ANISOU 7233  CD2 LEU C 941     4806   4324   4079    361    173    154       C  
ATOM   7234  N   PRO C 942     -71.520  17.433 -11.419  1.00 34.64           N  
ANISOU 7234  N   PRO C 942     4956   4271   3934    571    268    262       N  
ATOM   7235  CA  PRO C 942     -71.669  16.702 -10.187  1.00 34.42           C  
ANISOU 7235  CA  PRO C 942     4977   4236   3866    634    304    302       C  
ATOM   7236  C   PRO C 942     -73.134  16.567  -9.829  1.00 37.94           C  
ANISOU 7236  C   PRO C 942     5448   4625   4340    584    342    325       C  
ATOM   7237  O   PRO C 942     -73.950  17.428 -10.208  1.00 36.26           O  
ANISOU 7237  O   PRO C 942     5196   4412   4169    513    328    304       O  
ATOM   7238  CB  PRO C 942     -71.019  17.606  -9.146  1.00 34.26           C  
ANISOU 7238  CB  PRO C 942     4912   4306   3800    681    270    285       C  
ATOM   7239  CG  PRO C 942     -70.047  18.434  -9.901  1.00 34.15           C  
ANISOU 7239  CG  PRO C 942     4837   4347   3792    664    220    239       C  
ATOM   7240  CD  PRO C 942     -70.611  18.580 -11.284  1.00 35.43           C  
ANISOU 7240  CD  PRO C 942     4992   4455   4017    583    219    224       C  
ATOM   7241  N   LYS C 943     -73.437  15.536  -9.037  1.00 39.53           N  
ANISOU 7241  N   LYS C 943     5714   4788   4518    628    393    370       N  
ATOM   7242  CA  LYS C 943     -74.807  15.219  -8.673  1.00 37.98           C  
ANISOU 7242  CA  LYS C 943     5547   4536   4347    582    438    398       C  
ATOM   7243  C   LYS C 943     -75.367  16.348  -7.869  1.00 33.69           C  
ANISOU 7243  C   LYS C 943     4957   4043   3800    570    419    388       C  
ATOM   7244  O   LYS C 943     -74.721  16.856  -6.973  1.00 34.42           O  
ANISOU 7244  O   LYS C 943     5030   4200   3846    631    397    383       O  
ATOM   7245  CB  LYS C 943     -74.896  13.918  -7.860  1.00 41.68           C  
ANISOU 7245  CB  LYS C 943     6099   4954   4784    641    502    452       C  
ATOM   7246  CG  LYS C 943     -74.630  12.674  -8.671  1.00 43.65           C  
ANISOU 7246  CG  LYS C 943     6411   5128   5045    641    538    465       C  
ATOM   7247  CD  LYS C 943     -75.823  12.264  -9.496  1.00 47.78           C  
ANISOU 7247  CD  LYS C 943     6952   5573   5628    538    570    459       C  
ATOM   7248  CE  LYS C 943     -75.415  11.091 -10.393  1.00 53.96           C  
ANISOU 7248  CE  LYS C 943     7799   6282   6420    537    600    461       C  
ATOM   7249  NZ  LYS C 943     -76.503  10.654 -11.319  1.00 56.61           N  
ANISOU 7249  NZ  LYS C 943     8149   6546   6812    429    628    445       N  
ATOM   7250  N   GLY C 944     -76.562  16.780  -8.217  1.00 32.56           N  
ANISOU 7250  N   GLY C 944     4792   3877   3704    492    427    382       N  
ATOM   7251  CA  GLY C 944     -77.151  17.918  -7.535  1.00 34.43           C  
ANISOU 7251  CA  GLY C 944     4984   4158   3938    480    411    372       C  
ATOM   7252  C   GLY C 944     -76.786  19.296  -8.089  1.00 33.32           C  
ANISOU 7252  C   GLY C 944     4777   4069   3814    453    355    323       C  
ATOM   7253  O   GLY C 944     -77.271  20.290  -7.559  1.00 34.74           O  
ANISOU 7253  O   GLY C 944     4925   4280   3993    443    344    312       O  
ATOM   7254  N   LYS C 945     -75.899  19.356  -9.088  1.00 30.48           N  
ANISOU 7254  N   LYS C 945     4401   3716   3465    445    323    295       N  
ATOM   7255  CA  LYS C 945     -75.586  20.618  -9.775  1.00 29.63           C  
ANISOU 7255  CA  LYS C 945     4235   3645   3379    410    277    251       C  
ATOM   7256  C   LYS C 945     -76.299  20.690 -11.108  1.00 26.96           C  
ANISOU 7256  C   LYS C 945     3880   3270   3094    336    277    243       C  
ATOM   7257  O   LYS C 945     -76.390  19.706 -11.810  1.00 25.55           O  
ANISOU 7257  O   LYS C 945     3730   3047   2929    318    296    254       O  
ATOM   7258  CB  LYS C 945     -74.096  20.744 -10.011  1.00 28.80           C  
ANISOU 7258  CB  LYS C 945     4113   3582   3246    449    242    225       C  
ATOM   7259  CG  LYS C 945     -73.285  20.689  -8.744  1.00 28.97           C  
ANISOU 7259  CG  LYS C 945     4142   3657   3207    526    236    228       C  
ATOM   7260  CD  LYS C 945     -73.454  21.948  -7.931  1.00 30.66           C  
ANISOU 7260  CD  LYS C 945     4319   3919   3409    522    216    202       C  
ATOM   7261  CE  LYS C 945     -72.456  22.002  -6.794  1.00 32.65           C  
ANISOU 7261  CE  LYS C 945     4568   4243   3596    596    199    192       C  
ATOM   7262  NZ  LYS C 945     -72.635  23.242  -5.999  1.00 34.62           N  
ANISOU 7262  NZ  LYS C 945     4786   4537   3832    587    181    159       N  
ATOM   7263  N   HIS C 946     -76.802  21.868 -11.464  1.00 25.64           N  
ANISOU 7263  N   HIS C 946     3667   3121   2952    295    258    222       N  
ATOM   7264  CA  HIS C 946     -77.506  22.000 -12.730  1.00 23.87           C  
ANISOU 7264  CA  HIS C 946     3422   2874   2773    231    257    215       C  
ATOM   7265  C   HIS C 946     -76.856  22.902 -13.750  1.00 22.14           C  
ANISOU 7265  C   HIS C 946     3163   2677   2571    212    220    182       C  
ATOM   7266  O   HIS C 946     -77.340  23.031 -14.875  1.00 21.67           O  
ANISOU 7266  O   HIS C 946     3085   2606   2543    166    216    176       O  
ATOM   7267  CB  HIS C 946     -78.887  22.469 -12.403  1.00 24.78           C  
ANISOU 7267  CB  HIS C 946     3521   2988   2906    200    276    230       C  
ATOM   7268  CG  HIS C 946     -79.497  21.679 -11.302  1.00 27.69           C  
ANISOU 7268  CG  HIS C 946     3927   3339   3256    220    316    264       C  
ATOM   7269  ND1 HIS C 946     -79.529  22.127 -10.001  1.00 29.72           N  
ANISOU 7269  ND1 HIS C 946     4188   3622   3483    263    322    272       N  
ATOM   7270  CD2 HIS C 946     -79.998  20.426 -11.284  1.00 27.90           C  
ANISOU 7270  CD2 HIS C 946     3993   3322   3287    205    353    291       C  
ATOM   7271  CE1 HIS C 946     -80.051  21.192  -9.226  1.00 29.12           C  
ANISOU 7271  CE1 HIS C 946     4150   3521   3392    278    363    308       C  
ATOM   7272  NE2 HIS C 946     -80.343  20.152  -9.984  1.00 30.91           N  
ANISOU 7272  NE2 HIS C 946     4400   3703   3642    241    384    320       N  
ATOM   7273  N   SER C 947     -75.814  23.604 -13.327  1.00 20.94           N  
ANISOU 7273  N   SER C 947     2996   2564   2397    246    194    159       N  
ATOM   7274  CA  SER C 947     -75.155  24.553 -14.175  1.00 20.33           C  
ANISOU 7274  CA  SER C 947     2882   2507   2335    226    165    127       C  
ATOM   7275  C   SER C 947     -73.765  24.830 -13.673  1.00 20.03           C  
ANISOU 7275  C   SER C 947     2835   2512   2265    266    141    102       C  
ATOM   7276  O   SER C 947     -73.415  24.494 -12.558  1.00 21.00           O  
ANISOU 7276  O   SER C 947     2973   2655   2349    311    144    107       O  
ATOM   7277  CB  SER C 947     -75.953  25.863 -14.212  1.00 20.45           C  
ANISOU 7277  CB  SER C 947     2869   2529   2373    196    164    119       C  
ATOM   7278  OG  SER C 947     -76.020  26.455 -12.951  1.00 20.41           O  
ANISOU 7278  OG  SER C 947     2865   2544   2344    223    168    113       O  
ATOM   7279  N   VAL C 948     -72.979  25.479 -14.502  1.00 20.62           N  
ANISOU 7279  N   VAL C 948     2879   2605   2352    248    118     74       N  
ATOM   7280  CA  VAL C 948     -71.702  26.014 -14.083  1.00 20.96           C  
ANISOU 7280  CA  VAL C 948     2899   2698   2368    271     93     42       C  
ATOM   7281  C   VAL C 948     -71.766  27.539 -14.036  1.00 20.64           C  
ANISOU 7281  C   VAL C 948     2828   2669   2344    237     85     11       C  
ATOM   7282  O   VAL C 948     -72.383  28.179 -14.897  1.00 20.86           O  
ANISOU 7282  O   VAL C 948     2847   2670   2410    197     91     13       O  
ATOM   7283  CB  VAL C 948     -70.568  25.589 -15.043  1.00 21.41           C  
ANISOU 7283  CB  VAL C 948     2943   2771   2423    276     76     31       C  
ATOM   7284  CG1 VAL C 948     -69.309  26.396 -14.789  1.00 21.37           C  
ANISOU 7284  CG1 VAL C 948     2898   2824   2396    282     50     -8       C  
ATOM   7285  CG2 VAL C 948     -70.261  24.113 -14.875  1.00 22.10           C  
ANISOU 7285  CG2 VAL C 948     3066   2850   2482    324     87     58       C  
ATOM   7286  N   LYS C 949     -71.154  28.111 -13.003  1.00 21.75           N  
ANISOU 7286  N   LYS C 949     2958   2852   2453    256     73    -17       N  
ATOM   7287  CA  LYS C 949     -70.910  29.530 -12.937  1.00 21.24           C  
ANISOU 7287  CA  LYS C 949     2869   2801   2401    223     65    -57       C  
ATOM   7288  C   LYS C 949     -69.419  29.737 -12.911  1.00 22.18           C  
ANISOU 7288  C   LYS C 949     2956   2976   2496    227     39    -96       C  
ATOM   7289  O   LYS C 949     -68.755  29.327 -11.968  1.00 21.99           O  
ANISOU 7289  O   LYS C 949     2928   3002   2425    267     26   -108       O  
ATOM   7290  CB  LYS C 949     -71.503  30.153 -11.708  1.00 22.81           C  
ANISOU 7290  CB  LYS C 949     3080   3004   2582    233     75    -66       C  
ATOM   7291  CG  LYS C 949     -71.224  31.666 -11.600  1.00 23.98           C  
ANISOU 7291  CG  LYS C 949     3211   3158   2741    196     73   -113       C  
ATOM   7292  CD  LYS C 949     -71.836  32.258 -10.357  1.00 24.91           C  
ANISOU 7292  CD  LYS C 949     3347   3279   2839    210     85   -125       C  
ATOM   7293  CE  LYS C 949     -71.540  33.747 -10.283  1.00 27.61           C  
ANISOU 7293  CE  LYS C 949     3681   3617   3193    170     88   -176       C  
ATOM   7294  NZ  LYS C 949     -71.965  34.312  -8.970  1.00 29.03           N  
ANISOU 7294  NZ  LYS C 949     3879   3807   3344    187     97   -197       N  
ATOM   7295  N   GLY C 950     -68.891  30.393 -13.952  1.00 21.06           N  
ANISOU 7295  N   GLY C 950     2788   2829   2383    186     34   -116       N  
ATOM   7296  CA  GLY C 950     -67.518  30.834 -13.942  1.00 22.55           C  
ANISOU 7296  CA  GLY C 950     2940   3074   2554    175     12   -160       C  
ATOM   7297  C   GLY C 950     -67.452  32.113 -13.148  1.00 24.14           C  
ANISOU 7297  C   GLY C 950     3132   3288   2752    145     13   -206       C  
ATOM   7298  O   GLY C 950     -68.142  33.073 -13.464  1.00 26.18           O  
ANISOU 7298  O   GLY C 950     3403   3498   3047    108     33   -209       O  
ATOM   7299  N   LEU C 951     -66.628  32.137 -12.115  1.00 24.90           N  
ANISOU 7299  N   LEU C 951     3208   3452   2802    164     -7   -242       N  
ATOM   7300  CA  LEU C 951     -66.611  33.267 -11.159  1.00 25.89           C  
ANISOU 7300  CA  LEU C 951     3331   3593   2915    139     -6   -292       C  
ATOM   7301  C   LEU C 951     -65.730  34.424 -11.607  1.00 26.31           C  
ANISOU 7301  C   LEU C 951     3351   3659   2987     74     -8   -348       C  
ATOM   7302  O   LEU C 951     -64.516  34.258 -11.729  1.00 25.56           O  
ANISOU 7302  O   LEU C 951     3212   3630   2870     69    -31   -376       O  
ATOM   7303  CB  LEU C 951     -66.091  32.785  -9.811  1.00 26.16           C  
ANISOU 7303  CB  LEU C 951     3353   3703   2881    188    -28   -312       C  
ATOM   7304  CG  LEU C 951     -66.958  31.726  -9.168  1.00 27.43           C  
ANISOU 7304  CG  LEU C 951     3552   3850   3019    252    -18   -258       C  
ATOM   7305  CD1 LEU C 951     -66.374  31.289  -7.827  1.00 29.77           C  
ANISOU 7305  CD1 LEU C 951     3838   4229   3243    308    -38   -276       C  
ATOM   7306  CD2 LEU C 951     -68.350  32.253  -8.963  1.00 26.06           C  
ANISOU 7306  CD2 LEU C 951     3419   3607   2876    237     11   -240       C  
ATOM   7307  N   GLY C 952     -66.344  35.571 -11.902  1.00 25.44           N  
ANISOU 7307  N   GLY C 952     3262   3486   2918     26     19   -360       N  
ATOM   7308  CA  GLY C 952     -65.572  36.761 -12.286  1.00 28.57           C  
ANISOU 7308  CA  GLY C 952     3637   3882   3337    -42     26   -414       C  
ATOM   7309  C   GLY C 952     -65.017  37.547 -11.110  1.00 31.15           C  
ANISOU 7309  C   GLY C 952     3953   4254   3630    -68     18   -485       C  
ATOM   7310  O   GLY C 952     -65.485  37.384  -9.993  1.00 29.68           O  
ANISOU 7310  O   GLY C 952     3785   4085   3409    -32     12   -490       O  
ATOM   7311  N   LYS C 953     -64.040  38.416 -11.377  1.00 35.18           N  
ANISOU 7311  N   LYS C 953     4432   4784   4151   -133     19   -542       N  
ATOM   7312  CA  LYS C 953     -63.557  39.394 -10.392  1.00 38.97           C  
ANISOU 7312  CA  LYS C 953     4904   5295   4607   -178     18   -621       C  
ATOM   7313  C   LYS C 953     -64.578  40.507 -10.136  1.00 36.33           C  
ANISOU 7313  C   LYS C 953     4631   4870   4304   -204     60   -631       C  
ATOM   7314  O   LYS C 953     -64.597  41.092  -9.067  1.00 40.22           O  
ANISOU 7314  O   LYS C 953     5135   5377   4768   -217     60   -684       O  
ATOM   7315  CB  LYS C 953     -62.252  40.039 -10.849  1.00 45.09           C  
ANISOU 7315  CB  LYS C 953     5630   6111   5392   -252     14   -681       C  
ATOM   7316  CG  LYS C 953     -61.115  39.047 -10.974  1.00 52.16           C  
ANISOU 7316  CG  LYS C 953     6458   7113   6248   -226    -27   -681       C  
ATOM   7317  CD  LYS C 953     -59.807  39.712 -11.386  1.00 59.08           C  
ANISOU 7317  CD  LYS C 953     7277   8041   7131   -303    -30   -743       C  
ATOM   7318  CE  LYS C 953     -58.706  38.700 -11.647  1.00 63.39           C  
ANISOU 7318  CE  LYS C 953     7753   8694   7639   -269    -67   -734       C  
ATOM   7319  NZ  LYS C 953     -57.939  38.352 -10.418  1.00 67.71           N  
ANISOU 7319  NZ  LYS C 953     8249   9367   8110   -242   -110   -784       N  
ATOM   7320  N   THR C 954     -65.414  40.784 -11.122  1.00 32.21           N  
ANISOU 7320  N   THR C 954     4145   4258   3834   -207     94   -580       N  
ATOM   7321  CA  THR C 954     -66.427  41.793 -11.023  1.00 31.97           C  
ANISOU 7321  CA  THR C 954     4174   4140   3834   -219    138   -578       C  
ATOM   7322  C   THR C 954     -67.779  41.125 -11.213  1.00 34.12           C  
ANISOU 7322  C   THR C 954     4478   4372   4116   -154    147   -499       C  
ATOM   7323  O   THR C 954     -67.953  40.267 -12.090  1.00 37.80           O  
ANISOU 7323  O   THR C 954     4929   4837   4596   -127    138   -443       O  
ATOM   7324  CB  THR C 954     -66.200  42.874 -12.087  1.00 31.76           C  
ANISOU 7324  CB  THR C 954     4161   4045   3861   -283    179   -587       C  
ATOM   7325  OG1 THR C 954     -64.912  43.488 -11.881  1.00 30.92           O  
ANISOU 7325  OG1 THR C 954     4021   3979   3747   -355    173   -666       O  
ATOM   7326  CG2 THR C 954     -67.300  43.952 -12.061  1.00 31.49           C  
ANISOU 7326  CG2 THR C 954     4195   3913   3858   -286    232   -577       C  
ATOM   7327  N   THR C 955     -68.731  41.493 -10.367  1.00 32.79           N  
ANISOU 7327  N   THR C 955     4350   4173   3936   -128    166   -498       N  
ATOM   7328  CA  THR C 955     -70.072  40.954 -10.407  1.00 32.45           C  
ANISOU 7328  CA  THR C 955     4334   4098   3899    -70    178   -429       C  
ATOM   7329  C   THR C 955     -71.069  42.119 -10.284  1.00 33.16           C  
ANISOU 7329  C   THR C 955     4477   4110   4011    -73    226   -427       C  
ATOM   7330  O   THR C 955     -70.745  43.089  -9.663  1.00 32.56           O  
ANISOU 7330  O   THR C 955     4422   4021   3929   -106    242   -487       O  
ATOM   7331  CB  THR C 955     -70.277  39.928  -9.280  1.00 32.09           C  
ANISOU 7331  CB  THR C 955     4280   4111   3801    -16    148   -419       C  
ATOM   7332  OG1 THR C 955     -71.541  39.295  -9.431  1.00 32.87           O  
ANISOU 7332  OG1 THR C 955     4398   4181   3909     32    161   -350       O  
ATOM   7333  CG2 THR C 955     -70.223  40.565  -7.878  1.00 32.87           C  
ANISOU 7333  CG2 THR C 955     4398   4232   3861    -15    150   -477       C  
ATOM   7334  N   PRO C 956     -72.287  42.002 -10.855  1.00 33.78           N  
ANISOU 7334  N   PRO C 956     4577   4144   4115    -37    250   -361       N  
ATOM   7335  CA  PRO C 956     -73.304  42.980 -10.560  1.00 32.55           C  
ANISOU 7335  CA  PRO C 956     4470   3929   3970    -22    295   -354       C  
ATOM   7336  C   PRO C 956     -73.620  43.013  -9.082  1.00 32.03           C  
ANISOU 7336  C   PRO C 956     4423   3886   3861      5    291   -384       C  
ATOM   7337  O   PRO C 956     -73.682  41.969  -8.449  1.00 31.60           O  
ANISOU 7337  O   PRO C 956     4347   3887   3772     39    260   -369       O  
ATOM   7338  CB  PRO C 956     -74.518  42.473 -11.343  1.00 34.63           C  
ANISOU 7338  CB  PRO C 956     4733   4172   4253     22    307   -273       C  
ATOM   7339  CG  PRO C 956     -73.915  41.686 -12.461  1.00 33.71           C  
ANISOU 7339  CG  PRO C 956     4577   4077   4154      5    281   -250       C  
ATOM   7340  CD  PRO C 956     -72.798  40.967 -11.776  1.00 33.83           C  
ANISOU 7340  CD  PRO C 956     4562   4157   4136     -8    238   -292       C  
ATOM   7341  N   ASP C 957     -73.787  44.213  -8.541  1.00 31.94           N  
ANISOU 7341  N   ASP C 957     4455   3831   3849     -9    326   -426       N  
ATOM   7342  CA  ASP C 957     -74.047  44.402  -7.131  1.00 33.67           C  
ANISOU 7342  CA  ASP C 957     4697   4070   4025     14    327   -462       C  
ATOM   7343  C   ASP C 957     -75.273  43.611  -6.704  1.00 33.68           C  
ANISOU 7343  C   ASP C 957     4701   4088   4008     84    327   -398       C  
ATOM   7344  O   ASP C 957     -76.380  43.951  -7.077  1.00 34.86           O  
ANISOU 7344  O   ASP C 957     4875   4191   4179    114    363   -349       O  
ATOM   7345  CB  ASP C 957     -74.247  45.873  -6.873  1.00 35.78           C  
ANISOU 7345  CB  ASP C 957     5022   4267   4305     -9    377   -506       C  
ATOM   7346  CG  ASP C 957     -74.381  46.213  -5.401  1.00 38.36           C  
ANISOU 7346  CG  ASP C 957     5377   4614   4584      8    379   -559       C  
ATOM   7347  OD1 ASP C 957     -74.575  45.311  -4.557  1.00 40.42           O  
ANISOU 7347  OD1 ASP C 957     5616   4940   4802     50    347   -546       O  
ATOM   7348  OD2 ASP C 957     -74.256  47.413  -5.098  1.00 40.37           O  
ANISOU 7348  OD2 ASP C 957     5680   4816   4844    -24    416   -615       O  
ATOM   7349  N   PRO C 958     -75.080  42.563  -5.893  1.00 36.79           N  
ANISOU 7349  N   PRO C 958     5068   4551   4359    111    290   -396       N  
ATOM   7350  CA  PRO C 958     -76.211  41.735  -5.421  1.00 40.11           C  
ANISOU 7350  CA  PRO C 958     5490   4989   4762    173    293   -335       C  
ATOM   7351  C   PRO C 958     -77.331  42.497  -4.713  1.00 42.11           C  
ANISOU 7351  C   PRO C 958     5787   5208   5004    209    335   -328       C  
ATOM   7352  O   PRO C 958     -78.483  42.061  -4.763  1.00 45.51           O  
ANISOU 7352  O   PRO C 958     6218   5635   5439    252    352   -265       O  
ATOM   7353  CB  PRO C 958     -75.570  40.778  -4.431  1.00 40.44           C  
ANISOU 7353  CB  PRO C 958     5508   5106   4750    192    254   -354       C  
ATOM   7354  CG  PRO C 958     -74.116  40.786  -4.755  1.00 40.27           C  
ANISOU 7354  CG  PRO C 958     5456   5117   4726    145    221   -406       C  
ATOM   7355  CD  PRO C 958     -73.803  42.139  -5.301  1.00 37.60           C  
ANISOU 7355  CD  PRO C 958     5139   4722   4424     90    247   -452       C  
ATOM   7356  N   SER C 959     -77.023  43.616  -4.065  1.00 39.89           N  
ANISOU 7356  N   SER C 959     5541   4904   4709    191    354   -393       N  
ATOM   7357  CA  SER C 959     -78.054  44.347  -3.341  1.00 40.54           C  
ANISOU 7357  CA  SER C 959     5670   4955   4778    231    395   -390       C  
ATOM   7358  C   SER C 959     -79.002  45.080  -4.308  1.00 41.00           C  
ANISOU 7358  C   SER C 959     5753   4941   4882    243    443   -342       C  
ATOM   7359  O   SER C 959     -80.112  45.461  -3.907  1.00 44.48           O  
ANISOU 7359  O   SER C 959     6224   5362   5315    292    480   -313       O  
ATOM   7360  CB  SER C 959     -77.424  45.289  -2.330  1.00 43.55           C  
ANISOU 7360  CB  SER C 959     6087   5334   5127    207    402   -479       C  
ATOM   7361  OG  SER C 959     -76.859  46.412  -2.969  1.00 49.38           O  
ANISOU 7361  OG  SER C 959     6852   6010   5902    151    426   -526       O  
ATOM   7362  N   ALA C 960     -78.598  45.239  -5.577  1.00 34.89           N  
ANISOU 7362  N   ALA C 960     4967   4137   4153    206    444   -329       N  
ATOM   7363  CA  ALA C 960     -79.472  45.808  -6.598  1.00 33.87           C  
ANISOU 7363  CA  ALA C 960     4855   3952   4064    225    486   -276       C  
ATOM   7364  C   ALA C 960     -80.203  44.771  -7.467  1.00 31.16           C  
ANISOU 7364  C   ALA C 960     4465   3639   3737    251    471   -195       C  
ATOM   7365  O   ALA C 960     -80.960  45.137  -8.343  1.00 30.46           O  
ANISOU 7365  O   ALA C 960     4381   3520   3674    272    500   -146       O  
ATOM   7366  CB  ALA C 960     -78.682  46.752  -7.489  1.00 36.22           C  
ANISOU 7366  CB  ALA C 960     5173   4192   4398    172    506   -308       C  
ATOM   7367  N   ASN C 961     -80.015  43.494  -7.206  1.00 30.18           N  
ANISOU 7367  N   ASN C 961     4299   3574   3594    253    428   -180       N  
ATOM   7368  CA  ASN C 961     -80.789  42.467  -7.871  1.00 32.70           C  
ANISOU 7368  CA  ASN C 961     4580   3921   3925    274    417   -110       C  
ATOM   7369  C   ASN C 961     -82.255  42.661  -7.624  1.00 30.33           C  
ANISOU 7369  C   ASN C 961     4288   3617   3618    327    453    -61       C  
ATOM   7370  O   ASN C 961     -82.646  43.055  -6.517  1.00 31.01           O  
ANISOU 7370  O   ASN C 961     4403   3704   3675    358    473    -77       O  
ATOM   7371  CB  ASN C 961     -80.391  41.080  -7.381  1.00 37.65           C  
ANISOU 7371  CB  ASN C 961     5174   4604   4526    272    375   -106       C  
ATOM   7372  CG  ASN C 961     -81.151  40.005  -8.093  1.00 46.72           C  
ANISOU 7372  CG  ASN C 961     6288   5774   5689    283    368    -41       C  
ATOM   7373  OD1 ASN C 961     -80.877  39.720  -9.265  1.00 55.89           O  
ANISOU 7373  OD1 ASN C 961     7426   6929   6879    257    355    -25       O  
ATOM   7374  ND2 ASN C 961     -82.145  39.422  -7.423  1.00 51.49           N  
ANISOU 7374  ND2 ASN C 961     6887   6403   6274    319    378     -4       N  
ATOM   7375  N   ILE C 962     -83.082  42.429  -8.643  1.00 27.29           N  
ANISOU 7375  N   ILE C 962     3877   3234   3256    340    463     -2       N  
ATOM   7376  CA  ILE C 962     -84.517  42.452  -8.427  1.00 27.78           C  
ANISOU 7376  CA  ILE C 962     3935   3313   3310    391    494     50       C  
ATOM   7377  C   ILE C 962     -85.123  41.122  -8.860  1.00 27.78           C  
ANISOU 7377  C   ILE C 962     3881   3362   3312    389    471    101       C  
ATOM   7378  O   ILE C 962     -84.561  40.453  -9.696  1.00 27.75           O  
ANISOU 7378  O   ILE C 962     3851   3365   3326    353    442    104       O  
ATOM   7379  CB  ILE C 962     -85.209  43.604  -9.148  1.00 28.77           C  
ANISOU 7379  CB  ILE C 962     4079   3401   3453    421    538     75       C  
ATOM   7380  CG1 ILE C 962     -85.125  43.456 -10.656  1.00 29.64           C  
ANISOU 7380  CG1 ILE C 962     4159   3509   3594    401    528    106       C  
ATOM   7381  CG2 ILE C 962     -84.655  44.939  -8.650  1.00 28.99           C  
ANISOU 7381  CG2 ILE C 962     4170   3367   3477    421    569     22       C  
ATOM   7382  CD1 ILE C 962     -86.045  44.399 -11.375  1.00 31.71           C  
ANISOU 7382  CD1 ILE C 962     4430   3752   3865    447    573    148       C  
ATOM   7383  N   SER C 963     -86.263  40.762  -8.280  1.00 25.87           N  
ANISOU 7383  N   SER C 963     3625   3152   3051    425    489    139       N  
ATOM   7384  CA  SER C 963     -86.981  39.561  -8.658  1.00 25.73           C  
ANISOU 7384  CA  SER C 963     3558   3179   3037    417    477    186       C  
ATOM   7385  C   SER C 963     -88.279  39.920  -9.408  1.00 27.34           C  
ANISOU 7385  C   SER C 963     3732   3404   3251    446    505    238       C  
ATOM   7386  O   SER C 963     -89.085  40.739  -8.944  1.00 26.39           O  
ANISOU 7386  O   SER C 963     3627   3284   3117    494    542    253       O  
ATOM   7387  CB  SER C 963     -87.279  38.707  -7.438  1.00 24.82           C  
ANISOU 7387  CB  SER C 963     3442   3095   2892    429    476    193       C  
ATOM   7388  OG  SER C 963     -88.298  37.760  -7.744  1.00 24.17           O  
ANISOU 7388  OG  SER C 963     3315   3052   2814    426    481    244       O  
ATOM   7389  N   LEU C 964     -88.435  39.328 -10.588  1.00 27.11           N  
ANISOU 7389  N   LEU C 964     3661   3395   3243    419    487    263       N  
ATOM   7390  CA  LEU C 964     -89.496  39.665 -11.510  1.00 29.59           C  
ANISOU 7390  CA  LEU C 964     3940   3739   3564    442    506    308       C  
ATOM   7391  C   LEU C 964     -90.178  38.378 -11.957  1.00 29.81           C  
ANISOU 7391  C   LEU C 964     3909   3823   3594    412    488    340       C  
ATOM   7392  O   LEU C 964     -89.570  37.513 -12.598  1.00 30.92           O  
ANISOU 7392  O   LEU C 964     4035   3963   3750    364    456    329       O  
ATOM   7393  CB  LEU C 964     -88.818  40.450 -12.637  1.00 31.34           C  
ANISOU 7393  CB  LEU C 964     4176   3925   3808    435    503    296       C  
ATOM   7394  CG  LEU C 964     -89.436  41.535 -13.494  1.00 36.31           C  
ANISOU 7394  CG  LEU C 964     4804   4552   4441    479    534    327       C  
ATOM   7395  CD1 LEU C 964     -89.862  42.711 -12.605  1.00 35.62           C  
ANISOU 7395  CD1 LEU C 964     4763   4434   4336    537    581    326       C  
ATOM   7396  CD2 LEU C 964     -88.455  42.046 -14.563  1.00 37.47           C  
ANISOU 7396  CD2 LEU C 964     4970   4656   4611    457    526    310       C  
ATOM   7397  N   ASP C 965     -91.415  38.194 -11.523  1.00 30.83           N  
ANISOU 7397  N   ASP C 965     4007   3999   3707    437    511    375       N  
ATOM   7398  CA  ASP C 965     -92.141  36.970 -11.840  1.00 33.66           C  
ANISOU 7398  CA  ASP C 965     4310   4412   4068    401    500    401       C  
ATOM   7399  C   ASP C 965     -91.297  35.707 -11.451  1.00 30.31           C  
ANISOU 7399  C   ASP C 965     3901   3966   3650    348    473    377       C  
ATOM   7400  O   ASP C 965     -91.273  34.717 -12.157  1.00 29.34           O  
ANISOU 7400  O   ASP C 965     3750   3858   3540    301    453    380       O  
ATOM   7401  CB  ASP C 965     -92.486  36.949 -13.344  1.00 37.14           C  
ANISOU 7401  CB  ASP C 965     4703   4887   4522    386    487    419       C  
ATOM   7402  CG  ASP C 965     -93.657  35.986 -13.702  1.00 43.07           C  
ANISOU 7402  CG  ASP C 965     5384   5713   5268    357    487    450       C  
ATOM   7403  OD1 ASP C 965     -94.087  35.981 -14.885  1.00 56.08           O  
ANISOU 7403  OD1 ASP C 965     6985   7405   6920    348    476    465       O  
ATOM   7404  OD2 ASP C 965     -94.160  35.227 -12.853  1.00 44.63           O  
ANISOU 7404  OD2 ASP C 965     5570   5929   5458    341    499    459       O  
ATOM   7405  N   GLY C 966     -90.637  35.750 -10.301  1.00 28.85           N  
ANISOU 7405  N   GLY C 966     3763   3748   3451    361    475    353       N  
ATOM   7406  CA  GLY C 966     -89.882  34.604  -9.797  1.00 29.09           C  
ANISOU 7406  CA  GLY C 966     3812   3763   3480    328    456    336       C  
ATOM   7407  C   GLY C 966     -88.498  34.449 -10.430  1.00 27.65           C  
ANISOU 7407  C   GLY C 966     3650   3544   3312    298    420    300       C  
ATOM   7408  O   GLY C 966     -87.792  33.549 -10.100  1.00 31.18           O  
ANISOU 7408  O   GLY C 966     4113   3979   3755    278    403    287       O  
ATOM   7409  N   VAL C 967     -88.073  35.389 -11.258  1.00 27.23           N  
ANISOU 7409  N   VAL C 967     3601   3473   3273    302    412    285       N  
ATOM   7410  CA  VAL C 967     -86.744  35.361 -11.851  1.00 25.78           C  
ANISOU 7410  CA  VAL C 967     3434   3258   3103    276    382    251       C  
ATOM   7411  C   VAL C 967     -85.867  36.546 -11.387  1.00 25.90           C  
ANISOU 7411  C   VAL C 967     3490   3238   3114    295    385    212       C  
ATOM   7412  O   VAL C 967     -86.298  37.691 -11.358  1.00 25.69           O  
ANISOU 7412  O   VAL C 967     3475   3199   3086    325    411    215       O  
ATOM   7413  CB  VAL C 967     -86.887  35.450 -13.372  1.00 24.85           C  
ANISOU 7413  CB  VAL C 967     3285   3149   3008    255    372    264       C  
ATOM   7414  CG1 VAL C 967     -85.555  35.364 -14.067  1.00 24.99           C  
ANISOU 7414  CG1 VAL C 967     3315   3139   3040    228    343    232       C  
ATOM   7415  CG2 VAL C 967     -87.878  34.414 -13.862  1.00 24.96           C  
ANISOU 7415  CG2 VAL C 967     3254   3204   3025    232    371    296       C  
ATOM   7416  N   ASP C 968     -84.636  36.271 -11.021  1.00 26.68           N  
ANISOU 7416  N   ASP C 968     3611   3321   3207    278    361    174       N  
ATOM   7417  CA  ASP C 968     -83.723  37.334 -10.682  1.00 27.37           C  
ANISOU 7417  CA  ASP C 968     3730   3378   3290    283    362    130       C  
ATOM   7418  C   ASP C 968     -83.179  38.062 -11.924  1.00 28.06           C  
ANISOU 7418  C   ASP C 968     3816   3441   3406    261    358    119       C  
ATOM   7419  O   ASP C 968     -82.811  37.439 -12.912  1.00 26.24           O  
ANISOU 7419  O   ASP C 968     3562   3215   3191    234    337    127       O  
ATOM   7420  CB  ASP C 968     -82.568  36.753  -9.887  1.00 30.99           C  
ANISOU 7420  CB  ASP C 968     4203   3843   3728    272    335     92       C  
ATOM   7421  CG  ASP C 968     -82.983  36.273  -8.498  1.00 36.34           C  
ANISOU 7421  CG  ASP C 968     4895   4543   4371    302    344     98       C  
ATOM   7422  OD1 ASP C 968     -83.944  36.799  -7.905  1.00 40.07           O  
ANISOU 7422  OD1 ASP C 968     5375   5017   4832    332    374    114       O  
ATOM   7423  OD2 ASP C 968     -82.320  35.357  -7.979  1.00 44.26           O  
ANISOU 7423  OD2 ASP C 968     5899   5563   5353    300    323     89       O  
ATOM   7424  N   VAL C 969     -83.124  39.389 -11.843  1.00 28.09           N  
ANISOU 7424  N   VAL C 969     3848   3411   3414    275    384    101       N  
ATOM   7425  CA  VAL C 969     -82.467  40.212 -12.822  1.00 27.90           C  
ANISOU 7425  CA  VAL C 969     3833   3353   3414    256    388     86       C  
ATOM   7426  C   VAL C 969     -81.311  40.892 -12.114  1.00 29.25           C  
ANISOU 7426  C   VAL C 969     4038   3496   3578    236    386     25       C  
ATOM   7427  O   VAL C 969     -81.521  41.817 -11.315  1.00 29.67           O  
ANISOU 7427  O   VAL C 969     4128   3525   3621    255    415      4       O  
ATOM   7428  CB  VAL C 969     -83.408  41.270 -13.376  1.00 27.57           C  
ANISOU 7428  CB  VAL C 969     3801   3291   3383    290    430    118       C  
ATOM   7429  CG1 VAL C 969     -82.744  41.985 -14.545  1.00 27.21           C  
ANISOU 7429  CG1 VAL C 969     3765   3211   3364    270    437    112       C  
ATOM   7430  CG2 VAL C 969     -84.714  40.617 -13.825  1.00 27.68           C  
ANISOU 7430  CG2 VAL C 969     3774   3350   3394    314    432    175       C  
ATOM   7431  N   PRO C 970     -80.083  40.441 -12.385  1.00 28.67           N  
ANISOU 7431  N   PRO C 970     3953   3430   3509    197    354     -7       N  
ATOM   7432  CA  PRO C 970     -78.919  41.031 -11.726  1.00 30.15           C  
ANISOU 7432  CA  PRO C 970     4163   3605   3687    170    348    -71       C  
ATOM   7433  C   PRO C 970     -78.463  42.332 -12.399  1.00 30.49           C  
ANISOU 7433  C   PRO C 970     4231   3596   3757    146    377    -94       C  
ATOM   7434  O   PRO C 970     -77.377  42.385 -12.969  1.00 32.69           O  
ANISOU 7434  O   PRO C 970     4499   3871   4050    105    361   -122       O  
ATOM   7435  CB  PRO C 970     -77.851  39.934 -11.879  1.00 28.99           C  
ANISOU 7435  CB  PRO C 970     3985   3497   3534    144    303    -87       C  
ATOM   7436  CG  PRO C 970     -78.178  39.336 -13.201  1.00 29.01           C  
ANISOU 7436  CG  PRO C 970     3961   3502   3561    140    296    -41       C  
ATOM   7437  CD  PRO C 970     -79.683  39.419 -13.361  1.00 28.29           C  
ANISOU 7437  CD  PRO C 970     3869   3405   3474    175    323     11       C  
ATOM   7438  N   LEU C 971     -79.249  43.378 -12.254  1.00 29.08           N  
ANISOU 7438  N   LEU C 971     4089   3376   3584    172    421    -84       N  
ATOM   7439  CA  LEU C 971     -78.998  44.614 -12.941  1.00 31.10           C  
ANISOU 7439  CA  LEU C 971     4377   3573   3866    157    460    -94       C  
ATOM   7440  C   LEU C 971     -78.195  45.650 -12.140  1.00 31.11           C  
ANISOU 7440  C   LEU C 971     4423   3534   3863    124    480   -166       C  
ATOM   7441  O   LEU C 971     -78.055  46.795 -12.552  1.00 31.92           O  
ANISOU 7441  O   LEU C 971     4566   3575   3987    111    523   -178       O  
ATOM   7442  CB  LEU C 971     -80.314  45.226 -13.465  1.00 31.28           C  
ANISOU 7442  CB  LEU C 971     4417   3569   3897    210    504    -36       C  
ATOM   7443  CG  LEU C 971     -81.489  45.342 -12.541  1.00 32.57           C  
ANISOU 7443  CG  LEU C 971     4597   3742   4037    264    526    -15       C  
ATOM   7444  CD1 LEU C 971     -81.138  46.219 -11.364  1.00 34.38           C  
ANISOU 7444  CD1 LEU C 971     4878   3933   4251    259    549    -74       C  
ATOM   7445  CD2 LEU C 971     -82.665  45.902 -13.310  1.00 34.76           C  
ANISOU 7445  CD2 LEU C 971     4880   4005   4324    318    567     47       C  
ATOM   7446  N   GLY C 972     -77.609  45.242 -11.038  1.00 31.84           N  
ANISOU 7446  N   GLY C 972     4509   3663   3927    108    449   -215       N  
ATOM   7447  CA  GLY C 972     -76.679  46.121 -10.324  1.00 32.65           C  
ANISOU 7447  CA  GLY C 972     4642   3740   4021     64    460   -294       C  
ATOM   7448  C   GLY C 972     -75.433  46.496 -11.129  1.00 33.32           C  
ANISOU 7448  C   GLY C 972     4718   3808   4134     -3    457   -331       C  
ATOM   7449  O   GLY C 972     -74.991  45.737 -11.979  1.00 32.28           O  
ANISOU 7449  O   GLY C 972     4543   3707   4014    -16    427   -306       O  
ATOM   7450  N   THR C 973     -74.854  47.659 -10.849  1.00 35.84           N  
ANISOU 7450  N   THR C 973     5079   4078   4462    -47    490   -392       N  
ATOM   7451  CA  THR C 973     -73.556  48.016 -11.430  1.00 35.80           C  
ANISOU 7451  CA  THR C 973     5060   4063   4478   -121    487   -438       C  
ATOM   7452  C   THR C 973     -72.476  47.058 -10.955  1.00 35.38           C  
ANISOU 7452  C   THR C 973     4947   4098   4396   -152    424   -480       C  
ATOM   7453  O   THR C 973     -72.548  46.542  -9.859  1.00 32.71           O  
ANISOU 7453  O   THR C 973     4598   3812   4018   -129    394   -502       O  
ATOM   7454  CB  THR C 973     -73.125  49.474 -11.112  1.00 39.70           C  
ANISOU 7454  CB  THR C 973     5614   4484   4986   -173    540   -505       C  
ATOM   7455  OG1 THR C 973     -73.156  49.695  -9.704  1.00 44.90           O  
ANISOU 7455  OG1 THR C 973     6295   5159   5607   -172    534   -565       O  
ATOM   7456  CG2 THR C 973     -74.044  50.486 -11.779  1.00 40.90           C  
ANISOU 7456  CG2 THR C 973     5830   4541   5170   -141    611   -458       C  
ATOM   7457  N   GLY C 974     -71.449  46.884 -11.771  1.00 37.26           N  
ANISOU 7457  N   GLY C 974     5149   4354   4653   -200    408   -492       N  
ATOM   7458  CA  GLY C 974     -70.330  46.005 -11.455  1.00 39.63           C  
ANISOU 7458  CA  GLY C 974     5389   4743   4927   -226    351   -529       C  
ATOM   7459  C   GLY C 974     -69.464  46.446 -10.287  1.00 41.11           C  
ANISOU 7459  C   GLY C 974     5573   4966   5081   -272    337   -622       C  
ATOM   7460  O   GLY C 974     -68.961  47.563 -10.262  1.00 44.38           O  
ANISOU 7460  O   GLY C 974     6015   5337   5513   -334    371   -680       O  
ATOM   7461  N   ILE C 975     -69.316  45.555  -9.312  1.00 39.79           N  
ANISOU 7461  N   ILE C 975     5373   4881   4864   -240    290   -635       N  
ATOM   7462  CA  ILE C 975     -68.470  45.770  -8.155  1.00 40.56           C  
ANISOU 7462  CA  ILE C 975     5455   5038   4917   -273    266   -721       C  
ATOM   7463  C   ILE C 975     -67.576  44.566  -8.005  1.00 40.34           C  
ANISOU 7463  C   ILE C 975     5356   5118   4852   -260    205   -724       C  
ATOM   7464  O   ILE C 975     -67.754  43.547  -8.682  1.00 38.37           O  
ANISOU 7464  O   ILE C 975     5082   4886   4610   -219    186   -657       O  
ATOM   7465  CB  ILE C 975     -69.276  45.938  -6.845  1.00 43.08           C  
ANISOU 7465  CB  ILE C 975     5813   5358   5197   -230    272   -738       C  
ATOM   7466  CG1 ILE C 975     -69.982  44.644  -6.456  1.00 42.70           C  
ANISOU 7466  CG1 ILE C 975     5748   5360   5118   -146    240   -672       C  
ATOM   7467  CG2 ILE C 975     -70.290  47.084  -6.968  1.00 46.05           C  
ANISOU 7467  CG2 ILE C 975     6264   5626   5606   -226    336   -727       C  
ATOM   7468  CD1 ILE C 975     -70.627  44.671  -5.071  1.00 43.74           C  
ANISOU 7468  CD1 ILE C 975     5907   5511   5201   -101    240   -689       C  
ATOM   7469  N   SER C 976     -66.664  44.660  -7.058  1.00 38.22           N  
ANISOU 7469  N   SER C 976     5059   4926   4538   -289    176   -801       N  
ATOM   7470  CA  SER C 976     -65.724  43.601  -6.802  1.00 39.05           C  
ANISOU 7470  CA  SER C 976     5096   5144   4599   -271    120   -809       C  
ATOM   7471  C   SER C 976     -66.447  42.434  -6.178  1.00 36.37           C  
ANISOU 7471  C   SER C 976     4758   4841   4219   -178     96   -751       C  
ATOM   7472  O   SER C 976     -67.246  42.623  -5.282  1.00 36.41           O  
ANISOU 7472  O   SER C 976     4802   4830   4203   -145    107   -752       O  
ATOM   7473  CB  SER C 976     -64.630  44.087  -5.856  1.00 40.08           C  
ANISOU 7473  CB  SER C 976     5192   5354   4682   -322     96   -912       C  
ATOM   7474  OG  SER C 976     -63.664  43.072  -5.706  1.00 45.68           O  
ANISOU 7474  OG  SER C 976     5830   6180   5346   -299     43   -915       O  
ATOM   7475  N   SER C 977     -66.157  41.227  -6.650  1.00 33.25           N  
ANISOU 7475  N   SER C 977     4324   4493   3816   -138     65   -699       N  
ATOM   7476  CA  SER C 977     -66.777  40.039  -6.108  1.00 33.19           C  
ANISOU 7476  CA  SER C 977     4321   4517   3773    -54     47   -641       C  
ATOM   7477  C   SER C 977     -66.019  39.540  -4.904  1.00 34.12           C  
ANISOU 7477  C   SER C 977     4404   4745   3815    -23      7   -683       C  
ATOM   7478  O   SER C 977     -66.516  38.677  -4.174  1.00 33.32           O  
ANISOU 7478  O   SER C 977     4313   4673   3673     49     -4   -644       O  
ATOM   7479  CB  SER C 977     -66.822  38.925  -7.168  1.00 31.79           C  
ANISOU 7479  CB  SER C 977     4126   4334   3619    -22     38   -567       C  
ATOM   7480  OG  SER C 977     -65.520  38.626  -7.613  1.00 31.72           O  
ANISOU 7480  OG  SER C 977     4062   4391   3599    -46      9   -594       O  
ATOM   7481  N   GLY C 978     -64.787  40.014  -4.747  1.00 35.26           N  
ANISOU 7481  N   GLY C 978     4503   4957   3938    -75    -15   -759       N  
ATOM   7482  CA  GLY C 978     -63.914  39.505  -3.715  1.00 38.83           C  
ANISOU 7482  CA  GLY C 978     4908   5533   4312    -45    -59   -800       C  
ATOM   7483  C   GLY C 978     -63.224  38.206  -4.080  1.00 41.67           C  
ANISOU 7483  C   GLY C 978     5220   5967   4646      9    -92   -756       C  
ATOM   7484  O   GLY C 978     -62.498  37.652  -3.272  1.00 42.73           O  
ANISOU 7484  O   GLY C 978     5313   6212   4710     50   -128   -778       O  
ATOM   7485  N   VAL C 979     -63.443  37.704  -5.294  1.00 43.62           N  
ANISOU 7485  N   VAL C 979     5472   6156   4944     13    -79   -692       N  
ATOM   7486  CA  VAL C 979     -62.754  36.513  -5.781  1.00 46.12           C  
ANISOU 7486  CA  VAL C 979     5749   6532   5241     60   -105   -651       C  
ATOM   7487  C   VAL C 979     -61.527  37.020  -6.549  1.00 46.57           C  
ANISOU 7487  C   VAL C 979     5749   6630   5316     -9   -116   -701       C  
ATOM   7488  O   VAL C 979     -61.669  37.682  -7.562  1.00 43.38           O  
ANISOU 7488  O   VAL C 979     5357   6150   4976    -70    -90   -699       O  
ATOM   7489  CB  VAL C 979     -63.656  35.709  -6.741  1.00 46.80           C  
ANISOU 7489  CB  VAL C 979     5874   6533   5376     95    -82   -561       C  
ATOM   7490  CG1 VAL C 979     -62.873  34.605  -7.440  1.00 47.45           C  
ANISOU 7490  CG1 VAL C 979     5920   6662   5446    132   -102   -525       C  
ATOM   7491  CG2 VAL C 979     -64.839  35.140  -5.985  1.00 45.96           C  
ANISOU 7491  CG2 VAL C 979     5818   6392   5251    159    -68   -511       C  
ATOM   7492  N   ASN C 980     -60.338  36.740  -6.056  1.00 53.32           N  
ANISOU 7492  N   ASN C 980     6540   7609   6112      2   -153   -744       N  
ATOM   7493  CA  ASN C 980     -59.107  37.247  -6.686  1.00 58.20           C  
ANISOU 7493  CA  ASN C 980     7093   8281   6740    -68   -165   -797       C  
ATOM   7494  C   ASN C 980     -58.444  36.205  -7.583  1.00 58.07           C  
ANISOU 7494  C   ASN C 980     7037   8304   6722    -26   -180   -747       C  
ATOM   7495  O   ASN C 980     -57.889  36.551  -8.635  1.00 60.23           O  
ANISOU 7495  O   ASN C 980     7283   8564   7037    -82   -170   -756       O  
ATOM   7496  CB  ASN C 980     -58.117  37.726  -5.597  1.00 59.63           C  
ANISOU 7496  CB  ASN C 980     7214   8588   6853    -95   -198   -890       C  
ATOM   7497  N   ASP C 981     -58.503  34.934  -7.173  1.00 55.73           N  
ANISOU 7497  N   ASP C 981     6743   8055   6375     75   -198   -694       N  
ATOM   7498  CA  ASP C 981     -57.780  33.855  -7.867  1.00 54.72           C  
ANISOU 7498  CA  ASP C 981     6581   7977   6232    129   -213   -650       C  
ATOM   7499  C   ASP C 981     -58.578  33.193  -9.019  1.00 49.21           C  
ANISOU 7499  C   ASP C 981     5936   7168   5593    152   -185   -569       C  
ATOM   7500  O   ASP C 981     -58.950  32.026  -8.931  1.00 45.61           O  
ANISOU 7500  O   ASP C 981     5511   6703   5116    235   -184   -506       O  
ATOM   7501  CB  ASP C 981     -57.375  32.792  -6.840  1.00 59.58           C  
ANISOU 7501  CB  ASP C 981     7177   8701   6760    233   -242   -633       C  
ATOM   7502  CG  ASP C 981     -58.594  32.136  -6.140  1.00 68.87           C  
ANISOU 7502  CG  ASP C 981     8428   9814   7924    305   -226   -575       C  
ATOM   7503  OD1 ASP C 981     -59.609  32.831  -5.864  1.00 65.77           O  
ANISOU 7503  OD1 ASP C 981     8084   9338   7566    266   -204   -582       O  
ATOM   7504  OD2 ASP C 981     -58.515  30.919  -5.838  1.00 78.45           O  
ANISOU 7504  OD2 ASP C 981     9651  11065   9091    403   -232   -521       O  
ATOM   7505  N   THR C 982     -58.857  33.950 -10.071  1.00 40.62           N  
ANISOU 7505  N   THR C 982     4862   5995   4577     77   -159   -571       N  
ATOM   7506  CA  THR C 982     -59.727  33.481 -11.117  1.00 38.36           C  
ANISOU 7506  CA  THR C 982     4626   5605   4344     90   -133   -503       C  
ATOM   7507  C   THR C 982     -59.199  33.867 -12.478  1.00 38.25           C  
ANISOU 7507  C   THR C 982     4587   5569   4379     34   -122   -505       C  
ATOM   7508  O   THR C 982     -58.565  34.893 -12.652  1.00 37.66           O  
ANISOU 7508  O   THR C 982     4476   5514   4320    -40   -118   -560       O  
ATOM   7509  CB  THR C 982     -61.178  34.025 -10.961  1.00 39.74           C  
ANISOU 7509  CB  THR C 982     4868   5671   4561     70   -103   -484       C  
ATOM   7510  OG1 THR C 982     -61.940  33.700 -12.126  1.00 37.04           O  
ANISOU 7510  OG1 THR C 982     4562   5238   4272     70    -79   -425       O  
ATOM   7511  CG2 THR C 982     -61.187  35.540 -10.806  1.00 40.76           C  
ANISOU 7511  CG2 THR C 982     4995   5773   4718    -15    -88   -546       C  
ATOM   7512  N   SER C 983     -59.504  33.035 -13.459  1.00 38.85           N  
ANISOU 7512  N   SER C 983     4685   5599   4479     69   -112   -445       N  
ATOM   7513  CA  SER C 983     -59.156  33.312 -14.833  1.00 37.37           C  
ANISOU 7513  CA  SER C 983     4481   5381   4336     25    -97   -437       C  
ATOM   7514  C   SER C 983     -60.088  34.340 -15.490  1.00 35.75           C  
ANISOU 7514  C   SER C 983     4316   5069   4196    -38    -63   -431       C  
ATOM   7515  O   SER C 983     -59.847  34.714 -16.625  1.00 37.44           O  
ANISOU 7515  O   SER C 983     4521   5255   4450    -78    -46   -425       O  
ATOM   7516  CB  SER C 983     -59.219  32.009 -15.634  1.00 39.75           C  
ANISOU 7516  CB  SER C 983     4798   5670   4635     89    -98   -375       C  
ATOM   7517  OG  SER C 983     -58.461  30.986 -15.007  1.00 45.85           O  
ANISOU 7517  OG  SER C 983     5544   6532   5344    163   -124   -370       O  
ATOM   7518  N   LEU C 984     -61.138  34.799 -14.812  1.00 32.40           N  
ANISOU 7518  N   LEU C 984     3938   4589   3783    -44    -49   -431       N  
ATOM   7519  CA  LEU C 984     -62.186  35.557 -15.480  1.00 29.95           C  
ANISOU 7519  CA  LEU C 984     3674   4177   3530    -81    -14   -409       C  
ATOM   7520  C   LEU C 984     -62.348  36.944 -14.890  1.00 29.35           C  
ANISOU 7520  C   LEU C 984     3610   4074   3469   -140      6   -460       C  
ATOM   7521  O   LEU C 984     -62.423  37.109 -13.664  1.00 28.82           O  
ANISOU 7521  O   LEU C 984     3547   4036   3367   -131     -6   -494       O  
ATOM   7522  CB  LEU C 984     -63.522  34.800 -15.344  1.00 30.45           C  
ANISOU 7522  CB  LEU C 984     3789   4184   3596    -27     -6   -352       C  
ATOM   7523  CG  LEU C 984     -63.712  33.446 -16.073  1.00 29.26           C  
ANISOU 7523  CG  LEU C 984     3646   4028   3442     25    -14   -295       C  
ATOM   7524  CD1 LEU C 984     -64.996  32.788 -15.642  1.00 28.20           C  
ANISOU 7524  CD1 LEU C 984     3560   3848   3306     67     -5   -251       C  
ATOM   7525  CD2 LEU C 984     -63.723  33.642 -17.585  1.00 29.50           C  
ANISOU 7525  CD2 LEU C 984     3675   4017   3518     -4      3   -272       C  
ATOM   7526  N   LEU C 985     -62.460  37.941 -15.750  1.00 29.84           N  
ANISOU 7526  N   LEU C 985     3684   4074   3580   -198     38   -465       N  
ATOM   7527  CA  LEU C 985     -62.819  39.282 -15.312  1.00 30.63           C  
ANISOU 7527  CA  LEU C 985     3813   4122   3701   -251     69   -504       C  
ATOM   7528  C   LEU C 985     -64.278  39.348 -14.866  1.00 29.95           C  
ANISOU 7528  C   LEU C 985     3787   3970   3624   -214     87   -470       C  
ATOM   7529  O   LEU C 985     -64.611  40.003 -13.884  1.00 29.78           O  
ANISOU 7529  O   LEU C 985     3788   3935   3590   -225     96   -505       O  
ATOM   7530  CB  LEU C 985     -62.566  40.308 -16.429  1.00 34.09           C  
ANISOU 7530  CB  LEU C 985     4257   4505   4192   -315    108   -510       C  
ATOM   7531  CG  LEU C 985     -61.100  40.553 -16.865  1.00 36.98           C  
ANISOU 7531  CG  LEU C 985     4563   4931   4556   -371    101   -553       C  
ATOM   7532  CD1 LEU C 985     -61.014  41.551 -18.020  1.00 38.40           C  
ANISOU 7532  CD1 LEU C 985     4758   5041   4790   -430    149   -546       C  
ATOM   7533  CD2 LEU C 985     -60.246  41.047 -15.711  1.00 37.39           C  
ANISOU 7533  CD2 LEU C 985     4581   5051   4574   -415     85   -636       C  
ATOM   7534  N   TYR C 986     -65.156  38.666 -15.581  1.00 28.86           N  
ANISOU 7534  N   TYR C 986     3670   3792   3503   -172     92   -403       N  
ATOM   7535  CA  TYR C 986     -66.605  38.718 -15.298  1.00 27.88           C  
ANISOU 7535  CA  TYR C 986     3595   3609   3389   -139    111   -364       C  
ATOM   7536  C   TYR C 986     -67.197  37.298 -15.232  1.00 26.53           C  
ANISOU 7536  C   TYR C 986     3427   3457   3198    -75     90   -312       C  
ATOM   7537  O   TYR C 986     -66.633  36.349 -15.799  1.00 24.29           O  
ANISOU 7537  O   TYR C 986     3117   3207   2904    -57     68   -293       O  
ATOM   7538  CB  TYR C 986     -67.300  39.568 -16.369  1.00 27.32           C  
ANISOU 7538  CB  TYR C 986     3554   3459   3367   -161    153   -334       C  
ATOM   7539  CG  TYR C 986     -66.546  40.866 -16.620  1.00 29.67           C  
ANISOU 7539  CG  TYR C 986     3851   3733   3689   -227    181   -382       C  
ATOM   7540  CD1 TYR C 986     -66.597  41.911 -15.691  1.00 31.28           C  
ANISOU 7540  CD1 TYR C 986     4082   3914   3890   -258    202   -432       C  
ATOM   7541  CD2 TYR C 986     -65.765  41.040 -17.748  1.00 29.66           C  
ANISOU 7541  CD2 TYR C 986     3826   3732   3712   -261    189   -379       C  
ATOM   7542  CE1 TYR C 986     -65.913  43.094 -15.882  1.00 32.59           C  
ANISOU 7542  CE1 TYR C 986     4252   4050   4078   -326    232   -480       C  
ATOM   7543  CE2 TYR C 986     -65.070  42.221 -17.946  1.00 31.46           C  
ANISOU 7543  CE2 TYR C 986     4055   3935   3962   -328    220   -423       C  
ATOM   7544  CZ  TYR C 986     -65.143  43.244 -17.013  1.00 33.03           C  
ANISOU 7544  CZ  TYR C 986     4283   4105   4160   -363    243   -475       C  
ATOM   7545  OH  TYR C 986     -64.418  44.409 -17.195  1.00 34.97           O  
ANISOU 7545  OH  TYR C 986     4535   4322   4431   -438    278   -524       O  
ATOM   7546  N   ASN C 987     -68.346  37.181 -14.570  1.00 24.73           N  
ANISOU 7546  N   ASN C 987     3233   3202   2964    -43     99   -288       N  
ATOM   7547  CA  ASN C 987     -69.049  35.916 -14.475  1.00 23.80           C  
ANISOU 7547  CA  ASN C 987     3123   3089   2830      8     88   -238       C  
ATOM   7548  C   ASN C 987     -69.439  35.405 -15.846  1.00 23.19           C  
ANISOU 7548  C   ASN C 987     3045   2983   2784     10     94   -191       C  
ATOM   7549  O   ASN C 987     -69.562  36.160 -16.814  1.00 19.86           O  
ANISOU 7549  O   ASN C 987     2625   2526   2397    -20    114   -185       O  
ATOM   7550  CB  ASN C 987     -70.326  36.044 -13.662  1.00 23.87           C  
ANISOU 7550  CB  ASN C 987     3166   3068   2834     34    106   -218       C  
ATOM   7551  CG  ASN C 987     -70.072  36.478 -12.235  1.00 23.90           C  
ANISOU 7551  CG  ASN C 987     3177   3103   2802     40    100   -263       C  
ATOM   7552  OD1 ASN C 987     -69.099  36.105 -11.662  1.00 25.71           O  
ANISOU 7552  OD1 ASN C 987     3383   3392   2996     47     74   -294       O  
ATOM   7553  ND2 ASN C 987     -70.970  37.276 -11.678  1.00 23.83           N  
ANISOU 7553  ND2 ASN C 987     3199   3057   2799     41    126   -266       N  
ATOM   7554  N   GLU C 988     -69.602  34.095 -15.909  1.00 21.79           N  
ANISOU 7554  N   GLU C 988     2867   2823   2590     46     79   -158       N  
ATOM   7555  CA  GLU C 988     -70.373  33.505 -16.957  1.00 21.02           C  
ANISOU 7555  CA  GLU C 988     2777   2692   2515     52     87   -112       C  
ATOM   7556  C   GLU C 988     -71.098  32.298 -16.423  1.00 18.97           C  
ANISOU 7556  C   GLU C 988     2537   2435   2237     90     84    -80       C  
ATOM   7557  O   GLU C 988     -70.757  31.758 -15.390  1.00 20.01           O  
ANISOU 7557  O   GLU C 988     2673   2597   2334    118     72    -89       O  
ATOM   7558  CB  GLU C 988     -69.509  33.171 -18.178  1.00 22.89           C  
ANISOU 7558  CB  GLU C 988     2992   2942   2763     39     76   -111       C  
ATOM   7559  CG  GLU C 988     -68.263  32.380 -17.919  1.00 23.75           C  
ANISOU 7559  CG  GLU C 988     3079   3104   2841     58     51   -130       C  
ATOM   7560  CD  GLU C 988     -67.347  32.350 -19.141  1.00 25.66           C  
ANISOU 7560  CD  GLU C 988     3294   3359   3095     41     45   -134       C  
ATOM   7561  OE1 GLU C 988     -67.250  31.280 -19.780  1.00 26.61           O  
ANISOU 7561  OE1 GLU C 988     3417   3484   3209     64     37   -110       O  
ATOM   7562  OE2 GLU C 988     -66.765  33.401 -19.485  1.00 26.40           O  
ANISOU 7562  OE2 GLU C 988     3369   3456   3206      2     52   -161       O  
ATOM   7563  N   TYR C 989     -72.125  31.904 -17.130  1.00 18.64           N  
ANISOU 7563  N   TYR C 989     2506   2361   2215     88     96    -42       N  
ATOM   7564  CA  TYR C 989     -73.026  30.874 -16.693  1.00 19.09           C  
ANISOU 7564  CA  TYR C 989     2583   2410   2262    112    102    -10       C  
ATOM   7565  C   TYR C 989     -73.227  29.911 -17.846  1.00 19.12           C  
ANISOU 7565  C   TYR C 989     2586   2400   2278    106    100     15       C  
ATOM   7566  O   TYR C 989     -73.465  30.339 -18.982  1.00 18.58           O  
ANISOU 7566  O   TYR C 989     2505   2320   2235     82    103     21       O  
ATOM   7567  CB  TYR C 989     -74.369  31.482 -16.325  1.00 20.13           C  
ANISOU 7567  CB  TYR C 989     2725   2518   2406    109    125      8       C  
ATOM   7568  CG  TYR C 989     -74.312  32.538 -15.241  1.00 21.18           C  
ANISOU 7568  CG  TYR C 989     2865   2656   2528    114    132    -19       C  
ATOM   7569  CD1 TYR C 989     -74.031  33.854 -15.558  1.00 21.20           C  
ANISOU 7569  CD1 TYR C 989     2861   2646   2548     90    140    -43       C  
ATOM   7570  CD2 TYR C 989     -74.550  32.216 -13.927  1.00 20.79           C  
ANISOU 7570  CD2 TYR C 989     2831   2621   2449    142    134    -19       C  
ATOM   7571  CE1 TYR C 989     -73.982  34.823 -14.588  1.00 22.59           C  
ANISOU 7571  CE1 TYR C 989     3049   2820   2713     90    150    -73       C  
ATOM   7572  CE2 TYR C 989     -74.475  33.171 -12.950  1.00 21.90           C  
ANISOU 7572  CE2 TYR C 989     2979   2768   2574    146    140    -48       C  
ATOM   7573  CZ  TYR C 989     -74.217  34.481 -13.290  1.00 23.47           C  
ANISOU 7573  CZ  TYR C 989     3174   2951   2794    118    149    -77       C  
ATOM   7574  OH  TYR C 989     -74.115  35.457 -12.336  1.00 22.86           O  
ANISOU 7574  OH  TYR C 989     3109   2874   2701    117    157   -113       O  
ATOM   7575  N   ILE C 990     -73.136  28.624 -17.555  1.00 18.83           N  
ANISOU 7575  N   ILE C 990     2566   2366   2222    129     97     29       N  
ATOM   7576  CA  ILE C 990     -73.255  27.597 -18.589  1.00 19.06           C  
ANISOU 7576  CA  ILE C 990     2603   2380   2260    122     97     46       C  
ATOM   7577  C   ILE C 990     -74.289  26.528 -18.185  1.00 19.55           C  
ANISOU 7577  C   ILE C 990     2694   2417   2318    127    115     74       C  
ATOM   7578  O   ILE C 990     -74.240  26.001 -17.052  1.00 18.50           O  
ANISOU 7578  O   ILE C 990     2583   2287   2160    157    122     82       O  
ATOM   7579  CB  ILE C 990     -71.894  26.938 -18.864  1.00 19.23           C  
ANISOU 7579  CB  ILE C 990     2624   2422   2262    144     80     32       C  
ATOM   7580  CG1 ILE C 990     -70.832  27.975 -19.226  1.00 19.98           C  
ANISOU 7580  CG1 ILE C 990     2685   2546   2361    132     65      3       C  
ATOM   7581  CG2 ILE C 990     -71.991  25.992 -20.024  1.00 20.01           C  
ANISOU 7581  CG2 ILE C 990     2732   2500   2369    135     82     45       C  
ATOM   7582  CD1 ILE C 990     -70.101  28.555 -18.042  1.00 20.18           C  
ANISOU 7582  CD1 ILE C 990     2699   2606   2361    148     56    -24       C  
ATOM   7583  N   VAL C 991     -75.205  26.219 -19.103  1.00 19.12           N  
ANISOU 7583  N   VAL C 991     2637   2343   2284     97    123     89       N  
ATOM   7584  CA  VAL C 991     -76.077  25.062 -18.963  1.00 19.07           C  
ANISOU 7584  CA  VAL C 991     2656   2313   2277     89    142    111       C  
ATOM   7585  C   VAL C 991     -75.809  24.047 -20.070  1.00 20.45           C  
ANISOU 7585  C   VAL C 991     2843   2470   2456     75    140    108       C  
ATOM   7586  O   VAL C 991     -75.319  24.425 -21.134  1.00 20.17           O  
ANISOU 7586  O   VAL C 991     2788   2446   2429     65    124     95       O  
ATOM   7587  CB  VAL C 991     -77.557  25.450 -18.927  1.00 19.17           C  
ANISOU 7587  CB  VAL C 991     2654   2322   2306     61    158    128       C  
ATOM   7588  CG1 VAL C 991     -77.842  26.297 -17.690  1.00 19.79           C  
ANISOU 7588  CG1 VAL C 991     2730   2413   2377     83    166    132       C  
ATOM   7589  CG2 VAL C 991     -77.988  26.143 -20.168  1.00 18.06           C  
ANISOU 7589  CG2 VAL C 991     2481   2195   2188     33    150    125       C  
ATOM   7590  N   TYR C 992     -76.094  22.777 -19.791  1.00 19.87           N  
ANISOU 7590  N   TYR C 992     2808   2367   2374     77    159    121       N  
ATOM   7591  CA  TYR C 992     -75.696  21.656 -20.623  1.00 22.04           C  
ANISOU 7591  CA  TYR C 992     3111   2618   2647     72    162    116       C  
ATOM   7592  C   TYR C 992     -76.886  20.918 -21.187  1.00 23.50           C  
ANISOU 7592  C   TYR C 992     3306   2776   2848     22    181    121       C  
ATOM   7593  O   TYR C 992     -76.728  19.864 -21.726  1.00 25.41           O  
ANISOU 7593  O   TYR C 992     3580   2986   3087     13    192    115       O  
ATOM   7594  CB  TYR C 992     -74.764  20.685 -19.827  1.00 22.31           C  
ANISOU 7594  CB  TYR C 992     3191   2636   2652    124    173    124       C  
ATOM   7595  CG  TYR C 992     -73.539  21.437 -19.373  1.00 20.73           C  
ANISOU 7595  CG  TYR C 992     2968   2477   2431    168    150    112       C  
ATOM   7596  CD1 TYR C 992     -73.532  22.103 -18.170  1.00 21.28           C  
ANISOU 7596  CD1 TYR C 992     3027   2572   2488    191    147    115       C  
ATOM   7597  CD2 TYR C 992     -72.428  21.565 -20.210  1.00 19.78           C  
ANISOU 7597  CD2 TYR C 992     2831   2378   2306    181    129     94       C  
ATOM   7598  CE1 TYR C 992     -72.431  22.846 -17.766  1.00 22.36           C  
ANISOU 7598  CE1 TYR C 992     3138   2753   2605    222    124     97       C  
ATOM   7599  CE2 TYR C 992     -71.309  22.289 -19.821  1.00 20.08           C  
ANISOU 7599  CE2 TYR C 992     2840   2462   2326    212    107     79       C  
ATOM   7600  CZ  TYR C 992     -71.308  22.930 -18.600  1.00 21.04           C  
ANISOU 7600  CZ  TYR C 992     2951   2609   2434    230    104     78       C  
ATOM   7601  OH  TYR C 992     -70.241  23.685 -18.187  1.00 21.74           O  
ANISOU 7601  OH  TYR C 992     3008   2747   2504    251     83     56       O  
ATOM   7602  N   ASP C 993     -78.065  21.511 -21.088  1.00 24.24           N  
ANISOU 7602  N   ASP C 993     3370   2884   2957    -10    186    129       N  
ATOM   7603  CA  ASP C 993     -79.288  20.949 -21.617  1.00 24.55           C  
ANISOU 7603  CA  ASP C 993     3404   2913   3010    -65    202    130       C  
ATOM   7604  C   ASP C 993     -80.078  22.127 -22.199  1.00 24.33           C  
ANISOU 7604  C   ASP C 993     3318   2931   2995    -87    186    130       C  
ATOM   7605  O   ASP C 993     -80.360  23.058 -21.495  1.00 24.62           O  
ANISOU 7605  O   ASP C 993     3333   2987   3032    -69    187    142       O  
ATOM   7606  CB  ASP C 993     -80.064  20.267 -20.485  1.00 25.58           C  
ANISOU 7606  CB  ASP C 993     3563   3018   3138    -72    237    151       C  
ATOM   7607  CG  ASP C 993     -81.365  19.603 -20.956  1.00 27.48           C  
ANISOU 7607  CG  ASP C 993     3797   3251   3394   -139    257    149       C  
ATOM   7608  OD1 ASP C 993     -81.950  19.967 -21.997  1.00 27.54           O  
ANISOU 7608  OD1 ASP C 993     3761   3291   3411   -177    241    135       O  
ATOM   7609  OD2 ASP C 993     -81.846  18.718 -20.224  1.00 31.11           O  
ANISOU 7609  OD2 ASP C 993     4293   3676   3853   -153    292    163       O  
ATOM   7610  N   ILE C 994     -80.400  22.077 -23.484  1.00 24.42           N  
ANISOU 7610  N   ILE C 994     3305   2960   3013   -121    174    116       N  
ATOM   7611  CA  ILE C 994     -81.069  23.159 -24.164  1.00 23.76           C  
ANISOU 7611  CA  ILE C 994     3168   2925   2937   -132    161    119       C  
ATOM   7612  C   ILE C 994     -82.448  23.507 -23.598  1.00 23.51           C  
ANISOU 7612  C   ILE C 994     3106   2918   2909   -150    177    137       C  
ATOM   7613  O   ILE C 994     -82.945  24.624 -23.802  1.00 22.71           O  
ANISOU 7613  O   ILE C 994     2963   2856   2810   -138    170    149       O  
ATOM   7614  CB  ILE C 994     -81.240  22.868 -25.667  1.00 26.25           C  
ANISOU 7614  CB  ILE C 994     3462   3261   3250   -164    146    100       C  
ATOM   7615  CG1 ILE C 994     -82.144  21.642 -25.889  1.00 27.82           C  
ANISOU 7615  CG1 ILE C 994     3671   3449   3450   -220    162     87       C  
ATOM   7616  CG2 ILE C 994     -79.876  22.651 -26.292  1.00 27.35           C  
ANISOU 7616  CG2 ILE C 994     3626   3381   3383   -141    131     83       C  
ATOM   7617  CD1 ILE C 994     -82.354  21.294 -27.354  1.00 29.08           C  
ANISOU 7617  CD1 ILE C 994     3810   3635   3603   -256    146     62       C  
ATOM   7618  N   ALA C 995     -83.062  22.565 -22.890  1.00 23.16           N  
ANISOU 7618  N   ALA C 995     3083   2851   2866   -175    201    143       N  
ATOM   7619  CA  ALA C 995     -84.359  22.782 -22.276  1.00 23.95           C  
ANISOU 7619  CA  ALA C 995     3155   2977   2969   -193    220    162       C  
ATOM   7620  C   ALA C 995     -84.288  23.658 -21.023  1.00 24.34           C  
ANISOU 7620  C   ALA C 995     3207   3027   3015   -146    229    184       C  
ATOM   7621  O   ALA C 995     -85.329  24.071 -20.523  1.00 25.89           O  
ANISOU 7621  O   ALA C 995     3374   3251   3210   -150    244    202       O  
ATOM   7622  CB  ALA C 995     -85.011  21.430 -21.932  1.00 25.26           C  
ANISOU 7622  CB  ALA C 995     3345   3114   3138   -243    250    161       C  
ATOM   7623  N   GLN C 996     -83.086  23.937 -20.504  1.00 23.86           N  
ANISOU 7623  N   GLN C 996     3178   2940   2947   -101    220    180       N  
ATOM   7624  CA  GLN C 996     -82.923  24.828 -19.347  1.00 23.34           C  
ANISOU 7624  CA  GLN C 996     3116   2878   2873    -58    225    193       C  
ATOM   7625  C   GLN C 996     -83.006  26.332 -19.666  1.00 22.25           C  
ANISOU 7625  C   GLN C 996     2944   2772   2740    -36    213    193       C  
ATOM   7626  O   GLN C 996     -82.809  27.160 -18.785  1.00 21.18           O  
ANISOU 7626  O   GLN C 996     2813   2635   2598     -3    217    197       O  
ATOM   7627  CB  GLN C 996     -81.605  24.563 -18.617  1.00 24.52           C  
ANISOU 7627  CB  GLN C 996     3309   2998   3010    -19    220    184       C  
ATOM   7628  CG  GLN C 996     -81.668  23.436 -17.630  1.00 25.85           C  
ANISOU 7628  CG  GLN C 996     3519   3137   3166    -14    245    198       C  
ATOM   7629  CD  GLN C 996     -80.318  23.057 -17.068  1.00 24.97           C  
ANISOU 7629  CD  GLN C 996     3446   3006   3034     30    238    190       C  
ATOM   7630  OE1 GLN C 996     -79.639  22.201 -17.619  1.00 26.51           O  
ANISOU 7630  OE1 GLN C 996     3666   3179   3226     29    234    182       O  
ATOM   7631  NE2 GLN C 996     -79.936  23.672 -15.973  1.00 24.81           N  
ANISOU 7631  NE2 GLN C 996     3431   3000   2996     72    236    193       N  
ATOM   7632  N   VAL C 997     -83.344  26.678 -20.905  1.00 22.01           N  
ANISOU 7632  N   VAL C 997     2878   2767   2717    -55    201    190       N  
ATOM   7633  CA  VAL C 997     -83.381  28.066 -21.331  1.00 21.35           C  
ANISOU 7633  CA  VAL C 997     2769   2707   2637    -31    195    195       C  
ATOM   7634  C   VAL C 997     -84.762  28.419 -21.882  1.00 22.57           C  
ANISOU 7634  C   VAL C 997     2876   2908   2791    -43    203    215       C  
ATOM   7635  O   VAL C 997     -85.281  27.695 -22.717  1.00 22.86           O  
ANISOU 7635  O   VAL C 997     2890   2968   2827    -79    197    211       O  
ATOM   7636  CB  VAL C 997     -82.386  28.309 -22.473  1.00 20.90           C  
ANISOU 7636  CB  VAL C 997     2711   2646   2584    -30    173    179       C  
ATOM   7637  CG1 VAL C 997     -82.473  29.761 -22.915  1.00 22.75           C  
ANISOU 7637  CG1 VAL C 997     2924   2897   2822     -5    176    188       C  
ATOM   7638  CG2 VAL C 997     -80.963  27.999 -22.028  1.00 20.25           C  
ANISOU 7638  CG2 VAL C 997     2665   2529   2498    -16    163    159       C  
ATOM   7639  N   ASN C 998     -85.328  29.537 -21.428  1.00 22.84           N  
ANISOU 7639  N   ASN C 998     2895   2959   2822    -10    217    233       N  
ATOM   7640  CA  ASN C 998     -86.562  30.070 -21.984  1.00 23.24           C  
ANISOU 7640  CA  ASN C 998     2898   3064   2868     -6    226    256       C  
ATOM   7641  C   ASN C 998     -86.292  31.508 -22.408  1.00 21.91           C  
ANISOU 7641  C   ASN C 998     2728   2898   2700     39    229    265       C  
ATOM   7642  O   ASN C 998     -86.083  32.414 -21.570  1.00 21.27           O  
ANISOU 7642  O   ASN C 998     2670   2791   2619     74    245    270       O  
ATOM   7643  CB  ASN C 998     -87.683  29.949 -20.941  1.00 24.44           C  
ANISOU 7643  CB  ASN C 998     3037   3237   3014     -3    250    276       C  
ATOM   7644  CG  ASN C 998     -89.078  30.249 -21.503  1.00 25.74           C  
ANISOU 7644  CG  ASN C 998     3141   3473   3168     -4    258    299       C  
ATOM   7645  OD1 ASN C 998     -89.318  30.165 -22.699  1.00 28.70           O  
ANISOU 7645  OD1 ASN C 998     3480   3887   3538    -19    243    296       O  
ATOM   7646  ND2 ASN C 998     -90.004  30.569 -20.636  1.00 27.01           N  
ANISOU 7646  ND2 ASN C 998     3285   3656   3320     16    282    321       N  
ATOM   7647  N   LEU C 999     -86.187  31.702 -23.706  1.00 21.29           N  
ANISOU 7647  N   LEU C 999     2627   2843   2619     36    216    266       N  
ATOM   7648  CA  LEU C 999     -85.884  33.029 -24.259  1.00 22.83           C  
ANISOU 7648  CA  LEU C 999     2824   3034   2814     77    224    279       C  
ATOM   7649  C   LEU C 999     -87.047  33.979 -23.987  1.00 24.37           C  
ANISOU 7649  C   LEU C 999     2997   3265   2999    120    250    312       C  
ATOM   7650  O   LEU C 999     -88.198  33.594 -24.155  1.00 23.41           O  
ANISOU 7650  O   LEU C 999     2830   3201   2864    113    251    328       O  
ATOM   7651  CB  LEU C 999     -85.621  32.923 -25.767  1.00 23.12           C  
ANISOU 7651  CB  LEU C 999     2840   3098   2846     69    206    277       C  
ATOM   7652  CG  LEU C 999     -84.386  32.095 -26.120  1.00 23.49           C  
ANISOU 7652  CG  LEU C 999     2913   3111   2903     36    183    245       C  
ATOM   7653  CD1 LEU C 999     -84.188  32.117 -27.613  1.00 23.84           C  
ANISOU 7653  CD1 LEU C 999     2936   3185   2939     34    169    246       C  
ATOM   7654  CD2 LEU C 999     -83.126  32.624 -25.421  1.00 23.34           C  
ANISOU 7654  CD2 LEU C 999     2938   3032   2897     49    188    230       C  
ATOM   7655  N   LYS C1000     -86.738  35.185 -23.498  1.00 26.32           N  
ANISOU 7655  N   LYS C1000     3275   3475   3250    161    273    320       N  
ATOM   7656  CA  LYS C1000     -87.762  36.150 -23.118  1.00 26.73           C  
ANISOU 7656  CA  LYS C1000     3316   3549   3290    211    305    352       C  
ATOM   7657  C   LYS C1000     -87.768  37.416 -23.958  1.00 26.14           C  
ANISOU 7657  C   LYS C1000     3246   3475   3212    260    325    377       C  
ATOM   7658  O   LYS C1000     -88.815  37.872 -24.369  1.00 25.39           O  
ANISOU 7658  O   LYS C1000     3117   3433   3098    300    341    412       O  
ATOM   7659  CB  LYS C1000     -87.603  36.583 -21.654  1.00 27.81           C  
ANISOU 7659  CB  LYS C1000     3494   3640   3432    228    326    343       C  
ATOM   7660  CG  LYS C1000     -87.539  35.486 -20.625  1.00 28.96           C  
ANISOU 7660  CG  LYS C1000     3646   3778   3579    192    313    324       C  
ATOM   7661  CD  LYS C1000     -88.601  34.420 -20.775  1.00 31.27           C  
ANISOU 7661  CD  LYS C1000     3891   4129   3863    164    306    338       C  
ATOM   7662  CE  LYS C1000     -89.959  34.856 -20.310  1.00 33.59           C  
ANISOU 7662  CE  LYS C1000     4153   4470   4140    198    332    370       C  
ATOM   7663  NZ  LYS C1000     -90.854  33.665 -20.198  1.00 36.51           N  
ANISOU 7663  NZ  LYS C1000     4478   4889   4503    156    327    375       N  
ATOM   7664  N   TYR C1001     -86.606  38.024 -24.139  1.00 27.67           N  
ANISOU 7664  N   TYR C1001     3483   3608   3421    260    331    361       N  
ATOM   7665  CA  TYR C1001     -86.493  39.274 -24.884  1.00 27.89           C  
ANISOU 7665  CA  TYR C1001     3528   3620   3448    305    359    385       C  
ATOM   7666  C   TYR C1001     -85.406  39.229 -25.929  1.00 26.93           C  
ANISOU 7666  C   TYR C1001     3416   3479   3338    283    345    372       C  
ATOM   7667  O   TYR C1001     -84.417  38.490 -25.816  1.00 28.35           O  
ANISOU 7667  O   TYR C1001     3606   3634   3531    235    318    336       O  
ATOM   7668  CB  TYR C1001     -86.242  40.476 -23.959  1.00 29.62           C  
ANISOU 7668  CB  TYR C1001     3802   3774   3677    337    399    382       C  
ATOM   7669  CG  TYR C1001     -87.269  40.652 -22.876  1.00 30.95           C  
ANISOU 7669  CG  TYR C1001     3969   3958   3833    368    419    396       C  
ATOM   7670  CD1 TYR C1001     -88.480  41.288 -23.135  1.00 32.02           C  
ANISOU 7670  CD1 TYR C1001     4082   4138   3947    429    448    442       C  
ATOM   7671  CD2 TYR C1001     -87.039  40.172 -21.589  1.00 32.07           C  
ANISOU 7671  CD2 TYR C1001     4128   4076   3980    341    411    365       C  
ATOM   7672  CE1 TYR C1001     -89.432  41.442 -22.135  1.00 32.30           C  
ANISOU 7672  CE1 TYR C1001     4113   4192   3969    461    468    456       C  
ATOM   7673  CE2 TYR C1001     -87.986  40.304 -20.596  1.00 33.60           C  
ANISOU 7673  CE2 TYR C1001     4320   4288   4160    371    430    379       C  
ATOM   7674  CZ  TYR C1001     -89.181  40.950 -20.872  1.00 33.79           C  
ANISOU 7674  CZ  TYR C1001     4321   4354   4165    429    460    424       C  
ATOM   7675  OH  TYR C1001     -90.126  41.068 -19.866  1.00 35.85           O  
ANISOU 7675  OH  TYR C1001     4575   4635   4410    461    481    439       O  
ATOM   7676  N   LEU C1002     -85.603  40.038 -26.953  1.00 28.16           N  
ANISOU 7676  N   LEU C1002     3567   3647   3483    323    366    405       N  
ATOM   7677  CA  LEU C1002     -84.604  40.265 -27.983  1.00 27.52           C  
ANISOU 7677  CA  LEU C1002     3501   3544   3412    313    364    400       C  
ATOM   7678  C   LEU C1002     -84.424  41.750 -28.104  1.00 26.85           C  
ANISOU 7678  C   LEU C1002     3460   3407   3333    359    416    425       C  
ATOM   7679  O   LEU C1002     -85.394  42.451 -28.292  1.00 27.22           O  
ANISOU 7679  O   LEU C1002     3502   3479   3362    419    446    467       O  
ATOM   7680  CB  LEU C1002     -85.093  39.662 -29.288  1.00 28.53           C  
ANISOU 7680  CB  LEU C1002     3577   3748   3515    318    340    420       C  
ATOM   7681  CG  LEU C1002     -84.198  39.796 -30.520  1.00 29.10           C  
ANISOU 7681  CG  LEU C1002     3655   3813   3589    314    337    422       C  
ATOM   7682  CD1 LEU C1002     -82.908  39.095 -30.301  1.00 32.61           C  
ANISOU 7682  CD1 LEU C1002     4119   4216   4057    255    311    376       C  
ATOM   7683  CD2 LEU C1002     -84.859  39.142 -31.711  1.00 30.30           C  
ANISOU 7683  CD2 LEU C1002     3751   4052   3708    322    310    438       C  
ATOM   7684  N   LEU C1003     -83.206  42.236 -27.939  1.00 25.33           N  
ANISOU 7684  N   LEU C1003     3314   3145   3166    332    430    398       N  
ATOM   7685  CA  LEU C1003     -82.936  43.643 -28.052  1.00 26.80           C  
ANISOU 7685  CA  LEU C1003     3552   3269   3363    365    485    416       C  
ATOM   7686  C   LEU C1003     -82.183  43.933 -29.335  1.00 27.73           C  
ANISOU 7686  C   LEU C1003     3674   3377   3484    363    495    430       C  
ATOM   7687  O   LEU C1003     -81.230  43.227 -29.704  1.00 27.18           O  
ANISOU 7687  O   LEU C1003     3591   3312   3426    314    463    401       O  
ATOM   7688  CB  LEU C1003     -82.101  44.139 -26.887  1.00 27.70           C  
ANISOU 7688  CB  LEU C1003     3717   3306   3503    331    503    372       C  
ATOM   7689  CG  LEU C1003     -82.813  44.409 -25.573  1.00 30.64           C  
ANISOU 7689  CG  LEU C1003     4107   3664   3871    350    517    365       C  
ATOM   7690  CD1 LEU C1003     -83.410  43.142 -24.999  1.00 32.28           C  
ANISOU 7690  CD1 LEU C1003     4267   3933   4064    334    470    355       C  
ATOM   7691  CD2 LEU C1003     -81.828  45.019 -24.600  1.00 32.68           C  
ANISOU 7691  CD2 LEU C1003     4420   3846   4152    313    537    316       C  
ATOM   7692  N   LYS C1004     -82.619  44.973 -30.015  1.00 29.42           N  
ANISOU 7692  N   LYS C1004     3909   3581   3689    423    544    479       N  
ATOM   7693  CA  LYS C1004     -81.856  45.568 -31.112  1.00 31.53           C  
ANISOU 7693  CA  LYS C1004     4198   3820   3962    428    572    497       C  
ATOM   7694  C   LYS C1004     -81.048  46.697 -30.520  1.00 30.36           C  
ANISOU 7694  C   LYS C1004     4120   3569   3846    410    625    479       C  
ATOM   7695  O   LYS C1004     -81.614  47.640 -29.967  1.00 29.57           O  
ANISOU 7695  O   LYS C1004     4063   3427   3747    452    674    497       O  
ATOM   7696  CB  LYS C1004     -82.799  46.072 -32.169  1.00 34.73           C  
ANISOU 7696  CB  LYS C1004     4589   4272   4334    509    599    564       C  
ATOM   7697  CG  LYS C1004     -82.140  46.602 -33.433  1.00 41.19           C  
ANISOU 7697  CG  LYS C1004     5425   5074   5151    525    629    593       C  
ATOM   7698  CD  LYS C1004     -83.224  46.825 -34.493  1.00 45.77           C  
ANISOU 7698  CD  LYS C1004     5975   5732   5685    612    641    659       C  
ATOM   7699  CE  LYS C1004     -82.848  47.906 -35.473  1.00 49.47           C  
ANISOU 7699  CE  LYS C1004     6488   6159   6150    660    703    708       C  
ATOM   7700  NZ  LYS C1004     -83.900  48.065 -36.503  1.00 52.36           N  
ANISOU 7700  NZ  LYS C1004     6819   6614   6463    752    711    773       N  
ATOM   7701  N   LEU C1005     -79.729  46.569 -30.584  1.00 30.86           N  
ANISOU 7701  N   LEU C1005     4195   3595   3935    346    617    438       N  
ATOM   7702  CA  LEU C1005     -78.815  47.531 -29.991  1.00 33.01           C  
ANISOU 7702  CA  LEU C1005     4527   3774   4240    308    662    406       C  
ATOM   7703  C   LEU C1005     -77.976  48.263 -31.058  1.00 34.38           C  
ANISOU 7703  C   LEU C1005     4729   3906   4428    301    707    426       C  
ATOM   7704  O   LEU C1005     -77.479  47.632 -31.986  1.00 36.60           O  
ANISOU 7704  O   LEU C1005     4974   4230   4704    286    679    431       O  
ATOM   7705  CB  LEU C1005     -77.843  46.808 -29.060  1.00 34.80           C  
ANISOU 7705  CB  LEU C1005     4740   3997   4485    230    618    336       C  
ATOM   7706  CG  LEU C1005     -78.371  46.060 -27.838  1.00 33.81           C  
ANISOU 7706  CG  LEU C1005     4594   3901   4349    223    576    306       C  
ATOM   7707  CD1 LEU C1005     -77.212  45.443 -27.109  1.00 34.08           C  
ANISOU 7707  CD1 LEU C1005     4618   3933   4398    152    538    242       C  
ATOM   7708  CD2 LEU C1005     -79.106  47.012 -26.937  1.00 35.90           C  
ANISOU 7708  CD2 LEU C1005     4906   4119   4614    257    621    312       C  
ATOM   7709  N   LYS C1006     -77.775  49.570 -30.866  1.00 34.06           N  
ANISOU 7709  N   LYS C1006     4756   3777   4407    307    780    433       N  
ATOM   7710  CA  LYS C1006     -76.831  50.330 -31.637  1.00 34.97           C  
ANISOU 7710  CA  LYS C1006     4908   3836   4544    284    830    441       C  
ATOM   7711  C   LYS C1006     -75.599  50.389 -30.804  1.00 33.10           C  
ANISOU 7711  C   LYS C1006     4684   3551   4340    190    825    366       C  
ATOM   7712  O   LYS C1006     -75.658  50.762 -29.636  1.00 31.95           O  
ANISOU 7712  O   LYS C1006     4571   3364   4207    168    836    326       O  
ATOM   7713  CB  LYS C1006     -77.291  51.780 -31.930  1.00 37.48           C  
ANISOU 7713  CB  LYS C1006     5302   4074   4865    342    924    491       C  
ATOM   7714  N   PHE C1007     -74.490  50.001 -31.415  1.00 33.04           N  
ANISOU 7714  N   PHE C1007     4649   3559   4345    137    807    347       N  
ATOM   7715  CA  PHE C1007     -73.177  50.152 -30.824  1.00 35.41           C  
ANISOU 7715  CA  PHE C1007     4956   3824   4675     46    808    279       C  
ATOM   7716  C   PHE C1007     -72.601  51.483 -31.325  1.00 37.96           C  
ANISOU 7716  C   PHE C1007     5342   4056   5025     26    896    292       C  
ATOM   7717  O   PHE C1007     -72.401  51.645 -32.513  1.00 34.85           O  
ANISOU 7717  O   PHE C1007     4946   3665   4629     46    923    338       O  
ATOM   7718  CB  PHE C1007     -72.265  49.004 -31.300  1.00 33.78           C  
ANISOU 7718  CB  PHE C1007     4683   3689   4464      5    746    256       C  
ATOM   7719  CG  PHE C1007     -72.608  47.641 -30.714  1.00 30.73           C  
ANISOU 7719  CG  PHE C1007     4241   3380   4054      9    664    233       C  
ATOM   7720  CD1 PHE C1007     -73.792  47.003 -31.029  1.00 30.52           C  
ANISOU 7720  CD1 PHE C1007     4191   3406   4000     74    635    275       C  
ATOM   7721  CD2 PHE C1007     -71.713  46.988 -29.900  1.00 30.54           C  
ANISOU 7721  CD2 PHE C1007     4187   3379   4035    -51    619    169       C  
ATOM   7722  CE1 PHE C1007     -74.086  45.734 -30.534  1.00 29.03           C  
ANISOU 7722  CE1 PHE C1007     3956   3281   3792     72    566    255       C  
ATOM   7723  CE2 PHE C1007     -72.011  45.730 -29.378  1.00 29.53           C  
ANISOU 7723  CE2 PHE C1007     4017   3317   3887    -42    551    153       C  
ATOM   7724  CZ  PHE C1007     -73.194  45.102 -29.714  1.00 27.96           C  
ANISOU 7724  CZ  PHE C1007     3801   3159   3664     16    527    196       C  
ATOM   7725  N   ASN C1008     -72.344  52.413 -30.414  1.00 41.68           N  
ANISOU 7725  N   ASN C1008     5869   4446   5521    -15    943    251       N  
ATOM   7726  CA  ASN C1008     -71.687  53.668 -30.754  1.00 43.10           C  
ANISOU 7726  CA  ASN C1008     6114   4530   5733    -52   1031    250       C  
ATOM   7727  C   ASN C1008     -70.214  53.564 -30.416  1.00 41.43           C  
ANISOU 7727  C   ASN C1008     5878   4318   5547   -163   1017    175       C  
ATOM   7728  O   ASN C1008     -69.812  53.761 -29.270  1.00 39.85           O  
ANISOU 7728  O   ASN C1008     5687   4094   5358   -224   1010    104       O  
ATOM   7729  CB  ASN C1008     -72.333  54.824 -30.002  1.00 44.96           C  
ANISOU 7729  CB  ASN C1008     6434   4669   5977    -30   1100    249       C  
ATOM   7730  CG  ASN C1008     -73.767  55.045 -30.434  1.00 50.23           C  
ANISOU 7730  CG  ASN C1008     7127   5341   6616     88   1124    331       C  
ATOM   7731  OD1 ASN C1008     -74.071  55.089 -31.629  1.00 53.99           O  
ANISOU 7731  OD1 ASN C1008     7599   5836   7079    147   1145    402       O  
ATOM   7732  ND2 ASN C1008     -74.664  55.157 -29.469  1.00 55.98           N  
ANISOU 7732  ND2 ASN C1008     7877   6061   7332    127   1119    323       N  
ATOM   7733  N   PHE C1009     -69.405  53.271 -31.428  1.00 44.36           N  
ANISOU 7733  N   PHE C1009     6212   4719   5922   -188   1013    190       N  
ATOM   7734  CA  PHE C1009     -67.954  53.113 -31.243  1.00 47.47           C  
ANISOU 7734  CA  PHE C1009     6569   5128   6337   -290    999    124       C  
ATOM   7735  C   PHE C1009     -67.221  54.440 -30.943  1.00 49.75           C  
ANISOU 7735  C   PHE C1009     6922   5315   6666   -370   1084     84       C  
ATOM   7736  O   PHE C1009     -67.603  55.478 -31.459  1.00 54.23           O  
ANISOU 7736  O   PHE C1009     7562   5794   7248   -342   1169    130       O  
ATOM   7737  CB  PHE C1009     -67.377  52.409 -32.457  1.00 47.24           C  
ANISOU 7737  CB  PHE C1009     6485   5166   6300   -285    974    157       C  
ATOM   7738  CG  PHE C1009     -67.811  50.984 -32.565  1.00 46.22           C  
ANISOU 7738  CG  PHE C1009     6288   5139   6135   -235    883    170       C  
ATOM   7739  CD1 PHE C1009     -68.924  50.640 -33.324  1.00 48.11           C  
ANISOU 7739  CD1 PHE C1009     6527   5407   6347   -143    873    241       C  
ATOM   7740  CD2 PHE C1009     -67.126  49.982 -31.884  1.00 47.11           C  
ANISOU 7740  CD2 PHE C1009     6339   5322   6240   -280    810    110       C  
ATOM   7741  CE1 PHE C1009     -69.334  49.314 -33.418  1.00 46.85           C  
ANISOU 7741  CE1 PHE C1009     6308   5338   6157   -106    793    246       C  
ATOM   7742  CE2 PHE C1009     -67.529  48.651 -31.982  1.00 45.93           C  
ANISOU 7742  CE2 PHE C1009     6136   5258   6059   -236    733    122       C  
ATOM   7743  CZ  PHE C1009     -68.638  48.324 -32.744  1.00 44.79           C  
ANISOU 7743  CZ  PHE C1009     5993   5133   5891   -154    726    188       C  
ATOM   7744  N   LYS C1010     -66.225  54.400 -30.060  1.00 52.08           N  
ANISOU 7744  N   LYS C1010     7191   5621   6975   -466   1062     -3       N  
ATOM   7745  CA  LYS C1010     -65.492  55.613 -29.641  1.00 57.96           C  
ANISOU 7745  CA  LYS C1010     7992   6274   7757   -559   1138    -58       C  
ATOM   7746  C   LYS C1010     -64.306  55.954 -30.550  1.00 60.54           C  
ANISOU 7746  C   LYS C1010     8302   6590   8109   -630   1182    -59       C  
ATOM   7747  O   LYS C1010     -63.980  55.201 -31.466  1.00 61.78           O  
ANISOU 7747  O   LYS C1010     8401   6820   8254   -607   1148    -21       O  
ATOM   7748  CB  LYS C1010     -65.035  55.520 -28.166  1.00 58.50           C  
ANISOU 7748  CB  LYS C1010     8042   6363   7824   -632   1098   -159       C  
TER    7749      LYS C1010                                                      
ATOM   7750  N   SER D 663     -95.841   5.962 -42.016  1.00 94.09           N  
ANISOU 7750  N   SER D 663    11528  13740  10483   1484    363  -1340       N  
ATOM   7751  CA  SER D 663     -96.047   6.750 -40.758  1.00 88.61           C  
ANISOU 7751  CA  SER D 663    10895  12870   9902   1342    399  -1182       C  
ATOM   7752  C   SER D 663     -95.213   6.202 -39.607  1.00 87.83           C  
ANISOU 7752  C   SER D 663    10872  12597   9902   1318    398  -1170       C  
ATOM   7753  O   SER D 663     -95.241   4.999 -39.341  1.00 84.56           O  
ANISOU 7753  O   SER D 663    10519  12058   9552   1345    353  -1310       O  
ATOM   7754  CB  SER D 663     -97.527   6.785 -40.311  1.00 88.60           C  
ANISOU 7754  CB  SER D 663    10954  12718   9993   1233    378  -1214       C  
ATOM   7755  OG  SER D 663     -97.653   7.361 -39.007  1.00 85.05           O  
ANISOU 7755  OG  SER D 663    10569  12093   9655   1110    405  -1087       O  
ATOM   7756  N   LYS D 664     -94.521   7.090 -38.896  1.00 87.29           N  
ANISOU 7756  N   LYS D 664    10798  12511   9856   1264    445  -1002       N  
ATOM   7757  CA  LYS D 664     -93.828   6.714 -37.659  1.00 85.99           C  
ANISOU 7757  CA  LYS D 664    10705  12177   9788   1228    447   -973       C  
ATOM   7758  C   LYS D 664     -94.762   6.658 -36.432  1.00 78.21           C  
ANISOU 7758  C   LYS D 664     9815  10961   8941   1103    437   -959       C  
ATOM   7759  O   LYS D 664     -94.351   6.171 -35.391  1.00 76.75           O  
ANISOU 7759  O   LYS D 664     9695  10628   8839   1078    432   -953       O  
ATOM   7760  CB  LYS D 664     -92.668   7.675 -37.364  1.00 86.64           C  
ANISOU 7760  CB  LYS D 664    10736  12341   9843   1223    496   -810       C  
ATOM   7761  N   LEU D 665     -96.009   7.131 -36.553  1.00 72.92           N  
ANISOU 7761  N   LEU D 665     9148  10269   8288   1031    434   -952       N  
ATOM   7762  CA  LEU D 665     -96.910   7.223 -35.394  1.00 67.18           C  
ANISOU 7762  CA  LEU D 665     8498   9348   7680    912    430   -921       C  
ATOM   7763  C   LEU D 665     -97.410   5.857 -34.916  1.00 62.85           C  
ANISOU 7763  C   LEU D 665     8030   8625   7224    905    385  -1053       C  
ATOM   7764  O   LEU D 665     -97.680   4.983 -35.728  1.00 67.65           O  
ANISOU 7764  O   LEU D 665     8630   9262   7810    969    347  -1194       O  
ATOM   7765  CB  LEU D 665     -98.144   8.065 -35.716  1.00 65.81           C  
ANISOU 7765  CB  LEU D 665     8301   9208   7496    846    437   -885       C  
ATOM   7766  CG  LEU D 665     -97.930   9.516 -36.120  1.00 64.73           C  
ANISOU 7766  CG  LEU D 665     8087   9214   7294    833    479   -740       C  
ATOM   7767  CD1 LEU D 665     -99.220  10.095 -36.669  1.00 64.67           C  
ANISOU 7767  CD1 LEU D 665     8054   9253   7264    793    476   -739       C  
ATOM   7768  CD2 LEU D 665     -97.429  10.336 -34.949  1.00 64.79           C  
ANISOU 7768  CD2 LEU D 665     8113   9131   7372    759    509   -603       C  
ATOM   7769  N   PRO D 666     -97.561   5.680 -33.597  1.00 57.59           N  
ANISOU 7769  N   PRO D 666     7436   7781   6666    827    388  -1006       N  
ATOM   7770  CA  PRO D 666     -98.151   4.458 -33.055  1.00 57.05           C  
ANISOU 7770  CA  PRO D 666     7441   7533   6703    803    351  -1103       C  
ATOM   7771  C   PRO D 666     -99.549   4.204 -33.626  1.00 59.14           C  
ANISOU 7771  C   PRO D 666     7703   7779   6987    766    320  -1197       C  
ATOM   7772  O   PRO D 666    -100.258   5.157 -33.981  1.00 58.17           O  
ANISOU 7772  O   PRO D 666     7543   7740   6818    723    336  -1148       O  
ATOM   7773  CB  PRO D 666     -98.250   4.748 -31.562  1.00 58.27           C  
ANISOU 7773  CB  PRO D 666     7650   7545   6945    711    373   -992       C  
ATOM   7774  CG  PRO D 666     -97.269   5.836 -31.297  1.00 56.36           C  
ANISOU 7774  CG  PRO D 666     7369   7398   6646    717    414   -865       C  
ATOM   7775  CD  PRO D 666     -97.205   6.650 -32.548  1.00 55.99           C  
ANISOU 7775  CD  PRO D 666     7241   7540   6492    758    427   -856       C  
ATOM   7776  N   LYS D 667     -99.929   2.934 -33.731  1.00 61.73           N  
ANISOU 7776  N   LYS D 667     8068   7998   7388    785    273  -1331       N  
ATOM   7777  CA  LYS D 667    -101.217   2.561 -34.321  1.00 63.30           C  
ANISOU 7777  CA  LYS D 667     8260   8177   7614    756    236  -1441       C  
ATOM   7778  C   LYS D 667    -102.376   3.302 -33.629  1.00 62.13           C  
ANISOU 7778  C   LYS D 667     8129   7966   7510    632    257  -1351       C  
ATOM   7779  O   LYS D 667    -103.204   3.913 -34.312  1.00 59.85           O  
ANISOU 7779  O   LYS D 667     7798   7777   7167    612    256  -1365       O  
ATOM   7780  CB  LYS D 667    -101.432   1.035 -34.284  1.00 61.25           C  
ANISOU 7780  CB  LYS D 667     8043   7762   7465    778    180  -1589       C  
ATOM   7781  N   PRO D 668    -102.416   3.287 -32.278  1.00 60.74           N  
ANISOU 7781  N   PRO D 668     8012   7642   7426    555    276  -1254       N  
ATOM   7782  CA  PRO D 668    -103.494   3.981 -31.543  1.00 59.77           C  
ANISOU 7782  CA  PRO D 668     7902   7465   7341    444    295  -1170       C  
ATOM   7783  C   PRO D 668    -103.673   5.439 -31.935  1.00 55.28           C  
ANISOU 7783  C   PRO D 668     7281   7048   6676    428    328  -1084       C  
ATOM   7784  O   PRO D 668    -104.798   5.904 -32.089  1.00 53.92           O  
ANISOU 7784  O   PRO D 668     7093   6892   6502    370    326  -1083       O  
ATOM   7785  CB  PRO D 668    -103.046   3.885 -30.086  1.00 58.46           C  
ANISOU 7785  CB  PRO D 668     7791   7172   7251    401    318  -1064       C  
ATOM   7786  CG  PRO D 668    -102.185   2.663 -30.049  1.00 60.70           C  
ANISOU 7786  CG  PRO D 668     8105   7377   7582    471    295  -1132       C  
ATOM   7787  CD  PRO D 668    -101.451   2.665 -31.354  1.00 60.62           C  
ANISOU 7787  CD  PRO D 668     8044   7516   7471    576    282  -1215       C  
ATOM   7788  N   VAL D 669    -102.566   6.124 -32.174  1.00 55.55           N  
ANISOU 7788  N   VAL D 669     7280   7193   6632    484    355  -1016       N  
ATOM   7789  CA  VAL D 669    -102.597   7.518 -32.600  1.00 57.87           C  
ANISOU 7789  CA  VAL D 669     7516   7627   6845    476    387   -923       C  
ATOM   7790  C   VAL D 669    -103.139   7.632 -34.024  1.00 58.22           C  
ANISOU 7790  C   VAL D 669     7500   7817   6803    523    371  -1000       C  
ATOM   7791  O   VAL D 669    -103.998   8.480 -34.321  1.00 59.53           O  
ANISOU 7791  O   VAL D 669     7635   8045   6940    483    381   -962       O  
ATOM   7792  CB  VAL D 669    -101.200   8.163 -32.503  1.00 58.75           C  
ANISOU 7792  CB  VAL D 669     7599   7817   6908    522    419   -827       C  
ATOM   7793  CG1 VAL D 669    -101.242   9.611 -32.951  1.00 60.84           C  
ANISOU 7793  CG1 VAL D 669     7797   8211   7107    509    450   -722       C  
ATOM   7794  CG2 VAL D 669    -100.684   8.080 -31.074  1.00 58.41           C  
ANISOU 7794  CG2 VAL D 669     7608   7641   6942    480    432   -757       C  
ATOM   7795  N   GLN D 670    -102.647   6.767 -34.898  1.00 60.11           N  
ANISOU 7795  N   GLN D 670     7721   8119   7001    615    345  -1114       N  
ATOM   7796  CA  GLN D 670    -103.135   6.718 -36.266  1.00 63.14           C  
ANISOU 7796  CA  GLN D 670     8043   8652   7296    676    324  -1210       C  
ATOM   7797  C   GLN D 670    -104.640   6.503 -36.292  1.00 61.21           C  
ANISOU 7797  C   GLN D 670     7813   8344   7100    607    295  -1281       C  
ATOM   7798  O   GLN D 670    -105.349   7.195 -37.011  1.00 60.92           O  
ANISOU 7798  O   GLN D 670     7724   8429   6995    606    300  -1273       O  
ATOM   7799  CB  GLN D 670    -102.417   5.612 -37.061  1.00 69.96           C  
ANISOU 7799  CB  GLN D 670     8890   9568   8122    789    289  -1351       C  
ATOM   7800  CG  GLN D 670    -100.962   5.925 -37.418  1.00 70.08           C  
ANISOU 7800  CG  GLN D 670     8863   9716   8050    880    317  -1290       C  
ATOM   7801  CD  GLN D 670    -100.309   4.804 -38.212  1.00 68.20           C  
ANISOU 7801  CD  GLN D 670     8606   9536   7771   1000    278  -1444       C  
ATOM   7802  OE1 GLN D 670    -100.967   4.151 -39.012  1.00 69.33           O  
ANISOU 7802  OE1 GLN D 670     8730   9715   7898   1041    233  -1594       O  
ATOM   7803  NE2 GLN D 670     -99.019   4.590 -38.004  1.00 65.59           N  
ANISOU 7803  NE2 GLN D 670     8277   9220   7423   1061    291  -1413       N  
ATOM   7804  N   ASP D 671    -105.122   5.551 -35.502  1.00 61.65           N  
ANISOU 7804  N   ASP D 671     7934   8213   7276    551    268  -1342       N  
ATOM   7805  CA  ASP D 671    -106.564   5.292 -35.399  1.00 63.64           C  
ANISOU 7805  CA  ASP D 671     8200   8389   7593    473    242  -1403       C  
ATOM   7806  C   ASP D 671    -107.352   6.512 -34.893  1.00 61.00           C  
ANISOU 7806  C   ASP D 671     7859   8069   7250    386    276  -1275       C  
ATOM   7807  O   ASP D 671    -108.451   6.776 -35.371  1.00 59.20           O  
ANISOU 7807  O   ASP D 671     7601   7890   7001    357    264  -1313       O  
ATOM   7808  CB  ASP D 671    -106.832   4.051 -34.529  1.00 66.59           C  
ANISOU 7808  CB  ASP D 671     8641   8548   8112    423    211  -1465       C  
ATOM   7809  CG  ASP D 671    -106.433   2.722 -35.234  1.00 73.96           C  
ANISOU 7809  CG  ASP D 671     9574   9457   9073    507    159  -1635       C  
ATOM   7810  OD1 ASP D 671    -106.056   2.763 -36.434  1.00 73.57           O  
ANISOU 7810  OD1 ASP D 671     9466   9572   8917    606    143  -1719       O  
ATOM   7811  OD2 ASP D 671    -106.495   1.645 -34.584  1.00 71.31           O  
ANISOU 7811  OD2 ASP D 671     9289   8938   8866    479    132  -1683       O  
ATOM   7812  N   LEU D 672    -106.782   7.255 -33.943  1.00 59.33           N  
ANISOU 7812  N   LEU D 672     7671   7818   7054    351    317  -1133       N  
ATOM   7813  CA  LEU D 672    -107.406   8.482 -33.435  1.00 55.28           C  
ANISOU 7813  CA  LEU D 672     7148   7319   6535    279    347  -1015       C  
ATOM   7814  C   LEU D 672    -107.516   9.524 -34.545  1.00 55.52           C  
ANISOU 7814  C   LEU D 672     7105   7537   6455    322    361   -981       C  
ATOM   7815  O   LEU D 672    -108.564  10.142 -34.712  1.00 54.46           O  
ANISOU 7815  O   LEU D 672     6948   7437   6306    280    362   -964       O  
ATOM   7816  CB  LEU D 672    -106.601   9.048 -32.256  1.00 53.27           C  
ANISOU 7816  CB  LEU D 672     6925   6997   6318    249    380   -885       C  
ATOM   7817  CG  LEU D 672    -107.065  10.375 -31.654  1.00 52.38           C  
ANISOU 7817  CG  LEU D 672     6800   6895   6206    185    408   -766       C  
ATOM   7818  CD1 LEU D 672    -108.405  10.209 -30.965  1.00 50.95           C  
ANISOU 7818  CD1 LEU D 672     6650   6618   6091     99    395   -783       C  
ATOM   7819  CD2 LEU D 672    -106.036  10.925 -30.678  1.00 51.82           C  
ANISOU 7819  CD2 LEU D 672     6745   6785   6161    178    434   -659       C  
ATOM   7820  N   ILE D 673    -106.438   9.714 -35.304  1.00 56.97           N  
ANISOU 7820  N   ILE D 673     7245   7845   6557    410    374   -965       N  
ATOM   7821  CA  ILE D 673    -106.461  10.670 -36.410  1.00 58.16           C  
ANISOU 7821  CA  ILE D 673     7315   8186   6597    460    392   -917       C  
ATOM   7822  C   ILE D 673    -107.531  10.322 -37.450  1.00 58.78           C  
ANISOU 7822  C   ILE D 673     7356   8356   6623    486    360  -1035       C  
ATOM   7823  O   ILE D 673    -108.235  11.207 -37.935  1.00 57.17           O  
ANISOU 7823  O   ILE D 673     7105   8250   6366    477    372   -984       O  
ATOM   7824  CB  ILE D 673    -105.097  10.759 -37.113  1.00 59.34           C  
ANISOU 7824  CB  ILE D 673     7415   8467   6663    559    410   -888       C  
ATOM   7825  CG1 ILE D 673    -104.011  11.194 -36.128  1.00 59.09           C  
ANISOU 7825  CG1 ILE D 673     7411   8360   6682    534    441   -769       C  
ATOM   7826  CG2 ILE D 673    -105.147  11.747 -38.277  1.00 61.12           C  
ANISOU 7826  CG2 ILE D 673     7549   8901   6774    614    432   -821       C  
ATOM   7827  CD1 ILE D 673    -104.409  12.355 -35.250  1.00 59.12           C  
ANISOU 7827  CD1 ILE D 673     7424   8297   6741    445    466   -640       C  
ATOM   7828  N   LYS D 674    -107.640   9.046 -37.806  1.00 59.70           N  
ANISOU 7828  N   LYS D 674     7488   8440   6754    522    317  -1193       N  
ATOM   7829  CA  LYS D 674    -108.654   8.617 -38.781  1.00 60.87           C  
ANISOU 7829  CA  LYS D 674     7597   8672   6860    548    279  -1329       C  
ATOM   7830  C   LYS D 674    -110.047   8.868 -38.228  1.00 59.35           C  
ANISOU 7830  C   LYS D 674     7428   8389   6733    444    271  -1321       C  
ATOM   7831  O   LYS D 674    -110.900   9.389 -38.908  1.00 55.21           O  
ANISOU 7831  O   LYS D 674     6854   7978   6147    449    268  -1331       O  
ATOM   7832  CB  LYS D 674    -108.469   7.155 -39.185  1.00 57.92           C  
ANISOU 7832  CB  LYS D 674     7235   8258   6514    604    226  -1514       C  
ATOM   7833  N   MET D 675    -110.250   8.504 -36.970  1.00 61.03           N  
ANISOU 7833  N   MET D 675     7713   8407   7068    355    271  -1296       N  
ATOM   7834  CA  MET D 675    -111.501   8.732 -36.274  1.00 60.72           C  
ANISOU 7834  CA  MET D 675     7698   8276   7097    253    269  -1273       C  
ATOM   7835  C   MET D 675    -111.927  10.211 -36.310  1.00 58.99           C  
ANISOU 7835  C   MET D 675     7442   8153   6818    230    305  -1144       C  
ATOM   7836  O   MET D 675    -113.091  10.534 -36.615  1.00 59.72           O  
ANISOU 7836  O   MET D 675     7507   8290   6893    199    294  -1167       O  
ATOM   7837  CB  MET D 675    -111.304   8.274 -34.840  1.00 63.17           C  
ANISOU 7837  CB  MET D 675     8084   8389   7529    179    277  -1226       C  
ATOM   7838  CG  MET D 675    -112.554   8.082 -34.033  1.00 65.54           C  
ANISOU 7838  CG  MET D 675     8413   8571   7918     76    266  -1229       C  
ATOM   7839  SD  MET D 675    -112.004   7.546 -32.413  1.00 64.86           S  
ANISOU 7839  SD  MET D 675     8405   8288   7951     17    282  -1153       S  
ATOM   7840  CE  MET D 675    -113.587   7.644 -31.573  1.00 68.60           C  
ANISOU 7840  CE  MET D 675     8890   8678   8498    -99    280  -1130       C  
ATOM   7841  N   ILE D 676    -110.995  11.117 -36.021  1.00 55.62           N  
ANISOU 7841  N   ILE D 676     7011   7757   6366    247    344  -1010       N  
ATOM   7842  CA  ILE D 676    -111.383  12.529 -35.866  1.00 60.06           C  
ANISOU 7842  CA  ILE D 676     7545   8371   6903    215    374   -880       C  
ATOM   7843  C   ILE D 676    -111.491  13.266 -37.187  1.00 57.77           C  
ANISOU 7843  C   ILE D 676     7173   8279   6497    287    383   -858       C  
ATOM   7844  O   ILE D 676    -112.211  14.256 -37.269  1.00 53.84           O  
ANISOU 7844  O   ILE D 676     6646   7830   5980    262    396   -785       O  
ATOM   7845  CB  ILE D 676    -110.552  13.312 -34.812  1.00 58.04           C  
ANISOU 7845  CB  ILE D 676     7317   8039   6697    183    408   -742       C  
ATOM   7846  CG1 ILE D 676    -109.122  13.546 -35.235  1.00 57.75           C  
ANISOU 7846  CG1 ILE D 676     7252   8079   6612    255    430   -685       C  
ATOM   7847  CG2 ILE D 676    -110.590  12.591 -33.471  1.00 57.84           C  
ANISOU 7847  CG2 ILE D 676     7367   7834   6777    115    400   -760       C  
ATOM   7848  CD1 ILE D 676    -108.374  14.217 -34.100  1.00 61.07           C  
ANISOU 7848  CD1 ILE D 676     7699   8408   7096    215    455   -568       C  
ATOM   7849  N   PHE D 677    -110.804  12.776 -38.218  1.00 63.95           N  
ANISOU 7849  N   PHE D 677     7916   9184   7200    380    375   -920       N  
ATOM   7850  CA  PHE D 677    -110.924  13.356 -39.569  1.00 65.26           C  
ANISOU 7850  CA  PHE D 677     7992   9564   7239    462    383   -905       C  
ATOM   7851  C   PHE D 677    -111.821  12.537 -40.508  1.00 68.23           C  
ANISOU 7851  C   PHE D 677     8336  10027   7560    502    339  -1073       C  
ATOM   7852  O   PHE D 677    -111.776  12.711 -41.722  1.00 69.32           O  
ANISOU 7852  O   PHE D 677     8397  10362   7580    592    338  -1095       O  
ATOM   7853  CB  PHE D 677    -109.546  13.550 -40.189  1.00 65.26           C  
ANISOU 7853  CB  PHE D 677     7946   9687   7164    553    408   -844       C  
ATOM   7854  CG  PHE D 677    -108.813  14.741 -39.668  1.00 61.21           C  
ANISOU 7854  CG  PHE D 677     7425   9157   6677    527    454   -658       C  
ATOM   7855  CD1 PHE D 677    -109.230  16.017 -39.994  1.00 61.16           C  
ANISOU 7855  CD1 PHE D 677     7364   9234   6639    521    480   -530       C  
ATOM   7856  CD2 PHE D 677    -107.688  14.588 -38.881  1.00 59.90           C  
ANISOU 7856  CD2 PHE D 677     7298   8890   6569    514    468   -612       C  
ATOM   7857  CE1 PHE D 677    -108.549  17.130 -39.529  1.00 60.10           C  
ANISOU 7857  CE1 PHE D 677     7216   9072   6546    495    517   -362       C  
ATOM   7858  CE2 PHE D 677    -106.993  15.692 -38.420  1.00 57.09           C  
ANISOU 7858  CE2 PHE D 677     6926   8520   6246    490    505   -450       C  
ATOM   7859  CZ  PHE D 677    -107.423  16.967 -38.742  1.00 58.14           C  
ANISOU 7859  CZ  PHE D 677     7004   8724   6360    478    528   -326       C  
ATOM   7860  N   ASP D 678    -112.687  11.703 -39.934  1.00 70.52           N  
ANISOU 7860  N   ASP D 678     8678  10176   7939    432    303  -1184       N  
ATOM   7861  CA  ASP D 678    -113.585  10.850 -40.705  1.00 71.55           C  
ANISOU 7861  CA  ASP D 678     8781  10361   8045    456    254  -1358       C  
ATOM   7862  C   ASP D 678    -114.701  11.662 -41.385  1.00 72.35           C  
ANISOU 7862  C   ASP D 678     8819  10603   8068    460    255  -1339       C  
ATOM   7863  O   ASP D 678    -115.675  12.071 -40.752  1.00 72.56           O  
ANISOU 7863  O   ASP D 678     8869  10550   8151    374    258  -1300       O  
ATOM   7864  CB  ASP D 678    -114.179   9.776 -39.791  1.00 73.95           C  
ANISOU 7864  CB  ASP D 678     9155  10456   8487    366    218  -1460       C  
ATOM   7865  CG  ASP D 678    -114.860   8.657 -40.558  1.00 77.46           C  
ANISOU 7865  CG  ASP D 678     9571  10926   8932    394    158  -1664       C  
ATOM   7866  OD1 ASP D 678    -115.485   8.924 -41.600  1.00 78.68           O  
ANISOU 7866  OD1 ASP D 678     9655  11251   8989    446    142  -1723       O  
ATOM   7867  OD2 ASP D 678    -114.763   7.500 -40.115  1.00 79.25           O  
ANISOU 7867  OD2 ASP D 678     9845  11001   9265    366    124  -1767       O  
ATOM   7868  N   VAL D 679    -114.554  11.843 -42.695  1.00 74.33           N  
ANISOU 7868  N   VAL D 679     8987  11072   8184    567    252  -1371       N  
ATOM   7869  CA  VAL D 679    -115.493  12.618 -43.516  1.00 72.43           C  
ANISOU 7869  CA  VAL D 679     8672  11001   7846    596    255  -1348       C  
ATOM   7870  C   VAL D 679    -116.896  11.984 -43.543  1.00 69.19           C  
ANISOU 7870  C   VAL D 679     8264  10551   7475    545    206  -1499       C  
ATOM   7871  O   VAL D 679    -117.904  12.686 -43.506  1.00 63.02           O  
ANISOU 7871  O   VAL D 679     7464   9800   6682    505    213  -1451       O  
ATOM   7872  CB  VAL D 679    -114.932  12.763 -44.953  1.00 74.71           C  
ANISOU 7872  CB  VAL D 679     8864  11550   7972    737    259  -1363       C  
ATOM   7873  CG1 VAL D 679    -115.952  13.395 -45.888  1.00 75.88           C  
ANISOU 7873  CG1 VAL D 679     8929  11890   8011    780    255  -1361       C  
ATOM   7874  CG2 VAL D 679    -113.655  13.587 -44.919  1.00 74.31           C  
ANISOU 7874  CG2 VAL D 679     8799  11549   7886    777    314  -1181       C  
ATOM   7875  N   GLU D 680    -116.955  10.657 -43.587  1.00 68.83           N  
ANISOU 7875  N   GLU D 680     8240  10430   7484    544    154  -1682       N  
ATOM   7876  CA  GLU D 680    -118.239   9.959 -43.547  1.00 68.13           C  
ANISOU 7876  CA  GLU D 680     8150  10279   7456    485    104  -1830       C  
ATOM   7877  C   GLU D 680    -118.965  10.227 -42.212  1.00 67.78           C  
ANISOU 7877  C   GLU D 680     8175  10038   7540    346    121  -1744       C  
ATOM   7878  O   GLU D 680    -120.185  10.399 -42.211  1.00 62.03           O  
ANISOU 7878  O   GLU D 680     7426   9322   6820    296    105  -1775       O  
ATOM   7879  CB  GLU D 680    -118.079   8.443 -43.797  1.00 66.35           C  
ANISOU 7879  CB  GLU D 680     7935   9985   7292    507     42  -2042       C  
ATOM   7880  N   SER D 681    -118.226  10.292 -41.094  1.00 63.59           N  
ANISOU 7880  N   SER D 681     7719   9344   7099    291    152  -1637       N  
ATOM   7881  CA  SER D 681    -118.825  10.665 -39.801  1.00 62.86           C  
ANISOU 7881  CA  SER D 681     7684   9090   7109    173    173  -1540       C  
ATOM   7882  C   SER D 681    -119.375  12.078 -39.814  1.00 59.60           C  
ANISOU 7882  C   SER D 681     7240   8772   6634    164    208  -1404       C  
ATOM   7883  O   SER D 681    -120.433  12.332 -39.251  1.00 55.88           O  
ANISOU 7883  O   SER D 681     6779   8245   6208     87    206  -1388       O  
ATOM   7884  CB  SER D 681    -117.842  10.535 -38.653  1.00 61.10           C  
ANISOU 7884  CB  SER D 681     7537   8703   6976    133    200  -1449       C  
ATOM   7885  OG  SER D 681    -117.580   9.168 -38.400  1.00 62.58           O  
ANISOU 7885  OG  SER D 681     7762   8761   7253    118    165  -1569       O  
ATOM   7886  N   MET D 682    -118.664  12.986 -40.474  1.00 58.02           N  
ANISOU 7886  N   MET D 682     6998   8716   6332    245    240  -1304       N  
ATOM   7887  CA  MET D 682    -119.147  14.359 -40.646  1.00 59.71           C  
ANISOU 7887  CA  MET D 682     7172   9028   6486    250    271  -1172       C  
ATOM   7888  C   MET D 682    -120.490  14.389 -41.392  1.00 60.47           C  
ANISOU 7888  C   MET D 682     7210   9244   6522    260    243  -1258       C  
ATOM   7889  O   MET D 682    -121.450  15.001 -40.930  1.00 60.07           O  
ANISOU 7889  O   MET D 682     7163   9165   6497    201    248  -1208       O  
ATOM   7890  CB  MET D 682    -118.109  15.207 -41.382  1.00 60.11           C  
ANISOU 7890  CB  MET D 682     7175   9223   6442    344    307  -1053       C  
ATOM   7891  CG  MET D 682    -116.792  15.388 -40.632  1.00 62.56           C  
ANISOU 7891  CG  MET D 682     7533   9428   6810    332    339   -949       C  
ATOM   7892  SD  MET D 682    -115.580  16.249 -41.646  1.00 64.75           S  
ANISOU 7892  SD  MET D 682     7736   9892   6974    444    379   -818       S  
ATOM   7893  CE  MET D 682    -114.038  15.602 -41.031  1.00 61.58           C  
ANISOU 7893  CE  MET D 682     7389   9379   6631    448    389   -813       C  
ATOM   7894  N   LYS D 683    -120.568  13.685 -42.515  1.00 62.09           N  
ANISOU 7894  N   LYS D 683     7360   9583   6648    335    208  -1397       N  
ATOM   7895  CA  LYS D 683    -121.804  13.637 -43.292  1.00 63.46           C  
ANISOU 7895  CA  LYS D 683     7470   9885   6758    353    176  -1497       C  
ATOM   7896  C   LYS D 683    -122.938  12.930 -42.564  1.00 62.80           C  
ANISOU 7896  C   LYS D 683     7421   9657   6784    245    141  -1601       C  
ATOM   7897  O   LYS D 683    -124.066  13.397 -42.610  1.00 63.92           O  
ANISOU 7897  O   LYS D 683     7532   9846   6906    214    135  -1597       O  
ATOM   7898  CB  LYS D 683    -121.562  12.962 -44.636  1.00 66.56           C  
ANISOU 7898  CB  LYS D 683     7791  10459   7041    465    141  -1642       C  
ATOM   7899  N   LYS D 684    -122.642  11.815 -41.898  1.00 66.53           N  
ANISOU 7899  N   LYS D 684     7953   9955   7372    188    117  -1687       N  
ATOM   7900  CA  LYS D 684    -123.651  11.092 -41.130  1.00 69.85           C  
ANISOU 7900  CA  LYS D 684     8403  10223   7913     78     87  -1768       C  
ATOM   7901  C   LYS D 684    -124.251  12.015 -40.095  1.00 71.25           C  
ANISOU 7901  C   LYS D 684     8612  10327   8132     -5    124  -1623       C  
ATOM   7902  O   LYS D 684    -125.456  12.043 -39.923  1.00 73.86           O  
ANISOU 7902  O   LYS D 684     8922  10655   8484    -64    108  -1657       O  
ATOM   7903  CB  LYS D 684    -123.058   9.888 -40.383  1.00 74.41           C  
ANISOU 7903  CB  LYS D 684     9047  10601   8624     27     69  -1831       C  
ATOM   7904  CG  LYS D 684    -124.075   8.851 -39.935  1.00 81.98           C  
ANISOU 7904  CG  LYS D 684    10014  11427   9707    -68     24  -1952       C  
ATOM   7905  CD  LYS D 684    -123.452   7.864 -38.956  1.00 90.21           C  
ANISOU 7905  CD  LYS D 684    11131  12251  10895   -128     20  -1957       C  
ATOM   7906  CE  LYS D 684    -124.457   6.808 -38.500  1.00 97.32           C  
ANISOU 7906  CE  LYS D 684    12033  13010  11935   -228    -22  -2062       C  
ATOM   7907  NZ  LYS D 684    -123.940   5.951 -37.389  1.00 98.52           N  
ANISOU 7907  NZ  LYS D 684    12257  12940  12237   -296    -18  -2028       N  
ATOM   7908  N   ALA D 685    -123.399  12.756 -39.389  1.00 70.39           N  
ANISOU 7908  N   ALA D 685     8550  10159   8038     -9    170  -1467       N  
ATOM   7909  CA  ALA D 685    -123.856  13.698 -38.383  1.00 69.06           C  
ANISOU 7909  CA  ALA D 685     8409   9924   7907    -76    202  -1333       C  
ATOM   7910  C   ALA D 685    -124.859  14.652 -39.014  1.00 68.11           C  
ANISOU 7910  C   ALA D 685     8225   9955   7698    -50    204  -1306       C  
ATOM   7911  O   ALA D 685    -125.912  14.896 -38.439  1.00 64.74           O  
ANISOU 7911  O   ALA D 685     7798   9492   7307   -116    200  -1295       O  
ATOM   7912  CB  ALA D 685    -122.683  14.469 -37.784  1.00 67.92           C  
ANISOU 7912  CB  ALA D 685     8305   9729   7773    -59    245  -1181       C  
ATOM   7913  N   MET D 686    -124.524  15.183 -40.192  1.00 67.73           N  
ANISOU 7913  N   MET D 686     8117  10085   7532     52    210  -1289       N  
ATOM   7914  CA  MET D 686    -125.398  16.142 -40.884  1.00 68.27           C  
ANISOU 7914  CA  MET D 686     8119  10314   7507     92    214  -1249       C  
ATOM   7915  C   MET D 686    -126.722  15.498 -41.324  1.00 69.67           C  
ANISOU 7915  C   MET D 686     8252  10551   7669     69    170  -1401       C  
ATOM   7916  O   MET D 686    -127.793  16.107 -41.221  1.00 65.92           O  
ANISOU 7916  O   MET D 686     7750  10118   7177     43    170  -1374       O  
ATOM   7917  CB  MET D 686    -124.673  16.784 -42.072  1.00 67.14           C  
ANISOU 7917  CB  MET D 686     7915  10358   7238    213    234  -1186       C  
ATOM   7918  CG  MET D 686    -123.532  17.703 -41.649  1.00 66.02           C  
ANISOU 7918  CG  MET D 686     7801  10169   7114    229    281  -1009       C  
ATOM   7919  SD  MET D 686    -122.525  18.366 -42.984  1.00 67.20           S  
ANISOU 7919  SD  MET D 686     7874  10529   7129    365    310   -915       S  
ATOM   7920  CE  MET D 686    -123.699  19.582 -43.630  1.00 69.62           C  
ANISOU 7920  CE  MET D 686     8105  10995   7352    403    319   -832       C  
ATOM   7921  N   VAL D 687    -126.654  14.245 -41.760  1.00 67.58           N  
ANISOU 7921  N   VAL D 687     7979  10278   7420     75    128  -1565       N  
ATOM   7922  CA  VAL D 687    -127.863  13.524 -42.094  1.00 67.85           C  
ANISOU 7922  CA  VAL D 687     7971  10345   7466     41     80  -1722       C  
ATOM   7923  C   VAL D 687    -128.708  13.360 -40.837  1.00 69.74           C  
ANISOU 7923  C   VAL D 687     8255  10415   7827    -87     80  -1703       C  
ATOM   7924  O   VAL D 687    -129.901  13.632 -40.869  1.00 64.55           O  
ANISOU 7924  O   VAL D 687     7559   9813   7155   -120     68  -1725       O  
ATOM   7925  CB  VAL D 687    -127.565  12.167 -42.756  1.00 71.61           C  
ANISOU 7925  CB  VAL D 687     8428  10823   7958     71     28  -1913       C  
ATOM   7926  CG1 VAL D 687    -128.818  11.310 -42.821  1.00 72.29           C  
ANISOU 7926  CG1 VAL D 687     8480  10883   8104      6    -26  -2078       C  
ATOM   7927  CG2 VAL D 687    -126.990  12.388 -44.148  1.00 70.12           C  
ANISOU 7927  CG2 VAL D 687     8170  10855   7617    212     24  -1949       C  
ATOM   7928  N   GLU D 688    -128.097  12.961 -39.722  1.00 70.99           N  
ANISOU 7928  N   GLU D 688     8491  10383   8100   -155     96  -1652       N  
ATOM   7929  CA  GLU D 688    -128.845  12.797 -38.465  1.00 71.69           C  
ANISOU 7929  CA  GLU D 688     8617  10322   8299   -272    101  -1619       C  
ATOM   7930  C   GLU D 688    -129.466  14.094 -37.965  1.00 68.64           C  
ANISOU 7930  C   GLU D 688     8225   9979   7877   -288    134  -1486       C  
ATOM   7931  O   GLU D 688    -130.510  14.060 -37.323  1.00 67.71           O  
ANISOU 7931  O   GLU D 688     8101   9818   7806   -364    128  -1491       O  
ATOM   7932  CB  GLU D 688    -127.988  12.150 -37.377  1.00 76.10           C  
ANISOU 7932  CB  GLU D 688     9255  10686   8975   -328    115  -1578       C  
ATOM   7933  CG  GLU D 688    -127.933  10.629 -37.523  1.00 81.69           C  
ANISOU 7933  CG  GLU D 688     9967  11297   9773   -359     70  -1729       C  
ATOM   7934  CD  GLU D 688    -127.083   9.920 -36.461  1.00 86.19           C  
ANISOU 7934  CD  GLU D 688    10614  11673  10462   -410     84  -1685       C  
ATOM   7935  OE1 GLU D 688    -125.959   9.463 -36.788  1.00 88.25           O  
ANISOU 7935  OE1 GLU D 688    10898  11909  10722   -352     80  -1714       O  
ATOM   7936  OE2 GLU D 688    -127.545   9.802 -35.291  1.00 84.38           O  
ANISOU 7936  OE2 GLU D 688    10416  11322  10324   -502     99  -1619       O  
ATOM   7937  N   TYR D 689    -128.864  15.236 -38.289  1.00 68.65           N  
ANISOU 7937  N   TYR D 689     8221  10067   7797   -213    166  -1371       N  
ATOM   7938  CA  TYR D 689    -129.472  16.528 -37.961  1.00 69.69           C  
ANISOU 7938  CA  TYR D 689     8339  10247   7894   -213    190  -1254       C  
ATOM   7939  C   TYR D 689    -130.560  16.920 -38.945  1.00 70.81           C  
ANISOU 7939  C   TYR D 689     8401  10563   7940   -170    171  -1304       C  
ATOM   7940  O   TYR D 689    -131.167  17.954 -38.779  1.00 66.63           O  
ANISOU 7940  O   TYR D 689     7853  10084   7379   -163    186  -1220       O  
ATOM   7941  CB  TYR D 689    -128.435  17.646 -37.916  1.00 69.17           C  
ANISOU 7941  CB  TYR D 689     8291  10193   7797   -153    230  -1104       C  
ATOM   7942  CG  TYR D 689    -127.517  17.609 -36.721  1.00 67.83           C  
ANISOU 7942  CG  TYR D 689     8195   9856   7720   -199    253  -1027       C  
ATOM   7943  CD1 TYR D 689    -128.017  17.603 -35.412  1.00 66.81           C  
ANISOU 7943  CD1 TYR D 689     8105   9604   7675   -285    257   -999       C  
ATOM   7944  CD2 TYR D 689    -126.143  17.634 -36.899  1.00 67.17           C  
ANISOU 7944  CD2 TYR D 689     8135   9753   7632   -151    271   -978       C  
ATOM   7945  CE1 TYR D 689    -127.162  17.586 -34.324  1.00 63.42           C  
ANISOU 7945  CE1 TYR D 689     7738   9039   7320   -317    277   -930       C  
ATOM   7946  CE2 TYR D 689    -125.285  17.624 -35.829  1.00 63.91           C  
ANISOU 7946  CE2 TYR D 689     7785   9198   7299   -188    290   -911       C  
ATOM   7947  CZ  TYR D 689    -125.795  17.594 -34.551  1.00 63.85           C  
ANISOU 7947  CZ  TYR D 689     7815   9073   7370   -269    293   -889       C  
ATOM   7948  OH  TYR D 689    -124.917  17.590 -33.515  1.00 62.97           O  
ANISOU 7948  OH  TYR D 689     7760   8839   7327   -295    311   -825       O  
ATOM   7949  N   GLU D 690    -130.790  16.097 -39.969  1.00 76.77           N  
ANISOU 7949  N   GLU D 690     9108  11414   8649   -136    135  -1447       N  
ATOM   7950  CA  GLU D 690    -131.828  16.327 -40.974  1.00 74.66           C  
ANISOU 7950  CA  GLU D 690     8756  11327   8282    -89    111  -1517       C  
ATOM   7951  C   GLU D 690    -131.479  17.512 -41.853  1.00 71.88           C  
ANISOU 7951  C   GLU D 690     8361  11145   7807     23    137  -1409       C  
ATOM   7952  O   GLU D 690    -132.358  18.147 -42.431  1.00 72.89           O  
ANISOU 7952  O   GLU D 690     8427  11417   7853     63    132  -1401       O  
ATOM   7953  CB  GLU D 690    -133.208  16.518 -40.318  1.00 74.04           C  
ANISOU 7953  CB  GLU D 690     8665  11225   8243   -170    102  -1524       C  
ATOM   7954  N   ILE D 691    -130.186  17.786 -41.964  1.00 69.55           N  
ANISOU 7954  N   ILE D 691     8093  10833   7499     75    166  -1321       N  
ATOM   7955  CA  ILE D 691    -129.686  18.840 -42.815  1.00 71.48           C  
ANISOU 7955  CA  ILE D 691     8292  11230   7638    181    195  -1203       C  
ATOM   7956  C   ILE D 691    -129.806  18.397 -44.280  1.00 72.07           C  
ANISOU 7956  C   ILE D 691     8282  11517   7584    280    168  -1315       C  
ATOM   7957  O   ILE D 691    -129.584  17.236 -44.609  1.00 68.98           O  
ANISOU 7957  O   ILE D 691     7887  11121   7199    281    134  -1467       O  
ATOM   7958  CB  ILE D 691    -128.202  19.153 -42.458  1.00 70.96           C  
ANISOU 7958  CB  ILE D 691     8276  11077   7608    199    232  -1082       C  
ATOM   7959  CG1 ILE D 691    -128.017  19.522 -40.968  1.00 71.71           C  
ANISOU 7959  CG1 ILE D 691     8451  10965   7830    106    253   -989       C  
ATOM   7960  CG2 ILE D 691    -127.593  20.070 -43.523  1.00 71.59           C  
ANISOU 7960  CG2 ILE D 691     8293  11331   7575    316    260   -966       C  
ATOM   7961  CD1 ILE D 691    -128.482  20.888 -40.617  1.00 72.73           C  
ANISOU 7961  CD1 ILE D 691     8571  11103   7961    109    276   -850       C  
ATOM   7962  N   ASP D 692    -130.190  19.320 -45.155  1.00 74.20           N  
ANISOU 7962  N   ASP D 692     8479  11977   7738    367    180  -1243       N  
ATOM   7963  CA  ASP D 692    -130.286  19.016 -46.582  1.00 73.98           C  
ANISOU 7963  CA  ASP D 692     8359  12182   7568    477    158  -1336       C  
ATOM   7964  C   ASP D 692    -128.909  19.123 -47.224  1.00 73.12           C  
ANISOU 7964  C   ASP D 692     8236  12153   7395    570    185  -1264       C  
ATOM   7965  O   ASP D 692    -128.458  20.227 -47.548  1.00 66.30           O  
ANISOU 7965  O   ASP D 692     7344  11372   6475    634    228  -1086       O  
ATOM   7966  CB  ASP D 692    -131.272  19.942 -47.293  1.00 77.37           C  
ANISOU 7966  CB  ASP D 692     8707  12801   7887    542    162  -1281       C  
ATOM   7967  N   LEU D 693    -128.251  17.972 -47.389  1.00 75.77           N  
ANISOU 7967  N   LEU D 693     8587  12456   7746    575    158  -1401       N  
ATOM   7968  CA  LEU D 693    -126.891  17.907 -47.933  1.00 81.85           C  
ANISOU 7968  CA  LEU D 693     9345  13294   8460    660    180  -1353       C  
ATOM   7969  C   LEU D 693    -126.853  18.275 -49.432  1.00 86.90           C  
ANISOU 7969  C   LEU D 693     9870  14235   8914    809    183  -1343       C  
ATOM   7970  O   LEU D 693    -125.797  18.623 -49.962  1.00 85.34           O  
ANISOU 7970  O   LEU D 693     9642  14137   8647    894    217  -1240       O  
ATOM   7971  CB  LEU D 693    -126.259  16.515 -47.694  1.00 79.84           C  
ANISOU 7971  CB  LEU D 693     9137  12923   8276    630    145  -1518       C  
ATOM   7972  N   GLN D 694    -127.996  18.207 -50.114  1.00 89.13           N  
ANISOU 7972  N   GLN D 694    10081  14673   9113    845    150  -1444       N  
ATOM   7973  CA  GLN D 694    -128.066  18.651 -51.502  1.00 92.77           C  
ANISOU 7973  CA  GLN D 694    10425  15436   9388    992    155  -1420       C  
ATOM   7974  C   GLN D 694    -127.941  20.169 -51.550  1.00 89.89           C  
ANISOU 7974  C   GLN D 694    10037  15130   8986   1028    218  -1157       C  
ATOM   7975  O   GLN D 694    -127.181  20.691 -52.352  1.00 89.62           O  
ANISOU 7975  O   GLN D 694     9940  15266   8845   1136    253  -1036       O  
ATOM   7976  CB  GLN D 694    -129.350  18.174 -52.196  1.00 92.63           C  
ANISOU 7976  CB  GLN D 694    10332  15573   9290   1022     99  -1606       C  
ATOM   7977  N   LYS D 695    -128.671  20.873 -50.685  1.00 87.62           N  
ANISOU 7977  N   LYS D 695     9798  14702   8793    939    231  -1067       N  
ATOM   7978  CA  LYS D 695    -128.645  22.346 -50.680  1.00 86.17           C  
ANISOU 7978  CA  LYS D 695     9593  14551   8596    969    283   -824       C  
ATOM   7979  C   LYS D 695    -127.468  22.923 -49.878  1.00 85.83           C  
ANISOU 7979  C   LYS D 695     9619  14327   8664    924    329   -648       C  
ATOM   7980  O   LYS D 695    -126.984  24.015 -50.173  1.00 79.52           O  
ANISOU 7980  O   LYS D 695     8783  13589   7840    979    375   -442       O  
ATOM   7981  CB  LYS D 695    -129.976  22.906 -50.160  1.00 86.33           C  
ANISOU 7981  CB  LYS D 695     9625  14516   8662    909    272   -812       C  
ATOM   7982  N   MET D 696    -126.999  22.191 -48.868  1.00 86.06           N  
ANISOU 7982  N   MET D 696     9743  14134   8820    824    317   -725       N  
ATOM   7983  CA  MET D 696    -125.849  22.635 -48.068  1.00 86.67           C  
ANISOU 7983  CA  MET D 696     9886  14040   9005    779    356   -580       C  
ATOM   7984  C   MET D 696    -124.848  21.510 -47.817  1.00 81.01           C  
ANISOU 7984  C   MET D 696     9218  13235   8326    757    343   -689       C  
ATOM   7985  O   MET D 696    -124.835  20.926 -46.741  1.00 73.33           O  
ANISOU 7985  O   MET D 696     8333  12051   7477    654    327   -761       O  
ATOM   7986  CB  MET D 696    -126.300  23.225 -46.725  1.00 87.45           C  
ANISOU 7986  CB  MET D 696    10064  13911   9251    665    362   -512       C  
ATOM   7987  CG  MET D 696    -125.162  23.905 -45.967  1.00 90.37           C  
ANISOU 7987  CG  MET D 696    10485  14127   9726    631    400   -348       C  
ATOM   7988  SD  MET D 696    -125.756  24.805 -44.509  1.00 95.08           S  
ANISOU 7988  SD  MET D 696    11153  14497  10476    523    404   -263       S  
ATOM   7989  CE  MET D 696    -125.823  26.481 -45.145  1.00 97.59           C  
ANISOU 7989  CE  MET D 696    11394  14924  10761    603    440    -35       C  
ATOM   7990  N   PRO D 697    -123.989  21.216 -48.803  1.00 80.73           N  
ANISOU 7990  N   PRO D 697     9124  13367   8184    860    352   -694       N  
ATOM   7991  CA  PRO D 697    -122.968  20.179 -48.591  1.00 78.41           C  
ANISOU 7991  CA  PRO D 697     8875  12994   7925    850    340   -793       C  
ATOM   7992  C   PRO D 697    -121.897  20.580 -47.584  1.00 72.58           C  
ANISOU 7992  C   PRO D 697     8210  12059   7309    785    377   -655       C  
ATOM   7993  O   PRO D 697    -121.799  21.762 -47.242  1.00 71.42           O  
ANISOU 7993  O   PRO D 697     8064  11869   7205    767    414   -467       O  
ATOM   7994  CB  PRO D 697    -122.330  20.030 -49.969  1.00 79.09           C  
ANISOU 7994  CB  PRO D 697     8861  13344   7847    994    347   -799       C  
ATOM   7995  CG  PRO D 697    -122.584  21.333 -50.652  1.00 79.09           C  
ANISOU 7995  CG  PRO D 697     8778  13515   7757   1066    387   -606       C  
ATOM   7996  CD  PRO D 697    -123.916  21.797 -50.155  1.00 79.46           C  
ANISOU 7996  CD  PRO D 697     8847  13486   7858    996    372   -609       C  
ATOM   7997  N   LEU D 698    -121.122  19.588 -47.126  1.00 71.45           N  
ANISOU 7997  N   LEU D 698     8125  11797   7224    754    362   -754       N  
ATOM   7998  CA  LEU D 698    -119.972  19.789 -46.224  1.00 70.62           C  
ANISOU 7998  CA  LEU D 698     8087  11523   7224    703    392   -647       C  
ATOM   7999  C   LEU D 698    -119.107  20.974 -46.659  1.00 73.04           C  
ANISOU 7999  C   LEU D 698     8337  11926   7489    765    445   -427       C  
ATOM   8000  O   LEU D 698    -118.783  21.838 -45.844  1.00 71.34           O  
ANISOU 8000  O   LEU D 698     8159  11573   7376    705    474   -280       O  
ATOM   8001  CB  LEU D 698    -119.115  18.513 -46.103  1.00 69.23           C  
ANISOU 8001  CB  LEU D 698     7950  11285   7068    707    370   -784       C  
ATOM   8002  N   GLY D 699    -118.802  21.057 -47.953  1.00 74.58           N  
ANISOU 8002  N   GLY D 699     8434  12366   7537    885    457   -403       N  
ATOM   8003  CA  GLY D 699    -117.973  22.138 -48.471  1.00 75.51           C  
ANISOU 8003  CA  GLY D 699     8483  12596   7610    950    510   -183       C  
ATOM   8004  C   GLY D 699    -118.579  23.536 -48.407  1.00 80.30           C  
ANISOU 8004  C   GLY D 699     9060  13203   8248    935    538      2       C  
ATOM   8005  O   GLY D 699    -117.853  24.524 -48.502  1.00 81.34           O  
ANISOU 8005  O   GLY D 699     9153  13349   8402    955    582    206       O  
ATOM   8006  N   LYS D 700    -119.898  23.636 -48.245  1.00 85.64           N  
ANISOU 8006  N   LYS D 700     9748  13858   8931    901    512    -64       N  
ATOM   8007  CA  LYS D 700    -120.594  24.925 -48.297  1.00 89.80           C  
ANISOU 8007  CA  LYS D 700    10239  14405   9475    902    533     95       C  
ATOM   8008  C   LYS D 700    -120.849  25.547 -46.923  1.00 92.76           C  
ANISOU 8008  C   LYS D 700    10701  14522  10023    785    532    154       C  
ATOM   8009  O   LYS D 700    -121.201  26.725 -46.847  1.00 92.42           O  
ANISOU 8009  O   LYS D 700    10632  14462  10022    784    551    306       O  
ATOM   8010  CB  LYS D 700    -121.919  24.786 -49.059  1.00 94.09           C  
ANISOU 8010  CB  LYS D 700    10728  15117   9905    953    505      0       C  
ATOM   8011  N   LEU D 701    -120.701  24.773 -45.847  1.00 92.42           N  
ANISOU 8011  N   LEU D 701    10753  14282  10080    692    508     33       N  
ATOM   8012  CA  LEU D 701    -120.820  25.321 -44.484  1.00 88.04           C  
ANISOU 8012  CA  LEU D 701    10277  13492   9683    588    508     83       C  
ATOM   8013  C   LEU D 701    -119.898  26.540 -44.279  1.00 86.65           C  
ANISOU 8013  C   LEU D 701    10081  13259   9585    591    546    297       C  
ATOM   8014  O   LEU D 701    -118.709  26.473 -44.583  1.00 84.36           O  
ANISOU 8014  O   LEU D 701     9768  13003   9282    625    571    363       O  
ATOM   8015  CB  LEU D 701    -120.531  24.221 -43.459  1.00 85.51           C  
ANISOU 8015  CB  LEU D 701    10050  12997   9442    505    484    -61       C  
ATOM   8016  N   SER D 702    -120.453  27.658 -43.797  1.00 83.73           N  
ANISOU 8016  N   SER D 702     9712  12805   9298    560    549    403       N  
ATOM   8017  CA  SER D 702    -119.675  28.895 -43.642  1.00 83.71           C  
ANISOU 8017  CA  SER D 702     9680  12739   9387    562    580    606       C  
ATOM   8018  C   SER D 702    -119.811  29.500 -42.242  1.00 84.74           C  
ANISOU 8018  C   SER D 702     9879  12634   9683    470    564    623       C  
ATOM   8019  O   SER D 702    -120.891  29.479 -41.651  1.00 89.05           O  
ANISOU 8019  O   SER D 702    10465  13115  10254    428    536    538       O  
ATOM   8020  CB  SER D 702    -120.103  29.922 -44.698  1.00 83.47           C  
ANISOU 8020  CB  SER D 702     9552  12870   9294    645    602    761       C  
ATOM   8021  OG  SER D 702    -120.927  30.941 -44.162  1.00 80.27           O  
ANISOU 8021  OG  SER D 702     9155  12362   8981    613    591    827       O  
ATOM   8022  N   LYS D 703    -118.717  30.074 -41.743  1.00 81.40           N  
ANISOU 8022  N   LYS D 703     9462  12097   9369    444    580    734       N  
ATOM   8023  CA  LYS D 703    -118.699  30.726 -40.431  1.00 75.04           C  
ANISOU 8023  CA  LYS D 703     8710  11077   8723    367    563    752       C  
ATOM   8024  C   LYS D 703    -119.743  31.840 -40.337  1.00 75.28           C  
ANISOU 8024  C   LYS D 703     8718  11082   8805    371    550    819       C  
ATOM   8025  O   LYS D 703    -120.390  32.003 -39.300  1.00 81.57           O  
ANISOU 8025  O   LYS D 703     9567  11745   9679    315    521    748       O  
ATOM   8026  CB  LYS D 703    -117.302  31.263 -40.078  1.00 72.73           C  
ANISOU 8026  CB  LYS D 703     8408  10688   8539    349    581    871       C  
ATOM   8027  N   ARG D 704    -119.931  32.594 -41.420  1.00 72.50           N  
ANISOU 8027  N   ARG D 704     8281  10863   8403    444    572    956       N  
ATOM   8028  CA  ARG D 704    -120.841  33.745 -41.389  1.00 66.68           C  
ANISOU 8028  CA  ARG D 704     7514  10098   7724    458    561   1040       C  
ATOM   8029  C   ARG D 704    -122.316  33.323 -41.397  1.00 63.68           C  
ANISOU 8029  C   ARG D 704     7155   9781   7259    461    535    906       C  
ATOM   8030  O   ARG D 704    -123.163  33.975 -40.753  1.00 62.46           O  
ANISOU 8030  O   ARG D 704     7020   9535   7178    437    510    898       O  
ATOM   8031  CB  ARG D 704    -120.547  34.689 -42.557  1.00 65.40           C  
ANISOU 8031  CB  ARG D 704     7249  10060   7539    538    596   1248       C  
ATOM   8032  N   GLN D 705    -122.633  32.250 -42.122  1.00 61.66           N  
ANISOU 8032  N   GLN D 705     6891   9684   6852    493    537    798       N  
ATOM   8033  CA  GLN D 705    -124.009  31.723 -42.120  1.00 62.90           C  
ANISOU 8033  CA  GLN D 705     7064   9902   6931    487    510    655       C  
ATOM   8034  C   GLN D 705    -124.351  31.188 -40.726  1.00 60.84           C  
ANISOU 8034  C   GLN D 705     6896   9466   6754    391    479    513       C  
ATOM   8035  O   GLN D 705    -125.442  31.454 -40.181  1.00 56.75           O  
ANISOU 8035  O   GLN D 705     6397   8905   6261    365    455    461       O  
ATOM   8036  CB  GLN D 705    -124.185  30.618 -43.185  1.00 60.02           C  
ANISOU 8036  CB  GLN D 705     6668   9739   6400    540    513    552       C  
ATOM   8037  N   ILE D 706    -123.409  30.461 -40.139  1.00 60.94           N  
ANISOU 8037  N   ILE D 706     6962   9386   6808    343    481    458       N  
ATOM   8038  CA  ILE D 706    -123.634  29.870 -38.824  1.00 64.42           C  
ANISOU 8038  CA  ILE D 706     7484   9672   7319    258    456    334       C  
ATOM   8039  C   ILE D 706    -123.823  30.965 -37.762  1.00 60.94           C  
ANISOU 8039  C   ILE D 706     7065   9078   7011    221    441    394       C  
ATOM   8040  O   ILE D 706    -124.741  30.887 -36.948  1.00 59.11           O  
ANISOU 8040  O   ILE D 706     6868   8787   6804    179    417    309       O  
ATOM   8041  CB  ILE D 706    -122.517  28.870 -38.455  1.00 64.38           C  
ANISOU 8041  CB  ILE D 706     7528   9605   7328    223    462    273       C  
ATOM   8042  CG1 ILE D 706    -122.644  27.616 -39.344  1.00 67.91           C  
ANISOU 8042  CG1 ILE D 706     7963  10191   7649    253    462    161       C  
ATOM   8043  CG2 ILE D 706    -122.597  28.479 -36.987  1.00 63.07           C  
ANISOU 8043  CG2 ILE D 706     7441   9270   7254    139    442    186       C  
ATOM   8044  CD1 ILE D 706    -121.407  26.739 -39.389  1.00 68.50           C  
ANISOU 8044  CD1 ILE D 706     8062  10248   7716    252    473    128       C  
ATOM   8045  N   GLN D 707    -122.991  31.997 -37.814  1.00 58.77           N  
ANISOU 8045  N   GLN D 707     6760   8749   6821    242    455    539       N  
ATOM   8046  CA  GLN D 707    -123.126  33.129 -36.921  1.00 60.31           C  
ANISOU 8046  CA  GLN D 707     6963   8801   7152    220    436    596       C  
ATOM   8047  C   GLN D 707    -124.516  33.763 -37.038  1.00 63.18           C  
ANISOU 8047  C   GLN D 707     7301   9207   7496    245    417    593       C  
ATOM   8048  O   GLN D 707    -125.141  34.103 -36.021  1.00 62.94           O  
ANISOU 8048  O   GLN D 707     7303   9076   7536    211    388    536       O  
ATOM   8049  CB  GLN D 707    -122.028  34.128 -37.217  1.00 60.99           C  
ANISOU 8049  CB  GLN D 707     7002   8840   7331    245    454    763       C  
ATOM   8050  CG  GLN D 707    -122.078  35.424 -36.433  1.00 66.42           C  
ANISOU 8050  CG  GLN D 707     7683   9375   8177    231    430    833       C  
ATOM   8051  CD  GLN D 707    -120.920  36.334 -36.855  1.00 70.78           C  
ANISOU 8051  CD  GLN D 707     8179   9885   8829    252    450   1007       C  
ATOM   8052  OE1 GLN D 707    -119.916  35.860 -37.385  1.00 73.26           O  
ANISOU 8052  OE1 GLN D 707     8478  10255   9104    259    480   1053       O  
ATOM   8053  NE2 GLN D 707    -121.049  37.626 -36.620  1.00 71.59           N  
ANISOU 8053  NE2 GLN D 707     8248   9887   9067    261    431   1104       N  
ATOM   8054  N   ALA D 708    -125.014  33.906 -38.266  1.00 63.93           N  
ANISOU 8054  N   ALA D 708     7335   9464   7491    311    433    649       N  
ATOM   8055  CA  ALA D 708    -126.349  34.492 -38.476  1.00 63.55           C  
ANISOU 8055  CA  ALA D 708     7258   9475   7414    344    416    649       C  
ATOM   8056  C   ALA D 708    -127.464  33.571 -37.952  1.00 59.47           C  
ANISOU 8056  C   ALA D 708     6784   8982   6830    302    392    473       C  
ATOM   8057  O   ALA D 708    -128.497  34.033 -37.425  1.00 63.20           O  
ANISOU 8057  O   ALA D 708     7260   9426   7328    295    368    438       O  
ATOM   8058  CB  ALA D 708    -126.559  34.800 -39.949  1.00 66.52           C  
ANISOU 8058  CB  ALA D 708     7552  10036   7685    432    441    753       C  
ATOM   8059  N   ALA D 709    -127.242  32.268 -38.080  1.00 55.54           N  
ANISOU 8059  N   ALA D 709     6314   8533   6255    273    398    363       N  
ATOM   8060  CA  ALA D 709    -128.155  31.269 -37.533  1.00 54.88           C  
ANISOU 8060  CA  ALA D 709     6271   8454   6127    219    377    201       C  
ATOM   8061  C   ALA D 709    -128.220  31.336 -35.987  1.00 55.05           C  
ANISOU 8061  C   ALA D 709     6354   8306   6255    148    356    148       C  
ATOM   8062  O   ALA D 709    -129.312  31.236 -35.407  1.00 51.07           O  
ANISOU 8062  O   ALA D 709     5861   7799   5744    120    335     69       O  
ATOM   8063  CB  ALA D 709    -127.745  29.877 -37.997  1.00 54.55           C  
ANISOU 8063  CB  ALA D 709     6244   8478   6004    205    385    103       C  
ATOM   8064  N   TYR D 710    -127.067  31.531 -35.337  1.00 50.37           N  
ANISOU 8064  N   TYR D 710     5794   7587   5757    123    362    193       N  
ATOM   8065  CA  TYR D 710    -127.032  31.756 -33.889  1.00 50.91           C  
ANISOU 8065  CA  TYR D 710     5910   7506   5927     71    341    155       C  
ATOM   8066  C   TYR D 710    -127.935  32.933 -33.494  1.00 52.85           C  
ANISOU 8066  C   TYR D 710     6131   7725   6224     94    317    186       C  
ATOM   8067  O   TYR D 710    -128.754  32.823 -32.581  1.00 57.24           O  
ANISOU 8067  O   TYR D 710     6710   8250   6790     62    295    102       O  
ATOM   8068  CB  TYR D 710    -125.601  32.031 -33.375  1.00 47.65           C  
ANISOU 8068  CB  TYR D 710     5519   6972   5613     56    349    216       C  
ATOM   8069  CG  TYR D 710    -124.739  30.810 -33.107  1.00 46.16           C  
ANISOU 8069  CG  TYR D 710     5377   6756   5404     14    362    152       C  
ATOM   8070  CD1 TYR D 710    -125.147  29.819 -32.237  1.00 47.12           C  
ANISOU 8070  CD1 TYR D 710     5549   6844   5511    -42    351     35       C  
ATOM   8071  CD2 TYR D 710    -123.515  30.673 -33.698  1.00 48.94           C  
ANISOU 8071  CD2 TYR D 710     5720   7117   5758     34    385    217       C  
ATOM   8072  CE1 TYR D 710    -124.353  28.718 -31.980  1.00 48.54           C  
ANISOU 8072  CE1 TYR D 710     5771   6990   5682    -76    362    -16       C  
ATOM   8073  CE2 TYR D 710    -122.713  29.568 -33.455  1.00 49.92           C  
ANISOU 8073  CE2 TYR D 710     5886   7215   5865      2    396    158       C  
ATOM   8074  CZ  TYR D 710    -123.133  28.593 -32.596  1.00 49.44           C  
ANISOU 8074  CZ  TYR D 710     5877   7111   5795    -52    383     41       C  
ATOM   8075  OH  TYR D 710    -122.327  27.483 -32.387  1.00 50.85           O  
ANISOU 8075  OH  TYR D 710     6097   7259   5964    -78    393    -11       O  
ATOM   8076  N   SER D 711    -127.788  34.051 -34.183  1.00 53.31           N  
ANISOU 8076  N   SER D 711     6140   7799   6318    152    322    309       N  
ATOM   8077  CA  SER D 711    -128.602  35.223 -33.878  1.00 56.25           C  
ANISOU 8077  CA  SER D 711     6485   8138   6749    184    296    343       C  
ATOM   8078  C   SER D 711    -130.116  34.958 -34.000  1.00 57.78           C  
ANISOU 8078  C   SER D 711     6666   8439   6848    192    283    260       C  
ATOM   8079  O   SER D 711    -130.916  35.374 -33.152  1.00 57.21           O  
ANISOU 8079  O   SER D 711     6602   8324   6813    185    254    209       O  
ATOM   8080  CB  SER D 711    -128.217  36.374 -34.796  1.00 58.00           C  
ANISOU 8080  CB  SER D 711     6647   8371   7019    249    307    504       C  
ATOM   8081  OG  SER D 711    -126.857  36.737 -34.588  1.00 58.69           O  
ANISOU 8081  OG  SER D 711     6739   8348   7213    236    315    585       O  
ATOM   8082  N   ILE D 712    -130.513  34.281 -35.066  1.00 58.14           N  
ANISOU 8082  N   ILE D 712     6685   8634   6771    212    301    244       N  
ATOM   8083  CA  ILE D 712    -131.935  33.968 -35.257  1.00 61.58           C  
ANISOU 8083  CA  ILE D 712     7101   9183   7114    218    288    161       C  
ATOM   8084  C   ILE D 712    -132.442  33.084 -34.123  1.00 59.19           C  
ANISOU 8084  C   ILE D 712     6847   8833   6810    142    272     23       C  
ATOM   8085  O   ILE D 712    -133.548  33.296 -33.623  1.00 59.34           O  
ANISOU 8085  O   ILE D 712     6856   8871   6817    138    251    -30       O  
ATOM   8086  CB  ILE D 712    -132.185  33.283 -36.615  1.00 64.25           C  
ANISOU 8086  CB  ILE D 712     7399   9696   7319    253    307    150       C  
ATOM   8087  CG1 ILE D 712    -131.979  34.298 -37.732  1.00 67.29           C  
ANISOU 8087  CG1 ILE D 712     7720  10158   7690    342    322    299       C  
ATOM   8088  CG2 ILE D 712    -133.592  32.670 -36.686  1.00 65.75           C  
ANISOU 8088  CG2 ILE D 712     7573   9995   7415    239    290     31       C  
ATOM   8089  CD1 ILE D 712    -131.946  33.677 -39.105  1.00 72.11           C  
ANISOU 8089  CD1 ILE D 712     8283  10950   8166    389    344    302       C  
ATOM   8090  N   LEU D 713    -131.643  32.106 -33.717  1.00 55.36           N  
ANISOU 8090  N   LEU D 713     6409   8291   6335     86    283    -27       N  
ATOM   8091  CA  LEU D 713    -132.015  31.283 -32.588  1.00 56.66           C  
ANISOU 8091  CA  LEU D 713     6616   8402   6510     14    272   -135       C  
ATOM   8092  C   LEU D 713    -132.177  32.096 -31.321  1.00 59.98           C  
ANISOU 8092  C   LEU D 713     7052   8719   7018      7    249   -132       C  
ATOM   8093  O   LEU D 713    -133.053  31.786 -30.502  1.00 57.50           O  
ANISOU 8093  O   LEU D 713     6745   8413   6690    -28    235   -210       O  
ATOM   8094  CB  LEU D 713    -131.004  30.167 -32.360  1.00 56.07           C  
ANISOU 8094  CB  LEU D 713     6589   8271   6444    -37    287   -172       C  
ATOM   8095  CG  LEU D 713    -131.032  29.055 -33.401  1.00 56.33           C  
ANISOU 8095  CG  LEU D 713     6610   8405   6386    -40    300   -225       C  
ATOM   8096  CD1 LEU D 713    -130.000  27.983 -33.066  1.00 56.49           C  
ANISOU 8096  CD1 LEU D 713     6681   8353   6431    -87    312   -263       C  
ATOM   8097  CD2 LEU D 713    -132.422  28.435 -33.488  1.00 55.88           C  
ANISOU 8097  CD2 LEU D 713     6531   8439   6262    -67    286   -323       C  
ATOM   8098  N   SER D 714    -131.356  33.137 -31.165  1.00 59.43           N  
ANISOU 8098  N   SER D 714     6980   8559   7040     41    245    -45       N  
ATOM   8099  CA  SER D 714    -131.496  34.041 -30.023  1.00 61.12           C  
ANISOU 8099  CA  SER D 714     7200   8678   7346     47    215    -51       C  
ATOM   8100  C   SER D 714    -132.818  34.780 -30.077  1.00 61.88           C  
ANISOU 8100  C   SER D 714     7255   8837   7418     89    193    -62       C  
ATOM   8101  O   SER D 714    -133.504  34.915 -29.047  1.00 63.73           O  
ANISOU 8101  O   SER D 714     7495   9054   7666     78    169   -131       O  
ATOM   8102  CB  SER D 714    -130.324  35.039 -29.927  1.00 63.55           C  
ANISOU 8102  CB  SER D 714     7505   8867   7773     75    209     42       C  
ATOM   8103  OG  SER D 714    -129.145  34.427 -29.422  1.00 62.04           O  
ANISOU 8103  OG  SER D 714     7356   8598   7619     32    221     31       O  
ATOM   8104  N   GLU D 715    -133.176  35.262 -31.263  1.00 62.15           N  
ANISOU 8104  N   GLU D 715     7246   8955   7413    144    200      7       N  
ATOM   8105  CA  GLU D 715    -134.457  35.955 -31.428  1.00 61.76           C  
ANISOU 8105  CA  GLU D 715     7154   8978   7333    191    180      1       C  
ATOM   8106  C   GLU D 715    -135.622  35.006 -31.148  1.00 59.93           C  
ANISOU 8106  C   GLU D 715     6922   8848   7000    150    178   -114       C  
ATOM   8107  O   GLU D 715    -136.617  35.388 -30.524  1.00 58.04           O  
ANISOU 8107  O   GLU D 715     6666   8630   6756    162    154   -163       O  
ATOM   8108  CB  GLU D 715    -134.569  36.567 -32.819  1.00 65.45           C  
ANISOU 8108  CB  GLU D 715     7571   9530   7767    261    193    106       C  
ATOM   8109  CG  GLU D 715    -133.561  37.680 -33.080  1.00 69.63           C  
ANISOU 8109  CG  GLU D 715     8086   9958   8414    305    193    240       C  
ATOM   8110  CD  GLU D 715    -133.675  38.317 -34.466  1.00 78.65           C  
ANISOU 8110  CD  GLU D 715     9168  11193   9521    380    210    367       C  
ATOM   8111  OE1 GLU D 715    -134.636  38.009 -35.205  1.00 81.99           O  
ANISOU 8111  OE1 GLU D 715     9558  11767   9826    408    217    343       O  
ATOM   8112  OE2 GLU D 715    -132.788  39.129 -34.829  1.00 79.98           O  
ANISOU 8112  OE2 GLU D 715     9317  11289   9783    412    218    496       O  
ATOM   8113  N   VAL D 716    -135.496  33.759 -31.581  1.00 58.23           N  
ANISOU 8113  N   VAL D 716     6722   8693   6710    102    201   -161       N  
ATOM   8114  CA  VAL D 716    -136.532  32.752 -31.300  1.00 58.30           C  
ANISOU 8114  CA  VAL D 716     6728   8784   6641     50    198   -269       C  
ATOM   8115  C   VAL D 716    -136.750  32.563 -29.801  1.00 56.92           C  
ANISOU 8115  C   VAL D 716     6581   8537   6509      1    185   -332       C  
ATOM   8116  O   VAL D 716    -137.893  32.591 -29.323  1.00 51.38           O  
ANISOU 8116  O   VAL D 716     5854   7896   5773     -5    170   -386       O  
ATOM   8117  CB  VAL D 716    -136.190  31.386 -31.916  1.00 60.22           C  
ANISOU 8117  CB  VAL D 716     6985   9072   6825      1    220   -316       C  
ATOM   8118  CG1 VAL D 716    -137.109  30.294 -31.380  1.00 59.03           C  
ANISOU 8118  CG1 VAL D 716     6835   8964   6629    -71    215   -425       C  
ATOM   8119  CG2 VAL D 716    -136.274  31.451 -33.431  1.00 63.08           C  
ANISOU 8119  CG2 VAL D 716     7303   9553   7110     56    230   -279       C  
ATOM   8120  N   GLN D 717    -135.652  32.396 -29.069  1.00 53.39           N  
ANISOU 8120  N   GLN D 717     6179   7973   6132    -28    190   -321       N  
ATOM   8121  CA  GLN D 717    -135.713  32.189 -27.638  1.00 57.10           C  
ANISOU 8121  CA  GLN D 717     6673   8385   6638    -67    179   -373       C  
ATOM   8122  C   GLN D 717    -136.388  33.375 -26.959  1.00 53.76           C  
ANISOU 8122  C   GLN D 717     6221   7957   6247    -15    147   -377       C  
ATOM   8123  O   GLN D 717    -137.227  33.191 -26.083  1.00 52.56           O  
ANISOU 8123  O   GLN D 717     6057   7846   6069    -32    135   -439       O  
ATOM   8124  CB  GLN D 717    -134.311  31.979 -27.055  1.00 59.97           C  
ANISOU 8124  CB  GLN D 717     7085   8628   7074    -91    187   -351       C  
ATOM   8125  CG  GLN D 717    -134.325  31.501 -25.612  1.00 62.49           C  
ANISOU 8125  CG  GLN D 717     7427   8907   7410   -135    182   -407       C  
ATOM   8126  CD  GLN D 717    -135.165  30.235 -25.420  1.00 69.87           C  
ANISOU 8126  CD  GLN D 717     8359   9916   8273   -201    197   -468       C  
ATOM   8127  OE1 GLN D 717    -134.791  29.140 -25.872  1.00 77.87           O  
ANISOU 8127  OE1 GLN D 717     9395  10927   9266   -249    219   -478       O  
ATOM   8128  NE2 GLN D 717    -136.295  30.375 -24.728  1.00 67.82           N  
ANISOU 8128  NE2 GLN D 717     8068   9721   7981   -202    183   -510       N  
ATOM   8129  N   GLN D 718    -136.021  34.583 -27.374  1.00 55.17           N  
ANISOU 8129  N   GLN D 718     6385   8088   6489     52    131   -309       N  
ATOM   8130  CA  GLN D 718    -136.633  35.787 -26.850  1.00 61.29           C  
ANISOU 8130  CA  GLN D 718     7129   8848   7309    113     95   -315       C  
ATOM   8131  C   GLN D 718    -138.139  35.844 -27.149  1.00 64.27           C  
ANISOU 8131  C   GLN D 718     7462   9358   7599    136     87   -352       C  
ATOM   8132  O   GLN D 718    -138.936  36.173 -26.271  1.00 66.42           O  
ANISOU 8132  O   GLN D 718     7715   9656   7866    152     62   -410       O  
ATOM   8133  CB  GLN D 718    -135.918  37.006 -27.440  1.00 66.88           C  
ANISOU 8133  CB  GLN D 718     7826   9472   8114    176     82   -219       C  
ATOM   8134  CG  GLN D 718    -136.430  38.340 -26.923  1.00 75.75           C  
ANISOU 8134  CG  GLN D 718     8917  10553   9311    246     37   -224       C  
ATOM   8135  CD  GLN D 718    -135.881  39.532 -27.694  1.00 81.09           C  
ANISOU 8135  CD  GLN D 718     9571  11151  10089    308     26   -113       C  
ATOM   8136  OE1 GLN D 718    -135.501  39.428 -28.864  1.00 84.82           O  
ANISOU 8136  OE1 GLN D 718    10035  11653  10539    314     56    -23       O  
ATOM   8137  NE2 GLN D 718    -135.817  40.673 -27.018  1.00 82.23           N  
ANISOU 8137  NE2 GLN D 718     9701  11194  10350    357    -19   -120       N  
ATOM   8138  N   ALA D 719    -138.526  35.530 -28.386  1.00 63.51           N  
ANISOU 8138  N   ALA D 719     7344   9356   7431    142    106   -323       N  
ATOM   8139  CA  ALA D 719    -139.940  35.517 -28.766  1.00 60.93           C  
ANISOU 8139  CA  ALA D 719     6969   9166   7015    162    100   -361       C  
ATOM   8140  C   ALA D 719    -140.724  34.475 -27.981  1.00 59.30           C  
ANISOU 8140  C   ALA D 719     6761   9025   6744     92    104   -456       C  
ATOM   8141  O   ALA D 719    -141.820  34.733 -27.537  1.00 65.78           O  
ANISOU 8141  O   ALA D 719     7546   9919   7529    109     86   -501       O  
ATOM   8142  CB  ALA D 719    -140.085  35.283 -30.253  1.00 61.00           C  
ANISOU 8142  CB  ALA D 719     6952   9271   6954    182    119   -318       C  
ATOM   8143  N   VAL D 720    -140.156  33.301 -27.771  1.00 62.29           N  
ANISOU 8143  N   VAL D 720     7176   9375   7116     14    127   -483       N  
ATOM   8144  CA  VAL D 720    -140.798  32.289 -26.910  1.00 64.98           C  
ANISOU 8144  CA  VAL D 720     7514   9760   7417    -59    133   -557       C  
ATOM   8145  C   VAL D 720    -141.052  32.834 -25.471  1.00 69.41           C  
ANISOU 8145  C   VAL D 720     8070  10292   8009    -43    112   -584       C  
ATOM   8146  O   VAL D 720    -142.158  32.685 -24.941  1.00 70.97           O  
ANISOU 8146  O   VAL D 720     8229  10582   8156    -53    105   -632       O  
ATOM   8147  CB  VAL D 720    -140.003  30.957 -26.939  1.00 63.35           C  
ANISOU 8147  CB  VAL D 720     7349   9504   7215   -141    161   -569       C  
ATOM   8148  CG1 VAL D 720    -140.483  29.973 -25.880  1.00 64.32           C  
ANISOU 8148  CG1 VAL D 720     7473   9644   7324   -217    169   -622       C  
ATOM   8149  CG2 VAL D 720    -140.094  30.319 -28.328  1.00 66.36           C  
ANISOU 8149  CG2 VAL D 720     7718   9953   7544   -152    174   -574       C  
ATOM   8150  N   SER D 721    -140.066  33.496 -24.856  1.00 68.32           N  
ANISOU 8150  N   SER D 721     7964  10040   7954    -12    100   -557       N  
ATOM   8151  CA  SER D 721    -140.284  34.145 -23.535  1.00 66.22           C  
ANISOU 8151  CA  SER D 721     7685   9757   7718     22     72   -595       C  
ATOM   8152  C   SER D 721    -141.374  35.236 -23.555  1.00 61.41           C  
ANISOU 8152  C   SER D 721     7024   9218   7092    100     39   -614       C  
ATOM   8153  O   SER D 721    -141.170  36.347 -24.058  1.00 54.91           O  
ANISOU 8153  O   SER D 721     6193   8345   6325    172     16   -575       O  
ATOM   8154  CB  SER D 721    -138.978  34.756 -22.982  1.00 70.10           C  
ANISOU 8154  CB  SER D 721     8213  10110   8311     48     57   -571       C  
ATOM   8155  OG  SER D 721    -137.959  33.796 -22.697  1.00 63.18           O  
ANISOU 8155  OG  SER D 721     7384   9171   7451    -17     84   -561       O  
ATOM   8156  N   LEU D 730    -142.652  31.308 -35.300  1.00 77.77           N  
ANISOU 8156  N   LEU D 730     8904  12054   8592    130    163   -533       N  
ATOM   8157  CA  LEU D 730    -143.201  30.848 -36.585  1.00 81.27           C  
ANISOU 8157  CA  LEU D 730     9287  12663   8928    160    160   -578       C  
ATOM   8158  C   LEU D 730    -142.414  31.395 -37.819  1.00 78.68           C  
ANISOU 8158  C   LEU D 730     8940  12391   8563    252    175   -481       C  
ATOM   8159  O   LEU D 730    -141.702  30.645 -38.522  1.00 77.19           O  
ANISOU 8159  O   LEU D 730     8755  12229   8343    246    186   -503       O  
ATOM   8160  CB  LEU D 730    -144.712  31.182 -36.652  1.00 81.87           C  
ANISOU 8160  CB  LEU D 730     9300  12869   8938    184    140   -622       C  
ATOM   8161  N   ASP D 731    -142.509  32.695 -38.080  1.00 77.68           N  
ANISOU 8161  N   ASP D 731     8789  12283   8443    340    176   -369       N  
ATOM   8162  CA  ASP D 731    -141.677  33.319 -39.115  1.00 83.97           C  
ANISOU 8162  CA  ASP D 731     9566  13116   9223    426    195   -246       C  
ATOM   8163  C   ASP D 731    -140.171  33.202 -38.797  1.00 83.29           C  
ANISOU 8163  C   ASP D 731     9540  12881   9224    395    216   -186       C  
ATOM   8164  O   ASP D 731    -139.341  33.031 -39.701  1.00 83.79           O  
ANISOU 8164  O   ASP D 731     9590  12992   9252    432    235   -134       O  
ATOM   8165  CB  ASP D 731    -142.076  34.779 -39.334  1.00 87.19           C  
ANISOU 8165  CB  ASP D 731     9936  13546   9646    521    191   -124       C  
ATOM   8166  CG  ASP D 731    -141.214  35.452 -40.352  1.00 93.75           C  
ANISOU 8166  CG  ASP D 731    10740  14410  10470    606    215     25       C  
ATOM   8167  OD1 ASP D 731    -140.232  36.092 -39.950  1.00 98.97           O  
ANISOU 8167  OD1 ASP D 731    11438  14925  11242    607    225    127       O  
ATOM   8168  OD2 ASP D 731    -141.490  35.299 -41.563  1.00 98.66           O  
ANISOU 8168  OD2 ASP D 731    11300  15213  10976    670    223     38       O  
ATOM   8169  N   LEU D 732    -139.814  33.282 -37.519  1.00 79.43           N  
ANISOU 8169  N   LEU D 732     9112  12224   8843    333    211   -196       N  
ATOM   8170  CA  LEU D 732    -138.408  33.152 -37.120  1.00 77.41           C  
ANISOU 8170  CA  LEU D 732     8914  11826   8673    301    227   -149       C  
ATOM   8171  C   LEU D 732    -137.922  31.725 -37.342  1.00 71.29           C  
ANISOU 8171  C   LEU D 732     8162  11068   7857    240    237   -241       C  
ATOM   8172  O   LEU D 732    -136.811  31.532 -37.840  1.00 73.12           O  
ANISOU 8172  O   LEU D 732     8407  11281   8095    254    256   -192       O  
ATOM   8173  CB  LEU D 732    -138.214  33.563 -35.665  1.00 75.84           C  
ANISOU 8173  CB  LEU D 732     8766  11459   8590    255    215   -152       C  
ATOM   8174  CG  LEU D 732    -138.404  35.058 -35.391  1.00 77.19           C  
ANISOU 8174  CG  LEU D 732     8920  11575   8833    320    200    -56       C  
ATOM   8175  CD1 LEU D 732    -138.511  35.297 -33.897  1.00 75.10           C  
ANISOU 8175  CD1 LEU D 732     8696  11181   8659    277    179   -105       C  
ATOM   8176  CD2 LEU D 732    -137.289  35.900 -36.009  1.00 77.06           C  
ANISOU 8176  CD2 LEU D 732     8896  11505   8879    377    216     90       C  
ATOM   8177  N   SER D 733    -138.760  30.747 -36.988  1.00 70.15           N  
ANISOU 8177  N   SER D 733     8018  10958   7676    175    222   -372       N  
ATOM   8178  CA  SER D 733    -138.492  29.327 -37.277  1.00 72.43           C  
ANISOU 8178  CA  SER D 733     8320  11268   7931    118    224   -476       C  
ATOM   8179  C   SER D 733    -138.128  29.145 -38.744  1.00 77.25           C  
ANISOU 8179  C   SER D 733     8884  12016   8450    188    233   -461       C  
ATOM   8180  O   SER D 733    -137.105  28.546 -39.072  1.00 77.40           O  
ANISOU 8180  O   SER D 733     8926  12009   8473    182    245   -465       O  
ATOM   8181  CB  SER D 733    -139.711  28.447 -36.950  1.00 71.69           C  
ANISOU 8181  CB  SER D 733     8206  11227   7805     52    203   -608       C  
ATOM   8182  OG  SER D 733    -139.424  27.473 -35.975  1.00 64.61           O  
ANISOU 8182  OG  SER D 733     7362  10210   6975    -45    203   -674       O  
ATOM   8183  N   ASN D 734    -138.956  29.710 -39.616  1.00 79.99           N  
ANISOU 8183  N   ASN D 734     9162  12518   8711    262    226   -440       N  
ATOM   8184  CA  ASN D 734    -138.737  29.615 -41.047  1.00 83.17           C  
ANISOU 8184  CA  ASN D 734     9506  13086   9008    344    233   -424       C  
ATOM   8185  C   ASN D 734    -137.484  30.354 -41.500  1.00 84.19           C  
ANISOU 8185  C   ASN D 734     9640  13188   9159    409    263   -271       C  
ATOM   8186  O   ASN D 734    -136.806  29.898 -42.424  1.00 92.66           O  
ANISOU 8186  O   ASN D 734    10689  14351  10168    450    275   -270       O  
ATOM   8187  CB  ASN D 734    -139.967  30.119 -41.815  1.00 85.34           C  
ANISOU 8187  CB  ASN D 734     9701  13541   9182    414    220   -428       C  
ATOM   8188  CG  ASN D 734    -141.193  29.249 -41.588  1.00 83.52           C  
ANISOU 8188  CG  ASN D 734     9449  13369   8915    352    190   -590       C  
ATOM   8189  OD1 ASN D 734    -141.080  28.054 -41.310  1.00 82.94           O  
ANISOU 8189  OD1 ASN D 734     9402  13249   8862    272    179   -711       O  
ATOM   8190  ND2 ASN D 734    -142.371  29.842 -41.710  1.00 81.98           N  
ANISOU 8190  ND2 ASN D 734     9203  13274   8672    388    176   -590       N  
ATOM   8191  N   ARG D 735    -137.173  31.491 -40.876  1.00 80.50           N  
ANISOU 8191  N   ARG D 735     9197  12604   8784    421    273   -145       N  
ATOM   8192  CA  ARG D 735    -135.933  32.217 -41.225  1.00 80.55           C  
ANISOU 8192  CA  ARG D 735     9205  12565   8836    471    300     10       C  
ATOM   8193  C   ARG D 735    -134.713  31.324 -40.930  1.00 71.63           C  
ANISOU 8193  C   ARG D 735     8130  11340   7747    415    312    -28       C  
ATOM   8194  O   ARG D 735    -133.752  31.236 -41.714  1.00 69.55           O  
ANISOU 8194  O   ARG D 735     7847  11130   7450    459    335     36       O  
ATOM   8195  CB  ARG D 735    -135.844  33.563 -40.475  1.00 80.13           C  
ANISOU 8195  CB  ARG D 735     9168  12375   8902    483    300    134       C  
ATOM   8196  N   PHE D 736    -134.786  30.611 -39.815  1.00 65.95           N  
ANISOU 8196  N   PHE D 736     7474  10492   7091    320    298   -133       N  
ATOM   8197  CA  PHE D 736    -133.710  29.708 -39.441  1.00 65.73           C  
ANISOU 8197  CA  PHE D 736     7501  10368   7106    265    307   -176       C  
ATOM   8198  C   PHE D 736    -133.529  28.587 -40.464  1.00 64.15           C  
ANISOU 8198  C   PHE D 736     7273  10297   6804    283    307   -266       C  
ATOM   8199  O   PHE D 736    -132.414  28.322 -40.918  1.00 62.02           O  
ANISOU 8199  O   PHE D 736     7009  10032   6526    307    325   -231       O  
ATOM   8200  CB  PHE D 736    -133.959  29.107 -38.056  1.00 65.33           C  
ANISOU 8200  CB  PHE D 736     7515  10172   7135    164    291   -270       C  
ATOM   8201  CG  PHE D 736    -132.905  28.133 -37.639  1.00 64.45           C  
ANISOU 8201  CG  PHE D 736     7460   9961   7067    109    300   -315       C  
ATOM   8202  CD1 PHE D 736    -131.709  28.583 -37.093  1.00 62.60           C  
ANISOU 8202  CD1 PHE D 736     7267   9601   6919    104    316   -226       C  
ATOM   8203  CD2 PHE D 736    -133.091  26.770 -37.831  1.00 64.71           C  
ANISOU 8203  CD2 PHE D 736     7500  10026   7060     66    289   -447       C  
ATOM   8204  CE1 PHE D 736    -130.731  27.688 -36.718  1.00 63.06           C  
ANISOU 8204  CE1 PHE D 736     7374   9573   7012     59    323   -266       C  
ATOM   8205  CE2 PHE D 736    -132.112  25.872 -37.466  1.00 64.36           C  
ANISOU 8205  CE2 PHE D 736     7508   9887   7061     22    295   -486       C  
ATOM   8206  CZ  PHE D 736    -130.933  26.331 -36.909  1.00 62.77           C  
ANISOU 8206  CZ  PHE D 736     7348   9567   6933     20    314   -393       C  
ATOM   8207  N   TYR D 737    -134.631  27.934 -40.810  1.00 67.58           N  
ANISOU 8207  N   TYR D 737     7674  10838   7164    274    284   -389       N  
ATOM   8208  CA  TYR D 737    -134.601  26.833 -41.765  1.00 72.21           C  
ANISOU 8208  CA  TYR D 737     8228  11550   7659    292    273   -504       C  
ATOM   8209  C   TYR D 737    -134.192  27.260 -43.179  1.00 78.02           C  
ANISOU 8209  C   TYR D 737     8891  12469   8284    409    289   -427       C  
ATOM   8210  O   TYR D 737    -133.707  26.447 -43.962  1.00 79.26           O  
ANISOU 8210  O   TYR D 737     9026  12717   8373    440    286   -497       O  
ATOM   8211  CB  TYR D 737    -135.955  26.120 -41.785  1.00 70.76           C  
ANISOU 8211  CB  TYR D 737     8015  11437   7432    253    239   -654       C  
ATOM   8212  CG  TYR D 737    -136.216  25.330 -40.518  1.00 66.78           C  
ANISOU 8212  CG  TYR D 737     7574  10770   7028    134    225   -745       C  
ATOM   8213  CD1 TYR D 737    -135.334  24.341 -40.111  1.00 63.66           C  
ANISOU 8213  CD1 TYR D 737     7234  10261   6693     77    226   -800       C  
ATOM   8214  CD2 TYR D 737    -137.340  25.561 -39.737  1.00 66.08           C  
ANISOU 8214  CD2 TYR D 737     7485  10652   6970     83    212   -769       C  
ATOM   8215  CE1 TYR D 737    -135.556  23.617 -38.958  1.00 62.53           C  
ANISOU 8215  CE1 TYR D 737     7144   9975   6642    -27    217   -866       C  
ATOM   8216  CE2 TYR D 737    -137.576  24.827 -38.582  1.00 64.80           C  
ANISOU 8216  CE2 TYR D 737     7372  10357   6893    -22    203   -838       C  
ATOM   8217  CZ  TYR D 737    -136.676  23.855 -38.194  1.00 64.65           C  
ANISOU 8217  CZ  TYR D 737     7407  10222   6936    -77    206   -881       C  
ATOM   8218  OH  TYR D 737    -136.871  23.111 -37.052  1.00 62.12           O  
ANISOU 8218  OH  TYR D 737     7130   9772   6701   -178    201   -933       O  
ATOM   8219  N   THR D 738    -134.366  28.539 -43.492  1.00 80.01           N  
ANISOU 8219  N   THR D 738     9104  12775   8521    477    306   -280       N  
ATOM   8220  CA  THR D 738    -133.876  29.090 -44.742  1.00 82.10           C  
ANISOU 8220  CA  THR D 738     9298  13204   8693    590    329   -166       C  
ATOM   8221  C   THR D 738    -132.357  29.224 -44.716  1.00 76.93           C  
ANISOU 8221  C   THR D 738     8670  12469   8090    598    360    -60       C  
ATOM   8222  O   THR D 738    -131.695  28.937 -45.706  1.00 79.14           O  
ANISOU 8222  O   THR D 738     8904  12884   8282    667    375    -40       O  
ATOM   8223  CB  THR D 738    -134.528  30.458 -45.023  1.00 86.79           C  
ANISOU 8223  CB  THR D 738     9840  13862   9273    658    339    -23       C  
ATOM   8224  OG1 THR D 738    -135.934  30.277 -45.221  1.00 82.87           O  
ANISOU 8224  OG1 THR D 738     9305  13476   8704    665    311   -127       O  
ATOM   8225  CG2 THR D 738    -133.918  31.119 -46.260  1.00 89.00           C  
ANISOU 8225  CG2 THR D 738    10042  14303   9469    776    370    132       C  
ATOM   8226  N   LEU D 739    -131.804  29.668 -43.590  1.00 76.14           N  
ANISOU 8226  N   LEU D 739     8638  12161   8129    533    368      6       N  
ATOM   8227  CA  LEU D 739    -130.345  29.792 -43.453  1.00 72.94           C  
ANISOU 8227  CA  LEU D 739     8260  11666   7786    530    395    102       C  
ATOM   8228  C   LEU D 739    -129.672  28.431 -43.372  1.00 67.84           C  
ANISOU 8228  C   LEU D 739     7655  10995   7126    489    389    -30       C  
ATOM   8229  O   LEU D 739    -128.579  28.229 -43.878  1.00 67.00           O  
ANISOU 8229  O   LEU D 739     7536  10926   6995    525    409     16       O  
ATOM   8230  CB  LEU D 739    -129.996  30.565 -42.188  1.00 74.62           C  
ANISOU 8230  CB  LEU D 739     8535  11662   8156    468    398    181       C  
ATOM   8231  CG  LEU D 739    -128.930  31.637 -42.288  1.00 75.46           C  
ANISOU 8231  CG  LEU D 739     8624  11711   8336    504    427    372       C  
ATOM   8232  CD1 LEU D 739    -129.192  32.661 -43.371  1.00 75.23           C  
ANISOU 8232  CD1 LEU D 739     8506  11828   8249    604    445    523       C  
ATOM   8233  CD2 LEU D 739    -128.845  32.321 -40.933  1.00 76.52           C  
ANISOU 8233  CD2 LEU D 739     8817  11630   8627    438    415    403       C  
ATOM   8234  N   ILE D 740    -130.310  27.505 -42.672  1.00 67.39           N  
ANISOU 8234  N   ILE D 740     7646  10866   7094    410    360   -189       N  
ATOM   8235  CA  ILE D 740    -129.754  26.173 -42.497  1.00 66.10           C  
ANISOU 8235  CA  ILE D 740     7524  10654   6937    364    349   -320       C  
ATOM   8236  C   ILE D 740    -130.782  25.222 -43.052  1.00 67.13           C  
ANISOU 8236  C   ILE D 740     7620  10903   6982    364    316   -489       C  
ATOM   8237  O   ILE D 740    -131.686  24.786 -42.329  1.00 66.66           O  
ANISOU 8237  O   ILE D 740     7590  10772   6968    288    291   -587       O  
ATOM   8238  CB  ILE D 740    -129.441  25.868 -41.020  1.00 63.10           C  
ANISOU 8238  CB  ILE D 740     7235  10050   6691    259    344   -347       C  
ATOM   8239  CG1 ILE D 740    -128.649  27.023 -40.381  1.00 57.99           C  
ANISOU 8239  CG1 ILE D 740     6613   9284   6138    258    369   -185       C  
ATOM   8240  CG2 ILE D 740    -128.669  24.551 -40.907  1.00 63.27           C  
ANISOU 8240  CG2 ILE D 740     7298  10017   6725    224    338   -456       C  
ATOM   8241  CD1 ILE D 740    -127.216  27.139 -40.864  1.00 55.32           C  
ANISOU 8241  CD1 ILE D 740     6266   8956   5798    303    397    -93       C  
ATOM   8242  N   PRO D 741    -130.657  24.910 -44.352  1.00 70.84           N  
ANISOU 8242  N   PRO D 741     8021  11567   7329    452    313   -522       N  
ATOM   8243  CA  PRO D 741    -131.673  24.103 -45.011  1.00 71.70           C  
ANISOU 8243  CA  PRO D 741     8080  11812   7350    466    277   -688       C  
ATOM   8244  C   PRO D 741    -131.750  22.695 -44.455  1.00 71.48           C  
ANISOU 8244  C   PRO D 741     8102  11672   7383    378    244   -868       C  
ATOM   8245  O   PRO D 741    -130.724  22.025 -44.266  1.00 64.51           O  
ANISOU 8245  O   PRO D 741     7262  10706   6543    361    248   -896       O  
ATOM   8246  CB  PRO D 741    -131.248  24.072 -46.487  1.00 74.77           C  
ANISOU 8246  CB  PRO D 741     8383  12432   7594    591    283   -679       C  
ATOM   8247  CG  PRO D 741    -130.024  24.897 -46.610  1.00 72.83           C  
ANISOU 8247  CG  PRO D 741     8140  12172   7361    640    328   -492       C  
ATOM   8248  CD  PRO D 741    -129.550  25.286 -45.247  1.00 71.74           C  
ANISOU 8248  CD  PRO D 741     8092  11787   7378    545    344   -411       C  
ATOM   8249  N   HIS D 742    -132.976  22.291 -44.152  1.00 72.80           N  
ANISOU 8249  N   HIS D 742     8263  11833   7566    320    212   -980       N  
ATOM   8250  CA  HIS D 742    -133.261  20.986 -43.609  1.00 76.54           C  
ANISOU 8250  CA  HIS D 742     8773  12197   8111    228    179  -1145       C  
ATOM   8251  C   HIS D 742    -134.142  20.252 -44.592  1.00 77.64           C  
ANISOU 8251  C   HIS D 742     8835  12501   8163    260    135  -1312       C  
ATOM   8252  O   HIS D 742    -134.610  20.826 -45.556  1.00 80.89           O  
ANISOU 8252  O   HIS D 742     9170  13107   8457    349    134  -1293       O  
ATOM   8253  CB  HIS D 742    -134.004  21.119 -42.275  1.00 75.27           C  
ANISOU 8253  CB  HIS D 742     8664  11877   8058    119    178  -1130       C  
ATOM   8254  CG  HIS D 742    -133.121  21.455 -41.107  1.00 75.87           C  
ANISOU 8254  CG  HIS D 742     8823  11762   8242     67    208  -1019       C  
ATOM   8255  ND1 HIS D 742    -132.441  22.649 -41.000  1.00 74.94           N  
ANISOU 8255  ND1 HIS D 742     8717  11631   8126    115    243   -853       N  
ATOM   8256  CD2 HIS D 742    -132.835  20.761 -39.980  1.00 75.18           C  
ANISOU 8256  CD2 HIS D 742     8806  11493   8267    -27    206  -1050       C  
ATOM   8257  CE1 HIS D 742    -131.767  22.674 -39.862  1.00 74.89           C  
ANISOU 8257  CE1 HIS D 742     8784  11446   8225     53    258   -799       C  
ATOM   8258  NE2 HIS D 742    -131.991  21.541 -39.224  1.00 74.23           N  
ANISOU 8258  NE2 HIS D 742     8738  11264   8203    -31    239   -913       N  
ATOM   8259  N   ASP D 743    -134.389  18.982 -44.314  1.00 81.81           N  
ANISOU 8259  N   ASP D 743     9381  12946   8758    186     98  -1476       N  
ATOM   8260  CA  ASP D 743    -135.362  18.218 -45.091  1.00 81.60           C  
ANISOU 8260  CA  ASP D 743     9280  13047   8676    196     47  -1657       C  
ATOM   8261  C   ASP D 743    -136.164  17.234 -44.241  1.00 75.48           C  
ANISOU 8261  C   ASP D 743     8531  12124   8024     67     13  -1781       C  
ATOM   8262  O   ASP D 743    -135.645  16.187 -43.865  1.00 69.43           O  
ANISOU 8262  O   ASP D 743     7808  11220   7352     10     -4  -1865       O  
ATOM   8263  CB  ASP D 743    -134.624  17.478 -46.206  1.00 87.16           C  
ANISOU 8263  CB  ASP D 743     9943  13868   9305    283     24  -1769       C  
ATOM   8264  CG  ASP D 743    -135.576  16.776 -47.191  1.00 91.61           C  
ANISOU 8264  CG  ASP D 743    10413  14600   9794    318    -35  -1967       C  
ATOM   8265  OD1 ASP D 743    -136.658  17.331 -47.469  1.00 94.86           O  
ANISOU 8265  OD1 ASP D 743    10767  15134  10141    334    -41  -1963       O  
ATOM   8266  OD2 ASP D 743    -135.254  15.669 -47.682  1.00 92.61           O  
ANISOU 8266  OD2 ASP D 743    10522  14737   9929    332    -77  -2134       O  
ATOM   8267  N   PRO D 749    -141.793  20.214 -40.643  1.00 71.13           N  
ANISOU 8267  N   PRO D 749     7932  11522   7573   -199     43  -1541       N  
ATOM   8268  CA  PRO D 749    -140.631  21.037 -40.328  1.00 77.23           C  
ANISOU 8268  CA  PRO D 749     8770  12217   8358   -152     83  -1391       C  
ATOM   8269  C   PRO D 749    -140.804  21.514 -38.878  1.00 75.11           C  
ANISOU 8269  C   PRO D 749     8556  11806   8177   -222    105  -1299       C  
ATOM   8270  O   PRO D 749    -141.626  22.390 -38.616  1.00 70.15           O  
ANISOU 8270  O   PRO D 749     7901  11233   7519   -205    109  -1246       O  
ATOM   8271  CB  PRO D 749    -140.531  22.223 -41.302  1.00 75.78           C  
ANISOU 8271  CB  PRO D 749     8543  12194   8058    -24     97  -1299       C  
ATOM   8272  N   PRO D 750    -140.052  20.923 -37.928  1.00 73.07           N  
ANISOU 8272  N   PRO D 750     8368  11373   8021   -295    118  -1284       N  
ATOM   8273  CA  PRO D 750    -140.321  21.154 -36.477  1.00 71.68           C  
ANISOU 8273  CA  PRO D 750     8234  11074   7926   -369    134  -1221       C  
ATOM   8274  C   PRO D 750    -140.311  22.621 -36.017  1.00 66.83           C  
ANISOU 8274  C   PRO D 750     7633  10466   7293   -313    156  -1089       C  
ATOM   8275  O   PRO D 750    -139.341  23.348 -36.233  1.00 63.78           O  
ANISOU 8275  O   PRO D 750     7276  10057   6899   -248    175   -998       O  
ATOM   8276  CB  PRO D 750    -139.197  20.388 -35.757  1.00 70.55           C  
ANISOU 8276  CB  PRO D 750     8165  10760   7879   -424    147  -1209       C  
ATOM   8277  CG  PRO D 750    -138.406  19.665 -36.801  1.00 72.47           C  
ANISOU 8277  CG  PRO D 750     8407  11028   8100   -388    135  -1279       C  
ATOM   8278  CD  PRO D 750    -138.913  20.016 -38.172  1.00 72.28           C  
ANISOU 8278  CD  PRO D 750     8309  11194   7962   -303    116  -1326       C  
ATOM   8279  N   LEU D 751    -141.382  23.034 -35.360  1.00 63.81           N  
ANISOU 8279  N   LEU D 751     7225  10109   6911   -341    152  -1082       N  
ATOM   8280  CA  LEU D 751    -141.528  24.413 -34.922  1.00 66.34           C  
ANISOU 8280  CA  LEU D 751     7550  10438   7219   -284    164   -977       C  
ATOM   8281  C   LEU D 751    -140.593  24.699 -33.754  1.00 64.74           C  
ANISOU 8281  C   LEU D 751     7420  10079   7101   -308    185   -897       C  
ATOM   8282  O   LEU D 751    -140.547  23.936 -32.793  1.00 60.58           O  
ANISOU 8282  O   LEU D 751     6923   9458   6637   -390    188   -923       O  
ATOM   8283  CB  LEU D 751    -142.975  24.673 -34.510  1.00 67.18           C  
ANISOU 8283  CB  LEU D 751     7603  10624   7299   -307    151  -1007       C  
ATOM   8284  CG  LEU D 751    -143.358  26.140 -34.311  1.00 68.15           C  
ANISOU 8284  CG  LEU D 751     7711  10790   7393   -230    153   -920       C  
ATOM   8285  CD1 LEU D 751    -143.096  26.972 -35.562  1.00 65.98           C  
ANISOU 8285  CD1 LEU D 751     7408  10612   7048   -120    154   -867       C  
ATOM   8286  CD2 LEU D 751    -144.826  26.214 -33.906  1.00 72.04           C  
ANISOU 8286  CD2 LEU D 751     8147  11370   7855   -256    138   -966       C  
ATOM   8287  N   LEU D 752    -139.845  25.801 -33.846  1.00 66.35           N  
ANISOU 8287  N   LEU D 752     7645  10256   7308   -234    197   -797       N  
ATOM   8288  CA  LEU D 752    -138.908  26.192 -32.791  1.00 66.60           C  
ANISOU 8288  CA  LEU D 752     7738  10145   7420   -246    212   -725       C  
ATOM   8289  C   LEU D 752    -139.627  27.086 -31.775  1.00 63.66           C  
ANISOU 8289  C   LEU D 752     7358   9762   7068   -240    205   -693       C  
ATOM   8290  O   LEU D 752    -139.533  28.319 -31.826  1.00 62.97           O  
ANISOU 8290  O   LEU D 752     7263   9678   6985   -169    202   -622       O  
ATOM   8291  CB  LEU D 752    -137.661  26.863 -33.404  1.00 66.85           C  
ANISOU 8291  CB  LEU D 752     7794  10146   7462   -176    225   -638       C  
ATOM   8292  CG  LEU D 752    -136.916  25.947 -34.385  1.00 68.66           C  
ANISOU 8292  CG  LEU D 752     8026  10398   7662   -174    231   -676       C  
ATOM   8293  CD1 LEU D 752    -135.795  26.694 -35.103  1.00 68.94           C  
ANISOU 8293  CD1 LEU D 752     8067  10435   7692    -96    248   -577       C  
ATOM   8294  CD2 LEU D 752    -136.384  24.696 -33.693  1.00 66.23           C  
ANISOU 8294  CD2 LEU D 752     7769   9982   7414   -258    235   -735       C  
ATOM   8295  N   ASN D 753    -140.325  26.435 -30.846  1.00 60.78           N  
ANISOU 8295  N   ASN D 753     6990   9384   6721   -314    202   -746       N  
ATOM   8296  CA  ASN D 753    -141.261  27.106 -29.951  1.00 62.39           C  
ANISOU 8296  CA  ASN D 753     7168   9617   6921   -309    192   -739       C  
ATOM   8297  C   ASN D 753    -141.073  26.785 -28.471  1.00 59.19           C  
ANISOU 8297  C   ASN D 753     6794   9122   6573   -366    200   -734       C  
ATOM   8298  O   ASN D 753    -141.938  27.101 -27.651  1.00 58.28           O  
ANISOU 8298  O   ASN D 753     6649   9047   6446   -372    193   -743       O  
ATOM   8299  CB  ASN D 753    -142.706  26.804 -30.367  1.00 63.22           C  
ANISOU 8299  CB  ASN D 753     7204   9857   6960   -327    179   -806       C  
ATOM   8300  CG  ASN D 753    -143.137  25.375 -30.047  1.00 65.94           C  
ANISOU 8300  CG  ASN D 753     7539  10196   7321   -431    181   -879       C  
ATOM   8301  OD1 ASN D 753    -142.313  24.487 -29.796  1.00 67.70           O  
ANISOU 8301  OD1 ASN D 753     7806  10321   7598   -485    192   -886       O  
ATOM   8302  ND2 ASN D 753    -144.444  25.161 -30.032  1.00 63.57           N  
ANISOU 8302  ND2 ASN D 753     7175   9998   6980   -461    169   -930       N  
ATOM   8303  N   ASN D 754    -139.940  26.189 -28.129  1.00 58.21           N  
ANISOU 8303  N   ASN D 754     6726   8888   6504   -400    214   -718       N  
ATOM   8304  CA  ASN D 754    -139.615  25.926 -26.737  1.00 61.40           C  
ANISOU 8304  CA  ASN D 754     7160   9212   6958   -442    223   -702       C  
ATOM   8305  C   ASN D 754    -138.095  25.940 -26.549  1.00 57.62           C  
ANISOU 8305  C   ASN D 754     6744   8613   6537   -430    235   -658       C  
ATOM   8306  O   ASN D 754    -137.335  25.856 -27.512  1.00 63.87           O  
ANISOU 8306  O   ASN D 754     7555   9383   7329   -407    239   -647       O  
ATOM   8307  CB  ASN D 754    -140.249  24.605 -26.256  1.00 61.81           C  
ANISOU 8307  CB  ASN D 754     7196   9275   7016   -538    232   -748       C  
ATOM   8308  CG  ASN D 754    -139.682  23.400 -26.968  1.00 63.16           C  
ANISOU 8308  CG  ASN D 754     7390   9396   7212   -588    239   -781       C  
ATOM   8309  OD1 ASN D 754    -138.639  22.873 -26.580  1.00 63.37           O  
ANISOU 8309  OD1 ASN D 754     7468   9320   7290   -610    252   -760       O  
ATOM   8310  ND2 ASN D 754    -140.339  22.984 -28.041  1.00 63.75           N  
ANISOU 8310  ND2 ASN D 754     7425   9549   7249   -597    227   -841       N  
ATOM   8311  N   ALA D 755    -137.674  26.068 -25.297  1.00 53.84           N  
ANISOU 8311  N   ALA D 755     6291   8068   6098   -439    239   -634       N  
ATOM   8312  CA  ALA D 755    -136.275  26.202 -24.952  1.00 50.38           C  
ANISOU 8312  CA  ALA D 755     5905   7521   5715   -423    246   -593       C  
ATOM   8313  C   ALA D 755    -135.459  24.959 -25.343  1.00 52.92           C  
ANISOU 8313  C   ALA D 755     6266   7782   6059   -474    264   -603       C  
ATOM   8314  O   ALA D 755    -134.366  25.083 -25.885  1.00 52.08           O  
ANISOU 8314  O   ALA D 755     6191   7621   5974   -446    269   -576       O  
ATOM   8315  CB  ALA D 755    -136.139  26.498 -23.461  1.00 47.58           C  
ANISOU 8315  CB  ALA D 755     5559   7131   5389   -423    244   -580       C  
ATOM   8316  N   ASP D 756    -135.989  23.764 -25.088  1.00 54.78           N  
ANISOU 8316  N   ASP D 756     6494   8026   6293   -548    273   -640       N  
ATOM   8317  CA  ASP D 756    -135.281  22.526 -25.429  1.00 58.22           C  
ANISOU 8317  CA  ASP D 756     6964   8394   6761   -596    284   -658       C  
ATOM   8318  C   ASP D 756    -135.029  22.400 -26.933  1.00 59.54           C  
ANISOU 8318  C   ASP D 756     7127   8592   6902   -568    278   -689       C  
ATOM   8319  O   ASP D 756    -133.957  21.993 -27.333  1.00 56.01           O  
ANISOU 8319  O   ASP D 756     6718   8086   6478   -559    285   -684       O  
ATOM   8320  CB  ASP D 756    -136.045  21.310 -24.908  1.00 60.76           C  
ANISOU 8320  CB  ASP D 756     7267   8717   7101   -682    290   -690       C  
ATOM   8321  CG  ASP D 756    -135.223  19.992 -24.898  1.00 63.89           C  
ANISOU 8321  CG  ASP D 756     7705   9014   7556   -734    301   -700       C  
ATOM   8322  OD1 ASP D 756    -135.167  19.302 -25.945  1.00 66.91           O  
ANISOU 8322  OD1 ASP D 756     8086   9395   7943   -748    293   -754       O  
ATOM   8323  OD2 ASP D 756    -134.693  19.597 -23.834  1.00 62.39           O  
ANISOU 8323  OD2 ASP D 756     7545   8754   7409   -759    317   -658       O  
ATOM   8324  N   SER D 757    -136.020  22.730 -27.755  1.00 60.97           N  
ANISOU 8324  N   SER D 757     7259   8879   7029   -548    264   -723       N  
ATOM   8325  CA  SER D 757    -135.876  22.705 -29.217  1.00 64.75           C  
ANISOU 8325  CA  SER D 757     7720   9418   7464   -508    257   -752       C  
ATOM   8326  C   SER D 757    -134.810  23.707 -29.707  1.00 64.05           C  
ANISOU 8326  C   SER D 757     7652   9314   7371   -428    263   -683       C  
ATOM   8327  O   SER D 757    -134.046  23.412 -30.606  1.00 68.17           O  
ANISOU 8327  O   SER D 757     8184   9838   7880   -402    268   -687       O  
ATOM   8328  CB  SER D 757    -137.237  22.981 -29.897  1.00 62.73           C  
ANISOU 8328  CB  SER D 757     7398   9293   7143   -495    240   -796       C  
ATOM   8329  N   VAL D 758    -134.764  24.890 -29.109  1.00 61.09           N  
ANISOU 8329  N   VAL D 758     7278   8922   7011   -388    263   -620       N  
ATOM   8330  CA  VAL D 758    -133.777  25.912 -29.490  1.00 60.81           C  
ANISOU 8330  CA  VAL D 758     7255   8858   6991   -319    267   -544       C  
ATOM   8331  C   VAL D 758    -132.377  25.435 -29.133  1.00 56.58           C  
ANISOU 8331  C   VAL D 758     6773   8216   6510   -335    282   -521       C  
ATOM   8332  O   VAL D 758    -131.463  25.478 -29.943  1.00 56.95           O  
ANISOU 8332  O   VAL D 758     6828   8259   6552   -300    291   -490       O  
ATOM   8333  CB  VAL D 758    -134.069  27.242 -28.777  1.00 60.10           C  
ANISOU 8333  CB  VAL D 758     7153   8754   6929   -280    256   -495       C  
ATOM   8334  CG1 VAL D 758    -132.909  28.212 -28.922  1.00 61.72           C  
ANISOU 8334  CG1 VAL D 758     7374   8893   7184   -225    259   -413       C  
ATOM   8335  CG2 VAL D 758    -135.333  27.843 -29.348  1.00 59.75           C  
ANISOU 8335  CG2 VAL D 758     7053   8823   6827   -245    242   -507       C  
ATOM   8336  N   GLN D 759    -132.254  24.964 -27.909  1.00 56.26           N  
ANISOU 8336  N   GLN D 759     6764   8100   6513   -386    285   -533       N  
ATOM   8337  CA  GLN D 759    -131.009  24.439 -27.395  1.00 56.45           C  
ANISOU 8337  CA  GLN D 759     6837   8024   6586   -404    298   -515       C  
ATOM   8338  C   GLN D 759    -130.458  23.325 -28.296  1.00 54.50           C  
ANISOU 8338  C   GLN D 759     6607   7776   6326   -419    306   -551       C  
ATOM   8339  O   GLN D 759    -129.278  23.290 -28.584  1.00 54.38           O  
ANISOU 8339  O   GLN D 759     6618   7716   6329   -395    316   -521       O  
ATOM   8340  CB  GLN D 759    -131.235  23.946 -25.975  1.00 56.96           C  
ANISOU 8340  CB  GLN D 759     6921   8038   6684   -457    300   -528       C  
ATOM   8341  CG  GLN D 759    -130.036  23.807 -25.083  1.00 59.08           C  
ANISOU 8341  CG  GLN D 759     7233   8209   7005   -461    309   -496       C  
ATOM   8342  CD  GLN D 759    -130.499  23.334 -23.683  1.00 66.20           C  
ANISOU 8342  CD  GLN D 759     8138   9092   7921   -506    312   -505       C  
ATOM   8343  OE1 GLN D 759    -131.611  23.683 -23.238  1.00 62.31           O  
ANISOU 8343  OE1 GLN D 759     7610   8662   7404   -512    304   -518       O  
ATOM   8344  NE2 GLN D 759    -129.665  22.539 -22.994  1.00 62.31           N  
ANISOU 8344  NE2 GLN D 759     7684   8527   7464   -534    326   -492       N  
ATOM   8345  N   ALA D 760    -131.308  22.398 -28.721  1.00 52.62           N  
ANISOU 8345  N   ALA D 760     6348   7585   6059   -459    300   -622       N  
ATOM   8346  CA  ALA D 760    -130.874  21.324 -29.625  1.00 51.07           C  
ANISOU 8346  CA  ALA D 760     6160   7392   5853   -467    299   -677       C  
ATOM   8347  C   ALA D 760    -130.320  21.892 -30.956  1.00 47.17           C  
ANISOU 8347  C   ALA D 760     5644   6972   5306   -390    300   -656       C  
ATOM   8348  O   ALA D 760    -129.374  21.376 -31.506  1.00 47.12           O  
ANISOU 8348  O   ALA D 760     5656   6949   5298   -371    306   -666       O  
ATOM   8349  CB  ALA D 760    -132.028  20.371 -29.894  1.00 51.94           C  
ANISOU 8349  CB  ALA D 760     6238   7547   5949   -520    284   -766       C  
ATOM   8350  N   LYS D 761    -130.926  22.954 -31.461  1.00 45.65           N  
ANISOU 8350  N   LYS D 761     5409   6867   5068   -342    296   -622       N  
ATOM   8351  CA  LYS D 761    -130.426  23.631 -32.661  1.00 49.29           C  
ANISOU 8351  CA  LYS D 761     5841   7408   5478   -263    301   -574       C  
ATOM   8352  C   LYS D 761    -129.100  24.385 -32.450  1.00 48.70           C  
ANISOU 8352  C   LYS D 761     5792   7264   5447   -227    318   -475       C  
ATOM   8353  O   LYS D 761    -128.243  24.387 -33.350  1.00 46.12           O  
ANISOU 8353  O   LYS D 761     5455   6975   5093   -179    329   -445       O  
ATOM   8354  CB  LYS D 761    -131.514  24.551 -33.235  1.00 50.35           C  
ANISOU 8354  CB  LYS D 761     5918   7656   5557   -221    292   -556       C  
ATOM   8355  N   VAL D 762    -128.932  25.006 -31.277  1.00 43.92           N  
ANISOU 8355  N   VAL D 762     5213   6567   4909   -246    319   -430       N  
ATOM   8356  CA  VAL D 762    -127.671  25.656 -30.915  1.00 41.91           C  
ANISOU 8356  CA  VAL D 762     4981   6230   4712   -223    330   -348       C  
ATOM   8357  C   VAL D 762    -126.563  24.614 -30.862  1.00 41.31           C  
ANISOU 8357  C   VAL D 762     4946   6097   4652   -244    342   -372       C  
ATOM   8358  O   VAL D 762    -125.483  24.798 -31.425  1.00 40.88           O  
ANISOU 8358  O   VAL D 762     4891   6042   4599   -206    355   -321       O  
ATOM   8359  CB  VAL D 762    -127.746  26.357 -29.538  1.00 39.56           C  
ANISOU 8359  CB  VAL D 762     4703   5845   4485   -243    320   -324       C  
ATOM   8360  CG1 VAL D 762    -126.368  26.860 -29.108  1.00 37.68           C  
ANISOU 8360  CG1 VAL D 762     4488   5515   4315   -227    327   -259       C  
ATOM   8361  CG2 VAL D 762    -128.723  27.502 -29.595  1.00 38.61           C  
ANISOU 8361  CG2 VAL D 762     4540   5772   4357   -210    305   -297       C  
ATOM   8362  N   GLU D 763    -126.848  23.506 -30.210  1.00 43.13           N  
ANISOU 8362  N   GLU D 763     5208   6284   4896   -303    338   -445       N  
ATOM   8363  CA  GLU D 763    -125.892  22.406 -30.154  1.00 48.55           C  
ANISOU 8363  CA  GLU D 763     5934   6912   5601   -322    346   -475       C  
ATOM   8364  C   GLU D 763    -125.582  21.882 -31.549  1.00 49.72           C  
ANISOU 8364  C   GLU D 763     6061   7141   5690   -282    348   -509       C  
ATOM   8365  O   GLU D 763    -124.426  21.620 -31.862  1.00 50.49           O  
ANISOU 8365  O   GLU D 763     6173   7218   5791   -255    359   -491       O  
ATOM   8366  CB  GLU D 763    -126.280  21.325 -29.125  1.00 50.38           C  
ANISOU 8366  CB  GLU D 763     6200   7072   5871   -393    343   -533       C  
ATOM   8367  CG  GLU D 763    -126.016  21.858 -27.726  1.00 55.23           C  
ANISOU 8367  CG  GLU D 763     6838   7607   6539   -411    347   -483       C  
ATOM   8368  CD  GLU D 763    -126.554  20.965 -26.656  1.00 60.43           C  
ANISOU 8368  CD  GLU D 763     7517   8217   7226   -475    346   -518       C  
ATOM   8369  OE1 GLU D 763    -127.181  21.573 -25.768  1.00 62.78           O  
ANISOU 8369  OE1 GLU D 763     7803   8520   7532   -486    342   -498       O  
ATOM   8370  OE2 GLU D 763    -126.358  19.710 -26.708  1.00 59.82           O  
ANISOU 8370  OE2 GLU D 763     7463   8099   7166   -510    349   -560       O  
ATOM   8371  N   MET D 764    -126.593  21.768 -32.405  1.00 49.26           N  
ANISOU 8371  N   MET D 764     5959   7186   5571   -270    336   -561       N  
ATOM   8372  CA  MET D 764    -126.323  21.419 -33.787  1.00 51.65           C  
ANISOU 8372  CA  MET D 764     6228   7592   5803   -216    334   -594       C  
ATOM   8373  C   MET D 764    -125.348  22.412 -34.416  1.00 47.22           C  
ANISOU 8373  C   MET D 764     5645   7076   5219   -144    354   -488       C  
ATOM   8374  O   MET D 764    -124.371  22.006 -35.045  1.00 43.06           O  
ANISOU 8374  O   MET D 764     5118   6575   4668   -106    363   -488       O  
ATOM   8375  CB  MET D 764    -127.590  21.359 -34.621  1.00 56.21           C  
ANISOU 8375  CB  MET D 764     6753   8294   6312   -204    316   -659       C  
ATOM   8376  CG  MET D 764    -127.287  21.088 -36.100  1.00 60.96           C  
ANISOU 8376  CG  MET D 764     7308   9028   6826   -131    313   -694       C  
ATOM   8377  SD  MET D 764    -128.714  21.428 -37.102  1.00 68.55           S  
ANISOU 8377  SD  MET D 764     8193  10158   7693    -96    294   -739       S  
ATOM   8378  CE  MET D 764    -128.553  23.208 -37.223  1.00 71.12           C  
ANISOU 8378  CE  MET D 764     8491  10528   8004    -33    319   -571       C  
ATOM   8379  N   LEU D 765    -125.633  23.703 -34.278  1.00 43.79           N  
ANISOU 8379  N   LEU D 765     5187   6656   4795   -122    359   -397       N  
ATOM   8380  CA  LEU D 765    -124.751  24.713 -34.851  1.00 44.88           C  
ANISOU 8380  CA  LEU D 765     5297   6827   4930    -59    378   -279       C  
ATOM   8381  C   LEU D 765    -123.321  24.623 -34.305  1.00 45.09           C  
ANISOU 8381  C   LEU D 765     5362   6752   5018    -68    392   -233       C  
ATOM   8382  O   LEU D 765    -122.362  24.771 -35.049  1.00 49.88           O  
ANISOU 8382  O   LEU D 765     5945   7406   5601    -19    409   -176       O  
ATOM   8383  CB  LEU D 765    -125.297  26.107 -34.626  1.00 44.97           C  
ANISOU 8383  CB  LEU D 765     5279   6836   4969    -42    376   -191       C  
ATOM   8384  CG  LEU D 765    -126.553  26.490 -35.405  1.00 50.47           C  
ANISOU 8384  CG  LEU D 765     5923   7659   5594     -9    366   -202       C  
ATOM   8385  CD1 LEU D 765    -126.912  27.940 -35.117  1.00 53.47           C  
ANISOU 8385  CD1 LEU D 765     6279   8015   6022     15    364   -102       C  
ATOM   8386  CD2 LEU D 765    -126.358  26.283 -36.896  1.00 52.52           C  
ANISOU 8386  CD2 LEU D 765     6129   8072   5754     61    377   -193       C  
ATOM   8387  N   ASP D 766    -123.174  24.348 -33.014  1.00 44.21           N  
ANISOU 8387  N   ASP D 766     5303   6513   4980   -127    386   -258       N  
ATOM   8388  CA  ASP D 766    -121.844  24.171 -32.440  1.00 43.83           C  
ANISOU 8388  CA  ASP D 766     5291   6373   4988   -135    398   -226       C  
ATOM   8389  C   ASP D 766    -121.110  23.054 -33.168  1.00 40.95           C  
ANISOU 8389  C   ASP D 766     4935   6048   4577   -115    405   -277       C  
ATOM   8390  O   ASP D 766    -119.926  23.185 -33.483  1.00 39.22           O  
ANISOU 8390  O   ASP D 766     4710   5831   4362    -81    421   -221       O  
ATOM   8391  CB  ASP D 766    -121.919  23.829 -30.944  1.00 44.62           C  
ANISOU 8391  CB  ASP D 766     5445   6352   5158   -198    389   -262       C  
ATOM   8392  CG  ASP D 766    -122.574  24.921 -30.122  1.00 47.10           C  
ANISOU 8392  CG  ASP D 766     5748   6628   5518   -210    377   -225       C  
ATOM   8393  OD1 ASP D 766    -122.645  26.096 -30.575  1.00 44.55           O  
ANISOU 8393  OD1 ASP D 766     5386   6339   5204   -171    376   -151       O  
ATOM   8394  OD2 ASP D 766    -123.003  24.591 -28.989  1.00 53.34           O  
ANISOU 8394  OD2 ASP D 766     6569   7357   6340   -256    367   -268       O  
ATOM   8395  N   ASN D 767    -121.807  21.934 -33.373  1.00 42.34           N  
ANISOU 8395  N   ASN D 767     5123   6248   4718   -138    391   -387       N  
ATOM   8396  CA  ASN D 767    -121.210  20.749 -33.973  1.00 44.78           C  
ANISOU 8396  CA  ASN D 767     5441   6578   4994   -120    389   -461       C  
ATOM   8397  C   ASN D 767    -120.878  21.046 -35.429  1.00 46.20           C  
ANISOU 8397  C   ASN D 767     5562   6907   5086    -38    398   -436       C  
ATOM   8398  O   ASN D 767    -119.809  20.703 -35.903  1.00 46.40           O  
ANISOU 8398  O   ASN D 767     5584   6958   5089      3    409   -428       O  
ATOM   8399  CB  ASN D 767    -122.133  19.525 -33.794  1.00 44.50           C  
ANISOU 8399  CB  ASN D 767     5426   6518   4964   -170    366   -589       C  
ATOM   8400  CG  ASN D 767    -121.508  18.201 -34.276  1.00 48.84           C  
ANISOU 8400  CG  ASN D 767     5992   7061   5503   -156    356   -682       C  
ATOM   8401  OD1 ASN D 767    -122.211  17.261 -34.722  1.00 52.42           O  
ANISOU 8401  OD1 ASN D 767     6435   7540   5941   -169    332   -795       O  
ATOM   8402  ND2 ASN D 767    -120.192  18.113 -34.171  1.00 46.18           N  
ANISOU 8402  ND2 ASN D 767     5677   6686   5181   -128    371   -640       N  
ATOM   8403  N   LEU D 768    -121.762  21.774 -36.100  1.00 50.78           N  
ANISOU 8403  N   LEU D 768     6090   7593   5613    -10    396   -410       N  
ATOM   8404  CA  LEU D 768    -121.502  22.207 -37.478  1.00 53.74           C  
ANISOU 8404  CA  LEU D 768     6396   8129   5895     76    407   -363       C  
ATOM   8405  C   LEU D 768    -120.240  23.052 -37.567  1.00 52.50           C  
ANISOU 8405  C   LEU D 768     6223   7965   5759    114    437   -225       C  
ATOM   8406  O   LEU D 768    -119.431  22.857 -38.468  1.00 53.04           O  
ANISOU 8406  O   LEU D 768     6256   8131   5765    177    450   -205       O  
ATOM   8407  CB  LEU D 768    -122.699  22.998 -38.047  1.00 55.22           C  
ANISOU 8407  CB  LEU D 768     6529   8423   6030    101    402   -338       C  
ATOM   8408  CG  LEU D 768    -123.940  22.184 -38.438  1.00 57.09           C  
ANISOU 8408  CG  LEU D 768     6751   8729   6212     88    373   -476       C  
ATOM   8409  CD1 LEU D 768    -124.971  23.083 -39.105  1.00 56.82           C  
ANISOU 8409  CD1 LEU D 768     6655   8822   6115    129    372   -434       C  
ATOM   8410  CD2 LEU D 768    -123.573  21.023 -39.347  1.00 58.51           C  
ANISOU 8410  CD2 LEU D 768     6913   8995   6322    129    360   -589       C  
ATOM   8411  N   LEU D 769    -120.084  23.990 -36.643  1.00 50.61           N  
ANISOU 8411  N   LEU D 769     6004   7617   5610     78    444   -134       N  
ATOM   8412  CA  LEU D 769    -118.900  24.849 -36.629  1.00 54.01           C  
ANISOU 8412  CA  LEU D 769     6416   8022   6084    103    467     -1       C  
ATOM   8413  C   LEU D 769    -117.588  24.034 -36.563  1.00 55.01           C  
ANISOU 8413  C   LEU D 769     6568   8119   6214    109    478    -23       C  
ATOM   8414  O   LEU D 769    -116.668  24.239 -37.354  1.00 56.84           O  
ANISOU 8414  O   LEU D 769     6756   8434   6407    166    499     50       O  
ATOM   8415  CB  LEU D 769    -118.975  25.860 -35.478  1.00 58.62           C  
ANISOU 8415  CB  LEU D 769     7022   8471   6781     56    462     67       C  
ATOM   8416  CG  LEU D 769    -119.094  27.364 -35.798  1.00 60.37           C  
ANISOU 8416  CG  LEU D 769     7187   8714   7037     86    470    206       C  
ATOM   8417  CD1 LEU D 769    -118.759  28.103 -34.509  1.00 56.52           C  
ANISOU 8417  CD1 LEU D 769     6730   8067   6679     39    459    244       C  
ATOM   8418  CD2 LEU D 769    -118.253  27.902 -36.951  1.00 61.79           C  
ANISOU 8418  CD2 LEU D 769     7297   9000   7179    154    499    331       C  
ATOM   8419  N   ASP D 770    -117.506  23.104 -35.624  1.00 54.43           N  
ANISOU 8419  N   ASP D 770     6562   7934   6185     56    464   -117       N  
ATOM   8420  CA  ASP D 770    -116.296  22.320 -35.462  1.00 58.56           C  
ANISOU 8420  CA  ASP D 770     7113   8417   6718     62    471   -141       C  
ATOM   8421  C   ASP D 770    -116.111  21.345 -36.639  1.00 55.49           C  
ANISOU 8421  C   ASP D 770     6700   8156   6230    122    469   -220       C  
ATOM   8422  O   ASP D 770    -114.971  21.000 -37.000  1.00 49.19           O  
ANISOU 8422  O   ASP D 770     5893   7389   5409    164    482   -206       O  
ATOM   8423  CB  ASP D 770    -116.297  21.585 -34.112  1.00 62.57           C  
ANISOU 8423  CB  ASP D 770     7698   8773   7302     -7    457   -211       C  
ATOM   8424  CG  ASP D 770    -115.807  22.474 -32.926  1.00 65.85           C  
ANISOU 8424  CG  ASP D 770     8134   9072   7814    -44    462   -128       C  
ATOM   8425  OD1 ASP D 770    -114.915  23.337 -33.099  1.00 68.64           O  
ANISOU 8425  OD1 ASP D 770     8455   9434   8192    -18    478    -26       O  
ATOM   8426  OD2 ASP D 770    -116.307  22.287 -31.796  1.00 64.89           O  
ANISOU 8426  OD2 ASP D 770     8056   8852   7745    -99    448   -168       O  
ATOM   8427  N   ILE D 771    -117.214  20.896 -37.227  1.00 51.30           N  
ANISOU 8427  N   ILE D 771     6152   7701   5638    130    450   -310       N  
ATOM   8428  CA  ILE D 771    -117.131  20.098 -38.460  1.00 54.01           C  
ANISOU 8428  CA  ILE D 771     6455   8187   5879    200    442   -394       C  
ATOM   8429  C   ILE D 771    -116.507  20.915 -39.611  1.00 53.65           C  
ANISOU 8429  C   ILE D 771     6329   8307   5750    288    469   -281       C  
ATOM   8430  O   ILE D 771    -115.608  20.429 -40.291  1.00 49.44           O  
ANISOU 8430  O   ILE D 771     5769   7859   5156    351    477   -296       O  
ATOM   8431  CB  ILE D 771    -118.499  19.502 -38.857  1.00 52.57           C  
ANISOU 8431  CB  ILE D 771     6262   8058   5654    189    411   -521       C  
ATOM   8432  CG1 ILE D 771    -118.814  18.318 -37.940  1.00 52.54           C  
ANISOU 8432  CG1 ILE D 771     6329   7907   5728    115    384   -645       C  
ATOM   8433  CG2 ILE D 771    -118.481  19.017 -40.306  1.00 54.05           C  
ANISOU 8433  CG2 ILE D 771     6384   8434   5720    280    401   -593       C  
ATOM   8434  CD1 ILE D 771    -120.276  17.939 -37.893  1.00 54.24           C  
ANISOU 8434  CD1 ILE D 771     6542   8122   5945     70    356   -742       C  
ATOM   8435  N   GLU D 772    -116.946  22.159 -39.777  1.00 53.78           N  
ANISOU 8435  N   GLU D 772     6303   8365   5767    295    485   -160       N  
ATOM   8436  CA  GLU D 772    -116.330  23.056 -40.746  1.00 60.46           C  
ANISOU 8436  CA  GLU D 772     7069   9351   6554    371    516    -19       C  
ATOM   8437  C   GLU D 772    -114.817  23.183 -40.485  1.00 64.06           C  
ANISOU 8437  C   GLU D 772     7528   9760   7053    378    541     67       C  
ATOM   8438  O   GLU D 772    -114.017  23.140 -41.422  1.00 65.81           O  
ANISOU 8438  O   GLU D 772     7690  10120   7195    453    562    115       O  
ATOM   8439  CB  GLU D 772    -117.020  24.426 -40.730  1.00 63.40           C  
ANISOU 8439  CB  GLU D 772     7404   9727   6957    364    527    110       C  
ATOM   8440  CG  GLU D 772    -116.587  25.456 -41.794  1.00 69.88           C  
ANISOU 8440  CG  GLU D 772     8130  10699   7722    442    561    279       C  
ATOM   8441  CD  GLU D 772    -115.181  26.038 -41.604  1.00 70.73           C  
ANISOU 8441  CD  GLU D 772     8220  10760   7895    445    591    420       C  
ATOM   8442  OE1 GLU D 772    -114.784  26.328 -40.447  1.00 76.26           O  
ANISOU 8442  OE1 GLU D 772     8975  11278   8722    373    586    441       O  
ATOM   8443  OE2 GLU D 772    -114.485  26.246 -42.626  1.00 75.39           O  
ANISOU 8443  OE2 GLU D 772     8733  11504   8407    521    620    514       O  
ATOM   8444  N   VAL D 773    -114.423  23.327 -39.222  1.00 61.55           N  
ANISOU 8444  N   VAL D 773     7274   9258   6854    304    539     85       N  
ATOM   8445  CA  VAL D 773    -113.000  23.433 -38.887  1.00 63.27           C  
ANISOU 8445  CA  VAL D 773     7496   9425   7121    306    559    157       C  
ATOM   8446  C   VAL D 773    -112.259  22.188 -39.346  1.00 62.71           C  
ANISOU 8446  C   VAL D 773     7432   9416   6977    352    556     58       C  
ATOM   8447  O   VAL D 773    -111.178  22.273 -39.932  1.00 65.61           O  
ANISOU 8447  O   VAL D 773     7753   9872   7305    407    580    127       O  
ATOM   8448  CB  VAL D 773    -112.770  23.647 -37.365  1.00 62.80           C  
ANISOU 8448  CB  VAL D 773     7505   9160   7194    221    549    162       C  
ATOM   8449  CG1 VAL D 773    -111.294  23.508 -37.011  1.00 61.03           C  
ANISOU 8449  CG1 VAL D 773     7289   8890   7011    224    564    206       C  
ATOM   8450  CG2 VAL D 773    -113.305  25.011 -36.939  1.00 61.47           C  
ANISOU 8450  CG2 VAL D 773     7318   8933   7106    188    549    268       C  
ATOM   8451  N   ALA D 774    -112.837  21.032 -39.047  1.00 59.17           N  
ANISOU 8451  N   ALA D 774     7041   8918   6522    327    526   -102       N  
ATOM   8452  CA  ALA D 774    -112.213  19.767 -39.387  1.00 61.46           C  
ANISOU 8452  CA  ALA D 774     7347   9241   6764    368    515   -217       C  
ATOM   8453  C   ALA D 774    -112.099  19.632 -40.908  1.00 66.05           C  
ANISOU 8453  C   ALA D 774     7844  10046   7207    473    521   -228       C  
ATOM   8454  O   ALA D 774    -111.043  19.262 -41.416  1.00 73.29           O  
ANISOU 8454  O   ALA D 774     8732  11043   8071    536    533   -225       O  
ATOM   8455  CB  ALA D 774    -113.010  18.610 -38.804  1.00 57.32           C  
ANISOU 8455  CB  ALA D 774     6893   8611   6276    317    477   -380       C  
ATOM   8456  N   TYR D 775    -113.177  19.966 -41.617  1.00 66.55           N  
ANISOU 8456  N   TYR D 775     7862  10219   7205    496    513   -239       N  
ATOM   8457  CA  TYR D 775    -113.200  19.869 -43.073  1.00 68.89           C  
ANISOU 8457  CA  TYR D 775     8069  10748   7357    603    517   -254       C  
ATOM   8458  C   TYR D 775    -112.194  20.817 -43.720  1.00 67.44           C  
ANISOU 8458  C   TYR D 775     7806  10693   7126    667    562    -72       C  
ATOM   8459  O   TYR D 775    -111.510  20.418 -44.644  1.00 65.56           O  
ANISOU 8459  O   TYR D 775     7509  10617   6783    758    571    -88       O  
ATOM   8460  CB  TYR D 775    -114.602  20.114 -43.642  1.00 68.06           C  
ANISOU 8460  CB  TYR D 775     7928  10738   7194    614    500   -294       C  
ATOM   8461  N   SER D 776    -112.092  22.049 -43.217  1.00 65.14           N  
ANISOU 8461  N   SER D 776     7508  10325   6917    621    589     97       N  
ATOM   8462  CA  SER D 776    -111.103  23.018 -43.706  1.00 67.34           C  
ANISOU 8462  CA  SER D 776     7709  10694   7183    665    633    290       C  
ATOM   8463  C   SER D 776    -109.681  22.558 -43.520  1.00 70.84           C  
ANISOU 8463  C   SER D 776     8159  11119   7638    681    647    299       C  
ATOM   8464  O   SER D 776    -108.860  22.695 -44.420  1.00 78.80           O  
ANISOU 8464  O   SER D 776     9086  12295   8560    762    676    380       O  
ATOM   8465  CB  SER D 776    -111.239  24.354 -42.993  1.00 67.20           C  
ANISOU 8465  CB  SER D 776     7694  10548   7290    597    650    449       C  
ATOM   8466  OG  SER D 776    -112.435  24.977 -43.389  1.00 71.25           O  
ANISOU 8466  OG  SER D 776     8177  11119   7777    605    645    479       O  
ATOM   8467  N   LEU D 777    -109.372  22.043 -42.342  1.00 70.88           N  
ANISOU 8467  N   LEU D 777     8256  10929   7747    606    630    225       N  
ATOM   8468  CA  LEU D 777    -108.028  21.555 -42.088  1.00 72.77           C  
ANISOU 8468  CA  LEU D 777     8507  11143   8001    620    640    224       C  
ATOM   8469  C   LEU D 777    -107.686  20.463 -43.091  1.00 73.53           C  
ANISOU 8469  C   LEU D 777     8569  11406   7961    719    631    108       C  
ATOM   8470  O   LEU D 777    -106.595  20.453 -43.659  1.00 71.57           O  
ANISOU 8470  O   LEU D 777     8262  11277   7653    786    656    170       O  
ATOM   8471  CB  LEU D 777    -107.898  21.010 -40.665  1.00 73.16           C  
ANISOU 8471  CB  LEU D 777     8663  10964   8170    532    617    140       C  
ATOM   8472  CG  LEU D 777    -107.791  22.041 -39.539  1.00 73.03           C  
ANISOU 8472  CG  LEU D 777     8674  10781   8293    446    626    253       C  
ATOM   8473  CD1 LEU D 777    -107.737  21.306 -38.208  1.00 70.26           C  
ANISOU 8473  CD1 LEU D 777     8425  10240   8032    375    600    148       C  
ATOM   8474  CD2 LEU D 777    -106.567  22.937 -39.707  1.00 72.80           C  
ANISOU 8474  CD2 LEU D 777     8578  10789   8292    463    661    421       C  
ATOM   8475  N   LEU D 778    -108.634  19.553 -43.293  1.00 74.81           N  
ANISOU 8475  N   LEU D 778     8765  11579   8081    728    593    -65       N  
ATOM   8476  CA  LEU D 778    -108.438  18.392 -44.163  1.00 76.06           C  
ANISOU 8476  CA  LEU D 778     8899  11874   8125    820    570   -216       C  
ATOM   8477  C   LEU D 778    -108.239  18.838 -45.616  1.00 77.99           C  
ANISOU 8477  C   LEU D 778     9021  12396   8215    937    595   -141       C  
ATOM   8478  O   LEU D 778    -107.379  18.289 -46.308  1.00 80.07           O  
ANISOU 8478  O   LEU D 778     9237  12801   8386   1028    599   -178       O  
ATOM   8479  CB  LEU D 778    -109.594  17.392 -44.020  1.00 74.51           C  
ANISOU 8479  CB  LEU D 778     8759  11611   7939    792    519   -417       C  
ATOM   8480  N   ARG D 779    -109.002  19.853 -46.031  1.00 77.54           N  
ANISOU 8480  N   ARG D 779     8911  12417   8133    936    613    -28       N  
ATOM   8481  CA  ARG D 779    -108.889  20.523 -47.322  1.00 79.76           C  
ANISOU 8481  CA  ARG D 779     9068  12958   8279   1040    646     92       C  
ATOM   8482  C   ARG D 779    -108.212  21.880 -47.151  1.00 78.49           C  
ANISOU 8482  C   ARG D 779     8860  12781   8180   1013    698    346       C  
ATOM   8483  O   ARG D 779    -107.019  21.950 -46.880  1.00 69.52           O  
ANISOU 8483  O   ARG D 779     7717  11614   7081   1011    722    422       O  
ATOM   8484  CB  ARG D 779    -110.287  20.716 -47.941  1.00 77.04           C  
ANISOU 8484  CB  ARG D 779     8691  12716   7865   1063    627     46       C  
ATOM   8485  N   ASP D 788     -97.041  10.113 -45.573  1.00 68.67           N  
ANISOU 8485  N   ASP D 788     7920  11349   6822   1566    502   -911       N  
ATOM   8486  CA  ASP D 788     -98.289   9.437 -45.236  1.00 76.80           C  
ANISOU 8486  CA  ASP D 788     9033  12213   7936   1508    450  -1066       C  
ATOM   8487  C   ASP D 788     -99.371  10.472 -44.855  1.00 79.50           C  
ANISOU 8487  C   ASP D 788     9391  12479   8337   1390    472   -947       C  
ATOM   8488  O   ASP D 788     -99.123  11.335 -44.000  1.00 76.03           O  
ANISOU 8488  O   ASP D 788     8979  11930   7980   1295    511   -782       O  
ATOM   8489  CB  ASP D 788     -98.078   8.443 -44.074  1.00 77.53           C  
ANISOU 8489  CB  ASP D 788     9243  12041   8172   1452    416  -1166       C  
ATOM   8490  CG  ASP D 788     -99.273   7.487 -43.876  1.00 79.88           C  
ANISOU 8490  CG  ASP D 788     9615  12185   8553   1414    354  -1353       C  
ATOM   8491  OD1 ASP D 788    -100.401   7.832 -44.298  1.00 77.11           O  
ANISOU 8491  OD1 ASP D 788     9242  11877   8180   1385    344  -1371       O  
ATOM   8492  OD2 ASP D 788     -99.102   6.401 -43.268  1.00 82.95           O  
ANISOU 8492  OD2 ASP D 788    10080  12400   9037   1407    314  -1475       O  
ATOM   8493  N   PRO D 789    -100.575  10.384 -45.473  1.00 82.49           N  
ANISOU 8493  N   PRO D 789     9752  12916   8676   1397    443  -1037       N  
ATOM   8494  CA  PRO D 789    -101.643  11.344 -45.144  1.00 83.91           C  
ANISOU 8494  CA  PRO D 789     9945  13031   8907   1293    462   -931       C  
ATOM   8495  C   PRO D 789    -102.033  11.417 -43.653  1.00 81.41           C  
ANISOU 8495  C   PRO D 789     9743  12425   8765   1147    460   -896       C  
ATOM   8496  O   PRO D 789    -102.343  12.501 -43.164  1.00 79.28           O  
ANISOU 8496  O   PRO D 789     9476  12103   8544   1064    494   -743       O  
ATOM   8497  CB  PRO D 789    -102.826  10.853 -45.984  1.00 82.24           C  
ANISOU 8497  CB  PRO D 789     9707  12907   8632   1335    416  -1091       C  
ATOM   8498  CG  PRO D 789    -102.193  10.198 -47.149  1.00 83.81           C  
ANISOU 8498  CG  PRO D 789     9825  13333   8688   1490    397  -1204       C  
ATOM   8499  CD  PRO D 789    -100.950   9.539 -46.623  1.00 82.64           C  
ANISOU 8499  CD  PRO D 789     9717  13100   8583   1515    396  -1229       C  
ATOM   8500  N   ILE D 790    -102.000  10.291 -42.946  1.00 83.41           N  
ANISOU 8500  N   ILE D 790    10083  12499   9110   1122    420  -1033       N  
ATOM   8501  CA  ILE D 790    -102.247  10.289 -41.510  1.00 83.79           C  
ANISOU 8501  CA  ILE D 790    10233  12293   9312    998    421   -993       C  
ATOM   8502  C   ILE D 790    -101.285  11.255 -40.805  1.00 86.30           C  
ANISOU 8502  C   ILE D 790    10547  12579   9664    957    472   -803       C  
ATOM   8503  O   ILE D 790    -101.717  12.052 -39.962  1.00 91.81           O  
ANISOU 8503  O   ILE D 790    11278  13163  10444    856    491   -697       O  
ATOM   8504  CB  ILE D 790    -102.125   8.875 -40.917  1.00 84.55           C  
ANISOU 8504  CB  ILE D 790    10411  12218   9496    996    376  -1151       C  
ATOM   8505  CG1 ILE D 790    -103.273   7.991 -41.417  1.00 84.96           C  
ANISOU 8505  CG1 ILE D 790    10472  12252   9557   1005    320  -1335       C  
ATOM   8506  CG2 ILE D 790    -102.185   8.925 -39.396  1.00 85.37           C  
ANISOU 8506  CG2 ILE D 790    10609  12085   9745    879    385  -1082       C  
ATOM   8507  CD1 ILE D 790    -102.923   6.518 -41.491  1.00 87.32           C  
ANISOU 8507  CD1 ILE D 790    10805  12477   9894   1065    267  -1520       C  
ATOM   8508  N   ASP D 791    -100.000  11.208 -41.167  1.00 81.36           N  
ANISOU 8508  N   ASP D 791     9875  12064   8975   1037    492   -766       N  
ATOM   8509  CA  ASP D 791     -99.003  12.127 -40.594  1.00 76.70           C  
ANISOU 8509  CA  ASP D 791     9266  11461   8415   1004    538   -589       C  
ATOM   8510  C   ASP D 791     -99.255  13.590 -40.968  1.00 74.21           C  
ANISOU 8510  C   ASP D 791     8876  11248   8071    973    580   -415       C  
ATOM   8511  O   ASP D 791     -99.006  14.500 -40.171  1.00 69.38           O  
ANISOU 8511  O   ASP D 791     8274  10545   7542    895    606   -278       O  
ATOM   8512  CB  ASP D 791     -97.577  11.744 -41.026  1.00 79.92           C  
ANISOU 8512  CB  ASP D 791     9625  11989   8750   1105    550   -588       C  
ATOM   8513  CG  ASP D 791     -97.016  10.545 -40.255  1.00 81.72           C  
ANISOU 8513  CG  ASP D 791     9936  12067   9045   1114    520   -705       C  
ATOM   8514  OD1 ASP D 791     -95.773  10.371 -40.257  1.00 93.18           O  
ANISOU 8514  OD1 ASP D 791    11363  13575  10467   1173    535   -677       O  
ATOM   8515  OD2 ASP D 791     -97.794   9.772 -39.664  1.00 80.33           O  
ANISOU 8515  OD2 ASP D 791     9846  11723   8953   1066    482   -818       O  
ATOM   8516  N   VAL D 792     -99.723  13.827 -42.191  1.00 73.78           N  
ANISOU 8516  N   VAL D 792     8742  11388   7902   1041    583   -419       N  
ATOM   8517  CA  VAL D 792     -99.988  15.196 -42.638  1.00 72.03           C  
ANISOU 8517  CA  VAL D 792     8443  11272   7652   1022    623   -245       C  
ATOM   8518  C   VAL D 792    -101.112  15.799 -41.790  1.00 68.64           C  
ANISOU 8518  C   VAL D 792     8076  10669   7335    903    616   -211       C  
ATOM   8519  O   VAL D 792    -101.005  16.927 -41.315  1.00 65.79           O  
ANISOU 8519  O   VAL D 792     7700  10256   7042    838    645    -54       O  
ATOM   8520  CB  VAL D 792    -100.381  15.258 -44.136  1.00 71.56           C  
ANISOU 8520  CB  VAL D 792     8284  11468   7437   1127    626   -263       C  
ATOM   8521  CG1 VAL D 792    -100.846  16.663 -44.518  1.00 71.21           C  
ANISOU 8521  CG1 VAL D 792     8168  11507   7380   1099    664    -78       C  
ATOM   8522  CG2 VAL D 792     -99.217  14.819 -45.008  1.00 70.97           C  
ANISOU 8522  CG2 VAL D 792     8130  11596   7240   1254    638   -276       C  
ATOM   8523  N   ASN D 793    -102.180  15.036 -41.604  1.00 62.29           N  
ANISOU 8523  N   ASN D 793     7337   9777   6554    877    575   -361       N  
ATOM   8524  CA  ASN D 793    -103.318  15.500 -40.818  1.00 63.64           C  
ANISOU 8524  CA  ASN D 793     7564   9796   6820    771    566   -344       C  
ATOM   8525  C   ASN D 793    -103.029  15.592 -39.311  1.00 59.95           C  
ANISOU 8525  C   ASN D 793     7180   9105   6492    674    567   -307       C  
ATOM   8526  O   ASN D 793    -103.480  16.522 -38.667  1.00 62.05           O  
ANISOU 8526  O   ASN D 793     7458   9286   6831    596    578   -212       O  
ATOM   8527  CB  ASN D 793    -104.523  14.633 -41.125  1.00 59.68           C  
ANISOU 8527  CB  ASN D 793     7095   9282   6299    775    522   -513       C  
ATOM   8528  CG  ASN D 793    -104.996  14.839 -42.552  1.00 60.53           C  
ANISOU 8528  CG  ASN D 793     7109   9619   6270    862    522   -529       C  
ATOM   8529  OD1 ASN D 793    -105.367  15.951 -42.943  1.00 65.16           O  
ANISOU 8529  OD1 ASN D 793     7638  10295   6825    856    550   -399       O  
ATOM   8530  ND2 ASN D 793    -104.877  13.816 -43.365  1.00 60.98           N  
ANISOU 8530  ND2 ASN D 793     7144   9785   6242    954    492   -680       N  
ATOM   8531  N   TYR D 794    -102.223  14.676 -38.781  1.00 57.85           N  
ANISOU 8531  N   TYR D 794     6963   8759   6256    687    554   -377       N  
ATOM   8532  CA  TYR D 794    -101.714  14.787 -37.416  1.00 59.33           C  
ANISOU 8532  CA  TYR D 794     7214   8771   6556    614    560   -329       C  
ATOM   8533  C   TYR D 794    -101.072  16.147 -37.186  1.00 59.34           C  
ANISOU 8533  C   TYR D 794     7163   8796   6588    585    597   -152       C  
ATOM   8534  O   TYR D 794    -101.415  16.839 -36.241  1.00 58.60           O  
ANISOU 8534  O   TYR D 794     7100   8578   6586    502    599    -90       O  
ATOM   8535  CB  TYR D 794    -100.690  13.686 -37.126  1.00 58.95           C  
ANISOU 8535  CB  TYR D 794     7202   8683   6512    661    548   -409       C  
ATOM   8536  CG  TYR D 794     -99.926  13.844 -35.832  1.00 57.31           C  
ANISOU 8536  CG  TYR D 794     7041   8334   6398    607    558   -346       C  
ATOM   8537  CD1 TYR D 794    -100.533  13.598 -34.617  1.00 57.76           C  
ANISOU 8537  CD1 TYR D 794     7180   8210   6555    525    542   -375       C  
ATOM   8538  CD2 TYR D 794     -98.592  14.218 -35.822  1.00 57.06           C  
ANISOU 8538  CD2 TYR D 794     6966   8361   6352    641    584   -259       C  
ATOM   8539  CE1 TYR D 794     -99.841  13.736 -33.427  1.00 53.52           C  
ANISOU 8539  CE1 TYR D 794     6680   7562   6094    484    549   -323       C  
ATOM   8540  CE2 TYR D 794     -97.887  14.350 -34.639  1.00 55.20           C  
ANISOU 8540  CE2 TYR D 794     6768   8006   6199    596    590   -212       C  
ATOM   8541  CZ  TYR D 794     -98.522  14.115 -33.436  1.00 52.66           C  
ANISOU 8541  CZ  TYR D 794     6528   7511   5970    520    571   -246       C  
ATOM   8542  OH  TYR D 794     -97.835  14.245 -32.244  1.00 46.24           O  
ANISOU 8542  OH  TYR D 794     5745   6594   5228    483    575   -204       O  
ATOM   8543  N   GLU D 795    -100.166  16.535 -38.076  1.00 61.69           N  
ANISOU 8543  N   GLU D 795     7375   9257   6809    656    625    -72       N  
ATOM   8544  CA  GLU D 795     -99.451  17.808 -37.953  1.00 61.09           C  
ANISOU 8544  CA  GLU D 795     7236   9206   6771    630    660    104       C  
ATOM   8545  C   GLU D 795    -100.397  19.009 -37.988  1.00 57.20           C  
ANISOU 8545  C   GLU D 795     6715   8699   6319    572    669    203       C  
ATOM   8546  O   GLU D 795    -100.135  20.027 -37.355  1.00 51.13           O  
ANISOU 8546  O   GLU D 795     5932   7852   5643    512    682    319       O  
ATOM   8547  CB  GLU D 795     -98.356  17.929 -39.036  1.00 65.10           C  
ANISOU 8547  CB  GLU D 795     7643   9915   7177    723    690    177       C  
ATOM   8548  CG  GLU D 795     -97.153  17.018 -38.756  1.00 69.13           C  
ANISOU 8548  CG  GLU D 795     8173  10420   7673    770    687    115       C  
ATOM   8549  CD  GLU D 795     -96.091  16.959 -39.861  1.00 72.63           C  
ANISOU 8549  CD  GLU D 795     8517  11080   8000    875    713    164       C  
ATOM   8550  OE1 GLU D 795     -96.284  17.523 -40.967  1.00 72.49           O  
ANISOU 8550  OE1 GLU D 795     8407  11241   7894    925    736    242       O  
ATOM   8551  OE2 GLU D 795     -95.044  16.324 -39.607  1.00 71.25           O  
ANISOU 8551  OE2 GLU D 795     8352  10904   7816    914    712    126       O  
ATOM   8552  N   LYS D 796    -101.497  18.883 -38.722  1.00 57.91           N  
ANISOU 8552  N   LYS D 796     6797   8862   6345    594    658    151       N  
ATOM   8553  CA  LYS D 796    -102.479  19.967 -38.812  1.00 57.47           C  
ANISOU 8553  CA  LYS D 796     6716   8799   6321    549    664    237       C  
ATOM   8554  C   LYS D 796    -103.180  20.272 -37.489  1.00 56.45           C  
ANISOU 8554  C   LYS D 796     6666   8466   6318    446    644    220       C  
ATOM   8555  O   LYS D 796    -103.687  21.388 -37.301  1.00 54.62           O  
ANISOU 8555  O   LYS D 796     6410   8198   6144    401    650    317       O  
ATOM   8556  CB  LYS D 796    -103.528  19.642 -39.867  1.00 60.57           C  
ANISOU 8556  CB  LYS D 796     7083   9322   6608    600    653    166       C  
ATOM   8557  CG  LYS D 796    -103.042  19.748 -41.304  1.00 61.51           C  
ANISOU 8557  CG  LYS D 796     7096   9682   6592    707    678    221       C  
ATOM   8558  CD  LYS D 796    -104.087  19.172 -42.245  1.00 65.74           C  
ANISOU 8558  CD  LYS D 796     7616  10342   7019    764    656    104       C  
ATOM   8559  CE  LYS D 796    -103.650  19.195 -43.708  1.00 70.31           C  
ANISOU 8559  CE  LYS D 796     8083  11188   7443    886    678    144       C  
ATOM   8560  NZ  LYS D 796    -104.611  18.438 -44.563  1.00 70.49           N  
ANISOU 8560  NZ  LYS D 796     8095  11330   7357    949    647    -10       N  
ATOM   8561  N   LEU D 797    -103.235  19.278 -36.593  1.00 53.62           N  
ANISOU 8561  N   LEU D 797     6395   7980   5999    416    618     97       N  
ATOM   8562  CA  LEU D 797    -103.822  19.465 -35.265  1.00 53.24           C  
ANISOU 8562  CA  LEU D 797     6418   7751   6059    327    600     78       C  
ATOM   8563  C   LEU D 797    -102.957  20.337 -34.377  1.00 54.31           C  
ANISOU 8563  C   LEU D 797     6544   7803   6290    285    611    182       C  
ATOM   8564  O   LEU D 797    -103.461  20.881 -33.403  1.00 52.93           O  
ANISOU 8564  O   LEU D 797     6401   7509   6201    218    598    195       O  
ATOM   8565  CB  LEU D 797    -104.051  18.134 -34.560  1.00 52.03           C  
ANISOU 8565  CB  LEU D 797     6353   7494   5922    312    573    -64       C  
ATOM   8566  CG  LEU D 797    -104.968  17.159 -35.277  1.00 54.24           C  
ANISOU 8566  CG  LEU D 797     6650   7824   6134    342    551   -191       C  
ATOM   8567  CD1 LEU D 797    -104.953  15.818 -34.574  1.00 57.06           C  
ANISOU 8567  CD1 LEU D 797     7087   8066   6528    329    526   -314       C  
ATOM   8568  CD2 LEU D 797    -106.385  17.699 -35.387  1.00 54.67           C  
ANISOU 8568  CD2 LEU D 797     6700   7877   6194    300    542   -191       C  
ATOM   8569  N   LYS D 798    -101.666  20.470 -34.700  1.00 53.14           N  
ANISOU 8569  N   LYS D 798     6345   7721   6125    325    633    250       N  
ATOM   8570  CA  LYS D 798    -100.736  21.315 -33.918  1.00 51.93           C  
ANISOU 8570  CA  LYS D 798     6168   7496   6067    286    641    347       C  
ATOM   8571  C   LYS D 798    -100.772  20.882 -32.437  1.00 49.28           C  
ANISOU 8571  C   LYS D 798     5917   6996   5810    232    616    270       C  
ATOM   8572  O   LYS D 798    -100.828  21.691 -31.520  1.00 50.92           O  
ANISOU 8572  O   LYS D 798     6129   7105   6114    175    606    312       O  
ATOM   8573  CB  LYS D 798    -101.051  22.830 -34.077  1.00 50.31           C  
ANISOU 8573  CB  LYS D 798     5897   7289   5927    250    651    482       C  
ATOM   8574  N   THR D 799    -100.738  19.580 -32.232  1.00 47.21           N  
ANISOU 8574  N   THR D 799     5718   6712   5507    255    605    157       N  
ATOM   8575  CA  THR D 799    -100.872  18.984 -30.930  1.00 46.98           C  
ANISOU 8575  CA  THR D 799     5768   6545   5535    214    584     85       C  
ATOM   8576  C   THR D 799     -99.968  17.756 -30.852  1.00 48.17           C  
ANISOU 8576  C   THR D 799     5952   6699   5650    263    583     17       C  
ATOM   8577  O   THR D 799    -100.056  16.864 -31.691  1.00 50.75           O  
ANISOU 8577  O   THR D 799     6285   7094   5904    317    581    -51       O  
ATOM   8578  CB  THR D 799    -102.342  18.534 -30.675  1.00 48.00           C  
ANISOU 8578  CB  THR D 799     5956   6615   5667    178    563      3       C  
ATOM   8579  OG1 THR D 799    -103.216  19.665 -30.758  1.00 48.95           O  
ANISOU 8579  OG1 THR D 799     6046   6736   5816    139    563     61       O  
ATOM   8580  CG2 THR D 799    -102.504  17.904 -29.301  1.00 48.11           C  
ANISOU 8580  CG2 THR D 799     6045   6496   5737    137    546    -56       C  
ATOM   8581  N   ASP D 800     -99.100  17.713 -29.847  1.00 48.54           N  
ANISOU 8581  N   ASP D 800     6018   6676   5750    251    581     31       N  
ATOM   8582  CA  ASP D 800     -98.298  16.536 -29.610  1.00 48.25           C  
ANISOU 8582  CA  ASP D 800     6019   6624   5688    296    578    -33       C  
ATOM   8583  C   ASP D 800     -99.176  15.482 -28.937  1.00 49.28           C  
ANISOU 8583  C   ASP D 800     6237   6650   5839    273    557   -130       C  
ATOM   8584  O   ASP D 800     -99.780  15.750 -27.922  1.00 47.31           O  
ANISOU 8584  O   ASP D 800     6020   6307   5647    215    547   -126       O  
ATOM   8585  CB  ASP D 800     -97.092  16.875 -28.739  1.00 49.48           C  
ANISOU 8585  CB  ASP D 800     6161   6748   5892    291    583     18       C  
ATOM   8586  CG  ASP D 800     -96.173  15.680 -28.503  1.00 52.71           C  
ANISOU 8586  CG  ASP D 800     6605   7148   6274    347    581    -40       C  
ATOM   8587  OD1 ASP D 800     -96.398  14.935 -27.510  1.00 56.62           O  
ANISOU 8587  OD1 ASP D 800     7171   7541   6803    331    566    -95       O  
ATOM   8588  OD2 ASP D 800     -95.214  15.504 -29.277  1.00 48.42           O  
ANISOU 8588  OD2 ASP D 800     6017   6705   5677    409    595    -25       O  
ATOM   8589  N   ILE D 801     -99.251  14.292 -29.526  1.00 51.74           N  
ANISOU 8589  N   ILE D 801     6577   6980   6104    322    548   -218       N  
ATOM   8590  CA  ILE D 801    -100.036  13.197 -28.981  1.00 50.00           C  
ANISOU 8590  CA  ILE D 801     6431   6654   5913    301    527   -306       C  
ATOM   8591  C   ILE D 801     -99.149  11.971 -28.745  1.00 49.69           C  
ANISOU 8591  C   ILE D 801     6429   6576   5874    356    519   -363       C  
ATOM   8592  O   ILE D 801     -98.562  11.453 -29.673  1.00 49.58           O  
ANISOU 8592  O   ILE D 801     6393   6641   5804    427    518   -405       O  
ATOM   8593  CB  ILE D 801    -101.185  12.804 -29.931  1.00 50.07           C  
ANISOU 8593  CB  ILE D 801     6440   6697   5887    304    513   -379       C  
ATOM   8594  CG1 ILE D 801    -102.000  14.039 -30.322  1.00 49.52           C  
ANISOU 8594  CG1 ILE D 801     6324   6684   5806    264    521   -318       C  
ATOM   8595  CG2 ILE D 801    -102.079  11.752 -29.274  1.00 49.76           C  
ANISOU 8595  CG2 ILE D 801     6472   6534   5902    266    490   -459       C  
ATOM   8596  CD1 ILE D 801    -103.148  13.764 -31.282  1.00 50.96           C  
ANISOU 8596  CD1 ILE D 801     6499   6919   5946    269    508   -387       C  
ATOM   8597  N   LYS D 802     -99.095  11.504 -27.502  1.00 50.57           N  
ANISOU 8597  N   LYS D 802     6595   6572   6046    327    514   -363       N  
ATOM   8598  CA  LYS D 802     -98.346  10.310 -27.120  1.00 51.48           C  
ANISOU 8598  CA  LYS D 802     6754   6632   6175    375    506   -408       C  
ATOM   8599  C   LYS D 802     -99.269   9.307 -26.454  1.00 52.14           C  
ANISOU 8599  C   LYS D 802     6904   6587   6319    339    487   -460       C  
ATOM   8600  O   LYS D 802    -100.172   9.677 -25.704  1.00 50.34           O  
ANISOU 8600  O   LYS D 802     6694   6302   6132    270    488   -430       O  
ATOM   8601  CB  LYS D 802     -97.240  10.660 -26.123  1.00 51.83           C  
ANISOU 8601  CB  LYS D 802     6793   6662   6239    381    518   -341       C  
ATOM   8602  CG  LYS D 802     -96.040  11.366 -26.732  1.00 52.61           C  
ANISOU 8602  CG  LYS D 802     6824   6877   6288    428    535   -292       C  
ATOM   8603  CD  LYS D 802     -95.025  11.680 -25.641  1.00 54.90           C  
ANISOU 8603  CD  LYS D 802     7109   7144   6607    427    542   -236       C  
ATOM   8604  CE  LYS D 802     -93.703  12.237 -26.188  1.00 56.63           C  
ANISOU 8604  CE  LYS D 802     7257   7474   6786    475    558   -188       C  
ATOM   8605  NZ  LYS D 802     -93.790  13.662 -26.633  1.00 55.51           N  
ANISOU 8605  NZ  LYS D 802     7043   7403   6647    435    571   -111       N  
ATOM   8606  N   VAL D 803     -99.013   8.027 -26.693  1.00 51.42           N  
ANISOU 8606  N   VAL D 803     6848   6449   6241    388    471   -535       N  
ATOM   8607  CA  VAL D 803     -99.760   6.968 -26.052  1.00 49.87           C  
ANISOU 8607  CA  VAL D 803     6711   6118   6119    357    454   -575       C  
ATOM   8608  C   VAL D 803     -99.243   6.805 -24.640  1.00 48.76           C  
ANISOU 8608  C   VAL D 803     6603   5900   6022    345    465   -506       C  
ATOM   8609  O   VAL D 803     -98.044   6.768 -24.429  1.00 51.48           O  
ANISOU 8609  O   VAL D 803     6941   6274   6346    399    473   -482       O  
ATOM   8610  CB  VAL D 803     -99.586   5.639 -26.802  1.00 53.45           C  
ANISOU 8610  CB  VAL D 803     7186   6537   6586    419    426   -683       C  
ATOM   8611  CG1 VAL D 803    -100.315   4.513 -26.076  1.00 56.75           C  
ANISOU 8611  CG1 VAL D 803     7662   6796   7104    381    408   -711       C  
ATOM   8612  CG2 VAL D 803    -100.106   5.784 -28.214  1.00 54.44           C  
ANISOU 8612  CG2 VAL D 803     7270   6757   6656    440    412   -762       C  
ATOM   8613  N   VAL D 804    -100.148   6.712 -23.676  1.00 47.58           N  
ANISOU 8613  N   VAL D 804     6484   5666   5929    279    466   -473       N  
ATOM   8614  CA  VAL D 804     -99.772   6.391 -22.309  1.00 49.55           C  
ANISOU 8614  CA  VAL D 804     6764   5846   6218    274    475   -409       C  
ATOM   8615  C   VAL D 804     -99.768   4.858 -22.144  1.00 54.82           C  
ANISOU 8615  C   VAL D 804     7481   6397   6952    301    460   -448       C  
ATOM   8616  O   VAL D 804    -100.764   4.197 -22.443  1.00 51.47           O  
ANISOU 8616  O   VAL D 804     7076   5901   6580    266    444   -495       O  
ATOM   8617  CB  VAL D 804    -100.725   7.045 -21.297  1.00 47.22           C  
ANISOU 8617  CB  VAL D 804     6468   5531   5944    198    485   -347       C  
ATOM   8618  CG1 VAL D 804    -100.421   6.561 -19.886  1.00 45.16           C  
ANISOU 8618  CG1 VAL D 804     6234   5209   5717    202    495   -283       C  
ATOM   8619  CG2 VAL D 804    -100.624   8.563 -21.375  1.00 46.11           C  
ANISOU 8619  CG2 VAL D 804     6277   5489   5753    179    495   -311       C  
ATOM   8620  N   ASP D 805     -98.635   4.315 -21.690  1.00 56.65           N  
ANISOU 8620  N   ASP D 805     7728   6608   7186    364    464   -428       N  
ATOM   8621  CA  ASP D 805     -98.461   2.875 -21.562  1.00 64.85           C  
ANISOU 8621  CA  ASP D 805     8811   7533   8295    402    448   -460       C  
ATOM   8622  C   ASP D 805     -99.530   2.317 -20.621  1.00 67.46           C  
ANISOU 8622  C   ASP D 805     9174   7748   8710    335    449   -412       C  
ATOM   8623  O   ASP D 805     -99.711   2.830 -19.516  1.00 67.41           O  
ANISOU 8623  O   ASP D 805     9163   7754   8697    299    470   -323       O  
ATOM   8624  CB  ASP D 805     -97.048   2.537 -21.049  1.00 66.98           C  
ANISOU 8624  CB  ASP D 805     9089   7812   8548    481    456   -427       C  
ATOM   8625  N   ARG D 806    -100.242   1.283 -21.080  1.00 68.00           N  
ANISOU 8625  N   ARG D 806     9267   7711   8859    319    425   -475       N  
ATOM   8626  CA  ARG D 806    -101.329   0.645 -20.316  1.00 68.05           C  
ANISOU 8626  CA  ARG D 806     9296   7599   8960    250    425   -429       C  
ATOM   8627  C   ARG D 806    -100.916   0.172 -18.915  1.00 61.83           C  
ANISOU 8627  C   ARG D 806     8531   6750   8211    262    446   -315       C  
ATOM   8628  O   ARG D 806    -101.756   0.129 -18.024  1.00 60.84           O  
ANISOU 8628  O   ARG D 806     8406   6584   8125    200    460   -236       O  
ATOM   8629  CB  ARG D 806    -101.909  -0.540 -21.113  1.00 68.99           C  
ANISOU 8629  CB  ARG D 806     9435   7601   9178    245    388   -527       C  
ATOM   8630  N   ASP D 807     -99.632  -0.153 -18.744  1.00 60.66           N  
ANISOU 8630  N   ASP D 807     8394   6611   8043    346    448   -305       N  
ATOM   8631  CA  ASP D 807     -99.074  -0.659 -17.494  1.00 62.69           C  
ANISOU 8631  CA  ASP D 807     8670   6823   8328    377    466   -201       C  
ATOM   8632  C   ASP D 807     -98.504   0.428 -16.587  1.00 67.25           C  
ANISOU 8632  C   ASP D 807     9218   7524   8809    387    495   -121       C  
ATOM   8633  O   ASP D 807     -98.052   0.117 -15.490  1.00 72.93           O  
ANISOU 8633  O   ASP D 807     9944   8231   9534    417    511    -32       O  
ATOM   8634  CB  ASP D 807     -97.940  -1.694 -17.771  1.00 64.76           C  
ANISOU 8634  CB  ASP D 807     8959   7023   8625    473    450   -238       C  
ATOM   8635  N   SER D 808     -98.508   1.689 -17.018  1.00 67.08           N  
ANISOU 8635  N   SER D 808     9161   7621   8706    366    499   -151       N  
ATOM   8636  CA  SER D 808     -97.943   2.772 -16.210  1.00 62.28           C  
ANISOU 8636  CA  SER D 808     8519   7125   8019    376    518    -92       C  
ATOM   8637  C   SER D 808     -98.839   3.080 -15.031  1.00 60.98           C  
ANISOU 8637  C   SER D 808     8345   6963   7862    319    534     -9       C  
ATOM   8638  O   SER D 808    -100.016   2.689 -15.004  1.00 59.42           O  
ANISOU 8638  O   SER D 808     8160   6698   7720    258    533      1       O  
ATOM   8639  CB  SER D 808     -97.770   4.040 -17.047  1.00 61.27           C  
ANISOU 8639  CB  SER D 808     8351   7108   7822    364    514   -144       C  
ATOM   8640  OG  SER D 808     -99.016   4.541 -17.502  1.00 56.25           O  
ANISOU 8640  OG  SER D 808     7706   6473   7195    289    510   -169       O  
ATOM   8641  N   GLU D 809     -98.274   3.775 -14.051  1.00 61.29           N  
ANISOU 8641  N   GLU D 809     8355   7087   7844    343    547     47       N  
ATOM   8642  CA  GLU D 809     -99.046   4.234 -12.897  1.00 64.45           C  
ANISOU 8642  CA  GLU D 809     8734   7524   8230    302    560    118       C  
ATOM   8643  C   GLU D 809    -100.009   5.334 -13.334  1.00 61.50           C  
ANISOU 8643  C   GLU D 809     8333   7199   7834    232    554     78       C  
ATOM   8644  O   GLU D 809    -101.130   5.435 -12.841  1.00 61.38           O  
ANISOU 8644  O   GLU D 809     8311   7179   7833    177    560    113       O  
ATOM   8645  CB  GLU D 809     -98.110   4.751 -11.794  1.00 62.47           C  
ANISOU 8645  CB  GLU D 809     8452   7368   7917    356    568    166       C  
ATOM   8646  N   GLU D 810     -99.555   6.137 -14.281  1.00 58.47           N  
ANISOU 8646  N   GLU D 810     7932   6867   7418    237    543     12       N  
ATOM   8647  CA  GLU D 810    -100.369   7.177 -14.899  1.00 58.71           C  
ANISOU 8647  CA  GLU D 810     7937   6940   7432    179    535    -27       C  
ATOM   8648  C   GLU D 810    -101.689   6.583 -15.432  1.00 54.24           C  
ANISOU 8648  C   GLU D 810     7394   6300   6915    120    532    -48       C  
ATOM   8649  O   GLU D 810    -102.783   7.023 -15.069  1.00 46.12           O  
ANISOU 8649  O   GLU D 810     6351   5284   5888     64    534    -30       O  
ATOM   8650  CB  GLU D 810     -99.550   7.794 -16.027  1.00 62.37           C  
ANISOU 8650  CB  GLU D 810     8380   7453   7865    206    527    -84       C  
ATOM   8651  CG  GLU D 810    -100.014   9.125 -16.565  1.00 64.01           C  
ANISOU 8651  CG  GLU D 810     8547   7726   8048    164    520   -107       C  
ATOM   8652  CD  GLU D 810     -98.972   9.756 -17.484  1.00 64.57           C  
ANISOU 8652  CD  GLU D 810     8587   7859   8089    199    517   -135       C  
ATOM   8653  OE1 GLU D 810     -98.107   9.023 -18.036  1.00 73.19           O  
ANISOU 8653  OE1 GLU D 810     9694   8941   9175    252    518   -156       O  
ATOM   8654  OE2 GLU D 810     -99.012  10.986 -17.661  1.00 60.40           O  
ANISOU 8654  OE2 GLU D 810     8014   7389   7545    176    513   -132       O  
ATOM   8655  N   ALA D 811    -101.584   5.532 -16.230  1.00 51.35           N  
ANISOU 8655  N   ALA D 811     7062   5856   6594    136    524    -89       N  
ATOM   8656  CA  ALA D 811    -102.773   4.872 -16.772  1.00 53.65           C  
ANISOU 8656  CA  ALA D 811     7371   6069   6943     82    514   -121       C  
ATOM   8657  C   ALA D 811    -103.676   4.301 -15.666  1.00 52.50           C  
ANISOU 8657  C   ALA D 811     7234   5866   6848     37    527    -43       C  
ATOM   8658  O   ALA D 811    -104.900   4.343 -15.771  1.00 54.48           O  
ANISOU 8658  O   ALA D 811     7476   6097   7125    -29    525    -47       O  
ATOM   8659  CB  ALA D 811    -102.372   3.764 -17.747  1.00 54.93           C  
ANISOU 8659  CB  ALA D 811     7564   6154   7154    119    497   -190       C  
ATOM   8660  N   GLU D 812    -103.063   3.770 -14.618  1.00 52.33           N  
ANISOU 8660  N   GLU D 812     7222   5824   6836     76    541     34       N  
ATOM   8661  CA  GLU D 812    -103.796   3.155 -13.517  1.00 58.59           C  
ANISOU 8661  CA  GLU D 812     8016   6572   7674     45    558    129       C  
ATOM   8662  C   GLU D 812    -104.640   4.178 -12.766  1.00 53.26           C  
ANISOU 8662  C   GLU D 812     7300   5992   6944      0    570    169       C  
ATOM   8663  O   GLU D 812    -105.815   3.928 -12.458  1.00 49.51           O  
ANISOU 8663  O   GLU D 812     6816   5490   6505    -60    577    207       O  
ATOM   8664  CB  GLU D 812    -102.803   2.422 -12.606  1.00 65.59           C  
ANISOU 8664  CB  GLU D 812     8916   7435   8569    113    571    206       C  
ATOM   8665  CG  GLU D 812    -103.283   1.975 -11.237  1.00 74.95           C  
ANISOU 8665  CG  GLU D 812    10089   8618   9772    103    596    332       C  
ATOM   8666  CD  GLU D 812    -104.308   0.852 -11.266  1.00 80.92           C  
ANISOU 8666  CD  GLU D 812    10861   9246  10639     45    598    376       C  
ATOM   8667  OE1 GLU D 812    -104.666   0.354 -12.365  1.00 90.79           O  
ANISOU 8667  OE1 GLU D 812    12135  10400  11962     13    576    294       O  
ATOM   8668  OE2 GLU D 812    -104.766   0.477 -10.161  1.00 85.61           O  
ANISOU 8668  OE2 GLU D 812    11436   9842  11249     33    623    494       O  
ATOM   8669  N   ILE D 813    -104.036   5.334 -12.517  1.00 49.28           N  
ANISOU 8669  N   ILE D 813     6768   5598   6359     31    569    155       N  
ATOM   8670  CA  ILE D 813    -104.731   6.463 -11.907  1.00 46.68           C  
ANISOU 8670  CA  ILE D 813     6396   5365   5976      0    571    169       C  
ATOM   8671  C   ILE D 813    -105.931   6.839 -12.776  1.00 43.56           C  
ANISOU 8671  C   ILE D 813     5996   4957   5598    -70    561    116       C  
ATOM   8672  O   ILE D 813    -107.048   7.000 -12.278  1.00 42.37           O  
ANISOU 8672  O   ILE D 813     5824   4827   5448   -118    568    148       O  
ATOM   8673  CB  ILE D 813    -103.811   7.699 -11.790  1.00 48.37           C  
ANISOU 8673  CB  ILE D 813     6579   5678   6121     42    561    135       C  
ATOM   8674  CG1 ILE D 813    -102.582   7.464 -10.924  1.00 50.42           C  
ANISOU 8674  CG1 ILE D 813     6835   5971   6353    116    568    177       C  
ATOM   8675  CG2 ILE D 813    -104.550   8.898 -11.244  1.00 47.61           C  
ANISOU 8675  CG2 ILE D 813     6438   5672   5982     14    556    132       C  
ATOM   8676  CD1 ILE D 813    -102.912   7.172  -9.493  1.00 55.70           C  
ANISOU 8676  CD1 ILE D 813     7483   6680   7001    130    585    265       C  
ATOM   8677  N   ILE D 814    -105.707   6.942 -14.083  1.00 40.80           N  
ANISOU 8677  N   ILE D 814     5661   4583   5259    -72    546     35       N  
ATOM   8678  CA  ILE D 814    -106.759   7.359 -14.990  1.00 39.76           C  
ANISOU 8678  CA  ILE D 814     5519   4454   5133   -128    534    -21       C  
ATOM   8679  C   ILE D 814    -107.898   6.340 -15.041  1.00 41.29           C  
ANISOU 8679  C   ILE D 814     5727   4564   5396   -185    536     -8       C  
ATOM   8680  O   ILE D 814    -109.064   6.725 -15.038  1.00 41.53           O  
ANISOU 8680  O   ILE D 814     5736   4619   5425   -242    535    -10       O  
ATOM   8681  CB  ILE D 814    -106.191   7.689 -16.381  1.00 40.97           C  
ANISOU 8681  CB  ILE D 814     5676   4619   5270   -106    519   -103       C  
ATOM   8682  CG1 ILE D 814    -105.378   8.999 -16.282  1.00 43.12           C  
ANISOU 8682  CG1 ILE D 814     5917   4986   5482    -72    518   -103       C  
ATOM   8683  CG2 ILE D 814    -107.305   7.840 -17.405  1.00 41.89           C  
ANISOU 8683  CG2 ILE D 814     5785   4732   5397   -157    506   -162       C  
ATOM   8684  CD1 ILE D 814    -104.577   9.358 -17.513  1.00 42.73           C  
ANISOU 8684  CD1 ILE D 814     5861   4964   5410    -39    509   -158       C  
ATOM   8685  N   ARG D 815    -107.566   5.058 -15.054  1.00 42.76           N  
ANISOU 8685  N   ARG D 815     5946   4650   5650   -171    536      6       N  
ATOM   8686  CA  ARG D 815    -108.593   4.016 -15.045  1.00 46.57           C  
ANISOU 8686  CA  ARG D 815     6437   5035   6221   -228    535     24       C  
ATOM   8687  C   ARG D 815    -109.368   4.013 -13.735  1.00 42.60           C  
ANISOU 8687  C   ARG D 815     5909   4558   5720   -265    559    133       C  
ATOM   8688  O   ARG D 815    -110.576   3.762 -13.745  1.00 43.18           O  
ANISOU 8688  O   ARG D 815     5966   4604   5836   -333    560    145       O  
ATOM   8689  CB  ARG D 815    -108.005   2.619 -15.327  1.00 48.53           C  
ANISOU 8689  CB  ARG D 815     6724   5155   6559   -200    525     15       C  
ATOM   8690  CG  ARG D 815    -107.646   2.369 -16.787  1.00 49.39           C  
ANISOU 8690  CG  ARG D 815     6852   5229   6684   -177    496   -110       C  
ATOM   8691  CD  ARG D 815    -107.283   0.908 -17.022  1.00 53.77           C  
ANISOU 8691  CD  ARG D 815     7442   5643   7347   -154    479   -128       C  
ATOM   8692  NE  ARG D 815    -106.220   0.510 -16.105  1.00 54.02           N  
ANISOU 8692  NE  ARG D 815     7491   5655   7378    -93    497    -45       N  
ATOM   8693  CZ  ARG D 815    -104.926   0.422 -16.407  1.00 56.55           C  
ANISOU 8693  CZ  ARG D 815     7830   5989   7667    -11    491    -79       C  
ATOM   8694  NH1 ARG D 815    -104.065   0.070 -15.451  1.00 55.93           N  
ANISOU 8694  NH1 ARG D 815     7764   5901   7586     41    509      8       N  
ATOM   8695  NH2 ARG D 815    -104.475   0.673 -17.638  1.00 55.53           N  
ANISOU 8695  NH2 ARG D 815     7703   5894   7502     23    469   -193       N  
ATOM   8696  N   LYS D 816    -108.699   4.318 -12.625  1.00 40.88           N  
ANISOU 8696  N   LYS D 816     5680   4404   5449   -217    578    208       N  
ATOM   8697  CA  LYS D 816    -109.410   4.414 -11.336  1.00 41.56           C  
ANISOU 8697  CA  LYS D 816     5730   4546   5515   -239    601    312       C  
ATOM   8698  C   LYS D 816    -110.394   5.572 -11.384  1.00 42.61           C  
ANISOU 8698  C   LYS D 816     5825   4777   5589   -281    597    278       C  
ATOM   8699  O   LYS D 816    -111.523   5.459 -10.919  1.00 45.98           O  
ANISOU 8699  O   LYS D 816     6223   5219   6028   -333    608    328       O  
ATOM   8700  CB  LYS D 816    -108.471   4.501 -10.130  1.00 43.33           C  
ANISOU 8700  CB  LYS D 816     5943   4836   5684   -168    619    392       C  
ATOM   8701  N   TYR D 817    -109.977   6.696 -11.960  1.00 41.29           N  
ANISOU 8701  N   TYR D 817     5653   4675   5362   -258    580    198       N  
ATOM   8702  CA  TYR D 817    -110.831   7.877 -12.007  1.00 38.94           C  
ANISOU 8702  CA  TYR D 817     5318   4466   5012   -289    572    165       C  
ATOM   8703  C   TYR D 817    -112.080   7.523 -12.778  1.00 38.08           C  
ANISOU 8703  C   TYR D 817     5208   4309   4951   -362    566    133       C  
ATOM   8704  O   TYR D 817    -113.180   7.855 -12.364  1.00 34.88           O  
ANISOU 8704  O   TYR D 817     4769   3954   4530   -404    572    157       O  
ATOM   8705  CB  TYR D 817    -110.071   9.024 -12.692  1.00 39.16           C  
ANISOU 8705  CB  TYR D 817     5343   4544   4992   -253    553     87       C  
ATOM   8706  CG  TYR D 817    -110.596  10.422 -12.527  1.00 36.36           C  
ANISOU 8706  CG  TYR D 817     4946   4285   4582   -261    542     59       C  
ATOM   8707  CD1 TYR D 817    -111.722  10.722 -11.756  1.00 34.20           C  
ANISOU 8707  CD1 TYR D 817     4637   4069   4286   -292    548     92       C  
ATOM   8708  CD2 TYR D 817    -109.933  11.486 -13.174  1.00 34.23           C  
ANISOU 8708  CD2 TYR D 817     4669   4050   4287   -234    524      1       C  
ATOM   8709  CE1 TYR D 817    -112.158  12.044 -11.627  1.00 33.63           C  
ANISOU 8709  CE1 TYR D 817     4527   4083   4168   -290    532     56       C  
ATOM   8710  CE2 TYR D 817    -110.359  12.790 -13.050  1.00 31.37           C  
ANISOU 8710  CE2 TYR D 817     4267   3761   3890   -238    510    -26       C  
ATOM   8711  CZ  TYR D 817    -111.444  13.083 -12.288  1.00 31.05           C  
ANISOU 8711  CZ  TYR D 817     4197   3772   3829   -262    511     -5       C  
ATOM   8712  OH  TYR D 817    -111.808  14.398 -12.210  1.00 27.13           O  
ANISOU 8712  OH  TYR D 817     3661   3341   3304   -258    492    -42       O  
ATOM   8713  N   VAL D 818    -111.905   6.839 -13.905  1.00 40.48           N  
ANISOU 8713  N   VAL D 818     5545   4522   5312   -373    552     73       N  
ATOM   8714  CA  VAL D 818    -113.040   6.429 -14.723  1.00 41.64           C  
ANISOU 8714  CA  VAL D 818     5688   4621   5510   -439    541     28       C  
ATOM   8715  C   VAL D 818    -113.964   5.487 -13.937  1.00 44.23           C  
ANISOU 8715  C   VAL D 818     6002   4897   5905   -494    557    111       C  
ATOM   8716  O   VAL D 818    -115.175   5.673 -13.926  1.00 45.52           O  
ANISOU 8716  O   VAL D 818     6134   5089   6073   -553    558    114       O  
ATOM   8717  CB  VAL D 818    -112.604   5.724 -16.027  1.00 42.27           C  
ANISOU 8717  CB  VAL D 818     5802   4615   5642   -429    519    -61       C  
ATOM   8718  CG1 VAL D 818    -113.816   5.107 -16.741  1.00 43.67           C  
ANISOU 8718  CG1 VAL D 818     5969   4734   5887   -499    503   -109       C  
ATOM   8719  CG2 VAL D 818    -111.897   6.697 -16.969  1.00 41.35           C  
ANISOU 8719  CG2 VAL D 818     5687   4567   5458   -383    505   -138       C  
ATOM   8720  N   LYS D 819    -113.389   4.493 -13.276  1.00 44.91           N  
ANISOU 8720  N   LYS D 819     6108   4912   6045   -474    571    186       N  
ATOM   8721  CA  LYS D 819    -114.172   3.484 -12.568  1.00 47.86           C  
ANISOU 8721  CA  LYS D 819     6464   5221   6499   -526    589    282       C  
ATOM   8722  C   LYS D 819    -114.919   4.037 -11.365  1.00 49.72           C  
ANISOU 8722  C   LYS D 819     6649   5570   6674   -542    615    379       C  
ATOM   8723  O   LYS D 819    -116.088   3.750 -11.167  1.00 49.08           O  
ANISOU 8723  O   LYS D 819     6533   5485   6630   -609    624    420       O  
ATOM   8724  CB  LYS D 819    -113.246   2.367 -12.105  1.00 53.45           C  
ANISOU 8724  CB  LYS D 819     7203   5831   7275   -486    598    351       C  
ATOM   8725  CG  LYS D 819    -113.929   1.107 -11.602  1.00 58.34           C  
ANISOU 8725  CG  LYS D 819     7810   6343   8015   -541    612    451       C  
ATOM   8726  CD  LYS D 819    -112.994   0.370 -10.656  1.00 59.68           C  
ANISOU 8726  CD  LYS D 819     7995   6474   8209   -484    635    566       C  
ATOM   8727  CE  LYS D 819    -113.392  -1.085 -10.439  1.00 62.83           C  
ANISOU 8727  CE  LYS D 819     8393   6717   8763   -530    641    654       C  
ATOM   8728  NZ  LYS D 819    -114.246  -1.244  -9.243  1.00 62.44           N  
ANISOU 8728  NZ  LYS D 819     8287   6720   8716   -570    679    813       N  
ATOM   8729  N   ASN D 820    -114.237   4.822 -10.544  1.00 48.77           N  
ANISOU 8729  N   ASN D 820     6517   5557   6458   -478    627    411       N  
ATOM   8730  CA  ASN D 820    -114.843   5.314  -9.321  1.00 48.88           C  
ANISOU 8730  CA  ASN D 820     6476   5692   6403   -477    649    498       C  
ATOM   8731  C   ASN D 820    -115.861   6.418  -9.475  1.00 48.21           C  
ANISOU 8731  C   ASN D 820     6351   5710   6255   -508    640    445       C  
ATOM   8732  O   ASN D 820    -116.684   6.593  -8.573  1.00 46.85           O  
ANISOU 8732  O   ASN D 820     6128   5627   6046   -523    658    517       O  
ATOM   8733  CB  ASN D 820    -113.771   5.825  -8.384  1.00 52.41           C  
ANISOU 8733  CB  ASN D 820     6916   6230   6766   -390    658    533       C  
ATOM   8734  CG  ASN D 820    -112.976   4.719  -7.773  1.00 50.63           C  
ANISOU 8734  CG  ASN D 820     6711   5941   6587   -353    678    629       C  
ATOM   8735  OD1 ASN D 820    -113.322   3.548  -7.893  1.00 58.84           O  
ANISOU 8735  OD1 ASN D 820     7762   6866   7727   -396    688    689       O  
ATOM   8736  ND2 ASN D 820    -111.892   5.076  -7.136  1.00 51.99           N  
ANISOU 8736  ND2 ASN D 820     6882   6180   6691   -273    681    643       N  
ATOM   8737  N   THR D 821    -115.797   7.198 -10.560  1.00 45.48           N  
ANISOU 8737  N   THR D 821     6024   5364   5890   -510    612    327       N  
ATOM   8738  CA  THR D 821    -116.652   8.378 -10.649  1.00 41.98           C  
ANISOU 8738  CA  THR D 821     5543   5025   5382   -525    601    279       C  
ATOM   8739  C   THR D 821    -117.749   8.215 -11.682  1.00 45.14           C  
ANISOU 8739  C   THR D 821     5940   5383   5829   -598    589    222       C  
ATOM   8740  O   THR D 821    -118.358   9.194 -12.135  1.00 42.85           O  
ANISOU 8740  O   THR D 821     5629   5159   5492   -608    573    159       O  
ATOM   8741  CB  THR D 821    -115.832   9.659 -10.915  1.00 41.80           C  
ANISOU 8741  CB  THR D 821     5526   5064   5290   -466    580    202       C  
ATOM   8742  OG1 THR D 821    -115.315   9.657 -12.257  1.00 36.87           O  
ANISOU 8742  OG1 THR D 821     4942   4368   4699   -467    561    119       O  
ATOM   8743  CG2 THR D 821    -114.700   9.774  -9.905  1.00 42.07           C  
ANISOU 8743  CG2 THR D 821     5559   5141   5284   -394    589    248       C  
ATOM   8744  N   HIS D 822    -118.035   6.974 -12.053  1.00 49.02           N  
ANISOU 8744  N   HIS D 822     6447   5761   6416   -648    592    242       N  
ATOM   8745  CA  HIS D 822    -119.214   6.712 -12.852  1.00 51.53           C  
ANISOU 8745  CA  HIS D 822     6749   6047   6783   -722    580    195       C  
ATOM   8746  C   HIS D 822    -120.407   6.870 -11.940  1.00 50.98           C  
ANISOU 8746  C   HIS D 822     6620   6062   6690   -764    600    273       C  
ATOM   8747  O   HIS D 822    -120.484   6.191 -10.936  1.00 57.43           O  
ANISOU 8747  O   HIS D 822     7416   6873   7532   -773    626    386       O  
ATOM   8748  CB  HIS D 822    -119.191   5.314 -13.442  1.00 52.40           C  
ANISOU 8748  CB  HIS D 822     6886   6007   7017   -764    572    188       C  
ATOM   8749  CG  HIS D 822    -120.221   5.124 -14.500  1.00 53.90           C  
ANISOU 8749  CG  HIS D 822     7061   6163   7256   -830    548    103       C  
ATOM   8750  ND1 HIS D 822    -119.904   4.769 -15.790  1.00 54.24           N  
ANISOU 8750  ND1 HIS D 822     7136   6130   7343   -827    517    -10       N  
ATOM   8751  CD2 HIS D 822    -121.559   5.313 -14.479  1.00 54.26           C  
ANISOU 8751  CD2 HIS D 822     7057   6258   7301   -894    549    107       C  
ATOM   8752  CE1 HIS D 822    -121.008   4.706 -16.509  1.00 51.96           C  
ANISOU 8752  CE1 HIS D 822     6818   5842   7084   -887    499    -74       C  
ATOM   8753  NE2 HIS D 822    -122.025   5.040 -15.738  1.00 53.99           N  
ANISOU 8753  NE2 HIS D 822     7026   6172   7315   -931    518     -3       N  
ATOM   8754  N   ALA D 823    -121.334   7.768 -12.270  1.00 48.94           N  
ANISOU 8754  N   ALA D 823     6328   5889   6378   -786    588    219       N  
ATOM   8755  CA  ALA D 823    -122.444   8.050 -11.364  1.00 50.79           C  
ANISOU 8755  CA  ALA D 823     6499   6228   6572   -814    607    288       C  
ATOM   8756  C   ALA D 823    -123.456   6.901 -11.349  1.00 52.39           C  
ANISOU 8756  C   ALA D 823     6671   6364   6871   -902    619    347       C  
ATOM   8757  O   ALA D 823    -123.705   6.277 -12.366  1.00 50.66           O  
ANISOU 8757  O   ALA D 823     6470   6042   6735   -952    600    284       O  
ATOM   8758  CB  ALA D 823    -123.140   9.339 -11.753  1.00 47.91           C  
ANISOU 8758  CB  ALA D 823     6107   5970   6128   -806    588    210       C  
ATOM   8759  N   THR D 824    -124.050   6.681 -10.188  1.00 53.79           N  
ANISOU 8759  N   THR D 824     6794   6612   7032   -919    650    465       N  
ATOM   8760  CA  THR D 824    -125.038   5.637  -9.952  1.00 57.62           C  
ANISOU 8760  CA  THR D 824     7235   7049   7609  -1005    668    551       C  
ATOM   8761  C   THR D 824    -126.265   5.787 -10.885  1.00 57.45           C  
ANISOU 8761  C   THR D 824     7185   7029   7616  -1078    646    467       C  
ATOM   8762  O   THR D 824    -126.821   4.787 -11.354  1.00 61.58           O  
ANISOU 8762  O   THR D 824     7697   7444   8258  -1158    640    472       O  
ATOM   8763  CB  THR D 824    -125.396   5.633  -8.419  1.00 58.13           C  
ANISOU 8763  CB  THR D 824     7234   7237   7616   -989    709    704       C  
ATOM   8764  OG1 THR D 824    -125.578   4.303  -7.941  1.00 63.61           O  
ANISOU 8764  OG1 THR D 824     7906   7840   8422  -1043    736    837       O  
ATOM   8765  CG2 THR D 824    -126.629   6.494  -8.119  1.00 58.50           C  
ANISOU 8765  CG2 THR D 824     7210   7442   7575  -1005    713    698       C  
ATOM   8766  N   THR D 825    -126.669   7.023 -11.181  1.00 53.67           N  
ANISOU 8766  N   THR D 825     6692   6668   7034  -1050    630    385       N  
ATOM   8767  CA  THR D 825    -127.852   7.266 -12.015  1.00 53.25           C  
ANISOU 8767  CA  THR D 825     6605   6639   6989  -1110    610    308       C  
ATOM   8768  C   THR D 825    -127.601   7.243 -13.521  1.00 53.84           C  
ANISOU 8768  C   THR D 825     6727   6625   7105  -1117    572    168       C  
ATOM   8769  O   THR D 825    -128.521   7.456 -14.298  1.00 50.19           O  
ANISOU 8769  O   THR D 825     6238   6188   6645  -1158    552     94       O  
ATOM   8770  CB  THR D 825    -128.492   8.638 -11.702  1.00 53.56           C  
ANISOU 8770  CB  THR D 825     6602   6847   6899  -1072    608    280       C  
ATOM   8771  OG1 THR D 825    -127.566   9.696 -12.017  1.00 48.55           O  
ANISOU 8771  OG1 THR D 825     6014   6242   6190   -988    589    202       O  
ATOM   8772  CG2 THR D 825    -128.930   8.715 -10.229  1.00 53.50           C  
ANISOU 8772  CG2 THR D 825     6532   6962   6835  -1060    643    407       C  
ATOM   8773  N   HIS D 826    -126.356   7.074 -13.938  1.00 58.19           N  
ANISOU 8773  N   HIS D 826     7343   7093   7674  -1068    561    130       N  
ATOM   8774  CA  HIS D 826    -126.042   7.006 -15.360  1.00 59.72           C  
ANISOU 8774  CA  HIS D 826     7576   7217   7898  -1064    527      1       C  
ATOM   8775  C   HIS D 826    -125.821   5.542 -15.688  1.00 59.94           C  
ANISOU 8775  C   HIS D 826     7623   7086   8064  -1111    518      3       C  
ATOM   8776  O   HIS D 826    -124.727   5.114 -16.066  1.00 62.22           O  
ANISOU 8776  O   HIS D 826     7966   7287   8388  -1071    508    -29       O  
ATOM   8777  CB  HIS D 826    -124.826   7.864 -15.692  1.00 57.65           C  
ANISOU 8777  CB  HIS D 826     7364   6979   7561   -975    518    -49       C  
ATOM   8778  CG  HIS D 826    -125.049   9.322 -15.448  1.00 58.27           C  
ANISOU 8778  CG  HIS D 826     7421   7195   7524   -931    518    -60       C  
ATOM   8779  ND1 HIS D 826    -124.051  10.170 -15.017  1.00 57.66           N  
ANISOU 8779  ND1 HIS D 826     7367   7162   7380   -855    522    -49       N  
ATOM   8780  CD2 HIS D 826    -126.168  10.080 -15.544  1.00 59.77           C  
ANISOU 8780  CD2 HIS D 826     7563   7484   7662   -950    512    -84       C  
ATOM   8781  CE1 HIS D 826    -124.541  11.390 -14.877  1.00 55.19           C  
ANISOU 8781  CE1 HIS D 826     7023   6959   6988   -830    516    -69       C  
ATOM   8782  NE2 HIS D 826    -125.824  11.365 -15.192  1.00 57.49           N  
ANISOU 8782  NE2 HIS D 826     7273   7289   7283   -884    511    -89       N  
ATOM   8783  N   ASN D 827    -126.900   4.786 -15.558  1.00 60.65           N  
ANISOU 8783  N   ASN D 827     7666   7140   8240  -1197    520     36       N  
ATOM   8784  CA  ASN D 827    -126.836   3.323 -15.586  1.00 64.53           C  
ANISOU 8784  CA  ASN D 827     8161   7470   8887  -1253    515     66       C  
ATOM   8785  C   ASN D 827    -127.080   2.730 -16.971  1.00 62.90           C  
ANISOU 8785  C   ASN D 827     7962   7168   8768  -1288    468    -79       C  
ATOM   8786  O   ASN D 827    -127.014   1.521 -17.141  1.00 66.34           O  
ANISOU 8786  O   ASN D 827     8403   7456   9349  -1332    453    -81       O  
ATOM   8787  CB  ASN D 827    -127.777   2.728 -14.519  1.00 68.07           C  
ANISOU 8787  CB  ASN D 827     8544   7920   9399  -1329    547    209       C  
ATOM   8788  CG  ASN D 827    -129.196   3.295 -14.588  1.00 70.90           C  
ANISOU 8788  CG  ASN D 827     8832   8395   9711  -1384    546    193       C  
ATOM   8789  OD1 ASN D 827    -129.564   4.021 -15.517  1.00 71.35           O  
ANISOU 8789  OD1 ASN D 827     8889   8515   9706  -1374    519     70       O  
ATOM   8790  ND2 ASN D 827    -129.995   2.954 -13.598  1.00 73.24           N  
ANISOU 8790  ND2 ASN D 827     9064   8728  10036  -1440    579    326       N  
ATOM   8791  N   ALA D 828    -127.298   3.582 -17.971  1.00 62.71           N  
ANISOU 8791  N   ALA D 828     7939   7229   8659  -1261    443   -202       N  
ATOM   8792  CA  ALA D 828    -127.471   3.139 -19.358  1.00 64.64           C  
ANISOU 8792  CA  ALA D 828     8185   7414   8959  -1276    395   -355       C  
ATOM   8793  C   ALA D 828    -126.247   2.440 -19.975  1.00 67.13           C  
ANISOU 8793  C   ALA D 828     8560   7612   9333  -1224    371   -423       C  
ATOM   8794  O   ALA D 828    -126.384   1.754 -20.985  1.00 74.11           O  
ANISOU 8794  O   ALA D 828     9441   8422  10296  -1241    329   -545       O  
ATOM   8795  CB  ALA D 828    -127.898   4.318 -20.230  1.00 62.58           C  
ANISOU 8795  CB  ALA D 828     7910   7296   8573  -1242    379   -454       C  
ATOM   8796  N   TYR D 829    -125.060   2.615 -19.391  1.00 66.00           N  
ANISOU 8796  N   TYR D 829     8468   7459   9150  -1157    396   -355       N  
ATOM   8797  CA  TYR D 829    -123.829   2.042 -19.952  1.00 63.26           C  
ANISOU 8797  CA  TYR D 829     8176   7017   8842  -1097    375   -417       C  
ATOM   8798  C   TYR D 829    -122.749   1.861 -18.886  1.00 59.71           C  
ANISOU 8798  C   TYR D 829     7768   6527   8394  -1053    409   -296       C  
ATOM   8799  O   TYR D 829    -122.835   2.442 -17.821  1.00 58.48           O  
ANISOU 8799  O   TYR D 829     7599   6447   8173  -1050    447   -180       O  
ATOM   8800  CB  TYR D 829    -123.315   2.929 -21.112  1.00 65.18           C  
ANISOU 8800  CB  TYR D 829     8439   7356   8971  -1022    354   -539       C  
ATOM   8801  CG  TYR D 829    -123.048   4.382 -20.713  1.00 64.99           C  
ANISOU 8801  CG  TYR D 829     8418   7477   8797   -971    383   -485       C  
ATOM   8802  CD1 TYR D 829    -121.868   4.739 -20.094  1.00 64.39           C  
ANISOU 8802  CD1 TYR D 829     8383   7410   8673   -906    407   -417       C  
ATOM   8803  CD2 TYR D 829    -123.991   5.393 -20.953  1.00 64.39           C  
ANISOU 8803  CD2 TYR D 829     8301   7527   8637   -986    384   -505       C  
ATOM   8804  CE1 TYR D 829    -121.622   6.053 -19.722  1.00 64.29           C  
ANISOU 8804  CE1 TYR D 829     8368   7518   8543   -862    428   -377       C  
ATOM   8805  CE2 TYR D 829    -123.750   6.704 -20.576  1.00 63.31           C  
ANISOU 8805  CE2 TYR D 829     8166   7506   8383   -939    405   -460       C  
ATOM   8806  CZ  TYR D 829    -122.550   7.028 -19.961  1.00 62.09           C  
ANISOU 8806  CZ  TYR D 829     8050   7349   8192   -878    425   -398       C  
ATOM   8807  OH  TYR D 829    -122.255   8.313 -19.569  1.00 55.94           O  
ANISOU 8807  OH  TYR D 829     7269   6672   7313   -831    441   -362       O  
ATOM   8808  N   ASP D 830    -121.747   1.042 -19.178  1.00 59.52           N  
ANISOU 8808  N   ASP D 830     7788   6389   8439  -1013    393   -329       N  
ATOM   8809  CA  ASP D 830    -120.478   1.054 -18.432  1.00 60.33           C  
ANISOU 8809  CA  ASP D 830     7936   6476   8512   -944    419   -244       C  
ATOM   8810  C   ASP D 830    -119.391   1.482 -19.422  1.00 54.52           C  
ANISOU 8810  C   ASP D 830     7240   5774   7702   -856    398   -355       C  
ATOM   8811  O   ASP D 830    -119.584   1.489 -20.642  1.00 52.54           O  
ANISOU 8811  O   ASP D 830     6982   5533   7447   -850    362   -489       O  
ATOM   8812  CB  ASP D 830    -120.135  -0.252 -17.645  1.00 68.27           C  
ANISOU 8812  CB  ASP D 830     8956   7328   9657   -963    429   -146       C  
ATOM   8813  CG  ASP D 830    -120.355  -1.515 -18.440  1.00 74.99           C  
ANISOU 8813  CG  ASP D 830     9808   8017  10669  -1002    385   -237       C  
ATOM   8814  OD1 ASP D 830    -119.419  -1.899 -19.172  1.00 79.51           O  
ANISOU 8814  OD1 ASP D 830    10421   8529  11262   -939    357   -333       O  
ATOM   8815  OD2 ASP D 830    -121.434  -2.146 -18.296  1.00 81.29           O  
ANISOU 8815  OD2 ASP D 830    10561   8745  11579  -1092    378   -212       O  
ATOM   8816  N   LEU D 831    -118.275   1.936 -18.891  1.00 51.70           N  
ANISOU 8816  N   LEU D 831     6914   5455   7273   -787    421   -297       N  
ATOM   8817  CA  LEU D 831    -117.227   2.489 -19.725  1.00 53.09           C  
ANISOU 8817  CA  LEU D 831     7119   5684   7368   -705    408   -380       C  
ATOM   8818  C   LEU D 831    -116.019   1.595 -19.656  1.00 50.89           C  
ANISOU 8818  C   LEU D 831     6884   5303   7148   -650    403   -377       C  
ATOM   8819  O   LEU D 831    -115.656   1.111 -18.586  1.00 48.87           O  
ANISOU 8819  O   LEU D 831     6643   4990   6936   -649    427   -267       O  
ATOM   8820  CB  LEU D 831    -116.802   3.905 -19.276  1.00 52.63           C  
ANISOU 8820  CB  LEU D 831     7058   5766   7174   -661    435   -329       C  
ATOM   8821  CG  LEU D 831    -117.526   5.197 -19.618  1.00 50.15           C  
ANISOU 8821  CG  LEU D 831     6709   5582   6763   -672    436   -356       C  
ATOM   8822  CD1 LEU D 831    -117.917   5.284 -21.082  1.00 47.92           C  
ANISOU 8822  CD1 LEU D 831     6414   5327   6468   -671    404   -484       C  
ATOM   8823  CD2 LEU D 831    -118.698   5.292 -18.700  1.00 52.97           C  
ANISOU 8823  CD2 LEU D 831     7030   5962   7133   -740    454   -278       C  
ATOM   8824  N   GLU D 832    -115.355   1.466 -20.789  1.00 48.84           N  
ANISOU 8824  N   GLU D 832     6643   5041   6875   -594    374   -494       N  
ATOM   8825  CA  GLU D 832    -114.110   0.743 -20.864  1.00 52.42           C  
ANISOU 8825  CA  GLU D 832     7135   5416   7364   -526    366   -508       C  
ATOM   8826  C   GLU D 832    -113.094   1.626 -21.579  1.00 51.29           C  
ANISOU 8826  C   GLU D 832     7001   5387   7099   -443    366   -564       C  
ATOM   8827  O   GLU D 832    -113.351   2.137 -22.684  1.00 50.49           O  
ANISOU 8827  O   GLU D 832     6879   5366   6939   -430    346   -662       O  
ATOM   8828  CB  GLU D 832    -114.307  -0.583 -21.607  1.00 52.46           C  
ANISOU 8828  CB  GLU D 832     7147   5283   7503   -539    322   -611       C  
ATOM   8829  N   VAL D 833    -111.947   1.819 -20.943  1.00 51.62           N  
ANISOU 8829  N   VAL D 833     7068   5443   7101   -385    389   -494       N  
ATOM   8830  CA  VAL D 833    -110.906   2.651 -21.521  1.00 50.78           C  
ANISOU 8830  CA  VAL D 833     6965   5441   6888   -309    392   -528       C  
ATOM   8831  C   VAL D 833    -110.196   1.831 -22.582  1.00 50.99           C  
ANISOU 8831  C   VAL D 833     7007   5422   6944   -248    359   -640       C  
ATOM   8832  O   VAL D 833    -109.681   0.778 -22.291  1.00 53.71           O  
ANISOU 8832  O   VAL D 833     7380   5655   7371   -225    350   -636       O  
ATOM   8833  CB  VAL D 833    -109.921   3.145 -20.441  1.00 48.18           C  
ANISOU 8833  CB  VAL D 833     6649   5146   6510   -270    424   -421       C  
ATOM   8834  CG1 VAL D 833    -108.778   3.939 -21.059  1.00 45.69           C  
ANISOU 8834  CG1 VAL D 833     6331   4930   6100   -196    426   -453       C  
ATOM   8835  CG2 VAL D 833    -110.664   4.001 -19.408  1.00 46.87           C  
ANISOU 8835  CG2 VAL D 833     6460   5040   6308   -322    451   -326       C  
ATOM   8836  N   ILE D 834    -110.150   2.333 -23.804  1.00 52.12           N  
ANISOU 8836  N   ILE D 834     7127   5660   7016   -215    341   -737       N  
ATOM   8837  CA  ILE D 834    -109.447   1.642 -24.869  1.00 55.91           C  
ANISOU 8837  CA  ILE D 834     7613   6127   7503   -143    309   -853       C  
ATOM   8838  C   ILE D 834    -108.022   2.163 -24.958  1.00 56.93           C  
ANISOU 8838  C   ILE D 834     7749   6338   7544    -57    327   -827       C  
ATOM   8839  O   ILE D 834    -107.083   1.388 -24.851  1.00 59.88           O  
ANISOU 8839  O   ILE D 834     8148   6648   7953     -1    319   -839       O  
ATOM   8840  CB  ILE D 834    -110.164   1.814 -26.222  1.00 57.49           C  
ANISOU 8840  CB  ILE D 834     7775   6403   7666   -142    278   -980       C  
ATOM   8841  CG1 ILE D 834    -111.524   1.147 -26.171  1.00 58.33           C  
ANISOU 8841  CG1 ILE D 834     7870   6417   7874   -225    253  -1021       C  
ATOM   8842  CG2 ILE D 834    -109.356   1.191 -27.352  1.00 60.74           C  
ANISOU 8842  CG2 ILE D 834     8182   6832   8063    -51    243  -1107       C  
ATOM   8843  CD1 ILE D 834    -112.383   1.531 -27.344  1.00 61.24           C  
ANISOU 8843  CD1 ILE D 834     8193   6883   8191   -233    227  -1129       C  
ATOM   8844  N   ASP D 835    -107.874   3.471 -25.177  1.00 56.63           N  
ANISOU 8844  N   ASP D 835     7682   6437   7398    -48    349   -790       N  
ATOM   8845  CA  ASP D 835    -106.557   4.130 -25.270  1.00 52.98           C  
ANISOU 8845  CA  ASP D 835     7214   6065   6853     23    368   -754       C  
ATOM   8846  C   ASP D 835    -106.526   5.413 -24.442  1.00 51.72           C  
ANISOU 8846  C   ASP D 835     7040   5971   6642     -8    402   -642       C  
ATOM   8847  O   ASP D 835    -107.554   6.089 -24.287  1.00 48.98           O  
ANISOU 8847  O   ASP D 835     6674   5652   6285    -68    408   -618       O  
ATOM   8848  CB  ASP D 835    -106.238   4.531 -26.705  1.00 53.90           C  
ANISOU 8848  CB  ASP D 835     7291   6304   6884     84    355   -837       C  
ATOM   8849  CG  ASP D 835    -106.048   3.344 -27.637  1.00 57.87           C  
ANISOU 8849  CG  ASP D 835     7799   6770   7419    139    317   -968       C  
ATOM   8850  OD1 ASP D 835    -106.632   3.391 -28.745  1.00 54.98           O  
ANISOU 8850  OD1 ASP D 835     7399   6474   7018    150    293  -1062       O  
ATOM   8851  OD2 ASP D 835    -105.311   2.390 -27.269  1.00 58.97           O  
ANISOU 8851  OD2 ASP D 835     7973   6816   7617    178    307   -980       O  
ATOM   8852  N   ILE D 836    -105.346   5.707 -23.898  1.00 49.69           N  
ANISOU 8852  N   ILE D 836     6789   5735   6356     37    421   -582       N  
ATOM   8853  CA  ILE D 836    -105.103   6.905 -23.148  1.00 47.21           C  
ANISOU 8853  CA  ILE D 836     6456   5483   5998     21    446   -492       C  
ATOM   8854  C   ILE D 836    -103.989   7.634 -23.848  1.00 46.57           C  
ANISOU 8854  C   ILE D 836     6344   5505   5846     83    453   -492       C  
ATOM   8855  O   ILE D 836    -102.906   7.107 -24.010  1.00 45.59           O  
ANISOU 8855  O   ILE D 836     6229   5378   5715    145    452   -508       O  
ATOM   8856  CB  ILE D 836    -104.691   6.614 -21.692  1.00 47.74           C  
ANISOU 8856  CB  ILE D 836     6550   5487   6103     16    461   -411       C  
ATOM   8857  CG1 ILE D 836    -105.774   5.795 -20.986  1.00 48.29           C  
ANISOU 8857  CG1 ILE D 836     6644   5456   6248    -44    458   -394       C  
ATOM   8858  CG2 ILE D 836    -104.502   7.930 -20.935  1.00 47.93           C  
ANISOU 8858  CG2 ILE D 836     6545   5583   6082      2    479   -338       C  
ATOM   8859  CD1 ILE D 836    -105.355   5.280 -19.625  1.00 50.85           C  
ANISOU 8859  CD1 ILE D 836     6992   5719   6609    -37    474   -311       C  
ATOM   8860  N   PHE D 837    -104.271   8.864 -24.247  1.00 48.29           N  
ANISOU 8860  N   PHE D 837     6520   5814   6015     65    461   -469       N  
ATOM   8861  CA  PHE D 837    -103.298   9.712 -24.901  1.00 47.52           C  
ANISOU 8861  CA  PHE D 837     6380   5819   5856    113    471   -448       C  
ATOM   8862  C   PHE D 837    -102.940  10.929 -24.037  1.00 48.12           C  
ANISOU 8862  C   PHE D 837     6433   5923   5929     91    487   -362       C  
ATOM   8863  O   PHE D 837    -103.813  11.532 -23.395  1.00 43.73           O  
ANISOU 8863  O   PHE D 837     5874   5350   5392     35    487   -332       O  
ATOM   8864  CB  PHE D 837    -103.862  10.218 -26.215  1.00 50.11           C  
ANISOU 8864  CB  PHE D 837     6668   6238   6135    117    466   -486       C  
ATOM   8865  CG  PHE D 837    -104.279   9.126 -27.172  1.00 53.57           C  
ANISOU 8865  CG  PHE D 837     7116   6666   6570    144    443   -590       C  
ATOM   8866  CD1 PHE D 837    -103.351   8.540 -28.017  1.00 55.34           C  
ANISOU 8866  CD1 PHE D 837     7331   6938   6758    223    436   -644       C  
ATOM   8867  CD2 PHE D 837    -105.599   8.708 -27.238  1.00 52.86           C  
ANISOU 8867  CD2 PHE D 837     7041   6528   6515     92    426   -640       C  
ATOM   8868  CE1 PHE D 837    -103.729   7.545 -28.898  1.00 58.29           C  
ANISOU 8868  CE1 PHE D 837     7709   7305   7133    254    408   -757       C  
ATOM   8869  CE2 PHE D 837    -105.992   7.718 -28.123  1.00 56.80           C  
ANISOU 8869  CE2 PHE D 837     7543   7015   7022    115    399   -749       C  
ATOM   8870  CZ  PHE D 837    -105.049   7.131 -28.955  1.00 58.12           C  
ANISOU 8870  CZ  PHE D 837     7702   7226   7155    199    387   -813       C  
ATOM   8871  N   LYS D 838    -101.653  11.263 -24.015  1.00 45.49           N  
ANISOU 8871  N   LYS D 838     6077   5633   5573    137    496   -328       N  
ATOM   8872  CA  LYS D 838    -101.156  12.471 -23.379  1.00 46.41           C  
ANISOU 8872  CA  LYS D 838     6158   5782   5692    123    505   -259       C  
ATOM   8873  C   LYS D 838    -101.041  13.517 -24.448  1.00 42.47           C  
ANISOU 8873  C   LYS D 838     5600   5376   5159    130    511   -236       C  
ATOM   8874  O   LYS D 838    -100.444  13.264 -25.476  1.00 38.97           O  
ANISOU 8874  O   LYS D 838     5136   4997   4675    179    516   -254       O  
ATOM   8875  CB  LYS D 838     -99.795  12.229 -22.736  1.00 49.78           C  
ANISOU 8875  CB  LYS D 838     6588   6205   6122    167    511   -234       C  
ATOM   8876  CG  LYS D 838     -99.369  13.280 -21.727  1.00 53.56           C  
ANISOU 8876  CG  LYS D 838     7035   6693   6621    148    513   -177       C  
ATOM   8877  CD  LYS D 838     -98.299  12.766 -20.766  1.00 56.58           C  
ANISOU 8877  CD  LYS D 838     7432   7053   7010    186    514   -164       C  
ATOM   8878  CE  LYS D 838     -98.290  13.510 -19.424  1.00 58.54           C  
ANISOU 8878  CE  LYS D 838     7665   7293   7285    161    508   -130       C  
ATOM   8879  NZ  LYS D 838     -98.772  14.923 -19.483  1.00 57.88           N  
ANISOU 8879  NZ  LYS D 838     7534   7239   7220    117    500   -111       N  
ATOM   8880  N   ILE D 839    -101.679  14.664 -24.240  1.00 40.28           N  
ANISOU 8880  N   ILE D 839     5294   5111   4899     84    510   -197       N  
ATOM   8881  CA  ILE D 839    -101.751  15.683 -25.281  1.00 40.79           C  
ANISOU 8881  CA  ILE D 839     5300   5258   4939     86    516   -163       C  
ATOM   8882  C   ILE D 839    -101.169  17.040 -24.852  1.00 44.26           C  
ANISOU 8882  C   ILE D 839     5688   5713   5416     70    519    -89       C  
ATOM   8883  O   ILE D 839    -101.339  17.457 -23.716  1.00 44.78           O  
ANISOU 8883  O   ILE D 839     5762   5724   5527     37    508    -79       O  
ATOM   8884  CB  ILE D 839    -103.188  15.873 -25.797  1.00 39.78           C  
ANISOU 8884  CB  ILE D 839     5174   5139   4802     51    510   -187       C  
ATOM   8885  CG1 ILE D 839    -104.158  16.192 -24.671  1.00 41.00           C  
ANISOU 8885  CG1 ILE D 839     5353   5225   5001     -7    499   -184       C  
ATOM   8886  CG2 ILE D 839    -103.654  14.631 -26.525  1.00 39.35           C  
ANISOU 8886  CG2 ILE D 839     5152   5086   4713     72    504   -266       C  
ATOM   8887  CD1 ILE D 839    -105.517  16.602 -25.188  1.00 39.81           C  
ANISOU 8887  CD1 ILE D 839     5191   5095   4840    -41    493   -198       C  
ATOM   8888  N   GLU D 840    -100.469  17.700 -25.777  1.00 44.25           N  
ANISOU 8888  N   GLU D 840     5626   5789   5397     96    531    -39       N  
ATOM   8889  CA  GLU D 840     -99.928  19.038 -25.557  1.00 43.34           C  
ANISOU 8889  CA  GLU D 840     5450   5685   5333     77    531     37       C  
ATOM   8890  C   GLU D 840    -100.279  19.851 -26.775  1.00 40.58           C  
ANISOU 8890  C   GLU D 840     5043   5410   4966     79    542     92       C  
ATOM   8891  O   GLU D 840     -99.681  19.678 -27.844  1.00 39.20           O  
ANISOU 8891  O   GLU D 840     4831   5325   4738    125    561    118       O  
ATOM   8892  CB  GLU D 840     -98.408  19.025 -25.386  1.00 45.41           C  
ANISOU 8892  CB  GLU D 840     5681   5970   5603    111    539     68       C  
ATOM   8893  CG  GLU D 840     -97.908  18.123 -24.266  1.00 49.07           C  
ANISOU 8893  CG  GLU D 840     6198   6376   6072    124    531     20       C  
ATOM   8894  CD  GLU D 840     -96.390  17.870 -24.307  1.00 54.32           C  
ANISOU 8894  CD  GLU D 840     6835   7082   6724    171    541     40       C  
ATOM   8895  OE1 GLU D 840     -95.663  18.377 -25.208  1.00 56.55           O  
ANISOU 8895  OE1 GLU D 840     7052   7442   6992    192    556     94       O  
ATOM   8896  OE2 GLU D 840     -95.902  17.146 -23.408  1.00 59.29           O  
ANISOU 8896  OE2 GLU D 840     7502   7671   7354    189    535      7       O  
ATOM   8897  N   ARG D 841    -101.265  20.728 -26.632  1.00 36.85           N  
ANISOU 8897  N   ARG D 841     4559   4910   4532     37    532    111       N  
ATOM   8898  CA  ARG D 841    -101.576  21.664 -27.690  1.00 37.64           C  
ANISOU 8898  CA  ARG D 841     4598   5077   4628     39    542    182       C  
ATOM   8899  C   ARG D 841    -100.506  22.766 -27.780  1.00 38.09           C  
ANISOU 8899  C   ARG D 841     4577   5148   4746     38    549    281       C  
ATOM   8900  O   ARG D 841    -100.124  23.360 -26.784  1.00 40.29           O  
ANISOU 8900  O   ARG D 841     4847   5353   5107      7    531    290       O  
ATOM   8901  CB  ARG D 841    -102.926  22.327 -27.466  1.00 37.30           C  
ANISOU 8901  CB  ARG D 841     4562   4994   4616     -3    526    176       C  
ATOM   8902  CG  ARG D 841    -104.120  21.378 -27.501  1.00 39.11           C  
ANISOU 8902  CG  ARG D 841     4851   5216   4790     -9    520     90       C  
ATOM   8903  CD  ARG D 841    -105.307  22.070 -28.163  1.00 38.67           C  
ANISOU 8903  CD  ARG D 841     4771   5196   4725    -23    517    111       C  
ATOM   8904  NE  ARG D 841    -105.493  23.303 -27.481  1.00 38.96           N  
ANISOU 8904  NE  ARG D 841     4781   5176   4846    -58    502    159       N  
ATOM   8905  CZ  ARG D 841    -105.389  24.530 -27.978  1.00 37.04           C  
ANISOU 8905  CZ  ARG D 841     4473   4954   4648    -58    505    248       C  
ATOM   8906  NH1 ARG D 841    -105.253  24.798 -29.272  1.00 34.57           N  
ANISOU 8906  NH1 ARG D 841     4107   4735   4291    -25    527    316       N  
ATOM   8907  NH2 ARG D 841    -105.548  25.510 -27.119  1.00 34.84           N  
ANISOU 8907  NH2 ARG D 841     4179   4597   4461    -91    482    265       N  
ATOM   8908  N   GLU D 842    -100.048  23.045 -28.987  1.00 38.42           N  
ANISOU 8908  N   GLU D 842     4557   5291   4750     72    573    355       N  
ATOM   8909  CA  GLU D 842     -99.122  24.134 -29.220  1.00 40.72           C  
ANISOU 8909  CA  GLU D 842     4763   5602   5107     66    583    468       C  
ATOM   8910  C   GLU D 842     -99.654  25.437 -28.656  1.00 39.48           C  
ANISOU 8910  C   GLU D 842     4579   5358   5065     11    561    512       C  
ATOM   8911  O   GLU D 842    -100.800  25.847 -28.930  1.00 40.64           O  
ANISOU 8911  O   GLU D 842     4731   5498   5212     -3    555    516       O  
ATOM   8912  CB  GLU D 842     -98.847  24.303 -30.737  1.00 43.43           C  
ANISOU 8912  CB  GLU D 842     5034   6086   5381    113    617    557       C  
ATOM   8913  N   GLY D 843     -98.819  26.096 -27.869  1.00 36.79           N  
ANISOU 8913  N   GLY D 843     4204   4950   4824    -16    545    540       N  
ATOM   8914  CA  GLY D 843     -99.164  27.417 -27.349  1.00 36.56           C  
ANISOU 8914  CA  GLY D 843     4136   4832   4923    -63    518    578       C  
ATOM   8915  C   GLY D 843     -99.947  27.385 -26.039  1.00 34.79           C  
ANISOU 8915  C   GLY D 843     3975   4509   4736    -92    480    473       C  
ATOM   8916  O   GLY D 843    -100.101  28.413 -25.399  1.00 33.71           O  
ANISOU 8916  O   GLY D 843     3807   4292   4710   -125    448    480       O  
ATOM   8917  N   GLU D 844    -100.428  26.221 -25.627  1.00 31.96           N  
ANISOU 8917  N   GLU D 844     3697   4156   4291    -79    481    378       N  
ATOM   8918  CA  GLU D 844    -101.326  26.199 -24.478  1.00 33.00           C  
ANISOU 8918  CA  GLU D 844     3879   4214   4444   -103    449    293       C  
ATOM   8919  C   GLU D 844    -100.575  26.384 -23.166  1.00 31.98           C  
ANISOU 8919  C   GLU D 844     3747   4023   4382   -113    421    250       C  
ATOM   8920  O   GLU D 844    -101.103  27.006 -22.251  1.00 29.11           O  
ANISOU 8920  O   GLU D 844     3382   3599   4080   -135    387    208       O  
ATOM   8921  CB  GLU D 844    -102.160  24.927 -24.443  1.00 33.10           C  
ANISOU 8921  CB  GLU D 844     3972   4249   4355    -91    460    217       C  
ATOM   8922  CG  GLU D 844    -103.524  25.144 -23.828  1.00 37.15           C  
ANISOU 8922  CG  GLU D 844     4517   4719   4878   -118    438    166       C  
ATOM   8923  CD  GLU D 844    -104.399  23.883 -23.859  1.00 37.54           C  
ANISOU 8923  CD  GLU D 844     4637   4788   4838   -114    449     99       C  
ATOM   8924  OE1 GLU D 844    -103.975  22.915 -23.224  1.00 33.12           O  
ANISOU 8924  OE1 GLU D 844     4120   4213   4251   -104    451     55       O  
ATOM   8925  OE2 GLU D 844    -105.497  23.902 -24.521  1.00 38.90           O  
ANISOU 8925  OE2 GLU D 844     4816   4988   4976   -121    453     96       O  
ATOM   8926  N   CYS D 845     -99.343  25.874 -23.091  1.00 32.21           N  
ANISOU 8926  N   CYS D 845     3767   4077   4396    -92    433    257       N  
ATOM   8927  CA  CYS D 845     -98.510  26.041 -21.895  1.00 32.55           C  
ANISOU 8927  CA  CYS D 845     3796   4077   4496    -96    407    217       C  
ATOM   8928  C   CYS D 845     -98.258  27.522 -21.641  1.00 32.04           C  
ANISOU 8928  C   CYS D 845     3652   3955   4566   -127    374    252       C  
ATOM   8929  O   CYS D 845     -98.435  28.021 -20.538  1.00 30.74           O  
ANISOU 8929  O   CYS D 845     3482   3734   4465   -140    334    190       O  
ATOM   8930  CB  CYS D 845     -97.159  25.294 -22.007  1.00 32.50           C  
ANISOU 8930  CB  CYS D 845     3783   4117   4449    -64    427    230       C  
ATOM   8931  SG  CYS D 845     -96.008  25.651 -20.621  1.00 35.24           S  
ANISOU 8931  SG  CYS D 845     4093   4424   4872    -65    392    187       S  
ATOM   8932  N   GLN D 846     -97.882  28.224 -22.689  1.00 33.10           N  
ANISOU 8932  N   GLN D 846     3721   4107   4746   -136    390    352       N  
ATOM   8933  CA  GLN D 846     -97.644  29.665 -22.606  1.00 36.16           C  
ANISOU 8933  CA  GLN D 846     4026   4429   5283   -170    360    402       C  
ATOM   8934  C   GLN D 846     -98.934  30.420 -22.259  1.00 33.32           C  
ANISOU 8934  C   GLN D 846     3678   4005   4978   -190    327    367       C  
ATOM   8935  O   GLN D 846     -98.931  31.291 -21.393  1.00 31.64           O  
ANISOU 8935  O   GLN D 846     3431   3713   4877   -209    280    324       O  
ATOM   8936  CB  GLN D 846     -97.031  30.176 -23.918  1.00 37.85           C  
ANISOU 8936  CB  GLN D 846     4166   4688   5528   -173    393    540       C  
ATOM   8937  CG  GLN D 846     -96.573  31.629 -23.876  1.00 42.30           C  
ANISOU 8937  CG  GLN D 846     4631   5174   6266   -212    364    610       C  
ATOM   8938  CD  GLN D 846     -95.436  31.880 -22.876  1.00 44.31           C  
ANISOU 8938  CD  GLN D 846     4845   5380   6612   -227    329    563       C  
ATOM   8939  OE1 GLN D 846     -94.539  31.033 -22.684  1.00 45.95           O  
ANISOU 8939  OE1 GLN D 846     5066   5644   6748   -204    346    538       O  
ATOM   8940  NE2 GLN D 846     -95.432  33.073 -22.281  1.00 44.49           N  
ANISOU 8940  NE2 GLN D 846     4809   5299   6799   -262    278    550       N  
ATOM   8941  N   ARG D 847    -100.036  30.038 -22.881  1.00 31.39           N  
ANISOU 8941  N   ARG D 847     3479   3797   4650   -181    349    374       N  
ATOM   8942  CA  ARG D 847    -101.317  30.657 -22.547  1.00 35.55           C  
ANISOU 8942  CA  ARG D 847     4021   4275   5213   -194    320    336       C  
ATOM   8943  C   ARG D 847    -101.743  30.366 -21.084  1.00 36.25           C  
ANISOU 8943  C   ARG D 847     4155   4326   5291   -192    283    209       C  
ATOM   8944  O   ARG D 847    -102.260  31.236 -20.391  1.00 36.66           O  
ANISOU 8944  O   ARG D 847     4185   4316   5426   -202    239    164       O  
ATOM   8945  CB  ARG D 847    -102.391  30.176 -23.518  1.00 36.01           C  
ANISOU 8945  CB  ARG D 847     4118   4395   5169   -183    353    362       C  
ATOM   8946  CG  ARG D 847    -103.732  30.868 -23.383  1.00 35.34           C  
ANISOU 8946  CG  ARG D 847     4039   4272   5116   -193    328    340       C  
ATOM   8947  CD  ARG D 847    -104.701  30.295 -24.391  1.00 35.84           C  
ANISOU 8947  CD  ARG D 847     4136   4411   5069   -179    362    363       C  
ATOM   8948  NE  ARG D 847    -105.222  28.988 -23.966  1.00 36.42           N  
ANISOU 8948  NE  ARG D 847     4290   4520   5028   -172    372    272       N  
ATOM   8949  CZ  ARG D 847    -106.195  28.325 -24.591  1.00 35.45           C  
ANISOU 8949  CZ  ARG D 847     4205   4454   4809   -164    393    256       C  
ATOM   8950  NH1 ARG D 847    -106.782  28.847 -25.643  1.00 37.65           N  
ANISOU 8950  NH1 ARG D 847     4453   4773   5080   -157    405    320       N  
ATOM   8951  NH2 ARG D 847    -106.600  27.141 -24.145  1.00 37.95           N  
ANISOU 8951  NH2 ARG D 847     4588   4788   5043   -163    399    177       N  
ATOM   8952  N   TYR D 848    -101.466  29.157 -20.601  1.00 35.75           N  
ANISOU 8952  N   TYR D 848     4149   4305   5129   -173    300    154       N  
ATOM   8953  CA  TYR D 848    -101.856  28.760 -19.236  1.00 34.40           C  
ANISOU 8953  CA  TYR D 848     4019   4121   4932   -164    272     49       C  
ATOM   8954  C   TYR D 848    -100.970  29.346 -18.127  1.00 34.68           C  
ANISOU 8954  C   TYR D 848     4007   4117   5053   -160    229     -1       C  
ATOM   8955  O   TYR D 848    -101.368  29.392 -16.971  1.00 34.72           O  
ANISOU 8955  O   TYR D 848     4023   4113   5056   -149    196    -87       O  
ATOM   8956  CB  TYR D 848    -101.860  27.242 -19.157  1.00 31.62           C  
ANISOU 8956  CB  TYR D 848     3739   3822   4452   -144    307     24       C  
ATOM   8957  CG  TYR D 848    -102.392  26.662 -17.871  1.00 31.43           C  
ANISOU 8957  CG  TYR D 848     3760   3801   4382   -132    291    -60       C  
ATOM   8958  CD1 TYR D 848    -103.748  26.746 -17.547  1.00 29.52           C  
ANISOU 8958  CD1 TYR D 848     3542   3557   4116   -141    280    -97       C  
ATOM   8959  CD2 TYR D 848    -101.559  25.959 -17.007  1.00 29.75           C  
ANISOU 8959  CD2 TYR D 848     3561   3605   4137   -108    290    -95       C  
ATOM   8960  CE1 TYR D 848    -104.255  26.159 -16.380  1.00 30.18           C  
ANISOU 8960  CE1 TYR D 848     3660   3660   4148   -128    270   -161       C  
ATOM   8961  CE2 TYR D 848    -102.062  25.373 -15.842  1.00 29.86           C  
ANISOU 8961  CE2 TYR D 848     3611   3636   4100    -92    280   -156       C  
ATOM   8962  CZ  TYR D 848    -103.407  25.481 -15.533  1.00 28.98           C  
ANISOU 8962  CZ  TYR D 848     3519   3526   3966   -103    271   -186       C  
ATOM   8963  OH  TYR D 848    -103.923  24.926 -14.395  1.00 31.17           O  
ANISOU 8963  OH  TYR D 848     3822   3833   4189    -86    265   -233       O  
ATOM   8964  N   LYS D 849     -99.798  29.835 -18.505  1.00 36.47           N  
ANISOU 8964  N   LYS D 849     4173   4327   5355   -169    228     52       N  
ATOM   8965  CA  LYS D 849     -98.758  30.284 -17.569  1.00 36.71           C  
ANISOU 8965  CA  LYS D 849     4152   4329   5467   -165    189      5       C  
ATOM   8966  C   LYS D 849     -99.243  31.187 -16.434  1.00 34.34           C  
ANISOU 8966  C   LYS D 849     3820   3974   5251   -165    125    -90       C  
ATOM   8967  O   LYS D 849     -98.897  30.961 -15.291  1.00 35.80           O  
ANISOU 8967  O   LYS D 849     4005   4176   5421   -141     97   -177       O  
ATOM   8968  CB  LYS D 849     -97.632  30.975 -18.363  1.00 40.93           C  
ANISOU 8968  CB  LYS D 849     4607   4842   6101   -188    195     96       C  
ATOM   8969  CG  LYS D 849     -96.405  31.356 -17.558  1.00 43.58           C  
ANISOU 8969  CG  LYS D 849     4882   5155   6522   -188    159     55       C  
ATOM   8970  CD  LYS D 849     -95.358  31.911 -18.490  1.00 48.04           C  
ANISOU 8970  CD  LYS D 849     5369   5710   7176   -214    175    165       C  
ATOM   8971  CE  LYS D 849     -94.096  32.223 -17.728  1.00 51.58           C  
ANISOU 8971  CE  LYS D 849     5751   6141   7707   -217    140    123       C  
ATOM   8972  NZ  LYS D 849     -94.326  33.269 -16.697  1.00 53.79           N  
ANISOU 8972  NZ  LYS D 849     5982   6336   8118   -230     66     27       N  
ATOM   8973  N   PRO D 850    -100.057  32.215 -16.733  1.00 32.84           N  
ANISOU 8973  N   PRO D 850     3602   3727   5148   -184    100    -78       N  
ATOM   8974  CA  PRO D 850    -100.545  33.075 -15.632  1.00 33.44           C  
ANISOU 8974  CA  PRO D 850     3647   3754   5304   -175     33   -184       C  
ATOM   8975  C   PRO D 850    -101.374  32.315 -14.573  1.00 34.67           C  
ANISOU 8975  C   PRO D 850     3863   3973   5340   -139     27   -283       C  
ATOM   8976  O   PRO D 850    -101.443  32.736 -13.426  1.00 34.55           O  
ANISOU 8976  O   PRO D 850     3818   3953   5356   -115    -26   -388       O  
ATOM   8977  CB  PRO D 850    -101.394  34.129 -16.342  1.00 32.06           C  
ANISOU 8977  CB  PRO D 850     3444   3513   5224   -197     19   -137       C  
ATOM   8978  CG  PRO D 850    -100.946  34.095 -17.768  1.00 32.55           C  
ANISOU 8978  CG  PRO D 850     3493   3579   5295   -222     70      5       C  
ATOM   8979  CD  PRO D 850    -100.487  32.700 -18.050  1.00 31.98           C  
ANISOU 8979  CD  PRO D 850     3479   3598   5074   -209    127     30       C  
ATOM   8980  N   PHE D 851    -101.951  31.180 -14.957  1.00 32.97           N  
ANISOU 8980  N   PHE D 851     3723   3819   4987   -135     81   -249       N  
ATOM   8981  CA  PHE D 851    -102.785  30.413 -14.064  1.00 32.51           C  
ANISOU 8981  CA  PHE D 851     3716   3818   4817   -108     83   -317       C  
ATOM   8982  C   PHE D 851    -102.062  29.234 -13.431  1.00 33.53           C  
ANISOU 8982  C   PHE D 851     3880   4008   4852    -82    106   -334       C  
ATOM   8983  O   PHE D 851    -102.568  28.612 -12.509  1.00 30.14           O  
ANISOU 8983  O   PHE D 851     3482   3631   4339    -55    105   -386       O  
ATOM   8984  CB  PHE D 851    -104.065  30.019 -14.830  1.00 31.92           C  
ANISOU 8984  CB  PHE D 851     3696   3761   4673   -123    118   -275       C  
ATOM   8985  CG  PHE D 851    -104.881  31.220 -15.260  1.00 31.75           C  
ANISOU 8985  CG  PHE D 851     3638   3687   4740   -138     89   -269       C  
ATOM   8986  CD1 PHE D 851    -105.613  31.942 -14.334  1.00 31.88           C  
ANISOU 8986  CD1 PHE D 851     3628   3691   4792   -119     38   -357       C  
ATOM   8987  CD2 PHE D 851    -104.873  31.657 -16.588  1.00 32.95           C  
ANISOU 8987  CD2 PHE D 851     3774   3805   4939   -164    112   -173       C  
ATOM   8988  CE1 PHE D 851    -106.338  33.061 -14.723  1.00 33.16           C  
ANISOU 8988  CE1 PHE D 851     3756   3799   5044   -127      7   -353       C  
ATOM   8989  CE2 PHE D 851    -105.586  32.768 -16.991  1.00 31.54           C  
ANISOU 8989  CE2 PHE D 851     3560   3576   4848   -173     86   -157       C  
ATOM   8990  CZ  PHE D 851    -106.330  33.468 -16.054  1.00 33.50           C  
ANISOU 8990  CZ  PHE D 851     3789   3801   5140   -155     32   -249       C  
ATOM   8991  N   LYS D 852    -100.866  28.951 -13.923  1.00 36.32           N  
ANISOU 8991  N   LYS D 852     4223   4358   5220    -87    127   -284       N  
ATOM   8992  CA  LYS D 852    -100.070  27.778 -13.526  1.00 38.01           C  
ANISOU 8992  CA  LYS D 852     4470   4625   5346    -60    155   -284       C  
ATOM   8993  C   LYS D 852     -99.800  27.660 -12.026  1.00 37.90           C  
ANISOU 8993  C   LYS D 852     4440   4653   5308    -19    121   -372       C  
ATOM   8994  O   LYS D 852     -99.684  26.545 -11.516  1.00 35.75           O  
ANISOU 8994  O   LYS D 852     4213   4435   4937     10    146   -373       O  
ATOM   8995  CB  LYS D 852     -98.731  27.824 -14.295  1.00 40.53           C  
ANISOU 8995  CB  LYS D 852     4757   4932   5710    -70    172   -222       C  
ATOM   8996  CG  LYS D 852     -97.746  26.693 -14.089  1.00 42.82           C  
ANISOU 8996  CG  LYS D 852     5075   5272   5923    -39    201   -212       C  
ATOM   8997  CD  LYS D 852     -98.254  25.388 -14.664  1.00 47.40           C  
ANISOU 8997  CD  LYS D 852     5737   5881   6391    -32    254   -172       C  
ATOM   8998  CE  LYS D 852     -97.352  24.233 -14.221  1.00 47.18           C  
ANISOU 8998  CE  LYS D 852     5740   5896   6291      8    275   -175       C  
ATOM   8999  NZ  LYS D 852     -97.977  22.939 -14.555  1.00 50.45           N  
ANISOU 8999  NZ  LYS D 852     6234   6324   6611     16    315   -154       N  
ATOM   9000  N   GLN D 853     -99.773  28.794 -11.332  1.00 37.93           N  
ANISOU 9000  N   GLN D 853     4377   4634   5401    -12     61   -445       N  
ATOM   9001  CA  GLN D 853     -99.616  28.861  -9.882  1.00 41.26           C  
ANISOU 9001  CA  GLN D 853     4768   5109   5800     36     18   -545       C  
ATOM   9002  C   GLN D 853    -100.803  29.442  -9.109  1.00 40.53           C  
ANISOU 9002  C   GLN D 853     4660   5033   5705     55    -22   -625       C  
ATOM   9003  O   GLN D 853    -100.664  29.741  -7.934  1.00 40.15           O  
ANISOU 9003  O   GLN D 853     4569   5035   5653    101    -69   -720       O  
ATOM   9004  CB  GLN D 853     -98.332  29.633  -9.586  1.00 46.74           C  
ANISOU 9004  CB  GLN D 853     5381   5777   6599     41    -27   -587       C  
ATOM   9005  CG  GLN D 853     -97.101  28.841 -10.017  1.00 48.68           C  
ANISOU 9005  CG  GLN D 853     5641   6043   6813     41     13   -522       C  
ATOM   9006  CD  GLN D 853     -95.916  29.116  -9.154  1.00 51.91           C  
ANISOU 9006  CD  GLN D 853     5983   6481   7261     71    -28   -590       C  
ATOM   9007  OE1 GLN D 853     -95.266  30.135  -9.287  1.00 55.29           O  
ANISOU 9007  OE1 GLN D 853     6335   6853   7820     48    -70   -614       O  
ATOM   9008  NE2 GLN D 853     -95.648  28.208  -8.224  1.00 58.26           N  
ANISOU 9008  NE2 GLN D 853     6809   7373   7955    125    -19   -623       N  
ATOM   9009  N   LEU D 854    -101.978  29.593  -9.741  1.00 40.13           N  
ANISOU 9009  N   LEU D 854     4643   4956   5650     28     -7   -592       N  
ATOM   9010  CA  LEU D 854    -103.237  29.742  -8.984  1.00 38.96           C  
ANISOU 9010  CA  LEU D 854     4498   4853   5452     53    -28   -655       C  
ATOM   9011  C   LEU D 854    -103.355  28.475  -8.173  1.00 37.63           C  
ANISOU 9011  C   LEU D 854     4371   4783   5142     89      6   -651       C  
ATOM   9012  O   LEU D 854    -102.940  27.394  -8.597  1.00 38.88           O  
ANISOU 9012  O   LEU D 854     4582   4949   5240     78     58   -577       O  
ATOM   9013  CB  LEU D 854    -104.443  29.874  -9.929  1.00 38.96           C  
ANISOU 9013  CB  LEU D 854     4534   4816   5451     16     -4   -602       C  
ATOM   9014  CG  LEU D 854    -105.691  30.675  -9.562  1.00 40.54           C  
ANISOU 9014  CG  LEU D 854     4712   5021   5669     28    -42   -665       C  
ATOM   9015  CD1 LEU D 854    -105.325  32.053  -9.048  1.00 45.07           C  
ANISOU 9015  CD1 LEU D 854     5204   5547   6373     49   -119   -758       C  
ATOM   9016  CD2 LEU D 854    -106.613  30.790 -10.784  1.00 39.74           C  
ANISOU 9016  CD2 LEU D 854     4645   4874   5578    -15    -12   -592       C  
ATOM   9017  N   HIS D 855    -104.005  28.578  -7.041  1.00 37.29           N  
ANISOU 9017  N   HIS D 855     4305   4816   5046    134    -23   -724       N  
ATOM   9018  CA  HIS D 855    -104.289  27.406  -6.226  1.00 35.66           C  
ANISOU 9018  CA  HIS D 855     4132   4712   4705    169     12   -705       C  
ATOM   9019  C   HIS D 855    -105.542  26.666  -6.745  1.00 32.41           C  
ANISOU 9019  C   HIS D 855     3783   4304   4225    135     62   -635       C  
ATOM   9020  O   HIS D 855    -106.212  27.127  -7.679  1.00 30.10           O  
ANISOU 9020  O   HIS D 855     3507   3949   3982     92     65   -614       O  
ATOM   9021  CB  HIS D 855    -104.499  27.835  -4.784  1.00 36.90           C  
ANISOU 9021  CB  HIS D 855     4227   4971   4823    239    -39   -809       C  
ATOM   9022  CG  HIS D 855    -105.691  28.719  -4.592  1.00 36.34           C  
ANISOU 9022  CG  HIS D 855     4125   4908   4772    246    -76   -874       C  
ATOM   9023  ND1 HIS D 855    -105.794  29.974  -5.155  1.00 34.64           N  
ANISOU 9023  ND1 HIS D 855     3876   4600   4685    223   -123   -921       N  
ATOM   9024  CD2 HIS D 855    -106.833  28.525  -3.890  1.00 36.83           C  
ANISOU 9024  CD2 HIS D 855     4183   5066   4744    278    -74   -894       C  
ATOM   9025  CE1 HIS D 855    -106.955  30.510  -4.819  1.00 35.48           C  
ANISOU 9025  CE1 HIS D 855     3962   4740   4779    242   -150   -976       C  
ATOM   9026  NE2 HIS D 855    -107.591  29.663  -4.029  1.00 36.66           N  
ANISOU 9026  NE2 HIS D 855     4126   5010   4792    277   -122   -964       N  
ATOM   9027  N   ASN D 856    -105.803  25.494  -6.171  1.00 31.04           N  
ANISOU 9027  N   ASN D 856     3645   4205   3945    154    101   -592       N  
ATOM   9028  CA  ASN D 856    -106.979  24.716  -6.489  1.00 32.27           C  
ANISOU 9028  CA  ASN D 856     3851   4372   4039    123    145   -530       C  
ATOM   9029  C   ASN D 856    -107.079  24.367  -7.992  1.00 32.21           C  
ANISOU 9029  C   ASN D 856     3900   4268   4069     58    183   -461       C  
ATOM   9030  O   ASN D 856    -108.041  24.696  -8.704  1.00 31.41           O  
ANISOU 9030  O   ASN D 856     3811   4135   3986     21    187   -452       O  
ATOM   9031  CB  ASN D 856    -108.221  25.455  -5.985  1.00 34.97           C  
ANISOU 9031  CB  ASN D 856     4156   4766   4366    137    115   -587       C  
ATOM   9032  CG  ASN D 856    -109.464  24.614  -6.076  1.00 38.45           C  
ANISOU 9032  CG  ASN D 856     4635   5241   4733    110    158   -527       C  
ATOM   9033  OD1 ASN D 856    -109.392  23.397  -6.144  1.00 38.60           O  
ANISOU 9033  OD1 ASN D 856     4700   5264   4703     94    207   -450       O  
ATOM   9034  ND2 ASN D 856    -110.607  25.261  -6.102  1.00 43.00           N  
ANISOU 9034  ND2 ASN D 856     5189   5837   5310    104    139   -561       N  
ATOM   9035  N   ARG D 857    -106.031  23.718  -8.464  1.00 33.44           N  
ANISOU 9035  N   ARG D 857     4086   4385   4233     52    209   -416       N  
ATOM   9036  CA  ARG D 857    -105.958  23.228  -9.821  1.00 33.12           C  
ANISOU 9036  CA  ARG D 857     4096   4276   4214      5    245   -355       C  
ATOM   9037  C   ARG D 857    -106.424  21.791  -9.828  1.00 32.61           C  
ANISOU 9037  C   ARG D 857     4089   4223   4078     -6    292   -298       C  
ATOM   9038  O   ARG D 857    -105.970  20.992  -9.017  1.00 32.85           O  
ANISOU 9038  O   ARG D 857     4129   4291   4063     27    306   -280       O  
ATOM   9039  CB  ARG D 857    -104.538  23.350 -10.314  1.00 35.63           C  
ANISOU 9039  CB  ARG D 857     4404   4553   4579     11    244   -344       C  
ATOM   9040  CG  ARG D 857    -104.273  24.773 -10.735  1.00 38.59           C  
ANISOU 9040  CG  ARG D 857     4726   4887   5050     -1    203   -377       C  
ATOM   9041  CD  ARG D 857    -102.828  25.187 -10.855  1.00 38.12           C  
ANISOU 9041  CD  ARG D 857     4629   4805   5052     11    187   -381       C  
ATOM   9042  NE  ARG D 857    -101.865  24.111 -10.711  1.00 39.20           N  
ANISOU 9042  NE  ARG D 857     4794   4964   5137     34    217   -350       N  
ATOM   9043  CZ  ARG D 857    -100.986  24.001  -9.728  1.00 43.45           C  
ANISOU 9043  CZ  ARG D 857     5303   5544   5660     77    199   -383       C  
ATOM   9044  NH1 ARG D 857    -100.922  24.907  -8.753  1.00 45.37           N  
ANISOU 9044  NH1 ARG D 857     5485   5818   5936    104    148   -460       N  
ATOM   9045  NH2 ARG D 857    -100.153  22.970  -9.738  1.00 50.57           N  
ANISOU 9045  NH2 ARG D 857     6236   6461   6515     98    230   -345       N  
ATOM   9046  N   ARG D 858    -107.319  21.470 -10.745  1.00 31.71           N  
ANISOU 9046  N   ARG D 858     4010   4075   3962    -50    315   -269       N  
ATOM   9047  CA  ARG D 858    -107.998  20.200 -10.705  1.00 34.34           C  
ANISOU 9047  CA  ARG D 858     4389   4412   4245    -69    352   -224       C  
ATOM   9048  C   ARG D 858    -108.065  19.548 -12.061  1.00 30.93           C  
ANISOU 9048  C   ARG D 858     4004   3918   3828   -107    379   -194       C  
ATOM   9049  O   ARG D 858    -108.283  20.224 -13.071  1.00 30.22           O  
ANISOU 9049  O   ARG D 858     3908   3804   3771   -130    371   -206       O  
ATOM   9050  CB  ARG D 858    -109.439  20.392 -10.175  1.00 34.86           C  
ANISOU 9050  CB  ARG D 858     4439   4527   4280    -83    347   -235       C  
ATOM   9051  CG  ARG D 858    -109.819  19.348  -9.159  1.00 41.24           C  
ANISOU 9051  CG  ARG D 858     5256   5385   5029    -71    371   -194       C  
ATOM   9052  CD  ARG D 858    -111.112  19.635  -8.395  1.00 43.97           C  
ANISOU 9052  CD  ARG D 858     5568   5807   5333    -72    364   -204       C  
ATOM   9053  NE  ARG D 858    -110.919  20.525  -7.247  1.00 45.47           N  
ANISOU 9053  NE  ARG D 858     5698   6082   5499    -14    328   -256       N  
ATOM   9054  CZ  ARG D 858    -111.838  20.789  -6.322  1.00 49.86           C  
ANISOU 9054  CZ  ARG D 858     6211   6732   6002      8    318   -271       C  
ATOM   9055  NH1 ARG D 858    -113.047  20.224  -6.372  1.00 50.56           N  
ANISOU 9055  NH1 ARG D 858     6308   6842   6059    -28    345   -227       N  
ATOM   9056  NH2 ARG D 858    -111.553  21.644  -5.342  1.00 51.22           N  
ANISOU 9056  NH2 ARG D 858     6324   6984   6155     70    279   -337       N  
ATOM   9057  N   LEU D 859    -107.864  18.228 -12.065  1.00 30.31           N  
ANISOU 9057  N   LEU D 859     3970   3819   3729   -108    409   -156       N  
ATOM   9058  CA  LEU D 859    -107.968  17.411 -13.261  1.00 30.21           C  
ANISOU 9058  CA  LEU D 859     4002   3751   3727   -137    432   -140       C  
ATOM   9059  C   LEU D 859    -109.411  16.931 -13.426  1.00 32.37           C  
ANISOU 9059  C   LEU D 859     4290   4020   3989   -182    443   -133       C  
ATOM   9060  O   LEU D 859    -109.914  16.118 -12.640  1.00 32.12           O  
ANISOU 9060  O   LEU D 859     4270   3996   3940   -189    457   -103       O  
ATOM   9061  CB  LEU D 859    -107.000  16.231 -13.175  1.00 31.55           C  
ANISOU 9061  CB  LEU D 859     4207   3887   3892   -111    452   -111       C  
ATOM   9062  CG  LEU D 859    -106.714  15.575 -14.540  1.00 32.71           C  
ANISOU 9062  CG  LEU D 859     4389   3982   4055   -123    465   -116       C  
ATOM   9063  CD1 LEU D 859    -105.789  16.442 -15.401  1.00 31.83           C  
ANISOU 9063  CD1 LEU D 859     4255   3881   3959   -105    455   -132       C  
ATOM   9064  CD2 LEU D 859    -106.114  14.190 -14.337  1.00 33.78           C  
ANISOU 9064  CD2 LEU D 859     4567   4076   4191   -100    484    -90       C  
ATOM   9065  N   LEU D 860    -110.073  17.459 -14.450  1.00 31.52           N  
ANISOU 9065  N   LEU D 860     4177   3905   3893   -212    437   -156       N  
ATOM   9066  CA  LEU D 860    -111.517  17.329 -14.601  1.00 29.76           C  
ANISOU 9066  CA  LEU D 860     3953   3694   3659   -254    440   -161       C  
ATOM   9067  C   LEU D 860    -111.878  16.900 -16.025  1.00 30.72           C  
ANISOU 9067  C   LEU D 860     4098   3783   3792   -284    448   -176       C  
ATOM   9068  O   LEU D 860    -111.093  17.086 -16.960  1.00 29.13           O  
ANISOU 9068  O   LEU D 860     3901   3567   3599   -266    447   -186       O  
ATOM   9069  CB  LEU D 860    -112.188  18.667 -14.315  1.00 30.15           C  
ANISOU 9069  CB  LEU D 860     3957   3793   3705   -254    416   -186       C  
ATOM   9070  CG  LEU D 860    -112.036  19.212 -12.902  1.00 32.19           C  
ANISOU 9070  CG  LEU D 860     4181   4102   3948   -219    399   -192       C  
ATOM   9071  CD1 LEU D 860    -112.571  20.643 -12.830  1.00 31.22           C  
ANISOU 9071  CD1 LEU D 860     4012   4013   3837   -211    367   -233       C  
ATOM   9072  CD2 LEU D 860    -112.763  18.326 -11.882  1.00 33.69           C  
ANISOU 9072  CD2 LEU D 860     4374   4328   4100   -227    417   -160       C  
ATOM   9073  N   TRP D 861    -113.062  16.316 -16.160  1.00 28.61           N  
ANISOU 9073  N   TRP D 861     3838   3512   3520   -325    455   -179       N  
ATOM   9074  CA  TRP D 861    -113.509  15.763 -17.405  1.00 29.24           C  
ANISOU 9074  CA  TRP D 861     3936   3567   3608   -352    459   -206       C  
ATOM   9075  C   TRP D 861    -114.175  16.797 -18.293  1.00 28.61           C  
ANISOU 9075  C   TRP D 861     3827   3530   3515   -360    445   -232       C  
ATOM   9076  O   TRP D 861    -114.853  17.705 -17.803  1.00 26.02           O  
ANISOU 9076  O   TRP D 861     3468   3242   3176   -365    434   -231       O  
ATOM   9077  CB  TRP D 861    -114.536  14.638 -17.148  1.00 30.35           C  
ANISOU 9077  CB  TRP D 861     4090   3681   3761   -398    469   -200       C  
ATOM   9078  CG  TRP D 861    -114.033  13.496 -16.335  1.00 30.12           C  
ANISOU 9078  CG  TRP D 861     4088   3601   3755   -394    484   -160       C  
ATOM   9079  CD1 TRP D 861    -114.329  13.224 -15.022  1.00 29.85           C  
ANISOU 9079  CD1 TRP D 861     4043   3582   3716   -400    496   -108       C  
ATOM   9080  CD2 TRP D 861    -113.163  12.455 -16.774  1.00 30.53           C  
ANISOU 9080  CD2 TRP D 861     4178   3585   3838   -378    490   -165       C  
ATOM   9081  NE1 TRP D 861    -113.671  12.087 -14.608  1.00 31.26           N  
ANISOU 9081  NE1 TRP D 861     4251   3702   3924   -388    510    -69       N  
ATOM   9082  CE2 TRP D 861    -112.951  11.591 -15.666  1.00 32.06           C  
ANISOU 9082  CE2 TRP D 861     4386   3745   4052   -375    505   -108       C  
ATOM   9083  CE3 TRP D 861    -112.546  12.155 -17.991  1.00 31.45           C  
ANISOU 9083  CE3 TRP D 861     4314   3673   3964   -358    484   -211       C  
ATOM   9084  CZ2 TRP D 861    -112.148  10.457 -15.749  1.00 34.13           C  
ANISOU 9084  CZ2 TRP D 861     4683   3931   4352   -356    512    -97       C  
ATOM   9085  CZ3 TRP D 861    -111.739  11.014 -18.074  1.00 31.66           C  
ANISOU 9085  CZ3 TRP D 861     4376   3631   4023   -337    489   -211       C  
ATOM   9086  CH2 TRP D 861    -111.546  10.191 -16.963  1.00 33.91           C  
ANISOU 9086  CH2 TRP D 861     4677   3869   4336   -337    502   -154       C  
ATOM   9087  N   HIS D 862    -114.027  16.609 -19.605  1.00 27.78           N  
ANISOU 9087  N   HIS D 862     3729   3421   3406   -356    446   -258       N  
ATOM   9088  CA  HIS D 862    -114.870  17.319 -20.561  1.00 29.82           C  
ANISOU 9088  CA  HIS D 862     3960   3725   3646   -367    437   -279       C  
ATOM   9089  C   HIS D 862    -115.163  16.441 -21.777  1.00 29.86           C  
ANISOU 9089  C   HIS D 862     3977   3728   3641   -376    439   -321       C  
ATOM   9090  O   HIS D 862    -114.259  16.008 -22.460  1.00 27.21           O  
ANISOU 9090  O   HIS D 862     3655   3382   3303   -347    443   -332       O  
ATOM   9091  CB  HIS D 862    -114.222  18.610 -21.038  1.00 29.29           C  
ANISOU 9091  CB  HIS D 862     3863   3690   3578   -332    429   -259       C  
ATOM   9092  CG  HIS D 862    -115.084  19.387 -21.968  1.00 30.10           C  
ANISOU 9092  CG  HIS D 862     3933   3842   3662   -336    421   -267       C  
ATOM   9093  ND1 HIS D 862    -115.958  20.355 -21.537  1.00 31.54           N  
ANISOU 9093  ND1 HIS D 862     4086   4050   3847   -346    408   -262       N  
ATOM   9094  CD2 HIS D 862    -115.238  19.311 -23.307  1.00 34.01           C  
ANISOU 9094  CD2 HIS D 862     4416   4374   4130   -326    424   -281       C  
ATOM   9095  CE1 HIS D 862    -116.610  20.854 -22.571  1.00 33.51           C  
ANISOU 9095  CE1 HIS D 862     4311   4345   4077   -344    404   -267       C  
ATOM   9096  NE2 HIS D 862    -116.184  20.246 -23.660  1.00 35.17           N  
ANISOU 9096  NE2 HIS D 862     4529   4568   4265   -330    415   -276       N  
ATOM   9097  N   GLY D 863    -116.437  16.138 -21.982  1.00 34.48           N  
ANISOU 9097  N   GLY D 863     4554   4328   4221   -416    434   -350       N  
ATOM   9098  CA  GLY D 863    -116.871  15.276 -23.062  1.00 37.34           C  
ANISOU 9098  CA  GLY D 863     4920   4689   4578   -428    429   -407       C  
ATOM   9099  C   GLY D 863    -117.466  16.094 -24.168  1.00 38.28           C  
ANISOU 9099  C   GLY D 863     5002   4887   4655   -415    420   -428       C  
ATOM   9100  O   GLY D 863    -118.020  17.169 -23.921  1.00 42.63           O  
ANISOU 9100  O   GLY D 863     5526   5480   5192   -418    417   -401       O  
ATOM   9101  N   SER D 864    -117.401  15.554 -25.378  1.00 39.30           N  
ANISOU 9101  N   SER D 864     5127   5042   4763   -397    413   -481       N  
ATOM   9102  CA  SER D 864    -117.920  16.221 -26.570  1.00 40.90           C  
ANISOU 9102  CA  SER D 864     5289   5337   4915   -374    406   -501       C  
ATOM   9103  C   SER D 864    -118.062  15.185 -27.682  1.00 40.61           C  
ANISOU 9103  C   SER D 864     5249   5320   4860   -363    394   -585       C  
ATOM   9104  O   SER D 864    -117.476  14.126 -27.601  1.00 36.54           O  
ANISOU 9104  O   SER D 864     4765   4743   4377   -361    391   -620       O  
ATOM   9105  CB  SER D 864    -116.948  17.321 -27.004  1.00 41.89           C  
ANISOU 9105  CB  SER D 864     5393   5509   5015   -320    416   -441       C  
ATOM   9106  OG  SER D 864    -117.552  18.212 -27.905  1.00 44.39           O  
ANISOU 9106  OG  SER D 864     5664   5914   5287   -300    412   -431       O  
ATOM   9107  N   ARG D 865    -118.841  15.502 -28.709  1.00 41.94           N  
ANISOU 9107  N   ARG D 865     5378   5578   4980   -351    383   -623       N  
ATOM   9108  CA  ARG D 865    -119.009  14.606 -29.855  1.00 45.83           C  
ANISOU 9108  CA  ARG D 865     5855   6111   5446   -329    365   -719       C  
ATOM   9109  C   ARG D 865    -117.687  14.454 -30.570  1.00 46.56           C  
ANISOU 9109  C   ARG D 865     5949   6233   5507   -260    370   -720       C  
ATOM   9110  O   ARG D 865    -116.900  15.398 -30.653  1.00 47.79           O  
ANISOU 9110  O   ARG D 865     6092   6429   5635   -221    389   -641       O  
ATOM   9111  CB  ARG D 865    -120.039  15.126 -30.845  1.00 45.16           C  
ANISOU 9111  CB  ARG D 865     5718   6141   5299   -317    353   -753       C  
ATOM   9112  CG  ARG D 865    -121.470  15.051 -30.342  1.00 47.56           C  
ANISOU 9112  CG  ARG D 865     6012   6430   5627   -384    342   -777       C  
ATOM   9113  CD  ARG D 865    -122.366  15.896 -31.226  1.00 50.25           C  
ANISOU 9113  CD  ARG D 865     6298   6897   5899   -360    335   -784       C  
ATOM   9114  NE  ARG D 865    -123.672  16.110 -30.614  1.00 52.84           N  
ANISOU 9114  NE  ARG D 865     6612   7219   6243   -419    329   -785       N  
ATOM   9115  CZ  ARG D 865    -124.739  15.335 -30.802  1.00 56.39           C  
ANISOU 9115  CZ  ARG D 865     7044   7675   6707   -464    308   -869       C  
ATOM   9116  NH1 ARG D 865    -125.886  15.635 -30.199  1.00 55.73           N  
ANISOU 9116  NH1 ARG D 865     6943   7598   6635   -515    306   -856       N  
ATOM   9117  NH2 ARG D 865    -124.670  14.263 -31.579  1.00 57.91           N  
ANISOU 9117  NH2 ARG D 865     7230   7868   6906   -457    286   -970       N  
ATOM   9118  N   THR D 866    -117.455  13.247 -31.070  1.00 47.63           N  
ANISOU 9118  N   THR D 866     6096   6346   5655   -245    352   -813       N  
ATOM   9119  CA  THR D 866    -116.220  12.899 -31.761  1.00 47.31           C  
ANISOU 9119  CA  THR D 866     6055   6337   5582   -174    353   -833       C  
ATOM   9120  C   THR D 866    -115.902  13.846 -32.915  1.00 46.86           C  
ANISOU 9120  C   THR D 866     5942   6432   5429   -102    364   -800       C  
ATOM   9121  O   THR D 866    -114.746  14.211 -33.112  1.00 46.44           O  
ANISOU 9121  O   THR D 866     5883   6412   5349    -51    382   -743       O  
ATOM   9122  CB  THR D 866    -116.306  11.445 -32.238  1.00 48.85           C  
ANISOU 9122  CB  THR D 866     6262   6492   5807   -166    322   -963       C  
ATOM   9123  OG1 THR D 866    -116.578  10.626 -31.109  1.00 44.33           O  
ANISOU 9123  OG1 THR D 866     5738   5771   5335   -236    317   -967       O  
ATOM   9124  CG2 THR D 866    -115.001  10.980 -32.870  1.00 51.00           C  
ANISOU 9124  CG2 THR D 866     6536   6794   6049    -87    320   -994       C  
ATOM   9125  N   THR D 867    -116.942  14.256 -33.644  1.00 46.06           N  
ANISOU 9125  N   THR D 867     5796   6427   5277   -100    354   -828       N  
ATOM   9126  CA  THR D 867    -116.791  15.144 -34.788  1.00 48.51           C  
ANISOU 9126  CA  THR D 867     6044   6896   5492    -30    364   -788       C  
ATOM   9127  C   THR D 867    -116.358  16.560 -34.388  1.00 47.62           C  
ANISOU 9127  C   THR D 867     5919   6793   5381    -27    396   -640       C  
ATOM   9128  O   THR D 867    -116.100  17.389 -35.258  1.00 48.62           O  
ANISOU 9128  O   THR D 867     5992   7040   5441     30    410   -578       O  
ATOM   9129  CB  THR D 867    -118.089  15.190 -35.646  1.00 48.36           C  
ANISOU 9129  CB  THR D 867     5976   6981   5417    -25    343   -858       C  
ATOM   9130  OG1 THR D 867    -119.233  15.420 -34.795  1.00 47.26           O  
ANISOU 9130  OG1 THR D 867     5854   6771   5331   -104    338   -849       O  
ATOM   9131  CG2 THR D 867    -118.269  13.859 -36.396  1.00 50.13           C  
ANISOU 9131  CG2 THR D 867     6192   7230   5627      0    307  -1016       C  
ATOM   9132  N   ASN D 868    -116.292  16.848 -33.092  1.00 46.69           N  
ANISOU 9132  N   ASN D 868     5845   6554   5340    -86    404   -584       N  
ATOM   9133  CA  ASN D 868    -115.751  18.136 -32.619  1.00 44.67           C  
ANISOU 9133  CA  ASN D 868     5579   6289   5106    -84    426   -459       C  
ATOM   9134  C   ASN D 868    -114.263  18.132 -32.338  1.00 41.33           C  
ANISOU 9134  C   ASN D 868     5170   5829   4705    -57    443   -406       C  
ATOM   9135  O   ASN D 868    -113.695  19.179 -32.141  1.00 39.21           O  
ANISOU 9135  O   ASN D 868     4880   5563   4455    -48    459   -307       O  
ATOM   9136  CB  ASN D 868    -116.473  18.592 -31.353  1.00 41.85           C  
ANISOU 9136  CB  ASN D 868     5249   5838   4815   -151    423   -431       C  
ATOM   9137  CG  ASN D 868    -117.912  19.010 -31.615  1.00 41.67           C  
ANISOU 9137  CG  ASN D 868     5199   5868   4768   -172    411   -451       C  
ATOM   9138  OD1 ASN D 868    -118.250  19.516 -32.680  1.00 41.34           O  
ANISOU 9138  OD1 ASN D 868     5107   5937   4664   -130    412   -439       O  
ATOM   9139  ND2 ASN D 868    -118.768  18.802 -30.642  1.00 39.77           N  
ANISOU 9139  ND2 ASN D 868     4985   5557   4571   -233    401   -477       N  
ATOM   9140  N   PHE D 869    -113.642  16.961 -32.272  1.00 42.77           N  
ANISOU 9140  N   PHE D 869     5387   5970   4894    -46    437   -474       N  
ATOM   9141  CA  PHE D 869    -112.309  16.879 -31.679  1.00 43.57           C  
ANISOU 9141  CA  PHE D 869     5513   6013   5031    -34    450   -429       C  
ATOM   9142  C   PHE D 869    -111.171  17.418 -32.498  1.00 47.51           C  
ANISOU 9142  C   PHE D 869     5965   6605   5483     32    470   -363       C  
ATOM   9143  O   PHE D 869    -110.134  17.813 -31.942  1.00 45.79           O  
ANISOU 9143  O   PHE D 869     5752   6347   5301     35    484   -294       O  
ATOM   9144  CB  PHE D 869    -112.012  15.475 -31.194  1.00 44.42           C  
ANISOU 9144  CB  PHE D 869     5674   6030   5173    -45    438   -512       C  
ATOM   9145  CG  PHE D 869    -112.419  15.272 -29.770  1.00 42.89           C  
ANISOU 9145  CG  PHE D 869     5529   5711   5055   -113    435   -502       C  
ATOM   9146  CD1 PHE D 869    -113.730  14.958 -29.462  1.00 42.63           C  
ANISOU 9146  CD1 PHE D 869     5508   5645   5044   -167    420   -548       C  
ATOM   9147  CD2 PHE D 869    -111.522  15.486 -28.746  1.00 40.45           C  
ANISOU 9147  CD2 PHE D 869     5245   5333   4789   -120    447   -442       C  
ATOM   9148  CE1 PHE D 869    -114.129  14.804 -28.149  1.00 42.86           C  
ANISOU 9148  CE1 PHE D 869     5572   5577   5134   -225    421   -528       C  
ATOM   9149  CE2 PHE D 869    -111.910  15.334 -27.429  1.00 42.09           C  
ANISOU 9149  CE2 PHE D 869     5490   5448   5055   -174    445   -430       C  
ATOM   9150  CZ  PHE D 869    -113.218  14.988 -27.131  1.00 41.99           C  
ANISOU 9150  CZ  PHE D 869     5487   5407   5059   -225    433   -469       C  
ATOM   9151  N   ALA D 870    -111.349  17.486 -33.811  1.00 50.29           N  
ANISOU 9151  N   ALA D 870     6264   7091   5753     88    471   -378       N  
ATOM   9152  CA  ALA D 870    -110.345  18.151 -34.632  1.00 50.66           C  
ANISOU 9152  CA  ALA D 870     6251   7248   5750    151    494   -291       C  
ATOM   9153  C   ALA D 870    -110.335  19.636 -34.287  1.00 48.07           C  
ANISOU 9153  C   ALA D 870     5892   6907   5465    126    512   -157       C  
ATOM   9154  O   ALA D 870    -109.286  20.238 -34.175  1.00 45.30           O  
ANISOU 9154  O   ALA D 870     5516   6556   5138    140    530    -66       O  
ATOM   9155  CB  ALA D 870    -110.623  17.952 -36.121  1.00 51.42           C  
ANISOU 9155  CB  ALA D 870     6288   7512   5738    224    493   -331       C  
ATOM   9156  N   GLY D 871    -111.523  20.212 -34.126  1.00 47.73           N  
ANISOU 9156  N   GLY D 871     5845   6852   5437     89    502   -151       N  
ATOM   9157  CA  GLY D 871    -111.648  21.602 -33.720  1.00 48.54           C  
ANISOU 9157  CA  GLY D 871     5922   6925   5598     64    511    -39       C  
ATOM   9158  C   GLY D 871    -111.076  21.826 -32.316  1.00 44.55           C  
ANISOU 9158  C   GLY D 871     5460   6278   5191     14    507    -16       C  
ATOM   9159  O   GLY D 871    -110.313  22.750 -32.091  1.00 44.19           O  
ANISOU 9159  O   GLY D 871     5385   6211   5196     15    517     79       O  
ATOM   9160  N   ILE D 872    -111.435  20.964 -31.380  1.00 42.58           N  
ANISOU 9160  N   ILE D 872     5273   5936   4968    -28    491   -102       N  
ATOM   9161  CA  ILE D 872    -110.932  21.092 -30.004  1.00 41.94           C  
ANISOU 9161  CA  ILE D 872     5230   5739   4967    -67    486    -88       C  
ATOM   9162  C   ILE D 872    -109.421  20.950 -29.927  1.00 41.95           C  
ANISOU 9162  C   ILE D 872     5227   5731   4981    -39    499    -52       C  
ATOM   9163  O   ILE D 872    -108.762  21.729 -29.255  1.00 37.41           O  
ANISOU 9163  O   ILE D 872     4640   5107   4469    -52    500     10       O  
ATOM   9164  CB  ILE D 872    -111.573  20.055 -29.076  1.00 41.13           C  
ANISOU 9164  CB  ILE D 872     5191   5556   4881   -110    471   -177       C  
ATOM   9165  CG1 ILE D 872    -113.052  20.391 -28.893  1.00 41.73           C  
ANISOU 9165  CG1 ILE D 872     5265   5632   4959   -147    458   -200       C  
ATOM   9166  CG2 ILE D 872    -110.867  20.008 -27.723  1.00 39.29           C  
ANISOU 9166  CG2 ILE D 872     4993   5226   4712   -133    469   -164       C  
ATOM   9167  CD1 ILE D 872    -113.842  19.254 -28.308  1.00 42.78           C  
ANISOU 9167  CD1 ILE D 872     5446   5713   5096   -187    446   -285       C  
ATOM   9168  N   LEU D 873    -108.851  19.967 -30.613  1.00 43.35           N  
ANISOU 9168  N   LEU D 873     5410   5958   5102      3    507    -95       N  
ATOM   9169  CA  LEU D 873    -107.396  19.836 -30.578  1.00 44.42           C  
ANISOU 9169  CA  LEU D 873     5537   6098   5244     35    520    -59       C  
ATOM   9170  C   LEU D 873    -106.710  21.002 -31.264  1.00 44.31           C  
ANISOU 9170  C   LEU D 873     5448   6158   5230     63    539     55       C  
ATOM   9171  O   LEU D 873    -105.738  21.529 -30.743  1.00 43.74           O  
ANISOU 9171  O   LEU D 873     5359   6048   5213     57    545    117       O  
ATOM   9172  CB  LEU D 873    -106.941  18.505 -31.157  1.00 45.89           C  
ANISOU 9172  CB  LEU D 873     5743   6322   5371     81    520   -139       C  
ATOM   9173  CG  LEU D 873    -107.397  17.305 -30.310  1.00 43.18           C  
ANISOU 9173  CG  LEU D 873     5475   5876   5056     49    502   -237       C  
ATOM   9174  CD1 LEU D 873    -106.871  16.029 -30.955  1.00 46.14           C  
ANISOU 9174  CD1 LEU D 873     5864   6281   5385    101    497   -318       C  
ATOM   9175  CD2 LEU D 873    -106.911  17.408 -28.878  1.00 41.27           C  
ANISOU 9175  CD2 LEU D 873     5270   5525   4887     11    501   -209       C  
ATOM   9176  N   SER D 874    -107.221  21.447 -32.404  1.00 45.04           N  
ANISOU 9176  N   SER D 874     5489   6359   5268     93    548     90       N  
ATOM   9177  CA  SER D 874    -106.526  22.532 -33.084  1.00 45.88           C  
ANISOU 9177  CA  SER D 874     5515   6538   5378    121    570    219       C  
ATOM   9178  C   SER D 874    -106.782  23.886 -32.416  1.00 46.64           C  
ANISOU 9178  C   SER D 874     5591   6554   5577     73    563    304       C  
ATOM   9179  O   SER D 874    -105.893  24.736 -32.416  1.00 39.90           O  
ANISOU 9179  O   SER D 874     4686   5694   4779     74    574    406       O  
ATOM   9180  CB  SER D 874    -106.848  22.573 -34.569  1.00 47.34           C  
ANISOU 9180  CB  SER D 874     5641   6884   5463    181    585    245       C  
ATOM   9181  OG  SER D 874    -108.114  23.153 -34.766  1.00 50.07           O  
ANISOU 9181  OG  SER D 874     5976   7240   5808    163    576    253       O  
ATOM   9182  N   GLN D 875    -107.961  24.086 -31.807  1.00 43.97           N  
ANISOU 9182  N   GLN D 875     5287   6148   5269     31    542    258       N  
ATOM   9183  CA  GLN D 875    -108.278  25.399 -31.226  1.00 45.63           C  
ANISOU 9183  CA  GLN D 875     5474   6287   5577     -5    529    327       C  
ATOM   9184  C   GLN D 875    -108.505  25.448 -29.719  1.00 41.59           C  
ANISOU 9184  C   GLN D 875     5014   5645   5144    -56    503    268       C  
ATOM   9185  O   GLN D 875    -108.648  26.532 -29.168  1.00 39.75           O  
ANISOU 9185  O   GLN D 875     4758   5348   4998    -80    486    311       O  
ATOM   9186  CB  GLN D 875    -109.493  25.990 -31.922  1.00 50.16           C  
ANISOU 9186  CB  GLN D 875     6018   6917   6123      3    527    352       C  
ATOM   9187  CG  GLN D 875    -109.349  26.005 -33.430  1.00 56.01           C  
ANISOU 9187  CG  GLN D 875     6698   7808   6775     62    554    415       C  
ATOM   9188  CD  GLN D 875    -110.002  27.224 -34.037  1.00 66.48           C  
ANISOU 9188  CD  GLN D 875     7962   9175   8122     74    558    518       C  
ATOM   9189  OE1 GLN D 875    -111.006  27.141 -34.754  1.00 71.68           O  
ANISOU 9189  OE1 GLN D 875     8608   9919   8707     97    558    499       O  
ATOM   9190  NE2 GLN D 875    -109.438  28.385 -33.728  1.00 72.53           N  
ANISOU 9190  NE2 GLN D 875     8687   9875   8998     56    558    628       N  
ATOM   9191  N   GLY D 876    -108.531  24.296 -29.066  1.00 36.03           N  
ANISOU 9191  N   GLY D 876     4373   4905   4410    -68    496    172       N  
ATOM   9192  CA  GLY D 876    -108.736  24.249 -27.640  1.00 37.28           C  
ANISOU 9192  CA  GLY D 876     4576   4962   4627   -108    475    121       C  
ATOM   9193  C   GLY D 876    -110.207  24.387 -27.331  1.00 37.39           C  
ANISOU 9193  C   GLY D 876     4608   4962   4635   -135    458     77       C  
ATOM   9194  O   GLY D 876    -111.030  24.632 -28.211  1.00 36.43           O  
ANISOU 9194  O   GLY D 876     4464   4902   4474   -125    462     90       O  
ATOM   9195  N   LEU D 877    -110.542  24.200 -26.067  1.00 36.84           N  
ANISOU 9195  N   LEU D 877     4577   4822   4598   -166    440     25       N  
ATOM   9196  CA  LEU D 877    -111.907  24.408 -25.613  1.00 34.31           C  
ANISOU 9196  CA  LEU D 877     4268   4491   4277   -192    424    -14       C  
ATOM   9197  C   LEU D 877    -112.214  25.885 -25.650  1.00 34.72           C  
ANISOU 9197  C   LEU D 877     4271   4532   4390   -189    407     39       C  
ATOM   9198  O   LEU D 877    -111.376  26.715 -25.307  1.00 34.56           O  
ANISOU 9198  O   LEU D 877     4220   4468   4443   -184    398     84       O  
ATOM   9199  CB  LEU D 877    -112.082  23.875 -24.203  1.00 32.02           C  
ANISOU 9199  CB  LEU D 877     4021   4142   4003   -218    411    -71       C  
ATOM   9200  CG  LEU D 877    -111.962  22.373 -24.091  1.00 31.20           C  
ANISOU 9200  CG  LEU D 877     3967   4035   3853   -224    425   -120       C  
ATOM   9201  CD1 LEU D 877    -112.106  21.951 -22.638  1.00 31.46           C  
ANISOU 9201  CD1 LEU D 877     4032   4017   3904   -246    415   -154       C  
ATOM   9202  CD2 LEU D 877    -113.014  21.678 -24.958  1.00 32.94           C  
ANISOU 9202  CD2 LEU D 877     4198   4302   4015   -233    431   -159       C  
ATOM   9203  N   ARG D 878    -113.403  26.206 -26.123  1.00 35.06           N  
ANISOU 9203  N   ARG D 878     4302   4614   4407   -191    403     35       N  
ATOM   9204  CA  ARG D 878    -113.790  27.590 -26.330  1.00 37.67           C  
ANISOU 9204  CA  ARG D 878     4583   4937   4794   -182    388     91       C  
ATOM   9205  C   ARG D 878    -115.114  27.833 -25.650  1.00 33.58           C  
ANISOU 9205  C   ARG D 878     4075   4407   4275   -199    365     37       C  
ATOM   9206  O   ARG D 878    -115.762  26.926 -25.219  1.00 31.82           O  
ANISOU 9206  O   ARG D 878     3891   4197   4001   -220    366    -30       O  
ATOM   9207  CB  ARG D 878    -113.896  27.895 -27.826  1.00 40.24           C  
ANISOU 9207  CB  ARG D 878     4866   5346   5079   -151    408    162       C  
ATOM   9208  CG  ARG D 878    -112.565  28.104 -28.522  1.00 47.88           C  
ANISOU 9208  CG  ARG D 878     5797   6331   6065   -127    429    246       C  
ATOM   9209  CD  ARG D 878    -112.583  27.481 -29.920  1.00 54.30           C  
ANISOU 9209  CD  ARG D 878     6593   7263   6776    -92    458    267       C  
ATOM   9210  NE  ARG D 878    -112.720  26.022 -29.812  1.00 59.51           N  
ANISOU 9210  NE  ARG D 878     7309   7944   7359    -99    463    166       N  
ATOM   9211  CZ  ARG D 878    -113.302  25.203 -30.701  1.00 64.72           C  
ANISOU 9211  CZ  ARG D 878     7973   8692   7924    -79    472    119       C  
ATOM   9212  NH1 ARG D 878    -113.833  25.649 -31.833  1.00 67.28           N  
ANISOU 9212  NH1 ARG D 878     8249   9116   8198    -45    480    163       N  
ATOM   9213  NH2 ARG D 878    -113.355  23.901 -30.444  1.00 68.01           N  
ANISOU 9213  NH2 ARG D 878     8441   9097   8301    -92    470     24       N  
ATOM   9214  N   ILE D 879    -115.477  29.099 -25.559  1.00 34.85           N  
ANISOU 9214  N   ILE D 879     4196   4542   4502   -189    343     72       N  
ATOM   9215  CA  ILE D 879    -116.698  29.556 -24.931  1.00 34.42           C  
ANISOU 9215  CA  ILE D 879     4141   4482   4456   -195    317     25       C  
ATOM   9216  C   ILE D 879    -117.676  29.981 -26.049  1.00 38.60           C  
ANISOU 9216  C   ILE D 879     4640   5078   4947   -177    323     63       C  
ATOM   9217  O   ILE D 879    -117.264  30.508 -27.085  1.00 38.02           O  
ANISOU 9217  O   ILE D 879     4530   5030   4888   -152    337    147       O  
ATOM   9218  CB  ILE D 879    -116.380  30.759 -24.002  1.00 34.11           C  
ANISOU 9218  CB  ILE D 879     4072   4358   4529   -188    279     27       C  
ATOM   9219  CG1 ILE D 879    -115.558  30.292 -22.781  1.00 33.04           C  
ANISOU 9219  CG1 ILE D 879     3963   4175   4415   -201    269    -26       C  
ATOM   9220  CG2 ILE D 879    -117.646  31.478 -23.573  1.00 34.03           C  
ANISOU 9220  CG2 ILE D 879     4047   4351   4533   -179    249    -10       C  
ATOM   9221  CD1 ILE D 879    -115.003  31.440 -21.949  1.00 32.64           C  
ANISOU 9221  CD1 ILE D 879     3875   4044   4481   -189    229    -32       C  
ATOM   9222  N   ALA D 880    -118.963  29.718 -25.847  1.00 38.92           N  
ANISOU 9222  N   ALA D 880     4693   5159   4935   -186    315      5       N  
ATOM   9223  CA  ALA D 880    -119.997  30.064 -26.822  1.00 41.26           C  
ANISOU 9223  CA  ALA D 880     4961   5530   5187   -167    319     28       C  
ATOM   9224  C   ALA D 880    -119.928  31.526 -27.262  1.00 42.44           C  
ANISOU 9224  C   ALA D 880     5056   5654   5413   -132    305    114       C  
ATOM   9225  O   ALA D 880    -119.632  32.387 -26.437  1.00 40.65           O  
ANISOU 9225  O   ALA D 880     4818   5343   5285   -129    276    117       O  
ATOM   9226  CB  ALA D 880    -121.362  29.764 -26.226  1.00 39.51           C  
ANISOU 9226  CB  ALA D 880     4754   5338   4920   -185    304    -50       C  
ATOM   9227  N   PRO D 881    -120.219  31.803 -28.554  1.00 43.57           N  
ANISOU 9227  N   PRO D 881     5164   5874   5517   -101    322    183       N  
ATOM   9228  CA  PRO D 881    -120.127  33.180 -29.020  1.00 46.96           C  
ANISOU 9228  CA  PRO D 881     5537   6276   6028    -66    312    284       C  
ATOM   9229  C   PRO D 881    -121.229  34.073 -28.467  1.00 45.82           C  
ANISOU 9229  C   PRO D 881     5379   6101   5930    -54    276    257       C  
ATOM   9230  O   PRO D 881    -122.287  33.588 -28.084  1.00 47.88           O  
ANISOU 9230  O   PRO D 881     5663   6406   6124    -65    268    172       O  
ATOM   9231  CB  PRO D 881    -120.210  33.067 -30.562  1.00 47.68           C  
ANISOU 9231  CB  PRO D 881     5592   6485   6039    -30    345    365       C  
ATOM   9232  CG  PRO D 881    -120.817  31.742 -30.851  1.00 48.16           C  
ANISOU 9232  CG  PRO D 881     5688   6641   5971    -43    360    274       C  
ATOM   9233  CD  PRO D 881    -120.589  30.866 -29.634  1.00 47.33           C  
ANISOU 9233  CD  PRO D 881     5643   6467   5875    -92    350    172       C  
ATOM   9234  N   PRO D 882    -120.986  35.382 -28.437  1.00 49.38           N  
ANISOU 9234  N   PRO D 882     5787   6476   6500    -30    254    329       N  
ATOM   9235  CA  PRO D 882    -122.015  36.383 -28.055  1.00 50.07           C  
ANISOU 9235  CA  PRO D 882     5851   6531   6642     -5    216    312       C  
ATOM   9236  C   PRO D 882    -123.402  36.196 -28.733  1.00 48.41           C  
ANISOU 9236  C   PRO D 882     5632   6437   6323     18    225    298       C  
ATOM   9237  O   PRO D 882    -124.432  36.369 -28.093  1.00 45.68           O  
ANISOU 9237  O   PRO D 882     5293   6096   5966     23    198    223       O  
ATOM   9238  CB  PRO D 882    -121.396  37.717 -28.502  1.00 51.09           C  
ANISOU 9238  CB  PRO D 882     5923   6579   6911     23    204    435       C  
ATOM   9239  CG  PRO D 882    -119.931  37.463 -28.632  1.00 50.95           C  
ANISOU 9239  CG  PRO D 882     5903   6521   6935      0    225    491       C  
ATOM   9240  CD  PRO D 882    -119.738  36.001 -28.921  1.00 49.55           C  
ANISOU 9240  CD  PRO D 882     5771   6443   6615    -22    264    444       C  
ATOM   9241  N   GLU D 883    -123.408  35.823 -30.012  1.00 50.33           N  
ANISOU 9241  N   GLU D 883     5857   6784   6482     36    262    366       N  
ATOM   9242  CA  GLU D 883    -124.646  35.652 -30.790  1.00 52.50           C  
ANISOU 9242  CA  GLU D 883     6115   7184   6650     63    270    357       C  
ATOM   9243  C   GLU D 883    -125.488  34.447 -30.354  1.00 53.39           C  
ANISOU 9243  C   GLU D 883     6271   7363   6653     27    271    225       C  
ATOM   9244  O   GLU D 883    -126.702  34.396 -30.619  1.00 55.94           O  
ANISOU 9244  O   GLU D 883     6581   7769   6906     42    265    189       O  
ATOM   9245  CB  GLU D 883    -124.328  35.474 -32.269  1.00 57.20           C  
ANISOU 9245  CB  GLU D 883     6673   7889   7172     98    308    455       C  
ATOM   9246  CG  GLU D 883    -123.578  36.631 -32.908  1.00 62.24           C  
ANISOU 9246  CG  GLU D 883     7255   8487   7907    136    316    613       C  
ATOM   9247  CD  GLU D 883    -122.057  36.558 -32.772  1.00 66.58           C  
ANISOU 9247  CD  GLU D 883     7807   8962   8529    113    330    667       C  
ATOM   9248  OE1 GLU D 883    -121.418  37.600 -33.041  1.00 68.85           O  
ANISOU 9248  OE1 GLU D 883     8046   9184   8930    132    329    794       O  
ATOM   9249  OE2 GLU D 883    -121.502  35.483 -32.422  1.00 63.43           O  
ANISOU 9249  OE2 GLU D 883     7454   8568   8079     76    342    590       O  
ATOM   9250  N   ALA D 884    -124.860  33.478 -29.686  1.00 52.55           N  
ANISOU 9250  N   ALA D 884     6212   7220   6536    -20    279    159       N  
ATOM   9251  CA  ALA D 884    -125.577  32.294 -29.233  1.00 51.90           C  
ANISOU 9251  CA  ALA D 884     6167   7185   6368    -60    281     48       C  
ATOM   9252  C   ALA D 884    -126.507  32.639 -28.081  1.00 51.07           C  
ANISOU 9252  C   ALA D 884     6068   7049   6287    -71    250    -22       C  
ATOM   9253  O   ALA D 884    -126.168  33.455 -27.226  1.00 50.44           O  
ANISOU 9253  O   ALA D 884     5985   6878   6300    -62    224    -17       O  
ATOM   9254  CB  ALA D 884    -124.605  31.215 -28.799  1.00 52.55           C  
ANISOU 9254  CB  ALA D 884     6295   7227   6444   -102    297     10       C  
ATOM   9255  N   PRO D 885    -127.692  32.017 -28.057  1.00 51.55           N  
ANISOU 9255  N   PRO D 885     6131   7192   6265    -88    250    -92       N  
ATOM   9256  CA  PRO D 885    -128.545  32.176 -26.885  1.00 50.39           C  
ANISOU 9256  CA  PRO D 885     5987   7031   6127   -101    224   -161       C  
ATOM   9257  C   PRO D 885    -127.869  31.636 -25.644  1.00 45.52           C  
ANISOU 9257  C   PRO D 885     5409   6340   5545   -139    221   -207       C  
ATOM   9258  O   PRO D 885    -127.144  30.659 -25.724  1.00 45.52           O  
ANISOU 9258  O   PRO D 885     5441   6327   5526   -173    244   -212       O  
ATOM   9259  CB  PRO D 885    -129.809  31.349 -27.213  1.00 51.65           C  
ANISOU 9259  CB  PRO D 885     6139   7301   6185   -124    232   -221       C  
ATOM   9260  CG  PRO D 885    -129.630  30.801 -28.575  1.00 55.06           C  
ANISOU 9260  CG  PRO D 885     6563   7803   6556   -119    257   -194       C  
ATOM   9261  CD  PRO D 885    -128.232  31.062 -29.040  1.00 54.46           C  
ANISOU 9261  CD  PRO D 885     6494   7668   6528    -99    271   -117       C  
ATOM   9262  N   VAL D 886    -128.125  32.282 -24.518  1.00 45.74           N  
ANISOU 9262  N   VAL D 886     5430   6329   5621   -127    192   -242       N  
ATOM   9263  CA  VAL D 886    -127.614  31.850 -23.235  1.00 46.70           C  
ANISOU 9263  CA  VAL D 886     5578   6401   5764   -152    186   -289       C  
ATOM   9264  C   VAL D 886    -128.464  30.695 -22.672  1.00 48.11           C  
ANISOU 9264  C   VAL D 886     5771   6649   5860   -197    200   -349       C  
ATOM   9265  O   VAL D 886    -128.040  29.996 -21.761  1.00 41.05           O  
ANISOU 9265  O   VAL D 886     4902   5732   4964   -226    207   -376       O  
ATOM   9266  CB  VAL D 886    -127.600  33.022 -22.237  1.00 48.24           C  
ANISOU 9266  CB  VAL D 886     5749   6542   6037   -111    143   -314       C  
ATOM   9267  CG1 VAL D 886    -129.021  33.456 -21.875  1.00 47.91           C  
ANISOU 9267  CG1 VAL D 886     5676   6571   5958    -86    120   -362       C  
ATOM   9268  CG2 VAL D 886    -126.835  32.626 -20.975  1.00 50.95           C  
ANISOU 9268  CG2 VAL D 886     6115   6840   6404   -127    136   -356       C  
ATOM   9269  N   THR D 887    -129.676  30.513 -23.218  1.00 49.92           N  
ANISOU 9269  N   THR D 887     5978   6965   6023   -203    204   -366       N  
ATOM   9270  CA  THR D 887    -130.632  29.484 -22.765  1.00 46.12           C  
ANISOU 9270  CA  THR D 887     5498   6554   5473   -250    216   -417       C  
ATOM   9271  C   THR D 887    -129.974  28.123 -22.734  1.00 40.83           C  
ANISOU 9271  C   THR D 887     4868   5855   4789   -306    245   -420       C  
ATOM   9272  O   THR D 887    -129.265  27.723 -23.653  1.00 42.24           O  
ANISOU 9272  O   THR D 887     5066   6012   4971   -312    261   -395       O  
ATOM   9273  CB  THR D 887    -131.865  29.385 -23.687  1.00 51.60           C  
ANISOU 9273  CB  THR D 887     6160   7343   6102   -252    219   -430       C  
ATOM   9274  OG1 THR D 887    -132.873  28.525 -23.118  1.00 50.67           O  
ANISOU 9274  OG1 THR D 887     6031   7291   5931   -300    226   -478       O  
ATOM   9275  CG2 THR D 887    -131.494  28.827 -25.063  1.00 53.33           C  
ANISOU 9275  CG2 THR D 887     6389   7579   6297   -262    240   -406       C  
ATOM   9276  N   GLY D 888    -130.194  27.428 -21.644  1.00 37.16           N  
ANISOU 9276  N   GLY D 888     4411   5396   4311   -341    250   -448       N  
ATOM   9277  CA  GLY D 888    -129.564  26.143 -21.434  1.00 35.86           C  
ANISOU 9277  CA  GLY D 888     4284   5193   4147   -391    275   -446       C  
ATOM   9278  C   GLY D 888    -128.251  26.223 -20.681  1.00 34.34           C  
ANISOU 9278  C   GLY D 888     4122   4921   4004   -377    276   -425       C  
ATOM   9279  O   GLY D 888    -127.861  25.232 -20.102  1.00 36.18           O  
ANISOU 9279  O   GLY D 888     4380   5130   4236   -412    293   -424       O  
ATOM   9280  N   TYR D 889    -127.575  27.383 -20.693  1.00 34.72           N  
ANISOU 9280  N   TYR D 889     4163   4928   4100   -326    255   -408       N  
ATOM   9281  CA  TYR D 889    -126.365  27.599 -19.865  1.00 36.31           C  
ANISOU 9281  CA  TYR D 889     4383   5061   4353   -308    248   -398       C  
ATOM   9282  C   TYR D 889    -126.693  27.986 -18.419  1.00 36.15           C  
ANISOU 9282  C   TYR D 889     4340   5064   4332   -287    226   -434       C  
ATOM   9283  O   TYR D 889    -126.948  29.142 -18.090  1.00 37.09           O  
ANISOU 9283  O   TYR D 889     4426   5187   4479   -240    193   -456       O  
ATOM   9284  CB  TYR D 889    -125.473  28.682 -20.447  1.00 37.88           C  
ANISOU 9284  CB  TYR D 889     4575   5200   4619   -266    232   -365       C  
ATOM   9285  CG  TYR D 889    -124.698  28.210 -21.638  1.00 37.50           C  
ANISOU 9285  CG  TYR D 889     4548   5127   4571   -279    257   -322       C  
ATOM   9286  CD1 TYR D 889    -125.162  28.404 -22.937  1.00 38.49           C  
ANISOU 9286  CD1 TYR D 889     4658   5295   4672   -270    264   -297       C  
ATOM   9287  CD2 TYR D 889    -123.511  27.505 -21.455  1.00 39.71           C  
ANISOU 9287  CD2 TYR D 889     4863   5357   4869   -294    273   -308       C  
ATOM   9288  CE1 TYR D 889    -124.431  27.940 -24.032  1.00 38.51           C  
ANISOU 9288  CE1 TYR D 889     4674   5295   4663   -272    287   -262       C  
ATOM   9289  CE2 TYR D 889    -122.777  27.038 -22.531  1.00 36.65           C  
ANISOU 9289  CE2 TYR D 889     4492   4959   4475   -298    295   -275       C  
ATOM   9290  CZ  TYR D 889    -123.234  27.257 -23.824  1.00 37.93           C  
ANISOU 9290  CZ  TYR D 889     4633   5169   4608   -286    302   -253       C  
ATOM   9291  OH  TYR D 889    -122.482  26.764 -24.878  1.00 40.48           O  
ANISOU 9291  OH  TYR D 889     4967   5500   4915   -281    323   -224       O  
ATOM   9292  N   MET D 890    -126.706  26.982 -17.579  1.00 33.07           N  
ANISOU 9292  N   MET D 890     3963   4694   3908   -318    245   -440       N  
ATOM   9293  CA  MET D 890    -127.108  27.124 -16.200  1.00 35.16           C  
ANISOU 9293  CA  MET D 890     4200   5011   4149   -298    231   -469       C  
ATOM   9294  C   MET D 890    -126.285  28.161 -15.454  1.00 31.24           C  
ANISOU 9294  C   MET D 890     3690   4479   3703   -239    196   -495       C  
ATOM   9295  O   MET D 890    -126.811  28.847 -14.591  1.00 29.85           O  
ANISOU 9295  O   MET D 890     3473   4354   3514   -197    167   -539       O  
ATOM   9296  CB  MET D 890    -126.969  25.749 -15.535  1.00 38.49           C  
ANISOU 9296  CB  MET D 890     4642   5446   4536   -343    265   -446       C  
ATOM   9297  CG  MET D 890    -127.439  25.718 -14.120  1.00 43.35           C  
ANISOU 9297  CG  MET D 890     5221   6140   5108   -323    259   -460       C  
ATOM   9298  SD  MET D 890    -127.664  24.038 -13.503  1.00 45.66           S  
ANISOU 9298  SD  MET D 890     5526   6463   5362   -386    305   -408       S  
ATOM   9299  CE  MET D 890    -128.271  24.444 -11.865  1.00 44.57           C  
ANISOU 9299  CE  MET D 890     5325   6449   5162   -336    291   -425       C  
ATOM   9300  N   PHE D 891    -124.994  28.258 -15.770  1.00 28.95           N  
ANISOU 9300  N   PHE D 891     3426   4105   3470   -234    196   -474       N  
ATOM   9301  CA  PHE D 891    -124.119  29.211 -15.096  1.00 29.78           C  
ANISOU 9301  CA  PHE D 891     3513   4165   3636   -184    159   -503       C  
ATOM   9302  C   PHE D 891    -123.491  30.211 -16.054  1.00 29.66           C  
ANISOU 9302  C   PHE D 891     3495   4068   3708   -166    140   -482       C  
ATOM   9303  O   PHE D 891    -122.399  30.716 -15.813  1.00 27.22           O  
ANISOU 9303  O   PHE D 891     3181   3693   3467   -145    120   -485       O  
ATOM   9304  CB  PHE D 891    -123.074  28.457 -14.293  1.00 29.78           C  
ANISOU 9304  CB  PHE D 891     3535   4149   3631   -190    173   -496       C  
ATOM   9305  CG  PHE D 891    -123.682  27.570 -13.247  1.00 32.25           C  
ANISOU 9305  CG  PHE D 891     3841   4548   3865   -200    192   -502       C  
ATOM   9306  CD1 PHE D 891    -124.291  28.137 -12.132  1.00 32.27           C  
ANISOU 9306  CD1 PHE D 891     3794   4629   3836   -153    163   -554       C  
ATOM   9307  CD2 PHE D 891    -123.688  26.185 -13.381  1.00 31.14           C  
ANISOU 9307  CD2 PHE D 891     3735   4413   3684   -253    237   -454       C  
ATOM   9308  CE1 PHE D 891    -124.871  27.339 -11.156  1.00 33.27           C  
ANISOU 9308  CE1 PHE D 891     3904   4852   3884   -159    183   -546       C  
ATOM   9309  CE2 PHE D 891    -124.255  25.379 -12.398  1.00 33.40           C  
ANISOU 9309  CE2 PHE D 891     4007   4776   3907   -264    256   -442       C  
ATOM   9310  CZ  PHE D 891    -124.849  25.963 -11.283  1.00 32.75           C  
ANISOU 9310  CZ  PHE D 891     3872   4785   3786   -217    232   -482       C  
ATOM   9311  N   GLY D 892    -124.180  30.476 -17.163  1.00 28.84           N  
ANISOU 9311  N   GLY D 892     3387   3972   3599   -175    147   -455       N  
ATOM   9312  CA  GLY D 892    -123.654  31.374 -18.167  1.00 29.30           C  
ANISOU 9312  CA  GLY D 892     3436   3963   3734   -158    135   -413       C  
ATOM   9313  C   GLY D 892    -122.713  30.699 -19.137  1.00 30.31           C  
ANISOU 9313  C   GLY D 892     3597   4056   3864   -189    172   -351       C  
ATOM   9314  O   GLY D 892    -122.394  29.505 -19.038  1.00 29.99           O  
ANISOU 9314  O   GLY D 892     3592   4029   3774   -223    203   -347       O  
ATOM   9315  N   LYS D 893    -122.307  31.483 -20.127  1.00 33.33           N  
ANISOU 9315  N   LYS D 893     3963   4395   4306   -173    167   -298       N  
ATOM   9316  CA  LYS D 893    -121.407  31.033 -21.161  1.00 35.18           C  
ANISOU 9316  CA  LYS D 893     4215   4610   4542   -190    199   -233       C  
ATOM   9317  C   LYS D 893    -120.025  30.864 -20.563  1.00 33.87           C  
ANISOU 9317  C   LYS D 893     4063   4382   4425   -193    198   -231       C  
ATOM   9318  O   LYS D 893    -119.422  31.811 -20.145  1.00 35.53           O  
ANISOU 9318  O   LYS D 893     4245   4531   4723   -170    167   -231       O  
ATOM   9319  CB  LYS D 893    -121.406  32.019 -22.334  1.00 37.78           C  
ANISOU 9319  CB  LYS D 893     4510   4925   4919   -165    196   -163       C  
ATOM   9320  CG  LYS D 893    -122.716  32.044 -23.105  1.00 38.74           C  
ANISOU 9320  CG  LYS D 893     4620   5124   4977   -158    203   -159       C  
ATOM   9321  CD  LYS D 893    -122.713  33.143 -24.167  1.00 42.63           C  
ANISOU 9321  CD  LYS D 893     5071   5605   5523   -123    197    -79       C  
ATOM   9322  CE  LYS D 893    -124.074  33.313 -24.835  1.00 45.19           C  
ANISOU 9322  CE  LYS D 893     5375   6012   5785   -107    198    -79       C  
ATOM   9323  NZ  LYS D 893    -123.932  34.117 -26.070  1.00 50.71           N  
ANISOU 9323  NZ  LYS D 893     6035   6718   6514    -73    205     20       N  
ATOM   9324  N   GLY D 894    -119.548  29.632 -20.524  1.00 32.24           N  
ANISOU 9324  N   GLY D 894     3895   4190   4163   -220    229   -233       N  
ATOM   9325  CA  GLY D 894    -118.234  29.331 -20.018  1.00 30.23           C  
ANISOU 9325  CA  GLY D 894     3656   3888   3942   -222    232   -229       C  
ATOM   9326  C   GLY D 894    -117.840  27.953 -20.516  1.00 29.10           C  
ANISOU 9326  C   GLY D 894     3555   3766   3734   -248    273   -213       C  
ATOM   9327  O   GLY D 894    -118.530  27.386 -21.362  1.00 27.85           O  
ANISOU 9327  O   GLY D 894     3409   3653   3519   -263    293   -207       O  
ATOM   9328  N   ILE D 895    -116.743  27.410 -19.990  1.00 27.70           N  
ANISOU 9328  N   ILE D 895     3399   3558   3568   -250    280   -214       N  
ATOM   9329  CA  ILE D 895    -116.349  26.054 -20.290  1.00 28.94           C  
ANISOU 9329  CA  ILE D 895     3598   3725   3672   -270    314   -210       C  
ATOM   9330  C   ILE D 895    -116.695  25.239 -19.092  1.00 27.87           C  
ANISOU 9330  C   ILE D 895     3487   3600   3503   -284    315   -250       C  
ATOM   9331  O   ILE D 895    -116.262  25.559 -17.987  1.00 29.17           O  
ANISOU 9331  O   ILE D 895     3640   3749   3692   -267    297   -269       O  
ATOM   9332  CB  ILE D 895    -114.853  25.928 -20.574  1.00 30.49           C  
ANISOU 9332  CB  ILE D 895     3800   3886   3900   -257    324   -175       C  
ATOM   9333  CG1 ILE D 895    -114.442  26.910 -21.663  1.00 33.15           C  
ANISOU 9333  CG1 ILE D 895     4098   4217   4281   -240    322   -118       C  
ATOM   9334  CG2 ILE D 895    -114.512  24.515 -21.051  1.00 29.67           C  
ANISOU 9334  CG2 ILE D 895     3739   3794   3741   -270    356   -176       C  
ATOM   9335  CD1 ILE D 895    -112.933  27.072 -21.774  1.00 34.37           C  
ANISOU 9335  CD1 ILE D 895     4241   4337   4483   -227    327    -78       C  
ATOM   9336  N   TYR D 896    -117.442  24.160 -19.329  1.00 26.93           N  
ANISOU 9336  N   TYR D 896     3394   3509   3329   -314    337   -261       N  
ATOM   9337  CA  TYR D 896    -118.021  23.328 -18.295  1.00 26.75           C  
ANISOU 9337  CA  TYR D 896     3387   3503   3273   -334    343   -283       C  
ATOM   9338  C   TYR D 896    -117.259  21.997 -18.173  1.00 27.64           C  
ANISOU 9338  C   TYR D 896     3542   3585   3376   -348    368   -270       C  
ATOM   9339  O   TYR D 896    -116.918  21.360 -19.196  1.00 29.50           O  
ANISOU 9339  O   TYR D 896     3799   3802   3606   -356    384   -264       O  
ATOM   9340  CB  TYR D 896    -119.495  23.031 -18.649  1.00 27.92           C  
ANISOU 9340  CB  TYR D 896     3528   3698   3382   -365    348   -300       C  
ATOM   9341  CG  TYR D 896    -120.444  24.184 -18.431  1.00 27.21           C  
ANISOU 9341  CG  TYR D 896     3397   3649   3292   -349    323   -317       C  
ATOM   9342  CD1 TYR D 896    -120.338  25.346 -19.183  1.00 27.66           C  
ANISOU 9342  CD1 TYR D 896     3429   3699   3382   -322    305   -307       C  
ATOM   9343  CD2 TYR D 896    -121.440  24.119 -17.471  1.00 26.08           C  
ANISOU 9343  CD2 TYR D 896     3236   3555   3120   -358    317   -339       C  
ATOM   9344  CE1 TYR D 896    -121.205  26.404 -18.986  1.00 27.80           C  
ANISOU 9344  CE1 TYR D 896     3409   3745   3408   -303    279   -325       C  
ATOM   9345  CE2 TYR D 896    -122.307  25.179 -17.274  1.00 27.95           C  
ANISOU 9345  CE2 TYR D 896     3433   3832   3354   -336    291   -363       C  
ATOM   9346  CZ  TYR D 896    -122.187  26.314 -18.040  1.00 27.98           C  
ANISOU 9346  CZ  TYR D 896     3417   3817   3396   -308    271   -359       C  
ATOM   9347  OH  TYR D 896    -123.007  27.384 -17.830  1.00 32.27           O  
ANISOU 9347  OH  TYR D 896     3921   4392   3948   -280    242   -384       O  
ATOM   9348  N   PHE D 897    -117.041  21.559 -16.932  1.00 26.36           N  
ANISOU 9348  N   PHE D 897     3386   3422   3208   -344    370   -269       N  
ATOM   9349  CA  PHE D 897    -116.319  20.324 -16.604  1.00 25.64           C  
ANISOU 9349  CA  PHE D 897     3332   3298   3113   -350    392   -250       C  
ATOM   9350  C   PHE D 897    -117.021  19.590 -15.482  1.00 26.75           C  
ANISOU 9350  C   PHE D 897     3472   3465   3228   -368    402   -238       C  
ATOM   9351  O   PHE D 897    -117.694  20.205 -14.660  1.00 24.09           O  
ANISOU 9351  O   PHE D 897     3101   3180   2872   -359    389   -247       O  
ATOM   9352  CB  PHE D 897    -114.909  20.606 -16.109  1.00 26.31           C  
ANISOU 9352  CB  PHE D 897     3417   3358   3220   -311    386   -240       C  
ATOM   9353  CG  PHE D 897    -114.031  21.332 -17.100  1.00 27.74           C  
ANISOU 9353  CG  PHE D 897     3590   3515   3433   -292    378   -235       C  
ATOM   9354  CD1 PHE D 897    -114.043  22.711 -17.170  1.00 28.11           C  
ANISOU 9354  CD1 PHE D 897     3597   3570   3513   -274    353   -243       C  
ATOM   9355  CD2 PHE D 897    -113.169  20.622 -17.923  1.00 28.23           C  
ANISOU 9355  CD2 PHE D 897     3680   3548   3497   -289    396   -220       C  
ATOM   9356  CE1 PHE D 897    -113.243  23.375 -18.085  1.00 30.75           C  
ANISOU 9356  CE1 PHE D 897     3915   3882   3884   -260    349   -221       C  
ATOM   9357  CE2 PHE D 897    -112.363  21.261 -18.827  1.00 29.40           C  
ANISOU 9357  CE2 PHE D 897     3812   3690   3668   -269    394   -205       C  
ATOM   9358  CZ  PHE D 897    -112.394  22.648 -18.909  1.00 32.34           C  
ANISOU 9358  CZ  PHE D 897     4142   4070   4077   -258    372   -198       C  
ATOM   9359  N   ALA D 898    -116.820  18.272 -15.430  1.00 27.84           N  
ANISOU 9359  N   ALA D 898     3643   3566   3369   -390    426   -214       N  
ATOM   9360  CA  ALA D 898    -117.373  17.431 -14.367  1.00 28.87           C  
ANISOU 9360  CA  ALA D 898     3770   3714   3484   -409    441   -180       C  
ATOM   9361  C   ALA D 898    -116.257  16.726 -13.611  1.00 28.87           C  
ANISOU 9361  C   ALA D 898     3793   3686   3491   -382    455   -144       C  
ATOM   9362  O   ALA D 898    -115.166  16.534 -14.157  1.00 29.96           O  
ANISOU 9362  O   ALA D 898     3959   3773   3651   -362    455   -149       O  
ATOM   9363  CB  ALA D 898    -118.275  16.380 -14.985  1.00 29.81           C  
ANISOU 9363  CB  ALA D 898     3905   3804   3617   -466    457   -176       C  
ATOM   9364  N   ASP D 899    -116.518  16.377 -12.362  1.00 27.45           N  
ANISOU 9364  N   ASP D 899     3594   3548   3287   -375    465   -103       N  
ATOM   9365  CA  ASP D 899    -115.645  15.474 -11.629  1.00 31.43           C  
ANISOU 9365  CA  ASP D 899     4118   4028   3795   -352    483    -53       C  
ATOM   9366  C   ASP D 899    -116.165  14.026 -11.639  1.00 32.66           C  
ANISOU 9366  C   ASP D 899     4296   4132   3980   -400    510      1       C  
ATOM   9367  O   ASP D 899    -115.496  13.125 -11.105  1.00 34.95           O  
ANISOU 9367  O   ASP D 899     4606   4389   4286   -384    528     53       O  
ATOM   9368  CB  ASP D 899    -115.335  15.945 -10.176  1.00 31.47           C  
ANISOU 9368  CB  ASP D 899     4085   4119   3755   -299    478    -33       C  
ATOM   9369  CG  ASP D 899    -116.562  16.172  -9.324  1.00 33.10           C  
ANISOU 9369  CG  ASP D 899     4242   4418   3916   -307    480    -16       C  
ATOM   9370  OD1 ASP D 899    -117.650  15.587  -9.599  1.00 35.88           O  
ANISOU 9370  OD1 ASP D 899     4593   4763   4278   -362    497     11       O  
ATOM   9371  OD2 ASP D 899    -116.431  16.930  -8.335  1.00 31.22           O  
ANISOU 9371  OD2 ASP D 899     3961   4269   3632   -255    464    -32       O  
ATOM   9372  N   MET D 900    -117.326  13.814 -12.254  1.00 33.45           N  
ANISOU 9372  N   MET D 900     4390   4223   4096   -456    512    -12       N  
ATOM   9373  CA  MET D 900    -117.855  12.467 -12.483  1.00 34.66           C  
ANISOU 9373  CA  MET D 900     4560   4308   4301   -511    530     24       C  
ATOM   9374  C   MET D 900    -117.741  12.143 -13.963  1.00 34.30           C  
ANISOU 9374  C   MET D 900     4549   4184   4298   -535    518    -39       C  
ATOM   9375  O   MET D 900    -118.374  12.800 -14.795  1.00 32.68           O  
ANISOU 9375  O   MET D 900     4331   4007   4079   -552    503    -95       O  
ATOM   9376  CB  MET D 900    -119.326  12.385 -12.047  1.00 37.65           C  
ANISOU 9376  CB  MET D 900     4895   4742   4668   -561    539     54       C  
ATOM   9377  CG  MET D 900    -119.589  12.744 -10.582  1.00 43.64           C  
ANISOU 9377  CG  MET D 900     5606   5606   5368   -531    551    114       C  
ATOM   9378  SD  MET D 900    -119.062  11.460  -9.475  1.00 49.60           S  
ANISOU 9378  SD  MET D 900     6366   6336   6146   -521    584    230       S  
ATOM   9379  CE  MET D 900    -119.625  12.041  -7.891  1.00 59.12           C  
ANISOU 9379  CE  MET D 900     7497   7705   7259   -481    595    290       C  
ATOM   9380  N   VAL D 901    -116.993  11.095 -14.298  1.00 35.08           N  
ANISOU 9380  N   VAL D 901     4689   4193   4449   -533    524    -32       N  
ATOM   9381  CA  VAL D 901    -116.751  10.746 -15.697  1.00 34.87           C  
ANISOU 9381  CA  VAL D 901     4690   4103   4455   -541    509   -103       C  
ATOM   9382  C   VAL D 901    -118.029  10.621 -16.523  1.00 36.43           C  
ANISOU 9382  C   VAL D 901     4870   4302   4671   -599    498   -150       C  
ATOM   9383  O   VAL D 901    -118.084  11.067 -17.661  1.00 40.27           O  
ANISOU 9383  O   VAL D 901     5356   4804   5140   -592    482   -220       O  
ATOM   9384  CB  VAL D 901    -115.889   9.478 -15.837  1.00 37.32           C  
ANISOU 9384  CB  VAL D 901     5043   4312   4826   -529    514    -92       C  
ATOM   9385  CG1 VAL D 901    -116.605   8.227 -15.342  1.00 38.87           C  
ANISOU 9385  CG1 VAL D 901     5238   4438   5095   -583    526    -40       C  
ATOM   9386  CG2 VAL D 901    -115.447   9.274 -17.274  1.00 37.84           C  
ANISOU 9386  CG2 VAL D 901     5133   4338   4909   -515    495   -177       C  
ATOM   9387  N   SER D 902    -119.069  10.039 -15.951  1.00 37.53           N  
ANISOU 9387  N   SER D 902     4986   4435   4840   -654    508   -109       N  
ATOM   9388  CA  SER D 902    -120.303   9.788 -16.692  1.00 37.84           C  
ANISOU 9388  CA  SER D 902     5002   4471   4905   -715    497   -155       C  
ATOM   9389  C   SER D 902    -121.064  11.061 -17.023  1.00 34.18           C  
ANISOU 9389  C   SER D 902     4503   4110   4372   -712    486   -193       C  
ATOM   9390  O   SER D 902    -121.667  11.164 -18.081  1.00 36.94           O  
ANISOU 9390  O   SER D 902     4843   4471   4722   -733    469   -261       O  
ATOM   9391  CB  SER D 902    -121.192   8.791 -15.927  1.00 39.85           C  
ANISOU 9391  CB  SER D 902     5234   4688   5221   -779    512    -88       C  
ATOM   9392  OG  SER D 902    -121.556   9.273 -14.651  1.00 40.36           O  
ANISOU 9392  OG  SER D 902     5263   4834   5237   -774    534     -5       O  
ATOM   9393  N   LYS D 903    -121.016  12.046 -16.142  1.00 34.52           N  
ANISOU 9393  N   LYS D 903     4526   4233   4357   -680    493   -155       N  
ATOM   9394  CA  LYS D 903    -121.657  13.343 -16.416  1.00 33.16           C  
ANISOU 9394  CA  LYS D 903     4320   4151   4126   -667    479   -191       C  
ATOM   9395  C   LYS D 903    -121.083  13.956 -17.689  1.00 32.67           C  
ANISOU 9395  C   LYS D 903     4277   4086   4051   -633    461   -256       C  
ATOM   9396  O   LYS D 903    -121.832  14.467 -18.520  1.00 34.42           O  
ANISOU 9396  O   LYS D 903     4476   4349   4251   -644    448   -301       O  
ATOM   9397  CB  LYS D 903    -121.491  14.303 -15.239  1.00 31.67           C  
ANISOU 9397  CB  LYS D 903     4108   4038   3886   -625    482   -152       C  
ATOM   9398  CG  LYS D 903    -122.205  15.629 -15.445  1.00 31.50           C  
ANISOU 9398  CG  LYS D 903     4050   4101   3818   -609    464   -191       C  
ATOM   9399  CD  LYS D 903    -122.475  16.344 -14.116  1.00 31.05           C  
ANISOU 9399  CD  LYS D 903     3954   4127   3715   -579    464   -160       C  
ATOM   9400  CE  LYS D 903    -123.298  17.605 -14.322  1.00 31.10           C  
ANISOU 9400  CE  LYS D 903     3922   4210   3684   -563    442   -203       C  
ATOM   9401  NZ  LYS D 903    -123.381  18.433 -13.084  1.00 34.72           N  
ANISOU 9401  NZ  LYS D 903     4341   4751   4099   -516    433   -195       N  
ATOM   9402  N   SER D 904    -119.765  13.862 -17.857  1.00 30.56           N  
ANISOU 9402  N   SER D 904     4043   3775   3793   -591    462   -254       N  
ATOM   9403  CA  SER D 904    -119.111  14.334 -19.065  1.00 32.53           C  
ANISOU 9403  CA  SER D 904     4304   4026   4029   -556    450   -302       C  
ATOM   9404  C   SER D 904    -119.262  13.378 -20.246  1.00 32.99           C  
ANISOU 9404  C   SER D 904     4377   4043   4114   -576    443   -358       C  
ATOM   9405  O   SER D 904    -119.501  13.820 -21.356  1.00 33.26           O  
ANISOU 9405  O   SER D 904     4397   4119   4122   -564    430   -406       O  
ATOM   9406  CB  SER D 904    -117.625  14.630 -18.817  1.00 33.24           C  
ANISOU 9406  CB  SER D 904     4416   4096   4117   -501    454   -279       C  
ATOM   9407  OG  SER D 904    -117.483  15.856 -18.122  1.00 31.07           O  
ANISOU 9407  OG  SER D 904     4116   3873   3815   -473    449   -256       O  
ATOM   9408  N   ALA D 905    -119.161  12.079 -19.993  1.00 34.37           N  
ANISOU 9408  N   ALA D 905     4576   4140   4345   -602    448   -353       N  
ATOM   9409  CA  ALA D 905    -119.331  11.076 -21.047  1.00 37.02           C  
ANISOU 9409  CA  ALA D 905     4921   4425   4720   -621    433   -422       C  
ATOM   9410  C   ALA D 905    -120.702  11.150 -21.729  1.00 37.11           C  
ANISOU 9410  C   ALA D 905     4896   4480   4724   -666    418   -475       C  
ATOM   9411  O   ALA D 905    -120.809  10.851 -22.902  1.00 38.31           O  
ANISOU 9411  O   ALA D 905     5042   4637   4875   -659    399   -553       O  
ATOM   9412  CB  ALA D 905    -119.112   9.680 -20.485  1.00 38.84           C  
ANISOU 9412  CB  ALA D 905     5178   4549   5030   -648    439   -400       C  
ATOM   9413  N   ASN D 906    -121.735  11.562 -21.002  1.00 37.74           N  
ANISOU 9413  N   ASN D 906     4945   4602   4792   -705    426   -437       N  
ATOM   9414  CA  ASN D 906    -123.042  11.764 -21.616  1.00 38.49           C  
ANISOU 9414  CA  ASN D 906     5000   4754   4872   -743    412   -485       C  
ATOM   9415  C   ASN D 906    -123.001  12.738 -22.786  1.00 40.47           C  
ANISOU 9415  C   ASN D 906     5234   5085   5056   -697    398   -538       C  
ATOM   9416  O   ASN D 906    -123.778  12.593 -23.730  1.00 43.16           O  
ANISOU 9416  O   ASN D 906     5549   5462   5388   -714    380   -605       O  
ATOM   9417  CB  ASN D 906    -124.078  12.247 -20.596  1.00 36.76           C  
ANISOU 9417  CB  ASN D 906     4744   4587   4635   -780    423   -430       C  
ATOM   9418  CG  ASN D 906    -124.499  11.154 -19.623  1.00 37.53           C  
ANISOU 9418  CG  ASN D 906     4837   4622   4799   -839    438   -376       C  
ATOM   9419  OD1 ASN D 906    -124.286   9.964 -19.868  1.00 37.96           O  
ANISOU 9419  OD1 ASN D 906     4910   4582   4930   -868    433   -393       O  
ATOM   9420  ND2 ASN D 906    -125.071  11.557 -18.501  1.00 36.03           N  
ANISOU 9420  ND2 ASN D 906     4618   4486   4585   -854    454   -308       N  
ATOM   9421  N   TYR D 907    -122.099  13.718 -22.731  1.00 40.04           N  
ANISOU 9421  N   TYR D 907     5191   5062   4960   -639    405   -504       N  
ATOM   9422  CA  TYR D 907    -121.974  14.721 -23.801  1.00 38.20           C  
ANISOU 9422  CA  TYR D 907     4938   4905   4670   -592    396   -530       C  
ATOM   9423  C   TYR D 907    -121.169  14.217 -24.989  1.00 39.53           C  
ANISOU 9423  C   TYR D 907     5120   5068   4832   -553    387   -582       C  
ATOM   9424  O   TYR D 907    -121.016  14.932 -25.976  1.00 40.26           O  
ANISOU 9424  O   TYR D 907     5190   5232   4873   -509    382   -596       O  
ATOM   9425  CB  TYR D 907    -121.390  16.024 -23.252  1.00 35.88           C  
ANISOU 9425  CB  TYR D 907     4641   4642   4350   -550    404   -468       C  
ATOM   9426  CG  TYR D 907    -122.360  16.711 -22.307  1.00 35.92           C  
ANISOU 9426  CG  TYR D 907     4619   4683   4344   -574    404   -439       C  
ATOM   9427  CD1 TYR D 907    -123.477  17.377 -22.801  1.00 33.75           C  
ANISOU 9427  CD1 TYR D 907     4306   4481   4035   -581    393   -461       C  
ATOM   9428  CD2 TYR D 907    -122.200  16.640 -20.928  1.00 34.80           C  
ANISOU 9428  CD2 TYR D 907     4487   4514   4222   -585    414   -392       C  
ATOM   9429  CE1 TYR D 907    -124.376  17.984 -21.960  1.00 32.97           C  
ANISOU 9429  CE1 TYR D 907     4179   4423   3924   -596    391   -440       C  
ATOM   9430  CE2 TYR D 907    -123.108  17.244 -20.071  1.00 33.64           C  
ANISOU 9430  CE2 TYR D 907     4309   4418   4057   -598    412   -372       C  
ATOM   9431  CZ  TYR D 907    -124.184  17.918 -20.599  1.00 34.11           C  
ANISOU 9431  CZ  TYR D 907     4332   4545   4085   -603    400   -398       C  
ATOM   9432  OH  TYR D 907    -125.099  18.504 -19.768  1.00 36.53           O  
ANISOU 9432  OH  TYR D 907     4604   4907   4370   -611    397   -384       O  
ATOM   9433  N   CYS D 908    -120.705  12.969 -24.943  1.00 40.88           N  
ANISOU 9433  N   CYS D 908     5321   5158   5055   -566    385   -611       N  
ATOM   9434  CA  CYS D 908    -120.148  12.346 -26.147  1.00 43.09           C  
ANISOU 9434  CA  CYS D 908     5606   5441   5327   -528    370   -685       C  
ATOM   9435  C   CYS D 908    -121.230  12.001 -27.174  1.00 42.96           C  
ANISOU 9435  C   CYS D 908     5552   5474   5297   -547    345   -775       C  
ATOM   9436  O   CYS D 908    -120.938  11.934 -28.369  1.00 43.96           O  
ANISOU 9436  O   CYS D 908     5662   5658   5382   -498    331   -840       O  
ATOM   9437  CB  CYS D 908    -119.361  11.094 -25.787  1.00 44.28           C  
ANISOU 9437  CB  CYS D 908     5797   5483   5544   -531    369   -698       C  
ATOM   9438  SG  CYS D 908    -117.903  11.404 -24.750  1.00 42.54           S  
ANISOU 9438  SG  CYS D 908     5617   5218   5330   -493    394   -605       S  
ATOM   9439  N   HIS D 909    -122.462  11.784 -26.691  1.00 47.18           N  
ANISOU 9439  N   HIS D 909     6067   5995   5862   -614    340   -780       N  
ATOM   9440  CA  HIS D 909    -123.625  11.395 -27.513  1.00 49.76           C  
ANISOU 9440  CA  HIS D 909     6353   6365   6189   -644    315   -869       C  
ATOM   9441  C   HIS D 909    -123.317  10.142 -28.335  1.00 50.21           C  
ANISOU 9441  C   HIS D 909     6417   6371   6291   -636    286   -975       C  
ATOM   9442  O   HIS D 909    -123.525  10.096 -29.530  1.00 49.61           O  
ANISOU 9442  O   HIS D 909     6308   6369   6171   -601    262  -1065       O  
ATOM   9443  CB  HIS D 909    -124.106  12.558 -28.400  1.00 49.79           C  
ANISOU 9443  CB  HIS D 909     6314   6506   6098   -603    311   -880       C  
ATOM   9444  CG  HIS D 909    -124.715  13.687 -27.616  1.00 54.38           C  
ANISOU 9444  CG  HIS D 909     6880   7129   6651   -620    328   -799       C  
ATOM   9445  ND1 HIS D 909    -124.146  14.947 -27.529  1.00 51.08           N  
ANISOU 9445  ND1 HIS D 909     6464   6760   6183   -568    344   -728       N  
ATOM   9446  CD2 HIS D 909    -125.828  13.728 -26.848  1.00 54.77           C  
ANISOU 9446  CD2 HIS D 909     6911   7178   6721   -680    330   -780       C  
ATOM   9447  CE1 HIS D 909    -124.898  15.716 -26.765  1.00 50.42           C  
ANISOU 9447  CE1 HIS D 909     6364   6701   6092   -592    351   -680       C  
ATOM   9448  NE2 HIS D 909    -125.920  14.999 -26.333  1.00 52.10           N  
ANISOU 9448  NE2 HIS D 909     6564   6891   6340   -657    344   -708       N  
ATOM   9449  N   THR D 910    -122.766   9.143 -27.672  1.00 49.59           N  
ANISOU 9449  N   THR D 910     6377   6168   6299   -659    288   -963       N  
ATOM   9450  CA  THR D 910    -122.530   7.867 -28.315  1.00 50.43           C  
ANISOU 9450  CA  THR D 910     6489   6201   6472   -656    256  -1068       C  
ATOM   9451  C   THR D 910    -123.848   7.077 -28.341  1.00 53.21           C  
ANISOU 9451  C   THR D 910     6805   6509   6902   -737    229  -1132       C  
ATOM   9452  O   THR D 910    -124.819   7.485 -27.736  1.00 50.00           O  
ANISOU 9452  O   THR D 910     6376   6126   6496   -795    243  -1079       O  
ATOM   9453  CB  THR D 910    -121.428   7.080 -27.586  1.00 47.09           C  
ANISOU 9453  CB  THR D 910     6120   5652   6122   -647    267  -1025       C  
ATOM   9454  OG1 THR D 910    -121.711   7.034 -26.183  1.00 44.38           O  
ANISOU 9454  OG1 THR D 910     5792   5238   5832   -708    294   -915       O  
ATOM   9455  CG2 THR D 910    -120.088   7.725 -27.827  1.00 47.34           C  
ANISOU 9455  CG2 THR D 910     6176   5735   6078   -561    284   -991       C  
ATOM   9456  N   SER D 911    -123.858   5.941 -29.027  1.00 57.45           N  
ANISOU 9456  N   SER D 911     7335   6981   7511   -740    190  -1250       N  
ATOM   9457  CA  SER D 911    -125.043   5.079 -29.114  1.00 60.10           C  
ANISOU 9457  CA  SER D 911     7632   7260   7944   -821    157  -1324       C  
ATOM   9458  C   SER D 911    -124.600   3.648 -29.373  1.00 63.61           C  
ANISOU 9458  C   SER D 911     8092   7562   8514   -825    120  -1417       C  
ATOM   9459  O   SER D 911    -123.420   3.398 -29.589  1.00 66.47           O  
ANISOU 9459  O   SER D 911     8493   7894   8868   -756    118  -1433       O  
ATOM   9460  CB  SER D 911    -125.973   5.571 -30.238  1.00 59.18           C  
ANISOU 9460  CB  SER D 911     7454   7285   7749   -807    130  -1427       C  
ATOM   9461  OG  SER D 911    -125.268   5.634 -31.466  1.00 58.30           O  
ANISOU 9461  OG  SER D 911     7335   7254   7561   -712    106  -1528       O  
ATOM   9462  N   GLN D 912    -125.547   2.716 -29.396  1.00 70.30           N  
ANISOU 9462  N   GLN D 912     8905   8324   9482   -903     86  -1485       N  
ATOM   9463  CA  GLN D 912    -125.226   1.315 -29.673  1.00 74.73           C  
ANISOU 9463  CA  GLN D 912     9474   8734  10186   -912     41  -1586       C  
ATOM   9464  C   GLN D 912    -124.611   1.134 -31.061  1.00 72.95           C  
ANISOU 9464  C   GLN D 912     9238   8575   9903   -813     -4  -1752       C  
ATOM   9465  O   GLN D 912    -123.680   0.351 -31.236  1.00 70.41           O  
ANISOU 9465  O   GLN D 912     8949   8163   9642   -766    -25  -1805       O  
ATOM   9466  CB  GLN D 912    -126.469   0.447 -29.524  1.00 81.19           C  
ANISOU 9466  CB  GLN D 912    10242   9456  11150  -1020      8  -1633       C  
ATOM   9467  CG  GLN D 912    -126.885   0.243 -28.084  1.00 86.09           C  
ANISOU 9467  CG  GLN D 912    10874   9975  11863  -1115     49  -1466       C  
ATOM   9468  CD  GLN D 912    -128.115   1.063 -27.719  1.00 89.66           C  
ANISOU 9468  CD  GLN D 912    11277  10537  12252  -1178     74  -1400       C  
ATOM   9469  OE1 GLN D 912    -127.990   2.222 -27.318  1.00 85.51           O  
ANISOU 9469  OE1 GLN D 912    10766  10130  11594  -1145    118  -1303       O  
ATOM   9470  NE2 GLN D 912    -129.307   0.466 -27.858  1.00 87.82           N  
ANISOU 9470  NE2 GLN D 912    10982  10265  12122  -1267     43  -1458       N  
ATOM   9471  N   GLY D 913    -125.108   1.898 -32.028  1.00 72.13           N  
ANISOU 9471  N   GLY D 913     9087   8645   9675   -773    -17  -1827       N  
ATOM   9472  CA  GLY D 913    -124.568   1.907 -33.381  1.00 72.08           C  
ANISOU 9472  CA  GLY D 913     9058   8749   9579   -667    -53  -1972       C  
ATOM   9473  C   GLY D 913    -123.215   2.577 -33.549  1.00 75.57           C  
ANISOU 9473  C   GLY D 913     9541   9270   9902   -563    -19  -1909       C  
ATOM   9474  O   GLY D 913    -122.486   2.231 -34.485  1.00 69.76           O  
ANISOU 9474  O   GLY D 913     8797   8581   9127   -473    -50  -2022       O  
ATOM   9475  N   ASP D 914    -122.890   3.540 -32.669  1.00 76.42           N  
ANISOU 9475  N   ASP D 914     9684   9401   9951   -573     41  -1736       N  
ATOM   9476  CA  ASP D 914    -121.544   4.138 -32.588  1.00 76.48           C  
ANISOU 9476  CA  ASP D 914     9733   9453   9873   -491     77  -1654       C  
ATOM   9477  C   ASP D 914    -121.108   4.317 -31.107  1.00 74.25           C  
ANISOU 9477  C   ASP D 914     9507   9062   9642   -539    125  -1487       C  
ATOM   9478  O   ASP D 914    -121.228   5.411 -30.527  1.00 71.66           O  
ANISOU 9478  O   ASP D 914     9184   8798   9246   -552    166  -1366       O  
ATOM   9479  CB  ASP D 914    -121.483   5.470 -33.346  1.00 76.18           C  
ANISOU 9479  CB  ASP D 914     9660   9615   9668   -423     98  -1626       C  
ATOM   9480  CG  ASP D 914    -120.042   5.904 -33.647  1.00 77.60           C  
ANISOU 9480  CG  ASP D 914     9864   9856   9765   -326    121  -1583       C  
ATOM   9481  OD1 ASP D 914    -119.857   6.808 -34.489  1.00 78.58           O  
ANISOU 9481  OD1 ASP D 914     9951  10144   9761   -257    131  -1576       O  
ATOM   9482  OD2 ASP D 914    -119.085   5.324 -33.064  1.00 79.13           O  
ANISOU 9482  OD2 ASP D 914    10107   9937  10021   -316    129  -1552       O  
ATOM   9483  N   PRO D 915    -120.584   3.238 -30.499  1.00 70.13           N  
ANISOU 9483  N   PRO D 915     9026   8379   9242   -558    117  -1484       N  
ATOM   9484  CA  PRO D 915    -120.343   3.183 -29.067  1.00 64.11           C  
ANISOU 9484  CA  PRO D 915     8308   7508   8544   -610    156  -1336       C  
ATOM   9485  C   PRO D 915    -118.929   3.609 -28.621  1.00 62.72           C  
ANISOU 9485  C   PRO D 915     8179   7340   8312   -542    191  -1246       C  
ATOM   9486  O   PRO D 915    -118.570   3.407 -27.460  1.00 61.49           O  
ANISOU 9486  O   PRO D 915     8060   7092   8212   -570    219  -1136       O  
ATOM   9487  CB  PRO D 915    -120.567   1.701 -28.777  1.00 66.69           C  
ANISOU 9487  CB  PRO D 915     8643   7654   9040   -663    123  -1388       C  
ATOM   9488  CG  PRO D 915    -119.984   1.021 -29.986  1.00 65.11           C  
ANISOU 9488  CG  PRO D 915     8437   7456   8846   -586     73  -1551       C  
ATOM   9489  CD  PRO D 915    -120.225   1.957 -31.148  1.00 67.59           C  
ANISOU 9489  CD  PRO D 915     8705   7966   9009   -528     65  -1626       C  
ATOM   9490  N   ILE D 916    -118.132   4.176 -29.526  1.00 64.17           N  
ANISOU 9490  N   ILE D 916     8356   7639   8387   -452    190  -1287       N  
ATOM   9491  CA  ILE D 916    -116.794   4.658 -29.191  1.00 64.06           C  
ANISOU 9491  CA  ILE D 916     8376   7647   8317   -388    222  -1204       C  
ATOM   9492  C   ILE D 916    -116.823   6.172 -29.115  1.00 61.03           C  
ANISOU 9492  C   ILE D 916     7974   7396   7819   -376    257  -1112       C  
ATOM   9493  O   ILE D 916    -117.185   6.844 -30.084  1.00 61.53           O  
ANISOU 9493  O   ILE D 916     7995   7588   7796   -346    250  -1157       O  
ATOM   9494  CB  ILE D 916    -115.735   4.229 -30.230  1.00 66.33           C  
ANISOU 9494  CB  ILE D 916     8663   7972   8567   -289    199  -1302       C  
ATOM   9495  CG1 ILE D 916    -115.635   2.709 -30.281  1.00 70.93           C  
ANISOU 9495  CG1 ILE D 916     9266   8409   9277   -293    157  -1401       C  
ATOM   9496  CG2 ILE D 916    -114.363   4.748 -29.857  1.00 63.32           C  
ANISOU 9496  CG2 ILE D 916     8311   7618   8129   -229    233  -1210       C  
ATOM   9497  CD1 ILE D 916    -114.637   2.184 -31.298  1.00 78.23           C  
ANISOU 9497  CD1 ILE D 916    10186   9370  10169   -189    128  -1516       C  
ATOM   9498  N   GLY D 917    -116.421   6.693 -27.960  1.00 56.19           N  
ANISOU 9498  N   GLY D 917     7390   6752   7210   -395    294   -986       N  
ATOM   9499  CA  GLY D 917    -116.355   8.127 -27.728  1.00 55.46           C  
ANISOU 9499  CA  GLY D 917     7282   6760   7031   -384    324   -896       C  
ATOM   9500  C   GLY D 917    -114.980   8.628 -27.290  1.00 52.84           C  
ANISOU 9500  C   GLY D 917     6974   6436   6666   -331    350   -818       C  
ATOM   9501  O   GLY D 917    -114.090   7.845 -26.919  1.00 48.47           O  
ANISOU 9501  O   GLY D 917     6455   5802   6158   -308    350   -815       O  
ATOM   9502  N   LEU D 918    -114.834   9.954 -27.350  1.00 49.25           N  
ANISOU 9502  N   LEU D 918     6496   6077   6139   -312    369   -755       N  
ATOM   9503  CA  LEU D 918    -113.650  10.652 -26.907  1.00 45.76           C  
ANISOU 9503  CA  LEU D 918     6065   5653   5670   -271    392   -675       C  
ATOM   9504  C   LEU D 918    -113.989  11.612 -25.754  1.00 44.70           C  
ANISOU 9504  C   LEU D 918     5929   5515   5541   -311    411   -583       C  
ATOM   9505  O   LEU D 918    -114.979  12.356 -25.798  1.00 41.51           O  
ANISOU 9505  O   LEU D 918     5497   5160   5116   -342    410   -572       O  
ATOM   9506  CB  LEU D 918    -113.036  11.435 -28.056  1.00 44.25           C  
ANISOU 9506  CB  LEU D 918     5836   5578   5398   -206    396   -680       C  
ATOM   9507  CG  LEU D 918    -112.480  10.631 -29.227  1.00 45.78           C  
ANISOU 9507  CG  LEU D 918     6022   5808   5565   -144    378   -769       C  
ATOM   9508  CD1 LEU D 918    -111.998  11.555 -30.331  1.00 43.33           C  
ANISOU 9508  CD1 LEU D 918     5662   5639   5163    -79    387   -751       C  
ATOM   9509  CD2 LEU D 918    -111.359   9.723 -28.765  1.00 45.73           C  
ANISOU 9509  CD2 LEU D 918     6057   5718   5602   -114    379   -775       C  
ATOM   9510  N   ILE D 919    -113.131  11.588 -24.735  1.00 42.44           N  
ANISOU 9510  N   ILE D 919     5669   5177   5279   -303    426   -522       N  
ATOM   9511  CA  ILE D 919    -113.284  12.440 -23.578  1.00 41.34           C  
ANISOU 9511  CA  ILE D 919     5525   5040   5143   -327    439   -446       C  
ATOM   9512  C   ILE D 919    -111.931  13.040 -23.155  1.00 38.38           C  
ANISOU 9512  C   ILE D 919     5152   4675   4754   -281    451   -393       C  
ATOM   9513  O   ILE D 919    -110.886  12.365 -23.193  1.00 39.19           O  
ANISOU 9513  O   ILE D 919     5279   4745   4868   -245    454   -399       O  
ATOM   9514  CB  ILE D 919    -113.953  11.643 -22.441  1.00 40.27           C  
ANISOU 9514  CB  ILE D 919     5411   4829   5061   -380    442   -426       C  
ATOM   9515  CG1 ILE D 919    -114.418  12.559 -21.340  1.00 38.53           C  
ANISOU 9515  CG1 ILE D 919     5174   4637   4829   -403    451   -365       C  
ATOM   9516  CG2 ILE D 919    -113.000  10.617 -21.869  1.00 39.56           C  
ANISOU 9516  CG2 ILE D 919     5359   4658   5013   -359    448   -409       C  
ATOM   9517  CD1 ILE D 919    -115.427  11.887 -20.455  1.00 41.85           C  
ANISOU 9517  CD1 ILE D 919     5597   5017   5286   -459    455   -344       C  
ATOM   9518  N   LEU D 920    -111.961  14.291 -22.717  1.00 33.86           N  
ANISOU 9518  N   LEU D 920     4554   4145   4167   -283    455   -346       N  
ATOM   9519  CA  LEU D 920    -110.749  14.970 -22.248  1.00 33.94           C  
ANISOU 9519  CA  LEU D 920     4557   4163   4176   -247    461   -299       C  
ATOM   9520  C   LEU D 920    -110.577  14.959 -20.750  1.00 31.66           C  
ANISOU 9520  C   LEU D 920     4280   3838   3911   -257    465   -262       C  
ATOM   9521  O   LEU D 920    -111.549  15.014 -19.993  1.00 31.70           O  
ANISOU 9521  O   LEU D 920     4283   3839   3924   -293    463   -254       O  
ATOM   9522  CB  LEU D 920    -110.790  16.420 -22.674  1.00 34.45           C  
ANISOU 9522  CB  LEU D 920     4576   4290   4223   -238    458   -272       C  
ATOM   9523  CG  LEU D 920    -110.784  16.635 -24.176  1.00 37.71           C  
ANISOU 9523  CG  LEU D 920     4964   4764   4600   -214    458   -288       C  
ATOM   9524  CD1 LEU D 920    -111.247  18.038 -24.505  1.00 36.12           C  
ANISOU 9524  CD1 LEU D 920     4717   4616   4393   -217    454   -252       C  
ATOM   9525  CD2 LEU D 920    -109.395  16.395 -24.717  1.00 40.16           C  
ANISOU 9525  CD2 LEU D 920     5272   5090   4898   -163    467   -278       C  
ATOM   9526  N   LEU D 921    -109.329  14.922 -20.304  1.00 31.54           N  
ANISOU 9526  N   LEU D 921     4272   3810   3902   -220    470   -237       N  
ATOM   9527  CA  LEU D 921    -108.992  15.358 -18.952  1.00 32.21           C  
ANISOU 9527  CA  LEU D 921     4349   3892   3996   -215    469   -202       C  
ATOM   9528  C   LEU D 921    -108.224  16.654 -19.065  1.00 30.78           C  
ANISOU 9528  C   LEU D 921     4129   3749   3817   -190    460   -185       C  
ATOM   9529  O   LEU D 921    -107.200  16.718 -19.728  1.00 29.93           O  
ANISOU 9529  O   LEU D 921     4015   3652   3707   -159    464   -180       O  
ATOM   9530  CB  LEU D 921    -108.155  14.326 -18.206  1.00 35.05           C  
ANISOU 9530  CB  LEU D 921     4741   4210   4366   -190    479   -185       C  
ATOM   9531  CG  LEU D 921    -108.939  13.125 -17.668  1.00 36.50           C  
ANISOU 9531  CG  LEU D 921     4957   4344   4569   -219    486   -178       C  
ATOM   9532  CD1 LEU D 921    -107.957  12.036 -17.298  1.00 38.68           C  
ANISOU 9532  CD1 LEU D 921     5266   4570   4862   -185    496   -161       C  
ATOM   9533  CD2 LEU D 921    -109.791  13.504 -16.466  1.00 35.08           C  
ANISOU 9533  CD2 LEU D 921     4757   4188   4382   -245    487   -147       C  
ATOM   9534  N   GLY D 922    -108.733  17.688 -18.414  1.00 31.01           N  
ANISOU 9534  N   GLY D 922     4127   3800   3854   -204    447   -178       N  
ATOM   9535  CA  GLY D 922    -108.090  19.000 -18.396  1.00 30.15           C  
ANISOU 9535  CA  GLY D 922     3974   3712   3770   -186    432   -165       C  
ATOM   9536  C   GLY D 922    -107.621  19.394 -17.005  1.00 28.00           C  
ANISOU 9536  C   GLY D 922     3686   3442   3513   -169    418   -165       C  
ATOM   9537  O   GLY D 922    -108.289  19.104 -16.018  1.00 28.87           O  
ANISOU 9537  O   GLY D 922     3803   3559   3607   -177    415   -172       O  
ATOM   9538  N   GLU D 923    -106.479  20.070 -16.939  1.00 28.31           N  
ANISOU 9538  N   GLU D 923     3693   3482   3580   -144    407   -156       N  
ATOM   9539  CA  GLU D 923    -106.063  20.732 -15.705  1.00 28.72           C  
ANISOU 9539  CA  GLU D 923     3713   3545   3654   -124    383   -170       C  
ATOM   9540  C   GLU D 923    -106.740  22.080 -15.742  1.00 27.55           C  
ANISOU 9540  C   GLU D 923     3521   3402   3546   -140    356   -187       C  
ATOM   9541  O   GLU D 923    -106.568  22.835 -16.696  1.00 27.09           O  
ANISOU 9541  O   GLU D 923     3437   3332   3525   -148    352   -167       O  
ATOM   9542  CB  GLU D 923    -104.550  20.902 -15.636  1.00 28.96           C  
ANISOU 9542  CB  GLU D 923     3723   3573   3709    -94    379   -160       C  
ATOM   9543  CG  GLU D 923    -104.099  21.528 -14.335  1.00 32.23           C  
ANISOU 9543  CG  GLU D 923     4098   4005   4144    -70    350   -190       C  
ATOM   9544  CD  GLU D 923    -102.629  21.923 -14.323  1.00 33.23           C  
ANISOU 9544  CD  GLU D 923     4189   4130   4308    -45    339   -185       C  
ATOM   9545  OE1 GLU D 923    -101.830  21.193 -14.920  1.00 35.56           O  
ANISOU 9545  OE1 GLU D 923     4506   4421   4584    -33    364   -157       O  
ATOM   9546  OE2 GLU D 923    -102.269  22.909 -13.645  1.00 32.01           O  
ANISOU 9546  OE2 GLU D 923     3981   3980   4201    -35    304   -218       O  
ATOM   9547  N   VAL D 924    -107.596  22.325 -14.761  1.00 27.14           N  
ANISOU 9547  N   VAL D 924     3459   3371   3481   -140    339   -217       N  
ATOM   9548  CA  VAL D 924    -108.398  23.524 -14.730  1.00 27.09           C  
ANISOU 9548  CA  VAL D 924     3414   3370   3510   -150    310   -241       C  
ATOM   9549  C   VAL D 924    -107.999  24.325 -13.488  1.00 26.17           C  
ANISOU 9549  C   VAL D 924     3251   3268   3423   -118    271   -288       C  
ATOM   9550  O   VAL D 924    -108.017  23.813 -12.384  1.00 23.73           O  
ANISOU 9550  O   VAL D 924     2946   2999   3070    -95    269   -308       O  
ATOM   9551  CB  VAL D 924    -109.909  23.193 -14.654  1.00 26.80           C  
ANISOU 9551  CB  VAL D 924     3397   3359   3429   -173    318   -251       C  
ATOM   9552  CG1 VAL D 924    -110.739  24.481 -14.711  1.00 26.74           C  
ANISOU 9552  CG1 VAL D 924     3347   3356   3457   -176    286   -277       C  
ATOM   9553  CG2 VAL D 924    -110.320  22.250 -15.777  1.00 27.04           C  
ANISOU 9553  CG2 VAL D 924     3470   3378   3427   -202    352   -220       C  
ATOM   9554  N   ALA D 925    -107.656  25.588 -13.688  1.00 25.08           N  
ANISOU 9554  N   ALA D 925     3064   3101   3364   -114    237   -304       N  
ATOM   9555  CA  ALA D 925    -107.184  26.394 -12.593  1.00 27.12           C  
ANISOU 9555  CA  ALA D 925     3272   3368   3665    -82    192   -364       C  
ATOM   9556  C   ALA D 925    -108.399  27.092 -11.991  1.00 28.27           C  
ANISOU 9556  C   ALA D 925     3392   3539   3811    -73    160   -417       C  
ATOM   9557  O   ALA D 925    -108.815  28.149 -12.466  1.00 32.75           O  
ANISOU 9557  O   ALA D 925     3929   4069   4447    -83    133   -428       O  
ATOM   9558  CB  ALA D 925    -106.159  27.399 -13.097  1.00 28.67           C  
ANISOU 9558  CB  ALA D 925     3420   3507   3966    -86    167   -356       C  
ATOM   9559  N   LEU D 926    -108.968  26.499 -10.961  1.00 28.18           N  
ANISOU 9559  N   LEU D 926     3389   3595   3721    -51    163   -446       N  
ATOM   9560  CA  LEU D 926    -110.256  26.948 -10.436  1.00 28.25           C  
ANISOU 9560  CA  LEU D 926     3378   3649   3705    -41    142   -489       C  
ATOM   9561  C   LEU D 926    -110.103  28.078  -9.438  1.00 28.28           C  
ANISOU 9561  C   LEU D 926     3315   3674   3755      6     80   -580       C  
ATOM   9562  O   LEU D 926    -111.009  28.874  -9.271  1.00 27.17           O  
ANISOU 9562  O   LEU D 926     3145   3545   3633     18     48   -627       O  
ATOM   9563  CB  LEU D 926    -110.977  25.796  -9.753  1.00 26.91           C  
ANISOU 9563  CB  LEU D 926     3238   3557   3430    -37    175   -469       C  
ATOM   9564  CG  LEU D 926    -111.262  24.621 -10.654  1.00 27.69           C  
ANISOU 9564  CG  LEU D 926     3399   3631   3491    -84    229   -394       C  
ATOM   9565  CD1 LEU D 926    -111.655  23.424  -9.806  1.00 29.92           C  
ANISOU 9565  CD1 LEU D 926     3702   3975   3690    -78    260   -366       C  
ATOM   9566  CD2 LEU D 926    -112.372  24.961 -11.612  1.00 28.48           C  
ANISOU 9566  CD2 LEU D 926     3507   3711   3602   -120    234   -385       C  
ATOM   9567  N   GLY D 927    -108.971  28.119  -8.743  1.00 30.57           N  
ANISOU 9567  N   GLY D 927     3579   3974   4062     39     60   -613       N  
ATOM   9568  CA  GLY D 927    -108.747  29.133  -7.703  1.00 31.30           C  
ANISOU 9568  CA  GLY D 927     3601   4094   4198     91     -6   -718       C  
ATOM   9569  C   GLY D 927    -109.875  29.112  -6.676  1.00 30.05           C  
ANISOU 9569  C   GLY D 927     3422   4041   3956    133    -21   -773       C  
ATOM   9570  O   GLY D 927    -110.306  28.059  -6.272  1.00 28.66           O  
ANISOU 9570  O   GLY D 927     3275   3941   3674    136     21   -729       O  
ATOM   9571  N   ASN D 928    -110.308  30.291  -6.242  1.00 30.24           N  
ANISOU 9571  N   ASN D 928     3387   4069   4034    167    -83   -868       N  
ATOM   9572  CA  ASN D 928    -111.446  30.458  -5.359  1.00 31.41           C  
ANISOU 9572  CA  ASN D 928     3505   4322   4109    213   -103   -929       C  
ATOM   9573  C   ASN D 928    -112.770  30.326  -6.137  1.00 31.95           C  
ANISOU 9573  C   ASN D 928     3609   4380   4151    171    -72   -874       C  
ATOM   9574  O   ASN D 928    -113.093  31.143  -7.030  1.00 30.72           O  
ANISOU 9574  O   ASN D 928     3453   4136   4084    144    -89   -874       O  
ATOM   9575  CB  ASN D 928    -111.396  31.821  -4.701  1.00 32.91           C  
ANISOU 9575  CB  ASN D 928     3616   4510   4379    270   -188  -1063       C  
ATOM   9576  CG  ASN D 928    -110.183  32.007  -3.816  1.00 34.27           C  
ANISOU 9576  CG  ASN D 928     3739   4710   4573    318   -229  -1139       C  
ATOM   9577  OD1 ASN D 928    -109.792  31.098  -3.086  1.00 34.96           O  
ANISOU 9577  OD1 ASN D 928     3832   4895   4557    347   -202  -1120       O  
ATOM   9578  ND2 ASN D 928    -109.602  33.193  -3.860  1.00 33.18           N  
ANISOU 9578  ND2 ASN D 928     3547   4486   4574    330   -298  -1226       N  
ATOM   9579  N   MET D 929    -113.511  29.288  -5.779  1.00 29.68           N  
ANISOU 9579  N   MET D 929     3348   4186   3744    168    -25   -824       N  
ATOM   9580  CA  MET D 929    -114.713  28.911  -6.473  1.00 30.50           C  
ANISOU 9580  CA  MET D 929     3487   4292   3811    123     13   -766       C  
ATOM   9581  C   MET D 929    -115.910  29.655  -5.906  1.00 30.45           C  
ANISOU 9581  C   MET D 929     3431   4363   3776    164    -24   -838       C  
ATOM   9582  O   MET D 929    -116.075  29.727  -4.706  1.00 32.07           O  
ANISOU 9582  O   MET D 929     3587   4681   3918    227    -48   -899       O  
ATOM   9583  CB  MET D 929    -114.921  27.413  -6.339  1.00 32.09           C  
ANISOU 9583  CB  MET D 929     3733   4548   3912     95     78   -675       C  
ATOM   9584  CG  MET D 929    -113.828  26.591  -7.007  1.00 33.57           C  
ANISOU 9584  CG  MET D 929     3974   4655   4124     56    117   -603       C  
ATOM   9585  SD  MET D 929    -113.977  24.805  -6.768  1.00 34.34           S  
ANISOU 9585  SD  MET D 929     4122   4799   4126     29    187   -501       S  
ATOM   9586  CE  MET D 929    -114.017  24.707  -4.979  1.00 38.78           C  
ANISOU 9586  CE  MET D 929     4623   5514   4597    108    170   -537       C  
ATOM   9587  N   TYR D 930    -116.717  30.229  -6.798  1.00 28.71           N  
ANISOU 9587  N   TYR D 930     3218   4087   3601    135    -30   -832       N  
ATOM   9588  CA  TYR D 930    -118.012  30.770  -6.465  1.00 28.17           C  
ANISOU 9588  CA  TYR D 930     3113   4092   3498    165    -54   -883       C  
ATOM   9589  C   TYR D 930    -118.966  29.568  -6.449  1.00 29.30           C  
ANISOU 9589  C   TYR D 930     3285   4320   3525    130      8   -804       C  
ATOM   9590  O   TYR D 930    -119.297  29.016  -7.499  1.00 28.36           O  
ANISOU 9590  O   TYR D 930     3217   4148   3412     64     51   -727       O  
ATOM   9591  CB  TYR D 930    -118.408  31.786  -7.520  1.00 26.82           C  
ANISOU 9591  CB  TYR D 930     2943   3821   3427    146    -80   -893       C  
ATOM   9592  CG  TYR D 930    -119.652  32.612  -7.277  1.00 27.44           C  
ANISOU 9592  CG  TYR D 930     2978   3953   3495    186   -118   -960       C  
ATOM   9593  CD1 TYR D 930    -120.131  32.872  -5.997  1.00 28.72           C  
ANISOU 9593  CD1 TYR D 930     3081   4239   3591    259   -154  -1051       C  
ATOM   9594  CD2 TYR D 930    -120.332  33.177  -8.352  1.00 27.40           C  
ANISOU 9594  CD2 TYR D 930     2985   3880   3545    159   -120   -934       C  
ATOM   9595  CE1 TYR D 930    -121.256  33.660  -5.797  1.00 28.56           C  
ANISOU 9595  CE1 TYR D 930     3018   4270   3562    303   -192  -1119       C  
ATOM   9596  CE2 TYR D 930    -121.445  33.977  -8.175  1.00 28.43           C  
ANISOU 9596  CE2 TYR D 930     3076   4055   3673    200   -157   -996       C  
ATOM   9597  CZ  TYR D 930    -121.909  34.216  -6.896  1.00 31.56           C  
ANISOU 9597  CZ  TYR D 930     3416   4570   4006    272   -194  -1091       C  
ATOM   9598  OH  TYR D 930    -123.030  35.022  -6.742  1.00 32.70           O  
ANISOU 9598  OH  TYR D 930     3517   4761   4145    319   -233  -1158       O  
ATOM   9599  N   GLU D 931    -119.375  29.153  -5.260  1.00 30.30           N  
ANISOU 9599  N   GLU D 931     3376   4585   3553    174     12   -822       N  
ATOM   9600  CA  GLU D 931    -120.161  27.946  -5.113  1.00 33.05           C  
ANISOU 9600  CA  GLU D 931     3743   5014   3802    138     71   -735       C  
ATOM   9601  C   GLU D 931    -121.632  28.248  -5.234  1.00 31.96           C  
ANISOU 9601  C   GLU D 931     3578   4941   3624    135     69   -748       C  
ATOM   9602  O   GLU D 931    -122.153  29.047  -4.502  1.00 32.86           O  
ANISOU 9602  O   GLU D 931     3632   5142   3712    201     26   -830       O  
ATOM   9603  CB  GLU D 931    -119.857  27.305  -3.769  1.00 35.64           C  
ANISOU 9603  CB  GLU D 931     4036   5468   4038    188     83   -727       C  
ATOM   9604  CG  GLU D 931    -118.377  27.064  -3.594  1.00 39.06           C  
ANISOU 9604  CG  GLU D 931     4489   5846   4507    200     80   -722       C  
ATOM   9605  CD  GLU D 931    -118.054  26.068  -2.511  1.00 43.75           C  
ANISOU 9605  CD  GLU D 931     5066   6551   5005    232    112   -670       C  
ATOM   9606  OE1 GLU D 931    -118.928  25.747  -1.694  1.00 50.76           O  
ANISOU 9606  OE1 GLU D 931     5911   7579   5797    261    127   -651       O  
ATOM   9607  OE2 GLU D 931    -116.888  25.605  -2.471  1.00 52.84           O  
ANISOU 9607  OE2 GLU D 931     6244   7655   6176    231    124   -642       O  
ATOM   9608  N   LEU D 932    -122.309  27.606  -6.165  1.00 32.18           N  
ANISOU 9608  N   LEU D 932     3648   4931   3648     62    113   -673       N  
ATOM   9609  CA  LEU D 932    -123.716  27.920  -6.421  1.00 34.83           C  
ANISOU 9609  CA  LEU D 932     3959   5323   3952     54    110   -685       C  
ATOM   9610  C   LEU D 932    -124.527  26.638  -6.421  1.00 35.56           C  
ANISOU 9610  C   LEU D 932     4064   5478   3971     -4    170   -593       C  
ATOM   9611  O   LEU D 932    -124.059  25.577  -6.883  1.00 32.63           O  
ANISOU 9611  O   LEU D 932     3744   5041   3613    -64    214   -515       O  
ATOM   9612  CB  LEU D 932    -123.888  28.628  -7.769  1.00 33.69           C  
ANISOU 9612  CB  LEU D 932     3844   5065   3893     22     95   -696       C  
ATOM   9613  CG  LEU D 932    -123.215  29.996  -7.835  1.00 35.02           C  
ANISOU 9613  CG  LEU D 932     3991   5160   4155     75     33   -778       C  
ATOM   9614  CD1 LEU D 932    -123.271  30.557  -9.235  1.00 35.93           C  
ANISOU 9614  CD1 LEU D 932     4136   5160   4355     38     29   -757       C  
ATOM   9615  CD2 LEU D 932    -123.861  30.948  -6.861  1.00 36.12           C  
ANISOU 9615  CD2 LEU D 932     4060   5395   4269    156    -21   -878       C  
ATOM   9616  N   LYS D 933    -125.752  26.757  -5.951  1.00 35.30           N  
ANISOU 9616  N   LYS D 933     3979   5563   3868     13    169   -605       N  
ATOM   9617  CA  LYS D 933    -126.658  25.624  -5.916  1.00 39.12           C  
ANISOU 9617  CA  LYS D 933     4461   6113   4292    -45    223   -517       C  
ATOM   9618  C   LYS D 933    -127.713  25.682  -7.004  1.00 37.84           C  
ANISOU 9618  C   LYS D 933     4310   5920   4147   -102    231   -509       C  
ATOM   9619  O   LYS D 933    -128.353  24.673  -7.268  1.00 37.34           O  
ANISOU 9619  O   LYS D 933     4255   5871   4061   -169    275   -437       O  
ATOM   9620  CB  LYS D 933    -127.365  25.566  -4.563  1.00 38.86           C  
ANISOU 9620  CB  LYS D 933     4350   6262   4154     10    224   -519       C  
ATOM   9621  CG  LYS D 933    -126.443  25.325  -3.381  1.00 40.26           C  
ANISOU 9621  CG  LYS D 933     4503   6503   4289     70    223   -513       C  
ATOM   9622  CD  LYS D 933    -127.194  25.509  -2.048  1.00 44.29           C  
ANISOU 9622  CD  LYS D 933     4922   7222   4686    147    215   -532       C  
ATOM   9623  CE  LYS D 933    -126.394  26.208  -0.947  1.00 46.70           C  
ANISOU 9623  CE  LYS D 933     5178   7608   4956    256    168   -620       C  
ATOM   9624  NZ  LYS D 933    -127.137  26.721   0.272  1.00 48.19           N  
ANISOU 9624  NZ  LYS D 933     5266   8010   5032    355    142   -679       N  
ATOM   9625  N   HIS D 934    -127.918  26.853  -7.604  1.00 35.52           N  
ANISOU 9625  N   HIS D 934     4012   5587   3896    -73    188   -582       N  
ATOM   9626  CA  HIS D 934    -128.961  27.010  -8.610  1.00 36.45           C  
ANISOU 9626  CA  HIS D 934     4133   5694   4022   -113    193   -579       C  
ATOM   9627  C   HIS D 934    -128.467  27.874  -9.739  1.00 34.08           C  
ANISOU 9627  C   HIS D 934     3869   5270   3810   -110    164   -613       C  
ATOM   9628  O   HIS D 934    -127.476  28.565  -9.604  1.00 34.27           O  
ANISOU 9628  O   HIS D 934     3901   5230   3891    -68    132   -651       O  
ATOM   9629  CB  HIS D 934    -130.230  27.632  -7.984  1.00 36.62           C  
ANISOU 9629  CB  HIS D 934     4082   5855   3975    -65    171   -627       C  
ATOM   9630  CG  HIS D 934    -130.644  26.968  -6.718  1.00 39.67           C  
ANISOU 9630  CG  HIS D 934     4417   6388   4269    -49    194   -594       C  
ATOM   9631  ND1 HIS D 934    -131.255  25.729  -6.710  1.00 40.81           N  
ANISOU 9631  ND1 HIS D 934     4558   6575   4372   -122    249   -502       N  
ATOM   9632  CD2 HIS D 934    -130.488  27.328  -5.416  1.00 39.37           C  
ANISOU 9632  CD2 HIS D 934     4323   6464   4173     33    172   -635       C  
ATOM   9633  CE1 HIS D 934    -131.468  25.362  -5.456  1.00 41.49           C  
ANISOU 9633  CE1 HIS D 934     4588   6798   4377    -87    263   -473       C  
ATOM   9634  NE2 HIS D 934    -131.003  26.305  -4.654  1.00 40.60           N  
ANISOU 9634  NE2 HIS D 934     4442   6739   4245     10    218   -555       N  
ATOM   9635  N   ALA D 935    -129.192  27.842 -10.840  1.00 31.63           N  
ANISOU 9635  N   ALA D 935     3573   4936   3510   -153    176   -595       N  
ATOM   9636  CA  ALA D 935    -128.829  28.565 -12.043  1.00 32.24           C  
ANISOU 9636  CA  ALA D 935     3679   4910   3662   -154    157   -605       C  
ATOM   9637  C   ALA D 935    -128.527  30.042 -11.771  1.00 33.45           C  
ANISOU 9637  C   ALA D 935     3803   5036   3871    -76     99   -674       C  
ATOM   9638  O   ALA D 935    -129.226  30.706 -11.014  1.00 33.11           O  
ANISOU 9638  O   ALA D 935     3707   5074   3797    -20     67   -733       O  
ATOM   9639  CB  ALA D 935    -129.947  28.436 -13.084  1.00 29.52           C  
ANISOU 9639  CB  ALA D 935     3331   4588   3296   -193    172   -588       C  
ATOM   9640  N   SER D 936    -127.492  30.555 -12.433  1.00 33.14           N  
ANISOU 9640  N   SER D 936     3793   4880   3919    -71     85   -667       N  
ATOM   9641  CA  SER D 936    -127.109  31.942 -12.327  1.00 34.03           C  
ANISOU 9641  CA  SER D 936     3879   4937   4115     -8     29   -723       C  
ATOM   9642  C   SER D 936    -126.204  32.285 -13.514  1.00 33.48           C  
ANISOU 9642  C   SER D 936     3843   4741   4138    -30     31   -675       C  
ATOM   9643  O   SER D 936    -125.104  31.736 -13.655  1.00 33.15           O  
ANISOU 9643  O   SER D 936     3836   4641   4121    -59     53   -638       O  
ATOM   9644  CB  SER D 936    -126.357  32.171 -11.034  1.00 34.80           C  
ANISOU 9644  CB  SER D 936     3952   5050   4221     42     -2   -781       C  
ATOM   9645  OG  SER D 936    -126.192  33.566 -10.838  1.00 35.70           O  
ANISOU 9645  OG  SER D 936     4028   5116   4421    107    -66   -855       O  
ATOM   9646  N   HIS D 937    -126.701  33.150 -14.386  1.00 33.62           N  
ANISOU 9646  N   HIS D 937     3847   4725   4202    -15     13   -668       N  
ATOM   9647  CA  HIS D 937    -126.010  33.493 -15.623  1.00 33.42           C  
ANISOU 9647  CA  HIS D 937     3843   4601   4253    -33     21   -605       C  
ATOM   9648  C   HIS D 937    -124.906  34.495 -15.360  1.00 32.23           C  
ANISOU 9648  C   HIS D 937     3676   4348   4223      3    -22   -624       C  
ATOM   9649  O   HIS D 937    -125.114  35.694 -15.411  1.00 30.74           O  
ANISOU 9649  O   HIS D 937     3451   4114   4115     48    -68   -651       O  
ATOM   9650  CB  HIS D 937    -126.992  34.012 -16.664  1.00 37.04           C  
ANISOU 9650  CB  HIS D 937     4289   5076   4710    -27     20   -578       C  
ATOM   9651  CG  HIS D 937    -127.952  32.960 -17.123  1.00 42.75           C  
ANISOU 9651  CG  HIS D 937     5027   5890   5325    -72     63   -555       C  
ATOM   9652  ND1 HIS D 937    -129.099  33.245 -17.838  1.00 47.62           N  
ANISOU 9652  ND1 HIS D 937     5624   6561   5909    -65     64   -548       N  
ATOM   9653  CD2 HIS D 937    -127.951  31.616 -16.931  1.00 42.60           C  
ANISOU 9653  CD2 HIS D 937     5038   5916   5233   -125    105   -542       C  
ATOM   9654  CE1 HIS D 937    -129.748  32.121 -18.086  1.00 47.54           C  
ANISOU 9654  CE1 HIS D 937     5628   6625   5810   -115    102   -537       C  
ATOM   9655  NE2 HIS D 937    -129.067  31.119 -17.553  1.00 46.86           N  
ANISOU 9655  NE2 HIS D 937     5573   6527   5704   -154    127   -531       N  
ATOM   9656  N   ILE D 938    -123.725  33.972 -15.094  1.00 31.10           N  
ANISOU 9656  N   ILE D 938     3556   4163   4097    -18     -8   -609       N  
ATOM   9657  CA  ILE D 938    -122.579  34.783 -14.716  1.00 33.61           C  
ANISOU 9657  CA  ILE D 938     3854   4389   4528      9    -48   -633       C  
ATOM   9658  C   ILE D 938    -122.138  35.579 -15.924  1.00 33.11           C  
ANISOU 9658  C   ILE D 938     3784   4226   4569      3    -53   -563       C  
ATOM   9659  O   ILE D 938    -121.947  34.988 -16.970  1.00 35.26           O  
ANISOU 9659  O   ILE D 938     4088   4498   4813    -37     -6   -480       O  
ATOM   9660  CB  ILE D 938    -121.396  33.904 -14.279  1.00 32.90           C  
ANISOU 9660  CB  ILE D 938     3792   4287   4420    -16    -24   -621       C  
ATOM   9661  CG1 ILE D 938    -121.802  32.999 -13.123  1.00 31.85           C  
ANISOU 9661  CG1 ILE D 938     3664   4260   4178    -11    -11   -666       C  
ATOM   9662  CG2 ILE D 938    -120.211  34.778 -13.909  1.00 34.68           C  
ANISOU 9662  CG2 ILE D 938     3988   4420   4767     10    -69   -651       C  
ATOM   9663  CD1 ILE D 938    -122.338  33.744 -11.919  1.00 33.01           C  
ANISOU 9663  CD1 ILE D 938     3758   4462   4321     53    -65   -768       C  
ATOM   9664  N   SER D 939    -122.087  36.903 -15.795  1.00 35.61           N  
ANISOU 9664  N   SER D 939     4056   4470   5005     46   -109   -595       N  
ATOM   9665  CA  SER D 939    -121.443  37.761 -16.796  1.00 39.27           C  
ANISOU 9665  CA  SER D 939     4502   4822   5596     41   -118   -517       C  
ATOM   9666  C   SER D 939    -120.084  38.194 -16.295  1.00 36.93           C  
ANISOU 9666  C   SER D 939     4185   4432   5415     43   -149   -537       C  
ATOM   9667  O   SER D 939    -119.171  38.311 -17.073  1.00 38.90           O  
ANISOU 9667  O   SER D 939     4434   4612   5733     16   -131   -451       O  
ATOM   9668  CB  SER D 939    -122.282  38.968 -17.176  1.00 41.81           C  
ANISOU 9668  CB  SER D 939     4784   5107   5996     82   -157   -517       C  
ATOM   9669  OG  SER D 939    -123.485  38.534 -17.790  1.00 53.01           O  
ANISOU 9669  OG  SER D 939     6220   6619   7304     77   -124   -489       O  
ATOM   9670  N   LYS D 940    -119.953  38.412 -14.990  1.00 36.30           N  
ANISOU 9670  N   LYS D 940     4082   4361   5350     78   -197   -651       N  
ATOM   9671  CA  LYS D 940    -118.677  38.699 -14.375  1.00 35.18           C  
ANISOU 9671  CA  LYS D 940     3917   4148   5303     82   -229   -689       C  
ATOM   9672  C   LYS D 940    -118.686  38.057 -12.995  1.00 33.92           C  
ANISOU 9672  C   LYS D 940     3759   4082   5046    107   -241   -795       C  
ATOM   9673  O   LYS D 940    -119.630  38.231 -12.219  1.00 35.35           O  
ANISOU 9673  O   LYS D 940     3920   4337   5173    152   -270   -882       O  
ATOM   9674  CB  LYS D 940    -118.418  40.225 -14.262  1.00 35.36           C  
ANISOU 9674  CB  LYS D 940     3876   4044   5514    118   -305   -732       C  
ATOM   9675  N   LEU D 941    -117.627  37.344 -12.682  1.00 32.73           N  
ANISOU 9675  N   LEU D 941     3627   3937   4873     85   -219   -783       N  
ATOM   9676  CA  LEU D 941    -117.466  36.734 -11.371  1.00 34.85           C  
ANISOU 9676  CA  LEU D 941     3892   4296   5054    113   -228   -869       C  
ATOM   9677  C   LEU D 941    -117.327  37.791 -10.272  1.00 35.89           C  
ANISOU 9677  C   LEU D 941     3957   4410   5271    179   -313  -1006       C  
ATOM   9678  O   LEU D 941    -116.818  38.856 -10.519  1.00 35.70           O  
ANISOU 9678  O   LEU D 941     3894   4269   5402    187   -362  -1024       O  
ATOM   9679  CB  LEU D 941    -116.235  35.828 -11.366  1.00 33.17           C  
ANISOU 9679  CB  LEU D 941     3710   4079   4815     78   -188   -821       C  
ATOM   9680  CG  LEU D 941    -116.396  34.539 -12.167  1.00 34.23           C  
ANISOU 9680  CG  LEU D 941     3910   4256   4840     24   -108   -716       C  
ATOM   9681  CD1 LEU D 941    -115.053  33.790 -12.277  1.00 35.05           C  
ANISOU 9681  CD1 LEU D 941     4039   4335   4942     -4    -76   -668       C  
ATOM   9682  CD2 LEU D 941    -117.429  33.642 -11.512  1.00 34.14           C  
ANISOU 9682  CD2 LEU D 941     3919   4369   4685     33    -82   -739       C  
ATOM   9683  N   PRO D 942    -117.779  37.482  -9.054  1.00 37.93           N  
ANISOU 9683  N   PRO D 942     4196   4789   5428    230   -331  -1101       N  
ATOM   9684  CA  PRO D 942    -117.349  38.326  -7.926  1.00 38.48           C  
ANISOU 9684  CA  PRO D 942     4198   4855   5569    298   -413  -1243       C  
ATOM   9685  C   PRO D 942    -115.816  38.470  -7.875  1.00 38.36           C  
ANISOU 9685  C   PRO D 942     4168   4749   5657    280   -431  -1245       C  
ATOM   9686  O   PRO D 942    -115.080  37.498  -8.138  1.00 35.49           O  
ANISOU 9686  O   PRO D 942     3848   4399   5237    234   -372  -1161       O  
ATOM   9687  CB  PRO D 942    -117.849  37.564  -6.684  1.00 37.84           C  
ANISOU 9687  CB  PRO D 942     4105   4950   5321    347   -405  -1310       C  
ATOM   9688  CG  PRO D 942    -118.931  36.667  -7.188  1.00 39.24           C  
ANISOU 9688  CG  PRO D 942     4334   5207   5369    310   -334  -1216       C  
ATOM   9689  CD  PRO D 942    -118.589  36.330  -8.616  1.00 38.01           C  
ANISOU 9689  CD  PRO D 942     4236   4946   5260    228   -279  -1082       C  
ATOM   9690  N   LYS D 943    -115.341  39.670  -7.566  1.00 37.93           N  
ANISOU 9690  N   LYS D 943     4050   4600   5761    314   -512  -1340       N  
ATOM   9691  CA  LYS D 943    -113.905  39.922  -7.514  1.00 37.44           C  
ANISOU 9691  CA  LYS D 943     3963   4448   5816    295   -536  -1349       C  
ATOM   9692  C   LYS D 943    -113.310  38.958  -6.530  1.00 35.15           C  
ANISOU 9692  C   LYS D 943     3677   4281   5397    317   -518  -1388       C  
ATOM   9693  O   LYS D 943    -113.891  38.709  -5.470  1.00 35.73           O  
ANISOU 9693  O   LYS D 943     3731   4490   5356    380   -535  -1480       O  
ATOM   9694  CB  LYS D 943    -113.641  41.365  -7.084  1.00 43.39           C  
ANISOU 9694  CB  LYS D 943     4634   5095   6757    340   -640  -1478       C  
ATOM   9695  CG  LYS D 943    -114.094  42.368  -8.161  1.00 46.73           C  
ANISOU 9695  CG  LYS D 943     5049   5372   7334    314   -657  -1414       C  
ATOM   9696  CD  LYS D 943    -113.682  43.790  -7.869  1.00 52.59           C  
ANISOU 9696  CD  LYS D 943     5710   5973   8299    346   -760  -1523       C  
ATOM   9697  CE  LYS D 943    -114.280  44.721  -8.942  1.00 52.59           C  
ANISOU 9697  CE  LYS D 943     5705   5836   8440    326   -770  -1442       C  
ATOM   9698  NZ  LYS D 943    -113.828  46.134  -8.774  1.00 56.60           N  
ANISOU 9698  NZ  LYS D 943     6131   6175   9199    348   -870  -1529       N  
ATOM   9699  N   GLY D 944    -112.175  38.381  -6.878  1.00 33.15           N  
ANISOU 9699  N   GLY D 944     3449   3993   5155    269   -479  -1312       N  
ATOM   9700  CA  GLY D 944    -111.564  37.381  -6.032  1.00 34.04           C  
ANISOU 9700  CA  GLY D 944     3571   4219   5144    289   -454  -1330       C  
ATOM   9701  C   GLY D 944    -111.939  35.931  -6.303  1.00 34.55           C  
ANISOU 9701  C   GLY D 944     3713   4378   5038    256   -361  -1215       C  
ATOM   9702  O   GLY D 944    -111.294  35.024  -5.781  1.00 35.10           O  
ANISOU 9702  O   GLY D 944     3798   4520   5019    262   -331  -1200       O  
ATOM   9703  N   LYS D 945    -112.981  35.699  -7.096  1.00 34.28           N  
ANISOU 9703  N   LYS D 945     3723   4342   4959    223   -318  -1138       N  
ATOM   9704  CA  LYS D 945    -113.377  34.331  -7.504  1.00 33.93           C  
ANISOU 9704  CA  LYS D 945     3750   4366   4776    182   -233  -1027       C  
ATOM   9705  C   LYS D 945    -112.833  34.081  -8.880  1.00 31.05           C  
ANISOU 9705  C   LYS D 945     3432   3900   4466    112   -186   -907       C  
ATOM   9706  O   LYS D 945    -112.870  34.976  -9.726  1.00 30.41           O  
ANISOU 9706  O   LYS D 945     3336   3719   4500     92   -206   -884       O  
ATOM   9707  CB  LYS D 945    -114.904  34.222  -7.537  1.00 36.07           C  
ANISOU 9707  CB  LYS D 945     4033   4709   4963    190   -218  -1025       C  
ATOM   9708  CG  LYS D 945    -115.544  34.506  -6.178  1.00 38.31           C  
ANISOU 9708  CG  LYS D 945     4263   5114   5180    268   -265  -1144       C  
ATOM   9709  CD  LYS D 945    -115.293  33.363  -5.238  1.00 36.94           C  
ANISOU 9709  CD  LYS D 945     4097   5068   4870    288   -229  -1132       C  
ATOM   9710  CE  LYS D 945    -116.142  33.512  -3.993  1.00 38.37           C  
ANISOU 9710  CE  LYS D 945     4223   5401   4955    366   -261  -1226       C  
ATOM   9711  NZ  LYS D 945    -115.884  32.378  -3.065  1.00 40.46           N  
ANISOU 9711  NZ  LYS D 945     4489   5798   5084    389   -222  -1196       N  
ATOM   9712  N   HIS D 946    -112.409  32.856  -9.150  1.00 30.34           N  
ANISOU 9712  N   HIS D 946     3396   3841   4292     79   -122   -826       N  
ATOM   9713  CA  HIS D 946    -111.882  32.530 -10.483  1.00 31.01           C  
ANISOU 9713  CA  HIS D 946     3522   3849   4413     20    -76   -716       C  
ATOM   9714  C   HIS D 946    -112.701  31.515 -11.285  1.00 28.96           C  
ANISOU 9714  C   HIS D 946     3325   3624   4055    -19    -11   -632       C  
ATOM   9715  O   HIS D 946    -112.426  31.267 -12.471  1.00 27.35           O  
ANISOU 9715  O   HIS D 946     3151   3371   3870    -60     26   -549       O  
ATOM   9716  CB  HIS D 946    -110.457  32.037 -10.340  1.00 31.36           C  
ANISOU 9716  CB  HIS D 946     3570   3876   4468     15    -63   -696       C  
ATOM   9717  CG  HIS D 946    -109.633  32.897  -9.452  1.00 35.74           C  
ANISOU 9717  CG  HIS D 946     4060   4410   5110     54   -128   -790       C  
ATOM   9718  ND1 HIS D 946    -109.490  32.641  -8.105  1.00 35.32           N  
ANISOU 9718  ND1 HIS D 946     3981   4447   4992    107   -153   -876       N  
ATOM   9719  CD2 HIS D 946    -108.972  34.055  -9.693  1.00 36.92           C  
ANISOU 9719  CD2 HIS D 946     4155   4461   5412     51   -178   -816       C  
ATOM   9720  CE1 HIS D 946    -108.762  33.594  -7.555  1.00 37.36           C  
ANISOU 9720  CE1 HIS D 946     4174   4668   5355    137   -219   -965       C  
ATOM   9721  NE2 HIS D 946    -108.432  34.459  -8.502  1.00 38.95           N  
ANISOU 9721  NE2 HIS D 946     4356   4745   5696    100   -236   -929       N  
ATOM   9722  N   SER D 947    -113.689  30.925 -10.654  1.00 27.89           N  
ANISOU 9722  N   SER D 947     3202   3578   3815     -6      3   -654       N  
ATOM   9723  CA  SER D 947    -114.506  29.911 -11.319  1.00 26.30           C  
ANISOU 9723  CA  SER D 947     3054   3411   3528    -47     60   -585       C  
ATOM   9724  C   SER D 947    -115.837  29.745 -10.587  1.00 28.98           C  
ANISOU 9724  C   SER D 947     3383   3845   3785    -28     56   -623       C  
ATOM   9725  O   SER D 947    -116.015  30.247  -9.453  1.00 29.74           O  
ANISOU 9725  O   SER D 947     3433   3999   3870     24     15   -701       O  
ATOM   9726  CB  SER D 947    -113.767  28.596 -11.286  1.00 25.49           C  
ANISOU 9726  CB  SER D 947     2996   3322   3365    -66    107   -533       C  
ATOM   9727  OG  SER D 947    -113.533  28.170  -9.963  1.00 26.59           O  
ANISOU 9727  OG  SER D 947     3122   3534   3449    -29     99   -572       O  
ATOM   9728  N   VAL D 948    -116.758  29.018 -11.205  1.00 27.63           N  
ANISOU 9728  N   VAL D 948     3247   3700   3552    -67     98   -571       N  
ATOM   9729  CA  VAL D 948    -117.968  28.609 -10.526  1.00 27.95           C  
ANISOU 9729  CA  VAL D 948     3277   3839   3504    -59    107   -588       C  
ATOM   9730  C   VAL D 948    -117.909  27.109 -10.289  1.00 27.64           C  
ANISOU 9730  C   VAL D 948     3278   3839   3386    -90    160   -529       C  
ATOM   9731  O   VAL D 948    -117.462  26.345 -11.160  1.00 28.85           O  
ANISOU 9731  O   VAL D 948     3478   3936   3548   -133    196   -470       O  
ATOM   9732  CB  VAL D 948    -119.224  28.955 -11.355  1.00 28.46           C  
ANISOU 9732  CB  VAL D 948     3341   3909   3565    -81    110   -578       C  
ATOM   9733  CG1 VAL D 948    -120.441  28.216 -10.826  1.00 28.63           C  
ANISOU 9733  CG1 VAL D 948     3358   4032   3488    -91    134   -572       C  
ATOM   9734  CG2 VAL D 948    -119.477  30.446 -11.329  1.00 28.10           C  
ANISOU 9734  CG2 VAL D 948     3247   3837   3592    -39     53   -641       C  
ATOM   9735  N   LYS D 949    -118.354  26.700  -9.109  1.00 26.60           N  
ANISOU 9735  N   LYS D 949     3121   3805   3180    -63    163   -544       N  
ATOM   9736  CA  LYS D 949    -118.625  25.318  -8.836  1.00 27.10           C  
ANISOU 9736  CA  LYS D 949     3213   3912   3174    -94    212   -478       C  
ATOM   9737  C   LYS D 949    -120.134  25.184  -8.589  1.00 29.84           C  
ANISOU 9737  C   LYS D 949     3534   4346   3459   -105    222   -474       C  
ATOM   9738  O   LYS D 949    -120.653  25.728  -7.617  1.00 28.05           O  
ANISOU 9738  O   LYS D 949     3254   4215   3190    -55    196   -522       O  
ATOM   9739  CB  LYS D 949    -117.896  24.849  -7.616  1.00 27.09           C  
ANISOU 9739  CB  LYS D 949     3194   3968   3129    -52    215   -475       C  
ATOM   9740  CG  LYS D 949    -118.199  23.400  -7.289  1.00 29.60           C  
ANISOU 9740  CG  LYS D 949     3536   4325   3385    -83    268   -391       C  
ATOM   9741  CD  LYS D 949    -117.433  22.944  -6.076  1.00 32.14           C  
ANISOU 9741  CD  LYS D 949     3839   4712   3662    -34    273   -376       C  
ATOM   9742  CE  LYS D 949    -117.743  21.494  -5.775  1.00 36.57           C  
ANISOU 9742  CE  LYS D 949     4421   5299   4174    -67    327   -277       C  
ATOM   9743  NZ  LYS D 949    -117.150  21.098  -4.472  1.00 41.32           N  
ANISOU 9743  NZ  LYS D 949     4992   5992   4717     -7    332   -252       N  
ATOM   9744  N   GLY D 950    -120.819  24.448  -9.468  1.00 30.20           N  
ANISOU 9744  N   GLY D 950     3613   4364   3497   -169    258   -423       N  
ATOM   9745  CA  GLY D 950    -122.196  24.030  -9.214  1.00 30.85           C  
ANISOU 9745  CA  GLY D 950     3671   4530   3519   -192    276   -403       C  
ATOM   9746  C   GLY D 950    -122.169  22.861  -8.242  1.00 31.32           C  
ANISOU 9746  C   GLY D 950     3727   4650   3524   -198    312   -340       C  
ATOM   9747  O   GLY D 950    -121.549  21.844  -8.519  1.00 30.78           O  
ANISOU 9747  O   GLY D 950     3703   4519   3475   -234    344   -284       O  
ATOM   9748  N   LEU D 951    -122.822  23.014  -7.097  1.00 32.37           N  
ANISOU 9748  N   LEU D 951     3802   4910   3588   -158    306   -348       N  
ATOM   9749  CA  LEU D 951    -122.726  22.038  -6.010  1.00 33.78           C  
ANISOU 9749  CA  LEU D 951     3961   5165   3707   -149    339   -279       C  
ATOM   9750  C   LEU D 951    -123.671  20.878  -6.205  1.00 34.99           C  
ANISOU 9750  C   LEU D 951     4120   5330   3845   -220    386   -192       C  
ATOM   9751  O   LEU D 951    -124.882  21.057  -6.133  1.00 34.24           O  
ANISOU 9751  O   LEU D 951     3985   5312   3714   -234    387   -194       O  
ATOM   9752  CB  LEU D 951    -123.043  22.719  -4.683  1.00 36.46           C  
ANISOU 9752  CB  LEU D 951     4224   5657   3970    -66    312   -323       C  
ATOM   9753  CG  LEU D 951    -122.079  23.840  -4.303  1.00 37.51           C  
ANISOU 9753  CG  LEU D 951     4341   5786   4126     11    258   -421       C  
ATOM   9754  CD1 LEU D 951    -122.467  24.476  -2.976  1.00 37.62           C  
ANISOU 9754  CD1 LEU D 951     4271   5965   4058    101    227   -480       C  
ATOM   9755  CD2 LEU D 951    -120.666  23.278  -4.219  1.00 37.16           C  
ANISOU 9755  CD2 LEU D 951     4335   5672   4111     15    271   -389       C  
ATOM   9756  N   GLY D 952    -123.126  19.683  -6.420  1.00 35.71           N  
ANISOU 9756  N   GLY D 952     4256   5345   3968   -266    423   -115       N  
ATOM   9757  CA  GLY D 952    -123.957  18.475  -6.484  1.00 39.65           C  
ANISOU 9757  CA  GLY D 952     4753   5843   4468   -336    466    -26       C  
ATOM   9758  C   GLY D 952    -124.325  17.877  -5.124  1.00 40.99           C  
ANISOU 9758  C   GLY D 952     4865   6138   4570   -314    494     59       C  
ATOM   9759  O   GLY D 952    -123.713  18.196  -4.106  1.00 40.23           O  
ANISOU 9759  O   GLY D 952     4739   6124   4421   -238    485     55       O  
ATOM   9760  N   LYS D 953    -125.333  17.009  -5.112  1.00 44.72           N  
ANISOU 9760  N   LYS D 953     5316   6632   5045   -378    529    139       N  
ATOM   9761  CA  LYS D 953    -125.685  16.218  -3.903  1.00 47.91           C  
ANISOU 9761  CA  LYS D 953     5662   7144   5396   -370    567    254       C  
ATOM   9762  C   LYS D 953    -124.654  15.145  -3.599  1.00 44.05           C  
ANISOU 9762  C   LYS D 953     5210   6580   4945   -373    596    343       C  
ATOM   9763  O   LYS D 953    -124.482  14.736  -2.443  1.00 42.19           O  
ANISOU 9763  O   LYS D 953     4931   6445   4655   -330    620    429       O  
ATOM   9764  CB  LYS D 953    -127.048  15.548  -4.084  1.00 54.53           C  
ANISOU 9764  CB  LYS D 953     6465   8008   6248   -451    596    322       C  
ATOM   9765  CG  LYS D 953    -128.184  16.538  -4.205  1.00 63.32           C  
ANISOU 9765  CG  LYS D 953     7528   9224   7308   -441    572    249       C  
ATOM   9766  CD  LYS D 953    -129.541  15.860  -4.335  1.00 69.40           C  
ANISOU 9766  CD  LYS D 953     8251  10030   8088   -522    601    320       C  
ATOM   9767  CE  LYS D 953    -130.642  16.877  -4.576  1.00 79.32           C  
ANISOU 9767  CE  LYS D 953     9462  11384   9293   -509    574    237       C  
ATOM   9768  NZ  LYS D 953    -131.212  17.419  -3.306  1.00 83.37           N  
ANISOU 9768  NZ  LYS D 953     9883  12104   9691   -435    575    254       N  
ATOM   9769  N   THR D 954    -123.977  14.698  -4.654  1.00 41.23           N  
ANISOU 9769  N   THR D 954     4931   6055   4679   -418    593    321       N  
ATOM   9770  CA  THR D 954    -122.958  13.692  -4.537  1.00 43.96           C  
ANISOU 9770  CA  THR D 954     5321   6310   5073   -420    616    392       C  
ATOM   9771  C   THR D 954    -121.645  14.266  -5.043  1.00 44.75           C  
ANISOU 9771  C   THR D 954     5477   6333   5192   -375    585    305       C  
ATOM   9772  O   THR D 954    -121.608  14.955  -6.077  1.00 47.01           O  
ANISOU 9772  O   THR D 954     5797   6557   5510   -389    557    210       O  
ATOM   9773  CB  THR D 954    -123.343  12.462  -5.378  1.00 44.91           C  
ANISOU 9773  CB  THR D 954     5477   6291   5294   -518    640    448       C  
ATOM   9774  OG1 THR D 954    -124.598  11.952  -4.926  1.00 44.90           O  
ANISOU 9774  OG1 THR D 954     5415   6359   5286   -568    667    532       O  
ATOM   9775  CG2 THR D 954    -122.300  11.375  -5.269  1.00 45.68           C  
ANISOU 9775  CG2 THR D 954     5620   6284   5451   -517    661    520       C  
ATOM   9776  N   THR D 955    -120.582  13.999  -4.294  1.00 47.47           N  
ANISOU 9776  N   THR D 955     5827   6694   5517   -317    593    343       N  
ATOM   9777  CA  THR D 955    -119.266  14.493  -4.611  1.00 48.70           C  
ANISOU 9777  CA  THR D 955     6025   6790   5687   -270    567    272       C  
ATOM   9778  C   THR D 955    -118.261  13.361  -4.433  1.00 53.57           C  
ANISOU 9778  C   THR D 955     6681   7330   6341   -264    593    352       C  
ATOM   9779  O   THR D 955    -118.485  12.474  -3.621  1.00 51.55           O  
ANISOU 9779  O   THR D 955     6400   7115   6071   -264    627    463       O  
ATOM   9780  CB  THR D 955    -118.872  15.678  -3.723  1.00 49.77           C  
ANISOU 9780  CB  THR D 955     6113   7054   5745   -179    534    206       C  
ATOM   9781  OG1 THR D 955    -117.626  16.197  -4.187  1.00 53.38           O  
ANISOU 9781  OG1 THR D 955     6609   7438   6235   -147    506    133       O  
ATOM   9782  CG2 THR D 955    -118.695  15.275  -2.243  1.00 50.03           C  
ANISOU 9782  CG2 THR D 955     6089   7221   5698   -115    556    287       C  
ATOM   9783  N   PRO D 956    -117.170  13.356  -5.230  1.00 59.95           N  
ANISOU 9783  N   PRO D 956     7550   8027   7201   -258    579    302       N  
ATOM   9784  CA  PRO D 956    -116.143  12.343  -4.973  1.00 59.72           C  
ANISOU 9784  CA  PRO D 956     7555   7937   7200   -238    600    371       C  
ATOM   9785  C   PRO D 956    -115.568  12.505  -3.562  1.00 58.23           C  
ANISOU 9785  C   PRO D 956     7318   7877   6930   -152    605    414       C  
ATOM   9786  O   PRO D 956    -115.345  13.625  -3.118  1.00 55.72           O  
ANISOU 9786  O   PRO D 956     6964   7656   6553    -95    574    338       O  
ATOM   9787  CB  PRO D 956    -115.089  12.633  -6.060  1.00 59.46           C  
ANISOU 9787  CB  PRO D 956     7580   7796   7216   -234    577    288       C  
ATOM   9788  CG  PRO D 956    -115.865  13.268  -7.185  1.00 61.94           C  
ANISOU 9788  CG  PRO D 956     7904   8073   7558   -286    557    210       C  
ATOM   9789  CD  PRO D 956    -116.852  14.142  -6.445  1.00 61.40           C  
ANISOU 9789  CD  PRO D 956     7771   8134   7422   -273    547    195       C  
ATOM   9790  N   ASP D 957    -115.328  11.387  -2.886  1.00 56.88           N  
ANISOU 9790  N   ASP D 957     7144   7705   6762   -141    640    533       N  
ATOM   9791  CA  ASP D 957    -114.822  11.386  -1.522  1.00 58.50           C  
ANISOU 9791  CA  ASP D 957     7299   8046   6883    -55    650    590       C  
ATOM   9792  C   ASP D 957    -113.486  12.127  -1.410  1.00 58.29           C  
ANISOU 9792  C   ASP D 957     7281   8039   6827     20    617    501       C  
ATOM   9793  O   ASP D 957    -112.492  11.662  -1.939  1.00 51.53           O  
ANISOU 9793  O   ASP D 957     6480   7075   6024     21    618    499       O  
ATOM   9794  CB  ASP D 957    -114.635   9.943  -1.070  1.00 63.35           C  
ANISOU 9794  CB  ASP D 957     7922   8617   7530    -62    695    742       C  
ATOM   9795  CG  ASP D 957    -114.269   9.824   0.398  1.00 68.32           C  
ANISOU 9795  CG  ASP D 957     8489   9408   8062     29    713    828       C  
ATOM   9796  OD1 ASP D 957    -113.882  10.831   1.029  1.00 66.80           O  
ANISOU 9796  OD1 ASP D 957     8253   9351   7779    106    685    750       O  
ATOM   9797  OD2 ASP D 957    -114.376   8.694   0.918  1.00 75.27           O  
ANISOU 9797  OD2 ASP D 957     9358  10279   8961     24    755    976       O  
ATOM   9798  N   PRO D 958    -113.462  13.271  -0.704  1.00 63.67           N  
ANISOU 9798  N   PRO D 958     7904   8861   7428     84    585    424       N  
ATOM   9799  CA  PRO D 958    -112.239  14.079  -0.585  1.00 65.27           C  
ANISOU 9799  CA  PRO D 958     8104   9082   7614    151    547    328       C  
ATOM   9800  C   PRO D 958    -111.044  13.332   0.019  1.00 64.66           C  
ANISOU 9800  C   PRO D 958     8034   9016   7518    211    564    392       C  
ATOM   9801  O   PRO D 958    -109.917  13.676  -0.273  1.00 61.36           O  
ANISOU 9801  O   PRO D 958     7639   8555   7121    240    540    326       O  
ATOM   9802  CB  PRO D 958    -112.657  15.227   0.336  1.00 63.06           C  
ANISOU 9802  CB  PRO D 958     7742   8971   7247    215    513    252       C  
ATOM   9803  CG  PRO D 958    -114.136  15.294   0.242  1.00 63.16           C  
ANISOU 9803  CG  PRO D 958     7731   9018   7247    164    525    275       C  
ATOM   9804  CD  PRO D 958    -114.612  13.905  -0.029  1.00 66.50           C  
ANISOU 9804  CD  PRO D 958     8190   9363   7713     97    579    413       C  
ATOM   9805  N   SER D 959    -111.290  12.320   0.842  1.00 71.64           N  
ANISOU 9805  N   SER D 959     8897   9959   8366    230    606    526       N  
ATOM   9806  CA  SER D 959    -110.195  11.563   1.467  1.00 75.20           C  
ANISOU 9806  CA  SER D 959     9350  10427   8794    294    624    601       C  
ATOM   9807  C   SER D 959    -109.445  10.713   0.444  1.00 77.75           C  
ANISOU 9807  C   SER D 959     9760  10560   9219    250    637    623       C  
ATOM   9808  O   SER D 959    -108.300  10.314   0.685  1.00 75.54           O  
ANISOU 9808  O   SER D 959     9495  10271   8935    304    640    645       O  
ATOM   9809  CB  SER D 959    -110.709  10.659   2.604  1.00 71.97           C  
ANISOU 9809  CB  SER D 959     8890  10130   8324    326    670    761       C  
ATOM   9810  N   ALA D 960    -110.098  10.413  -0.684  1.00 78.71           N  
ANISOU 9810  N   ALA D 960     9935  10542   9430    157    644    615       N  
ATOM   9811  CA  ALA D 960    -109.465   9.646  -1.755  1.00 79.47           C  
ANISOU 9811  CA  ALA D 960    10109  10463   9622    118    650    617       C  
ATOM   9812  C   ALA D 960    -108.847  10.528  -2.843  1.00 74.79           C  
ANISOU 9812  C   ALA D 960     9552   9803   9063    104    612    480       C  
ATOM   9813  O   ALA D 960    -108.300   9.999  -3.799  1.00 80.29           O  
ANISOU 9813  O   ALA D 960    10307  10371   9828     79    613    467       O  
ATOM   9814  CB  ALA D 960    -110.457   8.667  -2.367  1.00 82.14           C  
ANISOU 9814  CB  ALA D 960    10479  10685  10043     31    677    687       C  
ATOM   9815  N   ASN D 961    -108.924  11.854  -2.713  1.00 68.55           N  
ANISOU 9815  N   ASN D 961     8721   9097   8227    124    577    382       N  
ATOM   9816  CA  ASN D 961    -108.258  12.747  -3.660  1.00 70.36           C  
ANISOU 9816  CA  ASN D 961     8972   9269   8492    116    542    269       C  
ATOM   9817  C   ASN D 961    -106.768  12.457  -3.641  1.00 67.49           C  
ANISOU 9817  C   ASN D 961     8629   8880   8135    169    539    267       C  
ATOM   9818  O   ASN D 961    -106.206  12.194  -2.584  1.00 66.01           O  
ANISOU 9818  O   ASN D 961     8411   8777   7893    237    546    310       O  
ATOM   9819  CB  ASN D 961    -108.496  14.236  -3.345  1.00 73.10           C  
ANISOU 9819  CB  ASN D 961     9263   9712   8801    139    501    170       C  
ATOM   9820  CG  ASN D 961    -109.923  14.714  -3.726  1.00 78.66           C  
ANISOU 9820  CG  ASN D 961     9955  10420   9512     80    497    147       C  
ATOM   9821  OD1 ASN D 961    -110.889  13.943  -3.765  1.00 81.41           O  
ANISOU 9821  OD1 ASN D 961    10313  10751   9866     35    527    219       O  
ATOM   9822  ND2 ASN D 961    -110.039  15.994  -4.053  1.00 81.81           N  
ANISOU 9822  ND2 ASN D 961    10330  10835   9919     80    458     48       N  
ATOM   9823  N   ILE D 962    -106.146  12.471  -4.814  1.00 58.99           N  
ANISOU 9823  N   ILE D 962     7599   7696   7119    143    531    220       N  
ATOM   9824  CA  ILE D 962    -104.706  12.304  -4.925  1.00 59.01           C  
ANISOU 9824  CA  ILE D 962     7616   7676   7128    191    525    207       C  
ATOM   9825  C   ILE D 962    -104.114  13.430  -5.779  1.00 63.16           C  
ANISOU 9825  C   ILE D 962     8135   8180   7682    181    492    107       C  
ATOM   9826  O   ILE D 962    -104.812  14.016  -6.593  1.00 68.91           O  
ANISOU 9826  O   ILE D 962     8869   8871   8442    127    481     65       O  
ATOM   9827  CB  ILE D 962    -104.334  10.944  -5.554  1.00 57.99           C  
ANISOU 9827  CB  ILE D 962     7552   7433   7050    178    554    267       C  
ATOM   9828  CG1 ILE D 962    -104.895  10.821  -6.998  1.00 54.94           C  
ANISOU 9828  CG1 ILE D 962     7211   6934   6729    105    553    230       C  
ATOM   9829  CG2 ILE D 962    -104.763   9.802  -4.643  1.00 59.28           C  
ANISOU 9829  CG2 ILE D 962     7715   7609   7199    193    587    382       C  
ATOM   9830  CD1 ILE D 962    -103.789  10.815  -7.998  1.00 56.13           C  
ANISOU 9830  CD1 ILE D 962     7392   7024   6911    119    544    182       C  
ATOM   9831  N   SER D 963    -102.836  13.748  -5.582  1.00 62.90           N  
ANISOU 9831  N   SER D 963     8085   8174   7641    233    475     76       N  
ATOM   9832  CA  SER D 963    -102.171  14.780  -6.378  1.00 61.54           C  
ANISOU 9832  CA  SER D 963     7899   7978   7507    222    446     -2       C  
ATOM   9833  C   SER D 963    -101.321  14.083  -7.424  1.00 61.43           C  
ANISOU 9833  C   SER D 963     7934   7877   7529    217    462     13       C  
ATOM   9834  O   SER D 963    -100.467  13.270  -7.087  1.00 66.78           O  
ANISOU 9834  O   SER D 963     8627   8556   8191    263    476     50       O  
ATOM   9835  CB  SER D 963    -101.373  15.757  -5.497  1.00 58.27           C  
ANISOU 9835  CB  SER D 963     7418   7655   7068    277    410    -60       C  
ATOM   9836  N   LEU D 964    -101.584  14.391  -8.695  1.00 67.94           N  
ANISOU 9836  N   LEU D 964     8780   8636   8399    166    460    -16       N  
ATOM   9837  CA  LEU D 964    -100.885  13.794  -9.845  1.00 74.54           C  
ANISOU 9837  CA  LEU D 964     9657   9401   9264    163    473    -12       C  
ATOM   9838  C   LEU D 964    -100.118  14.925 -10.511  1.00 83.56           C  
ANISOU 9838  C   LEU D 964    10762  10556  10431    161    451    -61       C  
ATOM   9839  O   LEU D 964    -100.716  15.854 -11.084  1.00 83.12           O  
ANISOU 9839  O   LEU D 964    10687  10495  10401    119    437    -91       O  
ATOM   9840  CB  LEU D 964    -101.850  13.161 -10.849  1.00 74.21           C  
ANISOU 9840  CB  LEU D 964     9662   9286   9248    110    490     -3       C  
ATOM   9841  CG  LEU D 964    -101.267  12.554 -12.118  1.00 73.89           C  
ANISOU 9841  CG  LEU D 964     9658   9183   9232    112    499    -14       C  
ATOM   9842  CD1 LEU D 964    -100.374  11.383 -11.762  1.00 79.63           C  
ANISOU 9842  CD1 LEU D 964    10415   9885   9955    164    514     20       C  
ATOM   9843  CD2 LEU D 964    -102.398  12.110 -13.016  1.00 70.36           C  
ANISOU 9843  CD2 LEU D 964     9244   8680   8809     59    507    -23       C  
ATOM   9844  N   ASP D 965     -98.794  14.857 -10.390  1.00 87.45           N  
ANISOU 9844  N   ASP D 965    11240  11068  10918    207    447    -63       N  
ATOM   9845  CA  ASP D 965     -97.889  15.857 -10.910  1.00 85.29           C  
ANISOU 9845  CA  ASP D 965    10922  10811  10675    209    428    -97       C  
ATOM   9846  C   ASP D 965     -98.368  17.270 -10.547  1.00 74.00           C  
ANISOU 9846  C   ASP D 965     9435   9410   9272    183    395   -139       C  
ATOM   9847  O   ASP D 965     -98.416  18.174 -11.386  1.00 69.23           O  
ANISOU 9847  O   ASP D 965     8806   8785   8713    148    382   -156       O  
ATOM   9848  CB  ASP D 965     -97.685  15.607 -12.398  1.00 93.68           C  
ANISOU 9848  CB  ASP D 965    12011  11826  11758    188    444    -90       C  
ATOM   9849  CG  ASP D 965     -97.039  14.215 -12.690  1.00 98.70           C  
ANISOU 9849  CG  ASP D 965    12696  12434  12371    228    468    -65       C  
ATOM   9850  OD1 ASP D 965     -96.233  13.774 -11.846  1.00 99.58           O  
ANISOU 9850  OD1 ASP D 965    12803  12572  12459    279    469    -51       O  
ATOM   9851  OD2 ASP D 965     -97.337  13.553 -13.730  1.00 95.25           O  
ANISOU 9851  OD2 ASP D 965    12299  11952  11939    215    484    -63       O  
ATOM   9852  N   GLY D 966     -98.727  17.423  -9.269  1.00 65.01           N  
ANISOU 9852  N   GLY D 966     8273   8324   8104    206    379   -154       N  
ATOM   9853  CA  GLY D 966     -99.103  18.708  -8.688  1.00 61.04           C  
ANISOU 9853  CA  GLY D 966     7710   7859   7625    199    340   -210       C  
ATOM   9854  C   GLY D 966    -100.576  19.057  -8.761  1.00 58.44           C  
ANISOU 9854  C   GLY D 966     7388   7520   7297    158    337   -217       C  
ATOM   9855  O   GLY D 966    -101.010  20.049  -8.190  1.00 54.94           O  
ANISOU 9855  O   GLY D 966     6897   7110   6867    159    303   -268       O  
ATOM   9856  N   VAL D 967    -101.355  18.257  -9.476  1.00 52.20           N  
ANISOU 9856  N   VAL D 967     6654   6683   6495    123    370   -174       N  
ATOM   9857  CA  VAL D 967    -102.747  18.587  -9.706  1.00 44.54           C  
ANISOU 9857  CA  VAL D 967     5691   5704   5530     79    369   -181       C  
ATOM   9858  C   VAL D 967    -103.644  17.638  -8.927  1.00 44.03           C  
ANISOU 9858  C   VAL D 967     5652   5666   5412     83    391   -143       C  
ATOM   9859  O   VAL D 967    -103.426  16.432  -8.948  1.00 40.84           O  
ANISOU 9859  O   VAL D 967     5291   5238   4989     92    421    -93       O  
ATOM   9860  CB  VAL D 967    -103.100  18.472 -11.197  1.00 40.35           C  
ANISOU 9860  CB  VAL D 967     5195   5106   5029     31    386   -165       C  
ATOM   9861  CG1 VAL D 967    -104.565  18.819 -11.428  1.00 37.72           C  
ANISOU 9861  CG1 VAL D 967     4865   4770   4697    -11    383   -173       C  
ATOM   9862  CG2 VAL D 967    -102.194  19.382 -12.027  1.00 40.80           C  
ANISOU 9862  CG2 VAL D 967     5219   5144   5138     28    370   -181       C  
ATOM   9863  N   ASP D 968    -104.701  18.161  -8.322  1.00 40.82           N  
ANISOU 9863  N   ASP D 968     5217   5305   4986     75    377   -163       N  
ATOM   9864  CA  ASP D 968    -105.629  17.293  -7.639  1.00 43.39           C  
ANISOU 9864  CA  ASP D 968     5559   5663   5264     72    402   -115       C  
ATOM   9865  C   ASP D 968    -106.527  16.478  -8.600  1.00 43.30           C  
ANISOU 9865  C   ASP D 968     5600   5581   5271     13    432    -75       C  
ATOM   9866  O   ASP D 968    -107.087  17.009  -9.552  1.00 38.09           O  
ANISOU 9866  O   ASP D 968     4946   4884   4642    -30    424   -103       O  
ATOM   9867  CB  ASP D 968    -106.462  18.107  -6.680  1.00 45.99           C  
ANISOU 9867  CB  ASP D 968     5834   6081   5560     88    377   -151       C  
ATOM   9868  CG  ASP D 968    -105.627  18.702  -5.553  1.00 52.93           C  
ANISOU 9868  CG  ASP D 968     6655   7044   6411    158    345   -196       C  
ATOM   9869  OD1 ASP D 968    -104.565  18.104  -5.186  1.00 56.89           O  
ANISOU 9869  OD1 ASP D 968     7163   7557   6895    198    356   -170       O  
ATOM   9870  OD2 ASP D 968    -106.037  19.765  -5.037  1.00 55.64           O  
ANISOU 9870  OD2 ASP D 968     6944   7445   6750    175    307   -263       O  
ATOM   9871  N   VAL D 969    -106.659  15.188  -8.307  1.00 39.55           N  
ANISOU 9871  N   VAL D 969     5159   5087   4781     13    463    -10       N  
ATOM   9872  CA  VAL D 969    -107.490  14.289  -9.071  1.00 39.99           C  
ANISOU 9872  CA  VAL D 969     5259   5073   4863    -42    487     23       C  
ATOM   9873  C   VAL D 969    -108.535  13.728  -8.127  1.00 38.96           C  
ANISOU 9873  C   VAL D 969     5114   4985   4703    -53    506     81       C  
ATOM   9874  O   VAL D 969    -108.216  12.924  -7.239  1.00 40.16           O  
ANISOU 9874  O   VAL D 969     5266   5160   4833    -20    525    146       O  
ATOM   9875  CB  VAL D 969    -106.671  13.131  -9.639  1.00 40.88           C  
ANISOU 9875  CB  VAL D 969     5423   5105   5005    -34    507     53       C  
ATOM   9876  CG1 VAL D 969    -107.522  12.299 -10.585  1.00 40.76           C  
ANISOU 9876  CG1 VAL D 969     5448   5009   5031    -91    522     62       C  
ATOM   9877  CG2 VAL D 969    -105.429  13.665 -10.337  1.00 40.07           C  
ANISOU 9877  CG2 VAL D 969     5321   4986   4916     -6    492      8       C  
ATOM   9878  N   PRO D 970    -109.774  14.182  -8.273  1.00 37.82           N  
ANISOU 9878  N   PRO D 970     4952   4864   4554    -95    501     65       N  
ATOM   9879  CA  PRO D 970    -110.825  13.773  -7.326  1.00 39.02           C  
ANISOU 9879  CA  PRO D 970     5076   5077   4671   -106    518    123       C  
ATOM   9880  C   PRO D 970    -111.420  12.426  -7.722  1.00 39.42           C  
ANISOU 9880  C   PRO D 970     5165   5046   4766   -158    549    190       C  
ATOM   9881  O   PRO D 970    -112.561  12.350  -8.132  1.00 36.67           O  
ANISOU 9881  O   PRO D 970     4813   4684   4434   -215    554    189       O  
ATOM   9882  CB  PRO D 970    -111.855  14.887  -7.454  1.00 36.84           C  
ANISOU 9882  CB  PRO D 970     4764   4856   4379   -128    496     67       C  
ATOM   9883  CG  PRO D 970    -111.732  15.301  -8.902  1.00 37.15           C  
ANISOU 9883  CG  PRO D 970     4835   4812   4469   -164    482      8       C  
ATOM   9884  CD  PRO D 970    -110.279  15.121  -9.283  1.00 36.15           C  
ANISOU 9884  CD  PRO D 970     4737   4634   4366   -132    480     -1       C  
ATOM   9885  N   LEU D 971    -110.631  11.371  -7.592  1.00 43.66           N  
ANISOU 9885  N   LEU D 971     5734   5526   5329   -139    568    244       N  
ATOM   9886  CA  LEU D 971    -111.038  10.075  -8.091  1.00 46.69           C  
ANISOU 9886  CA  LEU D 971     6157   5806   5778   -187    590    295       C  
ATOM   9887  C   LEU D 971    -111.766   9.217  -7.042  1.00 50.96           C  
ANISOU 9887  C   LEU D 971     6673   6374   6317   -199    620    407       C  
ATOM   9888  O   LEU D 971    -111.960   8.028  -7.255  1.00 50.98           O  
ANISOU 9888  O   LEU D 971     6702   6280   6387   -233    638    466       O  
ATOM   9889  CB  LEU D 971    -109.844   9.341  -8.716  1.00 49.12           C  
ANISOU 9889  CB  LEU D 971     6516   6016   6131   -162    590    286       C  
ATOM   9890  CG  LEU D 971    -108.517   9.283  -7.979  1.00 50.72           C  
ANISOU 9890  CG  LEU D 971     6717   6254   6301    -84    593    312       C  
ATOM   9891  CD1 LEU D 971    -108.695   8.564  -6.659  1.00 52.68           C  
ANISOU 9891  CD1 LEU D 971     6941   6548   6527    -59    619    423       C  
ATOM   9892  CD2 LEU D 971    -107.473   8.589  -8.839  1.00 47.59           C  
ANISOU 9892  CD2 LEU D 971     6372   5757   5954    -66    590    289       C  
ATOM   9893  N   GLY D 972    -112.141   9.805  -5.906  1.00 51.38           N  
ANISOU 9893  N   GLY D 972     6668   6559   6294   -168    623    439       N  
ATOM   9894  CA  GLY D 972    -112.907   9.086  -4.887  1.00 52.86           C  
ANISOU 9894  CA  GLY D 972     6818   6800   6467   -177    655    557       C  
ATOM   9895  C   GLY D 972    -114.278   8.674  -5.397  1.00 55.16           C  
ANISOU 9895  C   GLY D 972     7105   7042   6811   -265    666    578       C  
ATOM   9896  O   GLY D 972    -114.834   9.308  -6.319  1.00 57.38           O  
ANISOU 9896  O   GLY D 972     7395   7301   7105   -308    644    487       O  
ATOM   9897  N   THR D 973    -114.803   7.572  -4.861  1.00 51.48           N  
ANISOU 9897  N   THR D 973     6624   6552   6385   -294    698    700       N  
ATOM   9898  CA  THR D 973    -116.171   7.172  -5.175  1.00 53.41           C  
ANISOU 9898  CA  THR D 973     6849   6766   6680   -381    709    731       C  
ATOM   9899  C   THR D 973    -117.133   8.195  -4.551  1.00 50.19           C  
ANISOU 9899  C   THR D 973     6373   6520   6177   -375    707    719       C  
ATOM   9900  O   THR D 973    -116.822   8.877  -3.571  1.00 45.23           O  
ANISOU 9900  O   THR D 973     5702   6032   5451   -302    706    726       O  
ATOM   9901  CB  THR D 973    -116.526   5.770  -4.631  1.00 53.67           C  
ANISOU 9901  CB  THR D 973     6868   6737   6786   -415    746    882       C  
ATOM   9902  OG1 THR D 973    -116.140   5.704  -3.260  1.00 52.64           O  
ANISOU 9902  OG1 THR D 973     6693   6729   6580   -344    772    992       O  
ATOM   9903  CG2 THR D 973    -115.811   4.660  -5.391  1.00 54.13           C  
ANISOU 9903  CG2 THR D 973     6994   6611   6964   -434    743    884       C  
ATOM   9904  N   GLY D 974    -118.292   8.315  -5.172  1.00 51.70           N  
ANISOU 9904  N   GLY D 974     6552   6695   6398   -448    702    687       N  
ATOM   9905  CA  GLY D 974    -119.275   9.297  -4.764  1.00 52.76           C  
ANISOU 9905  CA  GLY D 974     6625   6972   6449   -445    695    659       C  
ATOM   9906  C   GLY D 974    -119.871   9.087  -3.384  1.00 55.94           C  
ANISOU 9906  C   GLY D 974     6950   7518   6786   -422    727    782       C  
ATOM   9907  O   GLY D 974    -120.396   8.010  -3.101  1.00 57.26           O  
ANISOU 9907  O   GLY D 974     7099   7650   7009   -471    761    904       O  
ATOM   9908  N   ILE D 975    -119.811  10.144  -2.567  1.00 51.78           N  
ANISOU 9908  N   ILE D 975     6375   7156   6145   -346    714    745       N  
ATOM   9909  CA  ILE D 975    -120.469  10.199  -1.285  1.00 50.69           C  
ANISOU 9909  CA  ILE D 975     6149   7195   5915   -309    738    836       C  
ATOM   9910  C   ILE D 975    -121.292  11.466  -1.206  1.00 47.00           C  
ANISOU 9910  C   ILE D 975     5633   6857   5367   -290    710    738       C  
ATOM   9911  O   ILE D 975    -121.272  12.308  -2.106  1.00 47.25           O  
ANISOU 9911  O   ILE D 975     5700   6834   5418   -302    672    608       O  
ATOM   9912  CB  ILE D 975    -119.473  10.217  -0.119  1.00 52.81           C  
ANISOU 9912  CB  ILE D 975     6391   7572   6104   -206    746    886       C  
ATOM   9913  CG1 ILE D 975    -118.700  11.538  -0.104  1.00 55.90           C  
ANISOU 9913  CG1 ILE D 975     6788   8023   6429   -128    698    736       C  
ATOM   9914  CG2 ILE D 975    -118.537   9.021  -0.220  1.00 53.25           C  
ANISOU 9914  CG2 ILE D 975     6499   7494   6238   -213    770    976       C  
ATOM   9915  CD1 ILE D 975    -117.836  11.724   1.120  1.00 56.06           C  
ANISOU 9915  CD1 ILE D 975     6765   8183   6355    -18    698    761       C  
ATOM   9916  N   SER D 976    -122.063  11.555  -0.142  1.00 48.06           N  
ANISOU 9916  N   SER D 976     5682   7166   5414   -260    730    810       N  
ATOM   9917  CA  SER D 976    -122.975  12.644   0.047  1.00 51.77           C  
ANISOU 9917  CA  SER D 976     6093   7772   5804   -238    706    730       C  
ATOM   9918  C   SER D 976    -122.168  13.879   0.359  1.00 50.24           C  
ANISOU 9918  C   SER D 976     5896   7652   5540   -138    659    599       C  
ATOM   9919  O   SER D 976    -121.228  13.810   1.139  1.00 50.16           O  
ANISOU 9919  O   SER D 976     5875   7699   5485    -63    660    621       O  
ATOM   9920  CB  SER D 976    -123.921  12.342   1.208  1.00 54.57           C  
ANISOU 9920  CB  SER D 976     6347   8313   6073   -218    742    852       C  
ATOM   9921  OG  SER D 976    -124.857  13.399   1.328  1.00 58.64           O  
ANISOU 9921  OG  SER D 976     6807   8961   6513   -195    716    764       O  
ATOM   9922  N   SER D 977    -122.517  14.991  -0.276  1.00 46.09           N  
ANISOU 9922  N   SER D 977     5378   7118   5016   -140    616    463       N  
ATOM   9923  CA  SER D 977    -121.817  16.230  -0.048  1.00 45.20           C  
ANISOU 9923  CA  SER D 977     5257   7057   4860    -54    565    331       C  
ATOM   9924  C   SER D 977    -122.378  16.945   1.143  1.00 48.16           C  
ANISOU 9924  C   SER D 977     5535   7650   5114     32    550    306       C  
ATOM   9925  O   SER D 977    -121.777  17.899   1.631  1.00 47.21           O  
ANISOU 9925  O   SER D 977     5389   7602   4947    120    506    202       O  
ATOM   9926  CB  SER D 977    -121.957  17.128  -1.266  1.00 47.38           C  
ANISOU 9926  CB  SER D 977     5580   7223   5200    -91    525    205       C  
ATOM   9927  OG  SER D 977    -123.322  17.384  -1.549  1.00 43.81           O  
ANISOU 9927  OG  SER D 977     5094   6816   4735   -133    526    196       O  
ATOM   9928  N   GLY D 978    -123.559  16.524   1.591  1.00 51.23           N  
ANISOU 9928  N   GLY D 978     5864   8149   5454      9    584    394       N  
ATOM   9929  CA  GLY D 978    -124.256  17.220   2.660  1.00 53.04           C  
ANISOU 9929  CA  GLY D 978     5991   8603   5558     92    570    367       C  
ATOM   9930  C   GLY D 978    -125.025  18.456   2.191  1.00 54.37           C  
ANISOU 9930  C   GLY D 978     6144   8795   5720    100    521    225       C  
ATOM   9931  O   GLY D 978    -125.589  19.171   3.017  1.00 53.14           O  
ANISOU 9931  O   GLY D 978     5904   8823   5463    179    499    174       O  
ATOM   9932  N   VAL D 979    -125.051  18.696   0.877  1.00 50.30           N  
ANISOU 9932  N   VAL D 979     5703   8100   5307     26    504    163       N  
ATOM   9933  CA  VAL D 979    -125.797  19.784   0.310  1.00 51.02           C  
ANISOU 9933  CA  VAL D 979     5785   8194   5406     26    462     46       C  
ATOM   9934  C   VAL D 979    -127.092  19.172  -0.193  1.00 51.89           C  
ANISOU 9934  C   VAL D 979     5885   8300   5531    -65    499    122       C  
ATOM   9935  O   VAL D 979    -127.081  18.384  -1.148  1.00 51.12           O  
ANISOU 9935  O   VAL D 979     5852   8049   5524   -161    524    175       O  
ATOM   9936  CB  VAL D 979    -125.045  20.420  -0.864  1.00 54.08           C  
ANISOU 9936  CB  VAL D 979     6254   8397   5896      1    423    -56       C  
ATOM   9937  CG1 VAL D 979    -125.917  21.433  -1.585  1.00 55.67           C  
ANISOU 9937  CG1 VAL D 979     6449   8586   6117     -9    387   -154       C  
ATOM   9938  CG2 VAL D 979    -123.766  21.074  -0.372  1.00 54.23           C  
ANISOU 9938  CG2 VAL D 979     6275   8418   5911     86    383   -137       C  
ATOM   9939  N   ASN D 980    -128.214  19.495   0.451  1.00 52.12           N  
ANISOU 9939  N   ASN D 980     5829   8503   5473    -34    500    126       N  
ATOM   9940  CA  ASN D 980    -129.509  18.930  -0.002  1.00 50.19           C  
ANISOU 9940  CA  ASN D 980     5563   8265   5242   -123    534    199       C  
ATOM   9941  C   ASN D 980    -130.258  19.892  -0.940  1.00 48.66           C  
ANISOU 9941  C   ASN D 980     5381   8032   5074   -141    495     82       C  
ATOM   9942  O   ASN D 980    -130.978  19.433  -1.819  1.00 51.81           O  
ANISOU 9942  O   ASN D 980     5802   8354   5529   -234    513    114       O  
ATOM   9943  CB  ASN D 980    -130.429  18.414   1.132  1.00 48.87           C  
ANISOU 9943  CB  ASN D 980     5292   8304   4973   -105    575    314       C  
ATOM   9944  CG  ASN D 980    -131.701  17.675   0.581  1.00 48.08           C  
ANISOU 9944  CG  ASN D 980     5171   8186   4910   -217    614    402       C  
ATOM   9945  OD1 ASN D 980    -131.629  16.903  -0.400  1.00 48.01           O  
ANISOU 9945  OD1 ASN D 980     5230   7998   5014   -321    632    442       O  
ATOM   9946  ND2 ASN D 980    -132.860  17.958   1.172  1.00 42.15           N  
ANISOU 9946  ND2 ASN D 980     4324   7622   4067   -192    621    420       N  
ATOM   9947  N   ASP D 981    -130.132  21.199  -0.704  1.00 45.91           N  
ANISOU 9947  N   ASP D 981     5012   7746   4688    -50    439    -50       N  
ATOM   9948  CA  ASP D 981    -130.909  22.205  -1.409  1.00 45.26           C  
ANISOU 9948  CA  ASP D 981     4925   7654   4619    -47    399   -156       C  
ATOM   9949  C   ASP D 981    -130.222  22.672  -2.680  1.00 43.45           C  
ANISOU 9949  C   ASP D 981     4785   7224   4498    -81    369   -230       C  
ATOM   9950  O   ASP D 981    -129.873  23.844  -2.825  1.00 39.94           O  
ANISOU 9950  O   ASP D 981     4346   6757   4072    -18    315   -345       O  
ATOM   9951  CB  ASP D 981    -131.213  23.403  -0.484  1.00 47.70           C  
ANISOU 9951  CB  ASP D 981     5154   8132   4836     75    350   -263       C  
ATOM   9952  CG  ASP D 981    -129.936  24.124   0.006  1.00 50.40           C  
ANISOU 9952  CG  ASP D 981     5509   8453   5187    166    303   -356       C  
ATOM   9953  OD1 ASP D 981    -128.889  23.459   0.228  1.00 48.79           O  
ANISOU 9953  OD1 ASP D 981     5342   8192   5005    157    325   -299       O  
ATOM   9954  OD2 ASP D 981    -129.987  25.362   0.147  1.00 54.97           O  
ANISOU 9954  OD2 ASP D 981     6060   9067   5760    246    242   -489       O  
ATOM   9955  N   THR D 982    -130.131  21.771  -3.648  1.00 44.66           N  
ANISOU 9955  N   THR D 982     5001   7238   4727   -181    403   -163       N  
ATOM   9956  CA  THR D 982    -129.456  22.075  -4.898  1.00 47.74           C  
ANISOU 9956  CA  THR D 982     5473   7452   5213   -214    382   -217       C  
ATOM   9957  C   THR D 982    -130.203  21.550  -6.110  1.00 47.07           C  
ANISOU 9957  C   THR D 982     5420   7285   5181   -310    402   -191       C  
ATOM   9958  O   THR D 982    -130.900  20.541  -6.040  1.00 52.60           O  
ANISOU 9958  O   THR D 982     6100   8012   5873   -376    442   -107       O  
ATOM   9959  CB  THR D 982    -128.023  21.504  -4.908  1.00 49.08           C  
ANISOU 9959  CB  THR D 982     5703   7512   5433   -218    394   -184       C  
ATOM   9960  OG1 THR D 982    -127.464  21.654  -6.210  1.00 49.83           O  
ANISOU 9960  OG1 THR D 982     5871   7446   5616   -259    381   -220       O  
ATOM   9961  CG2 THR D 982    -128.032  20.031  -4.564  1.00 51.72           C  
ANISOU 9961  CG2 THR D 982     6041   7843   5766   -276    449    -57       C  
ATOM   9962  N   SER D 983    -130.021  22.236  -7.235  1.00 44.92           N  
ANISOU 9962  N   SER D 983     5191   6911   4964   -317    373   -261       N  
ATOM   9963  CA  SER D 983    -130.578  21.804  -8.503  1.00 45.49           C  
ANISOU 9963  CA  SER D 983     5295   6903   5084   -398    386   -252       C  
ATOM   9964  C   SER D 983    -129.806  20.647  -9.143  1.00 44.45           C  
ANISOU 9964  C   SER D 983     5229   6639   5021   -465    415   -197       C  
ATOM   9965  O   SER D 983    -130.240  20.132 -10.158  1.00 47.11           O  
ANISOU 9965  O   SER D 983     5589   6914   5397   -532    426   -192       O  
ATOM   9966  CB  SER D 983    -130.616  22.986  -9.478  1.00 44.93           C  
ANISOU 9966  CB  SER D 983     5244   6785   5044   -369    345   -338       C  
ATOM   9967  OG  SER D 983    -131.265  24.123  -8.896  1.00 46.71           O  
ANISOU 9967  OG  SER D 983     5411   7119   5219   -298    310   -400       O  
ATOM   9968  N   LEU D 984    -128.686  20.228  -8.564  1.00 41.60           N  
ANISOU 9968  N   LEU D 984     4895   6240   4672   -443    426   -162       N  
ATOM   9969  CA  LEU D 984    -127.752  19.358  -9.277  1.00 40.56           C  
ANISOU 9969  CA  LEU D 984     4831   5969   4610   -488    443   -132       C  
ATOM   9970  C   LEU D 984    -127.500  18.060  -8.538  1.00 39.12           C  
ANISOU 9970  C   LEU D 984     4648   5781   4433   -518    483    -35       C  
ATOM   9971  O   LEU D 984    -127.271  18.055  -7.312  1.00 37.63           O  
ANISOU 9971  O   LEU D 984     4424   5680   4193   -470    491      5       O  
ATOM   9972  CB  LEU D 984    -126.403  20.075  -9.455  1.00 38.36           C  
ANISOU 9972  CB  LEU D 984     4593   5623   4357   -431    417   -182       C  
ATOM   9973  CG  LEU D 984    -126.317  21.282 -10.389  1.00 40.98           C  
ANISOU 9973  CG  LEU D 984     4938   5917   4714   -405    379   -262       C  
ATOM   9974  CD1 LEU D 984    -124.965  21.957 -10.236  1.00 42.10           C  
ANISOU 9974  CD1 LEU D 984     5103   6008   4884   -347    355   -295       C  
ATOM   9975  CD2 LEU D 984    -126.530  20.898 -11.850  1.00 39.15           C  
ANISOU 9975  CD2 LEU D 984     4746   5601   4528   -464    387   -268       C  
ATOM   9976  N   LEU D 985    -127.514  16.960  -9.274  1.00 40.11           N  
ANISOU 9976  N   LEU D 985     4811   5805   4624   -593    505      3       N  
ATOM   9977  CA  LEU D 985    -127.135  15.665  -8.703  1.00 45.65           C  
ANISOU 9977  CA  LEU D 985     5521   6467   5357   -624    540    101       C  
ATOM   9978  C   LEU D 985    -125.627  15.586  -8.456  1.00 42.23           C  
ANISOU 9978  C   LEU D 985     5137   5971   4939   -574    538    106       C  
ATOM   9979  O   LEU D 985    -125.174  15.065  -7.427  1.00 45.05           O  
ANISOU 9979  O   LEU D 985     5480   6361   5277   -548    560    181       O  
ATOM   9980  CB  LEU D 985    -127.579  14.518  -9.625  1.00 49.64           C  
ANISOU 9980  CB  LEU D 985     6050   6865   5945   -718    556    125       C  
ATOM   9981  CG  LEU D 985    -129.092  14.294  -9.814  1.00 53.75           C  
ANISOU 9981  CG  LEU D 985     6516   7440   6464   -784    563    136       C  
ATOM   9982  CD1 LEU D 985    -129.369  13.179 -10.814  1.00 54.54           C  
ANISOU 9982  CD1 LEU D 985     6642   7418   6662   -873    569    137       C  
ATOM   9983  CD2 LEU D 985    -129.780  13.969  -8.486  1.00 55.79           C  
ANISOU 9983  CD2 LEU D 985     6702   7820   6676   -786    593    238       C  
ATOM   9984  N   TYR D 986    -124.853  16.129  -9.383  1.00 39.23           N  
ANISOU 9984  N   TYR D 986     4806   5510   4588   -556    513     31       N  
ATOM   9985  CA  TYR D 986    -123.401  16.077  -9.297  1.00 37.81           C  
ANISOU 9985  CA  TYR D 986     4672   5267   4429   -512    509     28       C  
ATOM   9986  C   TYR D 986    -122.799  17.453  -9.529  1.00 35.41           C  
ANISOU 9986  C   TYR D 986     4371   4976   4106   -451    472    -56       C  
ATOM   9987  O   TYR D 986    -123.423  18.355 -10.122  1.00 35.30           O  
ANISOU 9987  O   TYR D 986     4342   4984   4086   -451    449   -116       O  
ATOM   9988  CB  TYR D 986    -122.863  15.077 -10.321  1.00 39.40           C  
ANISOU 9988  CB  TYR D 986     4934   5330   4707   -560    520     36       C  
ATOM   9989  CG  TYR D 986    -123.647  13.798 -10.273  1.00 39.38           C  
ANISOU 9989  CG  TYR D 986     4922   5295   4745   -632    548    104       C  
ATOM   9990  CD1 TYR D 986    -123.473  12.895  -9.229  1.00 40.07           C  
ANISOU 9990  CD1 TYR D 986     4994   5391   4838   -633    578    205       C  
ATOM   9991  CD2 TYR D 986    -124.608  13.512 -11.257  1.00 39.57           C  
ANISOU 9991  CD2 TYR D 986     4943   5284   4807   -699    544     71       C  
ATOM   9992  CE1 TYR D 986    -124.227  11.741  -9.168  1.00 40.89           C  
ANISOU 9992  CE1 TYR D 986     5082   5458   4996   -705    603    278       C  
ATOM   9993  CE2 TYR D 986    -125.360  12.356 -11.212  1.00 40.99           C  
ANISOU 9993  CE2 TYR D 986     5107   5428   5041   -771    565    130       C  
ATOM   9994  CZ  TYR D 986    -125.178  11.486 -10.150  1.00 41.96           C  
ANISOU 9994  CZ  TYR D 986     5214   5549   5179   -777    595    237       C  
ATOM   9995  OH  TYR D 986    -125.934  10.339 -10.103  1.00 46.85           O  
ANISOU 9995  OH  TYR D 986     5811   6121   5868   -854    615    305       O  
ATOM   9996  N   ASN D 987    -121.565  17.611  -9.061  1.00 33.01           N  
ANISOU 9996  N   ASN D 987     4083   4656   3802   -398    466    -57       N  
ATOM   9997  CA  ASN D 987    -120.848  18.866  -9.262  1.00 32.13           C  
ANISOU 9997  CA  ASN D 987     3973   4541   3694   -344    429   -132       C  
ATOM   9998  C   ASN D 987    -120.680  19.203 -10.744  1.00 30.80           C  
ANISOU 9998  C   ASN D 987     3842   4282   3577   -372    417   -175       C  
ATOM   9999  O   ASN D 987    -120.682  18.325 -11.601  1.00 27.82           O  
ANISOU 9999  O   ASN D 987     3503   3833   3234   -421    436   -154       O  
ATOM  10000  CB  ASN D 987    -119.467  18.792  -8.626  1.00 31.45           C  
ANISOU10000  CB  ASN D 987     3899   4440   3609   -293    427   -122       C  
ATOM  10001  CG  ASN D 987    -119.526  18.552  -7.132  1.00 31.49           C  
ANISOU10001  CG  ASN D 987     3860   4554   3552   -249    436    -81       C  
ATOM  10002  OD1 ASN D 987    -120.388  19.083  -6.456  1.00 31.45           O  
ANISOU10002  OD1 ASN D 987     3800   4657   3494   -226    426    -97       O  
ATOM  10003  ND2 ASN D 987    -118.587  17.807  -6.614  1.00 30.35           N  
ANISOU10003  ND2 ASN D 987     3732   4392   3406   -228    455    -31       N  
ATOM  10004  N   GLU D 988    -120.513  20.478 -11.013  1.00 29.93           N  
ANISOU10004  N   GLU D 988     3716   4180   3475   -336    383   -234       N  
ATOM  10005  CA  GLU D 988    -119.883  20.900 -12.241  1.00 30.34           C  
ANISOU10005  CA  GLU D 988     3799   4152   3576   -341    372   -260       C  
ATOM  10006  C   GLU D 988    -119.061  22.152 -11.978  1.00 28.91           C  
ANISOU10006  C   GLU D 988     3598   3970   3419   -284    336   -303       C  
ATOM  10007  O   GLU D 988    -119.221  22.815 -10.943  1.00 27.52           O  
ANISOU10007  O   GLU D 988     3378   3858   3219   -241    313   -333       O  
ATOM  10008  CB  GLU D 988    -120.889  21.112 -13.372  1.00 30.58           C  
ANISOU10008  CB  GLU D 988     3829   4178   3612   -379    370   -278       C  
ATOM  10009  CG  GLU D 988    -122.075  21.969 -13.033  1.00 31.59           C  
ANISOU10009  CG  GLU D 988     3909   4385   3710   -367    350   -308       C  
ATOM  10010  CD  GLU D 988    -123.145  21.862 -14.110  1.00 32.98           C  
ANISOU10010  CD  GLU D 988     4084   4564   3882   -411    356   -316       C  
ATOM  10011  OE1 GLU D 988    -123.313  22.829 -14.879  1.00 33.34           O  
ANISOU10011  OE1 GLU D 988     4120   4605   3943   -394    334   -346       O  
ATOM  10012  OE2 GLU D 988    -123.803  20.798 -14.185  1.00 34.98           O  
ANISOU10012  OE2 GLU D 988     4343   4824   4122   -462    381   -291       O  
ATOM  10013  N   TYR D 989    -118.140  22.425 -12.897  1.00 27.16           N  
ANISOU10013  N   TYR D 989     3400   3675   3244   -283    332   -306       N  
ATOM  10014  CA  TYR D 989    -117.152  23.448 -12.715  1.00 27.17           C  
ANISOU10014  CA  TYR D 989     3382   3653   3287   -239    301   -335       C  
ATOM  10015  C   TYR D 989    -117.115  24.239 -13.984  1.00 27.06           C  
ANISOU10015  C   TYR D 989     3369   3593   3322   -248    289   -340       C  
ATOM  10016  O   TYR D 989    -117.028  23.677 -15.061  1.00 27.75           O  
ANISOU10016  O   TYR D 989     3487   3646   3411   -278    313   -312       O  
ATOM  10017  CB  TYR D 989    -115.781  22.832 -12.439  1.00 27.35           C  
ANISOU10017  CB  TYR D 989     3430   3640   3321   -225    313   -313       C  
ATOM  10018  CG  TYR D 989    -115.720  21.937 -11.231  1.00 26.68           C  
ANISOU10018  CG  TYR D 989     3346   3602   3187   -212    330   -291       C  
ATOM  10019  CD1 TYR D 989    -116.034  20.609 -11.328  1.00 28.61           C  
ANISOU10019  CD1 TYR D 989     3625   3837   3409   -248    368   -240       C  
ATOM  10020  CD2 TYR D 989    -115.316  22.418 -10.001  1.00 29.34           C  
ANISOU10020  CD2 TYR D 989     3645   3996   3507   -159    307   -319       C  
ATOM  10021  CE1 TYR D 989    -115.992  19.772 -10.226  1.00 28.76           C  
ANISOU10021  CE1 TYR D 989     3640   3898   3388   -236    387   -201       C  
ATOM  10022  CE2 TYR D 989    -115.268  21.596  -8.886  1.00 29.93           C  
ANISOU10022  CE2 TYR D 989     3713   4131   3527   -139    325   -288       C  
ATOM  10023  CZ  TYR D 989    -115.603  20.267  -9.028  1.00 30.13           C  
ANISOU10023  CZ  TYR D 989     3774   4141   3532   -180    368   -219       C  
ATOM  10024  OH  TYR D 989    -115.553  19.436  -7.972  1.00 33.13           O  
ANISOU10024  OH  TYR D 989     4146   4577   3867   -161    390   -170       O  
ATOM  10025  N   ILE D 990    -117.139  25.554 -13.847  1.00 25.69           N  
ANISOU10025  N   ILE D 990     3155   3417   3188   -217    251   -376       N  
ATOM  10026  CA  ILE D 990    -117.142  26.431 -14.991  1.00 25.97           C  
ANISOU10026  CA  ILE D 990     3180   3410   3277   -220    239   -367       C  
ATOM  10027  C   ILE D 990    -116.055  27.519 -14.870  1.00 26.16           C  
ANISOU10027  C   ILE D 990     3174   3381   3384   -188    205   -380       C  
ATOM  10028  O   ILE D 990    -115.900  28.160 -13.813  1.00 26.35           O  
ANISOU10028  O   ILE D 990     3164   3417   3431   -152    169   -431       O  
ATOM  10029  CB  ILE D 990    -118.523  27.118 -15.159  1.00 25.29           C  
ANISOU10029  CB  ILE D 990     3067   3363   3179   -219    222   -390       C  
ATOM  10030  CG1 ILE D 990    -119.627  26.084 -15.227  1.00 25.18           C  
ANISOU10030  CG1 ILE D 990     3073   3404   3091   -255    252   -380       C  
ATOM  10031  CG2 ILE D 990    -118.562  27.939 -16.429  1.00 25.44           C  
ANISOU10031  CG2 ILE D 990     3076   3343   3248   -220    215   -364       C  
ATOM  10032  CD1 ILE D 990    -120.182  25.664 -13.881  1.00 25.56           C  
ANISOU10032  CD1 ILE D 990     3105   3521   3086   -246    252   -403       C  
ATOM  10033  N   VAL D 991    -115.303  27.702 -15.945  1.00 25.86           N  
ANISOU10033  N   VAL D 991     3144   3292   3392   -198    216   -335       N  
ATOM  10034  CA  VAL D 991    -114.377  28.830 -16.041  1.00 27.80           C  
ANISOU10034  CA  VAL D 991     3351   3478   3733   -178    185   -333       C  
ATOM  10035  C   VAL D 991    -114.790  29.726 -17.197  1.00 27.94           C  
ANISOU10035  C   VAL D 991     3346   3468   3800   -182    179   -293       C  
ATOM  10036  O   VAL D 991    -115.410  29.262 -18.137  1.00 27.67           O  
ANISOU10036  O   VAL D 991     3334   3464   3717   -202    209   -257       O  
ATOM  10037  CB  VAL D 991    -112.885  28.401 -16.155  1.00 26.53           C  
ANISOU10037  CB  VAL D 991     3201   3283   3595   -179    200   -302       C  
ATOM  10038  CG1 VAL D 991    -112.444  27.691 -14.887  1.00 26.72           C  
ANISOU10038  CG1 VAL D 991     3238   3336   3578   -163    199   -342       C  
ATOM  10039  CG2 VAL D 991    -112.636  27.549 -17.381  1.00 24.86           C  
ANISOU10039  CG2 VAL D 991     3026   3074   3345   -203    245   -240       C  
ATOM  10040  N   TYR D 992    -114.431  31.004 -17.092  1.00 28.70           N  
ANISOU10040  N   TYR D 992     3394   3510   4000   -162    138   -300       N  
ATOM  10041  CA  TYR D 992    -114.914  32.044 -18.000  1.00 31.07           C  
ANISOU10041  CA  TYR D 992     3662   3779   4363   -158    125   -260       C  
ATOM  10042  C   TYR D 992    -113.803  32.664 -18.811  1.00 29.89           C  
ANISOU10042  C   TYR D 992     3483   3564   4308   -163    127   -185       C  
ATOM  10043  O   TYR D 992    -114.012  33.646 -19.481  1.00 30.66           O  
ANISOU10043  O   TYR D 992     3544   3624   4480   -157    113   -139       O  
ATOM  10044  CB  TYR D 992    -115.689  33.116 -17.204  1.00 31.08           C  
ANISOU10044  CB  TYR D 992     3624   3765   4419   -128     71   -329       C  
ATOM  10045  CG  TYR D 992    -116.836  32.461 -16.509  1.00 29.54           C  
ANISOU10045  CG  TYR D 992     3452   3653   4118   -123     76   -388       C  
ATOM  10046  CD1 TYR D 992    -116.666  31.906 -15.264  1.00 30.07           C  
ANISOU10046  CD1 TYR D 992     3527   3760   4139   -111     69   -450       C  
ATOM  10047  CD2 TYR D 992    -118.080  32.297 -17.161  1.00 28.33           C  
ANISOU10047  CD2 TYR D 992     3310   3550   3904   -133     95   -369       C  
ATOM  10048  CE1 TYR D 992    -117.724  31.258 -14.633  1.00 30.94           C  
ANISOU10048  CE1 TYR D 992     3650   3956   4150   -109     80   -487       C  
ATOM  10049  CE2 TYR D 992    -119.137  31.642 -16.557  1.00 28.02           C  
ANISOU10049  CE2 TYR D 992     3285   3590   3769   -136    104   -414       C  
ATOM  10050  CZ  TYR D 992    -118.965  31.119 -15.285  1.00 29.50           C  
ANISOU10050  CZ  TYR D 992     3477   3816   3916   -125     97   -468       C  
ATOM  10051  OH  TYR D 992    -119.988  30.460 -14.650  1.00 24.45           O  
ANISOU10051  OH  TYR D 992     2844   3262   3185   -129    109   -497       O  
ATOM  10052  N   ASP D 993    -112.637  32.034 -18.801  1.00 31.62           N  
ANISOU10052  N   ASP D 993     3717   3778   4520   -173    148   -164       N  
ATOM  10053  CA  ASP D 993    -111.490  32.493 -19.582  1.00 31.40           C  
ANISOU10053  CA  ASP D 993     3656   3703   4571   -180    156    -85       C  
ATOM  10054  C   ASP D 993    -110.865  31.233 -20.129  1.00 30.55           C  
ANISOU10054  C   ASP D 993     3591   3645   4373   -192    207    -48       C  
ATOM  10055  O   ASP D 993    -110.467  30.359 -19.371  1.00 30.94           O  
ANISOU10055  O   ASP D 993     3673   3712   4371   -192    214    -95       O  
ATOM  10056  CB  ASP D 993    -110.539  33.253 -18.661  1.00 31.78           C  
ANISOU10056  CB  ASP D 993     3661   3682   4733   -172    111   -125       C  
ATOM  10057  CG  ASP D 993    -109.286  33.781 -19.367  1.00 32.67           C  
ANISOU10057  CG  ASP D 993     3729   3741   4943   -184    116    -39       C  
ATOM  10058  OD1 ASP D 993    -108.884  33.308 -20.459  1.00 35.16           O  
ANISOU10058  OD1 ASP D 993     4053   4091   5216   -194    163     50       O  
ATOM  10059  OD2 ASP D 993    -108.674  34.666 -18.770  1.00 34.64           O  
ANISOU10059  OD2 ASP D 993     3929   3919   5315   -181     71    -68       O  
ATOM  10060  N   ILE D 994    -110.738  31.141 -21.448  1.00 31.69           N  
ANISOU10060  N   ILE D 994     3729   3816   4497   -196    241     36       N  
ATOM  10061  CA  ILE D 994    -110.186  29.926 -22.095  1.00 31.25           C  
ANISOU10061  CA  ILE D 994     3709   3815   4351   -199    287     63       C  
ATOM  10062  C   ILE D 994    -108.747  29.575 -21.673  1.00 30.01           C  
ANISOU10062  C   ILE D 994     3549   3635   4217   -197    291     65       C  
ATOM  10063  O   ILE D 994    -108.307  28.427 -21.820  1.00 31.12           O  
ANISOU10063  O   ILE D 994     3729   3814   4281   -194    320     57       O  
ATOM  10064  CB  ILE D 994    -110.250  30.023 -23.632  1.00 33.72           C  
ANISOU10064  CB  ILE D 994     4000   4176   4635   -191    319    152       C  
ATOM  10065  CG1 ILE D 994    -109.360  31.179 -24.139  1.00 38.78           C  
ANISOU10065  CG1 ILE D 994     4572   4777   5387   -187    312    246       C  
ATOM  10066  CG2 ILE D 994    -111.677  30.229 -24.091  1.00 33.29           C  
ANISOU10066  CG2 ILE D 994     3950   4158   4541   -189    317    146       C  
ATOM  10067  CD1 ILE D 994    -109.369  31.357 -25.650  1.00 40.75           C  
ANISOU10067  CD1 ILE D 994     4786   5091   5606   -172    346    352       C  
ATOM  10068  N   ALA D 995    -108.019  30.560 -21.158  1.00 29.73           N  
ANISOU10068  N   ALA D 995     3465   3538   4294   -197    258     71       N  
ATOM  10069  CA  ALA D 995    -106.638  30.367 -20.718  1.00 30.63           C  
ANISOU10069  CA  ALA D 995     3565   3632   4441   -195    257     71       C  
ATOM  10070  C   ALA D 995    -106.519  29.645 -19.396  1.00 29.29           C  
ANISOU10070  C   ALA D 995     3433   3467   4228   -187    243    -21       C  
ATOM  10071  O   ALA D 995    -105.421  29.235 -19.021  1.00 25.79           O  
ANISOU10071  O   ALA D 995     2989   3024   3787   -180    247    -27       O  
ATOM  10072  CB  ALA D 995    -105.913  31.711 -20.645  1.00 32.93           C  
ANISOU10072  CB  ALA D 995     3780   3850   4880   -202    222    107       C  
ATOM  10073  N   GLN D 996    -107.646  29.463 -18.692  1.00 28.19           N  
ANISOU10073  N   GLN D 996     3323   3341   4045   -184    228    -87       N  
ATOM  10074  CA  GLN D 996    -107.622  28.719 -17.412  1.00 28.42           C  
ANISOU10074  CA  GLN D 996     3384   3392   4021   -171    220   -162       C  
ATOM  10075  C   GLN D 996    -107.626  27.190 -17.559  1.00 27.65           C  
ANISOU10075  C   GLN D 996     3351   3341   3815   -173    264   -155       C  
ATOM  10076  O   GLN D 996    -107.716  26.479 -16.571  1.00 25.90           O  
ANISOU10076  O   GLN D 996     3156   3141   3544   -162    263   -200       O  
ATOM  10077  CB  GLN D 996    -108.801  29.135 -16.545  1.00 28.88           C  
ANISOU10077  CB  GLN D 996     3439   3460   4075   -163    188   -229       C  
ATOM  10078  CG  GLN D 996    -108.534  30.383 -15.731  1.00 31.33           C  
ANISOU10078  CG  GLN D 996     3689   3726   4490   -146    130   -283       C  
ATOM  10079  CD  GLN D 996    -109.795  30.867 -15.029  1.00 29.74           C  
ANISOU10079  CD  GLN D 996     3478   3543   4278   -130     97   -350       C  
ATOM  10080  OE1 GLN D 996    -110.520  31.691 -15.570  1.00 27.48           O  
ANISOU10080  OE1 GLN D 996     3171   3229   4040   -134     82   -337       O  
ATOM  10081  NE2 GLN D 996    -110.044  30.360 -13.809  1.00 27.01           N  
ANISOU10081  NE2 GLN D 996     3143   3252   3867   -106     87   -419       N  
ATOM  10082  N   VAL D 997    -107.511  26.697 -18.785  1.00 28.53           N  
ANISOU10082  N   VAL D 997     3480   3469   3892   -181    299   -100       N  
ATOM  10083  CA  VAL D 997    -107.562  25.265 -19.063  1.00 28.19           C  
ANISOU10083  CA  VAL D 997     3494   3459   3760   -182    335   -101       C  
ATOM  10084  C   VAL D 997    -106.279  24.817 -19.760  1.00 29.03           C  
ANISOU10084  C   VAL D 997     3598   3571   3860   -167    359    -59       C  
ATOM  10085  O   VAL D 997    -105.889  25.396 -20.753  1.00 32.25           O  
ANISOU10085  O   VAL D 997     3970   3988   4297   -166    367     -5       O  
ATOM  10086  CB  VAL D 997    -108.722  24.923 -20.010  1.00 26.38           C  
ANISOU10086  CB  VAL D 997     3286   3258   3479   -197    354    -92       C  
ATOM  10087  CG1 VAL D 997    -108.739  23.440 -20.299  1.00 27.54           C  
ANISOU10087  CG1 VAL D 997     3486   3425   3551   -198    384   -105       C  
ATOM  10088  CG2 VAL D 997    -110.041  25.359 -19.403  1.00 27.78           C  
ANISOU10088  CG2 VAL D 997     3460   3438   3655   -210    333   -130       C  
ATOM  10089  N   ASN D 998    -105.670  23.762 -19.253  1.00 30.02           N  
ANISOU10089  N   ASN D 998     3759   3701   3945   -153    372    -79       N  
ATOM  10090  CA  ASN D 998    -104.565  23.124 -19.916  1.00 30.39           C  
ANISOU10090  CA  ASN D 998     3812   3764   3970   -133    396    -50       C  
ATOM  10091  C   ASN D 998    -104.930  21.634 -20.123  1.00 29.45           C  
ANISOU10091  C   ASN D 998     3757   3657   3777   -128    420    -74       C  
ATOM  10092  O   ASN D 998    -104.991  20.839 -19.152  1.00 26.39           O  
ANISOU10092  O   ASN D 998     3406   3254   3369   -124    420   -104       O  
ATOM  10093  CB  ASN D 998    -103.293  23.325 -19.082  1.00 31.65           C  
ANISOU10093  CB  ASN D 998     3948   3909   4168   -115    383    -53       C  
ATOM  10094  CG  ASN D 998    -102.015  22.911 -19.805  1.00 33.57           C  
ANISOU10094  CG  ASN D 998     4181   4176   4400    -91    405    -15       C  
ATOM  10095  OD1 ASN D 998    -100.991  22.653 -19.181  1.00 33.24           O  
ANISOU10095  OD1 ASN D 998     4133   4132   4364    -70    402    -23       O  
ATOM  10096  ND2 ASN D 998    -102.061  22.873 -21.131  1.00 36.34           N  
ANISOU10096  ND2 ASN D 998     4521   4559   4726    -88    427     27       N  
ATOM  10097  N   LEU D 999    -105.247  21.282 -21.373  1.00 27.90           N  
ANISOU10097  N   LEU D 999     3567   3490   3543   -127    439    -61       N  
ATOM  10098  CA  LEU D 999    -105.631  19.911 -21.696  1.00 30.51           C  
ANISOU10098  CA  LEU D 999     3951   3824   3819   -122    455    -96       C  
ATOM  10099  C   LEU D 999    -104.457  18.969 -21.459  1.00 29.90           C  
ANISOU10099  C   LEU D 999     3898   3737   3727    -90    466   -101       C  
ATOM  10100  O   LEU D 999    -103.339  19.271 -21.852  1.00 30.11           O  
ANISOU10100  O   LEU D 999     3893   3786   3760    -63    472    -71       O  
ATOM  10101  CB  LEU D 999    -106.113  19.839 -23.139  1.00 33.04           C  
ANISOU10101  CB  LEU D 999     4260   4191   4101   -118    467    -91       C  
ATOM  10102  CG  LEU D 999    -107.384  20.654 -23.405  1.00 33.54           C  
ANISOU10102  CG  LEU D 999     4304   4269   4171   -146    457    -88       C  
ATOM  10103  CD1 LEU D 999    -107.793  20.466 -24.863  1.00 35.64           C  
ANISOU10103  CD1 LEU D 999     4556   4599   4388   -132    469    -87       C  
ATOM  10104  CD2 LEU D 999    -108.526  20.260 -22.486  1.00 31.56           C  
ANISOU10104  CD2 LEU D 999     4087   3984   3919   -180    446   -131       C  
ATOM  10105  N   LYS D1000    -104.705  17.856 -20.777  1.00 33.30           N  
ANISOU10105  N   LYS D1000     4378   4132   4143    -91    469   -132       N  
ATOM  10106  CA  LYS D1000    -103.648  16.881 -20.429  1.00 36.16           C  
ANISOU10106  CA  LYS D1000     4767   4476   4495    -55    477   -136       C  
ATOM  10107  C   LYS D1000    -103.793  15.518 -21.109  1.00 36.55           C  
ANISOU10107  C   LYS D1000     4861   4508   4518    -41    488   -171       C  
ATOM  10108  O   LYS D1000    -102.826  14.984 -21.614  1.00 34.32           O  
ANISOU10108  O   LYS D1000     4582   4238   4219      1    495   -176       O  
ATOM  10109  CB  LYS D1000    -103.602  16.614 -18.923  1.00 38.19           C  
ANISOU10109  CB  LYS D1000     5044   4702   4767    -57    471   -136       C  
ATOM  10110  CG  LYS D1000    -103.479  17.835 -18.045  1.00 42.10           C  
ANISOU10110  CG  LYS D1000     5494   5211   5290    -64    453   -124       C  
ATOM  10111  CD  LYS D1000    -102.436  18.842 -18.497  1.00 44.95           C  
ANISOU10111  CD  LYS D1000     5804   5597   5680    -49    446   -102       C  
ATOM  10112  CE  LYS D1000    -101.026  18.423 -18.177  1.00 47.63           C  
ANISOU10112  CE  LYS D1000     6140   5944   6015     -8    451    -93       C  
ATOM  10113  NZ  LYS D1000    -100.108  19.594 -18.372  1.00 51.99           N  
ANISOU10113  NZ  LYS D1000     6626   6517   6611     -4    439    -69       N  
ATOM  10114  N   TYR D1001    -104.989  14.942 -21.057  1.00 36.55           N  
ANISOU10114  N   TYR D1001     4891   4478   4519    -74    485   -198       N  
ATOM  10115  CA  TYR D1001    -105.218  13.626 -21.618  1.00 35.81           C  
ANISOU10115  CA  TYR D1001     4835   4352   4419    -65    488   -241       C  
ATOM  10116  C   TYR D1001    -106.452  13.586 -22.494  1.00 36.25           C  
ANISOU10116  C   TYR D1001     4887   4422   4463    -97    481   -279       C  
ATOM  10117  O   TYR D1001    -107.398  14.363 -22.327  1.00 32.66           O  
ANISOU10117  O   TYR D1001     4414   3986   4011   -135    477   -268       O  
ATOM  10118  CB  TYR D1001    -105.345  12.561 -20.520  1.00 36.63           C  
ANISOU10118  CB  TYR D1001     4984   4383   4552    -74    490   -238       C  
ATOM  10119  CG  TYR D1001    -104.172  12.502 -19.566  1.00 34.71           C  
ANISOU10119  CG  TYR D1001     4744   4132   4313    -37    495   -202       C  
ATOM  10120  CD1 TYR D1001    -103.013  11.807 -19.910  1.00 37.18           C  
ANISOU10120  CD1 TYR D1001     5070   4437   4619     16    499   -212       C  
ATOM  10121  CD2 TYR D1001    -104.223  13.123 -18.346  1.00 31.98           C  
ANISOU10121  CD2 TYR D1001     4382   3795   3972    -49    494   -165       C  
ATOM  10122  CE1 TYR D1001    -101.941  11.736 -19.053  1.00 34.91           C  
ANISOU10122  CE1 TYR D1001     4783   4149   4332     53    504   -180       C  
ATOM  10123  CE2 TYR D1001    -103.160  13.066 -17.475  1.00 34.19           C  
ANISOU10123  CE2 TYR D1001     4659   4080   4250    -11    496   -139       C  
ATOM  10124  CZ  TYR D1001    -102.016  12.382 -17.832  1.00 36.93           C  
ANISOU10124  CZ  TYR D1001     5021   4417   4592     38    502   -143       C  
ATOM  10125  OH  TYR D1001    -100.963  12.367 -16.939  1.00 36.59           O  
ANISOU10125  OH  TYR D1001     4972   4388   4544     79    503   -117       O  
ATOM  10126  N   LEU D1002    -106.420  12.650 -23.439  1.00 41.01           N  
ANISOU10126  N   LEU D1002     5506   5022   5055    -74    478   -333       N  
ATOM  10127  CA  LEU D1002    -107.551  12.345 -24.280  1.00 42.19           C  
ANISOU10127  CA  LEU D1002     5652   5182   5196    -98    467   -387       C  
ATOM  10128  C   LEU D1002    -107.775  10.849 -24.170  1.00 43.88           C  
ANISOU10128  C   LEU D1002     5910   5314   5450   -102    457   -441       C  
ATOM  10129  O   LEU D1002    -106.864  10.084 -24.404  1.00 46.61           O  
ANISOU10129  O   LEU D1002     6273   5637   5799    -55    455   -466       O  
ATOM  10130  CB  LEU D1002    -107.242  12.750 -25.706  1.00 42.48           C  
ANISOU10130  CB  LEU D1002     5650   5312   5178    -55    467   -410       C  
ATOM  10131  CG  LEU D1002    -108.312  12.470 -26.765  1.00 43.66           C  
ANISOU10131  CG  LEU D1002     5786   5500   5304    -65    453   -477       C  
ATOM  10132  CD1 LEU D1002    -109.571  13.231 -26.469  1.00 46.51           C  
ANISOU10132  CD1 LEU D1002     6133   5869   5672   -122    451   -456       C  
ATOM  10133  CD2 LEU D1002    -107.812  12.940 -28.113  1.00 47.30           C  
ANISOU10133  CD2 LEU D1002     6199   6076   5696     -7    457   -484       C  
ATOM  10134  N   LEU D1003    -108.976  10.434 -23.796  1.00 43.48           N  
ANISOU10134  N   LEU D1003     5871   5213   5435   -159    450   -457       N  
ATOM  10135  CA  LEU D1003    -109.289   9.023 -23.685  1.00 45.37           C  
ANISOU10135  CA  LEU D1003     6146   5359   5734   -173    438   -502       C  
ATOM  10136  C   LEU D1003    -110.237   8.597 -24.796  1.00 47.40           C  
ANISOU10136  C   LEU D1003     6389   5628   5993   -189    416   -591       C  
ATOM  10137  O   LEU D1003    -111.217   9.281 -25.106  1.00 43.48           O  
ANISOU10137  O   LEU D1003     5863   5186   5470   -224    414   -597       O  
ATOM  10138  CB  LEU D1003    -109.950   8.714 -22.352  1.00 46.17           C  
ANISOU10138  CB  LEU D1003     6266   5389   5888   -229    447   -446       C  
ATOM  10139  CG  LEU D1003    -109.066   8.580 -21.123  1.00 48.25           C  
ANISOU10139  CG  LEU D1003     6550   5616   6166   -208    463   -372       C  
ATOM  10140  CD1 LEU D1003    -108.368   9.891 -20.804  1.00 49.54           C  
ANISOU10140  CD1 LEU D1003     6688   5860   6274   -182    474   -326       C  
ATOM  10141  CD2 LEU D1003    -109.914   8.127 -19.952  1.00 47.04           C  
ANISOU10141  CD2 LEU D1003     6406   5405   6060   -262    472   -318       C  
ATOM  10142  N   LYS D1004    -109.926   7.451 -25.394  1.00 50.39           N  
ANISOU10142  N   LYS D1004     6785   5957   6404   -159    396   -668       N  
ATOM  10143  CA  LYS D1004    -110.856   6.756 -26.286  1.00 52.42           C  
ANISOU10143  CA  LYS D1004     7031   6200   6687   -177    367   -770       C  
ATOM  10144  C   LYS D1004    -111.601   5.736 -25.446  1.00 49.81           C  
ANISOU10144  C   LYS D1004     6727   5737   6462   -242    359   -764       C  
ATOM  10145  O   LYS D1004    -110.980   4.865 -24.838  1.00 47.41           O  
ANISOU10145  O   LYS D1004     6458   5334   6221   -229    359   -744       O  
ATOM  10146  CB  LYS D1004    -110.080   6.074 -27.392  1.00 56.36           C  
ANISOU10146  CB  LYS D1004     7527   6720   7169   -101    344   -867       C  
ATOM  10147  CG  LYS D1004    -110.929   5.421 -28.456  1.00 63.05           C  
ANISOU10147  CG  LYS D1004     8352   7573   8031   -104    307   -995       C  
ATOM  10148  CD  LYS D1004    -110.023   5.027 -29.611  1.00 71.97           C  
ANISOU10148  CD  LYS D1004     9466   8768   9111     -9    286  -1089       C  
ATOM  10149  CE  LYS D1004    -110.559   3.841 -30.385  1.00 77.75           C  
ANISOU10149  CE  LYS D1004    10191   9449   9901      1    237  -1239       C  
ATOM  10150  NZ  LYS D1004    -109.645   3.507 -31.516  1.00 83.50           N  
ANISOU10150  NZ  LYS D1004    10898  10262  10568    107    216  -1337       N  
ATOM  10151  N   LEU D1005    -112.915   5.906 -25.355  1.00 51.19           N  
ANISOU10151  N   LEU D1005     6882   5914   6655   -311    354   -768       N  
ATOM  10152  CA  LEU D1005    -113.761   5.079 -24.501  1.00 56.10           C  
ANISOU10152  CA  LEU D1005     7516   6422   7377   -384    351   -742       C  
ATOM  10153  C   LEU D1005    -114.766   4.255 -25.306  1.00 52.99           C  
ANISOU10153  C   LEU D1005     7103   5985   7045   -422    315   -851       C  
ATOM  10154  O   LEU D1005    -115.389   4.776 -26.230  1.00 52.29           O  
ANISOU10154  O   LEU D1005     6978   5989   6899   -422    300   -918       O  
ATOM  10155  CB  LEU D1005    -114.557   5.972 -23.532  1.00 58.32           C  
ANISOU10155  CB  LEU D1005     7781   6745   7633   -441    378   -645       C  
ATOM  10156  CG  LEU D1005    -113.835   6.840 -22.504  1.00 59.08           C  
ANISOU10156  CG  LEU D1005     7887   6881   7680   -419    410   -539       C  
ATOM  10157  CD1 LEU D1005    -114.867   7.598 -21.692  1.00 59.74           C  
ANISOU10157  CD1 LEU D1005     7946   7009   7746   -475    425   -475       C  
ATOM  10158  CD2 LEU D1005    -112.991   5.973 -21.585  1.00 61.21           C  
ANISOU10158  CD2 LEU D1005     8193   7056   8007   -401    421   -482       C  
ATOM  10159  N   LYS D1006    -114.959   3.001 -24.902  1.00 51.62           N  
ANISOU10159  N   LYS D1006     6948   5671   6994   -457    299   -862       N  
ATOM  10160  CA  LYS D1006    -116.039   2.179 -25.415  1.00 52.68           C  
ANISOU10160  CA  LYS D1006     7059   5741   7216   -512    263   -953       C  
ATOM  10161  C   LYS D1006    -117.142   2.293 -24.391  1.00 53.40           C  
ANISOU10161  C   LYS D1006     7135   5803   7353   -606    284   -856       C  
ATOM  10162  O   LYS D1006    -116.911   2.061 -23.218  1.00 53.50           O  
ANISOU10162  O   LYS D1006     7169   5751   7408   -627    312   -741       O  
ATOM  10163  CB  LYS D1006    -115.645   0.695 -25.580  1.00 53.99           C  
ANISOU10163  CB  LYS D1006     7248   5753   7513   -500    228  -1022       C  
ATOM  10164  N   PHE D1007    -118.332   2.658 -24.857  1.00 54.47           N  
ANISOU10164  N   PHE D1007     7228   5999   7470   -656    272   -903       N  
ATOM  10165  CA  PHE D1007    -119.545   2.650 -24.069  1.00 54.29           C  
ANISOU10165  CA  PHE D1007     7177   5955   7495   -748    285   -834       C  
ATOM  10166  C   PHE D1007    -120.232   1.285 -24.281  1.00 58.49           C  
ANISOU10166  C   PHE D1007     7694   6348   8182   -811    248   -901       C  
ATOM  10167  O   PHE D1007    -120.617   0.964 -25.395  1.00 60.64           O  
ANISOU10167  O   PHE D1007     7941   6628   8471   -807    205  -1040       O  
ATOM  10168  CB  PHE D1007    -120.492   3.747 -24.565  1.00 53.62           C  
ANISOU10168  CB  PHE D1007     7049   6012   7312   -765    286   -862       C  
ATOM  10169  CG  PHE D1007    -120.044   5.145 -24.256  1.00 51.28           C  
ANISOU10169  CG  PHE D1007     6758   5839   6887   -719    319   -787       C  
ATOM  10170  CD1 PHE D1007    -118.876   5.670 -24.818  1.00 51.65           C  
ANISOU10170  CD1 PHE D1007     6826   5943   6856   -634    322   -808       C  
ATOM  10171  CD2 PHE D1007    -120.804   5.956 -23.409  1.00 50.46           C  
ANISOU10171  CD2 PHE D1007     6632   5795   6744   -761    346   -698       C  
ATOM  10172  CE1 PHE D1007    -118.470   6.972 -24.525  1.00 50.72           C  
ANISOU10172  CE1 PHE D1007     6707   5925   6639   -598    349   -738       C  
ATOM  10173  CE2 PHE D1007    -120.398   7.263 -23.116  1.00 49.56           C  
ANISOU10173  CE2 PHE D1007     6520   5784   6527   -718    369   -640       C  
ATOM  10174  CZ  PHE D1007    -119.239   7.771 -23.674  1.00 46.38           C  
ANISOU10174  CZ  PHE D1007     6138   5423   6063   -640    370   -659       C  
ATOM  10175  N   ASN D1008    -120.386   0.492 -23.225  1.00 60.29           N  
ANISOU10175  N   ASN D1008     7931   6453   8524   -866    264   -801       N  
ATOM  10176  CA  ASN D1008    -121.110  -0.787 -23.296  1.00 60.86           C  
ANISOU10176  CA  ASN D1008     7980   6377   8767   -939    231   -842       C  
ATOM  10177  C   ASN D1008    -122.516  -0.615 -22.752  1.00 60.31           C  
ANISOU10177  C   ASN D1008     7859   6332   8725  -1039    245   -777       C  
ATOM  10178  O   ASN D1008    -122.720  -0.624 -21.539  1.00 57.52           O  
ANISOU10178  O   ASN D1008     7501   5959   8395  -1081    286   -625       O  
ATOM  10179  CB  ASN D1008    -120.364  -1.857 -22.504  1.00 62.06           C  
ANISOU10179  CB  ASN D1008     8170   6367   9044   -935    239   -761       C  
ATOM  10180  CG  ASN D1008    -119.012  -2.172 -23.106  1.00 62.64           C  
ANISOU10180  CG  ASN D1008     8290   6407   9104   -836    218   -840       C  
ATOM  10181  OD1 ASN D1008    -118.893  -2.400 -24.316  1.00 63.39           O  
ANISOU10181  OD1 ASN D1008     8378   6509   9198   -797    171  -1002       O  
ATOM  10182  ND2 ASN D1008    -117.985  -2.191 -22.273  1.00 64.69           N  
ANISOU10182  ND2 ASN D1008     8592   6641   9346   -788    251   -731       N  
ATOM  10183  N   PHE D1009    -123.473  -0.428 -23.655  1.00 59.32           N  
ANISOU10183  N   PHE D1009     7688   6265   8587  -1072    213   -892       N  
ATOM  10184  CA  PHE D1009    -124.862  -0.142 -23.276  1.00 59.02           C  
ANISOU10184  CA  PHE D1009     7591   6276   8556  -1162    225   -846       C  
ATOM  10185  C   PHE D1009    -125.629  -1.343 -22.695  1.00 61.98           C  
ANISOU10185  C   PHE D1009     7932   6498   9118  -1265    216   -795       C  
ATOM  10186  O   PHE D1009    -125.336  -2.488 -23.035  1.00 60.49           O  
ANISOU10186  O   PHE D1009     7754   6154   9075  -1274    179   -860       O  
ATOM  10187  CB  PHE D1009    -125.607   0.418 -24.483  1.00 57.30           C  
ANISOU10187  CB  PHE D1009     7333   6176   8264  -1157    190   -990       C  
ATOM  10188  CG  PHE D1009    -125.163   1.792 -24.868  1.00 55.89           C  
ANISOU10188  CG  PHE D1009     7170   6167   7899  -1075    210   -996       C  
ATOM  10189  CD1 PHE D1009    -124.173   1.978 -25.815  1.00 55.52           C  
ANISOU10189  CD1 PHE D1009     7152   6159   7785   -981    190  -1090       C  
ATOM  10190  CD2 PHE D1009    -125.720   2.911 -24.250  1.00 56.40           C  
ANISOU10190  CD2 PHE D1009     7215   6354   7862  -1090    247   -901       C  
ATOM  10191  CE1 PHE D1009    -123.751   3.257 -26.157  1.00 57.72           C  
ANISOU10191  CE1 PHE D1009     7438   6588   7905   -910    210  -1079       C  
ATOM  10192  CE2 PHE D1009    -125.301   4.195 -24.587  1.00 55.19           C  
ANISOU10192  CE2 PHE D1009     7073   6340   7555  -1016    263   -901       C  
ATOM  10193  CZ  PHE D1009    -124.311   4.369 -25.540  1.00 55.91           C  
ANISOU10193  CZ  PHE D1009     7192   6462   7589   -930    246   -983       C  
TER   10194      PHE D1009                                                      
HETATM10195  S   SO4 A1101     -34.370  15.705 -12.542  1.00 37.32           S  
ANISOU10195  S   SO4 A1101     4548   4601   5031    -94     79   -213       S  
HETATM10196  O1  SO4 A1101     -33.126  16.535 -12.469  1.00 37.55           O  
ANISOU10196  O1  SO4 A1101     4546   4611   5109   -112     88   -221       O  
HETATM10197  O2  SO4 A1101     -34.504  14.830 -13.833  1.00 41.30           O  
ANISOU10197  O2  SO4 A1101     5065   5131   5495    -94    102   -190       O  
HETATM10198  O3  SO4 A1101     -34.353  14.759 -11.373  1.00 37.89           O  
ANISOU10198  O3  SO4 A1101     4619   4686   5090    -74     55   -247       O  
HETATM10199  O4  SO4 A1101     -35.532  16.589 -12.369  1.00 29.06           O  
ANISOU10199  O4  SO4 A1101     3520   3535   3988    -90     67   -200       O  
HETATM10200  S   SO4 A1102     -47.579  24.690  -7.071  0.50 32.00           S  
ANISOU10200  S   SO4 A1102     3948   3758   4451     79   -120   -289       S  
HETATM10201  O1  SO4 A1102     -47.621  25.235  -8.437  0.50 31.70           O  
ANISOU10201  O1  SO4 A1102     3922   3693   4431     65   -118   -248       O  
HETATM10202  O2  SO4 A1102     -46.895  23.376  -7.048  0.50 30.34           O  
ANISOU10202  O2  SO4 A1102     3741   3582   4207     66   -102   -283       O  
HETATM10203  O3  SO4 A1102     -48.932  24.534  -6.502  0.50 33.78           O  
ANISOU10203  O3  SO4 A1102     4170   4006   4658    104   -125   -307       O  
HETATM10204  O4  SO4 A1102     -46.986  25.703  -6.180  0.50 34.79           O  
ANISOU10204  O4  SO4 A1102     4290   4084   4844     85   -137   -323       O  
HETATM10205  S   SO4 A1103     -63.994   0.620  -2.925  1.00 43.38           S  
ANISOU10205  S   SO4 A1103     5185   5545   5754   -106    200    -86       S  
HETATM10206  O1  SO4 A1103     -63.179   1.066  -4.107  1.00 50.09           O  
ANISOU10206  O1  SO4 A1103     6055   6380   6598    -94    156   -108       O  
HETATM10207  O2  SO4 A1103     -65.325   1.154  -3.292  1.00 37.55           O  
ANISOU10207  O2  SO4 A1103     4402   4817   5050   -107    200   -105       O  
HETATM10208  O3  SO4 A1103     -63.243   1.195  -1.763  1.00 39.64           O  
ANISOU10208  O3  SO4 A1103     4738   5094   5231    -86    220    -78       O  
HETATM10209  O4  SO4 A1103     -64.126  -0.910  -2.872  1.00 44.06           O  
ANISOU10209  O4  SO4 A1103     5269   5607   5866   -136    210    -60       O  
HETATM10210  S   SO4 A1104     -66.232  13.306 -23.086  0.50 29.03           S  
ANISOU10210  S   SO4 A1104     3521   3664   3847    225   -413   -233       S  
HETATM10211  O1  SO4 A1104     -67.274  12.328 -22.711  0.50 32.22           O  
ANISOU10211  O1  SO4 A1104     3879   4076   4288    216   -420   -267       O  
HETATM10212  O2  SO4 A1104     -66.089  13.373 -24.560  0.50 28.52           O  
ANISOU10212  O2  SO4 A1104     3490   3607   3741    247   -447   -223       O  
HETATM10213  O3  SO4 A1104     -64.998  12.874 -22.397  0.50 28.67           O  
ANISOU10213  O3  SO4 A1104     3489   3617   3787    197   -368   -219       O  
HETATM10214  O4  SO4 A1104     -66.722  14.607 -22.606  0.50 28.99           O  
ANISOU10214  O4  SO4 A1104     3507   3643   3863    242   -417   -227       O  
HETATM10215  N1  2YQ A1105     -40.422   6.025 -10.001  1.00 19.14           N  
ANISOU10215  N1  2YQ A1105     2369   2404   2500     14     -4   -239       N  
HETATM10216  N3  2YQ A1105     -37.918   8.786  -8.269  1.00 18.48           N  
ANISOU10216  N3  2YQ A1105     2248   2304   2471     15    -12   -278       N  
HETATM10217  C4  2YQ A1105     -41.676   7.708 -11.076  1.00 19.31           C  
ANISOU10217  C4  2YQ A1105     2392   2420   2525      2      6   -217       C  
HETATM10218  C5  2YQ A1105     -38.493   6.442  -8.560  1.00 19.96           C  
ANISOU10218  C5  2YQ A1105     2455   2504   2622     25    -15   -269       C  
HETATM10219  C6  2YQ A1105     -38.006   7.503  -7.559  1.00 20.24           C  
ANISOU10219  C6  2YQ A1105     2481   2534   2673     28    -22   -283       C  
HETATM10220  C7  2YQ A1105     -38.923   9.161  -9.081  1.00 19.04           C  
ANISOU10220  C7  2YQ A1105     2327   2373   2536      7     -2   -257       C  
HETATM10221  C8  2YQ A1105     -39.129  10.515  -9.324  1.00 19.30           C  
ANISOU10221  C8  2YQ A1105     2355   2393   2586     -2      2   -251       C  
HETATM10222  C10 2YQ A1105     -41.029  10.025 -10.727  1.00 19.28           C  
ANISOU10222  C10 2YQ A1105     2374   2398   2554     -5     11   -218       C  
HETATM10223  C13 2YQ A1105     -34.287   6.636  -7.460  1.00 22.57           C  
ANISOU10223  C13 2YQ A1105     2734   2836   3006     39    -36   -335       C  
HETATM10224  C15 2YQ A1105     -35.378   5.776  -5.506  1.00 23.41           C  
ANISOU10224  C15 2YQ A1105     2873   2945   3078     66    -63   -333       C  
HETATM10225  C17 2YQ A1105     -38.769   5.199  -7.865  1.00 19.99           C  
ANISOU10225  C17 2YQ A1105     2473   2512   2612     36    -25   -269       C  
HETATM10226  F2  2YQ A1105     -33.098   5.382  -5.827  1.00 24.44           F  
ANISOU10226  F2  2YQ A1105     2970   3078   3239     72    -72   -367       F  
HETATM10227  C14 2YQ A1105     -34.229   5.945  -6.262  1.00 23.24           C  
ANISOU10227  C14 2YQ A1105     2829   2923   3079     59    -57   -346       C  
HETATM10228  C12 2YQ A1105     -35.519   7.161  -7.866  1.00 22.40           C  
ANISOU10228  C12 2YQ A1105     2726   2811   2974     29    -25   -313       C  
HETATM10229  C16 2YQ A1105     -36.592   6.314  -5.912  1.00 21.61           C  
ANISOU10229  C16 2YQ A1105     2653   2714   2843     54    -49   -313       C  
HETATM10230  C11 2YQ A1105     -36.676   6.995  -7.103  1.00 20.98           C  
ANISOU10230  C11 2YQ A1105     2565   2632   2776     37    -32   -304       C  
HETATM10231  N6  2YQ A1105     -39.695   4.942  -6.923  1.00 21.24           N  
ANISOU10231  N6  2YQ A1105     2642   2670   2758     42    -30   -262       N  
HETATM10232  C18 2YQ A1105     -39.523   3.660  -6.508  1.00 22.11           C  
ANISOU10232  C18 2YQ A1105     2762   2780   2858     51    -39   -262       C  
HETATM10233  N5  2YQ A1105     -38.495   3.098  -7.160  1.00 20.23           N  
ANISOU10233  N5  2YQ A1105     2518   2542   2628     53    -41   -272       N  
HETATM10234  N4  2YQ A1105     -38.021   4.092  -7.984  1.00 21.45           N  
ANISOU10234  N4  2YQ A1105     2657   2698   2794     43    -31   -278       N  
HETATM10235  C19 2YQ A1105     -36.860   3.733  -8.837  1.00 20.29           C  
ANISOU10235  C19 2YQ A1105     2497   2554   2656     42    -27   -290       C  
HETATM10236  C3  2YQ A1105     -39.614   6.907  -9.414  1.00 19.90           C  
ANISOU10236  C3  2YQ A1105     2455   2496   2610     15     -5   -250       C  
HETATM10237  C2  2YQ A1105     -39.791   8.250  -9.655  1.00 19.45           C  
ANISOU10237  C2  2YQ A1105     2392   2432   2566      7      1   -244       C  
HETATM10238  C9  2YQ A1105     -40.157  10.931 -10.120  1.00 19.62           C  
ANISOU10238  C9  2YQ A1105     2405   2431   2621     -7      9   -230       C  
HETATM10239  F1  2YQ A1105     -40.319  12.229 -10.275  1.00 20.94           F  
ANISOU10239  F1  2YQ A1105     2568   2582   2807    -13     10   -224       F  
HETATM10240  C1  2YQ A1105     -40.850   8.665 -10.476  1.00 19.59           C  
ANISOU10240  C1  2YQ A1105     2418   2449   2579      1      7   -226       C  
HETATM10241  O   2YQ A1105     -42.601   8.009 -11.835  1.00 18.52           O  
ANISOU10241  O   2YQ A1105     2298   2320   2420     -1      8   -204       O  
HETATM10242  N2  2YQ A1105     -41.467   6.427 -10.846  1.00 18.62           N  
ANISOU10242  N2  2YQ A1105     2308   2337   2428      8      1   -224       N  
HETATM10243  C1  GOL A1106     -33.462  23.360   1.707  1.00 53.63           C  
HETATM10244  O1  GOL A1106     -34.313  23.727   0.621  1.00 42.76           O  
HETATM10245  C2  GOL A1106     -32.898  21.999   1.335  1.00 56.18           C  
HETATM10246  O2  GOL A1106     -33.686  21.620   0.231  1.00 51.03           O  
HETATM10247  C3  GOL A1106     -33.010  20.917   2.421  1.00 62.55           C  
HETATM10248  O3  GOL A1106     -32.720  19.628   1.858  1.00 56.32           O  
HETATM10249  C1  GOL A1107     -52.358  19.076  11.923  1.00 60.91           C  
HETATM10250  O1  GOL A1107     -51.186  18.755  12.686  1.00 54.88           O  
HETATM10251  C2  GOL A1107     -52.387  18.260  10.628  1.00 62.05           C  
HETATM10252  O2  GOL A1107     -52.088  19.173   9.582  1.00 60.59           O  
HETATM10253  C3  GOL A1107     -53.756  17.593  10.383  1.00 65.19           C  
HETATM10254  O3  GOL A1107     -53.995  17.284   8.992  1.00 59.26           O  
HETATM10255  S   SO4 B1101     -96.011   4.644  10.082  1.00 55.52           S  
ANISOU10255  S   SO4 B1101     6348   7783   6963    -49    190    502       S  
HETATM10256  O1  SO4 B1101     -95.819   4.156   8.706  1.00 56.77           O  
ANISOU10256  O1  SO4 B1101     6506   7935   7129    -86    135    541       O  
HETATM10257  O2  SO4 B1101     -97.421   5.093  10.210  1.00 60.88           O  
ANISOU10257  O2  SO4 B1101     6933   8541   7658    -22    234    536       O  
HETATM10258  O3  SO4 B1101     -95.718   3.468  10.985  1.00 54.03           O  
ANISOU10258  O3  SO4 B1101     6221   7599   6709   -114    180    484       O  
HETATM10259  O4  SO4 B1101     -95.188   5.887  10.280  1.00 47.74           O  
ANISOU10259  O4  SO4 B1101     5390   6724   6024     25    211    456       O  
HETATM10260  S   SO4 B1102     -66.128   5.793   7.040  1.00 52.15           S  
ANISOU10260  S   SO4 B1102     6135   6303   7377    -30   -244   -222       S  
HETATM10261  O1  SO4 B1102     -66.422   5.175   5.737  1.00 57.49           O  
ANISOU10261  O1  SO4 B1102     6814   6991   8041    -25   -194   -196       O  
HETATM10262  O2  SO4 B1102     -65.353   7.062   6.964  1.00 53.35           O  
ANISOU10262  O2  SO4 B1102     6245   6434   7592    -54   -228   -244       O  
HETATM10263  O3  SO4 B1102     -65.329   4.817   7.806  1.00 57.10           O  
ANISOU10263  O3  SO4 B1102     6748   6931   8018    -10   -309   -244       O  
HETATM10264  O4  SO4 B1102     -67.429   6.081   7.668  1.00 52.68           O  
ANISOU10264  O4  SO4 B1102     6259   6379   7379    -30   -249   -205       O  
HETATM10265  S   SO4 B1103     -85.495  17.746   7.865  0.50 31.79           S  
ANISOU10265  S   SO4 B1103     3689   3781   4610    392    261    156       S  
HETATM10266  O1  SO4 B1103     -84.293  18.352   7.287  0.50 31.21           O  
ANISOU10266  O1  SO4 B1103     3643   3631   4584    368    249    148       O  
HETATM10267  O2  SO4 B1103     -85.722  16.433   7.244  0.50 33.84           O  
ANISOU10267  O2  SO4 B1103     3922   4120   4818    351    230    201       O  
HETATM10268  O3  SO4 B1103     -86.706  18.535   7.644  0.50 34.54           O  
ANISOU10268  O3  SO4 B1103     4003   4132   4990    458    295    196       O  
HETATM10269  O4  SO4 B1103     -85.310  17.628   9.317  0.50 34.53           O  
ANISOU10269  O4  SO4 B1103     4067   4126   4926    390    269     79       O  
HETATM10270  S   SO4 B1104     -81.509  16.695 -10.577  0.50 28.99           S  
ANISOU10270  S   SO4 B1104     3429   3560   4026    -55    178    900       S  
HETATM10271  O1  SO4 B1104     -80.730  17.171 -11.740  0.50 29.40           O  
ANISOU10271  O1  SO4 B1104     3516   3592   4061    -97    209    941       O  
HETATM10272  O2  SO4 B1104     -82.919  16.748 -10.985  0.50 25.60           O  
ANISOU10272  O2  SO4 B1104     2984   3182   3562    -29    136    973       O  
HETATM10273  O3  SO4 B1104     -81.021  15.334 -10.214  0.50 26.82           O  
ANISOU10273  O3  SO4 B1104     3151   3325   3715    -87    178    824       O  
HETATM10274  O4  SO4 B1104     -81.176  17.544  -9.408  0.50 27.40           O  
ANISOU10274  O4  SO4 B1104     3216   3282   3913    -15    196    859       O  
HETATM10275  N1  2YQ B1105     -88.298  -2.030   4.917  1.00 23.86           N  
ANISOU10275  N1  2YQ B1105     2804   3386   2876   -343   -156    411       N  
HETATM10276  N3  2YQ B1105     -91.425   0.554   4.037  1.00 26.14           N  
ANISOU10276  N3  2YQ B1105     2891   3843   3196   -288    -95    522       N  
HETATM10277  C4  2YQ B1105     -87.340  -0.490   6.484  1.00 24.46           C  
ANISOU10277  C4  2YQ B1105     2874   3419   3002   -252   -122    359       C  
HETATM10278  C5  2YQ B1105     -90.367  -1.635   3.664  1.00 27.45           C  
ANISOU10278  C5  2YQ B1105     3167   3953   3311   -378   -150    491       C  
HETATM10279  C6  2YQ B1105     -91.097  -0.423   2.983  1.00 27.86           C  
ANISOU10279  C6  2YQ B1105     3148   4049   3388   -343   -132    527       C  
HETATM10280  C7  2YQ B1105     -90.478   0.914   4.943  1.00 24.53           C  
ANISOU10280  C7  2YQ B1105     2722   3585   3012   -250    -79    476       C  
HETATM10281  C8  2YQ B1105     -90.564   2.148   5.569  1.00 23.82           C  
ANISOU10281  C8  2YQ B1105     2602   3491   2958   -187    -43    464       C  
HETATM10282  C10 2YQ B1105     -88.479   1.657   6.756  1.00 23.63           C  
ANISOU10282  C10 2YQ B1105     2678   3363   2936   -180    -60    379       C  
HETATM10283  C13 2YQ B1105     -94.586  -1.845   2.411  1.00 37.91           C  
ANISOU10283  C13 2YQ B1105     4305   5523   4578   -485   -170    649       C  
HETATM10284  C15 2YQ B1105     -93.423  -1.765   0.287  1.00 35.05           C  
ANISOU10284  C15 2YQ B1105     3999   5104   4216   -489   -209    639       C  
HETATM10285  C17 2YQ B1105     -89.892  -2.561   2.607  1.00 28.27           C  
ANISOU10285  C17 2YQ B1105     3317   4031   3395   -423   -180    486       C  
HETATM10286  F2  2YQ B1105     -95.611  -2.611   0.415  1.00 45.41           F  
ANISOU10286  F2  2YQ B1105     5228   6544   5483   -580   -235    709       F  
HETATM10287  C14 2YQ B1105     -94.552  -2.079   1.035  1.00 40.66           C  
ANISOU10287  C14 2YQ B1105     4662   5875   4912   -517   -205    666       C  
HETATM10288  C12 2YQ B1105     -93.470  -1.287   3.055  1.00 35.74           C  
ANISOU10288  C12 2YQ B1105     4068   5179   4332   -425   -146    603       C  
HETATM10289  C16 2YQ B1105     -92.327  -1.218   0.944  1.00 34.54           C  
ANISOU10289  C16 2YQ B1105     3965   4974   4186   -430   -181    596       C  
HETATM10290  C11 2YQ B1105     -92.326  -0.971   2.323  1.00 31.73           C  
ANISOU10290  C11 2YQ B1105     3602   4610   3845   -398   -153    577       C  
HETATM10291  N6  2YQ B1105     -88.939  -2.309   1.672  1.00 31.69           N  
ANISOU10291  N6  2YQ B1105     3772   4421   3847   -405   -182    465       N  
HETATM10292  C18 2YQ B1105     -88.827  -3.375   0.829  1.00 30.35           C  
ANISOU10292  C18 2YQ B1105     3645   4241   3645   -458   -208    462       C  
HETATM10293  N5  2YQ B1105     -89.724  -4.297   1.205  1.00 27.76           N  
ANISOU10293  N5  2YQ B1105     3321   3947   3279   -515   -227    483       N  
HETATM10294  N4  2YQ B1105     -90.368  -3.770   2.328  1.00 28.04           N  
ANISOU10294  N4  2YQ B1105     3314   4018   3324   -492   -208    499       N  
HETATM10295  C19 2YQ B1105     -91.382  -4.678   2.985  1.00 28.68           C  
ANISOU10295  C19 2YQ B1105     3391   4140   3365   -552   -220    525       C  
HETATM10296  C3  2YQ B1105     -89.318  -1.213   4.621  1.00 25.02           C  
ANISOU10296  C3  2YQ B1105     2888   3588   3029   -330   -135    446       C  
HETATM10297  C2  2YQ B1105     -89.398   0.041   5.247  1.00 25.25           C  
ANISOU10297  C2  2YQ B1105     2882   3622   3091   -271   -102    438       C  
HETATM10298  C9  2YQ B1105     -89.563   2.492   6.463  1.00 24.49           C  
ANISOU10298  C9  2YQ B1105     2726   3520   3059   -156    -33    413       C  
HETATM10299  F1  2YQ B1105     -89.589   3.675   7.051  1.00 27.60           F  
ANISOU10299  F1  2YQ B1105     3098   3902   3486   -100      1    395       F  
HETATM10300  C1  2YQ B1105     -88.382   0.409   6.155  1.00 23.68           C  
ANISOU10300  C1  2YQ B1105     2714   3370   2912   -234    -94    392       C  
HETATM10301  O   2YQ B1105     -86.405  -0.223   7.321  1.00 25.33           O  
ANISOU10301  O   2YQ B1105     3011   3485   3129   -223   -123    320       O  
HETATM10302  N2  2YQ B1105     -87.298  -1.684   5.848  1.00 22.75           N  
ANISOU10302  N2  2YQ B1105     2689   3197   2759   -302   -151    370       N  
HETATM10303  S   SO4 B1106     -81.718  11.489  -8.680  0.50 54.85           S  
HETATM10304  O1  SO4 B1106     -80.608  11.122  -9.598  0.50 49.89           O  
HETATM10305  O2  SO4 B1106     -82.510  12.609  -9.231  0.50 46.35           O  
HETATM10306  O3  SO4 B1106     -82.659  10.351  -8.464  0.50 54.35           O  
HETATM10307  O4  SO4 B1106     -81.080  11.865  -7.393  0.50 49.47           O  
HETATM10308  S   SO4 C1101     -63.783  37.785 -19.360  1.00 54.01           S  
ANISOU10308  S   SO4 C1101     6792   6982   6747   -193     97   -327       S  
HETATM10309  O1  SO4 C1101     -63.813  36.517 -20.149  1.00 53.91           O  
ANISOU10309  O1  SO4 C1101     6770   6987   6726   -146     78   -281       O  
HETATM10310  O2  SO4 C1101     -64.071  38.947 -20.348  1.00 40.09           O  
ANISOU10310  O2  SO4 C1101     5051   5149   5032   -237    142   -317       O  
HETATM10311  O3  SO4 C1101     -62.432  37.786 -18.699  1.00 43.29           O  
ANISOU10311  O3  SO4 C1101     5385   5706   5359   -215     73   -384       O  
HETATM10312  O4  SO4 C1101     -64.772  37.658 -18.281  1.00 36.26           O  
ANISOU10312  O4  SO4 C1101     4579   4716   4484   -162     94   -322       O  
HETATM10313  S   SO4 C1102     -93.949  35.578 -19.518  1.00 59.18           S  
ANISOU10313  S   SO4 C1102     7260   7900   7324    284    399    467       S  
HETATM10314  O1  SO4 C1102     -93.949  34.664 -20.681  1.00 67.11           O  
ANISOU10314  O1  SO4 C1102     8223   8946   8332    228    367    454       O  
HETATM10315  O2  SO4 C1102     -94.685  36.821 -19.834  1.00 64.24           O  
ANISOU10315  O2  SO4 C1102     7881   8581   7944    361    426    504       O  
HETATM10316  O3  SO4 C1102     -94.670  34.945 -18.394  1.00 61.69           O  
ANISOU10316  O3  SO4 C1102     7564   8238   7638    267    416    473       O  
HETATM10317  O4  SO4 C1102     -92.532  35.840 -19.139  1.00 55.28           O  
ANISOU10317  O4  SO4 C1102     6841   7312   6851    281    393    437       O  
HETATM10318  S   SO4 C1103     -78.259  18.570 -46.229  0.50 33.09           S  
ANISOU10318  S   SO4 C1103     4234   4602   3736   -258    -80   -301       S  
HETATM10319  O1  SO4 C1103     -77.289  18.468 -47.322  0.50 33.42           O  
ANISOU10319  O1  SO4 C1103     4295   4657   3745   -215    -83   -311       O  
HETATM10320  O2  SO4 C1103     -79.558  18.257 -46.832  0.50 31.70           O  
ANISOU10320  O2  SO4 C1103     4016   4500   3527   -315   -100   -343       O  
HETATM10321  O3  SO4 C1103     -77.805  17.570 -45.251  0.50 31.33           O  
ANISOU10321  O3  SO4 C1103     4081   4276   3546   -281    -57   -319       O  
HETATM10322  O4  SO4 C1103     -78.367  19.938 -45.622  0.50 30.03           O  
ANISOU10322  O4  SO4 C1103     3802   4237   3372   -217    -79   -236       O  
HETATM10323  N1  2YQ C1104     -71.491  33.627 -26.897  1.00 19.07           N  
ANISOU10323  N1  2YQ C1104     2474   2376   2398    -10    130     44       N  
HETATM10324  N3  2YQ C1104     -68.491  32.366 -24.299  1.00 17.77           N  
ANISOU10324  N3  2YQ C1104     2294   2275   2185     -1     81    -42       N  
HETATM10325  C4  2YQ C1104     -72.469  35.026 -25.267  1.00 19.46           C  
ANISOU10325  C4  2YQ C1104     2547   2388   2458    -10    159     40       C  
HETATM10326  C5  2YQ C1104     -69.458  32.292 -26.545  1.00 19.03           C  
ANISOU10326  C5  2YQ C1104     2454   2411   2366     -6     96      4       C  
HETATM10327  C6  2YQ C1104     -68.753  31.489 -25.429  1.00 19.63           C  
ANISOU10327  C6  2YQ C1104     2531   2508   2419     10     76    -19       C  
HETATM10328  C7  2YQ C1104     -69.447  33.244 -23.883  1.00 18.90           C  
ANISOU10328  C7  2YQ C1104     2451   2388   2343    -11    100    -35       C  
HETATM10329  C8  2YQ C1104     -69.417  33.744 -22.588  1.00 18.46           C  
ANISOU10329  C8  2YQ C1104     2403   2332   2280    -14    102    -58       C  
HETATM10330  C10 2YQ C1104     -71.403  35.049 -23.052  1.00 18.93           C  
ANISOU10330  C10 2YQ C1104     2489   2331   2373    -18    144    -17       C  
HETATM10331  C13 2YQ C1104     -65.261  31.071 -26.837  1.00 23.72           C  
ANISOU10331  C13 2YQ C1104     2982   3118   2912     14     57    -58       C  
HETATM10332  C15 2YQ C1104     -66.428  28.954 -27.004  1.00 22.67           C  
ANISOU10332  C15 2YQ C1104     2898   2958   2756     62     43    -26       C  
HETATM10333  C17 2YQ C1104     -69.947  31.353 -27.558  1.00 20.03           C  
ANISOU10333  C17 2YQ C1104     2585   2541   2487      5     88     24       C  
HETATM10334  F2  2YQ C1104     -64.247  29.168 -27.751  1.00 28.58           F  
ANISOU10334  F2  2YQ C1104     3595   3772   3490     67     37    -50       F  
HETATM10335  C14 2YQ C1104     -65.315  29.729 -27.220  1.00 24.89           C  
ANISOU10335  C14 2YQ C1104     3146   3271   3041     48     44    -44       C  
HETATM10336  C12 2YQ C1104     -66.388  31.646 -26.276  1.00 22.21           C  
ANISOU10336  C12 2YQ C1104     2812   2890   2736      1     67    -50       C  
HETATM10337  C16 2YQ C1104     -67.528  29.551 -26.393  1.00 21.90           C  
ANISOU10337  C16 2YQ C1104     2814   2832   2675     45     52    -19       C  
HETATM10338  C11 2YQ C1104     -67.522  30.884 -26.037  1.00 20.34           C  
ANISOU10338  C11 2YQ C1104     2603   2630   2495     20     64    -29       C  
HETATM10339  N6  2YQ C1104     -70.848  30.382 -27.356  1.00 22.43           N  
ANISOU10339  N6  2YQ C1104     2904   2837   2782     15     81     35       N  
HETATM10340  C18 2YQ C1104     -70.996  29.664 -28.527  1.00 21.53           C  
ANISOU10340  C18 2YQ C1104     2790   2730   2662     17     75     44       C  
HETATM10341  N5  2YQ C1104     -70.180  30.150 -29.451  1.00 18.24           N  
ANISOU10341  N5  2YQ C1104     2356   2326   2248     14     78     42       N  
HETATM10342  N4  2YQ C1104     -69.513  31.191 -28.828  1.00 20.31           N  
ANISOU10342  N4  2YQ C1104     2609   2588   2521      5     87     30       N  
HETATM10343  C19 2YQ C1104     -68.486  31.935 -29.645  1.00 20.05           C  
ANISOU10343  C19 2YQ C1104     2555   2568   2496     -5     98     26       C  
HETATM10344  C3  2YQ C1104     -70.510  33.210 -26.061  1.00 19.00           C  
ANISOU10344  C3  2YQ C1104     2463   2380   2377    -12    115     15       C  
HETATM10345  C2  2YQ C1104     -70.474  33.675 -24.765  1.00 18.87           C  
ANISOU10345  C2  2YQ C1104     2455   2357   2358    -15    118     -5       C  
HETATM10346  C9  2YQ C1104     -70.405  34.642 -22.185  1.00 19.78           C  
ANISOU10346  C9  2YQ C1104     2588   2466   2461    -19    124    -50       C  
HETATM10347  F1  2YQ C1104     -70.401  35.124 -20.915  1.00 20.71           F  
ANISOU10347  F1  2YQ C1104     2716   2583   2569    -20    127    -75       F  
HETATM10348  C1  2YQ C1104     -71.458  34.565 -24.361  1.00 19.02           C  
ANISOU10348  C1  2YQ C1104     2489   2349   2390    -16    140      6       C  
HETATM10349  O   2YQ C1104     -73.377  35.873 -24.924  1.00 19.59           O  
ANISOU10349  O   2YQ C1104     2577   2382   2483     -3    182     54       O  
HETATM10350  N2  2YQ C1104     -72.486  34.547 -26.520  1.00 17.45           N  
ANISOU10350  N2  2YQ C1104     2280   2148   2203     -8    152     58       N  
HETATM10351  C1  GOL C1105     -64.636  32.391 -22.449  1.00 36.90           C  
HETATM10352  O1  GOL C1105     -64.756  33.445 -21.434  1.00 31.84           O  
HETATM10353  C2  GOL C1105     -65.668  31.286 -22.190  1.00 32.91           C  
HETATM10354  O2  GOL C1105     -66.929  31.861 -22.353  1.00 28.13           O  
HETATM10355  C3  GOL C1105     -65.809  30.142 -23.168  1.00 35.07           C  
HETATM10356  O3  GOL C1105     -64.758  29.245 -23.151  1.00 31.56           O  
HETATM10357  S   SO4 D1101     -95.974  26.230 -25.978  1.00 44.87           S  
ANISOU10357  S   SO4 D1101     5146   6397   5507   -328    224    253       S  
HETATM10358  O1  SO4 D1101     -95.459  27.094 -27.054  1.00 50.00           O  
ANISOU10358  O1  SO4 D1101     5788   7070   6139   -271    197    259       O  
HETATM10359  O2  SO4 D1101     -96.697  25.170 -26.746  1.00 51.73           O  
ANISOU10359  O2  SO4 D1101     5961   7329   6364   -420    214    214       O  
HETATM10360  O3  SO4 D1101     -96.897  26.998 -25.123  1.00 46.43           O  
ANISOU10360  O3  SO4 D1101     5304   6643   5694   -281    250    295       O  
HETATM10361  O4  SO4 D1101     -94.900  25.599 -25.202  1.00 43.48           O  
ANISOU10361  O4  SO4 D1101     5060   6098   5361   -343    236    241       O  
HETATM10362  S   SO4 D1102    -126.742  16.777 -13.106  1.00 66.04           S  
ANISOU10362  S   SO4 D1102     8229   8809   8053   -670    470   -142       S  
HETATM10363  O1  SO4 D1102    -126.878  18.086 -13.831  1.00 58.88           O  
ANISOU10363  O1  SO4 D1102     7318   7933   7122   -631    440   -212       O  
HETATM10364  O2  SO4 D1102    -126.502  15.653 -14.105  1.00 51.19           O  
ANISOU10364  O2  SO4 D1102     6390   6819   6239   -725    478   -146       O  
HETATM10365  O3  SO4 D1102    -127.991  16.615 -12.317  1.00 61.22           O  
ANISOU10365  O3  SO4 D1102     7557   8295   7407   -698    483   -103       O  
HETATM10366  O4  SO4 D1102    -125.652  16.884 -12.090  1.00 50.54           O  
ANISOU10366  O4  SO4 D1102     6278   6848   6076   -615    475   -107       O  
HETATM10367  S   SO4 D1103    -113.863  21.268  -2.874  0.50 37.58           S  
ANISOU10367  S   SO4 D1103     4490   5558   4231    141    293   -305       S  
HETATM10368  O1  SO4 D1103    -112.447  21.654  -2.817  0.50 40.29           O  
ANISOU10368  O1  SO4 D1103     4833   5863   4612    178    265   -354       O  
HETATM10369  O2  SO4 D1103    -114.345  21.304  -4.286  0.50 37.63           O  
ANISOU10369  O2  SO4 D1103     4549   5440   4308     61    303   -296       O  
HETATM10370  O3  SO4 D1103    -114.028  19.896  -2.367  0.50 42.18           O  
ANISOU10370  O3  SO4 D1103     5087   6182   4758    133    347   -189       O  
HETATM10371  O4  SO4 D1103    -114.605  22.205  -2.022  0.50 39.62           O  
ANISOU10371  O4  SO4 D1103     4675   5941   4438    196    254   -381       O  
HETATM10372  N1  2YQ D1104    -120.146  19.642 -22.258  1.00 25.68           N  
ANISOU10372  N1  2YQ D1104     3309   3414   3033   -445    398   -352       N  
HETATM10373  N3  2YQ D1104    -122.729  21.210 -19.390  1.00 27.63           N  
ANISOU10373  N3  2YQ D1104     3483   3756   3258   -472    372   -345       N  
HETATM10374  C4  2YQ D1104    -118.968  18.368 -20.577  1.00 24.07           C  
ANISOU10374  C4  2YQ D1104     3157   3117   2872   -457    414   -323       C  
HETATM10375  C5  2YQ D1104    -122.081  21.079 -21.723  1.00 27.82           C  
ANISOU10375  C5  2YQ D1104     3521   3770   3279   -456    376   -357       C  
HETATM10376  C6  2YQ D1104    -122.581  22.004 -20.585  1.00 27.90           C  
ANISOU10376  C6  2YQ D1104     3506   3802   3293   -445    362   -348       C  
HETATM10377  C7  2YQ D1104    -121.735  20.344 -19.022  1.00 27.28           C  
ANISOU10377  C7  2YQ D1104     3474   3657   3235   -476    386   -328       C  
HETATM10378  C8  2YQ D1104    -121.621  19.992 -17.666  1.00 26.57           C  
ANISOU10378  C8  2YQ D1104     3385   3564   3145   -480    393   -307       C  
HETATM10379  C10 2YQ D1104    -119.735  18.566 -18.211  1.00 24.44           C  
ANISOU10379  C10 2YQ D1104     3183   3187   2915   -475    415   -288       C  
HETATM10380  C13 2YQ D1104    -126.182  22.193 -21.606  1.00 30.71           C  
ANISOU10380  C13 2YQ D1104     3783   4325   3562   -498    347   -415       C  
HETATM10381  C15 2YQ D1104    -125.104  24.267 -22.184  1.00 30.13           C  
ANISOU10381  C15 2YQ D1104     3692   4234   3521   -408    326   -372       C  
HETATM10382  C17 2YQ D1104    -121.729  21.889 -22.932  1.00 29.98           C  
ANISOU10382  C17 2YQ D1104     3777   4068   3545   -417    371   -345       C  
HETATM10383  F2  2YQ D1104    -127.363  23.913 -22.658  1.00 31.12           F  
ANISOU10383  F2  2YQ D1104     3774   4473   3577   -448    322   -422       F  
HETATM10384  C14 2YQ D1104    -126.221  23.458 -22.168  1.00 30.44           C  
ANISOU10384  C14 2YQ D1104     3724   4318   3523   -451    332   -405       C  
HETATM10385  C12 2YQ D1104    -124.993  21.726 -21.075  1.00 31.13           C  
ANISOU10385  C12 2YQ D1104     3871   4310   3646   -495    358   -393       C  
HETATM10386  C16 2YQ D1104    -123.913  23.776 -21.648  1.00 29.16           C  
ANISOU10386  C16 2YQ D1104     3604   4047   3429   -410    336   -356       C  
HETATM10387  C11 2YQ D1104    -123.858  22.522 -21.087  1.00 28.49           C  
ANISOU10387  C11 2YQ D1104     3546   3940   3338   -450    352   -368       C  
HETATM10388  N6  2YQ D1104    -120.734  22.827 -23.118  1.00 31.78           N  
ANISOU10388  N6  2YQ D1104     3998   4278   3800   -376    367   -305       N  
HETATM10389  C18 2YQ D1104    -120.810  23.314 -24.378  1.00 34.21           C  
ANISOU10389  C18 2YQ D1104     4281   4630   4088   -351    368   -290       C  
HETATM10390  N5  2YQ D1104    -121.860  22.718 -25.004  1.00 32.92           N  
ANISOU10390  N5  2YQ D1104     4110   4518   3879   -372    369   -331       N  
HETATM10391  N4  2YQ D1104    -122.414  21.849 -24.060  1.00 32.35           N  
ANISOU10391  N4  2YQ D1104     4059   4423   3811   -417    370   -365       N  
HETATM10392  C19 2YQ D1104    -123.580  21.017 -24.504  1.00 33.97           C  
ANISOU10392  C19 2YQ D1104     4256   4669   3984   -455    369   -416       C  
HETATM10393  C3  2YQ D1104    -120.990  20.167 -21.320  1.00 26.50           C  
ANISOU10393  C3  2YQ D1104     3394   3541   3136   -459    390   -346       C  
HETATM10394  C2  2YQ D1104    -120.844  19.821 -19.965  1.00 25.84           C  
ANISOU10394  C2  2YQ D1104     3321   3433   3066   -470    395   -329       C  
HETATM10395  C9  2YQ D1104    -120.620  19.118 -17.262  1.00 25.67           C  
ANISOU10395  C9  2YQ D1104     3305   3397   3051   -479    408   -283       C  
HETATM10396  F1  2YQ D1104    -120.545  18.836 -15.934  1.00 28.31           F  
ANISOU10396  F1  2YQ D1104     3633   3744   3377   -474    415   -255       F  
HETATM10397  C1  2YQ D1104    -119.832  18.914 -19.574  1.00 24.78           C  
ANISOU10397  C1  2YQ D1104     3222   3241   2953   -470    408   -314       C  
HETATM10398  O   2YQ D1104    -118.045  17.549 -20.297  1.00 24.03           O  
ANISOU10398  O   2YQ D1104     3184   3061   2886   -451    425   -313       O  
HETATM10399  N2  2YQ D1104    -119.120  18.715 -21.880  1.00 23.83           N  
ANISOU10399  N2  2YQ D1104     3113   3120   2823   -444    409   -344       N  
HETATM10400  O   HOH A1201     -38.125  -0.441 -31.066  1.00 37.54           O  
HETATM10401  O   HOH A1202     -51.481  25.262   1.204  0.50 28.02           O  
HETATM10402  O   HOH A1203     -27.878  26.141 -10.981  1.00 31.58           O  
HETATM10403  O   HOH A1204     -60.983  21.091   1.825  1.00 45.05           O  
HETATM10404  O   HOH A1205     -39.100  16.514   8.146  1.00 24.61           O  
HETATM10405  O   HOH A1206     -61.042   4.782   5.203  1.00 35.35           O  
HETATM10406  O   HOH A1207     -31.823  16.848   5.084  1.00 52.45           O  
HETATM10407  O   HOH A1208     -45.980  14.893  10.715  1.00 34.21           O  
HETATM10408  O   HOH A1209     -30.639 -19.228 -15.276  1.00 39.13           O  
HETATM10409  O   HOH A1210     -32.146  -0.107   6.155  1.00 37.86           O  
HETATM10410  O   HOH A1211     -38.742   2.491 -30.911  1.00 50.75           O  
HETATM10411  O   HOH A1212     -35.251   8.198   5.816  1.00 42.75           O  
HETATM10412  O   HOH A1213     -30.599   2.244   5.363  1.00 55.72           O  
HETATM10413  O   HOH A1214     -27.655   8.593  -0.595  1.00 56.90           O  
HETATM10414  O   HOH A1215     -36.326  23.793   5.401  1.00 50.22           O  
HETATM10415  O   HOH A1216     -67.717  20.672   1.890  1.00 46.59           O  
HETATM10416  O   HOH A1217     -38.512   6.102   6.845  0.50 13.85           O  
HETATM10417  O   HOH A1218     -31.551  21.720 -18.925  1.00 42.35           O  
HETATM10418  O   HOH A1219     -57.784   4.540 -25.509  1.00 24.12           O  
HETATM10419  O   HOH A1220     -36.131  11.082  -7.300  1.00 19.46           O  
HETATM10420  O   HOH A1221     -50.853   3.881  -2.985  1.00 20.60           O  
HETATM10421  O   HOH A1222     -52.033   3.069  -5.316  1.00 20.41           O  
HETATM10422  O   HOH A1223     -45.108   0.225  -5.767  1.00 33.53           O  
HETATM10423  O   HOH A1224     -43.560   0.305 -18.259  1.00 18.03           O  
HETATM10424  O   HOH A1225     -35.348   4.896 -20.021  1.00 37.56           O  
HETATM10425  O   HOH A1226     -56.405  -0.623  -1.621  1.00 32.66           O  
HETATM10426  O   HOH A1227     -56.808  -3.812  -6.451  1.00 29.82           O  
HETATM10427  O   HOH A1228     -46.234   0.442   1.564  1.00 31.13           O  
HETATM10428  O   HOH A1229     -48.647   4.011   4.315  1.00 30.92           O  
HETATM10429  O   HOH A1230     -43.604   9.544   7.656  1.00 35.23           O  
HETATM10430  O   HOH A1231     -42.128   5.746  -5.886  1.00 16.02           O  
HETATM10431  O   HOH A1232     -34.572   9.823  -5.725  1.00 26.87           O  
HETATM10432  O   HOH A1233     -60.001  -6.860 -11.928  1.00 28.68           O  
HETATM10433  O   HOH A1234     -65.988  -2.383 -16.519  1.00 37.66           O  
HETATM10434  O   HOH A1235     -61.013   4.302 -28.454  1.00 40.15           O  
HETATM10435  O   HOH A1236     -35.775  11.345 -11.271  1.00 32.14           O  
HETATM10436  O   HOH A1237     -55.341   8.433 -27.729  1.00 44.92           O  
HETATM10437  O   HOH A1238     -37.921   4.362 -20.388  1.00 25.39           O  
HETATM10438  O   HOH A1239     -43.565   1.410  -7.698  1.00 31.54           O  
HETATM10439  O   HOH A1240     -51.611   3.861   5.598  1.00 39.36           O  
HETATM10440  O   HOH A1241     -47.464  12.190   3.167  1.00 17.54           O  
HETATM10441  O   HOH A1242     -41.971  16.686 -12.880  1.00 20.51           O  
HETATM10442  O   HOH A1243     -50.174  23.516 -16.038  1.00 23.60           O  
HETATM10443  O   HOH A1244     -53.631  -2.544 -24.644  1.00 29.30           O  
HETATM10444  O   HOH A1245     -48.326  23.949  -0.207  1.00 33.52           O  
HETATM10445  O   HOH A1246     -57.864   3.347  -8.214  1.00 25.73           O  
HETATM10446  O   HOH A1247     -46.251  -7.431 -11.092  1.00 26.12           O  
HETATM10447  O   HOH A1248     -46.912  -6.983 -14.500  1.00 25.74           O  
HETATM10448  O   HOH A1249     -41.429  20.083 -13.557  1.00 21.02           O  
HETATM10449  O   HOH A1250     -36.470  10.527 -15.109  1.00 20.41           O  
HETATM10450  O   HOH A1251     -47.529  16.093   9.074  1.00 45.53           O  
HETATM10451  O   HOH A1252     -37.366  -0.925  -1.943  1.00 29.92           O  
HETATM10452  O   HOH A1253     -44.622  11.857   7.776  1.00 23.14           O  
HETATM10453  O   HOH A1254     -42.475  24.405   2.509  1.00 26.62           O  
HETATM10454  O   HOH A1255     -51.039   0.538  -2.105  1.00 25.22           O  
HETATM10455  O   HOH A1256     -40.233  24.430  -9.213  1.00 29.22           O  
HETATM10456  O   HOH A1257     -32.621  -2.849 -11.183  1.00 46.06           O  
HETATM10457  O   HOH A1258     -40.986  -1.897 -18.615  1.00 31.80           O  
HETATM10458  O   HOH A1259     -37.275   7.412   4.717  1.00 35.10           O  
HETATM10459  O   HOH A1260     -40.387   4.075  -1.433  1.00 25.68           O  
HETATM10460  O   HOH A1261     -35.188  12.673  -9.004  1.00 27.00           O  
HETATM10461  O   HOH A1262     -50.586  -7.664 -25.172  1.00 42.41           O  
HETATM10462  O   HOH A1263     -24.929 -16.670  -6.939  1.00 47.42           O  
HETATM10463  O   HOH A1264     -49.840  12.966 -26.658  1.00 34.15           O  
HETATM10464  O   HOH A1265     -38.765  21.058 -20.525  1.00 38.68           O  
HETATM10465  O   HOH A1266     -57.693   2.724 -27.146  1.00 33.56           O  
HETATM10466  O   HOH A1267     -33.042  -0.108 -12.160  1.00 44.72           O  
HETATM10467  O   HOH A1268     -64.282  -0.313 -21.577  1.00 32.68           O  
HETATM10468  O   HOH A1269     -50.689  10.165   6.845  1.00 41.19           O  
HETATM10469  O   HOH A1270     -55.779   5.318  -1.547  1.00 38.78           O  
HETATM10470  O   HOH A1271     -36.362   0.816  -3.509  1.00 39.01           O  
HETATM10471  O   HOH A1272     -40.270   3.152 -10.191  1.00 21.59           O  
HETATM10472  O   HOH A1273     -35.222  22.483 -16.252  1.00 30.04           O  
HETATM10473  O   HOH A1274     -31.833   2.057  -2.388  1.00 33.23           O  
HETATM10474  O   HOH A1275     -40.254   2.044   4.962  1.00 31.02           O  
HETATM10475  O   HOH A1276     -60.729  10.254  -6.372  1.00 38.49           O  
HETATM10476  O   HOH A1277     -59.920   1.682 -28.082  1.00 44.75           O  
HETATM10477  O   HOH A1278     -55.843  -3.164  -0.947  1.00 41.08           O  
HETATM10478  O   HOH A1279     -57.145   5.225   4.849  1.00 35.13           O  
HETATM10479  O   HOH A1280     -32.894   2.169  -5.062  1.00 46.10           O  
HETATM10480  O   HOH A1281     -35.247   3.304   6.519  0.50 21.59           O  
HETATM10481  O   HOH A1282     -24.042  -8.574  -9.295  1.00 52.80           O  
HETATM10482  O   HOH A1283     -20.974  -4.520  -8.484  1.00 52.99           O  
HETATM10483  O   HOH A1284     -64.650   6.903 -22.860  0.50 10.70           O  
HETATM10484  O   HOH A1285     -56.217   6.149 -26.789  1.00 38.42           O  
HETATM10485  O   HOH A1286     -64.861  10.242 -21.589  1.00 49.69           O  
HETATM10486  O   HOH A1287     -32.404   6.656 -28.412  1.00 49.69           O  
HETATM10487  O   HOH A1288     -62.703   1.797 -14.228  1.00 31.83           O  
HETATM10488  O   HOH A1289     -60.431   5.642  -9.493  1.00 41.78           O  
HETATM10489  O   HOH A1290     -60.601   6.087 -11.919  1.00 41.26           O  
HETATM10490  O   HOH A1291     -61.069  11.605 -13.829  1.00 38.52           O  
HETATM10491  O   HOH A1292     -34.665   3.132 -11.954  1.00 42.98           O  
HETATM10492  O   HOH A1293     -34.368  21.396 -18.392  0.50 16.85           O  
HETATM10493  O   HOH A1294     -49.276  25.456 -22.095  0.50 21.02           O  
HETATM10494  O   HOH A1295     -63.009  -4.454 -28.513  1.00 36.29           O  
HETATM10495  O   HOH A1296     -39.922  30.526 -19.150  1.00 36.82           O  
HETATM10496  O   HOH A1297     -58.856  23.707  -8.687  0.50 38.99           O  
HETATM10497  O   HOH A1298     -49.208  24.086 -12.282  1.00 47.02           O  
HETATM10498  O   HOH A1299     -60.059  -0.119   1.673  0.50 14.00           O  
HETATM10499  O   HOH A1300     -38.669   1.863 -12.282  0.50 18.16           O  
HETATM10500  O   HOH A1301     -44.085  17.175 -27.117  1.00 46.60           O  
HETATM10501  O   HOH A1302     -62.495   8.342  -1.726  1.00 34.69           O  
HETATM10502  O   HOH A1303     -34.874   5.710 -22.043  1.00 42.57           O  
HETATM10503  O   HOH A1304     -48.207   5.873   6.560  1.00 59.81           O  
HETATM10504  O   HOH A1305     -29.875  10.576  -1.905  1.00 52.51           O  
HETATM10505  O   HOH A1306     -56.612  23.571  -4.001  1.00 46.83           O  
HETATM10506  O   HOH A1307     -53.229  21.737  -7.599  1.00 42.08           O  
HETATM10507  O   HOH A1308     -57.400  20.610  -5.449  1.00 37.64           O  
HETATM10508  O   HOH B1201     -74.156  16.913   8.753  1.00 43.19           O  
HETATM10509  O   HOH B1202     -75.111  16.083   5.297  1.00 27.68           O  
HETATM10510  O   HOH B1203     -77.615  19.553  14.002  1.00 30.17           O  
HETATM10511  O   HOH B1204     -72.168   5.309  -9.096  1.00 31.47           O  
HETATM10512  O   HOH B1205     -76.470  -0.826  -0.354  1.00 22.57           O  
HETATM10513  O   HOH B1206     -78.073   0.472  -2.258  1.00 21.18           O  
HETATM10514  O   HOH B1207     -70.333  -6.732  -1.377  1.00 22.13           O  
HETATM10515  O   HOH B1208     -66.896  -0.072   0.368  1.00 40.98           O  
HETATM10516  O   HOH B1209     -70.703  -0.771   2.443  1.00 21.49           O  
HETATM10517  O   HOH B1210     -94.982   1.504   1.555  1.00 40.20           O  
HETATM10518  O   HOH B1211     -66.094 -10.802   2.791  1.00 40.28           O  
HETATM10519  O   HOH B1212     -65.425  -2.953   8.006  1.00 35.27           O  
HETATM10520  O   HOH B1213     -83.359   9.058  -5.778  1.00 21.91           O  
HETATM10521  O   HOH B1214     -77.195  -2.445  -4.270  1.00 31.53           O  
HETATM10522  O   HOH B1215     -90.111  10.038  12.298  1.00 27.46           O  
HETATM10523  O   HOH B1216     -80.548   2.086  -9.208  1.00 33.15           O  
HETATM10524  O   HOH B1217     -92.936  -0.429  11.083  1.00 29.12           O  
HETATM10525  O   HOH B1218     -88.887   7.118  10.996  1.00 28.98           O  
HETATM10526  O   HOH B1219     -83.708  -9.551  10.790  1.00 23.22           O  
HETATM10527  O   HOH B1220     -86.937  19.279   1.214  0.50 28.09           O  
HETATM10528  O   HOH B1221     -86.926  -0.881   0.792  1.00 27.15           O  
HETATM10529  O   HOH B1222     -69.735   7.255   3.421  1.00 26.97           O  
HETATM10530  O   HOH B1223     -61.305  -6.587   8.868  1.00 47.11           O  
HETATM10531  O   HOH B1224     -93.531   2.351   3.560  1.00 26.95           O  
HETATM10532  O   HOH B1225     -82.500  -5.165  -1.072  1.00 25.86           O  
HETATM10533  O   HOH B1226     -85.851 -12.331  10.521  1.00 41.41           O  
HETATM10534  O   HOH B1227     -81.058 -16.396   8.171  1.00 60.84           O  
HETATM10535  O   HOH B1228     -67.921   0.112  -7.638  1.00 36.83           O  
HETATM10536  O   HOH B1229     -72.947 -12.049  15.939  1.00 36.57           O  
HETATM10537  O   HOH B1230     -71.168  13.936  -8.285  1.00 32.74           O  
HETATM10538  O   HOH B1231     -73.676   3.260  -3.290  1.00 33.06           O  
HETATM10539  O   HOH B1232     -88.225  -1.506  -4.205  1.00 37.61           O  
HETATM10540  O   HOH B1233     -79.283 -14.267   4.877  1.00 41.82           O  
HETATM10541  O   HOH B1234     -78.901  16.506 -10.324  1.00 45.52           O  
HETATM10542  O   HOH B1235     -63.411  -8.850  11.809  1.00 39.92           O  
HETATM10543  O   HOH B1236     -69.992  -4.526  18.988  1.00 37.72           O  
HETATM10544  O   HOH B1237     -66.437  20.117  -4.516  1.00 51.33           O  
HETATM10545  O   HOH B1238     -81.932  -2.614  -7.674  1.00 33.16           O  
HETATM10546  O   HOH B1239     -89.570  -7.316  14.039  1.00 40.45           O  
HETATM10547  O   HOH B1240     -77.324   3.507 -10.278  1.00 45.04           O  
HETATM10548  O   HOH B1241     -68.399   5.393   9.879  1.00 46.91           O  
HETATM10549  O   HOH B1242     -69.797  -5.966  -3.604  1.00 34.16           O  
HETATM10550  O   HOH B1243     -95.277   2.844   5.247  1.00 52.59           O  
HETATM10551  O   HOH B1244     -60.811   4.456  -7.152  1.00 28.00           O  
HETATM10552  O   HOH B1245     -87.388 -14.108   8.968  1.00 55.78           O  
HETATM10553  O   HOH B1246     -92.079  -7.259  14.202  1.00 43.07           O  
HETATM10554  O   HOH B1247     -63.097   9.278 -10.893  1.00 52.04           O  
HETATM10555  O   HOH B1248     -68.759  10.334   5.798  1.00 48.52           O  
HETATM10556  O   HOH B1249     -67.791   7.277  -1.589  1.00 36.50           O  
HETATM10557  O   HOH B1250     -72.864  18.980  -0.446  1.00 52.23           O  
HETATM10558  O   HOH B1251     -68.994   1.952   4.613  0.50 14.81           O  
HETATM10559  O   HOH B1252     -85.625  -4.882   2.732  1.00 36.79           O  
HETATM10560  O   HOH B1253     -90.719  19.311  -1.051  1.00 38.85           O  
HETATM10561  O   HOH B1254     -96.970  10.121  15.407  1.00 41.15           O  
HETATM10562  O   HOH B1255     -95.849  -2.587   5.603  1.00 48.97           O  
HETATM10563  O   HOH C1201     -71.879  13.885 -42.643  1.00 44.82           O  
HETATM10564  O   HOH C1202     -86.539  35.710  -8.048  1.00 37.51           O  
HETATM10565  O   HOH C1203     -85.503  32.233  -9.225  1.00 29.92           O  
HETATM10566  O   HOH C1204     -72.221  32.304 -55.047  1.00 39.04           O  
HETATM10567  O   HOH C1205     -82.986  40.294  -4.783  1.00 32.93           O  
HETATM10568  O   HOH C1206     -80.429  41.069  -2.747  0.50 28.45           O  
HETATM10569  O   HOH C1207     -85.201  30.847  -6.614  1.00 40.08           O  
HETATM10570  O   HOH C1208     -73.717  32.543 -53.103  1.00 35.75           O  
HETATM10571  O   HOH C1209     -75.138  34.141  -7.016  1.00 33.43           O  
HETATM10572  O   HOH C1210     -73.749  22.675  -2.792  1.00 45.64           O  
HETATM10573  O   HOH C1211     -79.118  50.376  -9.348  1.00 41.35           O  
HETATM10574  O   HOH C1212     -63.347  22.655 -21.114  1.00 42.21           O  
HETATM10575  O   HOH C1213     -82.232  26.587 -25.567  1.00 19.51           O  
HETATM10576  O   HOH C1214     -69.899  24.860  -6.329  1.00 27.56           O  
HETATM10577  O   HOH C1215     -65.990  35.727 -22.898  1.00 35.32           O  
HETATM10578  O   HOH C1216     -91.119  33.230 -23.454  1.00 43.18           O  
HETATM10579  O   HOH C1217     -88.640  24.571 -28.692  1.00 46.44           O  
HETATM10580  O   HOH C1218     -74.540  17.293 -17.574  1.00 39.33           O  
HETATM10581  O   HOH C1219     -89.290  31.815 -26.049  1.00 20.52           O  
HETATM10582  O   HOH C1220     -83.545  28.642 -26.617  1.00 21.64           O  
HETATM10583  O   HOH C1221     -83.028  24.947 -28.696  1.00 23.41           O  
HETATM10584  O   HOH C1222     -69.747  39.659 -14.021  1.00 22.56           O  
HETATM10585  O   HOH C1223     -94.106  37.526 -27.379  1.00 36.81           O  
HETATM10586  O   HOH C1224     -71.810  33.595 -29.708  1.00 25.23           O  
HETATM10587  O   HOH C1225     -71.720  24.944 -27.500  1.00 26.60           O  
HETATM10588  O   HOH C1226     -78.142  21.410 -29.072  1.00 26.51           O  
HETATM10589  O   HOH C1227     -66.715  39.355 -24.180  1.00 21.28           O  
HETATM10590  O   HOH C1228     -79.733  19.388 -24.730  1.00 27.20           O  
HETATM10591  O   HOH C1229     -77.147  21.963 -17.185  1.00 16.01           O  
HETATM10592  O   HOH C1230     -68.464  26.173 -30.869  1.00 23.68           O  
HETATM10593  O   HOH C1231     -92.450  26.511 -18.655  1.00 39.84           O  
HETATM10594  O   HOH C1232     -52.042  24.579 -30.102  1.00 39.04           O  
HETATM10595  O   HOH C1233     -86.633  25.294 -22.964  1.00 27.74           O  
HETATM10596  O   HOH C1234     -59.994  25.556 -50.337  1.00 36.99           O  
HETATM10597  O   HOH C1235     -65.581  15.680 -30.982  1.00 33.40           O  
HETATM10598  O   HOH C1236     -90.531  31.423 -18.116  1.00 38.06           O  
HETATM10599  O   HOH C1237     -76.826  19.256 -16.974  0.50 24.25           O  
HETATM10600  O   HOH C1238     -92.759  29.141 -18.353  1.00 50.03           O  
HETATM10601  O   HOH C1239     -64.227  24.569 -30.591  1.00 33.64           O  
HETATM10602  O   HOH C1240     -64.983  19.978 -21.188  1.00 49.82           O  
HETATM10603  O   HOH C1241     -65.859  26.999 -30.753  1.00 32.96           O  
HETATM10604  O   HOH C1242     -71.457  22.894 -47.087  1.00 38.92           O  
HETATM10605  O   HOH C1243     -73.524  40.529 -36.205  1.00 26.34           O  
HETATM10606  O   HOH C1244     -78.770  37.375 -42.630  1.00 33.21           O  
HETATM10607  O   HOH C1245     -80.231  35.722 -38.962  1.00 26.72           O  
HETATM10608  O   HOH C1246     -79.748  32.338 -38.855  1.00 27.20           O  
HETATM10609  O   HOH C1247     -56.748  12.402 -35.748  1.00 38.07           O  
HETATM10610  O   HOH C1248     -93.342  33.224 -36.231  1.00 42.51           O  
HETATM10611  O   HOH C1249     -89.524  28.697 -32.645  1.00 30.45           O  
HETATM10612  O   HOH C1250     -96.276  42.274 -32.886  1.00 45.61           O  
HETATM10613  O   HOH C1251     -88.990  48.782 -27.549  1.00 31.56           O  
HETATM10614  O   HOH C1252     -79.788  51.761 -21.347  1.00 42.89           O  
HETATM10615  O   HOH C1253     -67.001  46.683 -14.831  1.00 34.46           O  
HETATM10616  O   HOH C1254     -63.250  42.385 -13.321  1.00 33.02           O  
HETATM10617  O   HOH C1255     -73.304  51.857 -22.985  1.00 48.37           O  
HETATM10618  O   HOH C1256     -73.222  29.413 -26.053  1.00 18.81           O  
HETATM10619  O   HOH C1257     -75.881  40.717 -33.481  1.00 22.43           O  
HETATM10620  O   HOH C1258     -67.691  19.447 -23.463  1.00 35.24           O  
HETATM10621  O   HOH C1259     -70.967  38.506 -17.056  1.00 19.79           O  
HETATM10622  O   HOH C1260     -76.307  27.732  -6.587  1.00 33.94           O  
HETATM10623  O   HOH C1261     -62.704  40.822  -7.064  1.00 43.12           O  
HETATM10624  O   HOH C1262     -77.519  42.991  -9.297  1.00 28.58           O  
HETATM10625  O   HOH C1263     -61.409  33.506  -3.967  1.00 53.63           O  
HETATM10626  O   HOH C1264     -73.951  27.635 -27.940  1.00 35.75           O  
HETATM10627  O   HOH C1265     -96.525  44.286 -31.126  1.00 44.75           O  
HETATM10628  O   HOH C1266     -64.615  38.114 -22.288  1.00 38.23           O  
HETATM10629  O   HOH C1267     -66.382  34.988 -31.158  1.00 41.98           O  
HETATM10630  O   HOH C1268     -70.594  35.256 -31.484  1.00 26.57           O  
HETATM10631  O   HOH C1269     -59.675  24.881 -24.787  1.00 57.58           O  
HETATM10632  O   HOH C1270     -61.519  15.964 -30.007  1.00 41.74           O  
HETATM10633  O   HOH C1271     -74.237  30.003 -34.574  1.00 33.89           O  
HETATM10634  O   HOH C1272     -97.974  39.949 -33.573  1.00 47.54           O  
HETATM10635  O   HOH C1273     -83.892  52.511 -16.953  1.00 46.40           O  
HETATM10636  O   HOH C1274     -69.595  43.424 -30.951  1.00 28.07           O  
HETATM10637  O   HOH C1275     -62.214  26.172  -9.778  1.00 41.21           O  
HETATM10638  O   HOH C1276     -78.515  19.447 -27.253  1.00 40.03           O  
HETATM10639  O   HOH C1277     -59.466  26.094 -22.190  1.00 56.32           O  
HETATM10640  O   HOH C1278     -99.659  21.939 -23.086  1.00 42.42           O  
HETATM10641  O   HOH C1279     -67.164  43.887 -30.860  1.00 46.23           O  
HETATM10642  O   HOH C1280     -58.173  29.052 -39.183  1.00 37.51           O  
HETATM10643  O   HOH C1281     -78.905  22.561 -38.446  1.00 44.01           O  
HETATM10644  O   HOH C1282     -81.523  22.251 -39.218  1.00 36.46           O  
HETATM10645  O   HOH C1283     -77.884  23.924 -40.950  1.00 41.01           O  
HETATM10646  O   HOH C1284     -90.207  26.508 -32.187  1.00 37.79           O  
HETATM10647  O   HOH C1285     -57.693  26.571 -26.324  0.50 37.38           O  
HETATM10648  O   HOH C1286     -77.890  18.358 -14.609  1.00 48.73           O  
HETATM10649  O   HOH C1287     -49.688  10.636 -28.112  1.00 36.83           O  
HETATM10650  O   HOH C1288     -78.441  39.220 -40.704  1.00 38.39           O  
HETATM10651  O   HOH C1289     -78.694  34.791 -41.729  1.00 47.17           O  
HETATM10652  O   HOH C1290     -79.173  23.479 -35.872  1.00 43.94           O  
HETATM10653  O   HOH C1291     -77.480  20.045 -38.289  1.00 41.43           O  
HETATM10654  O   HOH C1292     -76.393  40.794 -40.539  1.00 39.39           O  
HETATM10655  O   HOH C1293     -78.727  42.530 -41.474  1.00 39.16           O  
HETATM10656  O   HOH C1294     -83.087  22.146 -31.221  1.00 44.32           O  
HETATM10657  O   HOH C1295     -74.513  31.665 -30.325  1.00 38.94           O  
HETATM10658  O   HOH C1296     -77.389  28.442 -30.649  1.00 22.83           O  
HETATM10659  O   HOH C1297     -65.016  38.459 -26.913  1.00 56.99           O  
HETATM10660  O   HOH C1298     -65.084  31.624 -31.378  1.00 51.00           O  
HETATM10661  O   HOH C1299     -72.389  40.288 -42.363  1.00 42.02           O  
HETATM10662  O   HOH C1300     -74.267  25.568 -32.352  1.00 48.77           O  
HETATM10663  O   HOH D1201    -133.263  17.367  -3.107  1.00 35.99           O  
HETATM10664  O   HOH D1202     -99.491  31.381 -12.230  1.00 37.37           O  
HETATM10665  O   HOH D1203    -125.265  34.699  -8.220  1.00 43.91           O  
HETATM10666  O   HOH D1204    -129.058  35.683 -19.019  1.00 44.93           O  
HETATM10667  O   HOH D1205    -121.218  37.008 -10.264  1.00 29.98           O  
HETATM10668  O   HOH D1206     -99.813  29.365  -5.212  0.50 28.00           O  
HETATM10669  O   HOH D1207    -118.734  30.981  -2.862  1.00 31.00           O  
HETATM10670  O   HOH D1208    -132.949  14.644  -4.297  1.00 51.91           O  
HETATM10671  O   HOH D1209    -124.317  34.360  -3.563  1.00 44.89           O  
HETATM10672  O   HOH D1210    -108.382  24.076 -24.222  1.00 33.99           O  
HETATM10673  O   HOH D1211    -109.451  26.367 -23.237  1.00 26.23           O  
HETATM10674  O   HOH D1212    -124.549  22.054 -17.175  1.00 28.26           O  
HETATM10675  O   HOH D1213    -124.570  14.473 -17.914  1.00 33.18           O  
HETATM10676  O   HOH D1214    -113.045  32.040 -14.906  1.00 19.99           O  
HETATM10677  O   HOH D1215    -102.321  20.939 -23.907  1.00 37.09           O  
HETATM10678  O   HOH D1216    -119.399  16.073 -11.638  1.00 27.11           O  
HETATM10679  O   HOH D1217     -95.341  27.870 -17.059  1.00 37.05           O  
HETATM10680  O   HOH D1218     -98.072  27.080 -17.955  1.00 32.27           O  
HETATM10681  O   HOH D1219     -92.901  30.710 -20.691  1.00 33.43           O  
HETATM10682  O   HOH D1220    -122.662  34.095 -19.732  1.00 42.84           O  
HETATM10683  O   HOH D1221    -115.140  12.464 -36.064  1.00 57.60           O  
HETATM10684  O   HOH D1222    -113.955  18.928 -35.557  1.00 41.57           O  
HETATM10685  O   HOH D1223    -128.965  11.005 -13.738  1.00 38.00           O  
HETATM10686  O   HOH D1224    -104.506  27.649 -21.480  1.00 37.72           O  
HETATM10687  O   HOH D1225    -103.802  23.049  -6.692  1.00 47.46           O  
HETATM10688  O   HOH D1226    -116.999  11.322 -28.244  1.00 41.74           O  
HETATM10689  O   HOH D1227    -109.085  27.595 -26.728  1.00 34.80           O  
HETATM10690  O   HOH D1228    -113.801  31.288 -26.731  1.00 32.69           O  
HETATM10691  O   HOH D1229    -122.448  27.966 -28.710  1.00 37.31           O  
HETATM10692  O   HOH D1230    -126.046  24.142 -18.231  1.00 39.52           O  
HETATM10693  O   HOH D1231    -126.064  20.392 -15.477  1.00 36.43           O  
HETATM10694  O   HOH D1232    -119.977  15.295  -8.343  1.00 32.26           O  
HETATM10695  O   HOH D1233    -122.596   9.481 -24.586  1.00 38.37           O  
HETATM10696  O   HOH D1234    -107.865  21.007  -6.650  1.00 51.12           O  
HETATM10697  O   HOH D1235    -119.726  11.419 -31.072  1.00 41.20           O  
HETATM10698  O   HOH D1236     -91.966  31.078 -24.021  1.00 34.88           O  
HETATM10699  O   HOH D1237    -120.212  19.376 -25.068  1.00 37.34           O  
HETATM10700  O   HOH D1238    -119.511  27.538 -31.486  1.00 47.72           O  
HETATM10701  O   HOH D1239    -130.148  28.352 -17.675  0.50 25.72           O  
HETATM10702  O   HOH D1240    -120.079  12.737 -33.511  1.00 43.79           O  
HETATM10703  O   HOH D1241    -113.176  28.178  -3.159  1.00 42.67           O  
HETATM10704  O   HOH D1242    -118.442  23.743 -22.016  1.00 27.33           O  
HETATM10705  O   HOH D1243    -118.646  20.765 -26.347  1.00 41.02           O  
HETATM10706  O   HOH D1244     -99.916  17.853 -34.440  1.00 41.17           O  
HETATM10707  O   HOH D1245    -102.986  33.899 -21.316  1.00 39.03           O  
HETATM10708  O   HOH D1246    -116.629  21.900 -26.426  1.00 40.84           O  
HETATM10709  O   HOH D1247    -125.161   9.753 -24.250  1.00 52.71           O  
HETATM10710  O   HOH D1248    -103.784  24.186  -4.118  1.00 48.78           O  
HETATM10711  O   HOH D1249    -115.152  23.993 -27.218  1.00 34.18           O  
HETATM10712  O   HOH D1250    -119.803  26.926 -28.289  1.00 39.51           O  
HETATM10713  O   HOH D1251    -117.644  26.203 -27.991  1.00 54.07           O  
HETATM10714  O   HOH D1252    -111.708  33.492 -23.110  1.00 30.87           O  
HETATM10715  O   HOH D1253    -112.714  33.431 -25.369  1.00 40.48           O  
CONECT 1323 3868                                                                
CONECT 3868 1323                                                                
CONECT 6477 8931                                                                
CONECT 8931 6477                                                                
CONECT1019510196101971019810199                                                 
CONECT1019610195                                                                
CONECT1019710195                                                                
CONECT1019810195                                                                
CONECT1019910195                                                                
CONECT1020010201102021020310204                                                 
CONECT1020110200                                                                
CONECT1020210200                                                                
CONECT1020310200                                                                
CONECT1020410200                                                                
CONECT1020510206102071020810209                                                 
CONECT1020610205                                                                
CONECT1020710205                                                                
CONECT1020810205                                                                
CONECT1020910205                                                                
CONECT1021010211102121021310214                                                 
CONECT1021110210                                                                
CONECT1021210210                                                                
CONECT1021310210                                                                
CONECT1021410210                                                                
CONECT102151023610242                                                           
CONECT102161021910220                                                           
CONECT10217102401024110242                                                      
CONECT10218102191022510236                                                      
CONECT10219102161021810230                                                      
CONECT10220102161022110237                                                      
CONECT102211022010238                                                           
CONECT102221023810240                                                           
CONECT102231022710228                                                           
CONECT102241022710229                                                           
CONECT10225102181023110234                                                      
CONECT1022610227                                                                
CONECT10227102231022410226                                                      
CONECT102281022310230                                                           
CONECT102291022410230                                                           
CONECT10230102191022810229                                                      
CONECT102311022510232                                                           
CONECT102321023110233                                                           
CONECT102331023210234                                                           
CONECT10234102251023310235                                                      
CONECT1023510234                                                                
CONECT10236102151021810237                                                      
CONECT10237102201023610240                                                      
CONECT10238102211022210239                                                      
CONECT1023910238                                                                
CONECT10240102171022210237                                                      
CONECT1024110217                                                                
CONECT102421021510217                                                           
CONECT102431024410245                                                           
CONECT1024410243                                                                
CONECT10245102431024610247                                                      
CONECT1024610245                                                                
CONECT102471024510248                                                           
CONECT1024810247                                                                
CONECT102491025010251                                                           
CONECT1025010249                                                                
CONECT10251102491025210253                                                      
CONECT1025210251                                                                
CONECT102531025110254                                                           
CONECT1025410253                                                                
CONECT1025510256102571025810259                                                 
CONECT1025610255                                                                
CONECT1025710255                                                                
CONECT1025810255                                                                
CONECT1025910255                                                                
CONECT1026010261102621026310264                                                 
CONECT1026110260                                                                
CONECT1026210260                                                                
CONECT1026310260                                                                
CONECT1026410260                                                                
CONECT1026510266102671026810269                                                 
CONECT1026610265                                                                
CONECT1026710265                                                                
CONECT1026810265                                                                
CONECT1026910265                                                                
CONECT1027010271102721027310274                                                 
CONECT1027110270                                                                
CONECT1027210270                                                                
CONECT1027310270                                                                
CONECT1027410270                                                                
CONECT102751029610302                                                           
CONECT102761027910280                                                           
CONECT10277103001030110302                                                      
CONECT10278102791028510296                                                      
CONECT10279102761027810290                                                      
CONECT10280102761028110297                                                      
CONECT102811028010298                                                           
CONECT102821029810300                                                           
CONECT102831028710288                                                           
CONECT102841028710289                                                           
CONECT10285102781029110294                                                      
CONECT1028610287                                                                
CONECT10287102831028410286                                                      
CONECT102881028310290                                                           
CONECT102891028410290                                                           
CONECT10290102791028810289                                                      
CONECT102911028510292                                                           
CONECT102921029110293                                                           
CONECT102931029210294                                                           
CONECT10294102851029310295                                                      
CONECT1029510294                                                                
CONECT10296102751027810297                                                      
CONECT10297102801029610300                                                      
CONECT10298102811028210299                                                      
CONECT1029910298                                                                
CONECT10300102771028210297                                                      
CONECT1030110277                                                                
CONECT103021027510277                                                           
CONECT1030310304103051030610307                                                 
CONECT1030410303                                                                
CONECT1030510303                                                                
CONECT1030610303                                                                
CONECT1030710303                                                                
CONECT1030810309103101031110312                                                 
CONECT1030910308                                                                
CONECT1031010308                                                                
CONECT1031110308                                                                
CONECT1031210308                                                                
CONECT1031310314103151031610317                                                 
CONECT1031410313                                                                
CONECT1031510313                                                                
CONECT1031610313                                                                
CONECT1031710313                                                                
CONECT1031810319103201032110322                                                 
CONECT1031910318                                                                
CONECT1032010318                                                                
CONECT1032110318                                                                
CONECT1032210318                                                                
CONECT103231034410350                                                           
CONECT103241032710328                                                           
CONECT10325103481034910350                                                      
CONECT10326103271033310344                                                      
CONECT10327103241032610338                                                      
CONECT10328103241032910345                                                      
CONECT103291032810346                                                           
CONECT103301034610348                                                           
CONECT103311033510336                                                           
CONECT103321033510337                                                           
CONECT10333103261033910342                                                      
CONECT1033410335                                                                
CONECT10335103311033210334                                                      
CONECT103361033110338                                                           
CONECT103371033210338                                                           
CONECT10338103271033610337                                                      
CONECT103391033310340                                                           
CONECT103401033910341                                                           
CONECT103411034010342                                                           
CONECT10342103331034110343                                                      
CONECT1034310342                                                                
CONECT10344103231032610345                                                      
CONECT10345103281034410348                                                      
CONECT10346103291033010347                                                      
CONECT1034710346                                                                
CONECT10348103251033010345                                                      
CONECT1034910325                                                                
CONECT103501032310325                                                           
CONECT103511035210353                                                           
CONECT1035210351                                                                
CONECT10353103511035410355                                                      
CONECT1035410353                                                                
CONECT103551035310356                                                           
CONECT1035610355                                                                
CONECT1035710358103591036010361                                                 
CONECT1035810357                                                                
CONECT1035910357                                                                
CONECT1036010357                                                                
CONECT1036110357                                                                
CONECT1036210363103641036510366                                                 
CONECT1036310362                                                                
CONECT1036410362                                                                
CONECT1036510362                                                                
CONECT1036610362                                                                
CONECT1036710368103691037010371                                                 
CONECT1036810367                                                                
CONECT1036910367                                                                
CONECT1037010367                                                                
CONECT1037110367                                                                
CONECT103721039310399                                                           
CONECT103731037610377                                                           
CONECT10374103971039810399                                                      
CONECT10375103761038210393                                                      
CONECT10376103731037510387                                                      
CONECT10377103731037810394                                                      
CONECT103781037710395                                                           
CONECT103791039510397                                                           
CONECT103801038410385                                                           
CONECT103811038410386                                                           
CONECT10382103751038810391                                                      
CONECT1038310384                                                                
CONECT10384103801038110383                                                      
CONECT103851038010387                                                           
CONECT103861038110387                                                           
CONECT10387103761038510386                                                      
CONECT103881038210389                                                           
CONECT103891038810390                                                           
CONECT103901038910391                                                           
CONECT10391103821039010392                                                      
CONECT1039210391                                                                
CONECT10393103721037510394                                                      
CONECT10394103771039310397                                                      
CONECT10395103781037910396                                                      
CONECT1039610395                                                                
CONECT10397103741037910394                                                      
CONECT1039810374                                                                
CONECT103991037210374                                                           
MASTER      753    0   22   63   57    0   44    610694    4  209  116          
END