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

HEADER    OXIDOREDUCTASE                          20-MAR-14   4CUM              
TITLE     STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME            
TITLE    2 DOMAIN IN COMPLEX WITH (9AS)-2-AMINO-9A-METHYL-6,7,8,9,9A,           
TITLE    3 10-HEXAHYDROBENZO[G]PTERIDIN-4(3H)-ONE                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HEME DOMAIN, RESIDUES 40-482;                              
COMPND   5 SYNONYM: CONSTITUTIVE NOS, CNOS, EC-NOS, ENDOTHELIAL NOS, ENOS, NOS  
COMPND   6  TYPE III, NOSIII, ENDOTHELIAL NITRIC OXIDE SYNTHASE;                
COMPND   7 EC: 1.14.13.39;                                                      
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PCWORI                                     
KEYWDS    OXIDOREDUCTASE, COFACTOR ANALOG COMPLEX                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.CHREIFI,H.LI,T.L.POULOS                                             
REVDAT   2   16-JUL-14 4CUM    1       JRNL                                     
REVDAT   1   28-MAY-14 4CUM    0                                                
JRNL        AUTH   G.CHREIFI,H.LI,C.R.MCINNES,C.L.GIBSON,C.J.SUCKLING,          
JRNL        AUTH 2 T.L.POULOS                                                   
JRNL        TITL   COMMUNICATION BETWEEN THE ZINC AND TETRAHYDROBIOPTERIN       
JRNL        TITL 2 BINDING SITES IN NITRIC OXIDE SYNTHASE.                      
JRNL        REF    BIOCHEMISTRY                  V.  53  4216 2014              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   24819538                                                     
JRNL        DOI    10.1021/BI5003986                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 88.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.58                          
REMARK   3   NUMBER OF REFLECTIONS             : 40040                          
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) : 0.17233                         
REMARK   3   R VALUE            (WORKING SET) : 0.16951                         
REMARK   3   FREE R VALUE                     : 0.22703                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2102                            
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) : 2.330                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.390                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2677                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.268                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 134                          
REMARK   3   BIN FREE R VALUE                    : 0.335                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6446                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 169                                     
REMARK   3   SOLVENT ATOMS            : 214                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.678                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.67                                                 
REMARK   3    B22 (A**2) : -1.87                                                
REMARK   3    B33 (A**2) : -1.81                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.295         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.223         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.169         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.626        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6803 ; 0.011 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9289 ; 2.042 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   806 ; 6.290 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   320 ;35.057 ;23.375       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1046 ;16.745 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;19.405 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   971 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5314 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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    67        A   482                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.0950  10.3440  31.6990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0881 T22:   0.0160                                     
REMARK   3      T33:   0.0336 T12:  -0.0261                                     
REMARK   3      T13:   0.0101 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8477 L22:   1.3868                                     
REMARK   3      L33:   1.6729 L12:  -0.2545                                     
REMARK   3      L13:  -0.4463 L23:   0.2649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0160 S12:   0.0057 S13:   0.0381                       
REMARK   3      S21:  -0.1765 S22:   0.0533 S23:  -0.1851                       
REMARK   3      S31:  -0.0620 S32:   0.1193 S33:  -0.0694                       
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    69        B   482                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.7620   5.6990  67.5850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0325 T22:   0.0340                                     
REMARK   3      T33:   0.0445 T12:  -0.0204                                     
REMARK   3      T13:   0.0091 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7333 L22:   1.3430                                     
REMARK   3      L33:   2.6453 L12:  -0.1747                                     
REMARK   3      L13:   0.4440 L23:  -0.7869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0618 S12:  -0.1065 S13:  -0.0674                       
REMARK   3      S21:   0.1064 S22:   0.0582 S23:   0.0243                       
REMARK   3      S31:   0.0753 S32:  -0.0954 S33:  -0.1200                       
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          
REMARK   3   RIDING POSITIONS. U VALUES WITH TLS WITH TLS ADDED.                
REMARK   3 RESIDUES 110 TO 120 IN CHAIN A AND 112-120 IN CHAIN B ARE            
REMARK   3 DISORDERED.                                                          
REMARK   4                                                                      
REMARK   4 4CUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-MAR-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-60023.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.12709                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (Q315R)                        
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42159                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.33                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.4                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.03                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.86                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.13                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.7                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG3350, 250MM MAGNESIUM          
REMARK 280  ACETATE, 100MM CACODYLATE PH 6.25 AND 5MM TCEP                      
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       29.00550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.24000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.24650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.24000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.00550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.24650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10950 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     ARG A    40                                                      
REMARK 465     ALA A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     THR A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     HIS A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     PRO A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     HIS A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     PRO A    54                                                      
REMARK 465     ALA A    55                                                      
REMARK 465     PRO A    56                                                      
REMARK 465     ASN A    57                                                      
REMARK 465     SER A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     LEU A    61                                                      
REMARK 465     THR A    62                                                      
REMARK 465     ARG A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     GLU A    66                                                      
REMARK 465     LYS A   110                                                      
REMARK 465     LEU A   111                                                      
REMARK 465     GLN A   112                                                      
REMARK 465     THR A   113                                                      
REMARK 465     ARG A   114                                                      
REMARK 465     PRO A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     PRO A   117                                                      
REMARK 465     GLY A   118                                                      
REMARK 465     PRO A   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     ARG B    40                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     PRO B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     THR B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     HIS B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     HIS B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     PRO B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     PRO B    56                                                      
REMARK 465     ASN B    57                                                      
REMARK 465     SER B    58                                                      
REMARK 465     PRO B    59                                                      
REMARK 465     THR B    60                                                      
REMARK 465     LEU B    61                                                      
REMARK 465     THR B    62                                                      
REMARK 465     ARG B    63                                                      
REMARK 465     PRO B    64                                                      
REMARK 465     PRO B    65                                                      
REMARK 465     GLU B    66                                                      
REMARK 465     GLY B    67                                                      
REMARK 465     PRO B    68                                                      
REMARK 465     GLN B   112                                                      
REMARK 465     THR B   113                                                      
REMARK 465     ARG B   114                                                      
REMARK 465     PRO B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     PRO B   117                                                      
REMARK 465     GLY B   118                                                      
REMARK 465     PRO B   119                                                      
REMARK 465     PRO B   120                                                      
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   O    HOH B  2036     O    HOH B  2037              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B 256   CE1   TYR B 256   CZ      0.101                       
REMARK 500    TYR B 256   CG    TYR B 256   CD1     0.120                       
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    PRO B 238   C   -  N   -  CA  ANGL. DEV. =   9.8 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    ALA A 122     -107.36     62.06                                   
REMARK 500    ASN A 285       38.71   -156.06                                   
REMARK 500    PHE A 288       44.06   -143.69                                   
REMARK 500    ALA A 353       65.01   -153.64                                   
REMARK 500    ARG A 374     -130.82   -120.40                                   
REMARK 500    LYS B 141       -3.04     72.04                                   
REMARK 500    SER B 145      178.65    -59.48                                   
REMARK 500    ASP B 260       27.74    -72.44                                   
REMARK 500    ASN B 285       24.86   -155.33                                   
REMARK 500    PHE B 288       41.12   -141.00                                   
REMARK 500    ALA B 353       65.07   -155.20                                   
REMARK 500    THR B 366      -60.60   -102.41                                   
REMARK 500    ARG B 374     -131.82   -114.12                                   
REMARK 500    ASP B 386       33.25     71.40                                   
REMARK 500    ASP B 388       98.46    -69.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 CACODYLIC ACID (CAD): DIMETHYL ARSENIC MOIETY FROM                   
REMARK 600  CACODYLIC ACID                                                      
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM A 500   NC                                                     
REMARK 620 2 CYS A 186   SG  104.1                                              
REMARK 620 3 HEM A 500   NA  152.4 103.4                                        
REMARK 620 4 HEM A 500   NB   87.8  94.1  87.8                                  
REMARK 620 5 HEM A 500   ND   91.0 103.1  85.3 162.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM B 500   ND                                                     
REMARK 620 2 HEM B 500   NA   85.7                                              
REMARK 620 3 HEM B 500   NB  161.0  86.7                                        
REMARK 620 4 HEM B 500   NC   89.4 151.2  88.8                                  
REMARK 620 5 CYS B 186   SG   98.3 106.8 100.6 102.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1483  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 101   SG                                                     
REMARK 620 2 CYS B  96   SG  104.6                                              
REMARK 620 3 CYS B 101   SG  105.5 110.2                                        
REMARK 620 4 CYS A  96   SG  108.9 119.3 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WS7 A 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WS7 B 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 861                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 880                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1483                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CUL   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE               
REMARK 900  HEME DOMAIN IN COMPLEX WITH 6-ACETYL-2-AMINO-7,7-                   
REMARK 900  DIMETHYL-7,8-DIHYDROPTERIN-4-ONE                                    
REMARK 900 RELATED ID: 4CUN   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE               
REMARK 900  HEME DOMAIN IN COMPLEX WITH 2-AMINO-9A-METHYL-8,9                   
REMARK 900  ,9A,10-TETRAHYDROBENZO(G)PTERIN-4,6-DIONE                           
REMARK 900 RELATED ID: 4CVG   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE               
REMARK 900  HEME DOMAIN (H4B-FREE) SUPPLEMENTED WITH 50UM ZN                    
REMARK 900  ACETATE AND WITH POOR BINDING OF 6-ACETYL-2-AMINO-                  
REMARK 900  7,7-DIMETHYL-7,8-DIHYDROPTERIDIN-4(3H)-ONE.                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUE 100 IS FOUND AS AN ARG IN STRUCTURE BUT IS A CYS             
REMARK 999 IN DATABASE                                                          
DBREF  4CUM A   40   482  UNP    P29473   NOS3_BOVIN      40    482             
DBREF  4CUM B   40   482  UNP    P29473   NOS3_BOVIN      40    482             
SEQADV 4CUM ARG A  100  UNP  P29473    CYS   100 CONFLICT                       
SEQADV 4CUM ARG B  100  UNP  P29473    CYS   100 CONFLICT                       
SEQRES   1 A  443  ARG ALA PRO ALA PRO ALA THR PRO HIS ALA PRO ASP HIS          
SEQRES   2 A  443  SER PRO ALA PRO ASN SER PRO THR LEU THR ARG PRO PRO          
SEQRES   3 A  443  GLU GLY PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU LEU          
SEQRES   4 A  443  GLY SER ILE THR TYR ASP THR LEU CYS ALA GLN SER GLN          
SEQRES   5 A  443  GLN ASP GLY PRO CYS THR PRO ARG ARG CYS LEU GLY SER          
SEQRES   6 A  443  LEU VAL LEU PRO ARG LYS LEU GLN THR ARG PRO SER PRO          
SEQRES   7 A  443  GLY PRO PRO PRO ALA GLU GLN LEU LEU SER GLN ALA ARG          
SEQRES   8 A  443  ASP PHE ILE ASN GLN TYR TYR SER SER ILE LYS ARG SER          
SEQRES   9 A  443  GLY SER GLN ALA HIS GLU GLU ARG LEU GLN GLU VAL GLU          
SEQRES  10 A  443  ALA GLU VAL ALA SER THR GLY THR TYR HIS LEU ARG GLU          
SEQRES  11 A  443  SER GLU LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN          
SEQRES  12 A  443  ALA PRO ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU          
SEQRES  13 A  443  GLN VAL PHE ASP ALA ARG ASP CYS SER SER ALA GLN GLU          
SEQRES  14 A  443  MET PHE THR TYR ILE CYS ASN HIS ILE LYS TYR ALA THR          
SEQRES  15 A  443  ASN ARG GLY ASN LEU ARG SER ALA ILE THR VAL PHE PRO          
SEQRES  16 A  443  GLN ARG ALA PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN          
SEQRES  17 A  443  SER GLN LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP          
SEQRES  18 A  443  GLY SER VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE THR          
SEQRES  19 A  443  GLU LEU CYS ILE GLN HIS GLY TRP THR PRO GLY ASN GLY          
SEQRES  20 A  443  ARG PHE ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP          
SEQRES  21 A  443  GLU ALA PRO GLU LEU PHE VAL LEU PRO PRO GLU LEU VAL          
SEQRES  22 A  443  LEU GLU VAL PRO LEU GLU HIS PRO THR LEU GLU TRP PHE          
SEQRES  23 A  443  ALA ALA LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL          
SEQRES  24 A  443  SER ASN MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER          
SEQRES  25 A  443  ALA ALA PRO PHE SER GLY TRP TYR MET SER THR GLU ILE          
SEQRES  26 A  443  GLY THR ARG ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE          
SEQRES  27 A  443  LEU GLU ASP VAL ALA VAL CAS MET ASP LEU ASP THR ARG          
SEQRES  28 A  443  THR THR SER SER LEU TRP LYS ASP LYS ALA ALA VAL GLU          
SEQRES  29 A  443  ILE ASN LEU ALA VAL LEU HIS SER PHE GLN LEU ALA LYS          
SEQRES  30 A  443  VAL THR ILE VAL ASP HIS HIS ALA ALA THR VAL SER PHE          
SEQRES  31 A  443  MET LYS HIS LEU ASP ASN GLU GLN LYS ALA ARG GLY GLY          
SEQRES  32 A  443  CYS PRO ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE SER          
SEQRES  33 A  443  GLY SER LEU THR PRO VAL PHE HIS GLN GLU MET VAL ASN          
SEQRES  34 A  443  TYR ILE LEU SER PRO ALA PHE ARG TYR GLN PRO ASP PRO          
SEQRES  35 A  443  TRP                                                          
SEQRES   1 B  443  ARG ALA PRO ALA PRO ALA THR PRO HIS ALA PRO ASP HIS          
SEQRES   2 B  443  SER PRO ALA PRO ASN SER PRO THR LEU THR ARG PRO PRO          
SEQRES   3 B  443  GLU GLY PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU LEU          
SEQRES   4 B  443  GLY SER ILE THR TYR ASP THR LEU CYS ALA GLN SER GLN          
SEQRES   5 B  443  GLN ASP GLY PRO CYS THR PRO ARG ARG CYS LEU GLY SER          
SEQRES   6 B  443  LEU VAL LEU PRO ARG LYS LEU GLN THR ARG PRO SER PRO          
SEQRES   7 B  443  GLY PRO PRO PRO ALA GLU GLN LEU LEU SER GLN ALA ARG          
SEQRES   8 B  443  ASP PHE ILE ASN GLN TYR TYR SER SER ILE LYS ARG SER          
SEQRES   9 B  443  GLY SER GLN ALA HIS GLU GLU ARG LEU GLN GLU VAL GLU          
SEQRES  10 B  443  ALA GLU VAL ALA SER THR GLY THR TYR HIS LEU ARG GLU          
SEQRES  11 B  443  SER GLU LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN          
SEQRES  12 B  443  ALA PRO ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU          
SEQRES  13 B  443  GLN VAL PHE ASP ALA ARG ASP CYS SER SER ALA GLN GLU          
SEQRES  14 B  443  MET PHE THR TYR ILE CYS ASN HIS ILE LYS TYR ALA THR          
SEQRES  15 B  443  ASN ARG GLY ASN LEU ARG SER ALA ILE THR VAL PHE PRO          
SEQRES  16 B  443  GLN ARG ALA PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN          
SEQRES  17 B  443  SER GLN LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP          
SEQRES  18 B  443  GLY SER VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE THR          
SEQRES  19 B  443  GLU LEU CYS ILE GLN HIS GLY TRP THR PRO GLY ASN GLY          
SEQRES  20 B  443  ARG PHE ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP          
SEQRES  21 B  443  GLU ALA PRO GLU LEU PHE VAL LEU PRO PRO GLU LEU VAL          
SEQRES  22 B  443  LEU GLU VAL PRO LEU GLU HIS PRO THR LEU GLU TRP PHE          
SEQRES  23 B  443  ALA ALA LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL          
SEQRES  24 B  443  SER ASN MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER          
SEQRES  25 B  443  ALA ALA PRO PHE SER GLY TRP TYR MET SER THR GLU ILE          
SEQRES  26 B  443  GLY THR ARG ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE          
SEQRES  27 B  443  LEU GLU ASP VAL ALA VAL CAS MET ASP LEU ASP THR ARG          
SEQRES  28 B  443  THR THR SER SER LEU TRP LYS ASP LYS ALA ALA VAL GLU          
SEQRES  29 B  443  ILE ASN LEU ALA VAL LEU HIS SER PHE GLN LEU ALA LYS          
SEQRES  30 B  443  VAL THR ILE VAL ASP HIS HIS ALA ALA THR VAL SER PHE          
SEQRES  31 B  443  MET LYS HIS LEU ASP ASN GLU GLN LYS ALA ARG GLY GLY          
SEQRES  32 B  443  CYS PRO ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE SER          
SEQRES  33 B  443  GLY SER LEU THR PRO VAL PHE HIS GLN GLU MET VAL ASN          
SEQRES  34 B  443  TYR ILE LEU SER PRO ALA PHE ARG TYR GLN PRO ASP PRO          
SEQRES  35 B  443  TRP                                                          
MODRES 4CUM CAS A  384  CYS  S-(DIMETHYLARSENIC)CYSTEINE                        
MODRES 4CUM CAS B  384  CYS  S-(DIMETHYLARSENIC)CYSTEINE                        
HET    HEM  A 500      43                                                       
HET    ARG  A 700      12                                                       
HET    WS7  A 800      17                                                       
HET    ACT  A 860       4                                                       
HET    CAS  A 384       9                                                       
HET    HEM  B 500      43                                                       
HET    ARG  B 700      12                                                       
HET    WS7  B 800      17                                                       
HET    ACT  B 860       4                                                       
HET    ACT  B 861       4                                                       
HET    GOL  B 880       6                                                       
HET    CAS  B 384       9                                                       
HET     ZN  A1483       1                                                       
HETNAM     CAS S-(DIMETHYLARSENIC)CYSTEINE                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     WS7 (9AS)-2-AMINO-9A-METHYL-6,7,8,9,9A,10-                           
HETNAM   2 WS7  HEXAHYDROBENZO[G]PTERIDIN-4(3H)-ONE                             
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     ARG ARGININE                                                         
HETNAM     ACT ACETATE ION                                                      
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     CAS HYDROXYDIMETHYLARSINE OXIDE                                      
FORMUL   3  CAS    2(C5 H12 AS N O2 S)                                          
FORMUL   4  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   5  WS7    2(C11 H15 N5 O)                                              
FORMUL   6   ZN    ZN 2+                                                        
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  ARG    2(C6 H15 N4 O2 1+)                                           
FORMUL   9  ACT    3(C2 H3 O2 1-)                                               
FORMUL  10  HOH   *214(H2 O)                                                    
HELIX    1   1 THR A   85  SER A   90  5                                   6    
HELIX    2   2 ALA A  122  ILE A  140  1                                  19    
HELIX    3   3 SER A  145  GLY A  163  1                                  19    
HELIX    4   4 ARG A  168  ALA A  183  1                                  16    
HELIX    5   5 GLY A  188  TRP A  192  5                                   5    
HELIX    6   6 SER A  205  ASN A  222  1                                  18    
HELIX    7   7 ARG A  223  ASN A  225  5                                   3    
HELIX    8   8 ASN A  269  HIS A  279  1                                  11    
HELIX    9   9 PRO A  308  VAL A  312  5                                   5    
HELIX   10  10 LEU A  322  GLY A  329  5                                   8    
HELIX   11  11 SER A  361  THR A  366  1                                   6    
HELIX   12  12 THR A  366  ASP A  371  1                                   6    
HELIX   13  13 ILE A  377  MET A  385  1                                   9    
HELIX   14  14 THR A  391  SER A  394  5                                   4    
HELIX   15  15 LEU A  395  LYS A  416  1                                  22    
HELIX   16  16 ASP A  421  GLY A  441  1                                  21    
HELIX   17  17 ASP A  446  VAL A  451  1                                   6    
HELIX   18  18 SER A  455  THR A  459  5                                   5    
HELIX   19  19 THR A  459  HIS A  463  5                                   5    
HELIX   20  20 THR B   85  SER B   90  5                                   6    
HELIX   21  21 PRO B  121  ILE B  140  1                                  20    
HELIX   22  22 SER B  145  GLY B  163  1                                  19    
HELIX   23  23 ARG B  168  ASN B  182  1                                  15    
HELIX   24  24 GLY B  188  TRP B  192  5                                   5    
HELIX   25  25 SER B  205  ASN B  222  1                                  18    
HELIX   26  26 ARG B  223  ASN B  225  5                                   3    
HELIX   27  27 ASN B  269  HIS B  279  1                                  11    
HELIX   28  28 PRO B  308  VAL B  312  5                                   5    
HELIX   29  29 GLU B  323  LEU B  328  1                                   6    
HELIX   30  30 SER B  361  THR B  366  1                                   6    
HELIX   31  31 THR B  366  ASP B  371  1                                   6    
HELIX   32  32 ILE B  377  MET B  385  1                                   9    
HELIX   33  33 THR B  391  SER B  394  5                                   4    
HELIX   34  34 LEU B  395  ALA B  415  1                                  21    
HELIX   35  35 ASP B  421  GLY B  441  1                                  21    
HELIX   36  36 ASP B  446  VAL B  451  1                                   6    
HELIX   37  37 SER B  455  THR B  459  5                                   5    
HELIX   38  38 THR B  459  HIS B  463  5                                   5    
SHEET    1  AA 2 ARG A  72  LYS A  74  0                                        
SHEET    2  AA 2 ILE A  81  TYR A  83 -1  O  THR A  82   N  VAL A  73           
SHEET    1  AB 4 GLN A 196  ASP A 199  0                                        
SHEET    2  AB 4 ALA A 229  VAL A 232  1  O  ILE A 230   N  PHE A 198           
SHEET    3  AB 4 PHE A 355  SER A 356 -1  O  SER A 356   N  ALA A 229           
SHEET    4  AB 4 ALA A 337  VAL A 338 -1  O  VAL A 338   N  PHE A 355           
SHEET    1  AC 3 ARG A 244  ILE A 245  0                                        
SHEET    2  AC 3 LEU A 293  GLN A 296 -1  O  GLN A 296   N  ARG A 244           
SHEET    3  AC 3 GLU A 303  PHE A 305 -1  O  GLU A 303   N  LEU A 295           
SHEET    1  AD 2 GLY A 255  ARG A 257  0                                        
SHEET    2  AD 2 VAL A 263  GLY A 265 -1  O  ARG A 264   N  TYR A 256           
SHEET    1  AE 2 GLU A 314  PRO A 316  0                                        
SHEET    2  AE 2 ARG A 331  TYR A 333 -1  O  TRP A 332   N  VAL A 315           
SHEET    1  AF 3 LEU A 348  PHE A 350  0                                        
SHEET    2  AF 3 LEU A 342  ILE A 345 -1  O  LEU A 343   N  PHE A 350           
SHEET    3  AF 3 ALA A 474  ARG A 476 -1  O  ALA A 474   N  GLU A 344           
SHEET    1  AG 2 TYR A 359  MET A 360  0                                        
SHEET    2  AG 2 ILE A 419  VAL A 420  1  N  VAL A 420   O  TYR A 359           
SHEET    1  BA 2 ARG B  72  LYS B  74  0                                        
SHEET    2  BA 2 ILE B  81  TYR B  83 -1  O  THR B  82   N  VAL B  73           
SHEET    1  BB 4 GLN B 196  ASP B 199  0                                        
SHEET    2  BB 4 ALA B 229  VAL B 232  1  O  ILE B 230   N  PHE B 198           
SHEET    3  BB 4 PHE B 355  SER B 356 -1  O  SER B 356   N  ALA B 229           
SHEET    4  BB 4 ALA B 337  VAL B 338 -1  O  VAL B 338   N  PHE B 355           
SHEET    1  BC 3 ARG B 244  ILE B 245  0                                        
SHEET    2  BC 3 LEU B 293  GLN B 296 -1  O  GLN B 296   N  ARG B 244           
SHEET    3  BC 3 GLU B 303  PHE B 305 -1  O  GLU B 303   N  LEU B 295           
SHEET    1  BD 2 GLY B 255  ARG B 257  0                                        
SHEET    2  BD 2 VAL B 263  GLY B 265 -1  O  ARG B 264   N  TYR B 256           
SHEET    1  BE 2 GLU B 314  PRO B 316  0                                        
SHEET    2  BE 2 ARG B 331  TYR B 333 -1  O  TRP B 332   N  VAL B 315           
SHEET    1  BF 3 LEU B 348  PHE B 350  0                                        
SHEET    2  BF 3 LEU B 342  ILE B 345 -1  O  LEU B 343   N  PHE B 350           
SHEET    3  BF 3 ALA B 474  ARG B 476 -1  O  ALA B 474   N  GLU B 344           
SHEET    1  BG 2 TYR B 359  MET B 360  0                                        
SHEET    2  BG 2 ILE B 419  VAL B 420  1  N  VAL B 420   O  TYR B 359           
LINK         SG  CYS A 186                FE   HEM A 500     1555   1555  2.38  
LINK         C   VAL A 383                 N   CAS A 384     1555   1555  1.34  
LINK         C   CAS A 384                 N   MET A 385     1555   1555  1.33  
LINK        ZN    ZN A1483                 SG  CYS A  96     1555   1555  2.35  
LINK        ZN    ZN A1483                 SG  CYS B 101     1555   1555  2.32  
LINK        ZN    ZN A1483                 SG  CYS B  96     1555   1555  2.39  
LINK        ZN    ZN A1483                 SG  CYS A 101     1555   1555  2.38  
LINK         SG  CYS B 186                FE   HEM B 500     1555   1555  2.35  
LINK         C   VAL B 383                 N   CAS B 384     1555   1555  1.33  
LINK         C   CAS B 384                 N   MET B 385     1555   1555  1.33  
CISPEP   1 SER A  472    PRO A  473          0         5.89                     
CISPEP   2 SER B  472    PRO B  473          0        -2.09                     
SITE     1 AC1 15 TRP A 180  CYS A 186  SER A 228  PHE A 355                    
SITE     2 AC1 15 SER A 356  TRP A 358  MET A 360  GLU A 363                    
SITE     3 AC1 15 TRP A 449  PHE A 475  TYR A 477  ARG A 700                    
SITE     4 AC1 15 WS7 A 800  HOH A2113  HOH A2114                               
SITE     1 AC2  8 GLN A 249  TYR A 333  TRP A 358  TYR A 359                    
SITE     2 AC2  8 GLU A 363  ASN A 368  HEM A 500  HOH A2068                    
SITE     1 AC3 11 SER A 104  VAL A 106  ARG A 367  ALA A 448                    
SITE     2 AC3 11 TRP A 449  HEM A 500  HOH A2101  HOH A2114                    
SITE     3 AC3 11 HOH A2115  TRP B 447  PHE B 462                               
SITE     1 AC4  4 GLY A 188  TRP A 358  VAL A 420  SER A 428                    
SITE     1 AC5 16 TRP B 180  ARG B 185  CYS B 186  SER B 228                    
SITE     2 AC5 16 PHE B 355  SER B 356  TRP B 358  MET B 360                    
SITE     3 AC5 16 GLU B 363  TRP B 449  PHE B 475  TYR B 477                    
SITE     4 AC5 16 ARG B 700  WS7 B 800  HOH B2096  HOH B2099                    
SITE     1 AC6  9 GLN B 249  TYR B 333  TRP B 358  TYR B 359                    
SITE     2 AC6  9 GLU B 363  ASN B 368  HEM B 500  HOH B2067                    
SITE     3 AC6  9 HOH B2073                                                     
SITE     1 AC7 10 TRP A 447  PHE A 462  SER B 104  VAL B 106                    
SITE     2 AC7 10 ARG B 367  ALA B 448  TRP B 449  HEM B 500                    
SITE     3 AC7 10 GOL B 880  HOH B2094                                          
SITE     1 AC8  5 GLY B 188  ILE B 190  TRP B 358  VAL B 420                    
SITE     2 AC8  5 SER B 428                                                     
SITE     1 AC9  4 ILE A 454  SER A 455  ILE B 454  SER B 455                    
SITE     1 BC1  5 HOH A2109  VAL B 106  ARG B 367  HIS B 373                    
SITE     2 BC1  5 WS7 B 800                                                     
SITE     1 BC2  4 CYS A  96  CYS A 101  CYS B  96  CYS B 101                    
CRYST1   58.011  106.493  156.480  90.00  90.00  90.00 P 21 21 21    8          
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      0.017238  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009390  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006391        0.00000                         
ATOM      1  N   GLY A  67       7.862 -18.704  53.706  1.00 87.47           N  
ANISOU    1  N   GLY A  67    14193   9012  10029   1231    877   1410       N  
ATOM      2  CA  GLY A  67       8.915 -19.667  53.266  1.00 86.88           C  
ANISOU    2  CA  GLY A  67    14216   8838   9958   1397    867   1434       C  
ATOM      3  C   GLY A  67       9.940 -19.133  52.269  1.00 85.68           C  
ANISOU    3  C   GLY A  67    13873   8809   9874   1459    741   1341       C  
ATOM      4  O   GLY A  67      11.145 -19.271  52.513  1.00 83.23           O  
ANISOU    4  O   GLY A  67    13560   8550   9516   1673    653   1370       O  
ATOM      5  N   PRO A  68       9.475 -18.524  51.140  1.00 80.72           N  
ANISOU    5  N   PRO A  68    13081   8231   9357   1276    732   1231       N  
ATOM      6  CA  PRO A  68      10.362 -18.145  50.011  1.00 79.53           C  
ANISOU    6  CA  PRO A  68    12771   8166   9281   1311    644   1140       C  
ATOM      7  C   PRO A  68      11.457 -17.122  50.377  1.00 80.76           C  
ANISOU    7  C   PRO A  68    12754   8530   9400   1453    486   1120       C  
ATOM      8  O   PRO A  68      11.165 -16.119  51.023  1.00 76.15           O  
ANISOU    8  O   PRO A  68    12075   8079   8780   1410    426   1112       O  
ATOM      9  CB  PRO A  68       9.392 -17.540  48.978  1.00 72.47           C  
ANISOU    9  CB  PRO A  68    11752   7298   8486   1071    668   1040       C  
ATOM     10  CG  PRO A  68       8.046 -18.040  49.373  1.00 73.77           C  
ANISOU   10  CG  PRO A  68    12044   7337   8647    918    795   1078       C  
ATOM     11  CD  PRO A  68       8.067 -18.182  50.861  1.00 75.54           C  
ANISOU   11  CD  PRO A  68    12387   7557   8759   1031    808   1187       C  
ATOM     12  N   LYS A  69      12.702 -17.379  49.962  1.00 85.69           N  
ANISOU   12  N   LYS A  69    13337   9183  10036   1615    425   1106       N  
ATOM     13  CA  LYS A  69      13.823 -16.464  50.269  1.00 83.67           C  
ANISOU   13  CA  LYS A  69    12905   9129   9755   1746    275   1077       C  
ATOM     14  C   LYS A  69      13.956 -15.306  49.257  1.00 75.92           C  
ANISOU   14  C   LYS A  69    11693   8286   8867   1622    212    960       C  
ATOM     15  O   LYS A  69      14.982 -15.119  48.587  1.00 72.44           O  
ANISOU   15  O   LYS A  69    11131   7919   8472   1700    153    907       O  
ATOM     16  CB  LYS A  69      15.146 -17.233  50.488  1.00 93.22           C  
ANISOU   16  CB  LYS A  69    14165  10329  10926   2000    232   1124       C  
ATOM     17  CG  LYS A  69      16.252 -16.446  51.219  1.00102.13           C  
ANISOU   17  CG  LYS A  69    15144  11664  11999   2160     74   1118       C  
ATOM     18  CD  LYS A  69      15.892 -15.910  52.619  1.00101.82           C  
ANISOU   18  CD  LYS A  69    15138  11705  11845   2179     19   1171       C  
ATOM     19  CE  LYS A  69      15.200 -14.536  52.617  1.00 96.88           C  
ANISOU   19  CE  LYS A  69    14361  11203  11246   1985    -19   1097       C  
ATOM     20  NZ  LYS A  69      15.891 -13.437  51.868  1.00 93.60           N  
ANISOU   20  NZ  LYS A  69    13699  10951  10912   1940   -117    986       N  
ATOM     21  N   PHE A  70      12.878 -14.537  49.157  1.00 67.16           N  
ANISOU   21  N   PHE A  70    10529   7206   7782   1429    232    922       N  
ATOM     22  CA  PHE A  70      12.806 -13.377  48.295  1.00 58.73           C  
ANISOU   22  CA  PHE A  70     9267   6258   6790   1301    181    823       C  
ATOM     23  C   PHE A  70      11.958 -12.390  49.064  1.00 55.55           C  
ANISOU   23  C   PHE A  70     8817   5938   6350   1199    157    823       C  
ATOM     24  O   PHE A  70      11.188 -12.805  49.925  1.00 55.43           O  
ANISOU   24  O   PHE A  70     8933   5851   6275   1182    217    891       O  
ATOM     25  CB  PHE A  70      12.104 -13.737  46.992  1.00 57.95           C  
ANISOU   25  CB  PHE A  70     9187   6055   6777   1147    268    770       C  
ATOM     26  CG  PHE A  70      12.837 -14.749  46.162  1.00 58.32           C  
ANISOU   26  CG  PHE A  70     9299   6002   6860   1235    309    762       C  
ATOM     27  CD1 PHE A  70      13.874 -14.358  45.320  1.00 57.85           C  
ANISOU   27  CD1 PHE A  70     9103   6030   6849   1294    253    698       C  
ATOM     28  CD2 PHE A  70      12.492 -16.094  46.220  1.00 60.71           C  
ANISOU   28  CD2 PHE A  70     9803   6116   7147   1259    413    817       C  
ATOM     29  CE1 PHE A  70      14.554 -15.292  44.547  1.00 60.07           C  
ANISOU   29  CE1 PHE A  70     9445   6219   7161   1382    300    688       C  
ATOM     30  CE2 PHE A  70      13.178 -17.036  45.457  1.00 64.62           C  
ANISOU   30  CE2 PHE A  70    10370   6510   7674   1349    457    807       C  
ATOM     31  CZ  PHE A  70      14.211 -16.636  44.621  1.00 60.99           C  
ANISOU   31  CZ  PHE A  70     9769   6144   7259   1416    399    742       C  
ATOM     32  N   PRO A  71      12.087 -11.082  48.762  1.00 50.40           N  
ANISOU   32  N   PRO A  71     7986   5431   5732   1130     80    749       N  
ATOM     33  CA  PRO A  71      11.255 -10.082  49.430  1.00 47.63           C  
ANISOU   33  CA  PRO A  71     7590   5156   5352   1033     62    742       C  
ATOM     34  C   PRO A  71       9.757 -10.399  49.318  1.00 47.55           C  
ANISOU   34  C   PRO A  71     7666   5041   5360    877    172    760       C  
ATOM     35  O   PRO A  71       9.248 -10.683  48.221  1.00 46.14           O  
ANISOU   35  O   PRO A  71     7480   4794   5258    766    228    720       O  
ATOM     36  CB  PRO A  71      11.575  -8.773  48.673  1.00 44.07           C  
ANISOU   36  CB  PRO A  71     6946   4835   4964    960    -11    648       C  
ATOM     37  CG  PRO A  71      12.412  -9.164  47.514  1.00 45.00           C  
ANISOU   37  CG  PRO A  71     7016   4932   5149    995    -12    607       C  
ATOM     38  CD  PRO A  71      13.053 -10.475  47.835  1.00 45.97           C  
ANISOU   38  CD  PRO A  71     7265   4965   5236   1148     13    671       C  
ATOM     39  N   ARG A  72       9.081 -10.368  50.456  1.00 48.76           N  
ANISOU   39  N   ARG A  72     7898   5187   5441    872    202    816       N  
ATOM     40  CA  ARG A  72       7.639 -10.520  50.525  1.00 51.80           C  
ANISOU   40  CA  ARG A  72     8341   5499   5843    722    305    831       C  
ATOM     41  C   ARG A  72       7.016  -9.134  50.462  1.00 49.64           C  
ANISOU   41  C   ARG A  72     7921   5346   5594    614    265    771       C  
ATOM     42  O   ARG A  72       7.372  -8.264  51.252  1.00 51.51           O  
ANISOU   42  O   ARG A  72     8106   5692   5774    673    194    768       O  
ATOM     43  CB  ARG A  72       7.259 -11.203  51.828  1.00 55.34           C  
ANISOU   43  CB  ARG A  72     8956   5876   6195    780    372    928       C  
ATOM     44  CG  ARG A  72       5.786 -11.123  52.167  1.00 61.46           C  
ANISOU   44  CG  ARG A  72     9766   6611   6976    630    474    943       C  
ATOM     45  CD  ARG A  72       5.591 -11.175  53.682  1.00 72.01           C  
ANISOU   45  CD  ARG A  72    11217   7951   8193    706    504   1026       C  
ATOM     46  NE  ARG A  72       5.483 -12.547  54.178  1.00 81.02           N  
ANISOU   46  NE  ARG A  72    12566   8934   9284    758    609   1120       N  
ATOM     47  CZ  ARG A  72       4.327 -13.171  54.403  1.00 90.27           C  
ANISOU   47  CZ  ARG A  72    13842   9991  10465    640    752   1161       C  
ATOM     48  NH1 ARG A  72       3.172 -12.544  54.184  1.00 88.09           N  
ANISOU   48  NH1 ARG A  72    13466   9756  10249    471    799   1113       N  
ATOM     49  NH2 ARG A  72       4.320 -14.424  54.856  1.00 91.19           N  
ANISOU   49  NH2 ARG A  72    14163   9951  10535    693    852   1250       N  
ATOM     50  N   VAL A  73       6.066  -8.960  49.551  1.00 45.41           N  
ANISOU   50  N   VAL A  73     7329   4787   5138    460    313    723       N  
ATOM     51  CA  VAL A  73       5.495  -7.676  49.225  1.00 45.18           C  
ANISOU   51  CA  VAL A  73     7158   4863   5147    363    276    661       C  
ATOM     52  C   VAL A  73       3.982  -7.674  49.525  1.00 47.57           C  
ANISOU   52  C   VAL A  73     7480   5134   5460    235    367    674       C  
ATOM     53  O   VAL A  73       3.228  -8.533  49.050  1.00 46.82           O  
ANISOU   53  O   VAL A  73     7440   4940   5409    142    452    680       O  
ATOM     54  CB  VAL A  73       5.731  -7.397  47.723  1.00 46.24           C  
ANISOU   54  CB  VAL A  73     7189   5012   5367    302    242    585       C  
ATOM     55  CG1 VAL A  73       5.292  -5.995  47.322  1.00 42.30           C  
ANISOU   55  CG1 VAL A  73     6548   4622   4902    224    194    523       C  
ATOM     56  CG2 VAL A  73       7.189  -7.642  47.337  1.00 42.63           C  
ANISOU   56  CG2 VAL A  73     6720   4566   4910    422    180    574       C  
ATOM     57  N   LYS A  74       3.537  -6.688  50.298  1.00 46.98           N  
ANISOU   57  N   LYS A  74     7354   5147   5348    226    351    673       N  
ATOM     58  CA  LYS A  74       2.147  -6.643  50.760  1.00 45.39           C  
ANISOU   58  CA  LYS A  74     7165   4930   5150    123    443    691       C  
ATOM     59  C   LYS A  74       1.353  -5.455  50.225  1.00 41.33           C  
ANISOU   59  C   LYS A  74     6503   4508   4692     28    420    626       C  
ATOM     60  O   LYS A  74       1.855  -4.334  50.144  1.00 40.27           O  
ANISOU   60  O   LYS A  74     6280   4469   4552     68    334    585       O  
ATOM     61  CB  LYS A  74       2.088  -6.650  52.296  1.00 44.83           C  
ANISOU   61  CB  LYS A  74     7193   4868   4974    199    476    759       C  
ATOM     62  CG  LYS A  74       0.662  -6.605  52.829  1.00 47.96           C  
ANISOU   62  CG  LYS A  74     7600   5251   5372     96    587    780       C  
ATOM     63  CD  LYS A  74       0.477  -7.081  54.280  1.00 47.64           C  
ANISOU   63  CD  LYS A  74     7707   5170   5223    158    665    865       C  
ATOM     64  CE  LYS A  74      -0.998  -6.969  54.620  1.00 46.24           C  
ANISOU   64  CE  LYS A  74     7510   4988   5070     36    785    872       C  
ATOM     65  NZ  LYS A  74      -1.303  -7.421  55.991  1.00 51.00           N  
ANISOU   65  NZ  LYS A  74     8262   5548   5569     80    883    957       N  
ATOM     66  N   ASN A  75       0.102  -5.715  49.875  1.00 40.48           N  
ANISOU   66  N   ASN A  75     6371   4368   4639    -97    499    616       N  
ATOM     67  CA  ASN A  75      -0.833  -4.648  49.594  1.00 41.59           C  
ANISOU   67  CA  ASN A  75     6384   4598   4823   -174    492    568       C  
ATOM     68  C   ASN A  75      -1.780  -4.523  50.767  1.00 42.64           C  
ANISOU   68  C   ASN A  75     6544   4742   4914   -194    579    608       C  
ATOM     69  O   ASN A  75      -2.537  -5.444  51.048  1.00 43.34           O  
ANISOU   69  O   ASN A  75     6698   4756   5014   -263    684    644       O  
ATOM     70  CB  ASN A  75      -1.607  -4.871  48.297  1.00 41.71           C  
ANISOU   70  CB  ASN A  75     6319   4597   4931   -297    504    515       C  
ATOM     71  CG  ASN A  75      -2.623  -3.771  48.043  1.00 43.01           C  
ANISOU   71  CG  ASN A  75     6348   4858   5135   -359    493    471       C  
ATOM     72  OD1 ASN A  75      -3.525  -3.536  48.865  1.00 45.31           O  
ANISOU   72  OD1 ASN A  75     6625   5176   5413   -386    560    493       O  
ATOM     73  ND2 ASN A  75      -2.482  -3.085  46.920  1.00 38.54           N  
ANISOU   73  ND2 ASN A  75     5686   4346   4613   -374    415    414       N  
ATOM     74  N   TRP A  76      -1.739  -3.374  51.434  1.00 40.60           N  
ANISOU   74  N   TRP A  76     6241   4574   4610   -140    541    599       N  
ATOM     75  CA  TRP A  76      -2.463  -3.212  52.694  1.00 43.22           C  
ANISOU   75  CA  TRP A  76     6619   4921   4883   -133    624    641       C  
ATOM     76  C   TRP A  76      -3.928  -2.939  52.508  1.00 43.91           C  
ANISOU   76  C   TRP A  76     6612   5038   5033   -244    704    619       C  
ATOM     77  O   TRP A  76      -4.700  -3.120  53.439  1.00 46.71           O  
ANISOU   77  O   TRP A  76     7010   5384   5355   -265    807    658       O  
ATOM     78  CB  TRP A  76      -1.819  -2.145  53.568  1.00 39.98           C  
ANISOU   78  CB  TRP A  76     6214   4590   4387    -27    558    635       C  
ATOM     79  CG  TRP A  76      -0.535  -2.635  54.123  1.00 39.13           C  
ANISOU   79  CG  TRP A  76     6216   4455   4197     87    503    672       C  
ATOM     80  CD1 TRP A  76       0.736  -2.579  53.533  1.00 38.31           C  
ANISOU   80  CD1 TRP A  76     6091   4363   4102    151    393    645       C  
ATOM     81  CD2 TRP A  76      -0.347  -3.337  55.380  1.00 41.96           C  
ANISOU   81  CD2 TRP A  76     6726   4769   4448    161    556    748       C  
ATOM     82  NE1 TRP A  76       1.676  -3.179  54.330  1.00 38.74           N  
ANISOU   82  NE1 TRP A  76     6259   4393   4067    262    367    695       N  
ATOM     83  CE2 TRP A  76       1.099  -3.642  55.472  1.00 41.74           C  
ANISOU   83  CE2 TRP A  76     6754   4739   4368    279    457    760       C  
ATOM     84  CE3 TRP A  76      -1.189  -3.722  56.424  1.00 43.86           C  
ANISOU   84  CE3 TRP A  76     7061   4976   4627    147    675    808       C  
ATOM     85  CZ2 TRP A  76       1.642  -4.308  56.568  1.00 42.53           C  
ANISOU   85  CZ2 TRP A  76     7002   4805   4352    388    467    831       C  
ATOM     86  CZ3 TRP A  76      -0.619  -4.396  57.533  1.00 46.27           C  
ANISOU   86  CZ3 TRP A  76     7530   5239   4810    252    694    883       C  
ATOM     87  CH2 TRP A  76       0.763  -4.682  57.595  1.00 44.35           C  
ANISOU   87  CH2 TRP A  76     7342   4997   4514    374    586    895       C  
ATOM     88  N   GLU A  77      -4.327  -2.520  51.313  1.00 44.26           N  
ANISOU   88  N   GLU A  77     6529   5121   5167   -312    659    557       N  
ATOM     89  CA  GLU A  77      -5.741  -2.282  51.031  1.00 45.88           C  
ANISOU   89  CA  GLU A  77     6624   5368   5442   -414    722    530       C  
ATOM     90  C   GLU A  77      -6.469  -3.620  50.812  1.00 49.41           C  
ANISOU   90  C   GLU A  77     7106   5730   5939   -530    822    548       C  
ATOM     91  O   GLU A  77      -7.530  -3.851  51.384  1.00 51.85           O  
ANISOU   91  O   GLU A  77     7399   6040   6262   -599    932    566       O  
ATOM     92  CB  GLU A  77      -5.915  -1.385  49.802  1.00 44.64           C  
ANISOU   92  CB  GLU A  77     6325   5284   5353   -437    631    461       C  
ATOM     93  CG  GLU A  77      -7.359  -1.309  49.306  1.00 49.22           C  
ANISOU   93  CG  GLU A  77     6778   5910   6013   -543    680    427       C  
ATOM     94  CD  GLU A  77      -7.506  -0.624  47.951  1.00 50.26           C  
ANISOU   94  CD  GLU A  77     6787   6104   6205   -562    583    363       C  
ATOM     95  OE1 GLU A  77      -6.498  -0.136  47.394  1.00 46.61           O  
ANISOU   95  OE1 GLU A  77     6340   5646   5724   -498    488    346       O  
ATOM     96  OE2 GLU A  77      -8.648  -0.582  47.440  1.00 53.47           O  
ANISOU   96  OE2 GLU A  77     7080   6560   6677   -642    604    331       O  
ATOM     97  N   LEU A  78      -5.880  -4.489  49.989  1.00 49.71           N  
ANISOU   97  N   LEU A  78     7192   5691   6004   -555    790    540       N  
ATOM     98  CA  LEU A  78      -6.492  -5.757  49.578  1.00 50.60           C  
ANISOU   98  CA  LEU A  78     7341   5712   6174   -677    874    540       C  
ATOM     99  C   LEU A  78      -6.089  -6.930  50.456  1.00 51.53           C  
ANISOU   99  C   LEU A  78     7641   5704   6234   -653    966    617       C  
ATOM    100  O   LEU A  78      -6.702  -7.991  50.404  1.00 50.39           O  
ANISOU  100  O   LEU A  78     7550   5467   6128   -759   1068    629       O  
ATOM    101  CB  LEU A  78      -6.096  -6.055  48.129  1.00 51.59           C  
ANISOU  101  CB  LEU A  78     7429   5816   6357   -716    791    482       C  
ATOM    102  CG  LEU A  78      -6.641  -4.995  47.174  1.00 54.99           C  
ANISOU  102  CG  LEU A  78     7687   6364   6842   -748    709    410       C  
ATOM    103  CD1 LEU A  78      -6.002  -5.068  45.785  1.00 55.81           C  
ANISOU  103  CD1 LEU A  78     7770   6459   6975   -752    611    356       C  
ATOM    104  CD2 LEU A  78      -8.164  -5.124  47.127  1.00 51.59           C  
ANISOU  104  CD2 LEU A  78     7153   5971   6480   -879    785    383       C  
ATOM    105  N   GLY A  79      -5.022  -6.745  51.227  1.00 49.99           N  
ANISOU  105  N   GLY A  79     7546   5503   5946   -512    926    666       N  
ATOM    106  CA  GLY A  79      -4.502  -7.796  52.084  1.00 50.04           C  
ANISOU  106  CA  GLY A  79     7739   5395   5880   -455    997    747       C  
ATOM    107  C   GLY A  79      -3.744  -8.870  51.350  1.00 49.08           C  
ANISOU  107  C   GLY A  79     7708   5161   5779   -448    979    750       C  
ATOM    108  O   GLY A  79      -3.465  -9.915  51.918  1.00 52.72           O  
ANISOU  108  O   GLY A  79     8332   5505   6194   -417   1055    817       O  
ATOM    109  N   SER A  80      -3.419  -8.631  50.083  1.00 49.68           N  
ANISOU  109  N   SER A  80     7690   5266   5919   -472    887    679       N  
ATOM    110  CA  SER A  80      -2.724  -9.626  49.261  1.00 47.70           C  
ANISOU  110  CA  SER A  80     7520   4911   5694   -468    872    670       C  
ATOM    111  C   SER A  80      -1.186  -9.495  49.306  1.00 49.84           C  
ANISOU  111  C   SER A  80     7841   5190   5905   -301    774    689       C  
ATOM    112  O   SER A  80      -0.619  -8.430  49.601  1.00 48.11           O  
ANISOU  112  O   SER A  80     7551   5080   5648   -211    685    680       O  
ATOM    113  CB  SER A  80      -3.224  -9.562  47.824  1.00 43.44           C  
ANISOU  113  CB  SER A  80     6864   4392   5249   -587    835    581       C  
ATOM    114  OG  SER A  80      -2.896  -8.304  47.235  1.00 44.43           O  
ANISOU  114  OG  SER A  80     6850   4647   5384   -544    716    528       O  
ATOM    115  N   ILE A  81      -0.538 -10.598  48.958  1.00 53.92           N  
ANISOU  115  N   ILE A  81     8475   5589   6422   -268    794    708       N  
ATOM    116  CA  ILE A  81       0.877 -10.853  49.171  1.00 53.50           C  
ANISOU  116  CA  ILE A  81     8503   5515   6311   -103    733    744       C  
ATOM    117  C   ILE A  81       1.486 -11.409  47.872  1.00 53.23           C  
ANISOU  117  C   ILE A  81     8469   5422   6333   -108    700    693       C  
ATOM    118  O   ILE A  81       0.847 -12.218  47.189  1.00 51.61           O  
ANISOU  118  O   ILE A  81     8305   5121   6185   -225    769    666       O  
ATOM    119  CB  ILE A  81       1.003 -11.898  50.301  1.00 57.62           C  
ANISOU  119  CB  ILE A  81     9217   5918   6757    -32    825    843       C  
ATOM    120  CG1 ILE A  81       0.865 -11.232  51.689  1.00 59.92           C  
ANISOU  120  CG1 ILE A  81     9522   6286   6957     35    828    898       C  
ATOM    121  CG2 ILE A  81       2.238 -12.787  50.150  1.00 57.72           C  
ANISOU  121  CG2 ILE A  81     9349   5841   6739    105    801    877       C  
ATOM    122  CD1 ILE A  81       2.032 -10.349  52.090  1.00 60.45           C  
ANISOU  122  CD1 ILE A  81     9536   6472   6959    192    696    896       C  
ATOM    123  N   THR A  82       2.691 -10.943  47.525  1.00 50.29           N  
ANISOU  123  N   THR A  82     8047   5115   5947      9    597    672       N  
ATOM    124  CA  THR A  82       3.515 -11.528  46.456  1.00 48.89           C  
ANISOU  124  CA  THR A  82     7891   4880   5804     45    572    637       C  
ATOM    125  C   THR A  82       4.946 -11.582  46.947  1.00 48.95           C  
ANISOU  125  C   THR A  82     7936   4909   5755    233    510    677       C  
ATOM    126  O   THR A  82       5.293 -10.974  47.960  1.00 49.44           O  
ANISOU  126  O   THR A  82     7978   5052   5753    321    464    714       O  
ATOM    127  CB  THR A  82       3.498 -10.716  45.118  1.00 48.24           C  
ANISOU  127  CB  THR A  82     7660   4884   5787    -27    501    543       C  
ATOM    128  OG1 THR A  82       4.004  -9.378  45.323  1.00 45.60           O  
ANISOU  128  OG1 THR A  82     7198   4694   5433     34    407    526       O  
ATOM    129  CG2 THR A  82       2.082 -10.659  44.495  1.00 46.86           C  
ANISOU  129  CG2 THR A  82     7432   4703   5670   -208    545    494       C  
ATOM    130  N   TYR A  83       5.766 -12.331  46.224  1.00 48.90           N  
ANISOU  130  N   TYR A  83     7981   4831   5768    296    508    664       N  
ATOM    131  CA  TYR A  83       7.205 -12.368  46.428  1.00 48.58           C  
ANISOU  131  CA  TYR A  83     7942   4825   5690    476    441    685       C  
ATOM    132  C   TYR A  83       7.839 -11.865  45.152  1.00 47.55           C  
ANISOU  132  C   TYR A  83     7690   4758   5619    467    381    603       C  
ATOM    133  O   TYR A  83       7.485 -12.310  44.066  1.00 46.82           O  
ANISOU  133  O   TYR A  83     7613   4596   5579    377    422    555       O  
ATOM    134  CB  TYR A  83       7.712 -13.791  46.772  1.00 48.97           C  
ANISOU  134  CB  TYR A  83     8175   4726   5706    590    505    753       C  
ATOM    135  CG  TYR A  83       7.175 -14.282  48.086  1.00 49.93           C  
ANISOU  135  CG  TYR A  83     8435   4781   5756    614    570    845       C  
ATOM    136  CD1 TYR A  83       5.911 -14.885  48.161  1.00 52.04           C  
ANISOU  136  CD1 TYR A  83     8797   4934   6043    467    687    862       C  
ATOM    137  CD2 TYR A  83       7.901 -14.111  49.264  1.00 50.10           C  
ANISOU  137  CD2 TYR A  83     8487   4861   5686    777    517    912       C  
ATOM    138  CE1 TYR A  83       5.386 -15.309  49.376  1.00 56.66           C  
ANISOU  138  CE1 TYR A  83     9512   5455   6560    481    762    949       C  
ATOM    139  CE2 TYR A  83       7.388 -14.532  50.485  1.00 56.24           C  
ANISOU  139  CE2 TYR A  83     9404   5581   6385    802    581   1000       C  
ATOM    140  CZ  TYR A  83       6.135 -15.132  50.538  1.00 59.37           C  
ANISOU  140  CZ  TYR A  83     9901   5855   6803    654    711   1022       C  
ATOM    141  OH  TYR A  83       5.623 -15.549  51.740  1.00 63.72           O  
ANISOU  141  OH  TYR A  83    10595   6343   7274    674    790   1112       O  
ATOM    142  N   ASP A  84       8.767 -10.924  45.279  1.00 45.64           N  
ANISOU  142  N   ASP A  84     7329   4649   5365    553    286    583       N  
ATOM    143  CA  ASP A  84       9.488 -10.468  44.122  1.00 44.42           C  
ANISOU  143  CA  ASP A  84     7067   4551   5262    555    241    513       C  
ATOM    144  C   ASP A  84      10.699 -11.391  43.889  1.00 45.13           C  
ANISOU  144  C   ASP A  84     7216   4584   5349    703    246    528       C  
ATOM    145  O   ASP A  84      11.619 -11.443  44.697  1.00 44.18           O  
ANISOU  145  O   ASP A  84     7094   4508   5185    851    199    568       O  
ATOM    146  CB  ASP A  84       9.890  -9.010  44.306  1.00 43.94           C  
ANISOU  146  CB  ASP A  84     6848   4650   5199    561    150    478       C  
ATOM    147  CG  ASP A  84      10.570  -8.430  43.090  1.00 45.41           C  
ANISOU  147  CG  ASP A  84     6922   4895   5438    546    115    406       C  
ATOM    148  OD1 ASP A  84      11.614  -8.992  42.648  1.00 46.06           O  
ANISOU  148  OD1 ASP A  84     7011   4956   5533    644    115    399       O  
ATOM    149  OD2 ASP A  84      10.075  -7.373  42.621  1.00 44.58           O  
ANISOU  149  OD2 ASP A  84     6721   4860   5358    445     91    360       O  
ATOM    150  N   THR A  85      10.682 -12.116  42.774  1.00 44.54           N  
ANISOU  150  N   THR A  85     7191   4414   5317    666    301    492       N  
ATOM    151  CA  THR A  85      11.778 -13.008  42.427  1.00 44.82           C  
ANISOU  151  CA  THR A  85     7285   4387   5356    805    319    499       C  
ATOM    152  C   THR A  85      12.644 -12.366  41.367  1.00 44.14           C  
ANISOU  152  C   THR A  85     7065   4393   5315    820    278    427       C  
ATOM    153  O   THR A  85      13.811 -12.741  41.202  1.00 45.13           O  
ANISOU  153  O   THR A  85     7177   4525   5445    961    269    427       O  
ATOM    154  CB  THR A  85      11.278 -14.391  41.964  1.00 45.08           C  
ANISOU  154  CB  THR A  85     7494   4233   5400    770    423    510       C  
ATOM    155  OG1 THR A  85      10.461 -14.236  40.807  1.00 45.21           O  
ANISOU  155  OG1 THR A  85     7488   4226   5464    602    453    436       O  
ATOM    156  CG2 THR A  85      10.432 -14.988  43.025  1.00 46.48           C  
ANISOU  156  CG2 THR A  85     7806   4319   5537    745    477    583       C  
ATOM    157  N   LEU A  86      12.091 -11.365  40.685  1.00 43.02           N  
ANISOU  157  N   LEU A  86     6819   4325   5203    684    254    369       N  
ATOM    158  CA  LEU A  86      12.821 -10.693  39.603  1.00 42.37           C  
ANISOU  158  CA  LEU A  86     6618   4322   5159    680    229    301       C  
ATOM    159  C   LEU A  86      14.107 -10.009  40.076  1.00 44.60           C  
ANISOU  159  C   LEU A  86     6774   4732   5440    804    159    302       C  
ATOM    160  O   LEU A  86      15.091  -9.954  39.332  1.00 43.91           O  
ANISOU  160  O   LEU A  86     6621   4680   5384    862    161    263       O  
ATOM    161  CB  LEU A  86      11.930  -9.673  38.893  1.00 39.22           C  
ANISOU  161  CB  LEU A  86     6142   3979   4780    520    213    250       C  
ATOM    162  CG  LEU A  86      12.565  -8.847  37.762  1.00 37.51           C  
ANISOU  162  CG  LEU A  86     5815   3843   4595    500    195    185       C  
ATOM    163  CD1 LEU A  86      13.036  -9.743  36.629  1.00 39.17           C  
ANISOU  163  CD1 LEU A  86     6091   3969   4821    528    256    150       C  
ATOM    164  CD2 LEU A  86      11.585  -7.827  37.232  1.00 35.15           C  
ANISOU  164  CD2 LEU A  86     5458   3594   4303    356    175    150       C  
ATOM    165  N   CYS A  87      14.096  -9.502  41.314  1.00 45.28           N  
ANISOU  165  N   CYS A  87     6825   4889   5489    840    100    342       N  
ATOM    166  CA  CYS A  87      15.201  -8.710  41.832  1.00 46.80           C  
ANISOU  166  CA  CYS A  87     6884   5219   5680    932     20    331       C  
ATOM    167  C   CYS A  87      16.469  -9.563  41.860  1.00 50.20           C  
ANISOU  167  C   CYS A  87     7320   5640   6112   1106     20    346       C  
ATOM    168  O   CYS A  87      17.579  -9.048  41.993  1.00 49.53           O  
ANISOU  168  O   CYS A  87     7106   5671   6043   1188    -38    320       O  
ATOM    169  CB  CYS A  87      14.864  -8.161  43.229  1.00 47.54           C  
ANISOU  169  CB  CYS A  87     6969   5376   5718    942    -40    371       C  
ATOM    170  SG  CYS A  87      14.533  -9.430  44.496  1.00 54.75           S  
ANISOU  170  SG  CYS A  87     8063   6186   6555   1050    -14    470       S  
ATOM    171  N   ALA A  88      16.286 -10.879  41.736  1.00 57.07           N  
ANISOU  171  N   ALA A  88     8343   6370   6970   1161     89    385       N  
ATOM    172  CA  ALA A  88      17.397 -11.835  41.711  1.00 59.09           C  
ANISOU  172  CA  ALA A  88     8630   6593   7227   1341    103    405       C  
ATOM    173  C   ALA A  88      18.243 -11.608  40.474  1.00 59.32           C  
ANISOU  173  C   ALA A  88     8554   6667   7320   1348    123    334       C  
ATOM    174  O   ALA A  88      19.426 -11.950  40.463  1.00 58.30           O  
ANISOU  174  O   ALA A  88     8370   6578   7205   1501    111    332       O  
ATOM    175  CB  ALA A  88      16.886 -13.268  41.747  1.00 54.98           C  
ANISOU  175  CB  ALA A  88     8319   5889   6683   1378    189    458       C  
ATOM    176  N   GLN A  89      17.623 -11.018  39.448  1.00 59.32           N  
ANISOU  176  N   GLN A  89     8524   6662   7352   1187    156    277       N  
ATOM    177  CA  GLN A  89      18.270 -10.781  38.152  1.00 63.88           C  
ANISOU  177  CA  GLN A  89     9023   7268   7980   1171    193    209       C  
ATOM    178  C   GLN A  89      19.114  -9.502  38.109  1.00 62.23           C  
ANISOU  178  C   GLN A  89     8614   7226   7804   1164    134    165       C  
ATOM    179  O   GLN A  89      19.856  -9.286  37.147  1.00 60.30           O  
ANISOU  179  O   GLN A  89     8290   7020   7602   1172    169    114       O  
ATOM    180  CB  GLN A  89      17.236 -10.763  37.005  1.00 67.55           C  
ANISOU  180  CB  GLN A  89     9561   7652   8454   1007    254    168       C  
ATOM    181  CG  GLN A  89      16.533 -12.085  36.736  1.00 72.20           C  
ANISOU  181  CG  GLN A  89    10340   8069   9025    997    329    186       C  
ATOM    182  CD  GLN A  89      17.509 -13.240  36.669  1.00 82.31           C  
ANISOU  182  CD  GLN A  89    11689   9274  10309   1168    377    203       C  
ATOM    183  OE1 GLN A  89      18.258 -13.382  35.693  1.00 88.51           O  
ANISOU  183  OE1 GLN A  89    12443  10064  11123   1212    420    155       O  
ATOM    184  NE2 GLN A  89      17.520 -14.071  37.719  1.00 80.39           N  
ANISOU  184  NE2 GLN A  89    11547   8962  10034   1276    375    274       N  
ATOM    185  N   SER A  90      18.989  -8.660  39.140  1.00 61.84           N  
ANISOU  185  N   SER A  90     8491   7271   7733   1145     52    182       N  
ATOM    186  CA  SER A  90      19.770  -7.423  39.240  1.00 63.82           C  
ANISOU  186  CA  SER A  90     8557   7675   8015   1129     -8    136       C  
ATOM    187  C   SER A  90      21.289  -7.687  39.284  1.00 69.14           C  
ANISOU  187  C   SER A  90     9117   8431   8722   1283    -26    119       C  
ATOM    188  O   SER A  90      21.768  -8.423  40.149  1.00 69.11           O  
ANISOU  188  O   SER A  90     9139   8431   8689   1434    -64    163       O  
ATOM    189  CB  SER A  90      19.360  -6.665  40.490  1.00 61.11           C  
ANISOU  189  CB  SER A  90     8184   7402   7632   1099    -93    159       C  
ATOM    190  OG  SER A  90      19.987  -5.406  40.505  1.00 65.78           O  
ANISOU  190  OG  SER A  90     8611   8126   8256   1054   -143    105       O  
ATOM    191  N   GLN A  91      22.038  -7.106  38.348  1.00 74.53           N  
ANISOU  191  N   GLN A  91     9676   9181   9463   1251      6     56       N  
ATOM    192  CA  GLN A  91      23.506  -7.269  38.341  1.00 84.19           C  
ANISOU  192  CA  GLN A  91    10759  10499  10729   1388     -6     30       C  
ATOM    193  C   GLN A  91      24.162  -6.038  38.955  1.00 84.05           C  
ANISOU  193  C   GLN A  91    10553  10646  10737   1356    -91    -12       C  
ATOM    194  O   GLN A  91      25.386  -5.968  39.058  1.00 87.88           O  
ANISOU  194  O   GLN A  91    10886  11240  11264   1450   -117    -45       O  
ATOM    195  CB  GLN A  91      24.071  -7.504  36.922  1.00 85.91           C  
ANISOU  195  CB  GLN A  91    10950  10691  11000   1387     98    -17       C  
ATOM    196  CG  GLN A  91      23.277  -8.457  36.030  1.00 91.11           C  
ANISOU  196  CG  GLN A  91    11797  11184  11635   1362    192     -1       C  
ATOM    197  CD  GLN A  91      23.677  -9.917  36.186  1.00 95.80           C  
ANISOU  197  CD  GLN A  91    12493  11690  12216   1538    226     36       C  
ATOM    198  OE1 GLN A  91      23.633 -10.480  37.287  1.00 98.49           O  
ANISOU  198  OE1 GLN A  91    12887  12015  12520   1643    169     94       O  
ATOM    199  NE2 GLN A  91      24.053 -10.546  35.071  1.00 89.46           N  
ANISOU  199  NE2 GLN A  91    11732  10822  11437   1575    325      6       N  
ATOM    200  N   GLN A  92      23.340  -5.078  39.377  1.00 81.34           N  
ANISOU  200  N   GLN A  92    10218  10319  10369   1222   -134    -14       N  
ATOM    201  CA  GLN A  92      23.846  -3.770  39.771  1.00 81.15           C  
ANISOU  201  CA  GLN A  92    10031  10430  10372   1153   -198    -67       C  
ATOM    202  C   GLN A  92      23.341  -3.263  41.116  1.00 76.90           C  
ANISOU  202  C   GLN A  92     9508   9935   9776   1136   -299    -45       C  
ATOM    203  O   GLN A  92      22.138  -3.144  41.342  1.00 74.67           O  
ANISOU  203  O   GLN A  92     9348   9575   9447   1057   -293    -11       O  
ATOM    204  CB  GLN A  92      23.540  -2.748  38.685  1.00 81.94           C  
ANISOU  204  CB  GLN A  92    10099  10521  10515    985   -131   -115       C  
ATOM    205  CG  GLN A  92      24.222  -1.407  38.888  1.00 86.28           C  
ANISOU  205  CG  GLN A  92    10478  11196  11109    906   -172   -179       C  
ATOM    206  CD  GLN A  92      24.414  -0.672  37.579  1.00 91.42           C  
ANISOU  206  CD  GLN A  92    11080  11840  11816    788    -77   -226       C  
ATOM    207  OE1 GLN A  92      23.758  -0.978  36.572  1.00 87.40           O  
ANISOU  207  OE1 GLN A  92    10684  11229  11295    743      6   -209       O  
ATOM    208  NE2 GLN A  92      25.326   0.297  37.576  1.00 93.71           N  
ANISOU  208  NE2 GLN A  92    11204  12237  12164    736    -86   -289       N  
ATOM    209  N   ASP A  93      24.289  -2.941  41.986  1.00 74.36           N  
ANISOU  209  N   ASP A  93     9052   9744   9457   1210   -392    -73       N  
ATOM    210  CA  ASP A  93      23.996  -2.451  43.325  1.00 71.72           C  
ANISOU  210  CA  ASP A  93     8723   9469   9059   1211   -497    -62       C  
ATOM    211  C   ASP A  93      23.470  -1.012  43.297  1.00 66.97           C  
ANISOU  211  C   ASP A  93     8083   8894   8471   1032   -504   -111       C  
ATOM    212  O   ASP A  93      24.067  -0.135  42.677  1.00 63.40           O  
ANISOU  212  O   ASP A  93     7500   8502   8086    946   -483   -180       O  
ATOM    213  CB  ASP A  93      25.245  -2.542  44.216  1.00 73.28           C  
ANISOU  213  CB  ASP A  93     8780   9812   9252   1349   -604    -88       C  
ATOM    214  CG  ASP A  93      25.918  -3.921  44.165  1.00 78.76           C  
ANISOU  214  CG  ASP A  93     9496  10488   9942   1546   -594    -42       C  
ATOM    215  OD1 ASP A  93      25.220  -4.953  43.989  1.00 79.21           O  
ANISOU  215  OD1 ASP A  93     9730  10406   9960   1599   -533     30       O  
ATOM    216  OD2 ASP A  93      27.159  -3.967  44.307  1.00 81.91           O  
ANISOU  216  OD2 ASP A  93     9733  11012  10378   1649   -648    -83       O  
ATOM    217  N   GLY A  94      22.340  -0.795  43.969  1.00 62.46           N  
ANISOU  217  N   GLY A  94     7631   8270   7833    981   -524    -73       N  
ATOM    218  CA  GLY A  94      21.832   0.540  44.247  1.00 60.35           C  
ANISOU  218  CA  GLY A  94     7339   8032   7561    843   -548   -114       C  
ATOM    219  C   GLY A  94      22.518   1.110  45.484  1.00 59.73           C  
ANISOU  219  C   GLY A  94     7164   8081   7448    882   -666   -155       C  
ATOM    220  O   GLY A  94      23.599   0.647  45.873  1.00 58.83           O  
ANISOU  220  O   GLY A  94     6956   8058   7338   1001   -728   -169       O  
ATOM    221  N   PRO A  95      21.887   2.117  46.115  1.00 58.19           N  
ANISOU  221  N   PRO A  95     6993   7898   7217    788   -700   -177       N  
ATOM    222  CA  PRO A  95      22.479   2.948  47.174  1.00 55.58           C  
ANISOU  222  CA  PRO A  95     6571   7689   6860    783   -808   -239       C  
ATOM    223  C   PRO A  95      22.262   2.485  48.645  1.00 55.86           C  
ANISOU  223  C   PRO A  95     6686   7759   6780    896   -903   -198       C  
ATOM    224  O   PRO A  95      22.969   2.960  49.546  1.00 54.70           O  
ANISOU  224  O   PRO A  95     6453   7731   6601    924  -1010   -253       O  
ATOM    225  CB  PRO A  95      21.786   4.292  46.940  1.00 54.28           C  
ANISOU  225  CB  PRO A  95     6418   7490   6714    615   -771   -283       C  
ATOM    226  CG  PRO A  95      20.392   3.914  46.463  1.00 52.01           C  
ANISOU  226  CG  PRO A  95     6291   7068   6404    582   -684   -207       C  
ATOM    227  CD  PRO A  95      20.523   2.575  45.763  1.00 55.24           C  
ANISOU  227  CD  PRO A  95     6737   7420   6831    672   -631   -150       C  
ATOM    228  N   CYS A  96      21.305   1.580  48.886  1.00 54.71           N  
ANISOU  228  N   CYS A  96     6705   7512   6569    954   -863   -105       N  
ATOM    229  CA  CYS A  96      21.004   1.111  50.249  1.00 54.58           C  
ANISOU  229  CA  CYS A  96     6790   7512   6434   1059   -932    -54       C  
ATOM    230  C   CYS A  96      22.000   0.069  50.759  1.00 57.48           C  
ANISOU  230  C   CYS A  96     7132   7944   6764   1246  -1005    -24       C  
ATOM    231  O   CYS A  96      22.707  -0.564  49.969  1.00 57.56           O  
ANISOU  231  O   CYS A  96     7077   7952   6841   1306   -976    -21       O  
ATOM    232  CB  CYS A  96      19.568   0.590  50.347  1.00 51.88           C  
ANISOU  232  CB  CYS A  96     6636   7036   6042   1037   -850     32       C  
ATOM    233  SG  CYS A  96      18.315   1.846  49.963  1.00 49.01           S  
ANISOU  233  SG  CYS A  96     6303   6614   5705    845   -781      1       S  
ATOM    234  N   THR A  97      22.073  -0.069  52.084  1.00 58.88           N  
ANISOU  234  N   THR A  97     7361   8183   6829   1344  -1100     -2       N  
ATOM    235  CA  THR A  97      22.823  -1.146  52.746  1.00 62.78           C  
ANISOU  235  CA  THR A  97     7872   8724   7256   1546  -1173     49       C  
ATOM    236  C   THR A  97      22.014  -1.533  53.989  1.00 63.36           C  
ANISOU  236  C   THR A  97     8130   8757   7185   1616  -1196    127       C  
ATOM    237  O   THR A  97      21.124  -0.795  54.376  1.00 60.82           O  
ANISOU  237  O   THR A  97     7873   8410   6826   1505  -1175    116       O  
ATOM    238  CB  THR A  97      24.254  -0.732  53.217  1.00 62.78           C  
ANISOU  238  CB  THR A  97     7681   8912   7260   1622  -1316    -36       C  
ATOM    239  OG1 THR A  97      24.149   0.093  54.381  1.00 64.68           O  
ANISOU  239  OG1 THR A  97     7926   9241   7407   1595  -1418    -79       O  
ATOM    240  CG2 THR A  97      25.066   0.007  52.134  1.00 60.52           C  
ANISOU  240  CG2 THR A  97     7187   8690   7117   1513  -1296   -136       C  
ATOM    241  N   PRO A  98      22.336  -2.682  54.628  1.00 66.42           N  
ANISOU  241  N   PRO A  98     8609   9140   7489   1806  -1232    208       N  
ATOM    242  CA  PRO A  98      21.710  -3.047  55.909  1.00 66.58           C  
ANISOU  242  CA  PRO A  98     8807   9135   7357   1887  -1259    285       C  
ATOM    243  C   PRO A  98      21.685  -1.933  56.970  1.00 67.48           C  
ANISOU  243  C   PRO A  98     8890   9364   7384   1840  -1362    219       C  
ATOM    244  O   PRO A  98      20.783  -1.915  57.809  1.00 64.03           O  
ANISOU  244  O   PRO A  98     8610   8879   6840   1832  -1339    269       O  
ATOM    245  CB  PRO A  98      22.589  -4.209  56.402  1.00 65.79           C  
ANISOU  245  CB  PRO A  98     8740   9069   7189   2122  -1328    350       C  
ATOM    246  CG  PRO A  98      23.072  -4.858  55.144  1.00 65.15           C  
ANISOU  246  CG  PRO A  98     8588   8931   7234   2144  -1257    353       C  
ATOM    247  CD  PRO A  98      23.232  -3.754  54.132  1.00 65.05           C  
ANISOU  247  CD  PRO A  98     8395   8964   7355   1959  -1233    242       C  
ATOM    248  N   ARG A  99      22.675  -1.038  56.951  1.00 70.16           N  
ANISOU  248  N   ARG A  99     9034   9855   7767   1808  -1470    105       N  
ATOM    249  CA  ARG A  99      22.804   0.004  57.994  1.00 71.14           C  
ANISOU  249  CA  ARG A  99     9125  10100   7806   1770  -1584     27       C  
ATOM    250  C   ARG A  99      21.813   1.142  57.828  1.00 67.18           C  
ANISOU  250  C   ARG A  99     8652   9541   7334   1569  -1511    -21       C  
ATOM    251  O   ARG A  99      21.324   1.668  58.826  1.00 63.19           O  
ANISOU  251  O   ARG A  99     8232   9058   6719   1552  -1549    -33       O  
ATOM    252  CB  ARG A  99      24.224   0.583  58.075  1.00 76.34           C  
ANISOU  252  CB  ARG A  99     9558  10944   8503   1794  -1729    -89       C  
ATOM    253  CG  ARG A  99      25.024   0.118  59.279  1.00 85.14           C  
ANISOU  253  CG  ARG A  99    10674  12194   9480   1990  -1890    -78       C  
ATOM    254  CD  ARG A  99      26.146   1.099  59.622  1.00 88.76           C  
ANISOU  254  CD  ARG A  99    10916  12851   9957   1954  -2047   -224       C  
ATOM    255  NE  ARG A  99      26.894   0.706  60.820  1.00 90.01           N  
ANISOU  255  NE  ARG A  99    11071  13157   9971   2145  -2219   -222       N  
ATOM    256  CZ  ARG A  99      27.786  -0.290  60.871  1.00 95.85           C  
ANISOU  256  CZ  ARG A  99    11755  13968  10697   2349  -2292   -176       C  
ATOM    257  NH1 ARG A  99      28.048  -1.026  59.792  1.00 90.51           N  
ANISOU  257  NH1 ARG A  99    11025  13221  10142   2388  -2198   -129       N  
ATOM    258  NH2 ARG A  99      28.423  -0.560  62.010  1.00 97.87           N  
ANISOU  258  NH2 ARG A  99    12013  14367  10808   2524  -2460   -177       N  
ATOM    259  N   ARG A 100      21.535   1.517  56.577  1.00 61.92           N  
ANISOU  259  N   ARG A 100     7919   8800   6807   1429  -1408    -49       N  
ATOM    260  CA  ARG A 100      20.668   2.641  56.295  1.00 58.98           C  
ANISOU  260  CA  ARG A 100     7559   8376   6475   1248  -1340    -97       C  
ATOM    261  C   ARG A 100      20.052   2.598  54.905  1.00 57.96           C  
ANISOU  261  C   ARG A 100     7427   8124   6470   1138  -1201    -75       C  
ATOM    262  O   ARG A 100      20.701   2.181  53.915  1.00 55.06           O  
ANISOU  262  O   ARG A 100     6966   7754   6201   1151  -1176    -81       O  
ATOM    263  CB  ARG A 100      21.378   3.986  56.533  1.00 60.07           C  
ANISOU  263  CB  ARG A 100     7551   8636   6637   1154  -1433   -232       C  
ATOM    264  CG  ARG A 100      22.327   4.435  55.439  1.00 61.55           C  
ANISOU  264  CG  ARG A 100     7543   8871   6971   1076  -1432   -314       C  
ATOM    265  CD  ARG A 100      23.560   3.547  55.377  1.00 65.45           C  
ANISOU  265  CD  ARG A 100     7925   9461   7482   1223  -1509   -309       C  
ATOM    266  NE  ARG A 100      24.542   4.111  54.462  1.00 69.27           N  
ANISOU  266  NE  ARG A 100     8205  10012   8101   1140  -1511   -402       N  
ATOM    267  CZ  ARG A 100      24.534   3.958  53.137  1.00 70.12           C  
ANISOU  267  CZ  ARG A 100     8268  10043   8330   1078  -1398   -390       C  
ATOM    268  NH1 ARG A 100      23.592   3.231  52.526  1.00 65.31           N  
ANISOU  268  NH1 ARG A 100     7799   9289   7728   1088  -1280   -292       N  
ATOM    269  NH2 ARG A 100      25.493   4.535  52.421  1.00 68.25           N  
ANISOU  269  NH2 ARG A 100     7844   9880   8208   1003  -1400   -480       N  
ATOM    270  N   CYS A 101      18.785   3.019  54.865  1.00 51.15           N  
ANISOU  270  N   CYS A 101     6670   7166   5597   1037  -1113    -51       N  
ATOM    271  CA  CYS A 101      18.045   3.169  53.616  1.00 51.04           C  
ANISOU  271  CA  CYS A 101     6660   7046   5689    919   -992    -39       C  
ATOM    272  C   CYS A 101      18.230   4.571  53.006  1.00 49.33           C  
ANISOU  272  C   CYS A 101     6328   6859   5556    772   -988   -140       C  
ATOM    273  O   CYS A 101      18.000   5.594  53.664  1.00 45.57           O  
ANISOU  273  O   CYS A 101     5859   6417   5040    712  -1022   -195       O  
ATOM    274  CB  CYS A 101      16.554   2.857  53.818  1.00 47.66           C  
ANISOU  274  CB  CYS A 101     6392   6503   5213    890   -895     40       C  
ATOM    275  SG  CYS A 101      15.567   3.134  52.333  1.00 47.46           S  
ANISOU  275  SG  CYS A 101     6364   6364   5304    746   -765     46       S  
ATOM    276  N   LEU A 102      18.622   4.583  51.735  1.00 49.22           N  
ANISOU  276  N   LEU A 102     6225   6821   5655    719   -938   -160       N  
ATOM    277  CA  LEU A 102      18.881   5.798  50.962  1.00 51.11           C  
ANISOU  277  CA  LEU A 102     6362   7073   5985    583   -915   -244       C  
ATOM    278  C   LEU A 102      17.945   5.851  49.766  1.00 51.67           C  
ANISOU  278  C   LEU A 102     6484   7028   6122    496   -796   -208       C  
ATOM    279  O   LEU A 102      18.187   6.601  48.819  1.00 51.11           O  
ANISOU  279  O   LEU A 102     6340   6946   6133    399   -755   -257       O  
ATOM    280  CB  LEU A 102      20.355   5.819  50.480  1.00 53.39           C  
ANISOU  280  CB  LEU A 102     6483   7454   6350    598   -963   -309       C  
ATOM    281  CG  LEU A 102      21.399   6.780  51.091  1.00 53.98           C  
ANISOU  281  CG  LEU A 102     6425   7657   6430    562  -1064   -419       C  
ATOM    282  CD1 LEU A 102      21.083   7.170  52.535  1.00 50.60           C  
ANISOU  282  CD1 LEU A 102     6066   7275   5883    589  -1152   -438       C  
ATOM    283  CD2 LEU A 102      22.818   6.251  50.953  1.00 52.94           C  
ANISOU  283  CD2 LEU A 102     6138   7634   6342    644  -1129   -454       C  
ATOM    284  N   GLY A 103      16.856   5.077  49.838  1.00 52.13           N  
ANISOU  284  N   GLY A 103     6670   7001   6138    528   -740   -123       N  
ATOM    285  CA  GLY A 103      15.897   4.950  48.743  1.00 50.37           C  
ANISOU  285  CA  GLY A 103     6497   6675   5965    459   -638    -85       C  
ATOM    286  C   GLY A 103      15.188   6.236  48.372  1.00 49.33           C  
ANISOU  286  C   GLY A 103     6365   6515   5864    338   -599   -123       C  
ATOM    287  O   GLY A 103      14.596   6.327  47.287  1.00 47.67           O  
ANISOU  287  O   GLY A 103     6169   6239   5706    275   -526   -108       O  
ATOM    288  N   SER A 104      15.260   7.246  49.243  1.00 47.10           N  
ANISOU  288  N   SER A 104     6071   6282   5543    310   -648   -176       N  
ATOM    289  CA  SER A 104      14.554   8.511  48.990  1.00 46.99           C  
ANISOU  289  CA  SER A 104     6073   6231   5551    208   -607   -210       C  
ATOM    290  C   SER A 104      15.380   9.561  48.219  1.00 51.57           C  
ANISOU  290  C   SER A 104     6557   6830   6210    120   -603   -288       C  
ATOM    291  O   SER A 104      14.817  10.552  47.718  1.00 48.91           O  
ANISOU  291  O   SER A 104     6240   6441   5901     37   -553   -307       O  
ATOM    292  CB  SER A 104      14.013   9.100  50.295  1.00 47.29           C  
ANISOU  292  CB  SER A 104     6175   6289   5503    216   -641   -226       C  
ATOM    293  OG  SER A 104      14.930   9.984  50.880  1.00 42.83           O  
ANISOU  293  OG  SER A 104     5547   5796   4929    191   -712   -313       O  
ATOM    294  N   LEU A 105      16.703   9.339  48.121  1.00 53.25           N  
ANISOU  294  N   LEU A 105     6663   7113   6457    141   -651   -331       N  
ATOM    295  CA  LEU A 105      17.589  10.257  47.407  1.00 52.40           C  
ANISOU  295  CA  LEU A 105     6454   7027   6430     51   -638   -406       C  
ATOM    296  C   LEU A 105      17.336  10.239  45.909  1.00 49.18           C  
ANISOU  296  C   LEU A 105     6050   6544   6093      0   -541   -378       C  
ATOM    297  O   LEU A 105      17.223   9.158  45.292  1.00 48.75           O  
ANISOU  297  O   LEU A 105     6012   6463   6047     55   -510   -320       O  
ATOM    298  CB  LEU A 105      19.072   9.975  47.695  1.00 57.19           C  
ANISOU  298  CB  LEU A 105     6927   7741   7060     89   -712   -463       C  
ATOM    299  CG  LEU A 105      19.444   9.750  49.156  1.00 62.06           C  
ANISOU  299  CG  LEU A 105     7536   8449   7593    168   -826   -485       C  
ATOM    300  CD1 LEU A 105      20.825  10.323  49.421  1.00 62.97           C  
ANISOU  300  CD1 LEU A 105     7501   8677   7749    134   -900   -589       C  
ATOM    301  CD2 LEU A 105      18.404  10.308  50.124  1.00 55.68           C  
ANISOU  301  CD2 LEU A 105     6847   7609   6699    155   -838   -479       C  
ATOM    302  N   VAL A 106      17.237  11.438  45.338  1.00 46.28           N  
ANISOU  302  N   VAL A 106     5680   6137   5768   -104   -493   -418       N  
ATOM    303  CA  VAL A 106      16.922  11.599  43.912  1.00 52.49           C  
ANISOU  303  CA  VAL A 106     6487   6848   6606   -156   -400   -391       C  
ATOM    304  C   VAL A 106      18.038  11.061  43.010  1.00 53.29           C  
ANISOU  304  C   VAL A 106     6495   6981   6772   -151   -373   -405       C  
ATOM    305  O   VAL A 106      17.776  10.348  42.029  1.00 47.53           O  
ANISOU  305  O   VAL A 106     5796   6209   6057   -128   -318   -355       O  
ATOM    306  CB  VAL A 106      16.536  13.058  43.550  1.00 53.67           C  
ANISOU  306  CB  VAL A 106     6675   6939   6777   -257   -349   -424       C  
ATOM    307  CG1 VAL A 106      16.462  13.251  42.032  1.00 51.62           C  
ANISOU  307  CG1 VAL A 106     6431   6614   6567   -305   -258   -400       C  
ATOM    308  CG2 VAL A 106      15.208  13.435  44.202  1.00 51.77           C  
ANISOU  308  CG2 VAL A 106     6541   6653   6476   -243   -354   -393       C  
ATOM    309  N   LEU A 107      19.274  11.404  43.352  1.00 61.70           N  
ANISOU  309  N   LEU A 107     7443   8125   7875   -175   -411   -477       N  
ATOM    310  CA  LEU A 107      20.428  10.822  42.686  1.00 73.07           C  
ANISOU  310  CA  LEU A 107     8772   9616   9376   -154   -393   -496       C  
ATOM    311  C   LEU A 107      21.494  10.431  43.705  1.00 83.83           C  
ANISOU  311  C   LEU A 107    10018  11099  10734    -91   -493   -544       C  
ATOM    312  O   LEU A 107      22.209  11.283  44.234  1.00 87.79           O  
ANISOU  312  O   LEU A 107    10432  11665  11260   -154   -536   -627       O  
ATOM    313  CB  LEU A 107      20.969  11.734  41.572  1.00 76.87           C  
ANISOU  313  CB  LEU A 107     9206  10069   9934   -267   -302   -538       C  
ATOM    314  CG  LEU A 107      20.873  13.265  41.679  1.00 79.53           C  
ANISOU  314  CG  LEU A 107     9559  10369  10289   -392   -277   -594       C  
ATOM    315  CD1 LEU A 107      22.232  13.880  42.011  1.00 85.65           C  
ANISOU  315  CD1 LEU A 107    10184  11230  11128   -463   -301   -694       C  
ATOM    316  CD2 LEU A 107      20.322  13.848  40.379  1.00 76.03           C  
ANISOU  316  CD2 LEU A 107     9200   9820   9867   -460   -162   -559       C  
ATOM    317  N   PRO A 108      21.572   9.128  44.020  1.00 94.42           N  
ANISOU  317  N   PRO A 108    11364  12470  12040     38   -534   -494       N  
ATOM    318  CA  PRO A 108      22.659   8.652  44.874  1.00 98.96           C  
ANISOU  318  CA  PRO A 108    11824  13167  12610    122   -632   -533       C  
ATOM    319  C   PRO A 108      23.947   8.380  44.067  1.00100.84           C  
ANISOU  319  C   PRO A 108    11909  13467  12936    130   -600   -573       C  
ATOM    320  O   PRO A 108      23.884   7.938  42.912  1.00 92.41           O  
ANISOU  320  O   PRO A 108    10863  12339  11909    130   -505   -536       O  
ATOM    321  CB  PRO A 108      22.088   7.364  45.499  1.00 94.56           C  
ANISOU  321  CB  PRO A 108    11364  12592  11971    265   -674   -449       C  
ATOM    322  CG  PRO A 108      20.683   7.216  44.965  1.00 88.08           C  
ANISOU  322  CG  PRO A 108    10698  11644  11123    235   -595   -376       C  
ATOM    323  CD  PRO A 108      20.604   8.055  43.728  1.00 91.20           C  
ANISOU  323  CD  PRO A 108    11080  11984  11589    115   -501   -401       C  
ATOM    324  N   ARG A 109      25.092   8.656  44.689  1.00103.38           N  
ANISOU  324  N   ARG A 109    12078  13916  13287    135   -679   -652       N  
ATOM    325  CA  ARG A 109      26.403   8.611  44.040  1.00108.85           C  
ANISOU  325  CA  ARG A 109    12593  14691  14075    125   -651   -710       C  
ATOM    326  C   ARG A 109      26.786   7.185  43.656  1.00107.43           C  
ANISOU  326  C   ARG A 109    12394  14526  13899    279   -639   -652       C  
ATOM    327  O   ARG A 109      26.648   6.788  42.501  1.00 97.51           O  
ANISOU  327  O   ARG A 109    11175  13194  12679    275   -529   -613       O  
ATOM    328  CB  ARG A 109      27.476   9.217  44.963  1.00114.42           C  
ANISOU  328  CB  ARG A 109    13129  15544  14803     98   -759   -815       C  
ATOM    329  CG  ARG A 109      27.365  10.722  45.206  1.00120.55           C  
ANISOU  329  CG  ARG A 109    13898  16306  15598    -77   -756   -897       C  
ATOM    330  CD  ARG A 109      26.033  11.142  45.840  1.00126.14           C  
ANISOU  330  CD  ARG A 109    14795  16920  16213    -98   -774   -856       C  
ATOM    331  NE  ARG A 109      25.973  10.986  47.302  1.00130.85           N  
ANISOU  331  NE  ARG A 109    15407  17595  16715    -20   -915   -873       N  
ATOM    332  CZ  ARG A 109      25.293  10.041  47.959  1.00123.25           C  
ANISOU  332  CZ  ARG A 109    14559  16617  15655    117   -966   -790       C  
ATOM    333  NH1 ARG A 109      24.600   9.117  47.310  1.00121.68           N  
ANISOU  333  NH1 ARG A 109    14463  16326  15443    190   -893   -687       N  
ATOM    334  NH2 ARG A 109      25.309  10.014  49.284  1.00113.37           N  
ANISOU  334  NH2 ARG A 109    13322  15440  14312    180  -1089   -811       N  
ATOM    335  N   PRO A 121      36.246  -0.734  27.925  1.00 91.38           N  
ANISOU  335  N   PRO A 121     9705  12430  12584    970   1143   -745       N  
ATOM    336  CA  PRO A 121      35.745  -1.496  29.083  1.00 94.51           C  
ANISOU  336  CA  PRO A 121    10164  12815  12932   1100    972   -700       C  
ATOM    337  C   PRO A 121      36.075  -3.024  29.063  1.00 98.04           C  
ANISOU  337  C   PRO A 121    10650  13237  13364   1336    981   -674       C  
ATOM    338  O   PRO A 121      36.013  -3.682  30.108  1.00 98.22           O  
ANISOU  338  O   PRO A 121    10670  13281  13366   1472    847   -644       O  
ATOM    339  CB  PRO A 121      34.225  -1.230  29.043  1.00 94.11           C  
ANISOU  339  CB  PRO A 121    10366  12615  12776    991    929   -643       C  
ATOM    340  CG  PRO A 121      34.072   0.090  28.333  1.00 86.78           C  
ANISOU  340  CG  PRO A 121     9436  11674  11862    782   1018   -669       C  
ATOM    341  CD  PRO A 121      35.276   0.269  27.433  1.00 90.16           C  
ANISOU  341  CD  PRO A 121     9706  12177  12374    773   1177   -725       C  
ATOM    342  N   ALA A 122      36.401  -3.559  27.881  1.00 96.16           N  
ANISOU  342  N   ALA A 122    10461  12944  13130   1384   1143   -685       N  
ATOM    343  CA  ALA A 122      36.942  -4.929  27.669  1.00 97.66           C  
ANISOU  343  CA  ALA A 122    10665  13116  13324   1608   1191   -677       C  
ATOM    344  C   ALA A 122      36.064  -6.134  28.076  1.00 92.87           C  
ANISOU  344  C   ALA A 122    10290  12371  12627   1741   1115   -609       C  
ATOM    345  O   ALA A 122      35.094  -6.456  27.397  1.00 87.27           O  
ANISOU  345  O   ALA A 122     9818  11506  11836   1688   1167   -579       O  
ATOM    346  CB  ALA A 122      38.363  -5.052  28.241  1.00100.43           C  
ANISOU  346  CB  ALA A 122    10722  13654  13784   1742   1164   -724       C  
ATOM    347  N   GLU A 123      36.436  -6.802  29.165  1.00 94.62           N  
ANISOU  347  N   GLU A 123    10438  12652  12861   1914    995   -587       N  
ATOM    348  CA  GLU A 123      35.762  -8.010  29.659  1.00 95.01           C  
ANISOU  348  CA  GLU A 123    10692  12574  12832   2060    929   -520       C  
ATOM    349  C   GLU A 123      34.446  -7.669  30.379  1.00 90.68           C  
ANISOU  349  C   GLU A 123    10306  11945  12205   1940    808   -469       C  
ATOM    350  O   GLU A 123      33.496  -8.471  30.419  1.00 83.17           O  
ANISOU  350  O   GLU A 123     9586  10840  11175   1973    796   -416       O  
ATOM    351  CB  GLU A 123      36.747  -8.810  30.544  1.00101.81           C  
ANISOU  351  CB  GLU A 123    11409  13538  13736   2304    853   -512       C  
ATOM    352  CG  GLU A 123      36.330  -9.078  31.993  1.00107.09           C  
ANISOU  352  CG  GLU A 123    12116  14218  14354   2384    670   -454       C  
ATOM    353  CD  GLU A 123      37.442  -8.795  33.012  1.00113.45           C  
ANISOU  353  CD  GLU A 123    12645  15235  15225   2494    549   -483       C  
ATOM    354  OE1 GLU A 123      38.633  -9.091  32.730  1.00110.47           O  
ANISOU  354  OE1 GLU A 123    12079  14970  14926   2631    604   -525       O  
ATOM    355  OE2 GLU A 123      37.119  -8.272  34.109  1.00112.32           O  
ANISOU  355  OE2 GLU A 123    12470  15153  15052   2446    397   -466       O  
ATOM    356  N   GLN A 124      34.412  -6.464  30.940  1.00 89.39           N  
ANISOU  356  N   GLN A 124    10014  11885  12066   1798    726   -490       N  
ATOM    357  CA  GLN A 124      33.215  -5.905  31.550  1.00 87.32           C  
ANISOU  357  CA  GLN A 124     9877  11563  11737   1663    626   -453       C  
ATOM    358  C   GLN A 124      32.088  -5.756  30.509  1.00 82.09           C  
ANISOU  358  C   GLN A 124     9430  10746  11013   1517    717   -438       C  
ATOM    359  O   GLN A 124      30.928  -6.077  30.793  1.00 78.15           O  
ANISOU  359  O   GLN A 124     9122  10133  10440   1486    665   -388       O  
ATOM    360  CB  GLN A 124      33.556  -4.556  32.207  1.00 91.01           C  
ANISOU  360  CB  GLN A 124    10151  12176  12254   1535    544   -495       C  
ATOM    361  CG  GLN A 124      32.368  -3.727  32.685  1.00 90.09           C  
ANISOU  361  CG  GLN A 124    10147  12005  12078   1370    465   -469       C  
ATOM    362  CD  GLN A 124      31.806  -4.212  34.010  1.00 94.47           C  
ANISOU  362  CD  GLN A 124    10778  12545  12570   1458    316   -414       C  
ATOM    363  OE1 GLN A 124      31.645  -5.415  34.238  1.00 90.88           O  
ANISOU  363  OE1 GLN A 124    10438  12018  12075   1613    304   -364       O  
ATOM    364  NE2 GLN A 124      31.501  -3.271  34.895  1.00 93.89           N  
ANISOU  364  NE2 GLN A 124    10654  12535  12487   1358    209   -422       N  
ATOM    365  N   LEU A 125      32.438  -5.275  29.310  1.00 79.09           N  
ANISOU  365  N   LEU A 125     9016  10370  10664   1429    852   -482       N  
ATOM    366  CA  LEU A 125      31.470  -5.092  28.213  1.00 71.16           C  
ANISOU  366  CA  LEU A 125     8207   9236   9595   1299    940   -474       C  
ATOM    367  C   LEU A 125      30.903  -6.438  27.783  1.00 67.83           C  
ANISOU  367  C   LEU A 125     7998   8666   9107   1403    979   -443       C  
ATOM    368  O   LEU A 125      29.694  -6.605  27.654  1.00 63.79           O  
ANISOU  368  O   LEU A 125     7680   8037   8521   1330    953   -412       O  
ATOM    369  CB  LEU A 125      32.129  -4.416  27.002  1.00 67.63           C  
ANISOU  369  CB  LEU A 125     7681   8827   9188   1213   1090   -525       C  
ATOM    370  CG  LEU A 125      31.319  -3.447  26.135  1.00 64.60           C  
ANISOU  370  CG  LEU A 125     7411   8381   8755   1021   1148   -526       C  
ATOM    371  CD1 LEU A 125      31.975  -3.249  24.787  1.00 61.82           C  
ANISOU  371  CD1 LEU A 125     7040   8032   8419    990   1324   -565       C  
ATOM    372  CD2 LEU A 125      29.881  -3.880  25.934  1.00 64.09           C  
ANISOU  372  CD2 LEU A 125     7595   8171   8587    983   1107   -481       C  
ATOM    373  N   LEU A 126      31.799  -7.400  27.592  1.00 69.29           N  
ANISOU  373  N   LEU A 126     8142   8861   9326   1575   1041   -456       N  
ATOM    374  CA  LEU A 126      31.433  -8.683  27.044  1.00 68.96           C  
ANISOU  374  CA  LEU A 126     8299   8673   9229   1677   1105   -441       C  
ATOM    375  C   LEU A 126      30.316  -9.299  27.858  1.00 66.72           C  
ANISOU  375  C   LEU A 126     8191   8280   8880   1688    998   -382       C  
ATOM    376  O   LEU A 126      29.304  -9.705  27.297  1.00 65.68           O  
ANISOU  376  O   LEU A 126     8267   8010   8680   1622   1027   -372       O  
ATOM    377  CB  LEU A 126      32.644  -9.604  26.988  1.00 72.39           C  
ANISOU  377  CB  LEU A 126     8642   9147   9718   1889   1170   -458       C  
ATOM    378  CG  LEU A 126      32.784 -10.378  25.677  1.00 76.50           C  
ANISOU  378  CG  LEU A 126     9294   9561  10211   1940   1331   -489       C  
ATOM    379  CD1 LEU A 126      32.515  -9.497  24.463  1.00 72.18           C  
ANISOU  379  CD1 LEU A 126     8780   9005   9639   1759   1435   -527       C  
ATOM    380  CD2 LEU A 126      34.162 -11.028  25.566  1.00 79.69           C  
ANISOU  380  CD2 LEU A 126     9553  10039  10687   2144   1410   -516       C  
ATOM    381  N   SER A 127      30.478  -9.321  29.178  1.00 66.28           N  
ANISOU  381  N   SER A 127     8049   8291   8842   1763    873   -347       N  
ATOM    382  CA  SER A 127      29.506  -9.982  30.045  1.00 65.82           C  
ANISOU  382  CA  SER A 127     8154   8130   8722   1791    781   -285       C  
ATOM    383  C   SER A 127      28.162  -9.275  30.092  1.00 62.29           C  
ANISOU  383  C   SER A 127     7817   7630   8223   1596    731   -268       C  
ATOM    384  O   SER A 127      27.133  -9.922  30.255  1.00 64.36           O  
ANISOU  384  O   SER A 127     8265   7763   8425   1577    711   -231       O  
ATOM    385  CB  SER A 127      30.056 -10.172  31.450  1.00 69.40           C  
ANISOU  385  CB  SER A 127     8496   8677   9198   1931    662   -250       C  
ATOM    386  OG  SER A 127      30.353  -8.917  32.001  1.00 71.02           O  
ANISOU  386  OG  SER A 127     8511   9033   9439   1837    582   -272       O  
ATOM    387  N   GLN A 128      28.174  -7.951  29.951  1.00 61.33           N  
ANISOU  387  N   GLN A 128     7575   7603   8124   1451    715   -296       N  
ATOM    388  CA  GLN A 128      26.948  -7.182  29.844  1.00 55.31           C  
ANISOU  388  CA  GLN A 128     6905   6796   7313   1271    680   -285       C  
ATOM    389  C   GLN A 128      26.277  -7.388  28.488  1.00 54.19           C  
ANISOU  389  C   GLN A 128     6924   6542   7124   1186    780   -305       C  
ATOM    390  O   GLN A 128      25.055  -7.423  28.389  1.00 51.83           O  
ANISOU  390  O   GLN A 128     6772   6155   6767   1092    752   -285       O  
ATOM    391  CB  GLN A 128      27.256  -5.713  30.003  1.00 56.05           C  
ANISOU  391  CB  GLN A 128     6834   7014   7447   1153    650   -312       C  
ATOM    392  CG  GLN A 128      27.249  -5.235  31.431  1.00 58.25           C  
ANISOU  392  CG  GLN A 128     7016   7377   7737   1160    517   -290       C  
ATOM    393  CD  GLN A 128      27.524  -3.753  31.489  1.00 57.81           C  
ANISOU  393  CD  GLN A 128     6815   7429   7722   1027    499   -326       C  
ATOM    394  OE1 GLN A 128      28.682  -3.321  31.481  1.00 58.81           O  
ANISOU  394  OE1 GLN A 128     6757   7670   7918   1049    520   -370       O  
ATOM    395  NE2 GLN A 128      26.461  -2.964  31.513  1.00 54.94           N  
ANISOU  395  NE2 GLN A 128     6532   7025   7319    885    468   -312       N  
ATOM    396  N   ALA A 129      27.091  -7.493  27.446  1.00 52.48           N  
ANISOU  396  N   ALA A 129     6670   6338   6930   1220    896   -348       N  
ATOM    397  CA  ALA A 129      26.605  -7.760  26.113  1.00 54.44           C  
ANISOU  397  CA  ALA A 129     7072   6488   7125   1159    996   -373       C  
ATOM    398  C   ALA A 129      25.943  -9.148  26.072  1.00 55.56           C  
ANISOU  398  C   ALA A 129     7414   6483   7215   1230   1001   -357       C  
ATOM    399  O   ALA A 129      24.785  -9.295  25.617  1.00 52.94           O  
ANISOU  399  O   ALA A 129     7246   6052   6816   1129    993   -356       O  
ATOM    400  CB  ALA A 129      27.756  -7.683  25.123  1.00 53.36           C  
ANISOU  400  CB  ALA A 129     6850   6401   7025   1206   1128   -422       C  
ATOM    401  N   ARG A 130      26.672 -10.143  26.579  1.00 54.29           N  
ANISOU  401  N   ARG A 130     7235   6307   7085   1403   1010   -345       N  
ATOM    402  CA  ARG A 130      26.217 -11.534  26.563  1.00 55.98           C  
ANISOU  402  CA  ARG A 130     7641   6370   7259   1488   1031   -330       C  
ATOM    403  C   ARG A 130      24.884 -11.649  27.233  1.00 53.02           C  
ANISOU  403  C   ARG A 130     7391   5916   6837   1396    939   -289       C  
ATOM    404  O   ARG A 130      24.002 -12.332  26.731  1.00 52.67           O  
ANISOU  404  O   ARG A 130     7533   5739   6740   1345    968   -298       O  
ATOM    405  CB  ARG A 130      27.199 -12.462  27.272  1.00 59.02           C  
ANISOU  405  CB  ARG A 130     7975   6762   7687   1703   1034   -308       C  
ATOM    406  CG  ARG A 130      28.523 -12.689  26.562  1.00 66.63           C  
ANISOU  406  CG  ARG A 130     8836   7782   8700   1830   1144   -351       C  
ATOM    407  CD  ARG A 130      29.202 -13.936  27.109  1.00 70.27           C  
ANISOU  407  CD  ARG A 130     9324   8195   9181   2057   1157   -326       C  
ATOM    408  NE  ARG A 130      30.643 -13.872  26.918  1.00 79.96           N  
ANISOU  408  NE  ARG A 130    10357   9543  10479   2198   1217   -356       N  
ATOM    409  CZ  ARG A 130      31.504 -13.317  27.777  1.00 85.19           C  
ANISOU  409  CZ  ARG A 130    10789  10373  11207   2267   1141   -346       C  
ATOM    410  NH1 ARG A 130      31.084 -12.759  28.914  1.00 84.32           N  
ANISOU  410  NH1 ARG A 130    10622  10323  11091   2213   1001   -304       N  
ATOM    411  NH2 ARG A 130      32.804 -13.327  27.500  1.00 87.91           N  
ANISOU  411  NH2 ARG A 130    10953  10828  11621   2393   1208   -382       N  
ATOM    412  N   ASP A 131      24.757 -10.972  28.375  1.00 53.55           N  
ANISOU  412  N   ASP A 131     7351   6070   6924   1373    831   -248       N  
ATOM    413  CA  ASP A 131      23.540 -10.970  29.159  1.00 51.79           C  
ANISOU  413  CA  ASP A 131     7221   5793   6662   1289    744   -204       C  
ATOM    414  C   ASP A 131      22.405 -10.358  28.396  1.00 49.68           C  
ANISOU  414  C   ASP A 131     7032   5492   6351   1105    746   -227       C  
ATOM    415  O   ASP A 131      21.277 -10.884  28.428  1.00 51.60           O  
ANISOU  415  O   ASP A 131     7426   5629   6551   1038    729   -215       O  
ATOM    416  CB  ASP A 131      23.714 -10.191  30.470  1.00 55.75           C  
ANISOU  416  CB  ASP A 131     7579   6413   7190   1297    633   -166       C  
ATOM    417  CG  ASP A 131      22.377  -9.964  31.186  1.00 58.21           C  
ANISOU  417  CG  ASP A 131     7976   6681   7459   1185    555   -126       C  
ATOM    418  OD1 ASP A 131      21.585  -9.069  30.791  1.00 55.42           O  
ANISOU  418  OD1 ASP A 131     7623   6346   7088   1031    539   -142       O  
ATOM    419  OD2 ASP A 131      22.088 -10.726  32.121  1.00 63.02           O  
ANISOU  419  OD2 ASP A 131     8663   7233   8051   1258    516    -76       O  
ATOM    420  N   PHE A 132      22.668  -9.219  27.761  1.00 45.24           N  
ANISOU  420  N   PHE A 132     6366   5023   5801   1020    764   -259       N  
ATOM    421  CA  PHE A 132      21.621  -8.590  26.967  1.00 44.67           C  
ANISOU  421  CA  PHE A 132     6370   4925   5679    860    763   -278       C  
ATOM    422  C   PHE A 132      21.175  -9.472  25.788  1.00 45.21           C  
ANISOU  422  C   PHE A 132     6612   4874   5694    842    841   -317       C  
ATOM    423  O   PHE A 132      19.980  -9.608  25.537  1.00 45.06           O  
ANISOU  423  O   PHE A 132     6711   4786   5623    740    811   -321       O  
ATOM    424  CB  PHE A 132      21.978  -7.192  26.459  1.00 42.43           C  
ANISOU  424  CB  PHE A 132     5964   4748   5409    775    778   -299       C  
ATOM    425  CG  PHE A 132      21.016  -6.695  25.438  1.00 40.85           C  
ANISOU  425  CG  PHE A 132     5863   4511   5146    642    793   -319       C  
ATOM    426  CD1 PHE A 132      19.717  -6.359  25.811  1.00 39.87           C  
ANISOU  426  CD1 PHE A 132     5796   4366   4987    541    709   -295       C  
ATOM    427  CD2 PHE A 132      21.364  -6.645  24.081  1.00 41.74           C  
ANISOU  427  CD2 PHE A 132     6022   4610   5226    627    892   -362       C  
ATOM    428  CE1 PHE A 132      18.799  -5.929  24.858  1.00 39.24           C  
ANISOU  428  CE1 PHE A 132     5805   4261   4844    431    712   -314       C  
ATOM    429  CE2 PHE A 132      20.441  -6.216  23.128  1.00 40.58           C  
ANISOU  429  CE2 PHE A 132     5979   4433   5007    515    895   -378       C  
ATOM    430  CZ  PHE A 132      19.153  -5.875  23.518  1.00 39.08           C  
ANISOU  430  CZ  PHE A 132     5836   4229   4785    421    800   -355       C  
ATOM    431  N   ILE A 133      22.123 -10.043  25.062  1.00 44.85           N  
ANISOU  431  N   ILE A 133     6576   4808   5657    938    939   -351       N  
ATOM    432  CA  ILE A 133      21.770 -10.931  23.941  1.00 48.26           C  
ANISOU  432  CA  ILE A 133     7184   5122   6032    929   1017   -397       C  
ATOM    433  C   ILE A 133      20.929 -12.125  24.421  1.00 49.67           C  
ANISOU  433  C   ILE A 133     7521   5164   6187    940    988   -383       C  
ATOM    434  O   ILE A 133      19.940 -12.490  23.764  1.00 49.84           O  
ANISOU  434  O   ILE A 133     7690   5098   6151    842    991   -415       O  
ATOM    435  CB  ILE A 133      23.020 -11.388  23.168  1.00 48.77           C  
ANISOU  435  CB  ILE A 133     7229   5188   6114   1050   1139   -437       C  
ATOM    436  CG1 ILE A 133      23.705 -10.174  22.519  1.00 50.00           C  
ANISOU  436  CG1 ILE A 133     7249   5466   6285   1004   1187   -457       C  
ATOM    437  CG2 ILE A 133      22.693 -12.462  22.147  1.00 49.40           C  
ANISOU  437  CG2 ILE A 133     7508   5130   6131   1059   1220   -487       C  
ATOM    438  CD1 ILE A 133      22.839  -9.393  21.530  1.00 48.81           C  
ANISOU  438  CD1 ILE A 133     7176   5312   6059    849   1189   -479       C  
ATOM    439  N   ASN A 134      21.302 -12.697  25.576  1.00 48.34           N  
ANISOU  439  N   ASN A 134     7323   4982   6063   1054    956   -335       N  
ATOM    440  CA  ASN A 134      20.492 -13.734  26.221  1.00 49.16           C  
ANISOU  440  CA  ASN A 134     7573   4957   6149   1058    929   -307       C  
ATOM    441  C   ASN A 134      19.065 -13.259  26.498  1.00 47.14           C  
ANISOU  441  C   ASN A 134     7355   4693   5862    890    848   -294       C  
ATOM    442  O   ASN A 134      18.111 -13.975  26.248  1.00 48.17           O  
ANISOU  442  O   ASN A 134     7637   4708   5958    815    856   -313       O  
ATOM    443  CB  ASN A 134      21.152 -14.220  27.510  1.00 51.40           C  
ANISOU  443  CB  ASN A 134     7805   5248   6476   1213    899   -245       C  
ATOM    444  CG  ASN A 134      22.474 -14.928  27.260  1.00 55.65           C  
ANISOU  444  CG  ASN A 134     8324   5776   7045   1401    981   -257       C  
ATOM    445  OD1 ASN A 134      22.798 -15.273  26.125  1.00 56.75           O  
ANISOU  445  OD1 ASN A 134     8525   5869   7170   1415   1075   -314       O  
ATOM    446  ND2 ASN A 134      23.250 -15.151  28.328  1.00 53.93           N  
ANISOU  446  ND2 ASN A 134     8020   5606   6866   1554    944   -205       N  
ATOM    447  N   GLN A 135      18.922 -12.040  26.999  1.00 47.85           N  
ANISOU  447  N   GLN A 135     7306   4907   5968    827    774   -267       N  
ATOM    448  CA  GLN A 135      17.601 -11.445  27.208  1.00 47.17           C  
ANISOU  448  CA  GLN A 135     7236   4832   5855    674    700   -257       C  
ATOM    449  C   GLN A 135      16.787 -11.398  25.917  1.00 46.83           C  
ANISOU  449  C   GLN A 135     7290   4746   5756    552    723   -316       C  
ATOM    450  O   GLN A 135      15.604 -11.763  25.908  1.00 52.34           O  
ANISOU  450  O   GLN A 135     8084   5377   6426    452    693   -325       O  
ATOM    451  CB  GLN A 135      17.737 -10.051  27.797  1.00 46.06           C  
ANISOU  451  CB  GLN A 135     6930   4833   5739    639    632   -227       C  
ATOM    452  CG  GLN A 135      18.012 -10.049  29.280  1.00 46.12           C  
ANISOU  452  CG  GLN A 135     6864   4877   5780    716    572   -168       C  
ATOM    453  CD  GLN A 135      17.943  -8.657  29.887  1.00 46.02           C  
ANISOU  453  CD  GLN A 135     6710   4993   5785    658    499   -148       C  
ATOM    454  OE1 GLN A 135      16.940  -7.954  29.765  1.00 47.29           O  
ANISOU  454  OE1 GLN A 135     6878   5169   5922    535    460   -149       O  
ATOM    455  NE2 GLN A 135      19.011  -8.258  30.558  1.00 45.83           N  
ANISOU  455  NE2 GLN A 135     6553   5059   5799    749    478   -133       N  
ATOM    456  N   TYR A 136      17.429 -10.983  24.828  1.00 45.78           N  
ANISOU  456  N   TYR A 136     7133   4655   5606    560    780   -359       N  
ATOM    457  CA  TYR A 136      16.765 -10.842  23.541  1.00 44.97           C  
ANISOU  457  CA  TYR A 136     7122   4529   5436    457    798   -415       C  
ATOM    458  C   TYR A 136      16.269 -12.179  23.005  1.00 45.67           C  
ANISOU  458  C   TYR A 136     7391   4475   5486    445    839   -463       C  
ATOM    459  O   TYR A 136      15.097 -12.318  22.681  1.00 46.54           O  
ANISOU  459  O   TYR A 136     7584   4545   5554    327    797   -492       O  
ATOM    460  CB  TYR A 136      17.674 -10.176  22.502  1.00 45.79           C  
ANISOU  460  CB  TYR A 136     7175   4700   5522    483    868   -446       C  
ATOM    461  CG  TYR A 136      17.025 -10.099  21.127  1.00 45.57           C  
ANISOU  461  CG  TYR A 136     7263   4645   5407    392    888   -504       C  
ATOM    462  CD1 TYR A 136      15.974  -9.216  20.891  1.00 45.13           C  
ANISOU  462  CD1 TYR A 136     7201   4640   5307    270    811   -501       C  
ATOM    463  CD2 TYR A 136      17.440 -10.938  20.080  1.00 45.96           C  
ANISOU  463  CD2 TYR A 136     7433   4618   5410    435    981   -564       C  
ATOM    464  CE1 TYR A 136      15.358  -9.138  19.656  1.00 45.51           C  
ANISOU  464  CE1 TYR A 136     7354   4673   5265    195    815   -552       C  
ATOM    465  CE2 TYR A 136      16.822 -10.877  18.840  1.00 47.57           C  
ANISOU  465  CE2 TYR A 136     7751   4802   5521    352    990   -621       C  
ATOM    466  CZ  TYR A 136      15.786  -9.967  18.639  1.00 48.17           C  
ANISOU  466  CZ  TYR A 136     7813   4939   5551    234    902   -614       C  
ATOM    467  OH  TYR A 136      15.145  -9.887  17.426  1.00 52.20           O  
ANISOU  467  OH  TYR A 136     8434   5441   5959    160    896   -669       O  
ATOM    468  N   TYR A 137      17.152 -13.158  22.920  1.00 46.17           N  
ANISOU  468  N   TYR A 137     7513   4463   5567    567    922   -476       N  
ATOM    469  CA  TYR A 137      16.747 -14.465  22.417  1.00 52.93           C  
ANISOU  469  CA  TYR A 137     8555   5167   6388    560    972   -527       C  
ATOM    470  C   TYR A 137      15.621 -15.128  23.241  1.00 57.72           C  
ANISOU  470  C   TYR A 137     9244   5682   7005    485    918   -506       C  
ATOM    471  O   TYR A 137      14.800 -15.848  22.689  1.00 57.71           O  
ANISOU  471  O   TYR A 137     9384   5578   6963    395    928   -562       O  
ATOM    472  CB  TYR A 137      17.965 -15.371  22.168  1.00 52.77           C  
ANISOU  472  CB  TYR A 137     8586   5078   6387    723   1080   -543       C  
ATOM    473  CG  TYR A 137      18.603 -15.011  20.840  1.00 53.58           C  
ANISOU  473  CG  TYR A 137     8689   5222   6445    736   1157   -602       C  
ATOM    474  CD1 TYR A 137      19.581 -14.013  20.764  1.00 53.07           C  
ANISOU  474  CD1 TYR A 137     8460   5293   6410    792   1178   -580       C  
ATOM    475  CD2 TYR A 137      18.171 -15.608  19.642  1.00 53.05           C  
ANISOU  475  CD2 TYR A 137     8791   5064   6301    679   1207   -684       C  
ATOM    476  CE1 TYR A 137      20.134 -13.645  19.548  1.00 52.58           C  
ANISOU  476  CE1 TYR A 137     8405   5268   6305    796   1260   -629       C  
ATOM    477  CE2 TYR A 137      18.711 -15.249  18.423  1.00 51.73           C  
ANISOU  477  CE2 TYR A 137     8637   4937   6080    689   1280   -735       C  
ATOM    478  CZ  TYR A 137      19.702 -14.261  18.378  1.00 54.55           C  
ANISOU  478  CZ  TYR A 137     8832   5426   6470    750   1312   -704       C  
ATOM    479  OH  TYR A 137      20.269 -13.879  17.165  1.00 54.38           O  
ANISOU  479  OH  TYR A 137     8827   5443   6393    759   1401   -749       O  
ATOM    480  N   SER A 138      15.562 -14.839  24.543  1.00 60.26           N  
ANISOU  480  N   SER A 138     9474   6047   7377    511    861   -431       N  
ATOM    481  CA  SER A 138      14.491 -15.336  25.389  1.00 61.54           C  
ANISOU  481  CA  SER A 138     9700   6136   7549    434    818   -403       C  
ATOM    482  C   SER A 138      13.177 -14.674  25.025  1.00 60.38           C  
ANISOU  482  C   SER A 138     9537   6037   7369    256    746   -432       C  
ATOM    483  O   SER A 138      12.148 -15.337  24.930  1.00 62.51           O  
ANISOU  483  O   SER A 138     9910   6216   7623    150    739   -465       O  
ATOM    484  CB  SER A 138      14.800 -15.056  26.858  1.00 65.67           C  
ANISOU  484  CB  SER A 138    10123   6710   8120    512    775   -313       C  
ATOM    485  OG  SER A 138      15.936 -15.806  27.255  1.00 78.63           O  
ANISOU  485  OG  SER A 138    11788   8301   9788    687    832   -284       O  
ATOM    486  N   SER A 139      13.207 -13.365  24.832  1.00 53.42           N  
ANISOU  486  N   SER A 139     8521   5296   6479    224    693   -422       N  
ATOM    487  CA  SER A 139      11.989 -12.649  24.516  1.00 54.77           C  
ANISOU  487  CA  SER A 139     8665   5525   6619     76    619   -442       C  
ATOM    488  C   SER A 139      11.434 -13.090  23.152  1.00 55.76           C  
ANISOU  488  C   SER A 139     8910   5598   6678    -10    635   -532       C  
ATOM    489  O   SER A 139      10.261 -12.858  22.853  1.00 56.90           O  
ANISOU  489  O   SER A 139     9062   5764   6792   -137    572   -563       O  
ATOM    490  CB  SER A 139      12.237 -11.146  24.503  1.00 51.43           C  
ANISOU  490  CB  SER A 139     8093   5251   6196     76    571   -413       C  
ATOM    491  OG  SER A 139      12.788 -10.769  23.244  1.00 53.72           O  
ANISOU  491  OG  SER A 139     8398   5575   6440     89    611   -459       O  
ATOM    492  N   ILE A 140      12.274 -13.689  22.317  1.00 55.59           N  
ANISOU  492  N   ILE A 140     8975   5517   6631     63    716   -577       N  
ATOM    493  CA  ILE A 140      11.766 -14.298  21.078  1.00 60.73           C  
ANISOU  493  CA  ILE A 140     9765   6098   7210    -14    737   -670       C  
ATOM    494  C   ILE A 140      11.764 -15.831  21.124  1.00 63.85           C  
ANISOU  494  C   ILE A 140    10323   6321   7615      2    806   -710       C  
ATOM    495  O   ILE A 140      11.518 -16.473  20.113  1.00 70.30           O  
ANISOU  495  O   ILE A 140    11272   7062   8374    -47    837   -796       O  
ATOM    496  CB  ILE A 140      12.456 -13.760  19.788  1.00 59.38           C  
ANISOU  496  CB  ILE A 140     9603   5985   6974     22    778   -714       C  
ATOM    497  CG1 ILE A 140      13.929 -14.182  19.708  1.00 56.92           C  
ANISOU  497  CG1 ILE A 140     9302   5637   6688    179    887   -704       C  
ATOM    498  CG2 ILE A 140      12.262 -12.249  19.684  1.00 57.63           C  
ANISOU  498  CG2 ILE A 140     9246   5915   6735    -16    710   -677       C  
ATOM    499  CD1 ILE A 140      14.528 -14.069  18.324  1.00 56.09           C  
ANISOU  499  CD1 ILE A 140     9259   5543   6509    208    958   -766       C  
ATOM    500  N   LYS A 141      12.037 -16.392  22.306  1.00 66.66           N  
ANISOU  500  N   LYS A 141    10677   6612   8037     73    829   -646       N  
ATOM    501  CA  LYS A 141      11.969 -17.846  22.596  1.00 68.46           C  
ANISOU  501  CA  LYS A 141    11068   6661   8285     92    897   -664       C  
ATOM    502  C   LYS A 141      12.882 -18.731  21.734  1.00 74.35           C  
ANISOU  502  C   LYS A 141    11947   7300   9002    194   1003   -721       C  
ATOM    503  O   LYS A 141      12.468 -19.794  21.251  1.00 73.31           O  
ANISOU  503  O   LYS A 141    11987   7023   8846    139   1050   -791       O  
ATOM    504  CB  LYS A 141      10.519 -18.356  22.571  1.00 68.00           C  
ANISOU  504  CB  LYS A 141    11093   6529   8215    -88    858   -713       C  
ATOM    505  CG  LYS A 141       9.566 -17.537  23.420  1.00 68.23           C  
ANISOU  505  CG  LYS A 141    10990   6660   8273   -186    765   -660       C  
ATOM    506  CD  LYS A 141       9.851 -17.703  24.908  1.00 71.71           C  
ANISOU  506  CD  LYS A 141    11392   7075   8778   -102    778   -557       C  
ATOM    507  CE  LYS A 141       9.222 -16.577  25.720  1.00 71.87           C  
ANISOU  507  CE  LYS A 141    11251   7235   8821   -158    689   -497       C  
ATOM    508  NZ  LYS A 141       7.942 -16.131  25.101  1.00 73.65           N  
ANISOU  508  NZ  LYS A 141    11446   7519   9019   -331    619   -558       N  
ATOM    509  N   ARG A 142      14.125 -18.279  21.562  1.00 73.47           N  
ANISOU  509  N   ARG A 142    11755   7263   8899    339   1044   -695       N  
ATOM    510  CA  ARG A 142      15.153 -18.996  20.812  1.00 73.47           C  
ANISOU  510  CA  ARG A 142    11852   7184   8879    464   1154   -740       C  
ATOM    511  C   ARG A 142      16.364 -19.160  21.728  1.00 71.17           C  
ANISOU  511  C   ARG A 142    11484   6901   8655    658   1198   -660       C  
ATOM    512  O   ARG A 142      17.521 -19.206  21.287  1.00 67.59           O  
ANISOU  512  O   ARG A 142    11006   6469   8205    796   1273   -670       O  
ATOM    513  CB  ARG A 142      15.532 -18.228  19.529  1.00 75.74           C  
ANISOU  513  CB  ARG A 142    12103   7571   9103    451   1171   -796       C  
ATOM    514  CG  ARG A 142      14.391 -17.997  18.537  1.00 77.37           C  
ANISOU  514  CG  ARG A 142    12381   7788   9227    276   1116   -877       C  
ATOM    515  CD  ARG A 142      14.068 -19.250  17.727  1.00 84.91           C  
ANISOU  515  CD  ARG A 142    13554   8580  10129    236   1177   -977       C  
ATOM    516  NE  ARG A 142      12.820 -19.103  16.974  1.00 86.56           N  
ANISOU  516  NE  ARG A 142    13822   8803  10265     55   1100  -1056       N  
ATOM    517  CZ  ARG A 142      11.599 -19.357  17.448  1.00 84.76           C  
ANISOU  517  CZ  ARG A 142    13611   8540  10054    -88   1024  -1067       C  
ATOM    518  NH1 ARG A 142      11.417 -19.791  18.693  1.00 84.12           N  
ANISOU  518  NH1 ARG A 142    13510   8395  10056    -77   1023  -1000       N  
ATOM    519  NH2 ARG A 142      10.547 -19.175  16.667  1.00 82.39           N  
ANISOU  519  NH2 ARG A 142    13346   8274   9683   -242    949  -1146       N  
ATOM    520  N   SER A 143      16.085 -19.225  23.022  1.00 70.62           N  
ANISOU  520  N   SER A 143    11371   6825   8636    671   1148   -581       N  
ATOM    521  CA  SER A 143      17.139 -19.317  24.010  1.00 74.17           C  
ANISOU  521  CA  SER A 143    11740   7301   9142    853   1164   -500       C  
ATOM    522  C   SER A 143      17.859 -20.673  23.871  1.00 79.43           C  
ANISOU  522  C   SER A 143    12562   7805   9813   1004   1274   -515       C  
ATOM    523  O   SER A 143      17.218 -21.729  23.912  1.00 82.98           O  
ANISOU  523  O   SER A 143    13196   8083  10250    960   1311   -536       O  
ATOM    524  CB  SER A 143      16.541 -19.126  25.399  1.00 73.62           C  
ANISOU  524  CB  SER A 143    11616   7251   9106    821   1085   -417       C  
ATOM    525  OG  SER A 143      17.560 -19.013  26.361  1.00 77.34           O  
ANISOU  525  OG  SER A 143    11983   7782   9621    994   1078   -340       O  
ATOM    526  N   GLY A 144      19.178 -20.634  23.662  1.00 78.61           N  
ANISOU  526  N   GLY A 144    12385   7753   9730   1179   1332   -509       N  
ATOM    527  CA  GLY A 144      19.998 -21.846  23.509  1.00 75.71           C  
ANISOU  527  CA  GLY A 144    12148   7247   9371   1355   1441   -521       C  
ATOM    528  C   GLY A 144      20.169 -22.323  22.073  1.00 75.09           C  
ANISOU  528  C   GLY A 144    12200   7089   9243   1343   1541   -625       C  
ATOM    529  O   GLY A 144      20.990 -23.207  21.800  1.00 70.53           O  
ANISOU  529  O   GLY A 144    11715   6413   8671   1503   1644   -643       O  
ATOM    530  N   SER A 145      19.394 -21.729  21.161  1.00 74.12           N  
ANISOU  530  N   SER A 145    12086   7011   9065   1161   1510   -692       N  
ATOM    531  CA  SER A 145      19.416 -22.062  19.729  1.00 73.74           C  
ANISOU  531  CA  SER A 145    12168   6902   8948   1123   1591   -799       C  
ATOM    532  C   SER A 145      20.738 -21.724  19.032  1.00 74.28           C  
ANISOU  532  C   SER A 145    12146   7059   9017   1269   1679   -817       C  
ATOM    533  O   SER A 145      21.626 -21.090  19.590  1.00 72.84           O  
ANISOU  533  O   SER A 145    11775   7008   8893   1381   1668   -754       O  
ATOM    534  CB  SER A 145      18.288 -21.339  18.995  1.00 71.50           C  
ANISOU  534  CB  SER A 145    11888   6679   8599    904   1516   -856       C  
ATOM    535  OG  SER A 145      18.628 -19.967  18.782  1.00 73.87           O  
ANISOU  535  OG  SER A 145    11996   7175   8898    887   1471   -831       O  
ATOM    536  N   GLN A 146      20.838 -22.138  17.782  1.00 78.59           N  
ANISOU  536  N   GLN A 146    12828   7536   9496   1258   1768   -911       N  
ATOM    537  CA  GLN A 146      22.048 -21.955  17.021  1.00 79.43           C  
ANISOU  537  CA  GLN A 146    12878   7706   9596   1393   1876   -939       C  
ATOM    538  C   GLN A 146      22.196 -20.490  16.572  1.00 75.92           C  
ANISOU  538  C   GLN A 146    12251   7461   9134   1314   1836   -930       C  
ATOM    539  O   GLN A 146      23.312 -19.984  16.476  1.00 77.40           O  
ANISOU  539  O   GLN A 146    12290   7758   9359   1429   1896   -909       O  
ATOM    540  CB  GLN A 146      22.048 -22.919  15.841  1.00 84.20           C  
ANISOU  540  CB  GLN A 146    13710   8159  10123   1404   1990  -1045       C  
ATOM    541  CG  GLN A 146      23.415 -23.173  15.236  1.00 90.87           C  
ANISOU  541  CG  GLN A 146    14537   9015  10976   1597   2136  -1070       C  
ATOM    542  CD  GLN A 146      23.420 -22.855  13.755  1.00 96.83           C  
ANISOU  542  CD  GLN A 146    15366   9796  11627   1526   2206  -1165       C  
ATOM    543  OE1 GLN A 146      23.752 -23.697  12.921  1.00 95.31           O  
ANISOU  543  OE1 GLN A 146    15344   9485  11382   1597   2326  -1244       O  
ATOM    544  NE2 GLN A 146      23.023 -21.628  13.419  1.00 98.09           N  
ANISOU  544  NE2 GLN A 146    15413  10108  11751   1389   2132  -1156       N  
ATOM    545  N   ALA A 147      21.075 -19.814  16.318  1.00 68.19           N  
ANISOU  545  N   ALA A 147    11281   6527   8102   1121   1738   -945       N  
ATOM    546  CA  ALA A 147      21.090 -18.404  15.991  1.00 64.31           C  
ANISOU  546  CA  ALA A 147    10634   6209   7592   1042   1693   -927       C  
ATOM    547  C   ALA A 147      21.489 -17.569  17.229  1.00 63.59           C  
ANISOU  547  C   ALA A 147    10315   6247   7598   1084   1620   -827       C  
ATOM    548  O   ALA A 147      22.186 -16.552  17.106  1.00 62.75           O  
ANISOU  548  O   ALA A 147    10046   6283   7515   1105   1635   -803       O  
ATOM    549  CB  ALA A 147      19.738 -17.976  15.444  1.00 64.21           C  
ANISOU  549  CB  ALA A 147    10700   6203   7495    842   1600   -966       C  
ATOM    550  N   HIS A 148      21.063 -18.022  18.408  1.00 61.82           N  
ANISOU  550  N   HIS A 148    10090   5970   7428   1094   1548   -774       N  
ATOM    551  CA  HIS A 148      21.518 -17.472  19.691  1.00 61.72           C  
ANISOU  551  CA  HIS A 148     9888   6059   7503   1161   1483   -684       C  
ATOM    552  C   HIS A 148      23.026 -17.559  19.899  1.00 65.13           C  
ANISOU  552  C   HIS A 148    10196   6550   7999   1357   1563   -662       C  
ATOM    553  O   HIS A 148      23.662 -16.537  20.195  1.00 61.76           O  
ANISOU  553  O   HIS A 148     9569   6279   7619   1375   1540   -628       O  
ATOM    554  CB  HIS A 148      20.776 -18.137  20.842  1.00 58.81           C  
ANISOU  554  CB  HIS A 148     9584   5599   7163   1148   1410   -635       C  
ATOM    555  CG  HIS A 148      21.077 -17.541  22.199  1.00 60.73           C  
ANISOU  555  CG  HIS A 148     9649   5947   7477   1202   1328   -545       C  
ATOM    556  ND1 HIS A 148      20.644 -18.106  23.355  1.00 62.06           N  
ANISOU  556  ND1 HIS A 148     9860   6047   7673   1225   1274   -487       N  
ATOM    557  CD2 HIS A 148      21.784 -16.392  22.567  1.00 59.63           C  
ANISOU  557  CD2 HIS A 148     9293   5982   7383   1231   1291   -507       C  
ATOM    558  CE1 HIS A 148      21.047 -17.355  24.399  1.00 60.24           C  
ANISOU  558  CE1 HIS A 148     9450   5944   7493   1273   1201   -417       C  
ATOM    559  NE2 HIS A 148      21.740 -16.302  23.916  1.00 57.41           N  
ANISOU  559  NE2 HIS A 148     8931   5735   7149   1272   1209   -434       N  
ATOM    560  N   GLU A 149      23.610 -18.758  19.749  1.00 66.00           N  
ANISOU  560  N   GLU A 149    10420   6540   8116   1505   1658   -685       N  
ATOM    561  CA  GLU A 149      25.053 -18.966  19.984  1.00 71.30           C  
ANISOU  561  CA  GLU A 149    10971   7266   8854   1714   1735   -665       C  
ATOM    562  C   GLU A 149      25.926 -18.318  18.897  1.00 72.23           C  
ANISOU  562  C   GLU A 149    10993   7488   8962   1733   1836   -715       C  
ATOM    563  O   GLU A 149      27.071 -17.948  19.156  1.00 73.18           O  
ANISOU  563  O   GLU A 149    10927   7727   9151   1855   1872   -693       O  
ATOM    564  CB  GLU A 149      25.410 -20.463  20.157  1.00 79.00           C  
ANISOU  564  CB  GLU A 149    12105   8072   9838   1884   1812   -670       C  
ATOM    565  CG  GLU A 149      24.712 -21.207  21.317  1.00 89.84           C  
ANISOU  565  CG  GLU A 149    13580   9329  11226   1895   1736   -610       C  
ATOM    566  CD  GLU A 149      25.265 -20.915  22.730  1.00 96.46           C  
ANISOU  566  CD  GLU A 149    14241  10271  12138   2014   1652   -514       C  
ATOM    567  OE1 GLU A 149      26.508 -20.841  22.903  1.00102.17           O  
ANISOU  567  OE1 GLU A 149    14816  11089  12914   2191   1689   -498       O  
ATOM    568  OE2 GLU A 149      24.455 -20.784  23.690  1.00 91.14           O  
ANISOU  568  OE2 GLU A 149    13577   9587  11467   1934   1548   -457       O  
ATOM    569  N   GLU A 150      25.381 -18.176  17.688  1.00 71.89           N  
ANISOU  569  N   GLU A 150    11077   7406   8831   1611   1881   -783       N  
ATOM    570  CA  GLU A 150      26.064 -17.446  16.620  1.00 71.27           C  
ANISOU  570  CA  GLU A 150    10926   7427   8727   1602   1978   -824       C  
ATOM    571  C   GLU A 150      26.077 -15.957  16.915  1.00 68.06           C  
ANISOU  571  C   GLU A 150    10316   7192   8350   1498   1905   -780       C  
ATOM    572  O   GLU A 150      27.106 -15.300  16.762  1.00 67.17           O  
ANISOU  572  O   GLU A 150    10035   7202   8287   1554   1971   -775       O  
ATOM    573  CB  GLU A 150      25.430 -17.717  15.262  1.00 72.68           C  
ANISOU  573  CB  GLU A 150    11316   7513   8786   1503   2039   -907       C  
ATOM    574  CG  GLU A 150      25.918 -19.025  14.669  1.00 86.32           C  
ANISOU  574  CG  GLU A 150    13212   9097  10488   1639   2170   -969       C  
ATOM    575  CD  GLU A 150      25.373 -19.310  13.279  1.00 93.10           C  
ANISOU  575  CD  GLU A 150    14286   9870  11219   1548   2235  -1062       C  
ATOM    576  OE1 GLU A 150      25.066 -18.345  12.538  1.00 99.53           O  
ANISOU  576  OE1 GLU A 150    15078  10774  11965   1424   2223  -1079       O  
ATOM    577  OE2 GLU A 150      25.267 -20.508  12.923  1.00 93.16           O  
ANISOU  577  OE2 GLU A 150    14493   9716  11188   1605   2301  -1121       O  
ATOM    578  N   ARG A 151      24.940 -15.426  17.348  1.00 61.79           N  
ANISOU  578  N   ARG A 151     9538   6407   7533   1347   1775   -751       N  
ATOM    579  CA  ARG A 151      24.893 -14.017  17.718  1.00 61.57           C  
ANISOU  579  CA  ARG A 151     9331   6528   7534   1252   1701   -707       C  
ATOM    580  C   ARG A 151      25.889 -13.668  18.827  1.00 61.52           C  
ANISOU  580  C   ARG A 151     9100   6633   7642   1360   1677   -653       C  
ATOM    581  O   ARG A 151      26.490 -12.593  18.799  1.00 58.86           O  
ANISOU  581  O   ARG A 151     8591   6429   7343   1332   1690   -642       O  
ATOM    582  CB  ARG A 151      23.491 -13.607  18.127  1.00 55.76           C  
ANISOU  582  CB  ARG A 151     8648   5776   6760   1093   1563   -682       C  
ATOM    583  CG  ARG A 151      23.355 -12.121  18.416  1.00 56.15           C  
ANISOU  583  CG  ARG A 151     8539   5966   6830    991   1493   -642       C  
ATOM    584  CD  ARG A 151      23.649 -11.246  17.208  1.00 55.46           C  
ANISOU  584  CD  ARG A 151     8442   5941   6688    930   1575   -674       C  
ATOM    585  NE  ARG A 151      23.488  -9.846  17.577  1.00 53.42           N  
ANISOU  585  NE  ARG A 151     8046   5798   6454    834   1509   -630       N  
ATOM    586  CZ  ARG A 151      24.361  -8.880  17.318  1.00 51.68           C  
ANISOU  586  CZ  ARG A 151     7689   5681   6267    832   1576   -623       C  
ATOM    587  NH1 ARG A 151      25.465  -9.153  16.630  1.00 49.59           N  
ANISOU  587  NH1 ARG A 151     7399   5428   6014    921   1718   -657       N  
ATOM    588  NH2 ARG A 151      24.100  -7.637  17.729  1.00 46.37           N  
ANISOU  588  NH2 ARG A 151     6911   5093   5616    737   1509   -584       N  
ATOM    589  N   LEU A 152      26.057 -14.587  19.783  1.00 61.86           N  
ANISOU  589  N   LEU A 152     9152   6618   7732   1482   1642   -622       N  
ATOM    590  CA  LEU A 152      26.985 -14.409  20.897  1.00 61.79           C  
ANISOU  590  CA  LEU A 152     8943   6713   7821   1605   1604   -573       C  
ATOM    591  C   LEU A 152      28.399 -14.329  20.384  1.00 63.70           C  
ANISOU  591  C   LEU A 152     9049   7040   8114   1729   1726   -604       C  
ATOM    592  O   LEU A 152      29.155 -13.434  20.768  1.00 62.38           O  
ANISOU  592  O   LEU A 152     8662   7023   8014   1736   1711   -589       O  
ATOM    593  CB  LEU A 152      26.868 -15.563  21.890  1.00 61.03           C  
ANISOU  593  CB  LEU A 152     8926   6517   7746   1731   1557   -534       C  
ATOM    594  CG  LEU A 152      25.652 -15.442  22.804  1.00 60.39           C  
ANISOU  594  CG  LEU A 152     8904   6397   7645   1618   1423   -485       C  
ATOM    595  CD1 LEU A 152      25.280 -16.796  23.388  1.00 62.34           C  
ANISOU  595  CD1 LEU A 152     9321   6485   7881   1710   1416   -460       C  
ATOM    596  CD2 LEU A 152      25.886 -14.417  23.903  1.00 57.77           C  
ANISOU  596  CD2 LEU A 152     8363   6218   7370   1602   1315   -431       C  
ATOM    597  N   GLN A 153      28.722 -15.271  19.497  1.00 67.98           N  
ANISOU  597  N   GLN A 153     9727   7481   8621   1820   1850   -653       N  
ATOM    598  CA  GLN A 153      30.035 -15.412  18.866  1.00 70.06           C  
ANISOU  598  CA  GLN A 153     9893   7802   8925   1955   1994   -691       C  
ATOM    599  C   GLN A 153      30.381 -14.194  18.035  1.00 67.45           C  
ANISOU  599  C   GLN A 153     9448   7592   8589   1840   2061   -719       C  
ATOM    600  O   GLN A 153      31.529 -13.758  17.983  1.00 66.23           O  
ANISOU  600  O   GLN A 153     9097   7561   8507   1910   2134   -728       O  
ATOM    601  CB  GLN A 153      30.043 -16.633  17.945  1.00 74.76           C  
ANISOU  601  CB  GLN A 153    10707   8240   9459   2043   2117   -746       C  
ATOM    602  CG  GLN A 153      30.209 -17.981  18.620  1.00 79.21           C  
ANISOU  602  CG  GLN A 153    11365   8684  10048   2223   2113   -726       C  
ATOM    603  CD  GLN A 153      30.409 -19.097  17.597  1.00 86.04           C  
ANISOU  603  CD  GLN A 153    12434   9400  10859   2319   2261   -792       C  
ATOM    604  OE1 GLN A 153      30.507 -20.273  17.951  1.00 87.25           O  
ANISOU  604  OE1 GLN A 153    12707   9424  11019   2465   2283   -785       O  
ATOM    605  NE2 GLN A 153      30.476 -18.729  16.317  1.00 86.26           N  
ANISOU  605  NE2 GLN A 153    12511   9439  10824   2241   2369   -856       N  
ATOM    606  N   GLU A 154      29.361 -13.673  17.368  1.00 67.67           N  
ANISOU  606  N   GLU A 154     9606   7578   8526   1664   2038   -732       N  
ATOM    607  CA  GLU A 154      29.453 -12.470  16.561  1.00 68.24           C  
ANISOU  607  CA  GLU A 154     9616   7741   8570   1535   2091   -748       C  
ATOM    608  C   GLU A 154      29.807 -11.251  17.436  1.00 66.77           C  
ANISOU  608  C   GLU A 154     9188   7709   8472   1476   2013   -703       C  
ATOM    609  O   GLU A 154      30.728 -10.483  17.125  1.00 64.80           O  
ANISOU  609  O   GLU A 154     8777   7572   8272   1470   2099   -715       O  
ATOM    610  CB  GLU A 154      28.099 -12.249  15.899  1.00 68.90           C  
ANISOU  610  CB  GLU A 154     9901   7743   8534   1372   2041   -760       C  
ATOM    611  CG  GLU A 154      28.142 -12.101  14.403  1.00 74.04           C  
ANISOU  611  CG  GLU A 154    10677   8368   9086   1325   2171   -815       C  
ATOM    612  CD  GLU A 154      27.208 -11.006  13.961  1.00 74.35           C  
ANISOU  612  CD  GLU A 154    10766   8438   9047   1145   2108   -801       C  
ATOM    613  OE1 GLU A 154      25.982 -11.174  14.146  1.00 71.20           O  
ANISOU  613  OE1 GLU A 154    10491   7972   8589   1059   1988   -794       O  
ATOM    614  OE2 GLU A 154      27.720  -9.971  13.458  1.00 76.78           O  
ANISOU  614  OE2 GLU A 154    10981   8837   9354   1094   2182   -795       O  
ATOM    615  N   VAL A 155      29.063 -11.096  18.534  1.00 64.16           N  
ANISOU  615  N   VAL A 155     8841   7378   8159   1428   1855   -655       N  
ATOM    616  CA  VAL A 155      29.257  -9.996  19.473  1.00 61.78           C  
ANISOU  616  CA  VAL A 155     8335   7206   7931   1368   1762   -616       C  
ATOM    617  C   VAL A 155      30.685 -10.032  20.068  1.00 65.88           C  
ANISOU  617  C   VAL A 155     8621   7844   8565   1509   1798   -619       C  
ATOM    618  O   VAL A 155      31.368  -9.006  20.078  1.00 63.64           O  
ANISOU  618  O   VAL A 155     8152   7688   8342   1455   1826   -626       O  
ATOM    619  CB  VAL A 155      28.148  -9.985  20.553  1.00 58.11           C  
ANISOU  619  CB  VAL A 155     7921   6706   7453   1307   1593   -566       C  
ATOM    620  CG1 VAL A 155      28.520  -9.113  21.736  1.00 58.90           C  
ANISOU  620  CG1 VAL A 155     7808   6936   7636   1292   1494   -530       C  
ATOM    621  CG2 VAL A 155      26.819  -9.521  19.966  1.00 56.80           C  
ANISOU  621  CG2 VAL A 155     7914   6476   7191   1139   1551   -566       C  
ATOM    622  N   GLU A 156      31.153 -11.206  20.518  1.00 69.55           N  
ANISOU  622  N   GLU A 156     9097   8269   9062   1689   1802   -616       N  
ATOM    623  CA  GLU A 156      32.507 -11.292  21.115  1.00 72.60           C  
ANISOU  623  CA  GLU A 156     9251   8779   9556   1842   1822   -619       C  
ATOM    624  C   GLU A 156      33.645 -11.136  20.135  1.00 70.97           C  
ANISOU  624  C   GLU A 156     8935   8641   9387   1891   1995   -672       C  
ATOM    625  O   GLU A 156      34.685 -10.602  20.496  1.00 71.67           O  
ANISOU  625  O   GLU A 156     8779   8880   9573   1930   2010   -684       O  
ATOM    626  CB  GLU A 156      32.729 -12.515  22.018  1.00 77.93           C  
ANISOU  626  CB  GLU A 156     9951   9404  10256   2041   1764   -590       C  
ATOM    627  CG  GLU A 156      32.246 -13.849  21.494  1.00 84.41           C  
ANISOU  627  CG  GLU A 156    11027  10039  11005   2126   1825   -599       C  
ATOM    628  CD  GLU A 156      31.911 -14.827  22.620  1.00 92.16           C  
ANISOU  628  CD  GLU A 156    12090  10939  11987   2250   1720   -545       C  
ATOM    629  OE1 GLU A 156      31.735 -14.388  23.790  1.00 88.43           O  
ANISOU  629  OE1 GLU A 156    11514  10539  11544   2231   1581   -496       O  
ATOM    630  OE2 GLU A 156      31.819 -16.046  22.326  1.00 96.49           O  
ANISOU  630  OE2 GLU A 156    12820  11341  12501   2365   1783   -553       O  
ATOM    631  N   ALA A 157      33.441 -11.568  18.897  1.00 70.74           N  
ANISOU  631  N   ALA A 157     9086   8510   9283   1880   2125   -709       N  
ATOM    632  CA  ALA A 157      34.437 -11.349  17.856  1.00 74.94           C  
ANISOU  632  CA  ALA A 157     9536   9101   9836   1908   2307   -760       C  
ATOM    633  C   ALA A 157      34.547  -9.850  17.563  1.00 72.49           C  
ANISOU  633  C   ALA A 157     9096   8901   9544   1726   2331   -762       C  
ATOM    634  O   ALA A 157      35.648  -9.307  17.461  1.00 70.84           O  
ANISOU  634  O   ALA A 157     8672   8822   9423   1743   2420   -787       O  
ATOM    635  CB  ALA A 157      34.106 -12.142  16.593  1.00 73.74           C  
ANISOU  635  CB  ALA A 157     9633   8806   9580   1931   2438   -800       C  
ATOM    636  N   GLU A 158      33.398  -9.188  17.455  1.00 70.56           N  
ANISOU  636  N   GLU A 158     8982   8606   9222   1554   2251   -738       N  
ATOM    637  CA  GLU A 158      33.372  -7.753  17.217  1.00 71.27           C  
ANISOU  637  CA  GLU A 158     8981   8777   9319   1381   2265   -732       C  
ATOM    638  C   GLU A 158      34.028  -6.960  18.362  1.00 70.27           C  
ANISOU  638  C   GLU A 158     8583   8799   9317   1364   2180   -717       C  
ATOM    639  O   GLU A 158      34.799  -6.024  18.118  1.00 69.54           O  
ANISOU  639  O   GLU A 158     8323   8812   9287   1293   2265   -738       O  
ATOM    640  CB  GLU A 158      31.952  -7.263  16.934  1.00 67.51           C  
ANISOU  640  CB  GLU A 158     8705   8215   8733   1222   2183   -704       C  
ATOM    641  CG  GLU A 158      31.915  -6.273  15.778  1.00 71.05           C  
ANISOU  641  CG  GLU A 158     9204   8672   9119   1088   2300   -716       C  
ATOM    642  CD  GLU A 158      30.589  -5.549  15.621  1.00 71.52           C  
ANISOU  642  CD  GLU A 158     9415   8677   9082    933   2203   -683       C  
ATOM    643  OE1 GLU A 158      29.524  -6.199  15.752  1.00 70.67           O  
ANISOU  643  OE1 GLU A 158     9475   8474   8901    935   2100   -672       O  
ATOM    644  OE2 GLU A 158      30.622  -4.326  15.355  1.00 69.83           O  
ANISOU  644  OE2 GLU A 158     9151   8513   8867    810   2236   -668       O  
ATOM    645  N   VAL A 159      33.746  -7.344  19.603  1.00 69.60           N  
ANISOU  645  N   VAL A 159     8458   8722   9266   1427   2020   -686       N  
ATOM    646  CA  VAL A 159      34.387  -6.683  20.728  1.00 71.01           C  
ANISOU  646  CA  VAL A 159     8385   9044   9552   1424   1928   -680       C  
ATOM    647  C   VAL A 159      35.881  -7.013  20.716  1.00 74.66           C  
ANISOU  647  C   VAL A 159     8626   9623  10120   1568   2025   -721       C  
ATOM    648  O   VAL A 159      36.709  -6.144  20.987  1.00 75.18           O  
ANISOU  648  O   VAL A 159     8457   9829  10278   1515   2041   -746       O  
ATOM    649  CB  VAL A 159      33.713  -7.014  22.073  1.00 69.78           C  
ANISOU  649  CB  VAL A 159     8251   8871   9392   1463   1733   -633       C  
ATOM    650  CG1 VAL A 159      34.488  -6.409  23.237  1.00 69.81           C  
ANISOU  650  CG1 VAL A 159     7991   9034   9501   1480   1637   -637       C  
ATOM    651  CG2 VAL A 159      32.283  -6.492  22.088  1.00 65.16           C  
ANISOU  651  CG2 VAL A 159     7845   8196   8719   1303   1646   -598       C  
ATOM    652  N   ALA A 160      36.218  -8.250  20.350  1.00 76.37           N  
ANISOU  652  N   ALA A 160     8919   9778  10322   1744   2098   -733       N  
ATOM    653  CA  ALA A 160      37.617  -8.688  20.315  1.00 80.63           C  
ANISOU  653  CA  ALA A 160     9253  10424  10959   1909   2195   -772       C  
ATOM    654  C   ALA A 160      38.493  -7.781  19.459  1.00 83.92           C  
ANISOU  654  C   ALA A 160     9509  10943  11432   1815   2361   -821       C  
ATOM    655  O   ALA A 160      39.625  -7.510  19.836  1.00 87.53           O  
ANISOU  655  O   ALA A 160     9695  11555  12006   1869   2385   -853       O  
ATOM    656  CB  ALA A 160      37.743 -10.142  19.851  1.00 79.62           C  
ANISOU  656  CB  ALA A 160     9277  10185  10791   2106   2275   -779       C  
ATOM    657  N   SER A 161      37.980  -7.302  18.325  1.00 85.85           N  
ANISOU  657  N   SER A 161     9919  11108  11594   1674   2475   -827       N  
ATOM    658  CA  SER A 161      38.822  -6.543  17.383  1.00 87.43           C  
ANISOU  658  CA  SER A 161    10000  11384  11834   1593   2665   -870       C  
ATOM    659  C   SER A 161      38.611  -5.011  17.372  1.00 83.19           C  
ANISOU  659  C   SER A 161     9395  10901  11312   1363   2657   -862       C  
ATOM    660  O   SER A 161      39.415  -4.276  16.798  1.00 85.93           O  
ANISOU  660  O   SER A 161     9605  11329  11716   1285   2807   -896       O  
ATOM    661  CB  SER A 161      38.737  -7.137  15.962  1.00 87.68           C  
ANISOU  661  CB  SER A 161    10243  11304  11768   1631   2850   -891       C  
ATOM    662  OG  SER A 161      37.407  -7.117  15.469  1.00 85.01           O  
ANISOU  662  OG  SER A 161    10195  10818  11287   1528   2804   -862       O  
ATOM    663  N   THR A 162      37.555  -4.531  18.014  1.00 78.81           N  
ANISOU  663  N   THR A 162     8935  10298  10709   1255   2492   -819       N  
ATOM    664  CA  THR A 162      37.244  -3.095  17.995  1.00 76.37           C  
ANISOU  664  CA  THR A 162     8597  10017  10403   1044   2482   -808       C  
ATOM    665  C   THR A 162      36.926  -2.492  19.380  1.00 76.55           C  
ANISOU  665  C   THR A 162     8504  10103  10480    982   2282   -787       C  
ATOM    666  O   THR A 162      36.730  -1.269  19.510  1.00 77.68           O  
ANISOU  666  O   THR A 162     8605  10272  10638    812   2265   -782       O  
ATOM    667  CB  THR A 162      36.070  -2.782  17.038  1.00 73.01           C  
ANISOU  667  CB  THR A 162     8460   9451   9831    927   2516   -775       C  
ATOM    668  OG1 THR A 162      34.870  -3.350  17.563  1.00 70.76           O  
ANISOU  668  OG1 THR A 162     8351   9069   9465    954   2348   -736       O  
ATOM    669  CG2 THR A 162      36.322  -3.328  15.624  1.00 74.86           C  
ANISOU  669  CG2 THR A 162     8834   9619   9989    978   2712   -799       C  
ATOM    670  N   GLY A 163      36.848  -3.341  20.405  1.00 74.33           N  
ANISOU  670  N   GLY A 163     8187   9836  10219   1122   2134   -774       N  
ATOM    671  CA  GLY A 163      36.550  -2.885  21.762  1.00 70.57           C  
ANISOU  671  CA  GLY A 163     7613   9418   9781   1084   1942   -755       C  
ATOM    672  C   GLY A 163      35.080  -2.545  21.958  1.00 69.63           C  
ANISOU  672  C   GLY A 163     7712   9185   9559    974   1828   -703       C  
ATOM    673  O   GLY A 163      34.652  -2.205  23.067  1.00 69.04           O  
ANISOU  673  O   GLY A 163     7597   9139   9497    942   1669   -682       O  
ATOM    674  N   THR A 164      34.302  -2.629  20.881  1.00 65.60           N  
ANISOU  674  N   THR A 164     7430   8550   8944    919   1910   -685       N  
ATOM    675  CA  THR A 164      32.878  -2.372  20.954  1.00 60.70           C  
ANISOU  675  CA  THR A 164     7016   7825   8224    825   1809   -639       C  
ATOM    676  C   THR A 164      32.140  -3.304  20.001  1.00 61.92           C  
ANISOU  676  C   THR A 164     7419   7844   8264    873   1861   -629       C  
ATOM    677  O   THR A 164      32.768  -4.089  19.262  1.00 61.91           O  
ANISOU  677  O   THR A 164     7439   7826   8260    976   1986   -658       O  
ATOM    678  CB  THR A 164      32.546  -0.876  20.671  1.00 60.22           C  
ANISOU  678  CB  THR A 164     6956   7773   8151    630   1831   -631       C  
ATOM    679  OG1 THR A 164      31.230  -0.569  21.141  1.00 55.38           O  
ANISOU  679  OG1 THR A 164     6483   7091   7467    558   1693   -587       O  
ATOM    680  CG2 THR A 164      32.635  -0.533  19.188  1.00 59.89           C  
ANISOU  680  CG2 THR A 164     7024   7681   8049    564   2011   -641       C  
ATOM    681  N   TYR A 165      30.808  -3.204  20.023  1.00 57.42           N  
ANISOU  681  N   TYR A 165     7034   7181   7602    798   1767   -593       N  
ATOM    682  CA  TYR A 165      29.935  -3.907  19.073  1.00 55.83           C  
ANISOU  682  CA  TYR A 165     7078   6853   7281    805   1802   -589       C  
ATOM    683  C   TYR A 165      28.663  -3.105  18.751  1.00 54.04           C  
ANISOU  683  C   TYR A 165     7001   6569   6961    658   1741   -559       C  
ATOM    684  O   TYR A 165      28.373  -2.091  19.395  1.00 53.66           O  
ANISOU  684  O   TYR A 165     6879   6567   6943    564   1662   -534       O  
ATOM    685  CB  TYR A 165      29.562  -5.300  19.616  1.00 53.07           C  
ANISOU  685  CB  TYR A 165     6816   6432   6916    935   1723   -582       C  
ATOM    686  CG  TYR A 165      28.509  -5.288  20.704  1.00 49.36           C  
ANISOU  686  CG  TYR A 165     6388   5933   6433    897   1548   -539       C  
ATOM    687  CD1 TYR A 165      28.810  -4.842  21.982  1.00 49.61           C  
ANISOU  687  CD1 TYR A 165     6250   6055   6546    905   1444   -519       C  
ATOM    688  CD2 TYR A 165      27.220  -5.744  20.462  1.00 50.29           C  
ANISOU  688  CD2 TYR A 165     6713   5940   6456    854   1489   -524       C  
ATOM    689  CE1 TYR A 165      27.862  -4.841  22.989  1.00 47.94           C  
ANISOU  689  CE1 TYR A 165     6082   5818   6317    876   1295   -479       C  
ATOM    690  CE2 TYR A 165      26.253  -5.752  21.471  1.00 48.92           C  
ANISOU  690  CE2 TYR A 165     6570   5742   6274    819   1341   -485       C  
ATOM    691  CZ  TYR A 165      26.584  -5.295  22.733  1.00 47.56           C  
ANISOU  691  CZ  TYR A 165     6235   5656   6179    833   1250   -460       C  
ATOM    692  OH  TYR A 165      25.649  -5.288  23.750  1.00 45.20           O  
ANISOU  692  OH  TYR A 165     5970   5336   5868    801   1114   -421       O  
ATOM    693  N   HIS A 166      27.897  -3.603  17.786  1.00 54.39           N  
ANISOU  693  N   HIS A 166     7257   6515   6893    649   1773   -564       N  
ATOM    694  CA  HIS A 166      26.698  -2.941  17.275  1.00 55.60           C  
ANISOU  694  CA  HIS A 166     7564   6617   6943    528   1724   -540       C  
ATOM    695  C   HIS A 166      25.444  -3.785  17.457  1.00 50.14           C  
ANISOU  695  C   HIS A 166     7035   5836   6179    537   1608   -532       C  
ATOM    696  O   HIS A 166      25.487  -5.004  17.420  1.00 49.18           O  
ANISOU  696  O   HIS A 166     6982   5656   6048    630   1617   -556       O  
ATOM    697  CB  HIS A 166      26.916  -2.599  15.797  1.00 63.48           C  
ANISOU  697  CB  HIS A 166     8668   7593   7857    490   1875   -560       C  
ATOM    698  CG  HIS A 166      27.892  -1.447  15.560  1.00 73.45           C  
ANISOU  698  CG  HIS A 166     9793   8936   9179    431   1991   -558       C  
ATOM    699  ND1 HIS A 166      28.169  -0.971  14.322  1.00 78.82           N  
ANISOU  699  ND1 HIS A 166    10556   9602   9789    389   2139   -566       N  
ATOM    700  CD2 HIS A 166      28.628  -0.660  16.457  1.00 73.54           C  
ANISOU  700  CD2 HIS A 166     9589   9040   9314    399   1977   -551       C  
ATOM    701  CE1 HIS A 166      29.039   0.058  14.425  1.00 82.61           C  
ANISOU  701  CE1 HIS A 166    10882  10156  10352    327   2225   -561       C  
ATOM    702  NE2 HIS A 166      29.313   0.246  15.736  1.00 77.52           N  
ANISOU  702  NE2 HIS A 166    10050   9577   9827    329   2121   -557       N  
ATOM    703  N   LEU A 167      24.307  -3.148  17.678  1.00 47.53           N  
ANISOU  703  N   LEU A 167     6766   5492   5802    440   1499   -501       N  
ATOM    704  CA  LEU A 167      23.073  -3.903  17.884  1.00 45.38           C  
ANISOU  704  CA  LEU A 167     6630   5143   5469    433   1389   -497       C  
ATOM    705  C   LEU A 167      22.319  -4.056  16.586  1.00 45.74           C  
ANISOU  705  C   LEU A 167     6869   5126   5385    387   1420   -521       C  
ATOM    706  O   LEU A 167      22.279  -3.143  15.781  1.00 45.51           O  
ANISOU  706  O   LEU A 167     6875   5119   5297    325   1470   -513       O  
ATOM    707  CB  LEU A 167      22.181  -3.218  18.887  1.00 41.51           C  
ANISOU  707  CB  LEU A 167     6094   4678   4999    361   1248   -453       C  
ATOM    708  CG  LEU A 167      22.699  -2.945  20.300  1.00 41.90           C  
ANISOU  708  CG  LEU A 167     5965   4793   5160    390   1186   -428       C  
ATOM    709  CD1 LEU A 167      21.720  -2.006  20.992  1.00 40.54           C  
ANISOU  709  CD1 LEU A 167     5778   4642   4982    297   1070   -389       C  
ATOM    710  CD2 LEU A 167      22.888  -4.223  21.125  1.00 43.12           C  
ANISOU  710  CD2 LEU A 167     6108   4916   5359    498   1146   -430       C  
ATOM    711  N   ARG A 168      21.701  -5.208  16.376  1.00 46.38           N  
ANISOU  711  N   ARG A 168     7084   5125   5414    416   1388   -551       N  
ATOM    712  CA  ARG A 168      20.772  -5.326  15.262  1.00 47.59           C  
ANISOU  712  CA  ARG A 168     7420   5226   5436    357   1380   -579       C  
ATOM    713  C   ARG A 168      19.575  -4.391  15.506  1.00 46.53           C  
ANISOU  713  C   ARG A 168     7295   5121   5265    253   1255   -540       C  
ATOM    714  O   ARG A 168      19.313  -3.987  16.640  1.00 43.51           O  
ANISOU  714  O   ARG A 168     6802   4773   4957    233   1167   -500       O  
ATOM    715  CB  ARG A 168      20.357  -6.784  15.079  1.00 50.72           C  
ANISOU  715  CB  ARG A 168     7952   5526   5796    399   1368   -628       C  
ATOM    716  CG  ARG A 168      21.512  -7.630  14.577  1.00 53.76           C  
ANISOU  716  CG  ARG A 168     8356   5874   6194    508   1510   -671       C  
ATOM    717  CD  ARG A 168      21.133  -9.071  14.312  1.00 58.58           C  
ANISOU  717  CD  ARG A 168     9125   6372   6763    549   1513   -725       C  
ATOM    718  NE  ARG A 168      22.254  -9.754  13.672  1.00 65.64           N  
ANISOU  718  NE  ARG A 168    10049   7233   7657    659   1665   -768       N  
ATOM    719  CZ  ARG A 168      22.495 -11.058  13.755  1.00 69.99           C  
ANISOU  719  CZ  ARG A 168    10680   7690   8223    750   1705   -806       C  
ATOM    720  NH1 ARG A 168      21.686 -11.840  14.466  1.00 70.78           N  
ANISOU  720  NH1 ARG A 168    10842   7711   8339    735   1607   -805       N  
ATOM    721  NH2 ARG A 168      23.552 -11.580  13.138  1.00 70.46           N  
ANISOU  721  NH2 ARG A 168    10760   7729   8284    859   1852   -845       N  
ATOM    722  N   GLU A 169      18.885  -4.014  14.442  1.00 46.13           N  
ANISOU  722  N   GLU A 169     7372   5061   5094    197   1250   -553       N  
ATOM    723  CA  GLU A 169      17.744  -3.135  14.569  1.00 47.87           C  
ANISOU  723  CA  GLU A 169     7606   5312   5271    115   1135   -518       C  
ATOM    724  C   GLU A 169      16.734  -3.612  15.632  1.00 44.80           C  
ANISOU  724  C   GLU A 169     7187   4906   4927     87    996   -509       C  
ATOM    725  O   GLU A 169      16.396  -2.867  16.556  1.00 41.49           O  
ANISOU  725  O   GLU A 169     6667   4531   4567     56    921   -462       O  
ATOM    726  CB  GLU A 169      17.063  -2.956  13.211  1.00 52.71           C  
ANISOU  726  CB  GLU A 169     8383   5912   5731     77   1136   -542       C  
ATOM    727  CG  GLU A 169      15.678  -2.318  13.294  1.00 59.49           C  
ANISOU  727  CG  GLU A 169     9270   6797   6534      7    995   -517       C  
ATOM    728  CD  GLU A 169      14.805  -2.664  12.102  1.00 67.93           C  
ANISOU  728  CD  GLU A 169    10510   7848   7453    -19    955   -563       C  
ATOM    729  OE1 GLU A 169      14.412  -3.851  11.946  1.00 66.06           O  
ANISOU  729  OE1 GLU A 169    10350   7559   7192    -22    925   -626       O  
ATOM    730  OE2 GLU A 169      14.525  -1.739  11.308  1.00 75.57           O  
ANISOU  730  OE2 GLU A 169    11541   8849   8322    -37    955   -539       O  
ATOM    731  N   SER A 170      16.282  -4.855  15.517  1.00 46.26           N  
ANISOU  731  N   SER A 170     7466   5023   5087     97    971   -557       N  
ATOM    732  CA  SER A 170      15.219  -5.372  16.384  1.00 46.48           C  
ANISOU  732  CA  SER A 170     7488   5026   5145     56    852   -554       C  
ATOM    733  C   SER A 170      15.699  -5.555  17.829  1.00 45.30           C  
ANISOU  733  C   SER A 170     7208   4882   5123    101    837   -514       C  
ATOM    734  O   SER A 170      14.906  -5.508  18.771  1.00 44.77           O  
ANISOU  734  O   SER A 170     7096   4822   5094     63    742   -486       O  
ATOM    735  CB  SER A 170      14.703  -6.685  15.840  1.00 49.11           C  
ANISOU  735  CB  SER A 170     7965   5273   5422     46    848   -623       C  
ATOM    736  OG  SER A 170      15.704  -7.672  16.001  1.00 52.84           O  
ANISOU  736  OG  SER A 170     8449   5683   5945    133    942   -645       O  
ATOM    737  N   GLU A 171      17.004  -5.747  17.981  1.00 43.97           N  
ANISOU  737  N   GLU A 171     6976   4717   5013    186    933   -511       N  
ATOM    738  CA  GLU A 171      17.661  -5.686  19.273  1.00 42.66           C  
ANISOU  738  CA  GLU A 171     6669   4583   4958    240    920   -471       C  
ATOM    739  C   GLU A 171      17.538  -4.299  19.917  1.00 42.99           C  
ANISOU  739  C   GLU A 171     6586   4711   5036    190    864   -420       C  
ATOM    740  O   GLU A 171      17.228  -4.169  21.115  1.00 42.86           O  
ANISOU  740  O   GLU A 171     6492   4715   5078    185    785   -385       O  
ATOM    741  CB  GLU A 171      19.119  -6.093  19.132  1.00 43.68           C  
ANISOU  741  CB  GLU A 171     6745   4716   5136    345   1036   -486       C  
ATOM    742  CG  GLU A 171      19.306  -7.547  18.733  1.00 45.49           C  
ANISOU  742  CG  GLU A 171     7092   4848   5345    416   1093   -533       C  
ATOM    743  CD  GLU A 171      20.772  -7.887  18.521  1.00 51.20           C  
ANISOU  743  CD  GLU A 171     7754   5584   6115    532   1215   -549       C  
ATOM    744  OE1 GLU A 171      21.604  -6.954  18.482  1.00 54.39           O  
ANISOU  744  OE1 GLU A 171     8031   6077   6559    538   1264   -533       O  
ATOM    745  OE2 GLU A 171      21.099  -9.082  18.359  1.00 52.22           O  
ANISOU  745  OE2 GLU A 171     7963   5634   6244    617   1270   -581       O  
ATOM    746  N   LEU A 172      17.735  -3.256  19.132  1.00 41.10           N  
ANISOU  746  N   LEU A 172     6344   4516   4757    151    907   -416       N  
ATOM    747  CA  LEU A 172      17.612  -1.920  19.684  1.00 41.18           C  
ANISOU  747  CA  LEU A 172     6256   4593   4799    101    864   -371       C  
ATOM    748  C   LEU A 172      16.147  -1.623  20.081  1.00 40.95           C  
ANISOU  748  C   LEU A 172     6262   4561   4736     34    740   -349       C  
ATOM    749  O   LEU A 172      15.876  -1.065  21.156  1.00 41.71           O  
ANISOU  749  O   LEU A 172     6269   4693   4888     16    671   -313       O  
ATOM    750  CB  LEU A 172      18.176  -0.899  18.681  1.00 39.98           C  
ANISOU  750  CB  LEU A 172     6112   4472   4608     75    956   -369       C  
ATOM    751  CG  LEU A 172      17.954   0.583  18.997  1.00 38.97           C  
ANISOU  751  CG  LEU A 172     5921   4392   4492     13    925   -326       C  
ATOM    752  CD1 LEU A 172      18.736   1.054  20.213  1.00 34.39           C  
ANISOU  752  CD1 LEU A 172     5175   3863   4028     23    917   -309       C  
ATOM    753  CD2 LEU A 172      18.283   1.392  17.750  1.00 38.38           C  
ANISOU  753  CD2 LEU A 172     5915   4320   4347    -15   1023   -323       C  
ATOM    754  N   VAL A 173      15.205  -2.012  19.225  1.00 40.35           N  
ANISOU  754  N   VAL A 173     6314   4450   4569     -1    710   -374       N  
ATOM    755  CA  VAL A 173      13.770  -1.876  19.528  1.00 39.27           C  
ANISOU  755  CA  VAL A 173     6204   4317   4402    -62    593   -363       C  
ATOM    756  C   VAL A 173      13.444  -2.601  20.847  1.00 41.19           C  
ANISOU  756  C   VAL A 173     6390   4538   4720    -53    533   -351       C  
ATOM    757  O   VAL A 173      12.818  -2.026  21.746  1.00 41.22           O  
ANISOU  757  O   VAL A 173     6327   4577   4758    -83    459   -315       O  
ATOM    758  CB  VAL A 173      12.910  -2.453  18.382  1.00 39.92           C  
ANISOU  758  CB  VAL A 173     6426   4364   4377    -96    570   -409       C  
ATOM    759  CG1 VAL A 173      11.413  -2.471  18.739  1.00 38.55           C  
ANISOU  759  CG1 VAL A 173     6261   4202   4185   -160    447   -408       C  
ATOM    760  CG2 VAL A 173      13.180  -1.687  17.078  1.00 40.14           C  
ANISOU  760  CG2 VAL A 173     6526   4415   4312    -98    627   -413       C  
ATOM    761  N   PHE A 174      13.896  -3.848  20.975  1.00 41.71           N  
ANISOU  761  N   PHE A 174     6492   4544   4811     -5    573   -379       N  
ATOM    762  CA  PHE A 174      13.664  -4.601  22.191  1.00 39.72           C  
ANISOU  762  CA  PHE A 174     6208   4261   4623     13    530   -362       C  
ATOM    763  C   PHE A 174      14.289  -3.907  23.407  1.00 40.46           C  
ANISOU  763  C   PHE A 174     6165   4413   4796     50    515   -312       C  
ATOM    764  O   PHE A 174      13.662  -3.780  24.469  1.00 38.54           O  
ANISOU  764  O   PHE A 174     5876   4182   4584     30    444   -280       O  
ATOM    765  CB  PHE A 174      14.223  -5.992  22.050  1.00 40.29           C  
ANISOU  765  CB  PHE A 174     6353   4250   4704     76    592   -395       C  
ATOM    766  CG  PHE A 174      14.411  -6.693  23.362  1.00 43.19           C  
ANISOU  766  CG  PHE A 174     6681   4586   5143    130    574   -364       C  
ATOM    767  CD1 PHE A 174      13.331  -7.286  24.007  1.00 43.55           C  
ANISOU  767  CD1 PHE A 174     6772   4583   5192     80    514   -356       C  
ATOM    768  CD2 PHE A 174      15.682  -6.764  23.958  1.00 42.48           C  
ANISOU  768  CD2 PHE A 174     6506   4519   5115    233    619   -343       C  
ATOM    769  CE1 PHE A 174      13.513  -7.936  25.228  1.00 47.84           C  
ANISOU  769  CE1 PHE A 174     7296   5092   5791    136    505   -319       C  
ATOM    770  CE2 PHE A 174      15.868  -7.394  25.166  1.00 42.88           C  
ANISOU  770  CE2 PHE A 174     6529   4546   5219    296    596   -309       C  
ATOM    771  CZ  PHE A 174      14.787  -7.995  25.805  1.00 46.71           C  
ANISOU  771  CZ  PHE A 174     7079   4971   5697    250    543   -293       C  
ATOM    772  N   GLY A 175      15.536  -3.456  23.246  1.00 42.82           N  
ANISOU  772  N   GLY A 175     6393   4751   5126    102    583   -311       N  
ATOM    773  CA  GLY A 175      16.302  -2.881  24.354  1.00 41.56           C  
ANISOU  773  CA  GLY A 175     6097   4652   5043    140    570   -279       C  
ATOM    774  C   GLY A 175      15.653  -1.613  24.858  1.00 39.99           C  
ANISOU  774  C   GLY A 175     5840   4508   4846     72    503   -248       C  
ATOM    775  O   GLY A 175      15.492  -1.424  26.055  1.00 42.52           O  
ANISOU  775  O   GLY A 175     6093   4854   5209     78    443   -220       O  
ATOM    776  N   ALA A 176      15.250  -0.759  23.929  1.00 37.73           N  
ANISOU  776  N   ALA A 176     5593   4234   4506     13    514   -251       N  
ATOM    777  CA  ALA A 176      14.547   0.455  24.268  1.00 37.73           C  
ANISOU  777  CA  ALA A 176     5560   4274   4500    -45    457   -221       C  
ATOM    778  C   ALA A 176      13.267   0.204  25.065  1.00 40.26           C  
ANISOU  778  C   ALA A 176     5895   4586   4817    -73    362   -203       C  
ATOM    779  O   ALA A 176      13.015   0.896  26.075  1.00 41.69           O  
ANISOU  779  O   ALA A 176     6005   4802   5032    -86    312   -174       O  
ATOM    780  CB  ALA A 176      14.246   1.246  23.006  1.00 36.08           C  
ANISOU  780  CB  ALA A 176     5422   4069   4219    -87    487   -225       C  
ATOM    781  N   LYS A 177      12.440  -0.750  24.612  1.00 40.28           N  
ANISOU  781  N   LYS A 177     5989   4542   4776    -90    341   -224       N  
ATOM    782  CA  LYS A 177      11.213  -1.093  25.351  1.00 40.83           C  
ANISOU  782  CA  LYS A 177     6066   4601   4849   -127    263   -211       C  
ATOM    783  C   LYS A 177      11.520  -1.660  26.739  1.00 38.36           C  
ANISOU  783  C   LYS A 177     5699   4276   4599    -86    250   -187       C  
ATOM    784  O   LYS A 177      10.854  -1.332  27.712  1.00 39.10           O  
ANISOU  784  O   LYS A 177     5752   4393   4713   -106    196   -159       O  
ATOM    785  CB  LYS A 177      10.352  -2.085  24.591  1.00 43.59           C  
ANISOU  785  CB  LYS A 177     6517   4900   5147   -164    249   -248       C  
ATOM    786  CG  LYS A 177       9.674  -1.521  23.367  1.00 46.37           C  
ANISOU  786  CG  LYS A 177     6924   5275   5420   -210    228   -269       C  
ATOM    787  CD  LYS A 177       9.046  -2.659  22.573  1.00 48.00           C  
ANISOU  787  CD  LYS A 177     7233   5430   5576   -245    219   -323       C  
ATOM    788  CE  LYS A 177       8.185  -2.119  21.444  1.00 51.50           C  
ANISOU  788  CE  LYS A 177     7727   5910   5930   -290    172   -345       C  
ATOM    789  NZ  LYS A 177       7.998  -3.114  20.346  1.00 56.37           N  
ANISOU  789  NZ  LYS A 177     8459   6480   6479   -313    185   -412       N  
ATOM    790  N   GLN A 178      12.549  -2.487  26.823  1.00 39.12           N  
ANISOU  790  N   GLN A 178     5800   4341   4722    -19    302   -198       N  
ATOM    791  CA  GLN A 178      12.920  -3.104  28.069  1.00 38.83           C  
ANISOU  791  CA  GLN A 178     5728   4292   4734     39    290   -173       C  
ATOM    792  C   GLN A 178      13.422  -2.025  29.049  1.00 38.67           C  
ANISOU  792  C   GLN A 178     5591   4349   4753     57    259   -144       C  
ATOM    793  O   GLN A 178      13.045  -2.040  30.248  1.00 37.57           O  
ANISOU  793  O   GLN A 178     5423   4220   4631     64    210   -113       O  
ATOM    794  CB  GLN A 178      13.959  -4.188  27.813  1.00 41.17           C  
ANISOU  794  CB  GLN A 178     6057   4540   5046    123    355   -191       C  
ATOM    795  CG  GLN A 178      13.997  -5.286  28.866  1.00 47.75           C  
ANISOU  795  CG  GLN A 178     6917   5320   5904    185    345   -166       C  
ATOM    796  CD  GLN A 178      12.788  -6.244  28.878  1.00 47.58           C  
ANISOU  796  CD  GLN A 178     7009   5212   5857    130    332   -169       C  
ATOM    797  OE1 GLN A 178      11.799  -6.103  28.131  1.00 42.88           O  
ANISOU  797  OE1 GLN A 178     6462   4605   5225     38    316   -196       O  
ATOM    798  NE2 GLN A 178      12.876  -7.228  29.759  1.00 50.21           N  
ANISOU  798  NE2 GLN A 178     7384   5484   6209    186    339   -142       N  
ATOM    799  N   ALA A 179      14.215  -1.071  28.545  1.00 35.46           N  
ANISOU  799  N   ALA A 179     5124   3992   4356     55    291   -156       N  
ATOM    800  CA  ALA A 179      14.645   0.090  29.359  1.00 35.31           C  
ANISOU  800  CA  ALA A 179     4999   4044   4373     49    263   -141       C  
ATOM    801  C   ALA A 179      13.490   0.834  29.983  1.00 33.33           C  
ANISOU  801  C   ALA A 179     4748   3808   4106     -7    198   -116       C  
ATOM    802  O   ALA A 179      13.543   1.190  31.159  1.00 34.40           O  
ANISOU  802  O   ALA A 179     4825   3979   4267      6    155    -98       O  
ATOM    803  CB  ALA A 179      15.496   1.059  28.555  1.00 35.06           C  
ANISOU  803  CB  ALA A 179     4921   4050   4351     29    320   -161       C  
ATOM    804  N   TRP A 180      12.445   1.071  29.202  1.00 34.68           N  
ANISOU  804  N   TRP A 180     4984   3960   4233    -64    188   -117       N  
ATOM    805  CA  TRP A 180      11.242   1.710  29.724  1.00 33.79           C  
ANISOU  805  CA  TRP A 180     4869   3864   4106   -110    129    -95       C  
ATOM    806  C   TRP A 180      10.558   0.789  30.668  1.00 35.63           C  
ANISOU  806  C   TRP A 180     5119   4073   4347   -101     94    -78       C  
ATOM    807  O   TRP A 180      10.232   1.180  31.779  1.00 38.74           O  
ANISOU  807  O   TRP A 180     5471   4492   4755   -100     57    -55       O  
ATOM    808  CB  TRP A 180      10.337   2.142  28.595  1.00 35.37           C  
ANISOU  808  CB  TRP A 180     5127   4058   4253   -159    122   -102       C  
ATOM    809  CG  TRP A 180       9.027   2.800  28.984  1.00 36.41           C  
ANISOU  809  CG  TRP A 180     5251   4214   4369   -196     63    -81       C  
ATOM    810  CD1 TRP A 180       8.667   3.365  30.204  1.00 32.85           C  
ANISOU  810  CD1 TRP A 180     4746   3791   3946   -195     27    -57       C  
ATOM    811  CD2 TRP A 180       7.862   3.022  28.101  1.00 37.20           C  
ANISOU  811  CD2 TRP A 180     5398   4319   4417   -234     31    -86       C  
ATOM    812  NE1 TRP A 180       7.401   3.894  30.134  1.00 35.74           N  
ANISOU  812  NE1 TRP A 180     5118   4175   4288   -225    -15    -45       N  
ATOM    813  CE2 TRP A 180       6.855   3.700  28.914  1.00 33.78           C  
ANISOU  813  CE2 TRP A 180     4922   3918   3993   -248    -20    -61       C  
ATOM    814  CE3 TRP A 180       7.565   2.722  26.755  1.00 38.05           C  
ANISOU  814  CE3 TRP A 180     5575   4413   4467   -252     36   -111       C  
ATOM    815  CZ2 TRP A 180       5.614   4.050  28.408  1.00 34.46           C  
ANISOU  815  CZ2 TRP A 180     5022   4029   4041   -273    -66    -60       C  
ATOM    816  CZ3 TRP A 180       6.302   3.072  26.259  1.00 35.94           C  
ANISOU  816  CZ3 TRP A 180     5327   4173   4155   -281    -20   -111       C  
ATOM    817  CH2 TRP A 180       5.352   3.735  27.069  1.00 36.69           C  
ANISOU  817  CH2 TRP A 180     5366   4305   4267   -288    -71    -85       C  
ATOM    818  N   ARG A 181      10.383  -0.469  30.278  1.00 35.96           N  
ANISOU  818  N   ARG A 181     5229   4059   4377    -95    113    -91       N  
ATOM    819  CA  ARG A 181       9.852  -1.462  31.194  1.00 34.72           C  
ANISOU  819  CA  ARG A 181     5101   3862   4230    -87     97    -73       C  
ATOM    820  C   ARG A 181      10.601  -1.533  32.547  1.00 36.11           C  
ANISOU  820  C   ARG A 181     5226   4056   4437    -19     87    -43       C  
ATOM    821  O   ARG A 181      10.000  -1.766  33.594  1.00 35.88           O  
ANISOU  821  O   ARG A 181     5203   4021   4409    -20     62    -13       O  
ATOM    822  CB  ARG A 181       9.912  -2.808  30.517  1.00 35.84           C  
ANISOU  822  CB  ARG A 181     5331   3927   4361    -80    136    -97       C  
ATOM    823  CG  ARG A 181       9.052  -3.874  31.146  1.00 37.29           C  
ANISOU  823  CG  ARG A 181     5574   4049   4547   -104    131    -85       C  
ATOM    824  CD  ARG A 181       9.510  -5.242  30.653  1.00 37.75           C  
ANISOU  824  CD  ARG A 181     5724   4016   4602    -72    184   -108       C  
ATOM    825  NE  ARG A 181       8.538  -6.260  30.994  1.00 39.33           N  
ANISOU  825  NE  ARG A 181     6000   4141   4802   -123    190   -106       N  
ATOM    826  CZ  ARG A 181       8.499  -7.498  30.496  1.00 42.10           C  
ANISOU  826  CZ  ARG A 181     6456   4394   5147   -131    234   -134       C  
ATOM    827  NH1 ARG A 181       9.417  -7.917  29.607  1.00 37.84           N  
ANISOU  827  NH1 ARG A 181     5961   3820   4596    -78    278   -168       N  
ATOM    828  NH2 ARG A 181       7.524  -8.324  30.904  1.00 39.50           N  
ANISOU  828  NH2 ARG A 181     6189   3996   4823   -196    243   -132       N  
ATOM    829  N   ASN A 182      11.912  -1.320  32.516  1.00 37.67           N  
ANISOU  829  N   ASN A 182     5373   4283   4656     41    108    -52       N  
ATOM    830  CA  ASN A 182      12.730  -1.394  33.721  1.00 38.58           C  
ANISOU  830  CA  ASN A 182     5433   4430   4796    115     87    -31       C  
ATOM    831  C   ASN A 182      12.759  -0.125  34.627  1.00 39.07           C  
ANISOU  831  C   ASN A 182     5412   4566   4865     99     40    -23       C  
ATOM    832  O   ASN A 182      13.165  -0.217  35.786  1.00 40.14           O  
ANISOU  832  O   ASN A 182     5514   4731   5006    153      7     -5       O  
ATOM    833  CB  ASN A 182      14.145  -1.877  33.360  1.00 38.28           C  
ANISOU  833  CB  ASN A 182     5365   4397   4783    195    126    -51       C  
ATOM    834  CG  ASN A 182      14.179  -3.342  32.920  1.00 38.91           C  
ANISOU  834  CG  ASN A 182     5540   4391   4854    241    170    -52       C  
ATOM    835  OD1 ASN A 182      13.232  -4.106  33.157  1.00 39.99           O  
ANISOU  835  OD1 ASN A 182     5764   4462   4971    216    166    -34       O  
ATOM    836  ND2 ASN A 182      15.288  -3.750  32.316  1.00 37.77           N  
ANISOU  836  ND2 ASN A 182     5379   4244   4729    306    218    -75       N  
ATOM    837  N   ALA A 183      12.308   1.022  34.112  1.00 37.58           N  
ANISOU  837  N   ALA A 183     5202   4404   4672     31     36    -35       N  
ATOM    838  CA  ALA A 183      12.432   2.344  34.810  1.00 36.52           C  
ANISOU  838  CA  ALA A 183     4999   4331   4548     11      3    -37       C  
ATOM    839  C   ALA A 183      11.560   2.406  36.066  1.00 37.39           C  
ANISOU  839  C   ALA A 183     5119   4448   4640     10    -43     -8       C  
ATOM    840  O   ALA A 183      10.332   2.527  35.948  1.00 39.81           O  
ANISOU  840  O   ALA A 183     5465   4734   4926    -36    -49      6       O  
ATOM    841  CB  ALA A 183      12.063   3.494  33.858  1.00 30.97           C  
ANISOU  841  CB  ALA A 183     4297   3633   3837    -56     20    -51       C  
ATOM    842  N   PRO A 184      12.179   2.320  37.260  1.00 36.27           N  
ANISOU  842  N   PRO A 184     4939   4340   4501     64    -75     -1       N  
ATOM    843  CA  PRO A 184      11.442   2.223  38.519  1.00 35.14           C  
ANISOU  843  CA  PRO A 184     4821   4202   4330     76   -109     30       C  
ATOM    844  C   PRO A 184      10.601   3.442  38.862  1.00 37.50           C  
ANISOU  844  C   PRO A 184     5105   4525   4617     21   -128     28       C  
ATOM    845  O   PRO A 184       9.703   3.351  39.727  1.00 40.03           O  
ANISOU  845  O   PRO A 184     5456   4841   4911     20   -140     54       O  
ATOM    846  CB  PRO A 184      12.554   2.103  39.575  1.00 34.78           C  
ANISOU  846  CB  PRO A 184     4727   4204   4283    153   -147     28       C  
ATOM    847  CG  PRO A 184      13.775   1.713  38.844  1.00 35.30           C  
ANISOU  847  CG  PRO A 184     4751   4280   4383    193   -126      3       C  
ATOM    848  CD  PRO A 184      13.646   2.324  37.488  1.00 37.77           C  
ANISOU  848  CD  PRO A 184     5057   4576   4718    121    -82    -24       C  
ATOM    849  N   ARG A 185      10.873   4.570  38.205  1.00 35.83           N  
ANISOU  849  N   ARG A 185     4855   4334   4424    -20   -121     -2       N  
ATOM    850  CA  ARG A 185      10.249   5.828  38.590  1.00 33.36           C  
ANISOU  850  CA  ARG A 185     4532   4040   4101    -58   -135     -7       C  
ATOM    851  C   ARG A 185       9.079   6.183  37.697  1.00 36.35           C  
ANISOU  851  C   ARG A 185     4949   4391   4472   -104   -116      4       C  
ATOM    852  O   ARG A 185       8.354   7.164  37.977  1.00 36.27           O  
ANISOU  852  O   ARG A 185     4939   4390   4451   -125   -125      7       O  
ATOM    853  CB  ARG A 185      11.277   6.940  38.618  1.00 34.22           C  
ANISOU  853  CB  ARG A 185     4584   4184   4235    -74   -139    -47       C  
ATOM    854  CG  ARG A 185      12.325   6.680  39.690  1.00 35.37           C  
ANISOU  854  CG  ARG A 185     4678   4378   4384    -26   -178    -64       C  
ATOM    855  CD  ARG A 185      13.251   7.840  39.865  1.00 38.01           C  
ANISOU  855  CD  ARG A 185     4945   4752   4744    -58   -188   -114       C  
ATOM    856  NE  ARG A 185      13.966   7.716  41.140  1.00 44.51           N  
ANISOU  856  NE  ARG A 185     5722   5635   5556    -13   -247   -134       N  
ATOM    857  CZ  ARG A 185      15.030   8.441  41.500  1.00 42.38           C  
ANISOU  857  CZ  ARG A 185     5373   5418   5310    -31   -272   -189       C  
ATOM    858  NH1 ARG A 185      15.490   9.393  40.703  1.00 42.15           N  
ANISOU  858  NH1 ARG A 185     5307   5381   5325   -102   -231   -227       N  
ATOM    859  NH2 ARG A 185      15.622   8.225  42.674  1.00 43.95           N  
ANISOU  859  NH2 ARG A 185     5532   5681   5488     20   -339   -208       N  
ATOM    860  N   CYS A 186       8.875   5.384  36.644  1.00 33.59           N  
ANISOU  860  N   CYS A 186     4631   4009   4121   -114    -93      9       N  
ATOM    861  CA  CYS A 186       7.771   5.634  35.721  1.00 36.06           C  
ANISOU  861  CA  CYS A 186     4975   4307   4418   -153    -88     15       C  
ATOM    862  C   CYS A 186       6.478   4.902  36.064  1.00 38.99           C  
ANISOU  862  C   CYS A 186     5370   4668   4777   -167    -99     36       C  
ATOM    863  O   CYS A 186       6.401   3.655  36.006  1.00 39.71           O  
ANISOU  863  O   CYS A 186     5491   4728   4868   -166    -89     41       O  
ATOM    864  CB  CYS A 186       8.160   5.231  34.300  1.00 37.48           C  
ANISOU  864  CB  CYS A 186     5183   4463   4595   -165    -59     -1       C  
ATOM    865  SG  CYS A 186       6.835   5.552  33.110  1.00 39.21           S  
ANISOU  865  SG  CYS A 186     5442   4676   4780   -204    -69      3       S  
ATOM    866  N   VAL A 187       5.442   5.675  36.340  1.00 38.06           N  
ANISOU  866  N   VAL A 187     5240   4571   4650   -182   -114     46       N  
ATOM    867  CA  VAL A 187       4.113   5.113  36.607  1.00 34.65           C  
ANISOU  867  CA  VAL A 187     4812   4141   4213   -205   -119     62       C  
ATOM    868  C   VAL A 187       3.362   4.762  35.342  1.00 34.22           C  
ANISOU  868  C   VAL A 187     4772   4081   4150   -242   -126     49       C  
ATOM    869  O   VAL A 187       2.270   4.236  35.422  1.00 35.12           O  
ANISOU  869  O   VAL A 187     4877   4200   4265   -274   -132     52       O  
ATOM    870  CB  VAL A 187       3.277   6.105  37.476  1.00 34.18           C  
ANISOU  870  CB  VAL A 187     4723   4115   4148   -197   -129     75       C  
ATOM    871  CG1 VAL A 187       2.844   7.332  36.676  1.00 34.81           C  
ANISOU  871  CG1 VAL A 187     4793   4214   4221   -197   -141     68       C  
ATOM    872  CG2 VAL A 187       2.077   5.430  38.114  1.00 34.26           C  
ANISOU  872  CG2 VAL A 187     4724   4132   4160   -217   -120     92       C  
ATOM    873  N   GLY A 188       3.906   5.094  34.163  1.00 38.02           N  
ANISOU  873  N   GLY A 188     5272   4556   4619   -242   -126     32       N  
ATOM    874  CA  GLY A 188       3.152   4.925  32.919  1.00 33.26           C  
ANISOU  874  CA  GLY A 188     4688   3958   3992   -271   -143     18       C  
ATOM    875  C   GLY A 188       3.406   3.581  32.235  1.00 38.95           C  
ANISOU  875  C   GLY A 188     5452   4640   4708   -297   -130     -5       C  
ATOM    876  O   GLY A 188       3.094   3.398  31.040  1.00 38.41           O  
ANISOU  876  O   GLY A 188     5413   4571   4609   -319   -143    -28       O  
ATOM    877  N   ARG A 189       3.971   2.622  32.974  1.00 36.82           N  
ANISOU  877  N   ARG A 189     5196   4333   4461   -288   -103     -1       N  
ATOM    878  CA  ARG A 189       4.611   1.494  32.312  1.00 37.12           C  
ANISOU  878  CA  ARG A 189     5289   4321   4496   -291    -77    -23       C  
ATOM    879  C   ARG A 189       3.645   0.444  31.748  1.00 38.20           C  
ANISOU  879  C   ARG A 189     5463   4430   4623   -349    -83    -48       C  
ATOM    880  O   ARG A 189       4.080  -0.452  31.023  1.00 38.40           O  
ANISOU  880  O   ARG A 189     5545   4406   4637   -356    -60    -75       O  
ATOM    881  CB  ARG A 189       5.694   0.883  33.204  1.00 36.82           C  
ANISOU  881  CB  ARG A 189     5258   4250   4481   -242    -47     -8       C  
ATOM    882  CG  ARG A 189       7.055   1.589  33.159  1.00 32.86           C  
ANISOU  882  CG  ARG A 189     4729   3769   3987   -191    -34    -10       C  
ATOM    883  CD  ARG A 189       8.015   0.926  34.163  1.00 34.07           C  
ANISOU  883  CD  ARG A 189     4877   3906   4162   -133    -20      5       C  
ATOM    884  NE  ARG A 189       7.708   1.285  35.550  1.00 36.42           N  
ANISOU  884  NE  ARG A 189     5144   4232   4464   -119    -44     33       N  
ATOM    885  CZ  ARG A 189       8.174   0.656  36.635  1.00 38.05           C  
ANISOU  885  CZ  ARG A 189     5357   4427   4672    -67    -44     55       C  
ATOM    886  NH1 ARG A 189       9.016  -0.370  36.522  1.00 39.81           N  
ANISOU  886  NH1 ARG A 189     5612   4612   4902    -17    -22     55       N  
ATOM    887  NH2 ARG A 189       7.801   1.052  37.854  1.00 36.39           N  
ANISOU  887  NH2 ARG A 189     5129   4245   4452    -57    -66     79       N  
ATOM    888  N   ILE A 190       2.340   0.584  32.014  1.00 36.62           N  
ANISOU  888  N   ILE A 190     5226   4263   4427   -394   -112    -46       N  
ATOM    889  CA  ILE A 190       1.350  -0.287  31.397  1.00 36.20           C  
ANISOU  889  CA  ILE A 190     5190   4196   4368   -466   -126    -82       C  
ATOM    890  C   ILE A 190       1.460  -0.168  29.872  1.00 41.54           C  
ANISOU  890  C   ILE A 190     5902   4882   4998   -475   -151   -122       C  
ATOM    891  O   ILE A 190       0.967  -1.028  29.125  1.00 40.91           O  
ANISOU  891  O   ILE A 190     5860   4781   4903   -532   -161   -166       O  
ATOM    892  CB  ILE A 190      -0.101   0.071  31.847  1.00 39.20           C  
ANISOU  892  CB  ILE A 190     5496   4634   4763   -510   -157    -78       C  
ATOM    893  CG1 ILE A 190      -1.121  -0.986  31.386  1.00 37.72           C  
ANISOU  893  CG1 ILE A 190     5315   4434   4584   -602   -167   -122       C  
ATOM    894  CG2 ILE A 190      -0.604   1.378  31.243  1.00 36.85           C  
ANISOU  894  CG2 ILE A 190     5148   4415   4438   -486   -210    -77       C  
ATOM    895  CD1 ILE A 190      -1.343  -2.068  32.392  1.00 37.41           C  
ANISOU  895  CD1 ILE A 190     5297   4333   4584   -645   -112   -110       C  
ATOM    896  N   GLN A 191       2.078   0.924  29.407  1.00 42.36           N  
ANISOU  896  N   GLN A 191     6002   5018   5077   -424   -158   -108       N  
ATOM    897  CA  GLN A 191       2.151   1.232  27.970  1.00 43.02           C  
ANISOU  897  CA  GLN A 191     6127   5115   5102   -423   -178   -136       C  
ATOM    898  C   GLN A 191       3.454   0.770  27.328  1.00 43.27           C  
ANISOU  898  C   GLN A 191     6229   5093   5117   -395   -126   -151       C  
ATOM    899  O   GLN A 191       3.632   0.924  26.108  1.00 42.55           O  
ANISOU  899  O   GLN A 191     6189   5007   4970   -392   -128   -175       O  
ATOM    900  CB  GLN A 191       2.026   2.749  27.737  1.00 45.15           C  
ANISOU  900  CB  GLN A 191     6366   5441   5346   -381   -205   -107       C  
ATOM    901  CG  GLN A 191       0.657   3.332  27.972  1.00 40.68           C  
ANISOU  901  CG  GLN A 191     5736   4940   4779   -393   -263    -98       C  
ATOM    902  CD  GLN A 191      -0.319   2.911  26.913  1.00 47.05           C  
ANISOU  902  CD  GLN A 191     6553   5783   5541   -433   -322   -140       C  
ATOM    903  OE1 GLN A 191      -1.503   2.714  27.202  1.00 46.94           O  
ANISOU  903  OE1 GLN A 191     6474   5814   5545   -470   -365   -153       O  
ATOM    904  NE2 GLN A 191       0.157   2.775  25.668  1.00 44.53           N  
ANISOU  904  NE2 GLN A 191     6310   5449   5160   -427   -323   -165       N  
ATOM    905  N   TRP A 192       4.354   0.199  28.140  1.00 44.47           N  
ANISOU  905  N   TRP A 192     6384   5200   5313   -368    -77   -138       N  
ATOM    906  CA  TRP A 192       5.707  -0.173  27.691  1.00 41.40           C  
ANISOU  906  CA  TRP A 192     6041   4769   4921   -326    -20   -148       C  
ATOM    907  C   TRP A 192       5.805  -0.958  26.388  1.00 43.92           C  
ANISOU  907  C   TRP A 192     6445   5050   5192   -345     -2   -197       C  
ATOM    908  O   TRP A 192       6.786  -0.806  25.646  1.00 46.91           O  
ANISOU  908  O   TRP A 192     6857   5418   5548   -309     43   -207       O  
ATOM    909  CB  TRP A 192       6.496  -0.876  28.810  1.00 41.11           C  
ANISOU  909  CB  TRP A 192     5992   4692   4936   -286     17   -129       C  
ATOM    910  CG  TRP A 192       6.205  -2.353  28.921  1.00 42.10           C  
ANISOU  910  CG  TRP A 192     6180   4746   5070   -309     35   -149       C  
ATOM    911  CD1 TRP A 192       5.266  -2.967  29.732  1.00 40.88           C  
ANISOU  911  CD1 TRP A 192     6025   4570   4938   -352     21   -139       C  
ATOM    912  CD2 TRP A 192       6.841  -3.453  28.174  1.00 43.25           C  
ANISOU  912  CD2 TRP A 192     6409   4821   5202   -294     83   -185       C  
ATOM    913  NE1 TRP A 192       5.298  -4.323  29.574  1.00 44.09           N  
ANISOU  913  NE1 TRP A 192     6511   4891   5348   -369     57   -163       N  
ATOM    914  CE2 TRP A 192       6.196  -4.683  28.638  1.00 44.16           C  
ANISOU  914  CE2 TRP A 192     6577   4866   5335   -333     92   -194       C  
ATOM    915  CE3 TRP A 192       7.845  -3.536  27.218  1.00 44.04           C  
ANISOU  915  CE3 TRP A 192     6550   4905   5280   -253    127   -210       C  
ATOM    916  CZ2 TRP A 192       6.548  -5.940  28.141  1.00 46.91           C  
ANISOU  916  CZ2 TRP A 192     7024   5125   5677   -329    140   -229       C  
ATOM    917  CZ3 TRP A 192       8.197  -4.806  26.713  1.00 45.01           C  
ANISOU  917  CZ3 TRP A 192     6762   4945   5393   -242    175   -247       C  
ATOM    918  CH2 TRP A 192       7.567  -5.980  27.171  1.00 47.23           C  
ANISOU  918  CH2 TRP A 192     7102   5152   5691   -278    179   -256       C  
ATOM    919  N   GLY A 193       4.821  -1.803  26.076  1.00 41.72           N  
ANISOU  919  N   GLY A 193     6203   4751   4898   -405    -32   -233       N  
ATOM    920  CA  GLY A 193       4.906  -2.598  24.842  1.00 42.65           C  
ANISOU  920  CA  GLY A 193     6413   4829   4963   -427    -17   -291       C  
ATOM    921  C   GLY A 193       4.680  -1.768  23.589  1.00 44.79           C  
ANISOU  921  C   GLY A 193     6708   5153   5156   -429    -49   -308       C  
ATOM    922  O   GLY A 193       4.922  -2.220  22.484  1.00 46.01           O  
ANISOU  922  O   GLY A 193     6947   5283   5253   -433    -32   -352       O  
ATOM    923  N   LYS A 194       4.235  -0.532  23.767  1.00 45.77           N  
ANISOU  923  N   LYS A 194     6770   5347   5275   -417    -92   -270       N  
ATOM    924  CA  LYS A 194       3.796   0.285  22.647  1.00 51.47           C  
ANISOU  924  CA  LYS A 194     7520   6121   5915   -413   -134   -277       C  
ATOM    925  C   LYS A 194       4.659   1.560  22.578  1.00 50.52           C  
ANISOU  925  C   LYS A 194     7390   6018   5787   -353    -93   -227       C  
ATOM    926  O   LYS A 194       4.388   2.579  23.239  1.00 52.93           O  
ANISOU  926  O   LYS A 194     7632   6360   6120   -335   -115   -183       O  
ATOM    927  CB  LYS A 194       2.308   0.571  22.806  1.00 53.45           C  
ANISOU  927  CB  LYS A 194     7713   6436   6159   -452   -226   -280       C  
ATOM    928  CG  LYS A 194       1.666   1.317  21.662  1.00 64.44           C  
ANISOU  928  CG  LYS A 194     9133   7892   7459   -439   -290   -289       C  
ATOM    929  CD  LYS A 194       0.163   1.330  21.889  1.00 69.68           C  
ANISOU  929  CD  LYS A 194     9721   8626   8130   -480   -385   -306       C  
ATOM    930  CE  LYS A 194      -0.553   2.195  20.866  1.00 76.36           C  
ANISOU  930  CE  LYS A 194    10580   9550   8883   -447   -464   -305       C  
ATOM    931  NZ  LYS A 194      -2.026   2.121  21.093  1.00 81.11           N  
ANISOU  931  NZ  LYS A 194    11087  10233   9500   -486   -560   -329       N  
ATOM    932  N   LEU A 195       5.728   1.472  21.800  1.00 46.45           N  
ANISOU  932  N   LEU A 195     6941   5469   5239   -326    -24   -238       N  
ATOM    933  CA  LEU A 195       6.715   2.530  21.720  1.00 43.70           C  
ANISOU  933  CA  LEU A 195     6586   5124   4894   -284     38   -199       C  
ATOM    934  C   LEU A 195       7.241   2.550  20.286  1.00 45.95           C  
ANISOU  934  C   LEU A 195     6974   5396   5091   -269     87   -220       C  
ATOM    935  O   LEU A 195       7.764   1.531  19.815  1.00 46.59           O  
ANISOU  935  O   LEU A 195     7108   5436   5159   -269    132   -262       O  
ATOM    936  CB  LEU A 195       7.842   2.238  22.706  1.00 39.68           C  
ANISOU  936  CB  LEU A 195     6018   4584   4473   -263    101   -188       C  
ATOM    937  CG  LEU A 195       9.081   3.135  22.739  1.00 41.36           C  
ANISOU  937  CG  LEU A 195     6204   4799   4712   -232    177   -162       C  
ATOM    938  CD1 LEU A 195       8.781   4.517  23.306  1.00 39.46           C  
ANISOU  938  CD1 LEU A 195     5913   4591   4489   -234    151   -118       C  
ATOM    939  CD2 LEU A 195      10.208   2.499  23.526  1.00 39.69           C  
ANISOU  939  CD2 LEU A 195     5937   4566   4578   -206    230   -170       C  
ATOM    940  N   GLN A 196       7.059   3.673  19.584  1.00 42.99           N  
ANISOU  940  N   GLN A 196     6637   5049   4650   -251     82   -190       N  
ATOM    941  CA  GLN A 196       7.700   3.864  18.302  1.00 42.50           C  
ANISOU  941  CA  GLN A 196     6678   4971   4501   -231    148   -197       C  
ATOM    942  C   GLN A 196       9.185   4.148  18.514  1.00 41.56           C  
ANISOU  942  C   GLN A 196     6533   4818   4439   -213    268   -181       C  
ATOM    943  O   GLN A 196       9.535   5.103  19.185  1.00 43.37           O  
ANISOU  943  O   GLN A 196     6699   5054   4724   -210    290   -140       O  
ATOM    944  CB  GLN A 196       7.055   4.998  17.528  1.00 45.47           C  
ANISOU  944  CB  GLN A 196     7113   5380   4783   -209    110   -161       C  
ATOM    945  CG  GLN A 196       7.724   5.251  16.175  1.00 50.48           C  
ANISOU  945  CG  GLN A 196     7872   5995   5314   -185    190   -161       C  
ATOM    946  CD  GLN A 196       7.591   4.050  15.256  1.00 57.39           C  
ANISOU  946  CD  GLN A 196     8832   6861   6111   -196    178   -228       C  
ATOM    947  OE1 GLN A 196       6.520   3.427  15.177  1.00 57.12           O  
ANISOU  947  OE1 GLN A 196     8799   6857   6047   -219     73   -267       O  
ATOM    948  NE2 GLN A 196       8.689   3.687  14.586  1.00 59.96           N  
ANISOU  948  NE2 GLN A 196     9226   7147   6411   -184    291   -248       N  
ATOM    949  N   VAL A 197      10.055   3.314  17.955  1.00 43.67           N  
ANISOU  949  N   VAL A 197     6845   5052   4695   -203    346   -219       N  
ATOM    950  CA  VAL A 197      11.498   3.509  18.109  1.00 42.16           C  
ANISOU  950  CA  VAL A 197     6614   4842   4564   -185    463   -211       C  
ATOM    951  C   VAL A 197      12.051   4.014  16.798  1.00 44.23           C  
ANISOU  951  C   VAL A 197     6976   5093   4735   -173    554   -207       C  
ATOM    952  O   VAL A 197      12.077   3.272  15.838  1.00 44.46           O  
ANISOU  952  O   VAL A 197     7101   5104   4687   -162    579   -246       O  
ATOM    953  CB  VAL A 197      12.193   2.204  18.526  1.00 42.07           C  
ANISOU  953  CB  VAL A 197     6568   4801   4615   -167    500   -253       C  
ATOM    954  CG1 VAL A 197      13.719   2.318  18.519  1.00 41.53           C  
ANISOU  954  CG1 VAL A 197     6451   4725   4602   -138    623   -254       C  
ATOM    955  CG2 VAL A 197      11.703   1.781  19.891  1.00 37.87           C  
ANISOU  955  CG2 VAL A 197     5946   4275   4168   -175    421   -246       C  
ATOM    956  N   PHE A 198      12.458   5.287  16.747  1.00 44.99           N  
ANISOU  956  N   PHE A 198     7062   5194   4836   -179    607   -160       N  
ATOM    957  CA  PHE A 198      13.135   5.808  15.568  1.00 45.93           C  
ANISOU  957  CA  PHE A 198     7278   5296   4879   -171    720   -149       C  
ATOM    958  C   PHE A 198      14.610   5.537  15.653  1.00 47.60           C  
ANISOU  958  C   PHE A 198     7427   5494   5166   -168    852   -170       C  
ATOM    959  O   PHE A 198      15.289   5.989  16.576  1.00 49.13           O  
ANISOU  959  O   PHE A 198     7500   5698   5469   -184    882   -158       O  
ATOM    960  CB  PHE A 198      12.899   7.307  15.403  1.00 47.44           C  
ANISOU  960  CB  PHE A 198     7503   5485   5036   -181    732    -87       C  
ATOM    961  CG  PHE A 198      11.471   7.648  15.125  1.00 47.27           C  
ANISOU  961  CG  PHE A 198     7551   5484   4924   -164    609    -64       C  
ATOM    962  CD1 PHE A 198      10.878   7.274  13.929  1.00 47.25           C  
ANISOU  962  CD1 PHE A 198     7680   5490   4784   -140    577    -79       C  
ATOM    963  CD2 PHE A 198      10.704   8.320  16.076  1.00 47.61           C  
ANISOU  963  CD2 PHE A 198     7524   5545   5019   -169    519    -31       C  
ATOM    964  CE1 PHE A 198       9.542   7.589  13.669  1.00 50.29           C  
ANISOU  964  CE1 PHE A 198     8113   5909   5085   -119    452    -61       C  
ATOM    965  CE2 PHE A 198       9.365   8.636  15.823  1.00 47.87           C  
ANISOU  965  CE2 PHE A 198     7606   5608   4974   -144    404    -11       C  
ATOM    966  CZ  PHE A 198       8.785   8.272  14.620  1.00 49.11           C  
ANISOU  966  CZ  PHE A 198     7882   5782   4997   -119    366    -26       C  
ATOM    967  N   ASP A 199      15.115   4.774  14.698  1.00 47.83           N  
ANISOU  967  N   ASP A 199     7534   5504   5135   -145    930   -207       N  
ATOM    968  CA  ASP A 199      16.537   4.520  14.668  1.00 50.11           C  
ANISOU  968  CA  ASP A 199     7760   5786   5491   -133   1067   -228       C  
ATOM    969  C   ASP A 199      17.257   5.717  14.046  1.00 49.33           C  
ANISOU  969  C   ASP A 199     7690   5682   5372   -158   1194   -192       C  
ATOM    970  O   ASP A 199      17.073   6.000  12.882  1.00 56.00           O  
ANISOU  970  O   ASP A 199     8676   6507   6094   -153   1245   -179       O  
ATOM    971  CB  ASP A 199      16.816   3.246  13.885  1.00 51.98           C  
ANISOU  971  CB  ASP A 199     8075   6000   5674    -92   1115   -284       C  
ATOM    972  CG  ASP A 199      18.190   2.678  14.175  1.00 55.64           C  
ANISOU  972  CG  ASP A 199     8438   6465   6236    -60   1229   -314       C  
ATOM    973  OD1 ASP A 199      19.146   3.454  14.464  1.00 56.07           O  
ANISOU  973  OD1 ASP A 199     8393   6544   6369    -77   1317   -295       O  
ATOM    974  OD2 ASP A 199      18.311   1.441  14.105  1.00 56.28           O  
ANISOU  974  OD2 ASP A 199     8540   6524   6318    -16   1230   -361       O  
ATOM    975  N   ALA A 200      18.055   6.441  14.818  1.00 47.78           N  
ANISOU  975  N   ALA A 200     7365   5500   5289   -190   1247   -176       N  
ATOM    976  CA  ALA A 200      18.826   7.536  14.244  1.00 45.19           C  
ANISOU  976  CA  ALA A 200     7060   5157   4953   -229   1386   -147       C  
ATOM    977  C   ALA A 200      20.332   7.312  14.389  1.00 47.53           C  
ANISOU  977  C   ALA A 200     7231   5474   5354   -236   1524   -182       C  
ATOM    978  O   ALA A 200      21.100   8.271  14.476  1.00 48.81           O  
ANISOU  978  O   ALA A 200     7333   5637   5575   -290   1624   -167       O  
ATOM    979  CB  ALA A 200      18.402   8.863  14.827  1.00 43.31           C  
ANISOU  979  CB  ALA A 200     6802   4910   4743   -277   1345    -97       C  
ATOM    980  N   ARG A 201      20.754   6.047  14.364  1.00 46.32           N  
ANISOU  980  N   ARG A 201     7042   5336   5223   -181   1536   -231       N  
ATOM    981  CA  ARG A 201      22.168   5.705  14.520  1.00 47.50           C  
ANISOU  981  CA  ARG A 201     7058   5516   5474   -167   1658   -269       C  
ATOM    982  C   ARG A 201      23.037   6.058  13.320  1.00 49.13           C  
ANISOU  982  C   ARG A 201     7326   5708   5633   -182   1849   -271       C  
ATOM    983  O   ARG A 201      24.271   5.917  13.361  1.00 49.58           O  
ANISOU  983  O   ARG A 201     7261   5798   5779   -178   1971   -302       O  
ATOM    984  CB  ARG A 201      22.316   4.231  14.909  1.00 48.85           C  
ANISOU  984  CB  ARG A 201     7180   5699   5683    -88   1610   -316       C  
ATOM    985  CG  ARG A 201      21.749   3.959  16.309  1.00 48.55           C  
ANISOU  985  CG  ARG A 201     7043   5681   5721    -79   1448   -312       C  
ATOM    986  CD  ARG A 201      21.824   2.492  16.673  1.00 47.86           C  
ANISOU  986  CD  ARG A 201     6936   5589   5661      2   1405   -350       C  
ATOM    987  NE  ARG A 201      20.971   1.661  15.833  1.00 46.86           N  
ANISOU  987  NE  ARG A 201     6980   5408   5417     28   1377   -365       N  
ATOM    988  CZ  ARG A 201      21.159   0.351  15.647  1.00 47.69           C  
ANISOU  988  CZ  ARG A 201     7122   5483   5513     97   1393   -407       C  
ATOM    989  NH1 ARG A 201      22.157  -0.275  16.259  1.00 46.98           N  
ANISOU  989  NH1 ARG A 201     6909   5416   5525    163   1435   -429       N  
ATOM    990  NH2 ARG A 201      20.353  -0.342  14.847  1.00 46.02           N  
ANISOU  990  NH2 ARG A 201     7075   5221   5191    105   1366   -430       N  
ATOM    991  N   ASP A 202      22.398   6.541  12.259  1.00 48.91           N  
ANISOU  991  N   ASP A 202     7485   5636   5464   -196   1876   -236       N  
ATOM    992  CA  ASP A 202      23.130   7.058  11.089  1.00 51.54           C  
ANISOU  992  CA  ASP A 202     7904   5947   5733   -218   2067   -224       C  
ATOM    993  C   ASP A 202      23.438   8.570  11.180  1.00 49.73           C  
ANISOU  993  C   ASP A 202     7655   5702   5540   -307   2146   -174       C  
ATOM    994  O   ASP A 202      24.119   9.121  10.339  1.00 49.35           O  
ANISOU  994  O   ASP A 202     7663   5630   5456   -341   2318   -159       O  
ATOM    995  CB  ASP A 202      22.351   6.759   9.800  1.00 53.28           C  
ANISOU  995  CB  ASP A 202     8358   6126   5762   -179   2067   -212       C  
ATOM    996  CG  ASP A 202      21.030   7.518   9.717  1.00 55.21           C  
ANISOU  996  CG  ASP A 202     8727   6345   5905   -196   1938   -156       C  
ATOM    997  OD1 ASP A 202      20.636   8.219  10.677  1.00 55.35           O  
ANISOU  997  OD1 ASP A 202     8659   6370   6000   -234   1845   -126       O  
ATOM    998  OD2 ASP A 202      20.374   7.406   8.675  1.00 59.34           O  
ANISOU  998  OD2 ASP A 202     9436   6844   6266   -165   1927   -144       O  
ATOM    999  N   CYS A 203      22.921   9.229  12.208  1.00 49.36           N  
ANISOU  999  N   CYS A 203     7535   5659   5560   -346   2026   -151       N  
ATOM   1000  CA  CYS A 203      23.039  10.675  12.337  1.00 50.28           C  
ANISOU 1000  CA  CYS A 203     7658   5744   5703   -431   2085   -105       C  
ATOM   1001  C   CYS A 203      24.476  11.186  12.441  1.00 50.65           C  
ANISOU 1001  C   CYS A 203     7565   5808   5871   -504   2259   -130       C  
ATOM   1002  O   CYS A 203      25.258  10.691  13.242  1.00 53.22           O  
ANISOU 1002  O   CYS A 203     7694   6196   6330   -505   2252   -184       O  
ATOM   1003  CB  CYS A 203      22.259  11.114  13.555  1.00 50.18           C  
ANISOU 1003  CB  CYS A 203     7575   5738   5752   -449   1917    -91       C  
ATOM   1004  SG  CYS A 203      22.123  12.888  13.605  1.00 54.20           S  
ANISOU 1004  SG  CYS A 203     8147   6184   6263   -539   1973    -30       S  
ATOM   1005  N   SER A 204      24.842  12.182  11.651  1.00 51.18           N  
ANISOU 1005  N   SER A 204     7730   5823   5894   -568   2417    -91       N  
ATOM   1006  CA  SER A 204      26.241  12.588  11.654  1.00 53.71           C  
ANISOU 1006  CA  SER A 204     7912   6163   6331   -648   2600   -123       C  
ATOM   1007  C   SER A 204      26.449  14.090  11.784  1.00 55.49           C  
ANISOU 1007  C   SER A 204     8155   6332   6598   -766   2688    -85       C  
ATOM   1008  O   SER A 204      27.570  14.578  11.647  1.00 58.04           O  
ANISOU 1008  O   SER A 204     8385   6660   7008   -853   2861   -108       O  
ATOM   1009  CB  SER A 204      26.969  12.042  10.414  1.00 56.29           C  
ANISOU 1009  CB  SER A 204     8308   6491   6590   -616   2784   -135       C  
ATOM   1010  OG  SER A 204      26.261  12.374   9.244  1.00 58.52           O  
ANISOU 1010  OG  SER A 204     8848   6699   6688   -592   2828    -73       O  
ATOM   1011  N   SER A 205      25.380  14.835  12.034  1.00 54.92           N  
ANISOU 1011  N   SER A 205     8201   6201   6465   -771   2578    -31       N  
ATOM   1012  CA  SER A 205      25.555  16.259  12.282  1.00 55.66           C  
ANISOU 1012  CA  SER A 205     8313   6228   6607   -881   2654      1       C  
ATOM   1013  C   SER A 205      24.588  16.783  13.316  1.00 53.80           C  
ANISOU 1013  C   SER A 205     8072   5974   6394   -881   2473     19       C  
ATOM   1014  O   SER A 205      23.517  16.206  13.539  1.00 55.28           O  
ANISOU 1014  O   SER A 205     8310   6181   6513   -788   2299     33       O  
ATOM   1015  CB  SER A 205      25.475  17.084  10.975  1.00 57.60           C  
ANISOU 1015  CB  SER A 205     8796   6374   6717   -903   2821     76       C  
ATOM   1016  OG  SER A 205      24.136  17.396  10.613  1.00 55.68           O  
ANISOU 1016  OG  SER A 205     8764   6071   6321   -830   2708    149       O  
ATOM   1017  N   ALA A 206      24.972  17.886  13.947  1.00 53.68           N  
ANISOU 1017  N   ALA A 206     7998   5921   6478   -990   2521     13       N  
ATOM   1018  CA  ALA A 206      24.031  18.676  14.744  1.00 51.65           C  
ANISOU 1018  CA  ALA A 206     7788   5617   6222   -996   2389     43       C  
ATOM   1019  C   ALA A 206      22.751  19.043  13.953  1.00 51.60           C  
ANISOU 1019  C   ALA A 206     8035   5531   6039   -913   2341    135       C  
ATOM   1020  O   ALA A 206      21.653  18.911  14.481  1.00 48.55           O  
ANISOU 1020  O   ALA A 206     7675   5156   5616   -843   2165    152       O  
ATOM   1021  CB  ALA A 206      24.715  19.914  15.298  1.00 51.98           C  
ANISOU 1021  CB  ALA A 206     7767   5605   6378  -1137   2488     24       C  
ATOM   1022  N   GLN A 207      22.903  19.495  12.699  1.00 55.61           N  
ANISOU 1022  N   GLN A 207     8726   5966   6438   -918   2499    192       N  
ATOM   1023  CA  GLN A 207      21.772  19.808  11.806  1.00 56.59           C  
ANISOU 1023  CA  GLN A 207     9099   6025   6377   -827   2460    280       C  
ATOM   1024  C   GLN A 207      20.839  18.602  11.648  1.00 55.99           C  
ANISOU 1024  C   GLN A 207     9038   6027   6208   -700   2283    272       C  
ATOM   1025  O   GLN A 207      19.605  18.725  11.778  1.00 53.90           O  
ANISOU 1025  O   GLN A 207     8862   5755   5863   -623   2130    312       O  
ATOM   1026  CB  GLN A 207      22.286  20.249  10.429  1.00 62.21           C  
ANISOU 1026  CB  GLN A 207     9993   6663   6981   -847   2672    334       C  
ATOM   1027  CG  GLN A 207      21.197  20.442   9.373  1.00 67.02           C  
ANISOU 1027  CG  GLN A 207    10866   7221   7377   -735   2632    424       C  
ATOM   1028  CD  GLN A 207      20.244  21.594   9.713  1.00 75.48           C  
ANISOU 1028  CD  GLN A 207    12060   8207   8411   -713   2557    495       C  
ATOM   1029  OE1 GLN A 207      20.643  22.772   9.728  1.00 73.34           O  
ANISOU 1029  OE1 GLN A 207    11860   7831   8176   -795   2694    533       O  
ATOM   1030  NE2 GLN A 207      18.974  21.255   9.999  1.00 74.38           N  
ANISOU 1030  NE2 GLN A 207    11945   8111   8206   -604   2344    509       N  
ATOM   1031  N   GLU A 208      21.434  17.437  11.383  1.00 53.49           N  
ANISOU 1031  N   GLU A 208     8632   5784   5907   -680   2308    216       N  
ATOM   1032  CA  GLU A 208      20.661  16.232  11.246  1.00 55.21           C  
ANISOU 1032  CA  GLU A 208     8861   6068   6050   -577   2157    195       C  
ATOM   1033  C   GLU A 208      19.945  15.847  12.564  1.00 53.81           C  
ANISOU 1033  C   GLU A 208     8544   5944   5959   -554   1951    163       C  
ATOM   1034  O   GLU A 208      18.836  15.306  12.523  1.00 56.97           O  
ANISOU 1034  O   GLU A 208     9000   6369   6276   -474   1798    173       O  
ATOM   1035  CB  GLU A 208      21.511  15.091  10.693  1.00 57.49           C  
ANISOU 1035  CB  GLU A 208     9094   6409   6341   -560   2243    140       C  
ATOM   1036  CG  GLU A 208      20.681  13.906  10.219  1.00 60.46           C  
ANISOU 1036  CG  GLU A 208     9544   6827   6602   -457   2117    124       C  
ATOM   1037  CD  GLU A 208      21.490  12.834   9.488  1.00 67.52           C  
ANISOU 1037  CD  GLU A 208    10428   7754   7473   -430   2223     73       C  
ATOM   1038  OE1 GLU A 208      22.746  12.963   9.411  1.00 72.73           O  
ANISOU 1038  OE1 GLU A 208    10996   8416   8220   -487   2395     48       O  
ATOM   1039  OE2 GLU A 208      20.868  11.852   8.987  1.00 63.48           O  
ANISOU 1039  OE2 GLU A 208     9997   7266   6858   -354   2137     53       O  
ATOM   1040  N   MET A 209      20.549  16.116  13.723  1.00 50.59           N  
ANISOU 1040  N   MET A 209     7955   5556   5711   -624   1947    122       N  
ATOM   1041  CA  MET A 209      19.866  15.804  14.990  1.00 49.55           C  
ANISOU 1041  CA  MET A 209     7706   5471   5650   -600   1761     97       C  
ATOM   1042  C   MET A 209      18.587  16.609  15.068  1.00 47.27           C  
ANISOU 1042  C   MET A 209     7545   5133   5281   -564   1661    159       C  
ATOM   1043  O   MET A 209      17.556  16.102  15.512  1.00 44.94           O  
ANISOU 1043  O   MET A 209     7239   4876   4959   -500   1498    158       O  
ATOM   1044  CB  MET A 209      20.721  16.119  16.210  1.00 50.04           C  
ANISOU 1044  CB  MET A 209     7571   5561   5882   -682   1773     45       C  
ATOM   1045  CG  MET A 209      21.999  15.315  16.305  1.00 53.30           C  
ANISOU 1045  CG  MET A 209     7822   6040   6391   -707   1854    -22       C  
ATOM   1046  SD  MET A 209      23.025  15.835  17.695  1.00 57.27           S  
ANISOU 1046  SD  MET A 209     8092   6585   7084   -808   1862    -87       S  
ATOM   1047  CE  MET A 209      22.050  15.252  19.091  1.00 48.14           C  
ANISOU 1047  CE  MET A 209     6853   5482   5956   -742   1627   -103       C  
ATOM   1048  N   PHE A 210      18.670  17.849  14.583  1.00 48.35           N  
ANISOU 1048  N   PHE A 210     7808   5184   5379   -603   1769    214       N  
ATOM   1049  CA  PHE A 210      17.552  18.766  14.576  1.00 47.98           C  
ANISOU 1049  CA  PHE A 210     7897   5078   5255   -561   1698    280       C  
ATOM   1050  C   PHE A 210      16.390  18.215  13.781  1.00 47.04           C  
ANISOU 1050  C   PHE A 210     7909   4984   4980   -447   1588    318       C  
ATOM   1051  O   PHE A 210      15.276  18.187  14.299  1.00 45.83           O  
ANISOU 1051  O   PHE A 210     7749   4855   4807   -388   1432    330       O  
ATOM   1052  CB  PHE A 210      17.956  20.157  14.055  1.00 49.93           C  
ANISOU 1052  CB  PHE A 210     8282   5212   5478   -618   1859    338       C  
ATOM   1053  CG  PHE A 210      16.836  21.165  14.106  1.00 52.10           C  
ANISOU 1053  CG  PHE A 210     8700   5416   5678   -562   1791    410       C  
ATOM   1054  CD1 PHE A 210      16.170  21.434  15.311  1.00 52.27           C  
ANISOU 1054  CD1 PHE A 210     8635   5452   5774   -552   1657    394       C  
ATOM   1055  CD2 PHE A 210      16.434  21.848  12.961  1.00 53.73           C  
ANISOU 1055  CD2 PHE A 210     9134   5544   5735   -509   1862    495       C  
ATOM   1056  CE1 PHE A 210      15.129  22.365  15.371  1.00 53.66           C  
ANISOU 1056  CE1 PHE A 210     8938   5564   5885   -488   1598    459       C  
ATOM   1057  CE2 PHE A 210      15.396  22.786  13.016  1.00 55.17           C  
ANISOU 1057  CE2 PHE A 210     9450   5663   5850   -439   1796    565       C  
ATOM   1058  CZ  PHE A 210      14.741  23.043  14.218  1.00 55.24           C  
ANISOU 1058  CZ  PHE A 210     9361   5687   5942   -427   1665    546       C  
ATOM   1059  N   THR A 211      16.648  17.795  12.534  1.00 48.55           N  
ANISOU 1059  N   THR A 211     8215   5173   5059   -419   1671    332       N  
ATOM   1060  CA  THR A 211      15.622  17.150  11.685  1.00 48.90           C  
ANISOU 1060  CA  THR A 211     8381   5253   4945   -316   1565    352       C  
ATOM   1061  C   THR A 211      15.023  15.918  12.355  1.00 47.79           C  
ANISOU 1061  C   THR A 211     8109   5203   4845   -282   1394    291       C  
ATOM   1062  O   THR A 211      13.791  15.815  12.517  1.00 48.97           O  
ANISOU 1062  O   THR A 211     8284   5383   4940   -218   1238    306       O  
ATOM   1063  CB  THR A 211      16.160  16.777  10.302  1.00 52.02           C  
ANISOU 1063  CB  THR A 211     8910   5637   5219   -300   1691    361       C  
ATOM   1064  OG1 THR A 211      16.824  17.911   9.754  1.00 55.97           O  
ANISOU 1064  OG1 THR A 211     9525   6045   5695   -347   1872    418       O  
ATOM   1065  CG2 THR A 211      15.019  16.363   9.357  1.00 49.97           C  
ANISOU 1065  CG2 THR A 211     8807   5405   4773   -196   1576    387       C  
ATOM   1066  N   TYR A 212      15.885  15.006  12.793  1.00 46.27           N  
ANISOU 1066  N   TYR A 212     7771   5052   4757   -323   1427    223       N  
ATOM   1067  CA  TYR A 212      15.420  13.879  13.615  1.00 44.64           C  
ANISOU 1067  CA  TYR A 212     7434   4917   4611   -300   1280    167       C  
ATOM   1068  C   TYR A 212      14.518  14.294  14.767  1.00 43.19           C  
ANISOU 1068  C   TYR A 212     7176   4747   4488   -293   1141    179       C  
ATOM   1069  O   TYR A 212      13.430  13.726  14.942  1.00 43.51           O  
ANISOU 1069  O   TYR A 212     7215   4829   4489   -243    996    172       O  
ATOM   1070  CB  TYR A 212      16.598  13.052  14.121  1.00 44.94           C  
ANISOU 1070  CB  TYR A 212     7316   4988   4772   -341   1346    101       C  
ATOM   1071  CG  TYR A 212      17.037  11.968  13.157  1.00 45.93           C  
ANISOU 1071  CG  TYR A 212     7490   5130   4830   -310   1407     65       C  
ATOM   1072  CD1 TYR A 212      16.148  10.953  12.773  1.00 45.89           C  
ANISOU 1072  CD1 TYR A 212     7545   5155   4736   -251   1293     43       C  
ATOM   1073  CD2 TYR A 212      18.338  11.953  12.622  1.00 47.35           C  
ANISOU 1073  CD2 TYR A 212     7657   5296   5037   -344   1585     48       C  
ATOM   1074  CE1 TYR A 212      16.528   9.966  11.882  1.00 47.08           C  
ANISOU 1074  CE1 TYR A 212     7756   5312   4819   -223   1350      4       C  
ATOM   1075  CE2 TYR A 212      18.735  10.948  11.737  1.00 48.32           C  
ANISOU 1075  CE2 TYR A 212     7832   5433   5096   -307   1648     12       C  
ATOM   1076  CZ  TYR A 212      17.826   9.957  11.378  1.00 49.12           C  
ANISOU 1076  CZ  TYR A 212     8006   5555   5103   -246   1529    -11       C  
ATOM   1077  OH  TYR A 212      18.195   8.952  10.500  1.00 54.56           O  
ANISOU 1077  OH  TYR A 212     8761   6249   5722   -210   1591    -53       O  
ATOM   1078  N   ILE A 213      14.937  15.295  15.544  1.00 44.26           N  
ANISOU 1078  N   ILE A 213     7253   4846   4719   -347   1188    193       N  
ATOM   1079  CA  ILE A 213      14.132  15.726  16.706  1.00 43.09           C  
ANISOU 1079  CA  ILE A 213     7036   4707   4630   -340   1067    200       C  
ATOM   1080  C   ILE A 213      12.760  16.289  16.242  1.00 43.28           C  
ANISOU 1080  C   ILE A 213     7194   4716   4535   -264    976    261       C  
ATOM   1081  O   ILE A 213      11.711  15.985  16.829  1.00 41.63           O  
ANISOU 1081  O   ILE A 213     6939   4551   4328   -222    834    256       O  
ATOM   1082  CB  ILE A 213      14.935  16.707  17.601  1.00 45.57           C  
ANISOU 1082  CB  ILE A 213     7269   4980   5064   -419   1143    192       C  
ATOM   1083  CG1 ILE A 213      16.094  15.995  18.328  1.00 43.25           C  
ANISOU 1083  CG1 ILE A 213     6800   4735   4899   -476   1178    122       C  
ATOM   1084  CG2 ILE A 213      14.056  17.420  18.622  1.00 42.48           C  
ANISOU 1084  CG2 ILE A 213     6855   4579   4708   -405   1040    210       C  
ATOM   1085  CD1 ILE A 213      17.057  16.972  18.974  1.00 42.38           C  
ANISOU 1085  CD1 ILE A 213     6615   4589   4897   -569   1272    104       C  
ATOM   1086  N   CYS A 214      12.774  17.063  15.152  1.00 44.74           N  
ANISOU 1086  N   CYS A 214     7545   4841   4612   -243   1061    318       N  
ATOM   1087  CA  CYS A 214      11.556  17.649  14.599  1.00 46.06           C  
ANISOU 1087  CA  CYS A 214     7849   4996   4655   -156    982    381       C  
ATOM   1088  C   CYS A 214      10.632  16.562  14.100  1.00 45.79           C  
ANISOU 1088  C   CYS A 214     7826   5043   4529    -90    849    359       C  
ATOM   1089  O   CYS A 214       9.434  16.591  14.365  1.00 45.33           O  
ANISOU 1089  O   CYS A 214     7758   5025   4439    -30    710    372       O  
ATOM   1090  CB  CYS A 214      11.879  18.614  13.462  1.00 50.53           C  
ANISOU 1090  CB  CYS A 214     8607   5478   5112   -142   1113    450       C  
ATOM   1091  SG  CYS A 214      12.468  20.221  14.023  1.00 57.75           S  
ANISOU 1091  SG  CYS A 214     9556   6277   6111   -206   1243    494       S  
ATOM   1092  N   ASN A 215      11.194  15.587  13.396  1.00 44.92           N  
ANISOU 1092  N   ASN A 215     7729   4958   4381   -104    893    319       N  
ATOM   1093  CA  ASN A 215      10.429  14.401  13.045  1.00 47.94           C  
ANISOU 1093  CA  ASN A 215     8104   5414   4697    -63    770    277       C  
ATOM   1094  C   ASN A 215       9.788  13.679  14.261  1.00 47.93           C  
ANISOU 1094  C   ASN A 215     7939   5472   4801    -74    634    230       C  
ATOM   1095  O   ASN A 215       8.616  13.263  14.209  1.00 47.08           O  
ANISOU 1095  O   ASN A 215     7828   5419   4640    -30    495    221       O  
ATOM   1096  CB  ASN A 215      11.267  13.471  12.164  1.00 48.65           C  
ANISOU 1096  CB  ASN A 215     8238   5508   4740    -82    859    235       C  
ATOM   1097  CG  ASN A 215      11.382  13.991  10.728  1.00 53.04           C  
ANISOU 1097  CG  ASN A 215     8993   6026   5132    -42    945    284       C  
ATOM   1098  OD1 ASN A 215      10.773  15.009  10.378  1.00 56.55           O  
ANISOU 1098  OD1 ASN A 215     9550   6444   5494      7    926    353       O  
ATOM   1099  ND2 ASN A 215      12.136  13.292   9.895  1.00 51.49           N  
ANISOU 1099  ND2 ASN A 215     8853   5827   4883    -54   1041    250       N  
ATOM   1100  N   HIS A 216      10.540  13.577  15.359  1.00 46.39           N  
ANISOU 1100  N   HIS A 216     7606   5267   4751   -133    675    201       N  
ATOM   1101  CA  HIS A 216      10.035  12.950  16.585  1.00 44.40           C  
ANISOU 1101  CA  HIS A 216     7210   5063   4598   -145    565    164       C  
ATOM   1102  C   HIS A 216       8.830  13.697  17.095  1.00 44.87           C  
ANISOU 1102  C   HIS A 216     7265   5136   4648   -104    460    202       C  
ATOM   1103  O   HIS A 216       7.767  13.093  17.325  1.00 40.38           O  
ANISOU 1103  O   HIS A 216     6655   4624   4064    -77    335    184       O  
ATOM   1104  CB  HIS A 216      11.127  12.950  17.636  1.00 44.96           C  
ANISOU 1104  CB  HIS A 216     7153   5119   4811   -205    635    136       C  
ATOM   1105  CG  HIS A 216      10.749  12.272  18.917  1.00 46.81           C  
ANISOU 1105  CG  HIS A 216     7250   5397   5140   -213    537    101       C  
ATOM   1106  ND1 HIS A 216      11.465  11.262  19.428  1.00 44.92           N  
ANISOU 1106  ND1 HIS A 216     6915   5177   4975   -237    552     53       N  
ATOM   1107  CD2 HIS A 216       9.700  12.500  19.804  1.00 47.09           C  
ANISOU 1107  CD2 HIS A 216     7234   5456   5200   -195    428    113       C  
ATOM   1108  CE1 HIS A 216      10.915  10.863  20.578  1.00 44.79           C  
ANISOU 1108  CE1 HIS A 216     6803   5192   5024   -236    459     38       C  
ATOM   1109  NE2 HIS A 216       9.838  11.624  20.814  1.00 46.37           N  
ANISOU 1109  NE2 HIS A 216     7026   5396   5196   -215    387     73       N  
ATOM   1110  N   ILE A 217       8.994  15.018  17.257  1.00 44.50           N  
ANISOU 1110  N   ILE A 217     7263   5035   4612   -102    518    252       N  
ATOM   1111  CA  ILE A 217       7.974  15.881  17.850  1.00 43.68           C  
ANISOU 1111  CA  ILE A 217     7154   4930   4511    -57    439    291       C  
ATOM   1112  C   ILE A 217       6.687  15.831  17.028  1.00 45.98           C  
ANISOU 1112  C   ILE A 217     7527   5267   4677     29    332    318       C  
ATOM   1113  O   ILE A 217       5.603  15.681  17.590  1.00 43.85           O  
ANISOU 1113  O   ILE A 217     7187   5051   4421     64    213    313       O  
ATOM   1114  CB  ILE A 217       8.490  17.337  18.015  1.00 44.10           C  
ANISOU 1114  CB  ILE A 217     7271   4895   4588    -71    542    338       C  
ATOM   1115  CG1 ILE A 217       9.550  17.385  19.123  1.00 44.98           C  
ANISOU 1115  CG1 ILE A 217     7263   4985   4842   -159    610    296       C  
ATOM   1116  CG2 ILE A 217       7.348  18.300  18.341  1.00 41.27           C  
ANISOU 1116  CG2 ILE A 217     6951   4526   4204      2    469    388       C  
ATOM   1117  CD1 ILE A 217      10.476  18.587  19.069  1.00 43.67           C  
ANISOU 1117  CD1 ILE A 217     7158   4727   4707   -211    749    321       C  
ATOM   1118  N   LYS A 218       6.838  15.931  15.699  1.00 49.08           N  
ANISOU 1118  N   LYS A 218     8061   5642   4944     61    375    345       N  
ATOM   1119  CA  LYS A 218       5.744  15.816  14.738  1.00 49.82           C  
ANISOU 1119  CA  LYS A 218     8243   5787   4897    144    271    365       C  
ATOM   1120  C   LYS A 218       5.008  14.488  14.903  1.00 47.70           C  
ANISOU 1120  C   LYS A 218     7874   5612   4637    134    143    297       C  
ATOM   1121  O   LYS A 218       3.795  14.463  15.051  1.00 48.44           O  
ANISOU 1121  O   LYS A 218     7928   5771   4706    183     14    298       O  
ATOM   1122  CB  LYS A 218       6.268  15.938  13.302  1.00 54.16           C  
ANISOU 1122  CB  LYS A 218     8964   6303   5310    167    355    392       C  
ATOM   1123  CG  LYS A 218       6.683  17.339  12.872  1.00 59.25           C  
ANISOU 1123  CG  LYS A 218     9752   6855   5905    197    470    475       C  
ATOM   1124  CD  LYS A 218       6.540  17.543  11.360  1.00 64.50           C  
ANISOU 1124  CD  LYS A 218    10613   7512   6384    268    491    520       C  
ATOM   1125  CE  LYS A 218       7.755  17.105  10.544  1.00 64.81           C  
ANISOU 1125  CE  LYS A 218    10729   7511   6384    210    639    501       C  
ATOM   1126  NZ  LYS A 218       8.660  18.249  10.242  1.00 69.77           N  
ANISOU 1126  NZ  LYS A 218    11477   8028   7006    189    817    568       N  
ATOM   1127  N   TYR A 219       5.742  13.381  14.882  1.00 46.24           N  
ANISOU 1127  N   TYR A 219     7647   5432   4491     68    183    237       N  
ATOM   1128  CA  TYR A 219       5.106  12.074  15.022  1.00 45.94           C  
ANISOU 1128  CA  TYR A 219     7529   5463   4462     47     77    169       C  
ATOM   1129  C   TYR A 219       4.473  11.890  16.405  1.00 43.89           C  
ANISOU 1129  C   TYR A 219     7115   5238   4324     26      0    152       C  
ATOM   1130  O   TYR A 219       3.329  11.441  16.511  1.00 43.97           O  
ANISOU 1130  O   TYR A 219     7073   5316   4319     41   -122    129       O  
ATOM   1131  CB  TYR A 219       6.096  10.942  14.716  1.00 47.78           C  
ANISOU 1131  CB  TYR A 219     7765   5677   4711     -9    152    111       C  
ATOM   1132  CG  TYR A 219       5.517   9.564  14.948  1.00 48.31           C  
ANISOU 1132  CG  TYR A 219     7760   5794   4801    -40     58     39       C  
ATOM   1133  CD1 TYR A 219       5.490   9.025  16.223  1.00 46.63           C  
ANISOU 1133  CD1 TYR A 219     7409   5587   4720    -83     35     12       C  
ATOM   1134  CD2 TYR A 219       4.957   8.817  13.900  1.00 49.58           C  
ANISOU 1134  CD2 TYR A 219     7998   5994   4846    -30     -8     -4       C  
ATOM   1135  CE1 TYR A 219       4.945   7.782  16.465  1.00 47.24           C  
ANISOU 1135  CE1 TYR A 219     7430   5696   4821   -118    -39    -49       C  
ATOM   1136  CE2 TYR A 219       4.412   7.556  14.130  1.00 48.83           C  
ANISOU 1136  CE2 TYR A 219     7841   5934   4778    -73    -87    -76       C  
ATOM   1137  CZ  TYR A 219       4.419   7.046  15.431  1.00 47.18           C  
ANISOU 1137  CZ  TYR A 219     7497   5719   4710   -118    -96    -95       C  
ATOM   1138  OH  TYR A 219       3.912   5.816  15.743  1.00 47.69           O  
ANISOU 1138  OH  TYR A 219     7507   5802   4810   -167   -158   -160       O  
ATOM   1139  N   ALA A 220       5.191  12.279  17.453  1.00 41.24           N  
ANISOU 1139  N   ALA A 220     6707   4859   4105     -9     70    162       N  
ATOM   1140  CA  ALA A 220       4.749  11.979  18.826  1.00 41.15           C  
ANISOU 1140  CA  ALA A 220     6554   4874   4206    -34     12    142       C  
ATOM   1141  C   ALA A 220       3.528  12.815  19.211  1.00 41.10           C  
ANISOU 1141  C   ALA A 220     6524   4902   4189     23    -74    179       C  
ATOM   1142  O   ALA A 220       2.683  12.353  19.966  1.00 38.80           O  
ANISOU 1142  O   ALA A 220     6133   4663   3947     16   -156    156       O  
ATOM   1143  CB  ALA A 220       5.892  12.183  19.826  1.00 38.19           C  
ANISOU 1143  CB  ALA A 220     6114   4450   3946    -83    105    138       C  
ATOM   1144  N   THR A 221       3.443  14.033  18.668  1.00 42.20           N  
ANISOU 1144  N   THR A 221     6762   5009   4263     81    -47    238       N  
ATOM   1145  CA  THR A 221       2.406  14.995  19.043  1.00 42.88           C  
ANISOU 1145  CA  THR A 221     6837   5114   4342    153   -111    282       C  
ATOM   1146  C   THR A 221       1.127  14.631  18.339  1.00 44.25           C  
ANISOU 1146  C   THR A 221     7011   5375   4424    212   -238    275       C  
ATOM   1147  O   THR A 221       0.030  14.678  18.921  1.00 43.03           O  
ANISOU 1147  O   THR A 221     6766   5283   4299    246   -330    272       O  
ATOM   1148  CB  THR A 221       2.784  16.441  18.643  1.00 45.31           C  
ANISOU 1148  CB  THR A 221     7270   5342   4604    203    -29    351       C  
ATOM   1149  OG1 THR A 221       4.079  16.767  19.168  1.00 45.19           O  
ANISOU 1149  OG1 THR A 221     7254   5246   4671    131     96    347       O  
ATOM   1150  CG2 THR A 221       1.734  17.439  19.160  1.00 43.78           C  
ANISOU 1150  CG2 THR A 221     7062   5158   4414    287    -89    395       C  
ATOM   1151  N   ASN A 222       1.280  14.310  17.055  1.00 44.23           N  
ANISOU 1151  N   ASN A 222     7116   5383   4309    227   -241    271       N  
ATOM   1152  CA  ASN A 222       0.197  13.758  16.283  1.00 44.17           C  
ANISOU 1152  CA  ASN A 222     7108   5468   4207    266   -369    246       C  
ATOM   1153  C   ASN A 222      -1.067  14.598  16.459  1.00 47.27           C  
ANISOU 1153  C   ASN A 222     7467   5918   4575    364   -468    287       C  
ATOM   1154  O   ASN A 222      -2.172  14.055  16.678  1.00 47.64           O  
ANISOU 1154  O   ASN A 222     7404   6063   4635    370   -587    248       O  
ATOM   1155  CB  ASN A 222      -0.044  12.305  16.695  1.00 43.57           C  
ANISOU 1155  CB  ASN A 222     6916   5444   4193    182   -424    162       C  
ATOM   1156  CG  ASN A 222      -1.023  11.603  15.775  1.00 43.48           C  
ANISOU 1156  CG  ASN A 222     6912   5526   4082    198   -549    117       C  
ATOM   1157  OD1 ASN A 222      -1.146  11.960  14.609  1.00 42.26           O  
ANISOU 1157  OD1 ASN A 222     6878   5388   3793    260   -575    139       O  
ATOM   1158  ND2 ASN A 222      -1.716  10.606  16.294  1.00 42.36           N  
ANISOU 1158  ND2 ASN A 222     6647   5445   4002    138   -625     53       N  
ATOM   1159  N   ARG A 223      -0.875  15.923  16.356  1.00 48.77           N  
ANISOU 1159  N   ARG A 223     7753   6045   4734    440   -410    364       N  
ATOM   1160  CA  ARG A 223      -1.922  16.951  16.531  1.00 53.00           C  
ANISOU 1160  CA  ARG A 223     8282   6610   5245    556   -478    418       C  
ATOM   1161  C   ARG A 223      -2.774  16.830  17.827  1.00 51.24           C  
ANISOU 1161  C   ARG A 223     7883   6445   5142    549   -540    392       C  
ATOM   1162  O   ARG A 223      -3.932  17.196  17.828  1.00 56.81           O  
ANISOU 1162  O   ARG A 223     8539   7226   5822    640   -638    408       O  
ATOM   1163  CB  ARG A 223      -2.829  17.037  15.294  1.00 57.74           C  
ANISOU 1163  CB  ARG A 223     8955   7293   5692    661   -592    437       C  
ATOM   1164  CG  ARG A 223      -2.116  17.416  13.993  1.00 67.03           C  
ANISOU 1164  CG  ARG A 223    10334   8408   6726    698   -527    482       C  
ATOM   1165  CD  ARG A 223      -3.066  17.329  12.803  1.00 79.41           C  
ANISOU 1165  CD  ARG A 223    11964  10077   8132    800   -662    488       C  
ATOM   1166  NE  ARG A 223      -4.296  18.079  13.081  1.00 94.19           N  
ANISOU 1166  NE  ARG A 223    13777  12017   9995    926   -770    528       N  
ATOM   1167  CZ  ARG A 223      -5.474  17.536  13.400  1.00 95.20           C  
ANISOU 1167  CZ  ARG A 223    13738  12278  10153    940   -916    475       C  
ATOM   1168  NH1 ARG A 223      -5.620  16.215  13.461  1.00 93.59           N  
ANISOU 1168  NH1 ARG A 223    13422  12149   9988    828   -974    379       N  
ATOM   1169  NH2 ARG A 223      -6.513  18.324  13.654  1.00 91.84           N  
ANISOU 1169  NH2 ARG A 223    13261  11911   9724   1067   -997    517       N  
ATOM   1170  N   GLY A 224      -2.201  16.328  18.916  1.00 47.96           N  
ANISOU 1170  N   GLY A 224     7374   5996   4852    448   -481    353       N  
ATOM   1171  CA  GLY A 224      -2.936  16.202  20.160  1.00 45.79           C  
ANISOU 1171  CA  GLY A 224     6947   5768   4682    438   -522    331       C  
ATOM   1172  C   GLY A 224      -3.172  14.768  20.580  1.00 46.13           C  
ANISOU 1172  C   GLY A 224     6864   5877   4787    341   -570    255       C  
ATOM   1173  O   GLY A 224      -3.383  14.487  21.754  1.00 44.99           O  
ANISOU 1173  O   GLY A 224     6607   5744   4744    299   -563    233       O  
ATOM   1174  N   ASN A 225      -3.139  13.857  19.621  1.00 46.39           N  
ANISOU 1174  N   ASN A 225     6927   5946   4752    306   -612    215       N  
ATOM   1175  CA  ASN A 225      -3.407  12.454  19.898  1.00 48.22           C  
ANISOU 1175  CA  ASN A 225     7058   6229   5033    211   -655    141       C  
ATOM   1176  C   ASN A 225      -2.080  11.697  20.100  1.00 47.39           C  
ANISOU 1176  C   ASN A 225     6989   6043   4974    118   -555    113       C  
ATOM   1177  O   ASN A 225      -1.601  10.981  19.231  1.00 46.73           O  
ANISOU 1177  O   ASN A 225     6974   5949   4833     82   -546     80       O  
ATOM   1178  CB  ASN A 225      -4.270  11.855  18.783  1.00 47.17           C  
ANISOU 1178  CB  ASN A 225     6929   6191   4803    224   -771    100       C  
ATOM   1179  CG  ASN A 225      -4.576  10.392  19.019  1.00 50.49           C  
ANISOU 1179  CG  ASN A 225     7258   6654   5274    115   -811     16       C  
ATOM   1180  OD1 ASN A 225      -4.550   9.927  20.159  1.00 54.22           O  
ANISOU 1180  OD1 ASN A 225     7634   7109   5860     51   -775     -1       O  
ATOM   1181  ND2 ASN A 225      -4.849   9.650  17.949  1.00 52.01           N  
ANISOU 1181  ND2 ASN A 225     7489   6893   5379     91   -880    -37       N  
ATOM   1182  N   LEU A 226      -1.496  11.878  21.274  1.00 49.14           N  
ANISOU 1182  N   LEU A 226     7163   6211   5298     86   -482    124       N  
ATOM   1183  CA  LEU A 226      -0.069  11.634  21.482  1.00 44.90           C  
ANISOU 1183  CA  LEU A 226     6669   5590   4800     31   -375    119       C  
ATOM   1184  C   LEU A 226       0.370  10.177  21.365  1.00 43.98           C  
ANISOU 1184  C   LEU A 226     6536   5471   4703    -48   -366     59       C  
ATOM   1185  O   LEU A 226      -0.400   9.272  21.649  1.00 42.09           O  
ANISOU 1185  O   LEU A 226     6222   5280   4490    -86   -429     17       O  
ATOM   1186  CB  LEU A 226       0.326  12.207  22.834  1.00 44.71           C  
ANISOU 1186  CB  LEU A 226     6587   5526   4876     22   -319    140       C  
ATOM   1187  CG  LEU A 226       0.713  13.692  22.952  1.00 44.92           C  
ANISOU 1187  CG  LEU A 226     6676   5495   4896     74   -260    195       C  
ATOM   1188  CD1 LEU A 226      -0.213  14.646  22.221  1.00 43.13           C  
ANISOU 1188  CD1 LEU A 226     6508   5293   4585    170   -312    241       C  
ATOM   1189  CD2 LEU A 226       0.735  14.039  24.433  1.00 44.29           C  
ANISOU 1189  CD2 LEU A 226     6514   5401   4915     60   -238    196       C  
ATOM   1190  N   ARG A 227       1.614   9.966  20.944  1.00 41.22           N  
ANISOU 1190  N   ARG A 227     6257   5060   4343    -72   -280     53       N  
ATOM   1191  CA  ARG A 227       2.130   8.623  20.696  1.00 40.16           C  
ANISOU 1191  CA  ARG A 227     6130   4911   4217   -131   -260     -2       C  
ATOM   1192  C   ARG A 227       3.520   8.477  21.313  1.00 42.74           C  
ANISOU 1192  C   ARG A 227     6447   5174   4619   -159   -156     -1       C  
ATOM   1193  O   ARG A 227       4.429   9.284  21.054  1.00 41.21           O  
ANISOU 1193  O   ARG A 227     6303   4938   4415   -142    -78     29       O  
ATOM   1194  CB  ARG A 227       2.198   8.345  19.185  1.00 38.58           C  
ANISOU 1194  CB  ARG A 227     6042   4717   3899   -118   -269    -21       C  
ATOM   1195  CG  ARG A 227       0.846   8.058  18.537  1.00 39.87           C  
ANISOU 1195  CG  ARG A 227     6203   4959   3987   -105   -391    -48       C  
ATOM   1196  CD  ARG A 227       0.897   7.815  17.031  1.00 40.30           C  
ANISOU 1196  CD  ARG A 227     6379   5025   3907    -88   -408    -71       C  
ATOM   1197  NE  ARG A 227       1.471   8.959  16.338  1.00 41.07           N  
ANISOU 1197  NE  ARG A 227     6586   5089   3929    -23   -348    -10       N  
ATOM   1198  CZ  ARG A 227       1.219   9.323  15.078  1.00 43.14           C  
ANISOU 1198  CZ  ARG A 227     6964   5375   4051     31   -379      4       C  
ATOM   1199  NH1 ARG A 227       0.372   8.657  14.302  1.00 41.32           N  
ANISOU 1199  NH1 ARG A 227     6753   5213   3732     30   -485    -48       N  
ATOM   1200  NH2 ARG A 227       1.828  10.391  14.589  1.00 44.16           N  
ANISOU 1200  NH2 ARG A 227     7198   5457   4124     85   -301     69       N  
ATOM   1201  N   SER A 228       3.692   7.450  22.132  1.00 40.44           N  
ANISOU 1201  N   SER A 228     6088   4875   4402   -202   -153    -34       N  
ATOM   1202  CA  SER A 228       4.983   7.203  22.725  1.00 38.69           C  
ANISOU 1202  CA  SER A 228     5846   4606   4248   -217    -69    -38       C  
ATOM   1203  C   SER A 228       6.067   6.977  21.697  1.00 36.71           C  
ANISOU 1203  C   SER A 228     5675   4319   3954   -216     10    -53       C  
ATOM   1204  O   SER A 228       5.900   6.186  20.787  1.00 38.06           O  
ANISOU 1204  O   SER A 228     5907   4491   4063   -223     -2    -87       O  
ATOM   1205  CB  SER A 228       4.912   5.998  23.663  1.00 37.60           C  
ANISOU 1205  CB  SER A 228     5644   4464   4180   -250    -84    -69       C  
ATOM   1206  OG  SER A 228       4.167   6.365  24.790  1.00 38.49           O  
ANISOU 1206  OG  SER A 228     5679   4603   4342   -250   -128    -48       O  
ATOM   1207  N   ALA A 229       7.219   7.611  21.888  1.00 40.03           N  
ANISOU 1207  N   ALA A 229     6090   4708   4410   -211     95    -34       N  
ATOM   1208  CA  ALA A 229       8.317   7.467  20.918  1.00 40.11           C  
ANISOU 1208  CA  ALA A 229     6167   4688   4386   -210    188    -46       C  
ATOM   1209  C   ALA A 229       9.689   7.742  21.490  1.00 36.54           C  
ANISOU 1209  C   ALA A 229     5657   4212   4014   -220    280    -45       C  
ATOM   1210  O   ALA A 229       9.839   8.468  22.443  1.00 39.74           O  
ANISOU 1210  O   ALA A 229     5996   4621   4483   -228    277    -26       O  
ATOM   1211  CB  ALA A 229       8.060   8.366  19.718  1.00 41.85           C  
ANISOU 1211  CB  ALA A 229     6495   4904   4502   -187    203    -16       C  
ATOM   1212  N   ILE A 230      10.706   7.163  20.888  1.00 37.33           N  
ANISOU 1212  N   ILE A 230     5782   4293   4111   -220    361    -71       N  
ATOM   1213  CA  ILE A 230      12.050   7.440  21.298  1.00 37.67           C  
ANISOU 1213  CA  ILE A 230     5758   4325   4228   -230    451    -75       C  
ATOM   1214  C   ILE A 230      12.873   7.547  20.026  1.00 42.10           C  
ANISOU 1214  C   ILE A 230     6397   4864   4734   -228    560    -81       C  
ATOM   1215  O   ILE A 230      12.560   6.900  19.025  1.00 46.59           O  
ANISOU 1215  O   ILE A 230     7059   5424   5219   -212    561    -98       O  
ATOM   1216  CB  ILE A 230      12.596   6.376  22.292  1.00 36.46           C  
ANISOU 1216  CB  ILE A 230     5509   4183   4161   -219    439   -107       C  
ATOM   1217  CG1 ILE A 230      14.043   6.720  22.723  1.00 34.62           C  
ANISOU 1217  CG1 ILE A 230     5187   3958   4009   -225    524   -117       C  
ATOM   1218  CG2 ILE A 230      12.526   4.937  21.727  1.00 34.92           C  
ANISOU 1218  CG2 ILE A 230     5364   3971   3932   -197    439   -143       C  
ATOM   1219  CD1 ILE A 230      14.516   5.911  23.915  1.00 32.42           C  
ANISOU 1219  CD1 ILE A 230     4804   3700   3813   -201    492   -137       C  
ATOM   1220  N   THR A 231      13.895   8.392  20.055  1.00 40.60           N  
ANISOU 1220  N   THR A 231     6175   4664   4588   -251    655    -71       N  
ATOM   1221  CA  THR A 231      14.778   8.549  18.927  1.00 40.89           C  
ANISOU 1221  CA  THR A 231     6274   4678   4582   -256    780    -74       C  
ATOM   1222  C   THR A 231      16.192   8.246  19.466  1.00 40.89           C  
ANISOU 1222  C   THR A 231     6151   4695   4691   -267    863   -108       C  
ATOM   1223  O   THR A 231      16.668   8.886  20.404  1.00 38.55           O  
ANISOU 1223  O   THR A 231     5750   4413   4483   -297    865   -107       O  
ATOM   1224  CB  THR A 231      14.702   9.991  18.336  1.00 41.99           C  
ANISOU 1224  CB  THR A 231     6497   4786   4671   -280    838    -26       C  
ATOM   1225  OG1 THR A 231      13.380  10.283  17.849  1.00 41.55           O  
ANISOU 1225  OG1 THR A 231     6549   4726   4512   -252    751      7       O  
ATOM   1226  CG2 THR A 231      15.697  10.189  17.209  1.00 41.55           C  
ANISOU 1226  CG2 THR A 231     6509   4705   4575   -292    988    -27       C  
ATOM   1227  N   VAL A 232      16.853   7.275  18.859  1.00 38.85           N  
ANISOU 1227  N   VAL A 232     5904   4436   4421   -238    928   -142       N  
ATOM   1228  CA  VAL A 232      18.167   6.820  19.320  1.00 40.35           C  
ANISOU 1228  CA  VAL A 232     5968   4652   4711   -229    999   -178       C  
ATOM   1229  C   VAL A 232      19.301   7.310  18.422  1.00 40.42           C  
ANISOU 1229  C   VAL A 232     5983   4654   4719   -252   1159   -185       C  
ATOM   1230  O   VAL A 232      19.373   6.930  17.245  1.00 40.65           O  
ANISOU 1230  O   VAL A 232     6123   4660   4664   -231   1232   -190       O  
ATOM   1231  CB  VAL A 232      18.212   5.276  19.385  1.00 40.04           C  
ANISOU 1231  CB  VAL A 232     5923   4615   4675   -167    970   -215       C  
ATOM   1232  CG1 VAL A 232      19.540   4.819  19.953  1.00 38.01           C  
ANISOU 1232  CG1 VAL A 232     5526   4392   4523   -137   1031   -247       C  
ATOM   1233  CG2 VAL A 232      17.043   4.770  20.236  1.00 36.98           C  
ANISOU 1233  CG2 VAL A 232     5538   4226   4286   -155    825   -206       C  
ATOM   1234  N   PHE A 233      20.157   8.170  18.961  1.00 39.39           N  
ANISOU 1234  N   PHE A 233     5742   4545   4680   -301   1216   -187       N  
ATOM   1235  CA  PHE A 233      21.281   8.701  18.196  1.00 41.59           C  
ANISOU 1235  CA  PHE A 233     6009   4820   4975   -339   1381   -196       C  
ATOM   1236  C   PHE A 233      22.497   7.791  18.359  1.00 43.10           C  
ANISOU 1236  C   PHE A 233     6067   5059   5249   -301   1447   -247       C  
ATOM   1237  O   PHE A 233      22.430   6.839  19.132  1.00 44.05           O  
ANISOU 1237  O   PHE A 233     6115   5209   5411   -242   1356   -270       O  
ATOM   1238  CB  PHE A 233      21.560  10.137  18.623  1.00 42.24           C  
ANISOU 1238  CB  PHE A 233     6044   4893   5113   -426   1417   -178       C  
ATOM   1239  CG  PHE A 233      20.490  11.095  18.191  1.00 43.06           C  
ANISOU 1239  CG  PHE A 233     6303   4937   5121   -449   1388   -121       C  
ATOM   1240  CD1 PHE A 233      20.413  11.529  16.872  1.00 44.23           C  
ANISOU 1240  CD1 PHE A 233     6607   5034   5164   -456   1493    -86       C  
ATOM   1241  CD2 PHE A 233      19.533  11.536  19.087  1.00 42.27           C  
ANISOU 1241  CD2 PHE A 233     6199   4833   5029   -453   1257    -99       C  
ATOM   1242  CE1 PHE A 233      19.413  12.400  16.457  1.00 44.06           C  
ANISOU 1242  CE1 PHE A 233     6734   4960   5047   -460   1460    -29       C  
ATOM   1243  CE2 PHE A 233      18.526  12.410  18.681  1.00 42.44           C  
ANISOU 1243  CE2 PHE A 233     6360   4803   4963   -458   1229    -46       C  
ATOM   1244  CZ  PHE A 233      18.464  12.842  17.362  1.00 42.26           C  
ANISOU 1244  CZ  PHE A 233     6491   4730   4834   -457   1326     -8       C  
ATOM   1245  N   PRO A 234      23.610   8.052  17.635  1.00 44.33           N  
ANISOU 1245  N   PRO A 234     6191   5223   5428   -327   1609   -265       N  
ATOM   1246  CA  PRO A 234      24.703   7.059  17.757  1.00 45.79           C  
ANISOU 1246  CA  PRO A 234     6248   5461   5689   -267   1666   -316       C  
ATOM   1247  C   PRO A 234      25.273   6.870  19.161  1.00 45.53           C  
ANISOU 1247  C   PRO A 234     6012   5500   5788   -254   1585   -348       C  
ATOM   1248  O   PRO A 234      25.294   7.786  19.953  1.00 46.98           O  
ANISOU 1248  O   PRO A 234     6115   5703   6030   -321   1541   -344       O  
ATOM   1249  CB  PRO A 234      25.760   7.559  16.775  1.00 46.26           C  
ANISOU 1249  CB  PRO A 234     6299   5521   5757   -311   1863   -327       C  
ATOM   1250  CG  PRO A 234      24.960   8.349  15.773  1.00 46.43           C  
ANISOU 1250  CG  PRO A 234     6524   5467   5649   -357   1904   -275       C  
ATOM   1251  CD  PRO A 234      23.873   9.020  16.556  1.00 44.26           C  
ANISOU 1251  CD  PRO A 234     6282   5172   5363   -390   1755   -239       C  
ATOM   1252  N   GLN A 235      25.707   5.653  19.450  1.00 47.57           N  
ANISOU 1252  N   GLN A 235     6200   5794   6083   -158   1563   -379       N  
ATOM   1253  CA  GLN A 235      26.199   5.277  20.764  1.00 48.79           C  
ANISOU 1253  CA  GLN A 235     6177   6019   6342   -116   1472   -405       C  
ATOM   1254  C   GLN A 235      27.579   5.909  21.014  1.00 48.03           C  
ANISOU 1254  C   GLN A 235     5884   6003   6362   -162   1563   -446       C  
ATOM   1255  O   GLN A 235      28.269   6.252  20.076  1.00 48.56           O  
ANISOU 1255  O   GLN A 235     5949   6069   6433   -200   1717   -459       O  
ATOM   1256  CB  GLN A 235      26.285   3.748  20.833  1.00 48.92           C  
ANISOU 1256  CB  GLN A 235     6202   6036   6351     13   1442   -421       C  
ATOM   1257  CG  GLN A 235      27.343   3.160  19.893  1.00 50.37           C  
ANISOU 1257  CG  GLN A 235     6357   6233   6547     69   1596   -455       C  
ATOM   1258  CD  GLN A 235      27.066   1.723  19.515  1.00 49.35           C  
ANISOU 1258  CD  GLN A 235     6334   6056   6362    183   1589   -463       C  
ATOM   1259  OE1 GLN A 235      25.927   1.354  19.238  1.00 49.65           O  
ANISOU 1259  OE1 GLN A 235     6540   6020   6305    183   1523   -440       O  
ATOM   1260  NE2 GLN A 235      28.108   0.902  19.499  1.00 49.03           N  
ANISOU 1260  NE2 GLN A 235     6193   6056   6381    282   1658   -498       N  
ATOM   1261  N   ARG A 236      27.961   6.053  22.279  1.00 49.76           N  
ANISOU 1261  N   ARG A 236     5939   6295   6673   -161   1467   -469       N  
ATOM   1262  CA  ARG A 236      29.311   6.457  22.667  1.00 52.13           C  
ANISOU 1262  CA  ARG A 236     6021   6693   7095   -192   1527   -523       C  
ATOM   1263  C   ARG A 236      30.378   5.528  21.999  1.00 54.43           C  
ANISOU 1263  C   ARG A 236     6231   7028   7421   -101   1647   -557       C  
ATOM   1264  O   ARG A 236      30.186   4.314  21.894  1.00 52.59           O  
ANISOU 1264  O   ARG A 236     6055   6776   7149     24   1617   -549       O  
ATOM   1265  CB  ARG A 236      29.407   6.460  24.205  1.00 55.12           C  
ANISOU 1265  CB  ARG A 236     6255   7147   7542   -171   1370   -543       C  
ATOM   1266  CG  ARG A 236      30.751   6.895  24.788  1.00 63.97           C  
ANISOU 1266  CG  ARG A 236     7129   8388   8791   -206   1395   -608       C  
ATOM   1267  CD  ARG A 236      30.778   6.988  26.319  1.00 68.51           C  
ANISOU 1267  CD  ARG A 236     7577   9038   9413   -190   1226   -630       C  
ATOM   1268  NE  ARG A 236      30.189   8.222  26.846  1.00 72.34           N  
ANISOU 1268  NE  ARG A 236     8102   9494   9892   -319   1171   -627       N  
ATOM   1269  CZ  ARG A 236      29.100   8.273  27.616  1.00 75.04           C  
ANISOU 1269  CZ  ARG A 236     8545   9792  10173   -307   1036   -590       C  
ATOM   1270  NH1 ARG A 236      28.485   7.158  27.978  1.00 78.00           N  
ANISOU 1270  NH1 ARG A 236     8991  10151  10494   -182    943   -554       N  
ATOM   1271  NH2 ARG A 236      28.626   9.438  28.050  1.00 73.25           N  
ANISOU 1271  NH2 ARG A 236     8353   9535   9944   -420   1001   -591       N  
ATOM   1272  N   ALA A 237      31.475   6.103  21.523  1.00 54.67           N  
ANISOU 1272  N   ALA A 237     6137   7111   7525   -165   1792   -595       N  
ATOM   1273  CA  ALA A 237      32.523   5.317  20.850  1.00 61.74           C  
ANISOU 1273  CA  ALA A 237     6946   8053   8459    -80   1924   -630       C  
ATOM   1274  C   ALA A 237      33.901   5.616  21.426  1.00 64.16           C  
ANISOU 1274  C   ALA A 237     6972   8495   8913   -100   1960   -696       C  
ATOM   1275  O   ALA A 237      34.203   6.771  21.695  1.00 63.10           O  
ANISOU 1275  O   ALA A 237     6747   8390   8839   -239   1982   -718       O  
ATOM   1276  CB  ALA A 237      32.509   5.550  19.339  1.00 57.48           C  
ANISOU 1276  CB  ALA A 237     6556   7438   7844   -126   2109   -613       C  
ATOM   1277  N   PRO A 238      34.735   4.573  21.615  1.00 70.10           N  
ANISOU 1277  N   PRO A 238     7583   9327   9723     40   1966   -730       N  
ATOM   1278  CA  PRO A 238      36.073   4.737  22.201  1.00 76.62           C  
ANISOU 1278  CA  PRO A 238     8118  10304  10692     43   1984   -798       C  
ATOM   1279  C   PRO A 238      36.806   5.888  21.530  1.00 77.90           C  
ANISOU 1279  C   PRO A 238     8190  10489  10918   -121   2159   -833       C  
ATOM   1280  O   PRO A 238      36.840   5.942  20.300  1.00 75.20           O  
ANISOU 1280  O   PRO A 238     7966  10081  10526   -149   2332   -817       O  
ATOM   1281  CB  PRO A 238      36.777   3.406  21.866  1.00 78.66           C  
ANISOU 1281  CB  PRO A 238     8313  10606  10970    228   2042   -816       C  
ATOM   1282  CG  PRO A 238      35.945   2.771  20.786  1.00 78.37           C  
ANISOU 1282  CG  PRO A 238     8547  10430  10802    277   2114   -767       C  
ATOM   1283  CD  PRO A 238      34.539   3.199  21.121  1.00 71.21           C  
ANISOU 1283  CD  PRO A 238     7838   9422   9798    203   1982   -712       C  
ATOM   1284  N   GLY A 239      37.338   6.814  22.333  1.00 82.55           N  
ANISOU 1284  N   GLY A 239     8589  11166  11609   -236   2114   -882       N  
ATOM   1285  CA  GLY A 239      38.079   7.977  21.818  1.00 89.76           C  
ANISOU 1285  CA  GLY A 239     9403  12102  12601   -414   2280   -923       C  
ATOM   1286  C   GLY A 239      37.276   9.157  21.260  1.00 94.26           C  
ANISOU 1286  C   GLY A 239    10181  12537  13098   -582   2349   -877       C  
ATOM   1287  O   GLY A 239      37.741  10.302  21.337  1.00 97.50           O  
ANISOU 1287  O   GLY A 239    10500  12964  13583   -750   2421   -914       O  
ATOM   1288  N   ARG A 240      36.077   8.886  20.718  1.00 85.94           N  
ANISOU 1288  N   ARG A 240     9403  11351  11899   -536   2324   -800       N  
ATOM   1289  CA  ARG A 240      35.270   9.867  19.957  1.00 76.03           C  
ANISOU 1289  CA  ARG A 240     8377   9961  10552   -660   2404   -744       C  
ATOM   1290  C   ARG A 240      34.187  10.532  20.819  1.00 70.82           C  
ANISOU 1290  C   ARG A 240     7818   9242   9849   -716   2233   -712       C  
ATOM   1291  O   ARG A 240      33.498   9.856  21.591  1.00 74.47           O  
ANISOU 1291  O   ARG A 240     8310   9711  10273   -614   2055   -694       O  
ATOM   1292  CB  ARG A 240      34.655   9.168  18.728  1.00 74.06           C  
ANISOU 1292  CB  ARG A 240     8363   9614  10163   -572   2487   -686       C  
ATOM   1293  CG  ARG A 240      33.936  10.047  17.710  1.00 68.77           C  
ANISOU 1293  CG  ARG A 240     7936   8813   9380   -670   2593   -625       C  
ATOM   1294  CD  ARG A 240      32.457  10.130  18.035  1.00 67.87           C  
ANISOU 1294  CD  ARG A 240     8022   8610   9154   -648   2424   -564       C  
ATOM   1295  NE  ARG A 240      31.637   9.057  17.460  1.00 67.76           N  
ANISOU 1295  NE  ARG A 240     8188   8544   9014   -518   2377   -526       N  
ATOM   1296  CZ  ARG A 240      30.581   8.493  18.056  1.00 62.62           C  
ANISOU 1296  CZ  ARG A 240     7621   7868   8304   -443   2193   -499       C  
ATOM   1297  NH1 ARG A 240      30.189   8.846  19.279  1.00 55.71           N  
ANISOU 1297  NH1 ARG A 240     6673   7018   7478   -469   2035   -501       N  
ATOM   1298  NH2 ARG A 240      29.918   7.548  17.422  1.00 62.95           N  
ANISOU 1298  NH2 ARG A 240     7823   7860   8237   -344   2173   -474       N  
ATOM   1299  N   GLY A 241      34.024  11.847  20.667  1.00 64.38           N  
ANISOU 1299  N   GLY A 241     7065   8362   9037   -875   2298   -702       N  
ATOM   1300  CA  GLY A 241      33.069  12.621  21.465  1.00 58.00           C  
ANISOU 1300  CA  GLY A 241     6347   7495   8196   -936   2158   -677       C  
ATOM   1301  C   GLY A 241      31.611  12.164  21.378  1.00 55.91           C  
ANISOU 1301  C   GLY A 241     6314   7140   7791   -841   2037   -601       C  
ATOM   1302  O   GLY A 241      31.206  11.522  20.414  1.00 55.72           O  
ANISOU 1302  O   GLY A 241     6438   7062   7669   -764   2093   -557       O  
ATOM   1303  N   ASP A 242      30.826  12.491  22.392  1.00 51.38           N  
ANISOU 1303  N   ASP A 242     5765   6551   7204   -850   1873   -590       N  
ATOM   1304  CA  ASP A 242      29.438  12.040  22.473  1.00 54.45           C  
ANISOU 1304  CA  ASP A 242     6341   6872   7476   -763   1745   -526       C  
ATOM   1305  C   ASP A 242      28.477  12.885  21.636  1.00 51.96           C  
ANISOU 1305  C   ASP A 242     6258   6429   7054   -820   1803   -459       C  
ATOM   1306  O   ASP A 242      28.722  14.051  21.376  1.00 51.68           O  
ANISOU 1306  O   ASP A 242     6247   6346   7042   -941   1903   -459       O  
ATOM   1307  CB  ASP A 242      28.951  12.050  23.933  1.00 51.84           C  
ANISOU 1307  CB  ASP A 242     5945   6581   7172   -743   1552   -540       C  
ATOM   1308  CG  ASP A 242      29.655  11.005  24.821  1.00 54.42           C  
ANISOU 1308  CG  ASP A 242     6079   7028   7570   -643   1458   -589       C  
ATOM   1309  OD1 ASP A 242      30.433  10.133  24.337  1.00 52.42           O  
ANISOU 1309  OD1 ASP A 242     5745   6827   7345   -568   1528   -609       O  
ATOM   1310  OD2 ASP A 242      29.402  11.051  26.044  1.00 55.62           O  
ANISOU 1310  OD2 ASP A 242     6167   7221   7744   -630   1310   -605       O  
ATOM   1311  N   PHE A 243      27.383  12.271  21.216  1.00 51.59           N  
ANISOU 1311  N   PHE A 243     6383   6329   6892   -731   1737   -403       N  
ATOM   1312  CA  PHE A 243      26.195  13.016  20.810  1.00 48.91           C  
ANISOU 1312  CA  PHE A 243     6249   5887   6447   -758   1717   -339       C  
ATOM   1313  C   PHE A 243      25.490  13.415  22.086  1.00 49.57           C  
ANISOU 1313  C   PHE A 243     6304   5975   6553   -768   1557   -339       C  
ATOM   1314  O   PHE A 243      25.301  12.568  22.972  1.00 50.15           O  
ANISOU 1314  O   PHE A 243     6297   6109   6650   -693   1425   -358       O  
ATOM   1315  CB  PHE A 243      25.250  12.147  19.979  1.00 47.17           C  
ANISOU 1315  CB  PHE A 243     6200   5625   6096   -657   1685   -291       C  
ATOM   1316  CG  PHE A 243      25.672  11.983  18.557  1.00 47.92           C  
ANISOU 1316  CG  PHE A 243     6391   5688   6128   -652   1848   -277       C  
ATOM   1317  CD1 PHE A 243      26.626  11.026  18.207  1.00 49.63           C  
ANISOU 1317  CD1 PHE A 243     6512   5962   6384   -601   1927   -319       C  
ATOM   1318  CD2 PHE A 243      25.118  12.779  17.558  1.00 47.85           C  
ANISOU 1318  CD2 PHE A 243     6576   5591   6013   -688   1926   -220       C  
ATOM   1319  CE1 PHE A 243      27.031  10.875  16.886  1.00 50.20           C  
ANISOU 1319  CE1 PHE A 243     6679   6005   6392   -594   2089   -309       C  
ATOM   1320  CE2 PHE A 243      25.523  12.636  16.236  1.00 49.96           C  
ANISOU 1320  CE2 PHE A 243     6944   5830   6210   -681   2083   -206       C  
ATOM   1321  CZ  PHE A 243      26.481  11.689  15.904  1.00 50.27           C  
ANISOU 1321  CZ  PHE A 243     6885   5927   6289   -638   2168   -253       C  
ATOM   1322  N   ARG A 244      25.101  14.688  22.185  1.00 47.85           N  
ANISOU 1322  N   ARG A 244     6163   5690   6327   -856   1574   -317       N  
ATOM   1323  CA  ARG A 244      24.427  15.198  23.364  1.00 46.52           C  
ANISOU 1323  CA  ARG A 244     5981   5517   6176   -871   1438   -320       C  
ATOM   1324  C   ARG A 244      23.383  16.240  23.001  1.00 47.08           C  
ANISOU 1324  C   ARG A 244     6241   5481   6166   -900   1445   -258       C  
ATOM   1325  O   ARG A 244      23.608  17.128  22.175  1.00 52.58           O  
ANISOU 1325  O   ARG A 244     7032   6103   6842   -970   1580   -234       O  
ATOM   1326  CB  ARG A 244      25.435  15.818  24.345  1.00 49.29           C  
ANISOU 1326  CB  ARG A 244     6150   5924   6655   -966   1443   -394       C  
ATOM   1327  CG  ARG A 244      26.279  14.873  25.203  1.00 50.39           C  
ANISOU 1327  CG  ARG A 244     6078   6189   6879   -919   1369   -459       C  
ATOM   1328  CD  ARG A 244      25.478  13.782  25.928  1.00 50.93           C  
ANISOU 1328  CD  ARG A 244     6154   6295   6902   -792   1204   -439       C  
ATOM   1329  NE  ARG A 244      24.481  14.273  26.882  1.00 48.67           N  
ANISOU 1329  NE  ARG A 244     5926   5980   6587   -795   1078   -422       N  
ATOM   1330  CZ  ARG A 244      24.712  14.553  28.168  1.00 52.36           C  
ANISOU 1330  CZ  ARG A 244     6280   6503   7113   -820    982   -470       C  
ATOM   1331  NH1 ARG A 244      25.945  14.422  28.679  1.00 52.69           N  
ANISOU 1331  NH1 ARG A 244     6130   6642   7250   -847    987   -542       N  
ATOM   1332  NH2 ARG A 244      23.705  14.987  28.941  1.00 48.22           N  
ANISOU 1332  NH2 ARG A 244     5830   5942   6547   -815    881   -449       N  
ATOM   1333  N   ILE A 245      22.232  16.125  23.616  1.00 43.64           N  
ANISOU 1333  N   ILE A 245     5865   5035   5681   -841   1305   -230       N  
ATOM   1334  CA  ILE A 245      21.266  17.199  23.634  1.00 43.00           C  
ANISOU 1334  CA  ILE A 245     5925   4867   5547   -862   1287   -183       C  
ATOM   1335  C   ILE A 245      21.465  17.897  24.989  1.00 43.83           C  
ANISOU 1335  C   ILE A 245     5928   4987   5737   -926   1224   -232       C  
ATOM   1336  O   ILE A 245      21.207  17.310  26.030  1.00 42.42           O  
ANISOU 1336  O   ILE A 245     5662   4874   5582   -879   1095   -258       O  
ATOM   1337  CB  ILE A 245      19.827  16.646  23.570  1.00 41.28           C  
ANISOU 1337  CB  ILE A 245     5816   4640   5228   -756   1165   -130       C  
ATOM   1338  CG1 ILE A 245      19.680  15.763  22.326  1.00 40.46           C  
ANISOU 1338  CG1 ILE A 245     5796   4537   5039   -693   1206    -99       C  
ATOM   1339  CG2 ILE A 245      18.793  17.774  23.640  1.00 40.08           C  
ANISOU 1339  CG2 ILE A 245     5799   4406   5022   -761   1139    -81       C  
ATOM   1340  CD1 ILE A 245      18.359  15.049  22.244  1.00 38.18           C  
ANISOU 1340  CD1 ILE A 245     5589   4256   4662   -599   1083    -63       C  
ATOM   1341  N   TRP A 246      21.892  19.155  24.965  1.00 42.05           N  
ANISOU 1341  N   TRP A 246     5730   4697   5551  -1033   1318   -245       N  
ATOM   1342  CA  TRP A 246      22.104  19.912  26.175  1.00 42.40           C  
ANISOU 1342  CA  TRP A 246     5693   4745   5671  -1106   1269   -301       C  
ATOM   1343  C   TRP A 246      20.822  20.105  27.001  1.00 43.65           C  
ANISOU 1343  C   TRP A 246     5925   4880   5778  -1041   1133   -273       C  
ATOM   1344  O   TRP A 246      20.850  20.015  28.241  1.00 42.86           O  
ANISOU 1344  O   TRP A 246     5725   4837   5725  -1044   1029   -323       O  
ATOM   1345  CB  TRP A 246      22.834  21.217  25.823  1.00 42.67           C  
ANISOU 1345  CB  TRP A 246     5761   4695   5755  -1245   1419   -322       C  
ATOM   1346  CG  TRP A 246      24.318  20.995  25.521  1.00 43.49           C  
ANISOU 1346  CG  TRP A 246     5709   4862   5953  -1331   1531   -385       C  
ATOM   1347  CD1 TRP A 246      24.899  19.904  24.876  1.00 43.06           C  
ANISOU 1347  CD1 TRP A 246     5576   4884   5901  -1278   1568   -386       C  
ATOM   1348  CD2 TRP A 246      25.460  21.857  25.882  1.00 44.49           C  
ANISOU 1348  CD2 TRP A 246     5722   4988   6195  -1487   1622   -465       C  
ATOM   1349  NE1 TRP A 246      26.260  20.051  24.780  1.00 45.97           N  
ANISOU 1349  NE1 TRP A 246     5794   5301   6373  -1379   1679   -454       N  
ATOM   1350  CE2 TRP A 246      26.663  21.183  25.377  1.00 45.46           C  
ANISOU 1350  CE2 TRP A 246     5691   5200   6383  -1511   1711   -506       C  
ATOM   1351  CE3 TRP A 246      25.599  23.080  26.533  1.00 47.17           C  
ANISOU 1351  CE3 TRP A 246     6072   5263   6588  -1608   1642   -510       C  
ATOM   1352  CZ2 TRP A 246      27.931  21.714  25.542  1.00 48.23           C  
ANISOU 1352  CZ2 TRP A 246     5888   5584   6853  -1655   1810   -590       C  
ATOM   1353  CZ3 TRP A 246      26.891  23.610  26.692  1.00 47.47           C  
ANISOU 1353  CZ3 TRP A 246     5964   5327   6744  -1763   1741   -599       C  
ATOM   1354  CH2 TRP A 246      28.028  22.947  26.194  1.00 49.09           C  
ANISOU 1354  CH2 TRP A 246     6009   5628   7016  -1787   1824   -638       C  
ATOM   1355  N   ASN A 247      19.684  20.323  26.345  1.00 42.75           N  
ANISOU 1355  N   ASN A 247     5983   4695   5567   -976   1128   -195       N  
ATOM   1356  CA  ASN A 247      18.434  20.563  27.079  1.00 43.17           C  
ANISOU 1356  CA  ASN A 247     6100   4727   5574   -912   1011   -168       C  
ATOM   1357  C   ASN A 247      17.994  19.324  27.818  1.00 43.52           C  
ANISOU 1357  C   ASN A 247     6051   4870   5613   -826    873   -179       C  
ATOM   1358  O   ASN A 247      18.074  18.224  27.278  1.00 46.57           O  
ANISOU 1358  O   ASN A 247     6412   5307   5976   -772    862   -166       O  
ATOM   1359  CB  ASN A 247      17.332  20.950  26.111  1.00 43.83           C  
ANISOU 1359  CB  ASN A 247     6371   4730   5552   -846   1031    -81       C  
ATOM   1360  CG  ASN A 247      17.775  22.031  25.127  1.00 51.18           C  
ANISOU 1360  CG  ASN A 247     7424   5553   6468   -915   1187    -51       C  
ATOM   1361  OD1 ASN A 247      18.854  21.926  24.490  1.00 50.67           O  
ANISOU 1361  OD1 ASN A 247     7320   5493   6438   -982   1301    -72       O  
ATOM   1362  ND2 ASN A 247      16.945  23.086  24.991  1.00 48.57           N  
ANISOU 1362  ND2 ASN A 247     7247   5122   6084   -894   1201      0       N  
ATOM   1363  N   SER A 248      17.523  19.491  29.040  1.00 43.42           N  
ANISOU 1363  N   SER A 248     6001   4878   5618   -813    774   -202       N  
ATOM   1364  CA  SER A 248      16.924  18.380  29.789  1.00 44.36           C  
ANISOU 1364  CA  SER A 248     6060   5076   5720   -728    647   -201       C  
ATOM   1365  C   SER A 248      15.632  17.843  29.128  1.00 41.69           C  
ANISOU 1365  C   SER A 248     5826   4723   5292   -634    604   -131       C  
ATOM   1366  O   SER A 248      15.332  16.663  29.235  1.00 40.34           O  
ANISOU 1366  O   SER A 248     5613   4610   5104   -573    537   -125       O  
ATOM   1367  CB  SER A 248      16.652  18.797  31.240  1.00 41.40           C  
ANISOU 1367  CB  SER A 248     5639   4719   5371   -736    562   -238       C  
ATOM   1368  OG  SER A 248      15.667  19.800  31.245  1.00 45.45           O  
ANISOU 1368  OG  SER A 248     6276   5151   5842   -726    566   -202       O  
ATOM   1369  N   GLN A 249      14.879  18.700  28.447  1.00 39.93           N  
ANISOU 1369  N   GLN A 249     5738   4422   5013   -623    641    -80       N  
ATOM   1370  CA  GLN A 249      13.746  18.214  27.643  1.00 40.28           C  
ANISOU 1370  CA  GLN A 249     5873   4463   4969   -539    602    -19       C  
ATOM   1371  C   GLN A 249      13.709  18.871  26.270  1.00 43.92           C  
ANISOU 1371  C   GLN A 249     6468   4851   5368   -541    697     29       C  
ATOM   1372  O   GLN A 249      14.272  19.969  26.072  1.00 44.12           O  
ANISOU 1372  O   GLN A 249     6546   4804   5415   -604    792     29       O  
ATOM   1373  CB  GLN A 249      12.423  18.493  28.328  1.00 40.16           C  
ANISOU 1373  CB  GLN A 249     5892   4444   4922   -480    511      6       C  
ATOM   1374  CG  GLN A 249      12.130  17.701  29.587  1.00 40.48           C  
ANISOU 1374  CG  GLN A 249     5828   4556   4995   -455    412    -24       C  
ATOM   1375  CD  GLN A 249      10.722  17.976  30.116  1.00 41.30           C  
ANISOU 1375  CD  GLN A 249     5972   4658   5061   -393    338      7       C  
ATOM   1376  OE1 GLN A 249       9.847  18.499  29.379  1.00 39.47           O  
ANISOU 1376  OE1 GLN A 249     5838   4388   4772   -348    344     55       O  
ATOM   1377  NE2 GLN A 249      10.490  17.628  31.397  1.00 35.83           N  
ANISOU 1377  NE2 GLN A 249     5205   4011   4399   -382    270    -21       N  
ATOM   1378  N   LEU A 250      13.042  18.227  25.319  1.00 42.31           N  
ANISOU 1378  N   LEU A 250     6331   4661   5083   -476    673     70       N  
ATOM   1379  CA  LEU A 250      12.933  18.834  23.987  1.00 43.66           C  
ANISOU 1379  CA  LEU A 250     6646   4766   5174   -464    755    122       C  
ATOM   1380  C   LEU A 250      12.140  20.133  24.095  1.00 42.05           C  
ANISOU 1380  C   LEU A 250     6550   4488   4938   -438    755    168       C  
ATOM   1381  O   LEU A 250      12.393  21.100  23.383  1.00 44.57           O  
ANISOU 1381  O   LEU A 250     6986   4722   5224   -458    853    203       O  
ATOM   1382  CB  LEU A 250      12.293  17.888  22.950  1.00 40.98           C  
ANISOU 1382  CB  LEU A 250     6364   4464   4741   -393    713    151       C  
ATOM   1383  CG  LEU A 250      12.964  16.543  22.631  1.00 41.16           C  
ANISOU 1383  CG  LEU A 250     6315   4547   4778   -402    721    112       C  
ATOM   1384  CD1 LEU A 250      12.222  15.773  21.533  1.00 38.07           C  
ANISOU 1384  CD1 LEU A 250     6008   4176   4279   -338    681    137       C  
ATOM   1385  CD2 LEU A 250      14.445  16.709  22.261  1.00 40.84           C  
ANISOU 1385  CD2 LEU A 250     6245   4485   4788   -475    856     85       C  
ATOM   1386  N   VAL A 251      11.194  20.180  25.009  1.00 41.51           N  
ANISOU 1386  N   VAL A 251     6448   4445   4879   -392    653    167       N  
ATOM   1387  CA  VAL A 251      10.375  21.386  25.109  1.00 43.43           C  
ANISOU 1387  CA  VAL A 251     6795   4617   5088   -349    652    211       C  
ATOM   1388  C   VAL A 251      10.420  21.814  26.563  1.00 45.42           C  
ANISOU 1388  C   VAL A 251     6968   4868   5420   -383    621    166       C  
ATOM   1389  O   VAL A 251      10.013  21.044  27.433  1.00 44.79           O  
ANISOU 1389  O   VAL A 251     6785   4865   5367   -361    527    137       O  
ATOM   1390  CB  VAL A 251       8.927  21.135  24.626  1.00 37.96           C  
ANISOU 1390  CB  VAL A 251     6159   3959   4304   -234    557    263       C  
ATOM   1391  CG1 VAL A 251       8.097  22.397  24.710  1.00 38.76           C  
ANISOU 1391  CG1 VAL A 251     6366   3989   4371   -172    559    312       C  
ATOM   1392  CG2 VAL A 251       8.921  20.620  23.189  1.00 39.38           C  
ANISOU 1392  CG2 VAL A 251     6416   4151   4394   -203    577    297       C  
ATOM   1393  N   ARG A 252      10.943  23.020  26.807  1.00 49.80           N  
ANISOU 1393  N   ARG A 252     7581   5331   6011   -442    705    157       N  
ATOM   1394  CA  ARG A 252      11.010  23.643  28.145  1.00 51.59           C  
ANISOU 1394  CA  ARG A 252     7760   5538   6303   -480    686    108       C  
ATOM   1395  C   ARG A 252      10.821  25.163  28.042  1.00 52.36           C  
ANISOU 1395  C   ARG A 252     8002   5505   6388   -485    765    136       C  
ATOM   1396  O   ARG A 252      11.215  25.773  27.056  1.00 55.30           O  
ANISOU 1396  O   ARG A 252     8486   5794   6732   -510    868    173       O  
ATOM   1397  CB  ARG A 252      12.389  23.416  28.771  1.00 55.28           C  
ANISOU 1397  CB  ARG A 252     8107   6034   6862   -597    722     28       C  
ATOM   1398  CG  ARG A 252      12.841  21.978  28.947  1.00 57.67           C  
ANISOU 1398  CG  ARG A 252     8269   6453   7191   -598    663     -5       C  
ATOM   1399  CD  ARG A 252      12.965  21.627  30.411  1.00 56.88           C  
ANISOU 1399  CD  ARG A 252     8047   6419   7146   -613    580    -66       C  
ATOM   1400  NE  ARG A 252      11.653  21.392  30.971  1.00 61.56           N  
ANISOU 1400  NE  ARG A 252     8654   7038   7697   -522    485    -38       N  
ATOM   1401  CZ  ARG A 252      11.404  21.204  32.255  1.00 61.65           C  
ANISOU 1401  CZ  ARG A 252     8596   7095   7732   -512    412    -74       C  
ATOM   1402  NH1 ARG A 252      12.402  21.235  33.132  1.00 57.40           N  
ANISOU 1402  NH1 ARG A 252     7970   6585   7255   -583    410   -143       N  
ATOM   1403  NH2 ARG A 252      10.142  20.984  32.649  1.00 66.22           N  
ANISOU 1403  NH2 ARG A 252     9192   7698   8271   -428    341    -42       N  
ATOM   1404  N   TYR A 253      10.263  25.782  29.082  1.00 53.58           N  
ANISOU 1404  N   TYR A 253     8161   5634   6562   -463    726    116       N  
ATOM   1405  CA  TYR A 253      10.176  27.247  29.146  1.00 48.25           C  
ANISOU 1405  CA  TYR A 253     7624   4821   5886   -475    807    130       C  
ATOM   1406  C   TYR A 253      11.414  27.881  29.759  1.00 49.64           C  
ANISOU 1406  C   TYR A 253     7773   4940   6148   -622    887     50       C  
ATOM   1407  O   TYR A 253      12.036  27.314  30.676  1.00 50.13           O  
ANISOU 1407  O   TYR A 253     7690   5084   6273   -689    838    -27       O  
ATOM   1408  CB  TYR A 253       8.942  27.683  29.920  1.00 44.08           C  
ANISOU 1408  CB  TYR A 253     7129   4284   5334   -373    737    145       C  
ATOM   1409  CG  TYR A 253       7.665  27.220  29.296  1.00 44.57           C  
ANISOU 1409  CG  TYR A 253     7218   4401   5316   -230    662    220       C  
ATOM   1410  CD1 TYR A 253       7.373  27.518  27.971  1.00 43.03           C  
ANISOU 1410  CD1 TYR A 253     7147   4156   5045   -168    703    298       C  
ATOM   1411  CD2 TYR A 253       6.728  26.494  30.032  1.00 45.84           C  
ANISOU 1411  CD2 TYR A 253     7278   4666   5474   -157    549    211       C  
ATOM   1412  CE1 TYR A 253       6.183  27.135  27.393  1.00 43.05           C  
ANISOU 1412  CE1 TYR A 253     7168   4219   4970    -35    623    359       C  
ATOM   1413  CE2 TYR A 253       5.529  26.087  29.457  1.00 45.55           C  
ANISOU 1413  CE2 TYR A 253     7250   4687   5370    -35    478    271       C  
ATOM   1414  CZ  TYR A 253       5.267  26.418  28.129  1.00 44.74           C  
ANISOU 1414  CZ  TYR A 253     7266   4541   5193     26    509    343       C  
ATOM   1415  OH  TYR A 253       4.097  26.019  27.528  1.00 42.77           O  
ANISOU 1415  OH  TYR A 253     7018   4361   4873    146    427    395       O  
ATOM   1416  N   ALA A 254      11.755  29.072  29.264  1.00 47.94           N  
ANISOU 1416  N   ALA A 254     7699   4583   5931   -672   1008     69       N  
ATOM   1417  CA  ALA A 254      12.923  29.806  29.735  1.00 47.69           C  
ANISOU 1417  CA  ALA A 254     7655   4481   5984   -828   1099    -10       C  
ATOM   1418  C   ALA A 254      12.761  30.292  31.172  1.00 47.38           C  
ANISOU 1418  C   ALA A 254     7581   4433   5989   -853   1046    -86       C  
ATOM   1419  O   ALA A 254      11.653  30.448  31.665  1.00 47.74           O  
ANISOU 1419  O   ALA A 254     7670   4476   5993   -742    978    -59       O  
ATOM   1420  CB  ALA A 254      13.236  30.971  28.795  1.00 50.41           C  
ANISOU 1420  CB  ALA A 254     8183   4659   6311   -875   1255     36       C  
ATOM   1421  N   GLY A 255      13.881  30.483  31.858  1.00 46.97           N  
ANISOU 1421  N   GLY A 255     7439   4387   6022   -999   1074   -186       N  
ATOM   1422  CA  GLY A 255      13.869  31.081  33.171  1.00 47.37           C  
ANISOU 1422  CA  GLY A 255     7476   4414   6109  -1043   1038   -269       C  
ATOM   1423  C   GLY A 255      14.902  32.188  33.144  1.00 50.21           C  
ANISOU 1423  C   GLY A 255     7893   4649   6534  -1208   1165   -334       C  
ATOM   1424  O   GLY A 255      16.086  31.918  32.951  1.00 51.62           O  
ANISOU 1424  O   GLY A 255     7964   4871   6778  -1335   1208   -389       O  
ATOM   1425  N   TYR A 256      14.443  33.426  33.308  1.00 50.33           N  
ANISOU 1425  N   TYR A 256     8080   4507   6535  -1205   1231   -328       N  
ATOM   1426  CA  TYR A 256      15.304  34.601  33.274  1.00 55.01           C  
ANISOU 1426  CA  TYR A 256     8761   4952   7188  -1366   1366   -387       C  
ATOM   1427  C   TYR A 256      15.553  35.110  34.690  1.00 59.43           C  
ANISOU 1427  C   TYR A 256     9281   5504   7796  -1451   1320   -512       C  
ATOM   1428  O   TYR A 256      14.600  35.484  35.410  1.00 55.90           O  
ANISOU 1428  O   TYR A 256     8913   5021   7306  -1353   1267   -509       O  
ATOM   1429  CB  TYR A 256      14.663  35.731  32.458  1.00 54.72           C  
ANISOU 1429  CB  TYR A 256     8976   4717   7099  -1308   1488   -295       C  
ATOM   1430  CG  TYR A 256      14.213  35.325  31.084  1.00 55.83           C  
ANISOU 1430  CG  TYR A 256     9189   4859   7166  -1196   1521   -164       C  
ATOM   1431  CD1 TYR A 256      15.148  35.022  30.081  1.00 55.03           C  
ANISOU 1431  CD1 TYR A 256     9056   4767   7085  -1288   1613   -147       C  
ATOM   1432  CD2 TYR A 256      12.847  35.235  30.777  1.00 54.95           C  
ANISOU 1432  CD2 TYR A 256     9173   4747   6959   -996   1458    -62       C  
ATOM   1433  CE1 TYR A 256      14.738  34.635  28.812  1.00 55.66           C  
ANISOU 1433  CE1 TYR A 256     9213   4851   7085  -1183   1641    -30       C  
ATOM   1434  CE2 TYR A 256      12.428  34.862  29.509  1.00 54.49           C  
ANISOU 1434  CE2 TYR A 256     9181   4698   6823   -892   1476     51       C  
ATOM   1435  CZ  TYR A 256      13.371  34.560  28.528  1.00 55.79           C  
ANISOU 1435  CZ  TYR A 256     9329   4867   7000   -985   1566     67       C  
ATOM   1436  OH  TYR A 256      12.963  34.164  27.266  1.00 55.89           O  
ANISOU 1436  OH  TYR A 256     9417   4895   6925   -881   1581    175       O  
ATOM   1437  N   ARG A 257      16.832  35.113  35.074  1.00 63.17           N  
ANISOU 1437  N   ARG A 257     9626   6020   8357  -1630   1340   -625       N  
ATOM   1438  CA  ARG A 257      17.266  35.614  36.372  1.00 69.55           C  
ANISOU 1438  CA  ARG A 257    10386   6827   9213  -1739   1297   -762       C  
ATOM   1439  C   ARG A 257      17.095  37.145  36.401  1.00 69.84           C  
ANISOU 1439  C   ARG A 257    10641   6637   9256  -1804   1423   -782       C  
ATOM   1440  O   ARG A 257      17.622  37.841  35.544  1.00 69.99           O  
ANISOU 1440  O   ARG A 257    10759   6523   9309  -1906   1572   -763       O  
ATOM   1441  CB  ARG A 257      18.718  35.176  36.627  1.00 76.62           C  
ANISOU 1441  CB  ARG A 257    11072   7839  10200  -1910   1284   -875       C  
ATOM   1442  CG  ARG A 257      19.295  35.559  37.989  1.00 87.24           C  
ANISOU 1442  CG  ARG A 257    12335   9219  11593  -2031   1217  -1031       C  
ATOM   1443  CD  ARG A 257      20.238  34.492  38.553  1.00 89.08           C  
ANISOU 1443  CD  ARG A 257    12307   9667  11871  -2081   1099  -1115       C  
ATOM   1444  NE  ARG A 257      19.555  33.324  39.140  1.00 89.89           N  
ANISOU 1444  NE  ARG A 257    12321   9928  11907  -1912    940  -1074       N  
ATOM   1445  CZ  ARG A 257      18.454  33.357  39.900  1.00 87.32           C  
ANISOU 1445  CZ  ARG A 257    12081   9593  11505  -1785    861  -1051       C  
ATOM   1446  NH1 ARG A 257      17.872  34.512  40.203  1.00 88.70           N  
ANISOU 1446  NH1 ARG A 257    12436   9609  11658  -1794    919  -1067       N  
ATOM   1447  NH2 ARG A 257      17.935  32.226  40.375  1.00 75.52           N  
ANISOU 1447  NH2 ARG A 257    10493   8243   9957  -1649    731  -1014       N  
ATOM   1448  N   GLN A 258      16.328  37.657  37.361  1.00 70.92           N  
ANISOU 1448  N   GLN A 258    10866   6725   9356  -1739   1371   -815       N  
ATOM   1449  CA  GLN A 258      16.059  39.107  37.443  1.00 74.29           C  
ANISOU 1449  CA  GLN A 258    11520   6925   9783  -1780   1488   -833       C  
ATOM   1450  C   GLN A 258      17.164  39.856  38.188  1.00 80.55           C  
ANISOU 1450  C   GLN A 258    12284   7660  10660  -2008   1532   -996       C  
ATOM   1451  O   GLN A 258      18.080  39.239  38.724  1.00 82.85           O  
ANISOU 1451  O   GLN A 258    12369   8106  11006  -2119   1453  -1098       O  
ATOM   1452  CB  GLN A 258      14.697  39.385  38.097  1.00 71.23           C  
ANISOU 1452  CB  GLN A 258    11251   6497   9315  -1598   1428   -795       C  
ATOM   1453  CG  GLN A 258      13.519  38.685  37.430  1.00 69.95           C  
ANISOU 1453  CG  GLN A 258    11108   6399   9072  -1374   1376   -644       C  
ATOM   1454  CD  GLN A 258      13.316  39.116  35.994  1.00 72.09           C  
ANISOU 1454  CD  GLN A 258    11533   6540   9317  -1328   1500   -519       C  
ATOM   1455  OE1 GLN A 258      12.917  40.249  35.734  1.00 74.11           O  
ANISOU 1455  OE1 GLN A 258    12004   6600   9553  -1300   1608   -484       O  
ATOM   1456  NE2 GLN A 258      13.587  38.211  35.046  1.00 70.97           N  
ANISOU 1456  NE2 GLN A 258    11294   6502   9168  -1312   1489   -449       N  
ATOM   1457  N   GLN A 259      17.083  41.185  38.202  1.00 89.59           N  
ANISOU 1457  N   GLN A 259    13639   8583  11816  -2075   1657  -1023       N  
ATOM   1458  CA  GLN A 259      17.979  42.013  39.013  1.00 95.35           C  
ANISOU 1458  CA  GLN A 259    14369   9239  12621  -2291   1696  -1190       C  
ATOM   1459  C   GLN A 259      17.580  41.996  40.488  1.00 96.78           C  
ANISOU 1459  C   GLN A 259    14516   9490  12767  -2251   1560  -1295       C  
ATOM   1460  O   GLN A 259      18.437  42.058  41.372  1.00 98.18           O  
ANISOU 1460  O   GLN A 259    14575   9734  12996  -2412   1505  -1451       O  
ATOM   1461  CB  GLN A 259      18.009  43.445  38.490  1.00101.15           C  
ANISOU 1461  CB  GLN A 259    15363   9693  13377  -2379   1890  -1181       C  
ATOM   1462  CG  GLN A 259      18.864  43.614  37.241  1.00108.77           C  
ANISOU 1462  CG  GLN A 259    16340  10584  14402  -2511   2046  -1134       C  
ATOM   1463  CD  GLN A 259      18.462  44.813  36.396  1.00113.50           C  
ANISOU 1463  CD  GLN A 259    17242  10903  14980  -2497   2238  -1043       C  
ATOM   1464  OE1 GLN A 259      17.583  45.594  36.772  1.00113.77           O  
ANISOU 1464  OE1 GLN A 259    17480  10787  14962  -2394   2259  -1024       O  
ATOM   1465  NE2 GLN A 259      19.104  44.960  35.238  1.00113.15           N  
ANISOU 1465  NE2 GLN A 259    17236  10785  14971  -2592   2387   -982       N  
ATOM   1466  N   ASP A 260      16.278  41.897  40.744  1.00 94.55           N  
ANISOU 1466  N   ASP A 260    14330   9199  12394  -2035   1505  -1211       N  
ATOM   1467  CA  ASP A 260      15.757  41.774  42.107  1.00 93.15           C  
ANISOU 1467  CA  ASP A 260    14126   9098  12168  -1966   1379  -1291       C  
ATOM   1468  C   ASP A 260      15.837  40.345  42.651  1.00 90.74           C  
ANISOU 1468  C   ASP A 260    13578   9060  11840  -1902   1205  -1299       C  
ATOM   1469  O   ASP A 260      15.045  39.951  43.510  1.00 91.65           O  
ANISOU 1469  O   ASP A 260    13677   9258  11886  -1769   1100  -1298       O  
ATOM   1470  CB  ASP A 260      14.322  42.317  42.194  1.00 95.97           C  
ANISOU 1470  CB  ASP A 260    14688   9332  12442  -1763   1408  -1203       C  
ATOM   1471  CG  ASP A 260      13.445  41.873  41.029  1.00 99.55           C  
ANISOU 1471  CG  ASP A 260    15185   9790  12850  -1574   1432  -1017       C  
ATOM   1472  OD1 ASP A 260      13.648  42.365  39.885  1.00 97.92           O  
ANISOU 1472  OD1 ASP A 260    15091   9450  12665  -1606   1561   -941       O  
ATOM   1473  OD2 ASP A 260      12.550  41.032  41.269  1.00 99.26           O  
ANISOU 1473  OD2 ASP A 260    15071   9891  12752  -1398   1324   -950       O  
ATOM   1474  N   GLY A 261      16.791  39.573  42.131  1.00 90.05           N  
ANISOU 1474  N   GLY A 261    13307   9099  11809  -1994   1184  -1302       N  
ATOM   1475  CA  GLY A 261      17.057  38.206  42.591  1.00 80.13           C  
ANISOU 1475  CA  GLY A 261    11817   8087  10541  -1949   1028  -1315       C  
ATOM   1476  C   GLY A 261      16.112  37.126  42.091  1.00 76.01           C  
ANISOU 1476  C   GLY A 261    11255   7669   9955  -1743    967  -1166       C  
ATOM   1477  O   GLY A 261      16.517  35.979  41.971  1.00 71.90           O  
ANISOU 1477  O   GLY A 261    10553   7320   9445  -1726    884  -1149       O  
ATOM   1478  N   SER A 262      14.856  37.484  41.802  1.00 73.76           N  
ANISOU 1478  N   SER A 262    11136   7283   9608  -1584   1006  -1062       N  
ATOM   1479  CA  SER A 262      13.802  36.500  41.455  1.00 67.28           C  
ANISOU 1479  CA  SER A 262    10278   6563   8721  -1384    937   -932       C  
ATOM   1480  C   SER A 262      13.929  35.941  40.025  1.00 65.38           C  
ANISOU 1480  C   SER A 262    10005   6341   8493  -1357    985   -818       C  
ATOM   1481  O   SER A 262      14.870  36.273  39.299  1.00 68.13           O  
ANISOU 1481  O   SER A 262    10355   6630   8901  -1491   1077   -835       O  
ATOM   1482  CB  SER A 262      12.406  37.111  41.659  1.00 64.40           C  
ANISOU 1482  CB  SER A 262    10086   6094   8288  -1222    959   -869       C  
ATOM   1483  OG  SER A 262      12.104  38.029  40.627  1.00 62.85           O  
ANISOU 1483  OG  SER A 262    10070   5716   8093  -1200   1091   -791       O  
ATOM   1484  N   VAL A 263      12.982  35.093  39.621  1.00 61.10           N  
ANISOU 1484  N   VAL A 263     9437   5882   7895  -1189    927   -707       N  
ATOM   1485  CA  VAL A 263      13.036  34.462  38.293  1.00 57.31           C  
ANISOU 1485  CA  VAL A 263     8929   5435   7413  -1152    958   -603       C  
ATOM   1486  C   VAL A 263      11.743  34.648  37.509  1.00 53.69           C  
ANISOU 1486  C   VAL A 263     8607   4908   6885   -979    986   -472       C  
ATOM   1487  O   VAL A 263      10.660  34.427  38.037  1.00 53.39           O  
ANISOU 1487  O   VAL A 263     8577   4913   6797   -842    915   -441       O  
ATOM   1488  CB  VAL A 263      13.362  32.961  38.410  1.00 55.23           C  
ANISOU 1488  CB  VAL A 263     8457   5373   7154  -1133    846   -602       C  
ATOM   1489  CG1 VAL A 263      13.333  32.292  37.044  1.00 54.90           C  
ANISOU 1489  CG1 VAL A 263     8399   5361   7100  -1085    877   -499       C  
ATOM   1490  CG2 VAL A 263      14.719  32.791  39.072  1.00 57.42           C  
ANISOU 1490  CG2 VAL A 263     8591   5725   7500  -1295    818   -728       C  
ATOM   1491  N   ARG A 264      11.866  35.068  36.258  1.00 51.07           N  
ANISOU 1491  N   ARG A 264     8381   4474   6550   -986   1090   -396       N  
ATOM   1492  CA  ARG A 264      10.731  35.070  35.353  1.00 52.23           C  
ANISOU 1492  CA  ARG A 264     8635   4587   6624   -816   1100   -266       C  
ATOM   1493  C   ARG A 264      10.796  33.818  34.451  1.00 50.65           C  
ANISOU 1493  C   ARG A 264     8318   4523   6404   -775   1050   -199       C  
ATOM   1494  O   ARG A 264      11.824  33.542  33.793  1.00 47.30           O  
ANISOU 1494  O   ARG A 264     7844   4112   6017   -886   1103   -210       O  
ATOM   1495  CB  ARG A 264      10.663  36.369  34.522  1.00 56.84           C  
ANISOU 1495  CB  ARG A 264     9443   4961   7193   -817   1244   -211       C  
ATOM   1496  CG  ARG A 264       9.333  36.571  33.795  1.00 59.38           C  
ANISOU 1496  CG  ARG A 264     9894   5239   7428   -613   1241    -83       C  
ATOM   1497  CD  ARG A 264       9.342  37.750  32.837  1.00 64.83           C  
ANISOU 1497  CD  ARG A 264    10814   5725   8092   -603   1385    -13       C  
ATOM   1498  NE  ARG A 264       9.064  39.010  33.523  1.00 76.66           N  
ANISOU 1498  NE  ARG A 264    12471   7056   9600   -599   1452    -50       N  
ATOM   1499  CZ  ARG A 264       9.207  40.230  32.989  1.00 84.52           C  
ANISOU 1499  CZ  ARG A 264    13688   7838  10589   -620   1596    -16       C  
ATOM   1500  NH1 ARG A 264       9.630  40.383  31.731  1.00 86.41           N  
ANISOU 1500  NH1 ARG A 264    14021   8005  10807   -647   1693     63       N  
ATOM   1501  NH2 ARG A 264       8.931  41.309  33.722  1.00 78.68           N  
ANISOU 1501  NH2 ARG A 264    13088   6948   9859   -613   1650    -61       N  
ATOM   1502  N   GLY A 265       9.687  33.077  34.437  1.00 46.05           N  
ANISOU 1502  N   GLY A 265     7693   4039   5764   -620    953   -135       N  
ATOM   1503  CA  GLY A 265       9.615  31.809  33.755  1.00 46.05           C  
ANISOU 1503  CA  GLY A 265     7580   4175   5742   -576    888    -85       C  
ATOM   1504  C   GLY A 265       9.819  30.635  34.701  1.00 44.55           C  
ANISOU 1504  C   GLY A 265     7199   4148   5580   -597    775   -147       C  
ATOM   1505  O   GLY A 265       9.403  30.662  35.850  1.00 48.60           O  
ANISOU 1505  O   GLY A 265     7677   4693   6094   -571    715   -193       O  
ATOM   1506  N   ASP A 266      10.475  29.600  34.210  1.00 43.15           N  
ANISOU 1506  N   ASP A 266     6907   4069   5419   -640    751   -146       N  
ATOM   1507  CA  ASP A 266      10.697  28.395  34.976  1.00 42.50           C  
ANISOU 1507  CA  ASP A 266     6654   4136   5356   -648    649   -191       C  
ATOM   1508  C   ASP A 266      12.087  28.391  35.602  1.00 43.21           C  
ANISOU 1508  C   ASP A 266     6646   4253   5518   -794    661   -293       C  
ATOM   1509  O   ASP A 266      13.082  28.227  34.891  1.00 44.44           O  
ANISOU 1509  O   ASP A 266     6763   4411   5711   -880    718   -304       O  
ATOM   1510  CB  ASP A 266      10.554  27.186  34.066  1.00 41.84           C  
ANISOU 1510  CB  ASP A 266     6505   4146   5246   -595    612   -131       C  
ATOM   1511  CG  ASP A 266      10.392  25.912  34.830  1.00 45.58           C  
ANISOU 1511  CG  ASP A 266     6837   4760   5722   -562    502   -154       C  
ATOM   1512  OD1 ASP A 266      10.850  25.837  36.009  1.00 42.17           O  
ANISOU 1512  OD1 ASP A 266     6328   4370   5324   -611    461   -228       O  
ATOM   1513  OD2 ASP A 266       9.800  24.974  34.237  1.00 48.09           O  
ANISOU 1513  OD2 ASP A 266     7125   5143   6003   -487    458    -98       O  
ATOM   1514  N   PRO A 267      12.166  28.537  36.945  1.00 44.10           N  
ANISOU 1514  N   PRO A 267     6712   4397   5648   -820    604   -372       N  
ATOM   1515  CA  PRO A 267      13.449  28.583  37.658  1.00 43.87           C  
ANISOU 1515  CA  PRO A 267     6581   4406   5682   -955    596   -480       C  
ATOM   1516  C   PRO A 267      14.282  27.321  37.436  1.00 44.38           C  
ANISOU 1516  C   PRO A 267     6482   4604   5775   -979    550   -491       C  
ATOM   1517  O   PRO A 267      15.506  27.362  37.526  1.00 48.79           O  
ANISOU 1517  O   PRO A 267     6952   5191   6396  -1095    571   -564       O  
ATOM   1518  CB  PRO A 267      13.029  28.731  39.127  1.00 43.17           C  
ANISOU 1518  CB  PRO A 267     6480   4350   5573   -929    516   -542       C  
ATOM   1519  CG  PRO A 267      11.659  29.327  39.064  1.00 43.51           C  
ANISOU 1519  CG  PRO A 267     6664   4308   5559   -814    536   -475       C  
ATOM   1520  CD  PRO A 267      11.029  28.670  37.870  1.00 43.30           C  
ANISOU 1520  CD  PRO A 267     6648   4303   5501   -720    542   -365       C  
ATOM   1521  N   ALA A 268      13.620  26.219  37.119  1.00 44.32           N  
ANISOU 1521  N   ALA A 268     6437   4677   5727   -871    491   -421       N  
ATOM   1522  CA  ALA A 268      14.302  24.960  36.827  1.00 46.35           C  
ANISOU 1522  CA  ALA A 268     6559   5047   6004   -874    453   -421       C  
ATOM   1523  C   ALA A 268      15.262  25.074  35.659  1.00 48.77           C  
ANISOU 1523  C   ALA A 268     6856   5322   6353   -954    551   -416       C  
ATOM   1524  O   ALA A 268      16.195  24.278  35.556  1.00 46.48           O  
ANISOU 1524  O   ALA A 268     6440   5118   6101   -989    538   -447       O  
ATOM   1525  CB  ALA A 268      13.303  23.838  36.558  1.00 38.87           C  
ANISOU 1525  CB  ALA A 268     5603   4164   5002   -748    389   -342       C  
ATOM   1526  N   ASN A 269      15.018  26.057  34.785  1.00 50.85           N  
ANISOU 1526  N   ASN A 269     7258   5460   6603   -973    653   -374       N  
ATOM   1527  CA  ASN A 269      15.729  26.162  33.513  1.00 46.88           C  
ANISOU 1527  CA  ASN A 269     6778   4914   6120  -1032    762   -347       C  
ATOM   1528  C   ASN A 269      16.646  27.368  33.437  1.00 48.15           C  
ANISOU 1528  C   ASN A 269     6979   4974   6341  -1176    876   -405       C  
ATOM   1529  O   ASN A 269      17.021  27.823  32.353  1.00 48.08           O  
ANISOU 1529  O   ASN A 269     7048   4884   6338  -1225    997   -370       O  
ATOM   1530  CB  ASN A 269      14.734  26.128  32.361  1.00 44.50           C  
ANISOU 1530  CB  ASN A 269     6608   4557   5741   -929    794   -238       C  
ATOM   1531  CG  ASN A 269      13.884  24.869  32.384  1.00 46.19           C  
ANISOU 1531  CG  ASN A 269     6770   4876   5905   -807    685   -192       C  
ATOM   1532  OD1 ASN A 269      14.390  23.797  32.730  1.00 42.91           O  
ANISOU 1532  OD1 ASN A 269     6219   4569   5516   -811    626   -226       O  
ATOM   1533  ND2 ASN A 269      12.580  24.989  32.044  1.00 42.72           N  
ANISOU 1533  ND2 ASN A 269     6433   4405   5394   -697    657   -118       N  
ATOM   1534  N   VAL A 270      17.033  27.880  34.590  1.00 48.31           N  
ANISOU 1534  N   VAL A 270     6952   4999   6407  -1251    842   -497       N  
ATOM   1535  CA  VAL A 270      17.891  29.057  34.593  1.00 52.81           C  
ANISOU 1535  CA  VAL A 270     7559   5467   7040  -1405    949   -565       C  
ATOM   1536  C   VAL A 270      19.240  28.779  33.891  1.00 54.81           C  
ANISOU 1536  C   VAL A 270     7699   5761   7365  -1521   1032   -601       C  
ATOM   1537  O   VAL A 270      19.710  29.583  33.075  1.00 54.83           O  
ANISOU 1537  O   VAL A 270     7784   5652   7395  -1615   1175   -591       O  
ATOM   1538  CB  VAL A 270      18.058  29.630  36.026  1.00 54.63           C  
ANISOU 1538  CB  VAL A 270     7755   5702   7300  -1469    885   -673       C  
ATOM   1539  CG1 VAL A 270      19.316  30.500  36.149  1.00 57.44           C  
ANISOU 1539  CG1 VAL A 270     8071   6008   7746  -1662    973   -779       C  
ATOM   1540  CG2 VAL A 270      16.831  30.452  36.383  1.00 53.20           C  
ANISOU 1540  CG2 VAL A 270     7749   5407   7056  -1388    882   -635       C  
ATOM   1541  N   GLU A 271      19.840  27.630  34.181  1.00 54.15           N  
ANISOU 1541  N   GLU A 271     7431   5833   7309  -1506    951   -635       N  
ATOM   1542  CA  GLU A 271      21.159  27.351  33.672  1.00 56.22           C  
ANISOU 1542  CA  GLU A 271     7560   6152   7649  -1610   1022   -682       C  
ATOM   1543  C   GLU A 271      21.152  27.158  32.170  1.00 55.63           C  
ANISOU 1543  C   GLU A 271     7564   6026   7548  -1585   1141   -591       C  
ATOM   1544  O   GLU A 271      22.021  27.692  31.471  1.00 56.46           O  
ANISOU 1544  O   GLU A 271     7669   6076   7706  -1704   1279   -611       O  
ATOM   1545  CB  GLU A 271      21.762  26.138  34.358  1.00 60.62           C  
ANISOU 1545  CB  GLU A 271     7907   6889   8236  -1575    902   -736       C  
ATOM   1546  CG  GLU A 271      23.270  26.240  34.469  1.00 66.63           C  
ANISOU 1546  CG  GLU A 271     8494   7719   9104  -1719    947   -840       C  
ATOM   1547  CD  GLU A 271      23.953  24.964  34.959  1.00 71.62           C  
ANISOU 1547  CD  GLU A 271     8914   8534   9764  -1664    838   -881       C  
ATOM   1548  OE1 GLU A 271      23.264  24.015  35.428  1.00 72.30           O  
ANISOU 1548  OE1 GLU A 271     8993   8690   9787  -1523    716   -838       O  
ATOM   1549  OE2 GLU A 271      25.205  24.925  34.874  1.00 72.30           O  
ANISOU 1549  OE2 GLU A 271     8841   8692   9939  -1764    880   -957       O  
ATOM   1550  N   ILE A 272      20.191  26.390  31.664  1.00 53.11           N  
ANISOU 1550  N   ILE A 272     7309   5726   7144  -1437   1091   -496       N  
ATOM   1551  CA  ILE A 272      20.161  26.123  30.223  1.00 51.75           C  
ANISOU 1551  CA  ILE A 272     7216   5516   6931  -1404   1192   -413       C  
ATOM   1552  C   ILE A 272      19.732  27.402  29.471  1.00 51.74           C  
ANISOU 1552  C   ILE A 272     7428   5341   6892  -1435   1319   -355       C  
ATOM   1553  O   ILE A 272      20.106  27.621  28.313  1.00 53.16           O  
ANISOU 1553  O   ILE A 272     7683   5458   7059  -1470   1451   -310       O  
ATOM   1554  CB  ILE A 272      19.358  24.836  29.829  1.00 50.11           C  
ANISOU 1554  CB  ILE A 272     7004   5389   6645  -1247   1100   -340       C  
ATOM   1555  CG1 ILE A 272      19.565  24.489  28.352  1.00 50.12           C  
ANISOU 1555  CG1 ILE A 272     7068   5368   6608  -1229   1206   -276       C  
ATOM   1556  CG2 ILE A 272      17.863  24.946  30.119  1.00 46.25           C  
ANISOU 1556  CG2 ILE A 272     6636   4863   6072  -1128   1011   -277       C  
ATOM   1557  CD1 ILE A 272      20.873  23.795  28.067  1.00 51.07           C  
ANISOU 1557  CD1 ILE A 272     7030   5576   6799  -1293   1260   -328       C  
ATOM   1558  N   THR A 273      18.995  28.268  30.155  1.00 48.94           N  
ANISOU 1558  N   THR A 273     7176   4903   6518  -1422   1285   -357       N  
ATOM   1559  CA  THR A 273      18.611  29.520  29.548  1.00 49.50           C  
ANISOU 1559  CA  THR A 273     7454   4799   6554  -1443   1404   -304       C  
ATOM   1560  C   THR A 273      19.855  30.358  29.332  1.00 52.54           C  
ANISOU 1560  C   THR A 273     7829   5106   7026  -1629   1556   -368       C  
ATOM   1561  O   THR A 273      20.093  30.836  28.222  1.00 52.83           O  
ANISOU 1561  O   THR A 273     7986   5042   7044  -1666   1703   -311       O  
ATOM   1562  CB  THR A 273      17.531  30.260  30.357  1.00 46.71           C  
ANISOU 1562  CB  THR A 273     7214   4371   6162  -1376   1339   -295       C  
ATOM   1563  OG1 THR A 273      16.360  29.438  30.425  1.00 44.96           O  
ANISOU 1563  OG1 THR A 273     6994   4226   5862  -1207   1213   -230       O  
ATOM   1564  CG2 THR A 273      17.145  31.548  29.664  1.00 49.14           C  
ANISOU 1564  CG2 THR A 273     7752   4488   6432  -1383   1469   -232       C  
ATOM   1565  N   GLU A 274      20.657  30.498  30.382  1.00 55.58           N  
ANISOU 1565  N   GLU A 274     8068   5546   7505  -1747   1520   -487       N  
ATOM   1566  CA  GLU A 274      21.893  31.271  30.318  1.00 62.15           C  
ANISOU 1566  CA  GLU A 274     8856   6322   8437  -1945   1653   -570       C  
ATOM   1567  C   GLU A 274      22.898  30.677  29.338  1.00 62.78           C  
ANISOU 1567  C   GLU A 274     8833   6463   8556  -2003   1755   -564       C  
ATOM   1568  O   GLU A 274      23.631  31.421  28.689  1.00 64.82           O  
ANISOU 1568  O   GLU A 274     9143   6625   8862  -2139   1924   -574       O  
ATOM   1569  CB  GLU A 274      22.512  31.435  31.705  1.00 66.76           C  
ANISOU 1569  CB  GLU A 274     9283   6979   9106  -2051   1566   -710       C  
ATOM   1570  CG  GLU A 274      21.667  32.319  32.624  1.00 75.77           C  
ANISOU 1570  CG  GLU A 274    10555   8021  10215  -2030   1511   -731       C  
ATOM   1571  CD  GLU A 274      22.193  32.433  34.058  1.00 84.67           C  
ANISOU 1571  CD  GLU A 274    11538   9229  11405  -2120   1406   -873       C  
ATOM   1572  OE1 GLU A 274      23.322  31.955  34.346  1.00 90.60           O  
ANISOU 1572  OE1 GLU A 274    12078  10107  12236  -2219   1381   -965       O  
ATOM   1573  OE2 GLU A 274      21.469  33.016  34.909  1.00 89.22           O  
ANISOU 1573  OE2 GLU A 274    12211   9743  11946  -2087   1346   -895       O  
ATOM   1574  N   LEU A 275      22.915  29.348  29.206  1.00 60.76           N  
ANISOU 1574  N   LEU A 275     8445   6361   8279  -1900   1662   -545       N  
ATOM   1575  CA  LEU A 275      23.800  28.702  28.227  1.00 62.02           C  
ANISOU 1575  CA  LEU A 275     8516   6582   8467  -1931   1760   -533       C  
ATOM   1576  C   LEU A 275      23.377  29.005  26.778  1.00 60.87           C  
ANISOU 1576  C   LEU A 275     8579   6314   8236  -1888   1901   -415       C  
ATOM   1577  O   LEU A 275      24.222  29.163  25.893  1.00 64.12           O  
ANISOU 1577  O   LEU A 275     8989   6695   8679  -1978   2061   -411       O  
ATOM   1578  CB  LEU A 275      23.913  27.187  28.462  1.00 60.07           C  
ANISOU 1578  CB  LEU A 275     8089   6518   8216  -1823   1629   -543       C  
ATOM   1579  CG  LEU A 275      24.698  26.721  29.699  1.00 59.84           C  
ANISOU 1579  CG  LEU A 275     7822   6637   8279  -1872   1513   -662       C  
ATOM   1580  CD1 LEU A 275      24.289  25.300  30.065  1.00 58.88           C  
ANISOU 1580  CD1 LEU A 275     7603   6655   8113  -1714   1356   -640       C  
ATOM   1581  CD2 LEU A 275      26.203  26.819  29.523  1.00 59.20           C  
ANISOU 1581  CD2 LEU A 275     7566   6612   8315  -2024   1619   -751       C  
ATOM   1582  N   CYS A 276      22.076  29.087  26.543  1.00 57.71           N  
ANISOU 1582  N   CYS A 276     8355   5849   7723  -1746   1843   -320       N  
ATOM   1583  CA  CYS A 276      21.559  29.385  25.215  1.00 57.98           C  
ANISOU 1583  CA  CYS A 276     8601   5774   7657  -1683   1953   -204       C  
ATOM   1584  C   CYS A 276      21.936  30.805  24.810  1.00 59.97           C  
ANISOU 1584  C   CYS A 276     9011   5845   7931  -1811   2135   -195       C  
ATOM   1585  O   CYS A 276      22.371  31.054  23.681  1.00 63.72           O  
ANISOU 1585  O   CYS A 276     9583   6248   8381  -1854   2298   -143       O  
ATOM   1586  CB  CYS A 276      20.045  29.185  25.198  1.00 57.58           C  
ANISOU 1586  CB  CYS A 276     8680   5710   7487  -1499   1827   -116       C  
ATOM   1587  SG  CYS A 276      19.593  27.439  25.172  1.00 61.93           S  
ANISOU 1587  SG  CYS A 276     9094   6446   7989  -1352   1664   -100       S  
ATOM   1588  N   ILE A 277      21.801  31.726  25.762  1.00 59.32           N  
ANISOU 1588  N   ILE A 277     8958   5684   7896  -1879   2114   -249       N  
ATOM   1589  CA  ILE A 277      22.202  33.095  25.563  1.00 60.48           C  
ANISOU 1589  CA  ILE A 277     9248   5650   8080  -2019   2284   -258       C  
ATOM   1590  C   ILE A 277      23.694  33.171  25.200  1.00 62.71           C  
ANISOU 1590  C   ILE A 277     9406   5950   8473  -2212   2441   -330       C  
ATOM   1591  O   ILE A 277      24.053  33.794  24.208  1.00 61.74           O  
ANISOU 1591  O   ILE A 277     9422   5700   8335  -2283   2631   -278       O  
ATOM   1592  CB  ILE A 277      21.846  33.968  26.788  1.00 59.15           C  
ANISOU 1592  CB  ILE A 277     9113   5410   7953  -2062   2220   -326       C  
ATOM   1593  CG1 ILE A 277      20.326  33.923  27.020  1.00 56.25           C  
ANISOU 1593  CG1 ILE A 277     8878   5022   7474  -1859   2087   -243       C  
ATOM   1594  CG2 ILE A 277      22.355  35.402  26.586  1.00 59.21           C  
ANISOU 1594  CG2 ILE A 277     9274   5215   8010  -2228   2410   -347       C  
ATOM   1595  CD1 ILE A 277      19.831  34.571  28.297  1.00 54.46           C  
ANISOU 1595  CD1 ILE A 277     8670   4750   7271  -1864   1999   -308       C  
ATOM   1596  N   GLN A 278      24.546  32.518  25.987  1.00 63.96           N  
ANISOU 1596  N   GLN A 278     9299   6267   8734  -2290   2362   -447       N  
ATOM   1597  CA  GLN A 278      25.986  32.501  25.723  1.00 67.88           C  
ANISOU 1597  CA  GLN A 278     9633   6810   9347  -2468   2495   -528       C  
ATOM   1598  C   GLN A 278      26.336  32.029  24.313  1.00 67.70           C  
ANISOU 1598  C   GLN A 278     9653   6790   9279  -2441   2638   -446       C  
ATOM   1599  O   GLN A 278      27.310  32.501  23.734  1.00 68.11           O  
ANISOU 1599  O   GLN A 278     9691   6789   9399  -2596   2828   -471       O  
ATOM   1600  CB  GLN A 278      26.708  31.625  26.738  1.00 71.41           C  
ANISOU 1600  CB  GLN A 278     9778   7464   9891  -2498   2352   -650       C  
ATOM   1601  CG  GLN A 278      26.944  32.312  28.071  1.00 81.14           C  
ANISOU 1601  CG  GLN A 278    10931   8692  11207  -2616   2276   -773       C  
ATOM   1602  CD  GLN A 278      27.568  31.382  29.095  1.00 87.27           C  
ANISOU 1602  CD  GLN A 278    11419   9685  12056  -2615   2111   -884       C  
ATOM   1603  OE1 GLN A 278      28.369  30.502  28.748  1.00 92.51           O  
ANISOU 1603  OE1 GLN A 278    11898  10485  12766  -2615   2124   -905       O  
ATOM   1604  NE2 GLN A 278      27.199  31.562  30.363  1.00 84.71           N  
ANISOU 1604  NE2 GLN A 278    11060   9391  11737  -2604   1957   -953       N  
ATOM   1605  N   HIS A 279      25.546  31.092  23.781  1.00 66.60           N  
ANISOU 1605  N   HIS A 279     9563   6714   9026  -2249   2549   -353       N  
ATOM   1606  CA  HIS A 279      25.730  30.565  22.417  1.00 68.02           C  
ANISOU 1606  CA  HIS A 279     9808   6900   9137  -2197   2667   -271       C  
ATOM   1607  C   HIS A 279      24.915  31.338  21.397  1.00 67.04           C  
ANISOU 1607  C   HIS A 279     9993   6596   8883  -2132   2775   -140       C  
ATOM   1608  O   HIS A 279      24.595  30.834  20.312  1.00 64.71           O  
ANISOU 1608  O   HIS A 279     9804   6304   8478  -2024   2814    -48       O  
ATOM   1609  CB  HIS A 279      25.432  29.043  22.352  1.00 65.02           C  
ANISOU 1609  CB  HIS A 279     9304   6693   8707  -2035   2517   -255       C  
ATOM   1610  CG  HIS A 279      26.409  28.180  23.144  1.00 64.87           C  
ANISOU 1610  CG  HIS A 279     8982   6854   8810  -2087   2440   -372       C  
ATOM   1611  ND1 HIS A 279      26.218  27.868  24.453  1.00 64.33           N  
ANISOU 1611  ND1 HIS A 279     8772   6881   8790  -2062   2255   -444       N  
ATOM   1612  CD2 HIS A 279      27.602  27.566  22.769  1.00 65.74           C  
ANISOU 1612  CD2 HIS A 279     8911   7069   9000  -2153   2529   -426       C  
ATOM   1613  CE1 HIS A 279      27.240  27.102  24.893  1.00 63.21           C  
ANISOU 1613  CE1 HIS A 279     8374   6895   8748  -2105   2221   -536       C  
ATOM   1614  NE2 HIS A 279      28.089  26.918  23.864  1.00 68.84           N  
ANISOU 1614  NE2 HIS A 279     9055   7615   9484  -2160   2389   -527       N  
ATOM   1615  N   GLY A 280      24.537  32.558  21.768  1.00 68.36           N  
ANISOU 1615  N   GLY A 280    10314   6605   9054  -2187   2814   -132       N  
ATOM   1616  CA  GLY A 280      23.966  33.530  20.834  1.00 69.55           C  
ANISOU 1616  CA  GLY A 280    10769   6559   9099  -2153   2952    -15       C  
ATOM   1617  C   GLY A 280      22.459  33.532  20.636  1.00 67.24           C  
ANISOU 1617  C   GLY A 280    10670   6222   8656  -1939   2828     97       C  
ATOM   1618  O   GLY A 280      21.969  34.093  19.648  1.00 68.15           O  
ANISOU 1618  O   GLY A 280    11033   6204   8657  -1872   2930    211       O  
ATOM   1619  N   TRP A 281      21.709  32.912  21.543  1.00 62.57           N  
ANISOU 1619  N   TRP A 281     9971   5744   8059  -1828   2611     68       N  
ATOM   1620  CA  TRP A 281      20.250  33.023  21.459  1.00 60.52           C  
ANISOU 1620  CA  TRP A 281     9879   5442   7671  -1636   2495    163       C  
ATOM   1621  C   TRP A 281      19.788  34.381  21.905  1.00 61.58           C  
ANISOU 1621  C   TRP A 281    10190   5398   7808  -1658   2540    178       C  
ATOM   1622  O   TRP A 281      20.216  34.868  22.957  1.00 61.11           O  
ANISOU 1622  O   TRP A 281    10041   5319   7860  -1781   2531     77       O  
ATOM   1623  CB  TRP A 281      19.571  31.950  22.287  1.00 57.39           C  
ANISOU 1623  CB  TRP A 281     9317   5217   7271  -1516   2265    129       C  
ATOM   1624  CG  TRP A 281      18.058  32.012  22.231  1.00 56.33           C  
ANISOU 1624  CG  TRP A 281     9327   5059   7016  -1323   2142    218       C  
ATOM   1625  CD1 TRP A 281      17.234  32.003  21.093  1.00 54.36           C  
ANISOU 1625  CD1 TRP A 281     9265   4767   6622  -1178   2154    339       C  
ATOM   1626  CD2 TRP A 281      17.136  32.081  23.369  1.00 54.48           C  
ANISOU 1626  CD2 TRP A 281     9055   4854   6791  -1243   1981    192       C  
ATOM   1627  NE1 TRP A 281      15.909  32.061  21.445  1.00 54.61           N  
ANISOU 1627  NE1 TRP A 281     9359   4806   6583  -1020   2011    385       N  
ATOM   1628  CE2 TRP A 281      15.775  32.104  22.794  1.00 54.04           C  
ANISOU 1628  CE2 TRP A 281     9160   4774   6599  -1050   1909    303       C  
ATOM   1629  CE3 TRP A 281      17.290  32.112  24.753  1.00 53.67           C  
ANISOU 1629  CE3 TRP A 281     8807   4799   6785  -1305   1893     91       C  
ATOM   1630  CZ2 TRP A 281      14.643  32.171  23.591  1.00 53.24           C  
ANISOU 1630  CZ2 TRP A 281     9059   4695   6474   -933   1766    309       C  
ATOM   1631  CZ3 TRP A 281      16.132  32.174  25.551  1.00 52.22           C  
ANISOU 1631  CZ3 TRP A 281     8643   4631   6566  -1184   1752    101       C  
ATOM   1632  CH2 TRP A 281      14.843  32.208  24.984  1.00 51.76           C  
ANISOU 1632  CH2 TRP A 281     8730   4547   6388  -1004   1695    208       C  
ATOM   1633  N   THR A 282      18.932  35.014  21.102  1.00 61.70           N  
ANISOU 1633  N   THR A 282    10463   5282   7699  -1538   2589    300       N  
ATOM   1634  CA  THR A 282      18.298  36.258  21.527  1.00 64.29           C  
ANISOU 1634  CA  THR A 282    10977   5437   8013  -1516   2615    327       C  
ATOM   1635  C   THR A 282      17.101  35.920  22.395  1.00 62.78           C  
ANISOU 1635  C   THR A 282    10735   5328   7788  -1356   2402    325       C  
ATOM   1636  O   THR A 282      16.105  35.379  21.905  1.00 65.40           O  
ANISOU 1636  O   THR A 282    11116   5725   8007  -1171   2296    409       O  
ATOM   1637  CB  THR A 282      17.876  37.157  20.354  1.00 66.10           C  
ANISOU 1637  CB  THR A 282    11516   5479   8120  -1442   2761    464       C  
ATOM   1638  OG1 THR A 282      19.043  37.751  19.790  1.00 70.53           O  
ANISOU 1638  OG1 THR A 282    12139   5923   8736  -1628   2989    451       O  
ATOM   1639  CG2 THR A 282      16.960  38.279  20.824  1.00 66.14           C  
ANISOU 1639  CG2 THR A 282    11713   5324   8092  -1359   2747    504       C  
ATOM   1640  N   PRO A 283      17.193  36.242  23.689  1.00 63.42           N  
ANISOU 1640  N   PRO A 283    10718   5412   7968  -1431   2340    223       N  
ATOM   1641  CA  PRO A 283      16.171  35.813  24.644  1.00 61.31           C  
ANISOU 1641  CA  PRO A 283    10369   5244   7683  -1297   2142    205       C  
ATOM   1642  C   PRO A 283      14.881  36.635  24.528  1.00 63.54           C  
ANISOU 1642  C   PRO A 283    10874   5402   7868  -1129   2122    300       C  
ATOM   1643  O   PRO A 283      14.920  37.763  24.045  1.00 66.74           O  
ANISOU 1643  O   PRO A 283    11496   5614   8247  -1150   2268    352       O  
ATOM   1644  CB  PRO A 283      16.840  36.102  25.983  1.00 62.03           C  
ANISOU 1644  CB  PRO A 283    10320   5346   7904  -1452   2121     64       C  
ATOM   1645  CG  PRO A 283      17.692  37.322  25.716  1.00 62.87           C  
ANISOU 1645  CG  PRO A 283    10560   5260   8067  -1625   2325     42       C  
ATOM   1646  CD  PRO A 283      18.171  37.178  24.292  1.00 63.11           C  
ANISOU 1646  CD  PRO A 283    10673   5257   8048  -1642   2466    126       C  
ATOM   1647  N   GLY A 284      13.755  36.079  24.975  1.00 64.60           N  
ANISOU 1647  N   GLY A 284    10952   5643   7951   -962   1949    321       N  
ATOM   1648  CA  GLY A 284      12.519  36.866  25.185  1.00 63.16           C  
ANISOU 1648  CA  GLY A 284    10935   5363   7700   -803   1911    386       C  
ATOM   1649  C   GLY A 284      12.423  37.435  26.601  1.00 65.24           C  
ANISOU 1649  C   GLY A 284    11157   5586   8043   -854   1873    290       C  
ATOM   1650  O   GLY A 284      13.447  37.672  27.260  1.00 65.51           O  
ANISOU 1650  O   GLY A 284    11111   5598   8183  -1040   1930    182       O  
ATOM   1651  N   ASN A 285      11.199  37.670  27.078  1.00 63.83           N  
ANISOU 1651  N   ASN A 285    11033   5404   7815   -688   1778    324       N  
ATOM   1652  CA  ASN A 285      10.998  38.040  28.487  1.00 66.56           C  
ANISOU 1652  CA  ASN A 285    11324   5740   8225   -715   1723    230       C  
ATOM   1653  C   ASN A 285       9.593  37.714  29.015  1.00 62.94           C  
ANISOU 1653  C   ASN A 285    10832   5371   7710   -514   1575    264       C  
ATOM   1654  O   ASN A 285       9.011  38.486  29.783  1.00 66.53           O  
ANISOU 1654  O   ASN A 285    11369   5742   8170   -459   1572    244       O  
ATOM   1655  CB  ASN A 285      11.395  39.520  28.761  1.00 73.54           C  
ANISOU 1655  CB  ASN A 285    12399   6392   9149   -813   1875    198       C  
ATOM   1656  CG  ASN A 285      10.450  40.535  28.102  1.00 79.32           C  
ANISOU 1656  CG  ASN A 285    13399   6950   9789   -647   1945    319       C  
ATOM   1657  OD1 ASN A 285       9.644  40.192  27.227  1.00 81.07           O  
ANISOU 1657  OD1 ASN A 285    13673   7219   9912   -473   1898    433       O  
ATOM   1658  ND2 ASN A 285      10.549  41.796  28.527  1.00 78.33           N  
ANISOU 1658  ND2 ASN A 285    13447   6621   9693   -698   2056    289       N  
ATOM   1659  N   GLY A 286       9.057  36.570  28.594  1.00 57.36           N  
ANISOU 1659  N   GLY A 286    10007   4834   6954   -410   1458    311       N  
ATOM   1660  CA  GLY A 286       7.765  36.089  29.079  1.00 53.80           C  
ANISOU 1660  CA  GLY A 286     9486   4495   6459   -237   1314    335       C  
ATOM   1661  C   GLY A 286       7.980  35.009  30.130  1.00 53.15           C  
ANISOU 1661  C   GLY A 286     9168   4586   6439   -301   1198    240       C  
ATOM   1662  O   GLY A 286       9.134  34.629  30.427  1.00 49.35           O  
ANISOU 1662  O   GLY A 286     8578   4143   6029   -466   1220    160       O  
ATOM   1663  N   ARG A 287       6.876  34.519  30.699  1.00 51.07           N  
ANISOU 1663  N   ARG A 287     8825   4429   6149   -168   1077    251       N  
ATOM   1664  CA  ARG A 287       6.946  33.422  31.650  1.00 51.22           C  
ANISOU 1664  CA  ARG A 287     8637   4614   6212   -207    966    177       C  
ATOM   1665  C   ARG A 287       6.981  32.066  30.941  1.00 48.73           C  
ANISOU 1665  C   ARG A 287     8193   4448   5872   -193    891    209       C  
ATOM   1666  O   ARG A 287       7.191  31.047  31.594  1.00 46.28           O  
ANISOU 1666  O   ARG A 287     7717   4270   5598   -235    810    154       O  
ATOM   1667  CB  ARG A 287       5.758  33.419  32.600  1.00 53.48           C  
ANISOU 1667  CB  ARG A 287     8888   4950   6482    -82    880    172       C  
ATOM   1668  CG  ARG A 287       5.430  34.735  33.253  1.00 57.91           C  
ANISOU 1668  CG  ARG A 287     9590   5363   7048    -50    945    152       C  
ATOM   1669  CD  ARG A 287       4.139  34.598  34.046  1.00 59.13           C  
ANISOU 1669  CD  ARG A 287     9699   5590   7179     98    861    159       C  
ATOM   1670  NE  ARG A 287       4.280  33.822  35.284  1.00 60.22           N  
ANISOU 1670  NE  ARG A 287     9674   5850   7357     38    783     73       N  
ATOM   1671  CZ  ARG A 287       3.244  33.539  36.081  1.00 60.90           C  
ANISOU 1671  CZ  ARG A 287     9694   6017   7427    146    714     70       C  
ATOM   1672  NH1 ARG A 287       2.023  33.965  35.729  1.00 57.19           N  
ANISOU 1672  NH1 ARG A 287     9292   5526   6910    317    710    144       N  
ATOM   1673  NH2 ARG A 287       3.410  32.841  37.211  1.00 52.96           N  
ANISOU 1673  NH2 ARG A 287     8557   5115   6449     91    653     -4       N  
ATOM   1674  N   PHE A 288       6.777  32.061  29.624  1.00 45.97           N  
ANISOU 1674  N   PHE A 288     7934   4075   5457   -130    921    296       N  
ATOM   1675  CA  PHE A 288       6.511  30.833  28.870  1.00 44.76           C  
ANISOU 1675  CA  PHE A 288     7686   4059   5261    -82    842    334       C  
ATOM   1676  C   PHE A 288       7.150  30.853  27.488  1.00 46.16           C  
ANISOU 1676  C   PHE A 288     7956   4188   5394   -116    925    386       C  
ATOM   1677  O   PHE A 288       6.525  30.470  26.505  1.00 44.79           O  
ANISOU 1677  O   PHE A 288     7821   4058   5137    -14    885    458       O  
ATOM   1678  CB  PHE A 288       4.991  30.573  28.755  1.00 46.93           C  
ANISOU 1678  CB  PHE A 288     7953   4408   5468     96    737    394       C  
ATOM   1679  CG  PHE A 288       4.273  30.455  30.102  1.00 48.77           C  
ANISOU 1679  CG  PHE A 288     8088   4702   5740    137    660    346       C  
ATOM   1680  CD1 PHE A 288       4.406  29.302  30.900  1.00 47.09           C  
ANISOU 1680  CD1 PHE A 288     7695   4623   5573     83    579    285       C  
ATOM   1681  CD2 PHE A 288       3.462  31.479  30.565  1.00 48.66           C  
ANISOU 1681  CD2 PHE A 288     8168   4607   5712    237    677    366       C  
ATOM   1682  CE1 PHE A 288       3.767  29.201  32.135  1.00 46.76           C  
ANISOU 1682  CE1 PHE A 288     7576   4633   5558    119    521    245       C  
ATOM   1683  CE2 PHE A 288       2.811  31.371  31.800  1.00 50.12           C  
ANISOU 1683  CE2 PHE A 288     8266   4848   5928    276    618    320       C  
ATOM   1684  CZ  PHE A 288       2.965  30.232  32.585  1.00 48.53           C  
ANISOU 1684  CZ  PHE A 288     7890   4782   5768    213    542    261       C  
ATOM   1685  N   ASP A 289       8.402  31.300  27.419  1.00 46.82           N  
ANISOU 1685  N   ASP A 289     8072   4186   5531   -263   1041    347       N  
ATOM   1686  CA  ASP A 289       9.124  31.311  26.162  1.00 48.90           C  
ANISOU 1686  CA  ASP A 289     8418   4402   5760   -311   1140    390       C  
ATOM   1687  C   ASP A 289       9.699  29.932  25.943  1.00 47.61           C  
ANISOU 1687  C   ASP A 289     8090   4384   5616   -366   1089    354       C  
ATOM   1688  O   ASP A 289      10.376  29.411  26.811  1.00 47.18           O  
ANISOU 1688  O   ASP A 289     7882   4397   5646   -464   1062    269       O  
ATOM   1689  CB  ASP A 289      10.253  32.346  26.196  1.00 50.99           C  
ANISOU 1689  CB  ASP A 289     8772   4516   6084   -460   1298    356       C  
ATOM   1690  CG  ASP A 289       9.742  33.763  26.397  1.00 53.88           C  
ANISOU 1690  CG  ASP A 289     9326   4713   6432   -411   1366    390       C  
ATOM   1691  OD1 ASP A 289       8.570  34.018  26.064  1.00 55.26           O  
ANISOU 1691  OD1 ASP A 289     9600   4874   6524   -241   1315    471       O  
ATOM   1692  OD2 ASP A 289      10.501  34.628  26.889  1.00 54.30           O  
ANISOU 1692  OD2 ASP A 289     9428   4648   6557   -539   1469    334       O  
ATOM   1693  N   VAL A 290       9.439  29.342  24.782  1.00 48.77           N  
ANISOU 1693  N   VAL A 290     8274   4576   5679   -298   1075    417       N  
ATOM   1694  CA  VAL A 290      10.006  28.031  24.464  1.00 46.22           C  
ANISOU 1694  CA  VAL A 290     7816   4376   5368   -346   1040    385       C  
ATOM   1695  C   VAL A 290      11.521  28.120  24.206  1.00 49.18           C  
ANISOU 1695  C   VAL A 290     8169   4709   5808   -501   1174    340       C  
ATOM   1696  O   VAL A 290      11.993  28.958  23.409  1.00 53.01           O  
ANISOU 1696  O   VAL A 290     8800   5075   6266   -540   1310    381       O  
ATOM   1697  CB  VAL A 290       9.260  27.382  23.285  1.00 47.41           C  
ANISOU 1697  CB  VAL A 290     8022   4586   5403   -229    986    456       C  
ATOM   1698  CG1 VAL A 290       9.915  26.059  22.864  1.00 45.55           C  
ANISOU 1698  CG1 VAL A 290     7671   4459   5177   -281    969    420       C  
ATOM   1699  CG2 VAL A 290       7.789  27.171  23.651  1.00 45.17           C  
ANISOU 1699  CG2 VAL A 290     7715   4373   5076    -89    843    483       C  
ATOM   1700  N   LEU A 291      12.294  27.291  24.900  1.00 44.58           N  
ANISOU 1700  N   LEU A 291     7405   4221   5311   -589   1141    257       N  
ATOM   1701  CA  LEU A 291      13.741  27.317  24.701  1.00 47.24           C  
ANISOU 1701  CA  LEU A 291     7690   4540   5720   -733   1260    207       C  
ATOM   1702  C   LEU A 291      14.153  26.804  23.331  1.00 47.15           C  
ANISOU 1702  C   LEU A 291     7728   4540   5647   -727   1335    252       C  
ATOM   1703  O   LEU A 291      13.488  25.961  22.747  1.00 45.74           O  
ANISOU 1703  O   LEU A 291     7556   4433   5388   -626   1257    292       O  
ATOM   1704  CB  LEU A 291      14.468  26.543  25.811  1.00 44.94           C  
ANISOU 1704  CB  LEU A 291     7185   4358   5533   -811   1195    107       C  
ATOM   1705  CG  LEU A 291      14.492  27.310  27.144  1.00 45.07           C  
ANISOU 1705  CG  LEU A 291     7166   4339   5620   -866   1169     44       C  
ATOM   1706  CD1 LEU A 291      14.792  26.357  28.283  1.00 44.44           C  
ANISOU 1706  CD1 LEU A 291     6888   4392   5605   -885   1056    -35       C  
ATOM   1707  CD2 LEU A 291      15.505  28.446  27.096  1.00 45.43           C  
ANISOU 1707  CD2 LEU A 291     7265   4266   5729  -1009   1316      7       C  
ATOM   1708  N   PRO A 292      15.251  27.343  22.790  1.00 49.27           N  
ANISOU 1708  N   PRO A 292     8040   4733   5949   -840   1494    243       N  
ATOM   1709  CA  PRO A 292      15.822  26.685  21.634  1.00 48.97           C  
ANISOU 1709  CA  PRO A 292     8012   4726   5866   -848   1569    267       C  
ATOM   1710  C   PRO A 292      16.605  25.440  22.055  1.00 48.82           C  
ANISOU 1710  C   PRO A 292     7778   4846   5926   -894   1522    187       C  
ATOM   1711  O   PRO A 292      16.930  25.253  23.226  1.00 49.12           O  
ANISOU 1711  O   PRO A 292     7662   4940   6060   -946   1456    111       O  
ATOM   1712  CB  PRO A 292      16.780  27.737  21.093  1.00 51.78           C  
ANISOU 1712  CB  PRO A 292     8469   4953   6250   -968   1767    275       C  
ATOM   1713  CG  PRO A 292      17.198  28.487  22.304  1.00 52.15           C  
ANISOU 1713  CG  PRO A 292     8442   4959   6415  -1076   1774    200       C  
ATOM   1714  CD  PRO A 292      15.956  28.586  23.122  1.00 48.66           C  
ANISOU 1714  CD  PRO A 292     8016   4529   5942   -965   1621    214       C  
ATOM   1715  N   LEU A 293      16.907  24.593  21.091  1.00 49.79           N  
ANISOU 1715  N   LEU A 293     7899   5021   5999   -869   1556    205       N  
ATOM   1716  CA  LEU A 293      17.688  23.410  21.327  1.00 48.72           C  
ANISOU 1716  CA  LEU A 293     7580   5003   5928   -898   1529    138       C  
ATOM   1717  C   LEU A 293      19.154  23.737  21.180  1.00 50.32           C  
ANISOU 1717  C   LEU A 293     7711   5186   6223  -1037   1687     87       C  
ATOM   1718  O   LEU A 293      19.567  24.503  20.303  1.00 52.46           O  
ANISOU 1718  O   LEU A 293     8106   5360   6465  -1091   1843    125       O  
ATOM   1719  CB  LEU A 293      17.297  22.340  20.308  1.00 50.55           C  
ANISOU 1719  CB  LEU A 293     7857   5293   6058   -802   1499    176       C  
ATOM   1720  CG  LEU A 293      16.307  21.235  20.704  1.00 52.85           C  
ANISOU 1720  CG  LEU A 293     8089   5680   6313   -695   1321    173       C  
ATOM   1721  CD1 LEU A 293      15.458  21.565  21.931  1.00 51.47           C  
ANISOU 1721  CD1 LEU A 293     7871   5513   6173   -666   1194    163       C  
ATOM   1722  CD2 LEU A 293      15.442  20.881  19.506  1.00 55.17           C  
ANISOU 1722  CD2 LEU A 293     8530   5970   6463   -593   1297    240       C  
ATOM   1723  N   LEU A 294      19.953  23.146  22.036  1.00 48.92           N  
ANISOU 1723  N   LEU A 294     7329   5103   6156  -1093   1649      2       N  
ATOM   1724  CA  LEU A 294      21.376  23.263  21.904  1.00 49.67           C  
ANISOU 1724  CA  LEU A 294     7315   5211   6346  -1217   1784    -57       C  
ATOM   1725  C   LEU A 294      21.827  21.828  21.693  1.00 50.42           C  
ANISOU 1725  C   LEU A 294     7277   5431   6451  -1162   1747    -86       C  
ATOM   1726  O   LEU A 294      21.653  20.980  22.586  1.00 48.88           O  
ANISOU 1726  O   LEU A 294     6950   5332   6290  -1110   1605   -127       O  
ATOM   1727  CB  LEU A 294      21.922  23.838  23.198  1.00 49.62           C  
ANISOU 1727  CB  LEU A 294     7172   5218   6464  -1321   1753   -142       C  
ATOM   1728  CG  LEU A 294      23.054  24.866  23.260  1.00 53.04           C  
ANISOU 1728  CG  LEU A 294     7566   5590   6997  -1492   1907   -196       C  
ATOM   1729  CD1 LEU A 294      23.295  25.721  22.011  1.00 51.39           C  
ANISOU 1729  CD1 LEU A 294     7536   5250   6742  -1552   2107   -134       C  
ATOM   1730  CD2 LEU A 294      22.780  25.732  24.495  1.00 53.07           C  
ANISOU 1730  CD2 LEU A 294     7555   5554   7055  -1548   1832   -244       C  
ATOM   1731  N   LEU A 295      22.355  21.546  20.498  1.00 51.09           N  
ANISOU 1731  N   LEU A 295     7412   5505   6494  -1166   1879    -62       N  
ATOM   1732  CA  LEU A 295      22.645  20.170  20.062  1.00 48.95           C  
ANISOU 1732  CA  LEU A 295     7063   5332   6205  -1093   1858    -77       C  
ATOM   1733  C   LEU A 295      24.105  19.959  19.739  1.00 50.77           C  
ANISOU 1733  C   LEU A 295     7159   5606   6524  -1176   2005   -133       C  
ATOM   1734  O   LEU A 295      24.741  20.809  19.150  1.00 54.63           O  
ANISOU 1734  O   LEU A 295     7699   6027   7031  -1274   2172   -125       O  
ATOM   1735  CB  LEU A 295      21.817  19.826  18.854  1.00 46.68           C  
ANISOU 1735  CB  LEU A 295     6966   5006   5767   -994   1868      2       C  
ATOM   1736  CG  LEU A 295      20.330  20.079  19.044  1.00 43.94           C  
ANISOU 1736  CG  LEU A 295     6749   4620   5326   -907   1730     60       C  
ATOM   1737  CD1 LEU A 295      19.644  19.803  17.719  1.00 42.75           C  
ANISOU 1737  CD1 LEU A 295     6784   4438   5022   -819   1751    131       C  
ATOM   1738  CD2 LEU A 295      19.813  19.179  20.151  1.00 42.37           C  
ANISOU 1738  CD2 LEU A 295     6418   4512   5167   -846   1547     20       C  
ATOM   1739  N   GLN A 296      24.641  18.820  20.147  1.00 51.87           N  
ANISOU 1739  N   GLN A 296     7125   5862   6723  -1134   1945   -189       N  
ATOM   1740  CA  GLN A 296      26.068  18.645  20.125  1.00 53.10           C  
ANISOU 1740  CA  GLN A 296     7104   6082   6990  -1210   2060   -257       C  
ATOM   1741  C   GLN A 296      26.404  17.341  19.463  1.00 54.61           C  
ANISOU 1741  C   GLN A 296     7256   6343   7150  -1117   2083   -262       C  
ATOM   1742  O   GLN A 296      25.987  16.284  19.935  1.00 52.60           O  
ANISOU 1742  O   GLN A 296     6951   6154   6881  -1012   1942   -272       O  
ATOM   1743  CB  GLN A 296      26.650  18.672  21.537  1.00 54.61           C  
ANISOU 1743  CB  GLN A 296     7076   6360   7316  -1261   1965   -342       C  
ATOM   1744  CG  GLN A 296      28.041  18.056  21.595  1.00 56.49           C  
ANISOU 1744  CG  GLN A 296     7091   6708   7664  -1290   2034   -417       C  
ATOM   1745  CD  GLN A 296      28.779  18.408  22.852  1.00 58.79           C  
ANISOU 1745  CD  GLN A 296     7172   7078   8090  -1373   1971   -507       C  
ATOM   1746  OE1 GLN A 296      28.446  17.936  23.945  1.00 56.57           O  
ANISOU 1746  OE1 GLN A 296     6808   6863   7825  -1311   1798   -532       O  
ATOM   1747  NE2 GLN A 296      29.800  19.244  22.707  1.00 58.90           N  
ANISOU 1747  NE2 GLN A 296     7096   7085   8197  -1520   2115   -558       N  
ATOM   1748  N   ALA A 297      27.164  17.456  18.374  1.00 53.56           N  
ANISOU 1748  N   ALA A 297     7156   6187   7006  -1158   2271   -255       N  
ATOM   1749  CA  ALA A 297      27.700  16.359  17.611  1.00 54.91           C  
ANISOU 1749  CA  ALA A 297     7293   6415   7156  -1086   2341   -268       C  
ATOM   1750  C   ALA A 297      29.168  16.103  18.051  1.00 56.64           C  
ANISOU 1750  C   ALA A 297     7252   6737   7530  -1144   2417   -355       C  
ATOM   1751  O   ALA A 297      29.840  16.996  18.564  1.00 54.23           O  
ANISOU 1751  O   ALA A 297     6834   6438   7332  -1269   2471   -398       O  
ATOM   1752  CB  ALA A 297      27.634  16.692  16.116  1.00 54.08           C  
ANISOU 1752  CB  ALA A 297     7392   6222   6934  -1094   2513   -206       C  
ATOM   1753  N   PRO A 298      29.659  14.867  17.857  1.00 58.71           N  
ANISOU 1753  N   PRO A 298     7417   7084   7805  -1048   2417   -386       N  
ATOM   1754  CA  PRO A 298      30.981  14.498  18.353  1.00 59.48           C  
ANISOU 1754  CA  PRO A 298     7253   7299   8050  -1071   2461   -469       C  
ATOM   1755  C   PRO A 298      32.048  15.545  18.121  1.00 61.93           C  
ANISOU 1755  C   PRO A 298     7467   7606   8459  -1230   2644   -507       C  
ATOM   1756  O   PRO A 298      32.242  15.993  16.989  1.00 63.17           O  
ANISOU 1756  O   PRO A 298     7748   7690   8562  -1282   2830   -471       O  
ATOM   1757  CB  PRO A 298      31.280  13.233  17.560  1.00 60.79           C  
ANISOU 1757  CB  PRO A 298     7426   7503   8170   -949   2518   -471       C  
ATOM   1758  CG  PRO A 298      29.928  12.562  17.496  1.00 58.22           C  
ANISOU 1758  CG  PRO A 298     7284   7125   7710   -833   2368   -415       C  
ATOM   1759  CD  PRO A 298      28.946  13.693  17.301  1.00 56.02           C  
ANISOU 1759  CD  PRO A 298     7198   6739   7348   -903   2353   -352       C  
ATOM   1760  N   ASP A 299      32.697  15.950  19.213  1.00 63.79           N  
ANISOU 1760  N   ASP A 299     7488   7917   8831  -1312   2588   -579       N  
ATOM   1761  CA  ASP A 299      33.895  16.790  19.184  1.00 67.89           C  
ANISOU 1761  CA  ASP A 299     7849   8465   9479  -1472   2747   -642       C  
ATOM   1762  C   ASP A 299      33.644  18.162  18.598  1.00 69.33           C  
ANISOU 1762  C   ASP A 299     8210   8507   9627  -1618   2888   -598       C  
ATOM   1763  O   ASP A 299      34.568  18.829  18.130  1.00 70.55           O  
ANISOU 1763  O   ASP A 299     8300   8650   9856  -1753   3082   -629       O  
ATOM   1764  CB  ASP A 299      35.033  16.082  18.448  1.00 69.70           C  
ANISOU 1764  CB  ASP A 299     7939   8779   9763  -1442   2907   -680       C  
ATOM   1765  CG  ASP A 299      35.376  14.748  19.081  1.00 73.01           C  
ANISOU 1765  CG  ASP A 299     8174   9337  10229  -1291   2772   -726       C  
ATOM   1766  OD1 ASP A 299      36.019  14.753  20.150  1.00 74.77           O  
ANISOU 1766  OD1 ASP A 299     8159   9674  10576  -1317   2678   -803       O  
ATOM   1767  OD2 ASP A 299      34.991  13.695  18.521  1.00 73.41           O  
ANISOU 1767  OD2 ASP A 299     8324   9380  10187  -1143   2757   -686       O  
ATOM   1768  N   GLU A 300      32.389  18.590  18.647  1.00 69.40           N  
ANISOU 1768  N   GLU A 300     8441   8405   9522  -1589   2793   -526       N  
ATOM   1769  CA  GLU A 300      32.030  19.915  18.179  1.00 70.76           C  
ANISOU 1769  CA  GLU A 300     8805   8430   9651  -1707   2908   -475       C  
ATOM   1770  C   GLU A 300      31.363  20.682  19.279  1.00 67.73           C  
ANISOU 1770  C   GLU A 300     8442   8005   9288  -1753   2758   -485       C  
ATOM   1771  O   GLU A 300      30.789  20.089  20.190  1.00 67.47           O  
ANISOU 1771  O   GLU A 300     8354   8033   9248  -1658   2553   -498       O  
ATOM   1772  CB  GLU A 300      31.118  19.823  16.971  1.00 74.94           C  
ANISOU 1772  CB  GLU A 300     9620   8852  10003  -1618   2964   -368       C  
ATOM   1773  CG  GLU A 300      31.869  19.455  15.704  1.00 81.75           C  
ANISOU 1773  CG  GLU A 300    10508   9718  10835  -1616   3176   -355       C  
ATOM   1774  CD  GLU A 300      31.103  19.860  14.469  1.00 88.52           C  
ANISOU 1774  CD  GLU A 300    11673  10441  11520  -1583   3276   -250       C  
ATOM   1775  OE1 GLU A 300      29.974  19.339  14.295  1.00 86.03           O  
ANISOU 1775  OE1 GLU A 300    11510  10104  11071  -1449   3135   -193       O  
ATOM   1776  OE2 GLU A 300      31.629  20.703  13.689  1.00 92.05           O  
ANISOU 1776  OE2 GLU A 300    12207  10806  11963  -1693   3494   -225       O  
ATOM   1777  N   ALA A 301      31.468  22.004  19.214  1.00 67.46           N  
ANISOU 1777  N   ALA A 301     8490   7861   9282  -1903   2870   -480       N  
ATOM   1778  CA  ALA A 301      30.748  22.874  20.137  1.00 64.50           C  
ANISOU 1778  CA  ALA A 301     8182   7416   8910  -1947   2751   -482       C  
ATOM   1779  C   ALA A 301      29.259  22.666  19.848  1.00 60.81           C  
ANISOU 1779  C   ALA A 301     7954   6872   8280  -1798   2637   -378       C  
ATOM   1780  O   ALA A 301      28.887  22.267  18.739  1.00 59.95           O  
ANISOU 1780  O   ALA A 301     7999   6725   8056  -1713   2704   -303       O  
ATOM   1781  CB  ALA A 301      31.160  24.334  19.928  1.00 62.74           C  
ANISOU 1781  CB  ALA A 301     8036   7065   8738  -2136   2926   -490       C  
ATOM   1782  N   PRO A 302      28.395  22.919  20.829  1.00 59.62           N  
ANISOU 1782  N   PRO A 302     7833   6706   8116  -1764   2463   -378       N  
ATOM   1783  CA  PRO A 302      26.970  22.744  20.470  1.00 59.23           C  
ANISOU 1783  CA  PRO A 302     8002   6589   7914  -1624   2366   -280       C  
ATOM   1784  C   PRO A 302      26.473  23.844  19.526  1.00 60.69           C  
ANISOU 1784  C   PRO A 302     8447   6607   8004  -1658   2503   -193       C  
ATOM   1785  O   PRO A 302      27.003  24.960  19.549  1.00 61.54           O  
ANISOU 1785  O   PRO A 302     8580   6627   8175  -1802   2634   -211       O  
ATOM   1786  CB  PRO A 302      26.247  22.820  21.813  1.00 55.47           C  
ANISOU 1786  CB  PRO A 302     7479   6139   7460  -1590   2166   -308       C  
ATOM   1787  CG  PRO A 302      27.167  23.610  22.687  1.00 58.48           C  
ANISOU 1787  CG  PRO A 302     7708   6531   7979  -1748   2201   -402       C  
ATOM   1788  CD  PRO A 302      28.586  23.373  22.216  1.00 59.50           C  
ANISOU 1788  CD  PRO A 302     7674   6730   8206  -1841   2352   -462       C  
ATOM   1789  N   GLU A 303      25.493  23.504  18.691  1.00 59.79           N  
ANISOU 1789  N   GLU A 303     8524   6453   7742  -1528   2473   -100       N  
ATOM   1790  CA  GLU A 303      24.831  24.448  17.791  1.00 60.17           C  
ANISOU 1790  CA  GLU A 303     8840   6351   7672  -1519   2570     -3       C  
ATOM   1791  C   GLU A 303      23.399  24.676  18.224  1.00 56.50           C  
ANISOU 1791  C   GLU A 303     8502   5844   7120  -1409   2401     52       C  
ATOM   1792  O   GLU A 303      22.739  23.779  18.743  1.00 51.83           O  
ANISOU 1792  O   GLU A 303     7840   5345   6509  -1303   2222     41       O  
ATOM   1793  CB  GLU A 303      24.791  23.910  16.367  1.00 62.26           C  
ANISOU 1793  CB  GLU A 303     9239   6606   7810  -1443   2669     64       C  
ATOM   1794  CG  GLU A 303      26.047  24.148  15.560  1.00 71.96           C  
ANISOU 1794  CG  GLU A 303    10446   7812   9083  -1557   2906     48       C  
ATOM   1795  CD  GLU A 303      26.109  23.273  14.314  1.00 78.59           C  
ANISOU 1795  CD  GLU A 303    11369   8685   9808  -1466   2979     90       C  
ATOM   1796  OE1 GLU A 303      25.043  22.998  13.699  1.00 78.55           O  
ANISOU 1796  OE1 GLU A 303    11548   8654   9646  -1334   2898    165       O  
ATOM   1797  OE2 GLU A 303      27.235  22.855  13.958  1.00 82.38           O  
ANISOU 1797  OE2 GLU A 303    11723   9222  10355  -1526   3115     41       O  
ATOM   1798  N   LEU A 304      22.903  25.863  17.920  1.00 57.27           N  
ANISOU 1798  N   LEU A 304     8801   5798   7161  -1429   2470    117       N  
ATOM   1799  CA  LEU A 304      21.625  26.339  18.423  1.00 56.34           C  
ANISOU 1799  CA  LEU A 304     8798   5627   6981  -1340   2332    163       C  
ATOM   1800  C   LEU A 304      20.520  26.172  17.390  1.00 53.62           C  
ANISOU 1800  C   LEU A 304     8664   5247   6461  -1188   2296    270       C  
ATOM   1801  O   LEU A 304      20.690  26.509  16.238  1.00 55.28           O  
ANISOU 1801  O   LEU A 304     9037   5382   6584  -1187   2438    335       O  
ATOM   1802  CB  LEU A 304      21.804  27.811  18.756  1.00 58.00           C  
ANISOU 1802  CB  LEU A 304     9104   5692   7243  -1453   2436    165       C  
ATOM   1803  CG  LEU A 304      20.830  28.579  19.618  1.00 57.75           C  
ANISOU 1803  CG  LEU A 304     9148   5591   7204  -1412   2326    178       C  
ATOM   1804  CD1 LEU A 304      20.800  28.013  21.028  1.00 56.40           C  
ANISOU 1804  CD1 LEU A 304     8759   5540   7130  -1416   2155     85       C  
ATOM   1805  CD2 LEU A 304      21.322  30.021  19.601  1.00 60.61           C  
ANISOU 1805  CD2 LEU A 304     9629   5786   7613  -1548   2496    180       C  
ATOM   1806  N   PHE A 305      19.385  25.645  17.795  1.00 52.52           N  
ANISOU 1806  N   PHE A 305     8522   5169   6266  -1060   2106    287       N  
ATOM   1807  CA  PHE A 305      18.271  25.492  16.863  1.00 52.09           C  
ANISOU 1807  CA  PHE A 305     8650   5095   6045   -914   2051    380       C  
ATOM   1808  C   PHE A 305      16.978  25.919  17.526  1.00 53.06           C  
ANISOU 1808  C   PHE A 305     8828   5198   6134   -820   1899    412       C  
ATOM   1809  O   PHE A 305      16.621  25.400  18.603  1.00 50.62           O  
ANISOU 1809  O   PHE A 305     8367   4973   5892   -801   1753    357       O  
ATOM   1810  CB  PHE A 305      18.158  24.039  16.356  1.00 49.18           C  
ANISOU 1810  CB  PHE A 305     8213   4853   5620   -835   1972    365       C  
ATOM   1811  CG  PHE A 305      19.323  23.590  15.508  1.00 48.92           C  
ANISOU 1811  CG  PHE A 305     8155   4837   5594   -899   2130    345       C  
ATOM   1812  CD1 PHE A 305      19.327  23.800  14.139  1.00 49.69           C  
ANISOU 1812  CD1 PHE A 305     8448   4873   5559   -865   2252    417       C  
ATOM   1813  CD2 PHE A 305      20.419  22.948  16.080  1.00 49.57           C  
ANISOU 1813  CD2 PHE A 305     8020   5003   5812   -986   2159    254       C  
ATOM   1814  CE1 PHE A 305      20.416  23.406  13.362  1.00 51.34           C  
ANISOU 1814  CE1 PHE A 305     8635   5096   5774   -925   2413    397       C  
ATOM   1815  CE2 PHE A 305      21.502  22.536  15.307  1.00 47.37           C  
ANISOU 1815  CE2 PHE A 305     7707   4745   5546  -1038   2313    233       C  
ATOM   1816  CZ  PHE A 305      21.497  22.762  13.952  1.00 49.39           C  
ANISOU 1816  CZ  PHE A 305     8159   4935   5672  -1011   2444    303       C  
ATOM   1817  N   VAL A 306      16.283  26.864  16.887  1.00 54.40           N  
ANISOU 1817  N   VAL A 306     9218   5255   6197   -754   1940    503       N  
ATOM   1818  CA  VAL A 306      14.935  27.282  17.311  1.00 54.94           C  
ANISOU 1818  CA  VAL A 306     9360   5304   6209   -633   1801    548       C  
ATOM   1819  C   VAL A 306      13.826  26.360  16.754  1.00 54.34           C  
ANISOU 1819  C   VAL A 306     9308   5330   6010   -479   1649    587       C  
ATOM   1820  O   VAL A 306      13.647  26.233  15.550  1.00 54.54           O  
ANISOU 1820  O   VAL A 306     9473   5343   5905   -413   1687    649       O  
ATOM   1821  CB  VAL A 306      14.650  28.769  16.940  1.00 57.40           C  
ANISOU 1821  CB  VAL A 306     9901   5444   6465   -617   1909    630       C  
ATOM   1822  CG1 VAL A 306      13.234  29.182  17.354  1.00 54.09           C  
ANISOU 1822  CG1 VAL A 306     9551   5013   5987   -473   1765    677       C  
ATOM   1823  CG2 VAL A 306      15.681  29.689  17.586  1.00 54.49           C  
ANISOU 1823  CG2 VAL A 306     9505   4971   6229   -784   2052    578       C  
ATOM   1824  N   LEU A 307      13.074  25.713  17.632  1.00 53.90           N  
ANISOU 1824  N   LEU A 307     9117   5374   5990   -424   1476    548       N  
ATOM   1825  CA  LEU A 307      11.921  24.952  17.161  1.00 54.53           C  
ANISOU 1825  CA  LEU A 307     9218   5543   5959   -287   1329    580       C  
ATOM   1826  C   LEU A 307      10.915  25.859  16.460  1.00 57.10           C  
ANISOU 1826  C   LEU A 307     9749   5794   6152   -163   1316    679       C  
ATOM   1827  O   LEU A 307      10.598  26.933  16.967  1.00 59.88           O  
ANISOU 1827  O   LEU A 307    10167   6056   6529   -149   1335    708       O  
ATOM   1828  CB  LEU A 307      11.233  24.214  18.296  1.00 50.80           C  
ANISOU 1828  CB  LEU A 307     8571   5177   5554   -258   1160    525       C  
ATOM   1829  CG  LEU A 307      12.057  23.158  19.007  1.00 50.32           C  
ANISOU 1829  CG  LEU A 307     8310   5203   5605   -348   1142    434       C  
ATOM   1830  CD1 LEU A 307      11.442  22.928  20.375  1.00 47.31           C  
ANISOU 1830  CD1 LEU A 307     7792   4880   5304   -333   1011    391       C  
ATOM   1831  CD2 LEU A 307      12.163  21.876  18.202  1.00 45.99           C  
ANISOU 1831  CD2 LEU A 307     7734   4741   4999   -322   1114    420       C  
ATOM   1832  N   PRO A 308      10.415  25.428  15.289  1.00 59.13           N  
ANISOU 1832  N   PRO A 308    10113   6090   6264    -68   1281    729       N  
ATOM   1833  CA  PRO A 308       9.358  26.185  14.636  1.00 62.24           C  
ANISOU 1833  CA  PRO A 308    10689   6438   6521     74   1238    822       C  
ATOM   1834  C   PRO A 308       8.085  26.128  15.481  1.00 60.99           C  
ANISOU 1834  C   PRO A 308    10440   6349   6384    171   1060    814       C  
ATOM   1835  O   PRO A 308       7.585  25.055  15.750  1.00 61.97           O  
ANISOU 1835  O   PRO A 308    10423   6603   6521    191    925    765       O  
ATOM   1836  CB  PRO A 308       9.153  25.447  13.294  1.00 62.09           C  
ANISOU 1836  CB  PRO A 308    10760   6483   6347    145   1212    852       C  
ATOM   1837  CG  PRO A 308      10.352  24.561  13.118  1.00 62.79           C  
ANISOU 1837  CG  PRO A 308    10758   6607   6494     22   1303    785       C  
ATOM   1838  CD  PRO A 308      10.797  24.224  14.519  1.00 61.76           C  
ANISOU 1838  CD  PRO A 308    10407   6512   6546    -80   1276    698       C  
ATOM   1839  N   PRO A 309       7.543  27.290  15.856  1.00 64.05           N  
ANISOU 1839  N   PRO A 309    10918   6646   6771    233   1068    866       N  
ATOM   1840  CA  PRO A 309       6.414  27.389  16.783  1.00 64.11           C  
ANISOU 1840  CA  PRO A 309    10836   6707   6815    319    925    856       C  
ATOM   1841  C   PRO A 309       5.258  26.424  16.525  1.00 64.15           C  
ANISOU 1841  C   PRO A 309    10759   6867   6750    429    742    849       C  
ATOM   1842  O   PRO A 309       4.622  25.943  17.493  1.00 61.08           O  
ANISOU 1842  O   PRO A 309    10207   6566   6437    438    626    799       O  
ATOM   1843  CB  PRO A 309       5.935  28.834  16.593  1.00 62.05           C  
ANISOU 1843  CB  PRO A 309    10769   6312   6496    417    981    944       C  
ATOM   1844  CG  PRO A 309       7.161  29.559  16.183  1.00 64.99           C  
ANISOU 1844  CG  PRO A 309    11275   6536   6881    307   1182    965       C  
ATOM   1845  CD  PRO A 309       7.865  28.602  15.261  1.00 64.72           C  
ANISOU 1845  CD  PRO A 309    11227   6567   6797    248   1219    948       C  
ATOM   1846  N   GLU A 310       4.985  26.137  15.255  1.00 61.79           N  
ANISOU 1846  N   GLU A 310    10570   6602   6305    505    718    896       N  
ATOM   1847  CA  GLU A 310       3.800  25.357  14.928  1.00 67.01           C  
ANISOU 1847  CA  GLU A 310    11168   7405   6887    613    538    890       C  
ATOM   1848  C   GLU A 310       4.009  23.860  15.187  1.00 63.52           C  
ANISOU 1848  C   GLU A 310    10545   7087   6504    524    467    796       C  
ATOM   1849  O   GLU A 310       3.062  23.083  15.198  1.00 63.38           O  
ANISOU 1849  O   GLU A 310    10430   7191   6459    579    318    768       O  
ATOM   1850  CB  GLU A 310       3.315  25.638  13.496  1.00 77.24           C  
ANISOU 1850  CB  GLU A 310    12654   8701   7992    742    517    971       C  
ATOM   1851  CG  GLU A 310       4.198  25.077  12.390  1.00 83.88           C  
ANISOU 1851  CG  GLU A 310    13587   9536   8748    682    603    968       C  
ATOM   1852  CD  GLU A 310       5.359  25.996  12.016  1.00 94.16           C  
ANISOU 1852  CD  GLU A 310    15055  10676  10046    615    816   1019       C  
ATOM   1853  OE1 GLU A 310       5.720  26.900  12.820  1.00 90.58           O  
ANISOU 1853  OE1 GLU A 310    14605  10113   9697    566    907   1029       O  
ATOM   1854  OE2 GLU A 310       5.913  25.804  10.904  1.00 98.68           O  
ANISOU 1854  OE2 GLU A 310    15757  11229  10510    605    898   1045       O  
ATOM   1855  N   LEU A 311       5.257  23.465  15.406  1.00 61.57           N  
ANISOU 1855  N   LEU A 311    10250   6804   6340    386    579    747       N  
ATOM   1856  CA  LEU A 311       5.562  22.109  15.851  1.00 57.52           C  
ANISOU 1856  CA  LEU A 311     9563   6388   5905    301    528    659       C  
ATOM   1857  C   LEU A 311       5.277  21.900  17.328  1.00 54.09           C  
ANISOU 1857  C   LEU A 311     8950   5992   5610    264    461    606       C  
ATOM   1858  O   LEU A 311       4.994  20.776  17.740  1.00 52.41           O  
ANISOU 1858  O   LEU A 311     8597   5876   5438    239    369    546       O  
ATOM   1859  CB  LEU A 311       7.030  21.784  15.598  1.00 59.78           C  
ANISOU 1859  CB  LEU A 311     9853   6627   6234    181    673    626       C  
ATOM   1860  CG  LEU A 311       7.365  20.876  14.424  1.00 62.89           C  
ANISOU 1860  CG  LEU A 311    10302   7065   6529    178    689    613       C  
ATOM   1861  CD1 LEU A 311       6.759  21.362  13.110  1.00 63.90           C  
ANISOU 1861  CD1 LEU A 311    10628   7178   6475    290    677    690       C  
ATOM   1862  CD2 LEU A 311       8.880  20.780  14.326  1.00 66.07           C  
ANISOU 1862  CD2 LEU A 311    10698   7410   6996     62    857    585       C  
ATOM   1863  N   VAL A 312       5.365  22.974  18.124  1.00 51.19           N  
ANISOU 1863  N   VAL A 312     8597   5541   5310    257    514    626       N  
ATOM   1864  CA  VAL A 312       5.266  22.895  19.593  1.00 45.21           C  
ANISOU 1864  CA  VAL A 312     7687   4806   4684    212    474    574       C  
ATOM   1865  C   VAL A 312       3.818  23.141  20.059  1.00 45.79           C  
ANISOU 1865  C   VAL A 312     7725   4932   4740    326    349    595       C  
ATOM   1866  O   VAL A 312       3.412  24.281  20.247  1.00 48.25           O  
ANISOU 1866  O   VAL A 312     8120   5172   5040    393    372    642       O  
ATOM   1867  CB  VAL A 312       6.230  23.925  20.252  1.00 44.75           C  
ANISOU 1867  CB  VAL A 312     7662   4628   4714    129    606    569       C  
ATOM   1868  CG1 VAL A 312       6.228  23.805  21.753  1.00 42.21           C  
ANISOU 1868  CG1 VAL A 312     7190   4333   4515     78    566    508       C  
ATOM   1869  CG2 VAL A 312       7.657  23.769  19.733  1.00 46.38           C  
ANISOU 1869  CG2 VAL A 312     7895   4786   4940     17    740    549       C  
ATOM   1870  N   LEU A 313       3.036  22.089  20.256  1.00 43.69           N  
ANISOU 1870  N   LEU A 313     7334   4788   4476    348    223    558       N  
ATOM   1871  CA  LEU A 313       1.658  22.262  20.692  1.00 42.12           C  
ANISOU 1871  CA  LEU A 313     7080   4654   4269    451    109    572       C  
ATOM   1872  C   LEU A 313       1.603  22.629  22.177  1.00 45.10           C  
ANISOU 1872  C   LEU A 313     7362   5010   4763    420    119    543       C  
ATOM   1873  O   LEU A 313       2.176  21.935  23.033  1.00 45.29           O  
ANISOU 1873  O   LEU A 313     7271   5057   4878    322    130    482       O  
ATOM   1874  CB  LEU A 313       0.857  20.996  20.408  1.00 41.42           C  
ANISOU 1874  CB  LEU A 313     6886   4702   4151    466    -20    536       C  
ATOM   1875  CG  LEU A 313      -0.628  20.873  20.802  1.00 43.92           C  
ANISOU 1875  CG  LEU A 313     7104   5120   4466    556   -151    534       C  
ATOM   1876  CD1 LEU A 313      -1.556  21.845  20.070  1.00 42.86           C  
ANISOU 1876  CD1 LEU A 313     7072   4985   4228    708   -197    606       C  
ATOM   1877  CD2 LEU A 313      -1.091  19.433  20.553  1.00 44.60           C  
ANISOU 1877  CD2 LEU A 313     7077   5325   4542    517   -251    477       C  
ATOM   1878  N   GLU A 314       0.928  23.741  22.466  1.00 46.37           N  
ANISOU 1878  N   GLU A 314     7581   5124   4913    514    119    587       N  
ATOM   1879  CA  GLU A 314       0.684  24.191  23.818  1.00 45.57           C  
ANISOU 1879  CA  GLU A 314     7408   5004   4903    509    124    562       C  
ATOM   1880  C   GLU A 314      -0.810  24.232  24.105  1.00 44.85           C  
ANISOU 1880  C   GLU A 314     7248   4999   4794    633     15    578       C  
ATOM   1881  O   GLU A 314      -1.620  24.301  23.181  1.00 43.16           O  
ANISOU 1881  O   GLU A 314     7077   4831   4489    740    -51    623       O  
ATOM   1882  CB  GLU A 314       1.308  25.556  24.037  1.00 45.78           C  
ANISOU 1882  CB  GLU A 314     7567   4881   4947    501    242    590       C  
ATOM   1883  CG  GLU A 314       2.823  25.525  23.929  1.00 48.06           C  
ANISOU 1883  CG  GLU A 314     7892   5094   5276    361    355    560       C  
ATOM   1884  CD  GLU A 314       3.438  26.892  24.111  1.00 52.94           C  
ANISOU 1884  CD  GLU A 314     8643   5557   5915    336    479    581       C  
ATOM   1885  OE1 GLU A 314       3.478  27.384  25.258  1.00 55.81           O  
ANISOU 1885  OE1 GLU A 314     8969   5882   6354    307    496    544       O  
ATOM   1886  OE2 GLU A 314       3.856  27.494  23.098  1.00 56.86           O  
ANISOU 1886  OE2 GLU A 314     9293   5964   6346    345    563    634       O  
ATOM   1887  N   VAL A 315      -1.144  24.174  25.392  1.00 41.93           N  
ANISOU 1887  N   VAL A 315     6768   4655   4509    617     -1    538       N  
ATOM   1888  CA  VAL A 315      -2.511  24.225  25.890  1.00 44.40           C  
ANISOU 1888  CA  VAL A 315     6994   5050   4828    721    -85    544       C  
ATOM   1889  C   VAL A 315      -2.664  25.430  26.852  1.00 46.37           C  
ANISOU 1889  C   VAL A 315     7289   5210   5119    771    -25    554       C  
ATOM   1890  O   VAL A 315      -1.966  25.511  27.878  1.00 46.03           O  
ANISOU 1890  O   VAL A 315     7221   5116   5151    680     35    509       O  
ATOM   1891  CB  VAL A 315      -2.887  22.929  26.672  1.00 44.06           C  
ANISOU 1891  CB  VAL A 315     6765   5126   4848    655   -154    482       C  
ATOM   1892  CG1 VAL A 315      -4.375  22.931  27.015  1.00 43.26           C  
ANISOU 1892  CG1 VAL A 315     6563   5125   4748    762   -239    489       C  
ATOM   1893  CG2 VAL A 315      -2.538  21.683  25.882  1.00 41.84           C  
ANISOU 1893  CG2 VAL A 315     6446   4911   4540    580   -196    457       C  
ATOM   1894  N   PRO A 316      -3.577  26.369  26.531  1.00 48.62           N  
ANISOU 1894  N   PRO A 316     7646   5476   5353    923    -42    612       N  
ATOM   1895  CA  PRO A 316      -3.864  27.437  27.491  1.00 48.28           C  
ANISOU 1895  CA  PRO A 316     7640   5353   5351    983     12    615       C  
ATOM   1896  C   PRO A 316      -4.769  26.881  28.562  1.00 47.65           C  
ANISOU 1896  C   PRO A 316     7388   5385   5330   1001    -50    572       C  
ATOM   1897  O   PRO A 316      -5.694  26.120  28.269  1.00 47.47           O  
ANISOU 1897  O   PRO A 316     7247   5498   5291   1049   -147    572       O  
ATOM   1898  CB  PRO A 316      -4.618  28.500  26.647  1.00 46.83           C  
ANISOU 1898  CB  PRO A 316     7589   5124   5082   1160      4    698       C  
ATOM   1899  CG  PRO A 316      -4.299  28.153  25.230  1.00 50.43           C  
ANISOU 1899  CG  PRO A 316     8120   5594   5449   1159    -20    738       C  
ATOM   1900  CD  PRO A 316      -4.199  26.648  25.223  1.00 49.14           C  
ANISOU 1900  CD  PRO A 316     7794   5565   5312   1050    -94    679       C  
ATOM   1901  N   LEU A 317      -4.503  27.267  29.796  1.00 49.28           N  
ANISOU 1901  N   LEU A 317     7584   5537   5604    959     10    532       N  
ATOM   1902  CA  LEU A 317      -5.220  26.713  30.931  1.00 47.20           C  
ANISOU 1902  CA  LEU A 317     7167   5370   5398    958    -27    488       C  
ATOM   1903  C   LEU A 317      -6.446  27.542  31.308  1.00 49.21           C  
ANISOU 1903  C   LEU A 317     7415   5636   5646   1120    -35    515       C  
ATOM   1904  O   LEU A 317      -6.333  28.737  31.613  1.00 48.85           O  
ANISOU 1904  O   LEU A 317     7494   5470   5598   1181     37    532       O  
ATOM   1905  CB  LEU A 317      -4.266  26.573  32.104  1.00 48.22           C  
ANISOU 1905  CB  LEU A 317     7281   5447   5592    827     35    425       C  
ATOM   1906  CG  LEU A 317      -3.093  25.603  31.888  1.00 49.55           C  
ANISOU 1906  CG  LEU A 317     7421   5627   5778    673     36    390       C  
ATOM   1907  CD1 LEU A 317      -2.342  25.392  33.184  1.00 48.68           C  
ANISOU 1907  CD1 LEU A 317     7270   5497   5730    566     75    326       C  
ATOM   1908  CD2 LEU A 317      -3.592  24.264  31.356  1.00 45.78           C  
ANISOU 1908  CD2 LEU A 317     6821   5284   5288    658    -52    389       C  
ATOM   1909  N   GLU A 318      -7.614  26.915  31.240  1.00 46.42           N  
ANISOU 1909  N   GLU A 318     6918   5427   5292   1191   -121    518       N  
ATOM   1910  CA  GLU A 318      -8.806  27.503  31.803  1.00 50.66           C  
ANISOU 1910  CA  GLU A 318     7403   6003   5842   1334   -128    530       C  
ATOM   1911  C   GLU A 318      -9.381  26.560  32.848  1.00 48.70           C  
ANISOU 1911  C   GLU A 318     6970   5875   5658   1279   -151    476       C  
ATOM   1912  O   GLU A 318      -8.861  25.461  33.047  1.00 46.35           O  
ANISOU 1912  O   GLU A 318     6600   5623   5388   1138   -167    436       O  
ATOM   1913  CB  GLU A 318      -9.819  27.845  30.712  1.00 56.33           C  
ANISOU 1913  CB  GLU A 318     8121   6787   6497   1501   -203    591       C  
ATOM   1914  CG  GLU A 318     -10.330  26.669  29.900  1.00 62.69           C  
ANISOU 1914  CG  GLU A 318     8790   7750   7280   1475   -318    584       C  
ATOM   1915  CD  GLU A 318     -11.508  27.064  29.017  1.00 74.52           C  
ANISOU 1915  CD  GLU A 318    10261   9336   8718   1659   -406    635       C  
ATOM   1916  OE1 GLU A 318     -11.264  27.710  27.965  1.00 74.17           O  
ANISOU 1916  OE1 GLU A 318    10366   9226   8590   1740   -414    694       O  
ATOM   1917  OE2 GLU A 318     -12.675  26.733  29.381  1.00 74.58           O  
ANISOU 1917  OE2 GLU A 318    10096   9482   8759   1725   -465    616       O  
ATOM   1918  N   HIS A 319     -10.430  27.006  33.535  1.00 48.24           N  
ANISOU 1918  N   HIS A 319     6846   5860   5623   1394   -142    477       N  
ATOM   1919  CA  HIS A 319     -11.055  26.234  34.604  1.00 45.22           C  
ANISOU 1919  CA  HIS A 319     6298   5584   5300   1352   -143    430       C  
ATOM   1920  C   HIS A 319     -12.507  26.041  34.243  1.00 47.05           C  
ANISOU 1920  C   HIS A 319     6381   5963   5533   1474   -216    448       C  
ATOM   1921  O   HIS A 319     -13.127  26.925  33.648  1.00 46.73           O  
ANISOU 1921  O   HIS A 319     6383   5917   5456   1636   -237    494       O  
ATOM   1922  CB  HIS A 319     -10.870  26.934  35.954  1.00 45.09           C  
ANISOU 1922  CB  HIS A 319     6336   5481   5315   1359    -46    401       C  
ATOM   1923  CG  HIS A 319     -11.364  26.130  37.154  1.00 44.92           C  
ANISOU 1923  CG  HIS A 319     6169   5554   5346   1303    -28    354       C  
ATOM   1924  ND1 HIS A 319     -12.684  26.035  37.485  1.00 44.64           N  
ANISOU 1924  ND1 HIS A 319     5994   5633   5335   1400    -40    356       N  
ATOM   1925  CD2 HIS A 319     -10.667  25.362  38.095  1.00 42.87           C  
ANISOU 1925  CD2 HIS A 319     5886   5289   5113   1158      4    306       C  
ATOM   1926  CE1 HIS A 319     -12.816  25.255  38.577  1.00 43.87           C  
ANISOU 1926  CE1 HIS A 319     5799   5591   5277   1313     -6    313       C  
ATOM   1927  NE2 HIS A 319     -11.581  24.841  38.949  1.00 42.06           N  
ANISOU 1927  NE2 HIS A 319     5648   5287   5046   1170     18    286       N  
ATOM   1928  N   PRO A 320     -13.060  24.846  34.524  1.00 47.51           N  
ANISOU 1928  N   PRO A 320     6261   6158   5634   1397   -258    411       N  
ATOM   1929  CA  PRO A 320     -14.425  24.544  34.063  1.00 46.90           C  
ANISOU 1929  CA  PRO A 320     6017   6239   5563   1492   -339    418       C  
ATOM   1930  C   PRO A 320     -15.467  25.502  34.611  1.00 49.40           C  
ANISOU 1930  C   PRO A 320     6291   6581   5897   1666   -305    435       C  
ATOM   1931  O   PRO A 320     -16.386  25.848  33.890  1.00 48.94           O  
ANISOU 1931  O   PRO A 320     6172   6608   5817   1808   -374    464       O  
ATOM   1932  CB  PRO A 320     -14.679  23.110  34.579  1.00 44.83           C  
ANISOU 1932  CB  PRO A 320     5587   6087   5358   1344   -355    365       C  
ATOM   1933  CG  PRO A 320     -13.545  22.828  35.539  1.00 43.89           C  
ANISOU 1933  CG  PRO A 320     5554   5861   5261   1208   -270    338       C  
ATOM   1934  CD  PRO A 320     -12.389  23.649  35.073  1.00 43.76           C  
ANISOU 1934  CD  PRO A 320     5736   5697   5195   1214   -245    365       C  
ATOM   1935  N   THR A 321     -15.326  25.922  35.869  1.00 51.83           N  
ANISOU 1935  N   THR A 321     6632   6820   6239   1661   -203    414       N  
ATOM   1936  CA  THR A 321     -16.294  26.837  36.517  1.00 54.93           C  
ANISOU 1936  CA  THR A 321     6992   7229   6652   1829   -151    423       C  
ATOM   1937  C   THR A 321     -15.763  28.230  36.904  1.00 54.48           C  
ANISOU 1937  C   THR A 321     7139   6994   6565   1921    -62    443       C  
ATOM   1938  O   THR A 321     -16.512  29.204  36.896  1.00 56.24           O  
ANISOU 1938  O   THR A 321     7382   7208   6778   2104    -43    472       O  
ATOM   1939  CB  THR A 321     -16.892  26.215  37.807  1.00 57.67           C  
ANISOU 1939  CB  THR A 321     7188   7660   7064   1774    -91    375       C  
ATOM   1940  OG1 THR A 321     -15.830  25.771  38.672  1.00 54.82           O  
ANISOU 1940  OG1 THR A 321     6907   7212   6712   1611    -26    339       O  
ATOM   1941  CG2 THR A 321     -17.820  25.058  37.458  1.00 57.89           C  
ANISOU 1941  CG2 THR A 321     6988   7875   7132   1727   -168    356       C  
ATOM   1942  N   LEU A 322     -14.488  28.304  37.281  1.00 53.87           N  
ANISOU 1942  N   LEU A 322     7209   6781   6477   1792     -6    423       N  
ATOM   1943  CA  LEU A 322     -13.873  29.550  37.737  1.00 52.74           C  
ANISOU 1943  CA  LEU A 322     7264   6462   6313   1841     85    426       C  
ATOM   1944  C   LEU A 322     -13.395  30.364  36.530  1.00 52.77           C  
ANISOU 1944  C   LEU A 322     7433   6357   6260   1908     63    483       C  
ATOM   1945  O   LEU A 322     -12.306  30.130  35.972  1.00 52.43           O  
ANISOU 1945  O   LEU A 322     7483   6244   6195   1786     52    485       O  
ATOM   1946  CB  LEU A 322     -12.737  29.264  38.718  1.00 49.50           C  
ANISOU 1946  CB  LEU A 322     6923   5967   5919   1669    149    370       C  
ATOM   1947  CG  LEU A 322     -13.101  28.563  40.039  1.00 51.46           C  
ANISOU 1947  CG  LEU A 322     7048   6297   6209   1607    188    318       C  
ATOM   1948  CD1 LEU A 322     -11.830  28.248  40.823  1.00 48.48           C  
ANISOU 1948  CD1 LEU A 322     6753   5837   5830   1439    228    268       C  
ATOM   1949  CD2 LEU A 322     -14.109  29.340  40.910  1.00 51.38           C  
ANISOU 1949  CD2 LEU A 322     7017   6294   6210   1757    259    310       C  
ATOM   1950  N   GLU A 323     -14.231  31.318  36.133  1.00 52.45           N  
ANISOU 1950  N   GLU A 323     7430   6304   6194   2110     62    531       N  
ATOM   1951  CA  GLU A 323     -14.060  32.012  34.861  1.00 53.30           C  
ANISOU 1951  CA  GLU A 323     7677   6338   6236   2209     28    600       C  
ATOM   1952  C   GLU A 323     -12.789  32.851  34.806  1.00 50.57           C  
ANISOU 1952  C   GLU A 323     7573   5776   5863   2141    115    607       C  
ATOM   1953  O   GLU A 323     -12.232  33.047  33.707  1.00 48.45           O  
ANISOU 1953  O   GLU A 323     7422   5444   5543   2134     92    654       O  
ATOM   1954  CB  GLU A 323     -15.288  32.850  34.547  1.00 58.94           C  
ANISOU 1954  CB  GLU A 323     8376   7090   6929   2459      9    653       C  
ATOM   1955  CG  GLU A 323     -16.594  32.114  34.813  1.00 66.49           C  
ANISOU 1955  CG  GLU A 323     9072   8263   7930   2523    -58    633       C  
ATOM   1956  CD  GLU A 323     -17.766  32.735  34.085  1.00 76.41           C  
ANISOU 1956  CD  GLU A 323    10283   9597   9152   2770   -122    692       C  
ATOM   1957  OE1 GLU A 323     -17.786  32.677  32.836  1.00 81.17           O  
ANISOU 1957  OE1 GLU A 323    10914  10234   9692   2821   -216    743       O  
ATOM   1958  OE2 GLU A 323     -18.663  33.283  34.761  1.00 80.45           O  
ANISOU 1958  OE2 GLU A 323    10732  10139   9695   2920    -78    688       O  
ATOM   1959  N   TRP A 324     -12.333  33.309  35.985  1.00 47.96           N  
ANISOU 1959  N   TRP A 324     7313   5340   5567   2083    214    554       N  
ATOM   1960  CA  TRP A 324     -11.143  34.165  36.126  1.00 47.19           C  
ANISOU 1960  CA  TRP A 324     7436   5036   5457   2004    306    542       C  
ATOM   1961  C   TRP A 324      -9.849  33.427  35.878  1.00 45.56           C  
ANISOU 1961  C   TRP A 324     7244   4810   5257   1788    294    512       C  
ATOM   1962  O   TRP A 324      -8.818  34.043  35.594  1.00 47.89           O  
ANISOU 1962  O   TRP A 324     7709   4950   5536   1715    354    513       O  
ATOM   1963  CB  TRP A 324     -11.117  34.897  37.481  1.00 47.84           C  
ANISOU 1963  CB  TRP A 324     7587   5021   5569   2014    408    484       C  
ATOM   1964  CG  TRP A 324     -11.309  34.010  38.689  1.00 47.11           C  
ANISOU 1964  CG  TRP A 324     7331   5047   5523   1923    405    413       C  
ATOM   1965  CD1 TRP A 324     -12.457  33.882  39.490  1.00 48.43           C  
ANISOU 1965  CD1 TRP A 324     7367   5321   5715   2029    413    397       C  
ATOM   1966  CD2 TRP A 324     -10.321  33.086  39.283  1.00 45.73           C  
ANISOU 1966  CD2 TRP A 324     7106   4897   5372   1708    398    349       C  
ATOM   1967  NE1 TRP A 324     -12.251  32.961  40.498  1.00 46.96           N  
ANISOU 1967  NE1 TRP A 324     7067   5215   5559   1892    418    333       N  
ATOM   1968  CE2 TRP A 324     -10.996  32.441  40.426  1.00 45.66           C  
ANISOU 1968  CE2 TRP A 324     6946   5008   5394   1704    403    304       C  
ATOM   1969  CE3 TRP A 324      -8.991  32.736  38.988  1.00 44.43           C  
ANISOU 1969  CE3 TRP A 324     7002   4673   5207   1531    391    328       C  
ATOM   1970  CZ2 TRP A 324     -10.349  31.494  41.222  1.00 44.82           C  
ANISOU 1970  CZ2 TRP A 324     6771   4952   5308   1536    397    247       C  
ATOM   1971  CZ3 TRP A 324      -8.360  31.766  39.780  1.00 43.73           C  
ANISOU 1971  CZ3 TRP A 324     6824   4646   5144   1368    377    266       C  
ATOM   1972  CH2 TRP A 324      -9.023  31.159  40.870  1.00 42.77           C  
ANISOU 1972  CH2 TRP A 324     6573   4633   5044   1374    378    229       C  
ATOM   1973  N   PHE A 325      -9.884  32.101  35.949  1.00 43.19           N  
ANISOU 1973  N   PHE A 325     6767   4662   4981   1683    222    484       N  
ATOM   1974  CA  PHE A 325      -8.660  31.312  35.871  1.00 42.73           C  
ANISOU 1974  CA  PHE A 325     6706   4594   4935   1482    214    448       C  
ATOM   1975  C   PHE A 325      -7.980  31.459  34.505  1.00 44.51           C  
ANISOU 1975  C   PHE A 325     7041   4756   5115   1459    199    499       C  
ATOM   1976  O   PHE A 325      -6.755  31.517  34.426  1.00 45.87           O  
ANISOU 1976  O   PHE A 325     7304   4832   5292   1323    244    477       O  
ATOM   1977  CB  PHE A 325      -8.949  29.843  36.199  1.00 41.46           C  
ANISOU 1977  CB  PHE A 325     6341   4604   4807   1395    143    415       C  
ATOM   1978  CG  PHE A 325      -7.719  29.035  36.485  1.00 42.56           C  
ANISOU 1978  CG  PHE A 325     6471   4733   4969   1200    148    367       C  
ATOM   1979  CD1 PHE A 325      -6.832  28.694  35.470  1.00 41.46           C  
ANISOU 1979  CD1 PHE A 325     6379   4566   4808   1114    125    385       C  
ATOM   1980  CD2 PHE A 325      -7.455  28.584  37.770  1.00 41.10           C  
ANISOU 1980  CD2 PHE A 325     6225   4569   4820   1111    174    305       C  
ATOM   1981  CE1 PHE A 325      -5.693  27.968  35.742  1.00 39.97           C  
ANISOU 1981  CE1 PHE A 325     6174   4370   4643    949    131    340       C  
ATOM   1982  CE2 PHE A 325      -6.326  27.843  38.036  1.00 40.18           C  
ANISOU 1982  CE2 PHE A 325     6097   4449   4720    949    171    263       C  
ATOM   1983  CZ  PHE A 325      -5.440  27.536  37.020  1.00 38.56           C  
ANISOU 1983  CZ  PHE A 325     5932   4216   4502    870    149    280       C  
ATOM   1984  N   ALA A 326      -8.769  31.484  33.428  1.00 44.72           N  
ANISOU 1984  N   ALA A 326     7054   4845   5094   1590    134    566       N  
ATOM   1985  CA  ALA A 326      -8.230  31.750  32.083  1.00 45.12           C  
ANISOU 1985  CA  ALA A 326     7234   4828   5082   1596    126    624       C  
ATOM   1986  C   ALA A 326      -7.450  33.075  32.016  1.00 47.54           C  
ANISOU 1986  C   ALA A 326     7772   4921   5371   1602    240    645       C  
ATOM   1987  O   ALA A 326      -6.405  33.150  31.354  1.00 48.44           O  
ANISOU 1987  O   ALA A 326     7996   4946   5463   1501    279    657       O  
ATOM   1988  CB  ALA A 326      -9.327  31.726  31.032  1.00 42.78           C  
ANISOU 1988  CB  ALA A 326     6898   4633   4725   1766     35    692       C  
ATOM   1989  N   ALA A 327      -7.943  34.093  32.723  1.00 46.75           N  
ANISOU 1989  N   ALA A 327     7745   4736   5282   1713    301    645       N  
ATOM   1990  CA  ALA A 327      -7.271  35.387  32.790  1.00 48.88           C  
ANISOU 1990  CA  ALA A 327     8241   4789   5542   1715    418    655       C  
ATOM   1991  C   ALA A 327      -5.859  35.360  33.382  1.00 48.78           C  
ANISOU 1991  C   ALA A 327     8282   4675   5576   1496    494    581       C  
ATOM   1992  O   ALA A 327      -5.105  36.307  33.207  1.00 51.25           O  
ANISOU 1992  O   ALA A 327     8782   4810   5882   1456    590    587       O  
ATOM   1993  CB  ALA A 327      -8.128  36.384  33.534  1.00 49.12           C  
ANISOU 1993  CB  ALA A 327     8327   4755   5579   1877    468    658       C  
ATOM   1994  N   LEU A 328      -5.496  34.284  34.064  1.00 46.54           N  
ANISOU 1994  N   LEU A 328     7837   4506   5340   1355    451    511       N  
ATOM   1995  CA  LEU A 328      -4.150  34.136  34.607  1.00 45.78           C  
ANISOU 1995  CA  LEU A 328     7764   4344   5287   1153    503    438       C  
ATOM   1996  C   LEU A 328      -3.063  33.967  33.534  1.00 46.44           C  
ANISOU 1996  C   LEU A 328     7916   4375   5354   1039    523    462       C  
ATOM   1997  O   LEU A 328      -1.884  34.170  33.815  1.00 46.00           O  
ANISOU 1997  O   LEU A 328     7916   4230   5332    886    587    409       O  
ATOM   1998  CB  LEU A 328      -4.111  32.957  35.566  1.00 43.60           C  
ANISOU 1998  CB  LEU A 328     7297   4214   5056   1055    443    369       C  
ATOM   1999  CG  LEU A 328      -4.190  33.036  37.099  1.00 45.65           C  
ANISOU 1999  CG  LEU A 328     7513   4478   5353   1024    468    291       C  
ATOM   2000  CD1 LEU A 328      -4.648  34.357  37.718  1.00 45.66           C  
ANISOU 2000  CD1 LEU A 328     7648   4352   5348   1130    547    281       C  
ATOM   2001  CD2 LEU A 328      -4.977  31.860  37.643  1.00 42.14           C  
ANISOU 2001  CD2 LEU A 328     6872   4216   4923   1042    389    278       C  
ATOM   2002  N   GLY A 329      -3.467  33.590  32.317  1.00 49.38           N  
ANISOU 2002  N   GLY A 329     8279   4811   5672   1115    467    536       N  
ATOM   2003  CA  GLY A 329      -2.540  33.392  31.195  1.00 47.73           C  
ANISOU 2003  CA  GLY A 329     8140   4562   5434   1026    489    566       C  
ATOM   2004  C   GLY A 329      -1.544  32.272  31.426  1.00 48.54           C  
ANISOU 2004  C   GLY A 329     8117   4742   5582    841    467    501       C  
ATOM   2005  O   GLY A 329      -0.442  32.292  30.888  1.00 49.39           O  
ANISOU 2005  O   GLY A 329     8290   4784   5693    724    524    496       O  
ATOM   2006  N   LEU A 330      -1.908  31.294  32.249  1.00 47.73           N  
ANISOU 2006  N   LEU A 330     7839   4779   5519    814    393    451       N  
ATOM   2007  CA  LEU A 330      -1.062  30.122  32.413  1.00 46.64           C  
ANISOU 2007  CA  LEU A 330     7579   4725   5417    663    362    399       C  
ATOM   2008  C   LEU A 330      -1.213  29.152  31.201  1.00 46.21           C  
ANISOU 2008  C   LEU A 330     7470   4770   5318    675    294    444       C  
ATOM   2009  O   LEU A 330      -2.273  29.067  30.571  1.00 43.53           O  
ANISOU 2009  O   LEU A 330     7117   4496   4928    804    232    497       O  
ATOM   2010  CB  LEU A 330      -1.356  29.430  33.748  1.00 45.51           C  
ANISOU 2010  CB  LEU A 330     7289   4679   5322    630    317    335       C  
ATOM   2011  CG  LEU A 330      -1.315  30.260  35.049  1.00 46.25           C  
ANISOU 2011  CG  LEU A 330     7426   4697   5450    624    371    281       C  
ATOM   2012  CD1 LEU A 330      -1.831  29.454  36.226  1.00 41.13           C  
ANISOU 2012  CD1 LEU A 330     6632   4166   4829    620    319    235       C  
ATOM   2013  CD2 LEU A 330       0.088  30.752  35.358  1.00 46.21           C  
ANISOU 2013  CD2 LEU A 330     7499   4580   5478    478    445    224       C  
ATOM   2014  N   ARG A 331      -0.144  28.448  30.857  1.00 44.40           N  
ANISOU 2014  N   ARG A 331     7212   4555   5105    544    305    417       N  
ATOM   2015  CA  ARG A 331      -0.211  27.492  29.765  1.00 46.18           C  
ANISOU 2015  CA  ARG A 331     7393   4868   5287    545    247    447       C  
ATOM   2016  C   ARG A 331       0.777  26.350  29.994  1.00 45.00           C  
ANISOU 2016  C   ARG A 331     7140   4777   5183    401    239    390       C  
ATOM   2017  O   ARG A 331       1.684  26.460  30.814  1.00 46.28           O  
ANISOU 2017  O   ARG A 331     7285   4896   5403    299    286    335       O  
ATOM   2018  CB  ARG A 331       0.023  28.192  28.418  1.00 49.51           C  
ANISOU 2018  CB  ARG A 331     7976   5200   5635    590    297    515       C  
ATOM   2019  CG  ARG A 331       1.394  28.835  28.247  1.00 53.43           C  
ANISOU 2019  CG  ARG A 331     8586   5561   6154    474    417    502       C  
ATOM   2020  CD  ARG A 331       1.333  30.042  27.310  1.00 58.68           C  
ANISOU 2020  CD  ARG A 331     9454   6092   6751    553    494    578       C  
ATOM   2021  NE  ARG A 331       1.282  29.654  25.898  1.00 66.31           N  
ANISOU 2021  NE  ARG A 331    10474   7090   7629    595    474    639       N  
ATOM   2022  CZ  ARG A 331       0.198  29.731  25.117  1.00 70.24           C  
ANISOU 2022  CZ  ARG A 331    11014   7635   8038    752    403    708       C  
ATOM   2023  NH1 ARG A 331      -0.956  30.190  25.587  1.00 71.70           N  
ANISOU 2023  NH1 ARG A 331    11183   7843   8217    888    348    729       N  
ATOM   2024  NH2 ARG A 331       0.264  29.339  23.854  1.00 73.84           N  
ANISOU 2024  NH2 ARG A 331    11525   8123   8407    777    385    753       N  
ATOM   2025  N   TRP A 332       0.614  25.248  29.286  1.00 42.35           N  
ANISOU 2025  N   TRP A 332     6734   4539   4819    396    175    398       N  
ATOM   2026  CA  TRP A 332       1.661  24.233  29.327  1.00 39.40           C  
ANISOU 2026  CA  TRP A 332     6287   4200   4482    271    182    352       C  
ATOM   2027  C   TRP A 332       1.722  23.606  27.971  1.00 40.44           C  
ANISOU 2027  C   TRP A 332     6445   4368   4552    280    160    383       C  
ATOM   2028  O   TRP A 332       0.745  23.677  27.205  1.00 39.93           O  
ANISOU 2028  O   TRP A 332     6412   4341   4420    382    106    431       O  
ATOM   2029  CB  TRP A 332       1.449  23.207  30.451  1.00 36.13           C  
ANISOU 2029  CB  TRP A 332     5723   3883   4123    232    122    299       C  
ATOM   2030  CG  TRP A 332       2.777  22.675  30.893  1.00 36.60           C  
ANISOU 2030  CG  TRP A 332     5738   3934   4235    109    158    246       C  
ATOM   2031  CD1 TRP A 332       3.369  21.473  30.531  1.00 34.96           C  
ANISOU 2031  CD1 TRP A 332     5464   3785   4036     47    138    226       C  
ATOM   2032  CD2 TRP A 332       3.778  23.358  31.733  1.00 36.46           C  
ANISOU 2032  CD2 TRP A 332     5740   3845   4269     32    223    201       C  
ATOM   2033  NE1 TRP A 332       4.606  21.355  31.091  1.00 36.54           N  
ANISOU 2033  NE1 TRP A 332     5632   3962   4288    -47    181    177       N  
ATOM   2034  CE2 TRP A 332       4.918  22.458  31.813  1.00 35.98           C  
ANISOU 2034  CE2 TRP A 332     5605   3819   4246    -67    229    157       C  
ATOM   2035  CE3 TRP A 332       3.834  24.595  32.399  1.00 38.38           C  
ANISOU 2035  CE3 TRP A 332     6054   3999   4530     35    273    187       C  
ATOM   2036  CZ2 TRP A 332       6.058  22.778  32.535  1.00 35.60           C  
ANISOU 2036  CZ2 TRP A 332     5539   3735   4252   -158    274    102       C  
ATOM   2037  CZ3 TRP A 332       4.979  24.907  33.128  1.00 37.24           C  
ANISOU 2037  CZ3 TRP A 332     5900   3811   4438    -69    321    126       C  
ATOM   2038  CH2 TRP A 332       6.073  24.026  33.181  1.00 38.64           C  
ANISOU 2038  CH2 TRP A 332     5992   4037   4652   -164    317     84       C  
ATOM   2039  N   TYR A 333       2.871  23.018  27.647  1.00 37.19           N  
ANISOU 2039  N   TYR A 333     6022   3950   4158    178    201    356       N  
ATOM   2040  CA  TYR A 333       3.028  22.276  26.391  1.00 39.68           C  
ANISOU 2040  CA  TYR A 333     6361   4303   4414    176    186    375       C  
ATOM   2041  C   TYR A 333       2.593  20.817  26.471  1.00 38.40           C  
ANISOU 2041  C   TYR A 333     6074   4258   4258    164     96    343       C  
ATOM   2042  O   TYR A 333       2.618  20.187  27.522  1.00 37.54           O  
ANISOU 2042  O   TYR A 333     5856   4193   4214    122     68    299       O  
ATOM   2043  CB  TYR A 333       4.481  22.328  25.928  1.00 40.54           C  
ANISOU 2043  CB  TYR A 333     6518   4346   4538     78    286    359       C  
ATOM   2044  CG  TYR A 333       5.468  21.880  26.969  1.00 40.15           C  
ANISOU 2044  CG  TYR A 333     6364   4307   4583    -27    311    292       C  
ATOM   2045  CD1 TYR A 333       5.843  20.527  27.072  1.00 39.25           C  
ANISOU 2045  CD1 TYR A 333     6143   4274   4495    -74    272    253       C  
ATOM   2046  CD2 TYR A 333       6.031  22.806  27.862  1.00 42.42           C  
ANISOU 2046  CD2 TYR A 333     6663   4524   4931    -77    370    266       C  
ATOM   2047  CE1 TYR A 333       6.764  20.115  28.019  1.00 41.07           C  
ANISOU 2047  CE1 TYR A 333     6280   4520   4806   -154    288    196       C  
ATOM   2048  CE2 TYR A 333       6.949  22.398  28.826  1.00 43.31           C  
ANISOU 2048  CE2 TYR A 333     6674   4658   5123   -168    380    200       C  
ATOM   2049  CZ  TYR A 333       7.311  21.064  28.890  1.00 42.10           C  
ANISOU 2049  CZ  TYR A 333     6414   4591   4989   -199    337    169       C  
ATOM   2050  OH  TYR A 333       8.202  20.682  29.834  1.00 46.84           O  
ANISOU 2050  OH  TYR A 333     6919   5219   5661   -271    340    110       O  
ATOM   2051  N   ALA A 334       2.275  20.260  25.323  1.00 42.17           N  
ANISOU 2051  N   ALA A 334     6582   4779   4664    195     58    363       N  
ATOM   2052  CA  ALA A 334       1.650  18.950  25.262  1.00 41.52           C  
ANISOU 2052  CA  ALA A 334     6399   4800   4576    191    -33    334       C  
ATOM   2053  C   ALA A 334       2.608  17.808  25.479  1.00 41.57           C  
ANISOU 2053  C   ALA A 334     6342   4823   4630     93    -11    283       C  
ATOM   2054  O   ALA A 334       2.186  16.760  25.940  1.00 41.62           O  
ANISOU 2054  O   ALA A 334     6251   4897   4666     73    -70    251       O  
ATOM   2055  CB  ALA A 334       0.960  18.778  23.919  1.00 42.54           C  
ANISOU 2055  CB  ALA A 334     6591   4971   4602    258    -89    365       C  
ATOM   2056  N   LEU A 335       3.883  17.993  25.129  1.00 40.02           N  
ANISOU 2056  N   LEU A 335     6199   4564   4443     36     79    278       N  
ATOM   2057  CA  LEU A 335       4.752  16.845  24.925  1.00 37.51           C  
ANISOU 2057  CA  LEU A 335     5838   4268   4146    -32     98    237       C  
ATOM   2058  C   LEU A 335       5.844  16.779  25.938  1.00 37.22           C  
ANISOU 2058  C   LEU A 335     5733   4208   4200   -103    151    199       C  
ATOM   2059  O   LEU A 335       6.761  17.608  25.915  1.00 40.64           O  
ANISOU 2059  O   LEU A 335     6209   4578   4656   -139    236    201       O  
ATOM   2060  CB  LEU A 335       5.338  16.807  23.501  1.00 38.22           C  
ANISOU 2060  CB  LEU A 335     6031   4330   4163    -35    153    254       C  
ATOM   2061  CG  LEU A 335       5.995  15.485  23.052  1.00 39.51           C  
ANISOU 2061  CG  LEU A 335     6161   4524   4326    -82    163    213       C  
ATOM   2062  CD1 LEU A 335       4.951  14.419  22.779  1.00 35.76           C  
ANISOU 2062  CD1 LEU A 335     5652   4123   3811    -55     60    196       C  
ATOM   2063  CD2 LEU A 335       6.889  15.663  21.828  1.00 38.25           C  
ANISOU 2063  CD2 LEU A 335     6105   4319   4108    -96    255    227       C  
ATOM   2064  N   PRO A 336       5.762  15.793  26.846  1.00 35.17           N  
ANISOU 2064  N   PRO A 336     5369   4002   3994   -125    103    163       N  
ATOM   2065  CA  PRO A 336       6.877  15.682  27.763  1.00 35.76           C  
ANISOU 2065  CA  PRO A 336     5379   4064   4144   -183    145    125       C  
ATOM   2066  C   PRO A 336       7.981  14.812  27.145  1.00 35.33           C  
ANISOU 2066  C   PRO A 336     5313   4013   4098   -224    191    100       C  
ATOM   2067  O   PRO A 336       7.803  13.607  26.976  1.00 37.04           O  
ANISOU 2067  O   PRO A 336     5498   4269   4305   -219    153     85       O  
ATOM   2068  CB  PRO A 336       6.243  15.014  29.001  1.00 35.83           C  
ANISOU 2068  CB  PRO A 336     5298   4125   4192   -174     74    107       C  
ATOM   2069  CG  PRO A 336       5.099  14.207  28.454  1.00 36.13           C  
ANISOU 2069  CG  PRO A 336     5334   4209   4183   -139      8    120       C  
ATOM   2070  CD  PRO A 336       4.641  14.896  27.198  1.00 35.48           C  
ANISOU 2070  CD  PRO A 336     5345   4108   4028    -99     13    155       C  
ATOM   2071  N   ALA A 337       9.119  15.405  26.832  1.00 34.36           N  
ANISOU 2071  N   ALA A 337     5213   3847   3995   -266    278     92       N  
ATOM   2072  CA  ALA A 337      10.136  14.673  26.109  1.00 35.22           C  
ANISOU 2072  CA  ALA A 337     5314   3960   4106   -295    335     71       C  
ATOM   2073  C   ALA A 337      11.501  14.792  26.758  1.00 37.46           C  
ANISOU 2073  C   ALA A 337     5518   4242   4473   -352    393     30       C  
ATOM   2074  O   ALA A 337      12.264  15.726  26.477  1.00 43.55           O  
ANISOU 2074  O   ALA A 337     6316   4968   5262   -397    478     29       O  
ATOM   2075  CB  ALA A 337      10.175  15.141  24.679  1.00 33.30           C  
ANISOU 2075  CB  ALA A 337     5189   3677   3788   -285    397    104       C  
ATOM   2076  N   VAL A 338      11.816  13.833  27.609  1.00 36.14           N  
ANISOU 2076  N   VAL A 338     5252   4124   4355   -351    349     -3       N  
ATOM   2077  CA  VAL A 338      13.047  13.868  28.388  1.00 36.87           C  
ANISOU 2077  CA  VAL A 338     5248   4236   4526   -393    379    -48       C  
ATOM   2078  C   VAL A 338      14.206  13.638  27.429  1.00 37.93           C  
ANISOU 2078  C   VAL A 338     5376   4364   4672   -421    474    -64       C  
ATOM   2079  O   VAL A 338      14.178  12.679  26.631  1.00 36.30           O  
ANISOU 2079  O   VAL A 338     5196   4168   4429   -389    483    -59       O  
ATOM   2080  CB  VAL A 338      13.013  12.765  29.487  1.00 38.28           C  
ANISOU 2080  CB  VAL A 338     5336   4471   4737   -363    301    -70       C  
ATOM   2081  CG1 VAL A 338      14.326  12.653  30.271  1.00 33.15           C  
ANISOU 2081  CG1 VAL A 338     4576   3859   4161   -389    316   -118       C  
ATOM   2082  CG2 VAL A 338      11.832  12.999  30.419  1.00 35.95           C  
ANISOU 2082  CG2 VAL A 338     5050   4182   4427   -337    222    -52       C  
ATOM   2083  N   SER A 339      15.219  14.504  27.491  1.00 36.37           N  
ANISOU 2083  N   SER A 339     5145   4149   4524   -484    550    -89       N  
ATOM   2084  CA  SER A 339      16.292  14.414  26.523  1.00 37.50           C  
ANISOU 2084  CA  SER A 339     5284   4284   4680   -516    659   -102       C  
ATOM   2085  C   SER A 339      17.713  14.386  27.094  1.00 41.80           C  
ANISOU 2085  C   SER A 339     5689   4874   5320   -566    701   -161       C  
ATOM   2086  O   SER A 339      18.676  14.409  26.336  1.00 44.10           O  
ANISOU 2086  O   SER A 339     5960   5163   5633   -601    804   -177       O  
ATOM   2087  CB  SER A 339      16.149  15.551  25.530  1.00 36.90           C  
ANISOU 2087  CB  SER A 339     5330   4132   4556   -550    748    -65       C  
ATOM   2088  OG  SER A 339      16.118  16.784  26.233  1.00 37.96           O  
ANISOU 2088  OG  SER A 339     5469   4228   4727   -601    754    -71       O  
ATOM   2089  N   ASN A 340      17.861  14.348  28.410  1.00 41.65           N  
ANISOU 2089  N   ASN A 340     5571   4901   5355   -569    623   -196       N  
ATOM   2090  CA  ASN A 340      19.206  14.350  28.990  1.00 42.87           C  
ANISOU 2090  CA  ASN A 340     5579   5111   5597   -613    647   -258       C  
ATOM   2091  C   ASN A 340      19.594  13.007  29.602  1.00 46.80           C  
ANISOU 2091  C   ASN A 340     5972   5690   6120   -541    578   -280       C  
ATOM   2092  O   ASN A 340      20.667  12.890  30.227  1.00 48.82           O  
ANISOU 2092  O   ASN A 340     6092   6012   6447   -556    572   -333       O  
ATOM   2093  CB  ASN A 340      19.349  15.469  30.047  1.00 42.92           C  
ANISOU 2093  CB  ASN A 340     5544   5115   5650   -681    619   -295       C  
ATOM   2094  CG  ASN A 340      18.362  15.335  31.229  1.00 41.14           C  
ANISOU 2094  CG  ASN A 340     5330   4905   5396   -631    494   -285       C  
ATOM   2095  OD1 ASN A 340      18.473  16.082  32.205  1.00 41.49           O  
ANISOU 2095  OD1 ASN A 340     5339   4955   5471   -673    458   -322       O  
ATOM   2096  ND2 ASN A 340      17.385  14.423  31.139  1.00 38.71           N  
ANISOU 2096  ND2 ASN A 340     5078   4600   5031   -548    434   -239       N  
ATOM   2097  N   MET A 341      18.728  11.999  29.446  1.00 42.61           N  
ANISOU 2097  N   MET A 341     5505   5153   5531   -462    523   -242       N  
ATOM   2098  CA  MET A 341      19.035  10.684  29.994  1.00 42.47           C  
ANISOU 2098  CA  MET A 341     5413   5192   5531   -387    466   -255       C  
ATOM   2099  C   MET A 341      19.840   9.782  29.045  1.00 46.69           C  
ANISOU 2099  C   MET A 341     5926   5739   6075   -351    541   -265       C  
ATOM   2100  O   MET A 341      19.715   9.862  27.802  1.00 45.58           O  
ANISOU 2100  O   MET A 341     5872   5552   5893   -366    623   -246       O  
ATOM   2101  CB  MET A 341      17.766   9.993  30.483  1.00 44.18           C  
ANISOU 2101  CB  MET A 341     5700   5394   5693   -328    373   -217       C  
ATOM   2102  CG  MET A 341      17.163  10.705  31.696  1.00 40.23           C  
ANISOU 2102  CG  MET A 341     5191   4901   5193   -345    295   -216       C  
ATOM   2103  SD  MET A 341      15.860   9.784  32.524  1.00 43.36           S  
ANISOU 2103  SD  MET A 341     5636   5298   5542   -278    195   -179       S  
ATOM   2104  CE  MET A 341      16.886   8.852  33.676  1.00 41.94           C  
ANISOU 2104  CE  MET A 341     5341   5190   5405   -219    143   -209       C  
ATOM   2105  N   LEU A 342      20.669   8.932  29.641  1.00 40.71           N  
ANISOU 2105  N   LEU A 342     5059   5045   5365   -296    514   -295       N  
ATOM   2106  CA  LEU A 342      21.408   7.936  28.895  1.00 41.37           C  
ANISOU 2106  CA  LEU A 342     5116   5142   5459   -241    578   -306       C  
ATOM   2107  C   LEU A 342      20.634   6.602  28.838  1.00 40.98           C  
ANISOU 2107  C   LEU A 342     5153   5062   5356   -153    529   -274       C  
ATOM   2108  O   LEU A 342      20.183   6.100  29.866  1.00 41.16           O  
ANISOU 2108  O   LEU A 342     5167   5098   5374   -108    435   -262       O  
ATOM   2109  CB  LEU A 342      22.779   7.728  29.539  1.00 43.99           C  
ANISOU 2109  CB  LEU A 342     5276   5563   5876   -216    579   -356       C  
ATOM   2110  CG  LEU A 342      23.755   6.766  28.894  1.00 48.17           C  
ANISOU 2110  CG  LEU A 342     5747   6122   6435   -147    651   -376       C  
ATOM   2111  CD1 LEU A 342      25.145   7.387  28.861  1.00 49.55           C  
ANISOU 2111  CD1 LEU A 342     5758   6370   6698   -196    722   -433       C  
ATOM   2112  CD2 LEU A 342      23.773   5.442  29.630  1.00 48.17           C  
ANISOU 2112  CD2 LEU A 342     5723   6147   6431    -25    571   -368       C  
ATOM   2113  N   LEU A 343      20.481   6.059  27.631  1.00 38.15           N  
ANISOU 2113  N   LEU A 343     4885   4658   4954   -137    598   -264       N  
ATOM   2114  CA  LEU A 343      19.912   4.748  27.406  1.00 38.90           C  
ANISOU 2114  CA  LEU A 343     5062   4715   5003    -65    572   -248       C  
ATOM   2115  C   LEU A 343      21.046   3.746  27.290  1.00 39.98           C  
ANISOU 2115  C   LEU A 343     5128   4880   5182     15    621   -276       C  
ATOM   2116  O   LEU A 343      21.854   3.851  26.373  1.00 42.24           O  
ANISOU 2116  O   LEU A 343     5395   5174   5482      8    724   -299       O  
ATOM   2117  CB  LEU A 343      19.081   4.755  26.119  1.00 36.77           C  
ANISOU 2117  CB  LEU A 343     4937   4381   4652    -94    614   -230       C  
ATOM   2118  CG  LEU A 343      18.601   3.400  25.620  1.00 38.36           C  
ANISOU 2118  CG  LEU A 343     5233   4538   4805    -37    609   -229       C  
ATOM   2119  CD1 LEU A 343      17.638   2.753  26.597  1.00 36.37           C  
ANISOU 2119  CD1 LEU A 343     5006   4271   4544    -13    503   -209       C  
ATOM   2120  CD2 LEU A 343      17.996   3.487  24.212  1.00 39.04           C  
ANISOU 2120  CD2 LEU A 343     5453   4575   4805    -69    657   -225       C  
ATOM   2121  N   GLU A 344      21.134   2.818  28.247  1.00 40.23           N  
ANISOU 2121  N   GLU A 344     5122   4930   5234     96    552   -272       N  
ATOM   2122  CA  GLU A 344      22.172   1.771  28.250  1.00 42.20           C  
ANISOU 2122  CA  GLU A 344     5309   5204   5522    197    588   -293       C  
ATOM   2123  C   GLU A 344      21.562   0.404  27.926  1.00 43.60           C  
ANISOU 2123  C   GLU A 344     5614   5304   5649    267    585   -276       C  
ATOM   2124  O   GLU A 344      20.570  -0.016  28.546  1.00 42.69           O  
ANISOU 2124  O   GLU A 344     5572   5147   5499    271    508   -246       O  
ATOM   2125  CB  GLU A 344      22.887   1.726  29.596  1.00 45.60           C  
ANISOU 2125  CB  GLU A 344     5599   5715   6012    254    513   -303       C  
ATOM   2126  CG  GLU A 344      23.959   0.648  29.727  1.00 52.42           C  
ANISOU 2126  CG  GLU A 344     6387   6613   6916    381    536   -320       C  
ATOM   2127  CD  GLU A 344      23.465  -0.649  30.378  1.00 54.86           C  
ANISOU 2127  CD  GLU A 344     6779   6872   7192    487    473   -284       C  
ATOM   2128  OE1 GLU A 344      22.497  -0.597  31.159  1.00 57.83           O  
ANISOU 2128  OE1 GLU A 344     7219   7222   7532    463    390   -251       O  
ATOM   2129  OE2 GLU A 344      24.052  -1.733  30.119  1.00 59.48           O  
ANISOU 2129  OE2 GLU A 344     7371   7440   7787    597    515   -289       O  
ATOM   2130  N   ILE A 345      22.141  -0.257  26.922  1.00 44.58           N  
ANISOU 2130  N   ILE A 345     5768   5402   5768    312    680   -298       N  
ATOM   2131  CA  ILE A 345      21.683  -1.549  26.428  1.00 43.23           C  
ANISOU 2131  CA  ILE A 345     5729   5147   5550    371    698   -295       C  
ATOM   2132  C   ILE A 345      22.919  -2.414  26.200  1.00 46.71           C  
ANISOU 2132  C   ILE A 345     6113   5602   6032    485    773   -322       C  
ATOM   2133  O   ILE A 345      23.804  -2.056  25.410  1.00 44.38           O  
ANISOU 2133  O   ILE A 345     5759   5343   5761    482    870   -352       O  
ATOM   2134  CB  ILE A 345      20.910  -1.423  25.097  1.00 41.59           C  
ANISOU 2134  CB  ILE A 345     5663   4875   5265    299    750   -303       C  
ATOM   2135  CG1 ILE A 345      19.702  -0.488  25.249  1.00 43.15           C  
ANISOU 2135  CG1 ILE A 345     5907   5068   5422    197    678   -277       C  
ATOM   2136  CG2 ILE A 345      20.445  -2.805  24.640  1.00 42.07           C  
ANISOU 2136  CG2 ILE A 345     5861   4846   5279    351    764   -312       C  
ATOM   2137  CD1 ILE A 345      18.919  -0.218  23.967  1.00 42.20           C  
ANISOU 2137  CD1 ILE A 345     5915   4900   5217    132    712   -282       C  
ATOM   2138  N   GLY A 346      22.986  -3.545  26.901  1.00 48.35           N  
ANISOU 2138  N   GLY A 346     6340   5781   6250    591    734   -308       N  
ATOM   2139  CA  GLY A 346      24.108  -4.492  26.743  1.00 46.53           C  
ANISOU 2139  CA  GLY A 346     6065   5556   6057    726    800   -329       C  
ATOM   2140  C   GLY A 346      25.508  -3.895  26.861  1.00 47.50           C  
ANISOU 2140  C   GLY A 346     5990   5798   6259    762    840   -357       C  
ATOM   2141  O   GLY A 346      26.452  -4.348  26.190  1.00 46.83           O  
ANISOU 2141  O   GLY A 346     5865   5726   6202    838    939   -388       O  
ATOM   2142  N   GLY A 347      25.628  -2.869  27.705  1.00 46.96           N  
ANISOU 2142  N   GLY A 347     5798   5817   6229    703    767   -352       N  
ATOM   2143  CA  GLY A 347      26.889  -2.176  27.932  1.00 48.74           C  
ANISOU 2143  CA  GLY A 347     5818   6165   6535    711    791   -388       C  
ATOM   2144  C   GLY A 347      27.117  -1.022  26.968  1.00 49.11           C  
ANISOU 2144  C   GLY A 347     5830   6234   6593    583    885   -417       C  
ATOM   2145  O   GLY A 347      28.020  -0.217  27.177  1.00 49.04           O  
ANISOU 2145  O   GLY A 347     5654   6324   6655    546    905   -449       O  
ATOM   2146  N   LEU A 348      26.303  -0.934  25.920  1.00 47.15           N  
ANISOU 2146  N   LEU A 348     5744   5897   6275    512    943   -406       N  
ATOM   2147  CA  LEU A 348      26.428   0.157  24.963  1.00 47.16           C  
ANISOU 2147  CA  LEU A 348     5744   5906   6269    396   1037   -422       C  
ATOM   2148  C   LEU A 348      25.678   1.364  25.503  1.00 49.81           C  
ANISOU 2148  C   LEU A 348     6083   6248   6594    276    959   -401       C  
ATOM   2149  O   LEU A 348      24.612   1.221  26.108  1.00 47.15           O  
ANISOU 2149  O   LEU A 348     5832   5871   6214    269    855   -368       O  
ATOM   2150  CB  LEU A 348      25.885  -0.244  23.598  1.00 44.09           C  
ANISOU 2150  CB  LEU A 348     5534   5423   5794    382   1126   -420       C  
ATOM   2151  CG  LEU A 348      26.571  -1.427  22.903  1.00 47.91           C  
ANISOU 2151  CG  LEU A 348     6044   5882   6276    497   1223   -446       C  
ATOM   2152  CD1 LEU A 348      25.830  -1.753  21.609  1.00 46.37           C  
ANISOU 2152  CD1 LEU A 348     6051   5590   5977    467   1289   -447       C  
ATOM   2153  CD2 LEU A 348      28.069  -1.176  22.618  1.00 48.60           C  
ANISOU 2153  CD2 LEU A 348     5959   6059   6448    530   1338   -486       C  
ATOM   2154  N   GLU A 349      26.235   2.551  25.277  1.00 50.30           N  
ANISOU 2154  N   GLU A 349     6055   6358   6697    182   1018   -422       N  
ATOM   2155  CA  GLU A 349      25.707   3.756  25.900  1.00 48.97           C  
ANISOU 2155  CA  GLU A 349     5873   6200   6533     77    950   -409       C  
ATOM   2156  C   GLU A 349      25.203   4.733  24.848  1.00 47.55           C  
ANISOU 2156  C   GLU A 349     5806   5961   6300    -32   1031   -393       C  
ATOM   2157  O   GLU A 349      25.980   5.260  24.056  1.00 51.69           O  
ANISOU 2157  O   GLU A 349     6292   6500   6850    -80   1155   -415       O  
ATOM   2158  CB  GLU A 349      26.774   4.387  26.793  1.00 48.83           C  
ANISOU 2158  CB  GLU A 349     5649   6288   6614     54    929   -450       C  
ATOM   2159  CG  GLU A 349      27.082   3.553  28.032  1.00 50.91           C  
ANISOU 2159  CG  GLU A 349     5815   6615   6913    166    814   -456       C  
ATOM   2160  CD  GLU A 349      28.329   4.022  28.760  1.00 55.09           C  
ANISOU 2160  CD  GLU A 349     6122   7268   7541    161    799   -510       C  
ATOM   2161  OE1 GLU A 349      29.446   3.907  28.221  1.00 61.11           O  
ANISOU 2161  OE1 GLU A 349     6765   8088   8365    181    896   -550       O  
ATOM   2162  OE2 GLU A 349      28.208   4.510  29.885  1.00 60.17           O  
ANISOU 2162  OE2 GLU A 349     6703   7959   8201    135    688   -518       O  
ATOM   2163  N   PHE A 350      23.895   4.930  24.804  1.00 43.31           N  
ANISOU 2163  N   PHE A 350     5412   5358   5685    -64    965   -354       N  
ATOM   2164  CA  PHE A 350      23.314   5.914  23.918  1.00 42.91           C  
ANISOU 2164  CA  PHE A 350     5476   5254   5575   -152   1021   -331       C  
ATOM   2165  C   PHE A 350      23.091   7.204  24.697  1.00 44.33           C  
ANISOU 2165  C   PHE A 350     5609   5448   5787   -239    971   -324       C  
ATOM   2166  O   PHE A 350      22.056   7.390  25.358  1.00 43.41           O  
ANISOU 2166  O   PHE A 350     5546   5310   5639   -245    864   -297       O  
ATOM   2167  CB  PHE A 350      22.034   5.378  23.297  1.00 42.43           C  
ANISOU 2167  CB  PHE A 350     5594   5121   5408   -130    981   -297       C  
ATOM   2168  CG  PHE A 350      22.253   4.137  22.468  1.00 42.52           C  
ANISOU 2168  CG  PHE A 350     5669   5107   5382    -55   1038   -312       C  
ATOM   2169  CD1 PHE A 350      22.262   2.883  23.061  1.00 41.64           C  
ANISOU 2169  CD1 PHE A 350     5536   4998   5289     34    979   -322       C  
ATOM   2170  CD2 PHE A 350      22.485   4.231  21.100  1.00 42.04           C  
ANISOU 2170  CD2 PHE A 350     5697   5013   5262    -70   1158   -317       C  
ATOM   2171  CE1 PHE A 350      22.496   1.737  22.306  1.00 43.80           C  
ANISOU 2171  CE1 PHE A 350     5876   5236   5530    106   1039   -341       C  
ATOM   2172  CE2 PHE A 350      22.700   3.091  20.342  1.00 45.88           C  
ANISOU 2172  CE2 PHE A 350     6250   5473   5710      1   1214   -339       C  
ATOM   2173  CZ  PHE A 350      22.708   1.839  20.943  1.00 45.14           C  
ANISOU 2173  CZ  PHE A 350     6134   5376   5641     88   1155   -354       C  
ATOM   2174  N   SER A 351      24.106   8.070  24.647  1.00 42.95           N  
ANISOU 2174  N   SER A 351     5328   5309   5681   -307   1054   -355       N  
ATOM   2175  CA  SER A 351      24.107   9.358  25.343  1.00 43.61           C  
ANISOU 2175  CA  SER A 351     5362   5402   5807   -401   1028   -363       C  
ATOM   2176  C   SER A 351      23.028  10.373  24.854  1.00 41.37           C  
ANISOU 2176  C   SER A 351     5239   5033   5447   -466   1036   -316       C  
ATOM   2177  O   SER A 351      22.722  11.323  25.553  1.00 40.44           O  
ANISOU 2177  O   SER A 351     5111   4905   5348   -525    989   -315       O  
ATOM   2178  CB  SER A 351      25.487   9.974  25.228  1.00 42.37           C  
ANISOU 2178  CB  SER A 351     5060   5297   5743   -470   1135   -413       C  
ATOM   2179  OG  SER A 351      25.708  10.286  23.867  1.00 48.10           O  
ANISOU 2179  OG  SER A 351     5872   5971   6432   -510   1286   -399       O  
ATOM   2180  N   ALA A 352      22.475  10.178  23.662  1.00 39.99           N  
ANISOU 2180  N   ALA A 352     5214   4798   5184   -449   1093   -279       N  
ATOM   2181  CA  ALA A 352      21.386  11.023  23.187  1.00 42.30           C  
ANISOU 2181  CA  ALA A 352     5662   5018   5393   -484   1084   -229       C  
ATOM   2182  C   ALA A 352      20.246  10.126  22.677  1.00 43.31           C  
ANISOU 2182  C   ALA A 352     5918   5117   5420   -410   1017   -196       C  
ATOM   2183  O   ALA A 352      20.343   9.480  21.639  1.00 44.80           O  
ANISOU 2183  O   ALA A 352     6179   5289   5552   -376   1079   -194       O  
ATOM   2184  CB  ALA A 352      21.886  11.973  22.103  1.00 42.82           C  
ANISOU 2184  CB  ALA A 352     5794   5037   5440   -555   1235   -217       C  
ATOM   2185  N   ALA A 353      19.175  10.038  23.446  1.00 42.55           N  
ANISOU 2185  N   ALA A 353     5845   5018   5304   -388    890   -177       N  
ATOM   2186  CA  ALA A 353      18.091   9.102  23.122  1.00 42.53           C  
ANISOU 2186  CA  ALA A 353     5938   4999   5223   -328    815   -157       C  
ATOM   2187  C   ALA A 353      16.806   9.643  23.713  1.00 39.07           C  
ANISOU 2187  C   ALA A 353     5546   4546   4753   -335    710   -124       C  
ATOM   2188  O   ALA A 353      16.244   9.058  24.615  1.00 41.02           O  
ANISOU 2188  O   ALA A 353     5755   4813   5017   -305    613   -126       O  
ATOM   2189  CB  ALA A 353      18.389   7.706  23.666  1.00 39.69           C  
ANISOU 2189  CB  ALA A 353     5507   4673   4900   -265    771   -185       C  
ATOM   2190  N   PRO A 354      16.354  10.788  23.219  1.00 39.12           N  
ANISOU 2190  N   PRO A 354     5636   4514   4715   -369    737    -91       N  
ATOM   2191  CA  PRO A 354      15.183  11.433  23.842  1.00 39.72           C  
ANISOU 2191  CA  PRO A 354     5744   4577   4770   -368    645    -61       C  
ATOM   2192  C   PRO A 354      13.918  10.607  23.688  1.00 36.52           C  
ANISOU 2192  C   PRO A 354     5396   4180   4298   -319    549    -45       C  
ATOM   2193  O   PRO A 354      13.659  10.058  22.632  1.00 40.70           O  
ANISOU 2193  O   PRO A 354     6008   4699   4756   -297    564    -42       O  
ATOM   2194  CB  PRO A 354      15.056  12.731  23.042  1.00 39.79           C  
ANISOU 2194  CB  PRO A 354     5856   4533   4730   -400    715    -24       C  
ATOM   2195  CG  PRO A 354      15.651  12.382  21.708  1.00 40.53           C  
ANISOU 2195  CG  PRO A 354     6017   4610   4771   -397    816    -25       C  
ATOM   2196  CD  PRO A 354      16.870  11.584  22.091  1.00 37.78           C  
ANISOU 2196  CD  PRO A 354     5543   4303   4508   -405    859    -75       C  
ATOM   2197  N   PHE A 355      13.125  10.529  24.735  1.00 36.56           N  
ANISOU 2197  N   PHE A 355     5360   4205   4327   -306    452    -41       N  
ATOM   2198  CA  PHE A 355      11.861   9.768  24.688  1.00 36.45           C  
ANISOU 2198  CA  PHE A 355     5385   4203   4262   -272    362    -30       C  
ATOM   2199  C   PHE A 355      10.716  10.646  25.167  1.00 36.84           C  
ANISOU 2199  C   PHE A 355     5452   4253   4294   -267    296      1       C  
ATOM   2200  O   PHE A 355      10.955  11.600  25.936  1.00 37.79           O  
ANISOU 2200  O   PHE A 355     5534   4365   4459   -286    306      7       O  
ATOM   2201  CB  PHE A 355      11.969   8.525  25.584  1.00 34.42           C  
ANISOU 2201  CB  PHE A 355     5052   3971   4054   -255    316    -57       C  
ATOM   2202  CG  PHE A 355      12.313   8.837  27.045  1.00 35.79           C  
ANISOU 2202  CG  PHE A 355     5126   4168   4304   -261    287    -63       C  
ATOM   2203  CD1 PHE A 355      13.651   8.898  27.474  1.00 35.13           C  
ANISOU 2203  CD1 PHE A 355     4962   4100   4285   -270    335    -90       C  
ATOM   2204  CD2 PHE A 355      11.309   9.039  27.989  1.00 35.12           C  
ANISOU 2204  CD2 PHE A 355     5026   4096   4222   -255    210    -47       C  
ATOM   2205  CE1 PHE A 355      13.958   9.154  28.810  1.00 36.96           C  
ANISOU 2205  CE1 PHE A 355     5107   4362   4575   -274    296   -102       C  
ATOM   2206  CE2 PHE A 355      11.608   9.290  29.328  1.00 34.55           C  
ANISOU 2206  CE2 PHE A 355     4876   4045   4205   -257    182    -55       C  
ATOM   2207  CZ  PHE A 355      12.930   9.356  29.739  1.00 34.93           C  
ANISOU 2207  CZ  PHE A 355     4852   4112   4309   -266    220    -84       C  
ATOM   2208  N   SER A 356       9.489  10.307  24.759  1.00 34.18           N  
ANISOU 2208  N   SER A 356     5163   3927   3895   -242    228     15       N  
ATOM   2209  CA  SER A 356       8.283  11.057  25.154  1.00 35.74           C  
ANISOU 2209  CA  SER A 356     5370   4136   4075   -223    161     45       C  
ATOM   2210  C   SER A 356       7.068  10.153  25.250  1.00 39.23           C  
ANISOU 2210  C   SER A 356     5797   4615   4492   -208     72     37       C  
ATOM   2211  O   SER A 356       6.939   9.164  24.502  1.00 40.79           O  
ANISOU 2211  O   SER A 356     6026   4819   4651   -211     61     16       O  
ATOM   2212  CB  SER A 356       7.959  12.167  24.135  1.00 37.49           C  
ANISOU 2212  CB  SER A 356     5691   4331   4223   -203    186     82       C  
ATOM   2213  OG  SER A 356       7.606  11.641  22.854  1.00 36.90           O  
ANISOU 2213  OG  SER A 356     5696   4265   4061   -184    176     83       O  
ATOM   2214  N   GLY A 357       6.157  10.514  26.143  1.00 39.76           N  
ANISOU 2214  N   GLY A 357     5820   4705   4582   -196     15     51       N  
ATOM   2215  CA  GLY A 357       4.863   9.847  26.248  1.00 40.95           C  
ANISOU 2215  CA  GLY A 357     5947   4897   4715   -188    -65     46       C  
ATOM   2216  C   GLY A 357       3.802  10.905  26.220  1.00 43.24           C  
ANISOU 2216  C   GLY A 357     6248   5208   4975   -149   -108     79       C  
ATOM   2217  O   GLY A 357       3.793  11.742  25.316  1.00 49.32           O  
ANISOU 2217  O   GLY A 357     7090   5961   5686   -119    -92    104       O  
ATOM   2218  N   TRP A 358       2.890  10.844  27.185  1.00 39.99           N  
ANISOU 2218  N   TRP A 358     5767   4830   4597   -142   -156     81       N  
ATOM   2219  CA  TRP A 358       1.972  11.944  27.488  1.00 38.23           C  
ANISOU 2219  CA  TRP A 358     5536   4625   4365    -95   -186    111       C  
ATOM   2220  C   TRP A 358       2.024  12.201  28.978  1.00 38.80           C  
ANISOU 2220  C   TRP A 358     5546   4693   4505   -101   -172    111       C  
ATOM   2221  O   TRP A 358       2.523  11.365  29.755  1.00 40.40           O  
ANISOU 2221  O   TRP A 358     5704   4893   4752   -138   -160     88       O  
ATOM   2222  CB  TRP A 358       0.550  11.682  26.999  1.00 35.11           C  
ANISOU 2222  CB  TRP A 358     5117   4293   3930    -68   -266    112       C  
ATOM   2223  CG  TRP A 358       0.013  10.359  27.437  1.00 37.49           C  
ANISOU 2223  CG  TRP A 358     5346   4633   4264   -116   -302     76       C  
ATOM   2224  CD1 TRP A 358      -0.519  10.033  28.687  1.00 35.81           C  
ANISOU 2224  CD1 TRP A 358     5051   4442   4111   -133   -310     71       C  
ATOM   2225  CD2 TRP A 358      -0.030   9.093  26.649  1.00 36.53           C  
ANISOU 2225  CD2 TRP A 358     5239   4524   4117   -162   -326     38       C  
ATOM   2226  NE1 TRP A 358      -0.877   8.695  28.726  1.00 37.56           N  
ANISOU 2226  NE1 TRP A 358     5237   4683   4349   -188   -331     38       N  
ATOM   2227  CE2 TRP A 358      -0.605   8.075  27.541  1.00 36.83           C  
ANISOU 2227  CE2 TRP A 358     5200   4583   4210   -210   -343     13       C  
ATOM   2228  CE3 TRP A 358       0.320   8.730  25.348  1.00 39.43           C  
ANISOU 2228  CE3 TRP A 358     5680   4882   4418   -168   -329     21       C  
ATOM   2229  CZ2 TRP A 358      -0.810   6.755  27.127  1.00 36.74           C  
ANISOU 2229  CZ2 TRP A 358     5189   4574   4194   -267   -362    -29       C  
ATOM   2230  CZ3 TRP A 358       0.105   7.386  24.932  1.00 38.47           C  
ANISOU 2230  CZ3 TRP A 358     5558   4770   4289   -222   -355    -28       C  
ATOM   2231  CH2 TRP A 358      -0.443   6.424  25.804  1.00 35.86           C  
ANISOU 2231  CH2 TRP A 358     5154   4451   4018   -273   -370    -53       C  
ATOM   2232  N   TYR A 359       1.555  13.380  29.385  1.00 38.81           N  
ANISOU 2232  N   TYR A 359     5552   4687   4505    -57   -172    136       N  
ATOM   2233  CA  TYR A 359       1.600  13.833  30.779  1.00 38.12           C  
ANISOU 2233  CA  TYR A 359     5423   4591   4469    -56   -154    133       C  
ATOM   2234  C   TYR A 359       0.610  13.096  31.681  1.00 37.25           C  
ANISOU 2234  C   TYR A 359     5232   4536   4386    -58   -194    124       C  
ATOM   2235  O   TYR A 359      -0.493  12.723  31.259  1.00 36.97           O  
ANISOU 2235  O   TYR A 359     5164   4550   4331    -42   -242    127       O  
ATOM   2236  CB  TYR A 359       1.299  15.348  30.837  1.00 37.67           C  
ANISOU 2236  CB  TYR A 359     5414   4502   4398     -2   -136    160       C  
ATOM   2237  CG  TYR A 359       2.524  16.209  30.823  1.00 38.37           C  
ANISOU 2237  CG  TYR A 359     5565   4518   4498    -26    -69    158       C  
ATOM   2238  CD1 TYR A 359       3.435  16.169  31.880  1.00 38.14           C  
ANISOU 2238  CD1 TYR A 359     5501   4470   4519    -73    -39    126       C  
ATOM   2239  CD2 TYR A 359       2.783  17.085  29.751  1.00 40.61           C  
ANISOU 2239  CD2 TYR A 359     5942   4750   4737     -5    -33    185       C  
ATOM   2240  CE1 TYR A 359       4.571  16.976  31.881  1.00 41.56           C  
ANISOU 2240  CE1 TYR A 359     5977   4844   4971   -109     22    113       C  
ATOM   2241  CE2 TYR A 359       3.915  17.898  29.737  1.00 38.25           C  
ANISOU 2241  CE2 TYR A 359     5699   4378   4456    -42     42    180       C  
ATOM   2242  CZ  TYR A 359       4.810  17.847  30.801  1.00 40.88           C  
ANISOU 2242  CZ  TYR A 359     5982   4701   4851   -100     68    139       C  
ATOM   2243  OH  TYR A 359       5.950  18.649  30.806  1.00 41.23           O  
ANISOU 2243  OH  TYR A 359     6065   4679   4920   -152    141    123       O  
ATOM   2244  N   MET A 360       1.021  12.877  32.921  1.00 37.45           N  
ANISOU 2244  N   MET A 360     5222   4553   4452    -80   -173    110       N  
ATOM   2245  CA  MET A 360       0.061  12.686  33.980  1.00 36.29           C  
ANISOU 2245  CA  MET A 360     5017   4446   4327    -67   -189    112       C  
ATOM   2246  C   MET A 360      -0.122  14.040  34.653  1.00 35.87           C  
ANISOU 2246  C   MET A 360     4980   4373   4275    -21   -168    123       C  
ATOM   2247  O   MET A 360       0.858  14.754  34.930  1.00 38.06           O  
ANISOU 2247  O   MET A 360     5300   4601   4559    -29   -134    114       O  
ATOM   2248  CB  MET A 360       0.481  11.635  34.995  1.00 37.52           C  
ANISOU 2248  CB  MET A 360     5139   4604   4512   -107   -178     97       C  
ATOM   2249  CG  MET A 360      -0.310  11.784  36.283  1.00 43.65           C  
ANISOU 2249  CG  MET A 360     5874   5407   5304    -89   -172    102       C  
ATOM   2250  SD  MET A 360       0.235  10.695  37.562  1.00 61.88           S  
ANISOU 2250  SD  MET A 360     8169   7712   7631   -121   -153     94       S  
ATOM   2251  CE  MET A 360       1.765  11.480  38.051  1.00 52.94           C  
ANISOU 2251  CE  MET A 360     7076   6541   6499   -115   -137     76       C  
ATOM   2252  N   SER A 361      -1.376  14.364  34.945  1.00 32.73           N  
ANISOU 2252  N   SER A 361     4545   4016   3876     25   -186    136       N  
ATOM   2253  CA  SER A 361      -1.766  15.715  35.233  1.00 35.49           C  
ANISOU 2253  CA  SER A 361     4923   4343   4217     89   -169    150       C  
ATOM   2254  C   SER A 361      -1.098  16.345  36.453  1.00 35.26           C  
ANISOU 2254  C   SER A 361     4920   4270   4205     82   -126    132       C  
ATOM   2255  O   SER A 361      -0.931  17.575  36.511  1.00 33.90           O  
ANISOU 2255  O   SER A 361     4808   4048   4025    117    -99    135       O  
ATOM   2256  CB  SER A 361      -3.280  15.783  35.354  1.00 36.15           C  
ANISOU 2256  CB  SER A 361     4942   4492   4301    144   -195    164       C  
ATOM   2257  OG  SER A 361      -3.675  14.896  36.363  1.00 40.68           O  
ANISOU 2257  OG  SER A 361     5447   5107   4904    109   -188    150       O  
ATOM   2258  N   THR A 362      -0.713  15.530  37.428  1.00 34.37           N  
ANISOU 2258  N   THR A 362     4774   4174   4111     39   -121    112       N  
ATOM   2259  CA  THR A 362      -0.019  16.116  38.574  1.00 36.76           C  
ANISOU 2259  CA  THR A 362     5104   4443   4419     32    -92     88       C  
ATOM   2260  C   THR A 362       1.391  16.653  38.224  1.00 37.83           C  
ANISOU 2260  C   THR A 362     5292   4521   4559     -7    -74     67       C  
ATOM   2261  O   THR A 362       1.930  17.475  38.955  1.00 38.12           O  
ANISOU 2261  O   THR A 362     5362   4523   4599    -13    -52     40       O  
ATOM   2262  CB  THR A 362       0.041  15.161  39.787  1.00 35.75           C  
ANISOU 2262  CB  THR A 362     4936   4350   4297      8    -93     76       C  
ATOM   2263  OG1 THR A 362       0.837  14.014  39.449  1.00 34.04           O  
ANISOU 2263  OG1 THR A 362     4706   4139   4089    -40   -109     72       O  
ATOM   2264  CG2 THR A 362      -1.386  14.740  40.244  1.00 32.70           C  
ANISOU 2264  CG2 THR A 362     4497   4016   3912     37    -91     95       C  
ATOM   2265  N   GLU A 363       1.991  16.213  37.115  1.00 38.54           N  
ANISOU 2265  N   GLU A 363     5391   4602   4650    -37    -80     73       N  
ATOM   2266  CA  GLU A 363       3.351  16.687  36.801  1.00 37.96           C  
ANISOU 2266  CA  GLU A 363     5354   4480   4588    -81    -51     50       C  
ATOM   2267  C   GLU A 363       3.271  18.189  36.525  1.00 38.48           C  
ANISOU 2267  C   GLU A 363     5493   4482   4646    -59    -15     55       C  
ATOM   2268  O   GLU A 363       4.169  18.973  36.902  1.00 36.66           O  
ANISOU 2268  O   GLU A 363     5295   4204   4432    -96     19     23       O  
ATOM   2269  CB  GLU A 363       3.915  15.976  35.563  1.00 38.43           C  
ANISOU 2269  CB  GLU A 363     5416   4541   4646   -110    -50     58       C  
ATOM   2270  CG  GLU A 363       4.122  14.505  35.738  1.00 37.73           C  
ANISOU 2270  CG  GLU A 363     5274   4496   4567   -131    -76     51       C  
ATOM   2271  CD  GLU A 363       4.591  13.833  34.468  1.00 41.23           C  
ANISOU 2271  CD  GLU A 363     5729   4935   5002   -151    -70     56       C  
ATOM   2272  OE1 GLU A 363       5.838  13.807  34.247  1.00 39.59           O  
ANISOU 2272  OE1 GLU A 363     5524   4708   4813   -185    -40     35       O  
ATOM   2273  OE2 GLU A 363       3.706  13.335  33.708  1.00 35.35           O  
ANISOU 2273  OE2 GLU A 363     4989   4210   4231   -135    -95     76       O  
ATOM   2274  N   ILE A 364       2.164  18.589  35.900  1.00 35.79           N  
ANISOU 2274  N   ILE A 364     5178   4142   4279      3    -22     93       N  
ATOM   2275  CA  ILE A 364       2.005  19.974  35.497  1.00 38.46           C  
ANISOU 2275  CA  ILE A 364     5602   4410   4602     41     15    110       C  
ATOM   2276  C   ILE A 364       1.353  20.727  36.605  1.00 36.28           C  
ANISOU 2276  C   ILE A 364     5334   4122   4329     86     25     99       C  
ATOM   2277  O   ILE A 364       1.936  21.685  37.133  1.00 36.99           O  
ANISOU 2277  O   ILE A 364     5481   4145   4429     66     66     70       O  
ATOM   2278  CB  ILE A 364       1.141  20.109  34.231  1.00 38.62           C  
ANISOU 2278  CB  ILE A 364     5655   4439   4582    106     -3    160       C  
ATOM   2279  CG1 ILE A 364       1.750  19.270  33.102  1.00 34.61           C  
ANISOU 2279  CG1 ILE A 364     5145   3945   4059     62    -12    166       C  
ATOM   2280  CG2 ILE A 364       0.923  21.587  33.901  1.00 35.64           C  
ANISOU 2280  CG2 ILE A 364     5381   3979   4182    164     39    186       C  
ATOM   2281  CD1 ILE A 364       0.922  19.260  31.826  1.00 38.09           C  
ANISOU 2281  CD1 ILE A 364     5617   4408   4447    124    -44    210       C  
ATOM   2282  N   GLY A 365       0.155  20.257  36.967  1.00 37.68           N  
ANISOU 2282  N   GLY A 365     5451   4365   4499    142     -9    116       N  
ATOM   2283  CA  GLY A 365      -0.727  20.961  37.890  1.00 37.08           C  
ANISOU 2283  CA  GLY A 365     5380   4287   4420    207      5    113       C  
ATOM   2284  C   GLY A 365      -0.255  21.013  39.328  1.00 40.25           C  
ANISOU 2284  C   GLY A 365     5776   4683   4834    171     24     67       C  
ATOM   2285  O   GLY A 365      -0.572  21.951  40.045  1.00 47.57           O  
ANISOU 2285  O   GLY A 365     6748   5572   5755    212     55     52       O  
ATOM   2286  N   THR A 366       0.516  20.029  39.768  1.00 37.45           N  
ANISOU 2286  N   THR A 366     5375   4364   4492    102      4     42       N  
ATOM   2287  CA  THR A 366       1.076  20.088  41.119  1.00 35.58           C  
ANISOU 2287  CA  THR A 366     5139   4125   4253     71     11     -5       C  
ATOM   2288  C   THR A 366       2.563  20.409  41.131  1.00 37.18           C  
ANISOU 2288  C   THR A 366     5373   4284   4471     -4     18    -49       C  
ATOM   2289  O   THR A 366       2.963  21.321  41.824  1.00 42.29           O  
ANISOU 2289  O   THR A 366     6069   4885   5115    -19     40    -91       O  
ATOM   2290  CB  THR A 366       0.891  18.766  41.849  1.00 34.96           C  
ANISOU 2290  CB  THR A 366     4990   4123   4172     58    -17     -2       C  
ATOM   2291  OG1 THR A 366      -0.492  18.421  41.785  1.00 35.02           O  
ANISOU 2291  OG1 THR A 366     4955   4176   4175    113    -18     34       O  
ATOM   2292  CG2 THR A 366       1.388  18.858  43.297  1.00 34.59           C  
ANISOU 2292  CG2 THR A 366     4956   4082   4107     43    -15    -46       C  
ATOM   2293  N   ARG A 367       3.393  19.673  40.396  1.00 35.61           N  
ANISOU 2293  N   ARG A 367     5142   4100   4289    -55      2    -45       N  
ATOM   2294  CA  ARG A 367       4.831  19.903  40.536  1.00 35.60           C  
ANISOU 2294  CA  ARG A 367     5144   4074   4309   -129      9    -95       C  
ATOM   2295  C   ARG A 367       5.246  21.192  39.809  1.00 38.02           C  
ANISOU 2295  C   ARG A 367     5527   4291   4628   -154     61   -104       C  
ATOM   2296  O   ARG A 367       5.685  22.135  40.470  1.00 36.71           O  
ANISOU 2296  O   ARG A 367     5404   4077   4468   -185     85   -152       O  
ATOM   2297  CB  ARG A 367       5.688  18.687  40.109  1.00 32.06           C  
ANISOU 2297  CB  ARG A 367     4631   3674   3878   -169    -17    -94       C  
ATOM   2298  CG  ARG A 367       5.407  17.374  40.865  1.00 32.41           C  
ANISOU 2298  CG  ARG A 367     4616   3790   3909   -147    -60    -84       C  
ATOM   2299  CD  ARG A 367       5.642  17.479  42.375  1.00 31.87           C  
ANISOU 2299  CD  ARG A 367     4542   3745   3822   -145    -81   -124       C  
ATOM   2300  NE  ARG A 367       6.964  18.053  42.628  1.00 33.31           N  
ANISOU 2300  NE  ARG A 367     4720   3913   4022   -202    -84   -184       N  
ATOM   2301  CZ  ARG A 367       8.086  17.354  42.502  1.00 35.65           C  
ANISOU 2301  CZ  ARG A 367     4961   4245   4340   -235   -108   -203       C  
ATOM   2302  NH1 ARG A 367       7.994  16.054  42.187  1.00 35.14           N  
ANISOU 2302  NH1 ARG A 367     4858   4220   4274   -210   -127   -165       N  
ATOM   2303  NH2 ARG A 367       9.284  17.930  42.691  1.00 34.63           N  
ANISOU 2303  NH2 ARG A 367     4811   4112   4235   -294   -110   -265       N  
ATOM   2304  N   ASN A 368       5.090  21.223  38.472  1.00 36.65           N  
ANISOU 2304  N   ASN A 368     5381   4092   4453   -143     82    -59       N  
ATOM   2305  CA  ASN A 368       5.568  22.336  37.648  1.00 37.20           C  
ANISOU 2305  CA  ASN A 368     5535   4069   4529   -170    143    -57       C  
ATOM   2306  C   ASN A 368       4.922  23.660  38.018  1.00 38.21           C  
ANISOU 2306  C   ASN A 368     5754   4119   4643   -126    179    -57       C  
ATOM   2307  O   ASN A 368       5.612  24.668  38.120  1.00 37.50           O  
ANISOU 2307  O   ASN A 368     5731   3947   4571   -179    231    -93       O  
ATOM   2308  CB  ASN A 368       5.388  22.073  36.140  1.00 37.75           C  
ANISOU 2308  CB  ASN A 368     5631   4131   4582   -149    156      0       C  
ATOM   2309  CG  ASN A 368       6.053  20.778  35.681  1.00 39.93           C  
ANISOU 2309  CG  ASN A 368     5830   4472   4870   -190    131     -3       C  
ATOM   2310  OD1 ASN A 368       6.873  20.196  36.392  1.00 39.13           O  
ANISOU 2310  OD1 ASN A 368     5660   4410   4797   -240    112    -47       O  
ATOM   2311  ND2 ASN A 368       5.681  20.311  34.505  1.00 38.18           N  
ANISOU 2311  ND2 ASN A 368     5623   4262   4620   -161    126     42       N  
ATOM   2312  N   LEU A 369       3.607  23.668  38.221  1.00 37.86           N  
ANISOU 2312  N   LEU A 369     5714   4100   4572    -31    158    -20       N  
ATOM   2313  CA  LEU A 369       2.939  24.926  38.606  1.00 37.05           C  
ANISOU 2313  CA  LEU A 369     5699   3921   4455     29    197    -19       C  
ATOM   2314  C   LEU A 369       3.019  25.296  40.123  1.00 39.79           C  
ANISOU 2314  C   LEU A 369     6049   4265   4806     14    199    -83       C  
ATOM   2315  O   LEU A 369       3.094  26.486  40.449  1.00 41.25           O  
ANISOU 2315  O   LEU A 369     6327   4355   4989     15    249   -111       O  
ATOM   2316  CB  LEU A 369       1.500  24.959  38.073  1.00 37.03           C  
ANISOU 2316  CB  LEU A 369     5704   3945   4423    150    181     47       C  
ATOM   2317  CG  LEU A 369       1.313  24.979  36.543  1.00 37.76           C  
ANISOU 2317  CG  LEU A 369     5833   4020   4492    185    182    109       C  
ATOM   2318  CD1 LEU A 369      -0.164  25.037  36.236  1.00 39.40           C  
ANISOU 2318  CD1 LEU A 369     6029   4272   4670    312    151    162       C  
ATOM   2319  CD2 LEU A 369       1.985  26.180  35.896  1.00 39.39           C  
ANISOU 2319  CD2 LEU A 369     6173   4100   4695    163    255    116       C  
ATOM   2320  N   CYS A 370       3.049  24.301  41.033  1.00 37.34           N  
ANISOU 2320  N   CYS A 370     5648   4047   4494     -2    150   -108       N  
ATOM   2321  CA  CYS A 370       2.967  24.584  42.471  1.00 37.98           C  
ANISOU 2321  CA  CYS A 370     5738   4135   4560      1    148   -162       C  
ATOM   2322  C   CYS A 370       4.205  24.405  43.336  1.00 38.18           C  
ANISOU 2322  C   CYS A 370     5738   4178   4593    -92    125   -237       C  
ATOM   2323  O   CYS A 370       4.232  24.950  44.439  1.00 40.15           O  
ANISOU 2323  O   CYS A 370     6025   4410   4821    -95    130   -292       O  
ATOM   2324  CB  CYS A 370       1.798  23.853  43.138  1.00 38.23           C  
ANISOU 2324  CB  CYS A 370     5712   4249   4566     78    123   -133       C  
ATOM   2325  SG  CYS A 370       0.233  24.241  42.351  1.00 43.04           S  
ANISOU 2325  SG  CYS A 370     6335   4851   5167    199    144    -61       S  
ATOM   2326  N   ASP A 371       5.215  23.662  42.883  1.00 37.15           N  
ANISOU 2326  N   ASP A 371     5544   4085   4488   -161     97   -244       N  
ATOM   2327  CA  ASP A 371       6.477  23.602  43.647  1.00 39.99           C  
ANISOU 2327  CA  ASP A 371     5870   4466   4858   -247     70   -322       C  
ATOM   2328  C   ASP A 371       6.956  25.002  44.031  1.00 40.24           C  
ANISOU 2328  C   ASP A 371     5985   4405   4898   -301    112   -391       C  
ATOM   2329  O   ASP A 371       6.882  25.932  43.247  1.00 42.67           O  
ANISOU 2329  O   ASP A 371     6371   4617   5225   -311    174   -377       O  
ATOM   2330  CB  ASP A 371       7.577  22.828  42.917  1.00 39.97           C  
ANISOU 2330  CB  ASP A 371     5791   4503   4893   -311     51   -322       C  
ATOM   2331  CG  ASP A 371       7.450  21.321  43.093  1.00 41.70           C  
ANISOU 2331  CG  ASP A 371     5924   4822   5098   -275     -6   -288       C  
ATOM   2332  OD1 ASP A 371       6.440  20.865  43.655  1.00 40.80           O  
ANISOU 2332  OD1 ASP A 371     5809   4743   4949   -207    -23   -256       O  
ATOM   2333  OD2 ASP A 371       8.379  20.581  42.678  1.00 46.73           O  
ANISOU 2333  OD2 ASP A 371     6495   5499   5762   -315    -26   -294       O  
ATOM   2334  N   PRO A 372       7.416  25.166  45.260  1.00 43.78           N  
ANISOU 2334  N   PRO A 372     6429   4879   5326   -335     80   -468       N  
ATOM   2335  CA  PRO A 372       7.853  26.522  45.617  1.00 48.23           C  
ANISOU 2335  CA  PRO A 372     7080   5346   5898   -397    122   -545       C  
ATOM   2336  C   PRO A 372       9.052  27.018  44.776  1.00 50.05           C  
ANISOU 2336  C   PRO A 372     7305   5520   6190   -513    158   -580       C  
ATOM   2337  O   PRO A 372       9.191  28.220  44.584  1.00 52.39           O  
ANISOU 2337  O   PRO A 372     7698   5702   6505   -560    225   -614       O  
ATOM   2338  CB  PRO A 372       8.217  26.406  47.095  1.00 44.89           C  
ANISOU 2338  CB  PRO A 372     6637   4984   5434   -417     63   -627       C  
ATOM   2339  CG  PRO A 372       8.393  24.936  47.349  1.00 45.80           C  
ANISOU 2339  CG  PRO A 372     6641   5228   5532   -387    -11   -595       C  
ATOM   2340  CD  PRO A 372       7.562  24.191  46.359  1.00 42.96           C  
ANISOU 2340  CD  PRO A 372     6256   4883   5185   -318      8   -490       C  
ATOM   2341  N   HIS A 373       9.864  26.085  44.266  1.00 47.90           N  
ANISOU 2341  N   HIS A 373     6925   5324   5949   -554    125   -569       N  
ATOM   2342  CA  HIS A 373      11.064  26.377  43.488  1.00 43.81           C  
ANISOU 2342  CA  HIS A 373     6377   4776   5494   -665    162   -603       C  
ATOM   2343  C   HIS A 373      10.806  26.247  42.013  1.00 44.68           C  
ANISOU 2343  C   HIS A 373     6511   4842   5623   -641    221   -516       C  
ATOM   2344  O   HIS A 373      11.747  26.170  41.215  1.00 44.95           O  
ANISOU 2344  O   HIS A 373     6504   4872   5704   -718    255   -524       O  
ATOM   2345  CB  HIS A 373      12.222  25.476  43.918  1.00 44.21           C  
ANISOU 2345  CB  HIS A 373     6288   4945   5566   -720     90   -657       C  
ATOM   2346  CG  HIS A 373      11.906  23.983  43.851  1.00 46.59           C  
ANISOU 2346  CG  HIS A 373     6505   5355   5844   -634     28   -590       C  
ATOM   2347  ND1 HIS A 373      11.010  23.384  44.676  1.00 43.70           N  
ANISOU 2347  ND1 HIS A 373     6146   5040   5418   -542    -23   -560       N  
ATOM   2348  CD2 HIS A 373      12.402  22.972  43.013  1.00 44.06           C  
ANISOU 2348  CD2 HIS A 373     6099   5090   5552   -632     21   -549       C  
ATOM   2349  CE1 HIS A 373      10.931  22.074  44.379  1.00 43.41           C  
ANISOU 2349  CE1 HIS A 373     6037   5081   5377   -490    -60   -503       C  
ATOM   2350  NE2 HIS A 373      11.777  21.821  43.357  1.00 44.24           N  
ANISOU 2350  NE2 HIS A 373     6087   5187   5534   -541    -35   -497       N  
ATOM   2351  N   ARG A 374       9.532  26.200  41.628  1.00 39.91           N  
ANISOU 2351  N   ARG A 374     5970   4214   4981   -533    234   -434       N  
ATOM   2352  CA  ARG A 374       9.177  26.262  40.227  1.00 39.65           C  
ANISOU 2352  CA  ARG A 374     5984   4130   4951   -502    287   -353       C  
ATOM   2353  C   ARG A 374       8.278  27.502  40.066  1.00 42.07           C  
ANISOU 2353  C   ARG A 374     6434   4316   5234   -447    349   -325       C  
ATOM   2354  O   ARG A 374       8.644  28.558  40.552  1.00 40.87           O  
ANISOU 2354  O   ARG A 374     6355   4078   5097   -505    393   -386       O  
ATOM   2355  CB  ARG A 374       8.506  24.979  39.742  1.00 36.85           C  
ANISOU 2355  CB  ARG A 374     5563   3866   4572   -419    237   -279       C  
ATOM   2356  CG  ARG A 374       9.353  23.713  39.844  1.00 38.80           C  
ANISOU 2356  CG  ARG A 374     5683   4219   4839   -457    183   -299       C  
ATOM   2357  CD  ARG A 374      10.433  23.557  38.761  1.00 36.67           C  
ANISOU 2357  CD  ARG A 374     5384   3939   4610   -530    227   -299       C  
ATOM   2358  NE  ARG A 374       9.887  23.601  37.401  1.00 34.33           N  
ANISOU 2358  NE  ARG A 374     5152   3596   4294   -488    274   -222       N  
ATOM   2359  CZ  ARG A 374       9.419  22.548  36.753  1.00 37.96           C  
ANISOU 2359  CZ  ARG A 374     5578   4114   4732   -431    242   -167       C  
ATOM   2360  NH1 ARG A 374       9.444  21.358  37.335  1.00 38.08           N  
ANISOU 2360  NH1 ARG A 374     5499   4225   4747   -410    174   -176       N  
ATOM   2361  NH2 ARG A 374       8.925  22.671  35.519  1.00 38.83           N  
ANISOU 2361  NH2 ARG A 374     5756   4184   4814   -392    278   -103       N  
ATOM   2362  N   TYR A 375       7.119  27.384  39.410  1.00 42.65           N  
ANISOU 2362  N   TYR A 375     6548   4384   5271   -335    351   -239       N  
ATOM   2363  CA  TYR A 375       6.270  28.548  39.138  1.00 41.70           C  
ANISOU 2363  CA  TYR A 375     6565   4152   5128   -262    410   -203       C  
ATOM   2364  C   TYR A 375       5.602  29.098  40.394  1.00 43.91           C  
ANISOU 2364  C   TYR A 375     6882   4415   5389   -212    401   -244       C  
ATOM   2365  O   TYR A 375       5.323  30.291  40.474  1.00 45.90           O  
ANISOU 2365  O   TYR A 375     7258   4548   5633   -189    463   -252       O  
ATOM   2366  CB  TYR A 375       5.236  28.227  38.045  1.00 42.10           C  
ANISOU 2366  CB  TYR A 375     6633   4220   5143   -148    401   -102       C  
ATOM   2367  CG  TYR A 375       5.810  28.350  36.637  1.00 40.21           C  
ANISOU 2367  CG  TYR A 375     6442   3929   4906   -185    452    -58       C  
ATOM   2368  CD1 TYR A 375       6.440  27.263  36.031  1.00 39.26           C  
ANISOU 2368  CD1 TYR A 375     6229   3890   4798   -235    424    -50       C  
ATOM   2369  CD2 TYR A 375       5.768  29.579  35.937  1.00 40.16           C  
ANISOU 2369  CD2 TYR A 375     6589   3783   4888   -169    539    -26       C  
ATOM   2370  CE1 TYR A 375       7.000  27.377  34.758  1.00 41.40           C  
ANISOU 2370  CE1 TYR A 375     6550   4114   5065   -270    481    -13       C  
ATOM   2371  CE2 TYR A 375       6.327  29.710  34.674  1.00 40.29           C  
ANISOU 2371  CE2 TYR A 375     6663   3746   4897   -206    597     17       C  
ATOM   2372  CZ  TYR A 375       6.935  28.608  34.087  1.00 41.48           C  
ANISOU 2372  CZ  TYR A 375     6714   3989   5058   -256    568     22       C  
ATOM   2373  OH  TYR A 375       7.478  28.707  32.837  1.00 41.81           O  
ANISOU 2373  OH  TYR A 375     6816   3983   5087   -289    633     63       O  
ATOM   2374  N   ASN A 376       5.320  28.222  41.362  1.00 43.57           N  
ANISOU 2374  N   ASN A 376     6741   4483   5331   -189    330   -266       N  
ATOM   2375  CA  ASN A 376       4.961  28.650  42.706  1.00 42.31           C  
ANISOU 2375  CA  ASN A 376     6608   4319   5148   -166    323   -323       C  
ATOM   2376  C   ASN A 376       3.687  29.469  42.738  1.00 42.86           C  
ANISOU 2376  C   ASN A 376     6774   4323   5190    -44    366   -283       C  
ATOM   2377  O   ASN A 376       3.640  30.492  43.408  1.00 45.11           O  
ANISOU 2377  O   ASN A 376     7155   4518   5465    -43    410   -334       O  
ATOM   2378  CB  ASN A 376       6.132  29.456  43.321  1.00 43.36           C  
ANISOU 2378  CB  ASN A 376     6787   4383   5305   -290    349   -426       C  
ATOM   2379  CG  ASN A 376       5.953  29.723  44.817  1.00 48.89           C  
ANISOU 2379  CG  ASN A 376     7506   5099   5972   -282    326   -502       C  
ATOM   2380  OD1 ASN A 376       6.450  30.731  45.353  1.00 47.63           O  
ANISOU 2380  OD1 ASN A 376     7430   4851   5817   -349    361   -583       O  
ATOM   2381  ND2 ASN A 376       5.236  28.834  45.498  1.00 43.69           N  
ANISOU 2381  ND2 ASN A 376     6778   4548   5276   -205    271   -478       N  
ATOM   2382  N   ILE A 377       2.647  29.021  42.044  1.00 41.77           N  
ANISOU 2382  N   ILE A 377     6606   4230   5036     63    351   -198       N  
ATOM   2383  CA  ILE A 377       1.437  29.861  41.824  1.00 44.55           C  
ANISOU 2383  CA  ILE A 377     7042   4519   5364    196    393   -149       C  
ATOM   2384  C   ILE A 377       0.309  29.673  42.851  1.00 45.63           C  
ANISOU 2384  C   ILE A 377     7140   4722   5476    295    377   -152       C  
ATOM   2385  O   ILE A 377      -0.748  30.299  42.747  1.00 46.84           O  
ANISOU 2385  O   ILE A 377     7344   4842   5613    417    409   -114       O  
ATOM   2386  CB  ILE A 377       0.845  29.632  40.416  1.00 43.19           C  
ANISOU 2386  CB  ILE A 377     6864   4361   5185    271    384    -54       C  
ATOM   2387  CG1 ILE A 377       0.291  28.191  40.303  1.00 44.85           C  
ANISOU 2387  CG1 ILE A 377     6924   4725   5391    297    307    -19       C  
ATOM   2388  CG2 ILE A 377       1.907  29.885  39.368  1.00 43.50           C  
ANISOU 2388  CG2 ILE A 377     6958   4327   5241    181    417    -45       C  
ATOM   2389  CD1 ILE A 377      -0.812  28.009  39.284  1.00 42.16           C  
ANISOU 2389  CD1 ILE A 377     6563   4425   5031    411    285     64       C  
ATOM   2390  N   LEU A 378       0.528  28.762  43.798  1.00 46.28           N  
ANISOU 2390  N   LEU A 378     7129   4903   5552    248    331   -192       N  
ATOM   2391  CA  LEU A 378      -0.441  28.420  44.832  1.00 42.78           C  
ANISOU 2391  CA  LEU A 378     6640   4532   5080    324    323   -196       C  
ATOM   2392  C   LEU A 378      -1.011  29.660  45.560  1.00 44.91           C  
ANISOU 2392  C   LEU A 378     7023   4712   5328    399    388   -229       C  
ATOM   2393  O   LEU A 378      -2.251  29.818  45.668  1.00 42.11           O  
ANISOU 2393  O   LEU A 378     6659   4381   4961    524    411   -190       O  
ATOM   2394  CB  LEU A 378       0.257  27.508  45.822  1.00 41.63           C  
ANISOU 2394  CB  LEU A 378     6426   4469   4923    240    276   -248       C  
ATOM   2395  CG  LEU A 378      -0.351  26.218  46.338  1.00 41.71           C  
ANISOU 2395  CG  LEU A 378     6324   4607   4917    269    236   -219       C  
ATOM   2396  CD1 LEU A 378      -1.234  25.524  45.318  1.00 38.72           C  
ANISOU 2396  CD1 LEU A 378     5865   4287   4559    326    219   -137       C  
ATOM   2397  CD2 LEU A 378       0.801  25.317  46.764  1.00 39.65           C  
ANISOU 2397  CD2 LEU A 378     6010   4402   4653    166    181   -257       C  
ATOM   2398  N   GLU A 379      -0.125  30.536  46.053  1.00 44.65           N  
ANISOU 2398  N   GLU A 379     7093   4579   5292    324    420   -306       N  
ATOM   2399  CA  GLU A 379      -0.573  31.749  46.736  1.00 48.18           C  
ANISOU 2399  CA  GLU A 379     7667   4923   5716    386    488   -348       C  
ATOM   2400  C   GLU A 379      -1.460  32.597  45.818  1.00 49.65           C  
ANISOU 2400  C   GLU A 379     7930   5024   5911    512    543   -278       C  
ATOM   2401  O   GLU A 379      -2.565  32.963  46.216  1.00 51.70           O  
ANISOU 2401  O   GLU A 379     8210   5284   6150    642    578   -260       O  
ATOM   2402  CB  GLU A 379       0.595  32.590  47.253  1.00 51.47           C  
ANISOU 2402  CB  GLU A 379     8188   5233   6134    266    513   -449       C  
ATOM   2403  CG  GLU A 379       0.360  33.127  48.655  1.00 58.01           C  
ANISOU 2403  CG  GLU A 379     9089   6037   6917    288    540   -531       C  
ATOM   2404  CD  GLU A 379       1.087  34.430  48.968  1.00 67.77           C  
ANISOU 2404  CD  GLU A 379    10479   7115   8153    213    596   -624       C  
ATOM   2405  OE1 GLU A 379       1.731  35.027  48.074  1.00 73.69           O  
ANISOU 2405  OE1 GLU A 379    11293   7761   8946    145    628   -619       O  
ATOM   2406  OE2 GLU A 379       0.999  34.877  50.130  1.00 71.77           O  
ANISOU 2406  OE2 GLU A 379    11054   7599   8616    218    614   -705       O  
ATOM   2407  N   ASP A 380      -0.989  32.895  44.599  1.00 47.63           N  
ANISOU 2407  N   ASP A 380     7717   4699   5680    481    553   -236       N  
ATOM   2408  CA  ASP A 380      -1.755  33.714  43.645  1.00 47.51           C  
ANISOU 2408  CA  ASP A 380     7791   4599   5664    607    600   -162       C  
ATOM   2409  C   ASP A 380      -3.140  33.103  43.453  1.00 46.57           C  
ANISOU 2409  C   ASP A 380     7562   4599   5531    755    564    -89       C  
ATOM   2410  O   ASP A 380      -4.135  33.805  43.536  1.00 45.79           O  
ANISOU 2410  O   ASP A 380     7515   4463   5418    899    605    -62       O  
ATOM   2411  CB  ASP A 380      -1.081  33.801  42.266  1.00 51.23           C  
ANISOU 2411  CB  ASP A 380     8301   5013   6153    552    603   -112       C  
ATOM   2412  CG  ASP A 380       0.324  34.464  42.288  1.00 55.47           C  
ANISOU 2412  CG  ASP A 380     8939   5423   6713    394    652   -181       C  
ATOM   2413  OD1 ASP A 380       0.595  35.399  43.089  1.00 53.82           O  
ANISOU 2413  OD1 ASP A 380     8841   5105   6503    362    708   -255       O  
ATOM   2414  OD2 ASP A 380       1.164  34.033  41.451  1.00 58.09           O  
ANISOU 2414  OD2 ASP A 380     9238   5768   7067    297    636   -164       O  
ATOM   2415  N   VAL A 381      -3.206  31.787  43.217  1.00 44.30           N  
ANISOU 2415  N   VAL A 381     7121   4459   5254    719    490    -61       N  
ATOM   2416  CA  VAL A 381      -4.498  31.141  42.935  1.00 43.75           C  
ANISOU 2416  CA  VAL A 381     6933   4511   5180    839    453      3       C  
ATOM   2417  C   VAL A 381      -5.422  31.180  44.142  1.00 44.04           C  
ANISOU 2417  C   VAL A 381     6932   4597   5204    920    480    -25       C  
ATOM   2418  O   VAL A 381      -6.603  31.469  43.987  1.00 49.03           O  
ANISOU 2418  O   VAL A 381     7539   5258   5834   1065    496     18       O  
ATOM   2419  CB  VAL A 381      -4.357  29.723  42.335  1.00 43.39           C  
ANISOU 2419  CB  VAL A 381     6743   4596   5148    773    374     35       C  
ATOM   2420  CG1 VAL A 381      -5.690  28.957  42.408  1.00 40.07           C  
ANISOU 2420  CG1 VAL A 381     6182   4313   4729    868    339     75       C  
ATOM   2421  CG2 VAL A 381      -3.849  29.834  40.898  1.00 40.82           C  
ANISOU 2421  CG2 VAL A 381     6462   4224   4825    750    357     84       C  
ATOM   2422  N   ALA A 382      -4.871  30.973  45.333  1.00 41.55           N  
ANISOU 2422  N   ALA A 382     6621   4289   4877    835    490    -98       N  
ATOM   2423  CA  ALA A 382      -5.667  30.997  46.555  1.00 43.34           C  
ANISOU 2423  CA  ALA A 382     6826   4559   5081    904    527   -129       C  
ATOM   2424  C   ALA A 382      -6.234  32.363  46.859  1.00 45.33           C  
ANISOU 2424  C   ALA A 382     7207   4698   5319   1024    608   -144       C  
ATOM   2425  O   ALA A 382      -7.373  32.455  47.296  1.00 45.75           O  
ANISOU 2425  O   ALA A 382     7219   4801   5365   1148    642   -128       O  
ATOM   2426  CB  ALA A 382      -4.877  30.469  47.759  1.00 41.93           C  
ANISOU 2426  CB  ALA A 382     6641   4413   4879    789    514   -203       C  
ATOM   2427  N   VAL A 383      -5.446  33.420  46.639  1.00 47.16           N  
ANISOU 2427  N   VAL A 383     7595   4775   5548    985    645   -177       N  
ATOM   2428  CA  VAL A 383      -5.957  34.795  46.744  1.00 47.66           C  
ANISOU 2428  CA  VAL A 383     7807   4703   5600   1105    729   -183       C  
ATOM   2429  C   VAL A 383      -7.161  34.991  45.802  1.00 48.60           C  
ANISOU 2429  C   VAL A 383     7887   4850   5730   1282    731    -88       C  
ATOM   2430  O   VAL A 383      -8.199  35.488  46.223  1.00 49.43           O  
ANISOU 2430  O   VAL A 383     8002   4955   5824   1432    781    -79       O  
ATOM   2431  CB  VAL A 383      -4.848  35.879  46.493  1.00 48.29           C  
ANISOU 2431  CB  VAL A 383     8070   4596   5681   1017    774   -230       C  
ATOM   2432  CG1 VAL A 383      -5.473  37.255  46.309  1.00 44.35           C  
ANISOU 2432  CG1 VAL A 383     7733   3945   5174   1161    862   -213       C  
ATOM   2433  CG2 VAL A 383      -3.862  35.916  47.665  1.00 46.23           C  
ANISOU 2433  CG2 VAL A 383     7854   4307   5403    871    778   -344       C  
HETATM 2434  N   CAS A 384      -7.035  34.580  44.538  1.00 49.12           N  
ANISOU 2434  N   CAS A 384     7903   4948   5812   1270    675    -18       N  
HETATM 2435  CA  CAS A 384      -8.155  34.700  43.594  1.00 49.76           C  
ANISOU 2435  CA  CAS A 384     7937   5074   5895   1438    658     71       C  
HETATM 2436  CB  CAS A 384      -7.776  34.229  42.194  1.00 51.53           C  
ANISOU 2436  CB  CAS A 384     8131   5325   6124   1396    591    136       C  
HETATM 2437  C   CAS A 384      -9.376  33.927  44.087  1.00 50.28           C  
ANISOU 2437  C   CAS A 384     7824   5310   5969   1527    633     86       C  
HETATM 2438  O   CAS A 384     -10.525  34.328  43.855  1.00 49.24           O  
ANISOU 2438  O   CAS A 384     7661   5209   5839   1701    648    131       O  
HETATM 2439  SG  CAS A 384      -6.306  34.994  41.449  1.00 57.36           S  
ANISOU 2439  SG  CAS A 384     9058   5878   6857   1273    628    128       S  
HETATM 2440  CE1 CAS A 384      -7.661  38.029  41.948  1.00 75.21           C  
HETATM 2441  CE2 CAS A 384      -7.120  37.171  38.626  1.00 82.58           C  
HETATM 2442 AS   CAS A 384      -8.065  36.879  40.369  1.00 93.63          AS  
ATOM   2443  N   MET A 385      -9.117  32.832  44.797  1.00 47.03           N  
ANISOU 2443  N   MET A 385     7297   5007   5566   1410    601     47       N  
ATOM   2444  CA  MET A 385     -10.180  31.995  45.314  1.00 48.35           C  
ANISOU 2444  CA  MET A 385     7294   5332   5745   1464    589     57       C  
ATOM   2445  C   MET A 385     -10.723  32.558  46.602  1.00 51.22           C  
ANISOU 2445  C   MET A 385     7697   5672   6091   1539    675      8       C  
ATOM   2446  O   MET A 385     -11.733  32.077  47.114  1.00 52.31           O  
ANISOU 2446  O   MET A 385     7708   5928   6239   1607    692     16       O  
ATOM   2447  CB  MET A 385      -9.676  30.570  45.542  1.00 46.80           C  
ANISOU 2447  CB  MET A 385     6976   5247   5559   1310    530     42       C  
ATOM   2448  CG  MET A 385      -9.467  29.809  44.255  1.00 43.65           C  
ANISOU 2448  CG  MET A 385     6499   4906   5178   1259    445     94       C  
ATOM   2449  SD  MET A 385      -8.916  28.130  44.573  1.00 47.75           S  
ANISOU 2449  SD  MET A 385     6890   5544   5711   1092    387     76       S  
ATOM   2450  CE  MET A 385     -10.341  27.390  45.367  1.00 44.16           C  
ANISOU 2450  CE  MET A 385     6271   5237   5272   1159    410     83       C  
ATOM   2451  N   ASP A 386     -10.040  33.583  47.113  1.00 54.41           N  
ANISOU 2451  N   ASP A 386     8282   5923   6469   1521    735    -46       N  
ATOM   2452  CA  ASP A 386     -10.440  34.302  48.320  1.00 54.26           C  
ANISOU 2452  CA  ASP A 386     8343   5851   6422   1595    825   -103       C  
ATOM   2453  C   ASP A 386     -10.290  33.442  49.586  1.00 53.70           C  
ANISOU 2453  C   ASP A 386     8204   5872   6327   1501    831   -160       C  
ATOM   2454  O   ASP A 386     -11.124  33.485  50.496  1.00 54.15           O  
ANISOU 2454  O   ASP A 386     8231   5977   6367   1586    894   -179       O  
ATOM   2455  CB  ASP A 386     -11.871  34.846  48.160  1.00 60.12           C  
ANISOU 2455  CB  ASP A 386     9043   6623   7177   1809    873    -56       C  
ATOM   2456  CG  ASP A 386     -12.150  35.995  49.090  1.00 67.47           C  
ANISOU 2456  CG  ASP A 386    10120   7438   8077   1910    981   -110       C  
ATOM   2457  OD1 ASP A 386     -11.321  36.940  49.093  1.00 67.95           O  
ANISOU 2457  OD1 ASP A 386    10374   7326   8119   1870   1014   -150       O  
ATOM   2458  OD2 ASP A 386     -13.171  35.933  49.829  1.00 70.84           O  
ANISOU 2458  OD2 ASP A 386    10471   7943   8501   2020   1037   -117       O  
ATOM   2459  N   LEU A 387      -9.218  32.656  49.643  1.00 49.03           N  
ANISOU 2459  N   LEU A 387     7594   5306   5731   1332    769   -184       N  
ATOM   2460  CA  LEU A 387      -8.992  31.766  50.758  1.00 46.29           C  
ANISOU 2460  CA  LEU A 387     7190   5045   5351   1245    763   -227       C  
ATOM   2461  C   LEU A 387      -8.160  32.486  51.796  1.00 48.97           C  
ANISOU 2461  C   LEU A 387     7689   5279   5638   1186    801   -322       C  
ATOM   2462  O   LEU A 387      -7.503  33.459  51.486  1.00 47.03           O  
ANISOU 2462  O   LEU A 387     7579   4897   5394   1163    813   -355       O  
ATOM   2463  CB  LEU A 387      -8.281  30.505  50.283  1.00 41.81           C  
ANISOU 2463  CB  LEU A 387     6519   4563   4803   1108    672   -203       C  
ATOM   2464  CG  LEU A 387      -9.045  29.773  49.178  1.00 42.54           C  
ANISOU 2464  CG  LEU A 387     6461   4756   4945   1151    627   -119       C  
ATOM   2465  CD1 LEU A 387      -8.186  28.655  48.605  1.00 39.20           C  
ANISOU 2465  CD1 LEU A 387     5969   4387   4540   1013    542   -102       C  
ATOM   2466  CD2 LEU A 387     -10.431  29.283  49.616  1.00 39.81           C  
ANISOU 2466  CD2 LEU A 387     5985   4531   4610   1248    666    -90       C  
ATOM   2467  N   ASP A 388      -8.176  31.986  53.031  1.00 52.66           N  
ANISOU 2467  N   ASP A 388     8143   5809   6055   1155    820   -368       N  
ATOM   2468  CA  ASP A 388      -7.347  32.532  54.088  1.00 52.40           C  
ANISOU 2468  CA  ASP A 388     8252   5698   5959   1088    839   -467       C  
ATOM   2469  C   ASP A 388      -5.909  32.033  53.969  1.00 52.77           C  
ANISOU 2469  C   ASP A 388     8304   5745   6003    918    748   -502       C  
ATOM   2470  O   ASP A 388      -5.597  30.924  54.353  1.00 52.78           O  
ANISOU 2470  O   ASP A 388     8219   5851   5983    848    696   -495       O  
ATOM   2471  CB  ASP A 388      -7.925  32.121  55.423  1.00 55.10           C  
ANISOU 2471  CB  ASP A 388     8580   6120   6236   1126    889   -496       C  
ATOM   2472  CG  ASP A 388      -7.333  32.882  56.570  1.00 57.43           C  
ANISOU 2472  CG  ASP A 388     9039   6330   6453   1095    923   -604       C  
ATOM   2473  OD1 ASP A 388      -6.284  33.558  56.388  1.00 54.77           O  
ANISOU 2473  OD1 ASP A 388     8810   5885   6116   1007    889   -665       O  
ATOM   2474  OD2 ASP A 388      -7.925  32.773  57.667  1.00 58.13           O  
ANISOU 2474  OD2 ASP A 388     9145   6465   6478   1153    985   -630       O  
ATOM   2475  N   THR A 389      -5.024  32.866  53.450  1.00 53.68           N  
ANISOU 2475  N   THR A 389     8521   5738   6139    854    735   -540       N  
ATOM   2476  CA  THR A 389      -3.645  32.458  53.254  1.00 54.61           C  
ANISOU 2476  CA  THR A 389     8629   5858   6264    695    655   -576       C  
ATOM   2477  C   THR A 389      -2.743  32.739  54.461  1.00 55.13           C  
ANISOU 2477  C   THR A 389     8787   5897   6265    604    640   -692       C  
ATOM   2478  O   THR A 389      -1.549  32.435  54.429  1.00 55.78           O  
ANISOU 2478  O   THR A 389     8853   5991   6351    473    569   -735       O  
ATOM   2479  CB  THR A 389      -3.057  33.096  51.988  1.00 57.39           C  
ANISOU 2479  CB  THR A 389     9025   6103   6678    651    648   -556       C  
ATOM   2480  OG1 THR A 389      -3.031  34.525  52.140  1.00 61.61           O  
ANISOU 2480  OG1 THR A 389     9728   6478   7204    681    722   -613       O  
ATOM   2481  CG2 THR A 389      -3.902  32.710  50.754  1.00 55.25           C  
ANISOU 2481  CG2 THR A 389     8659   5877   6459    740    643   -442       C  
ATOM   2482  N   ARG A 390      -3.313  33.294  55.519  1.00 56.49           N  
ANISOU 2482  N   ARG A 390     9048   6042   6374    677    705   -745       N  
ATOM   2483  CA  ARG A 390      -2.550  33.610  56.730  1.00 63.62           C  
ANISOU 2483  CA  ARG A 390    10051   6924   7200    601    690   -863       C  
ATOM   2484  C   ARG A 390      -2.495  32.411  57.707  1.00 61.76           C  
ANISOU 2484  C   ARG A 390     9737   6837   6892    583    639   -863       C  
ATOM   2485  O   ARG A 390      -1.822  32.461  58.724  1.00 59.19           O  
ANISOU 2485  O   ARG A 390     9477   6524   6489    522    605   -954       O  
ATOM   2486  CB  ARG A 390      -3.146  34.823  57.461  1.00 68.17           C  
ANISOU 2486  CB  ARG A 390    10785   7388   7727    689    789   -930       C  
ATOM   2487  CG  ARG A 390      -3.231  36.156  56.711  1.00 77.45           C  
ANISOU 2487  CG  ARG A 390    12082   8388   8955    722    857   -940       C  
ATOM   2488  CD  ARG A 390      -4.186  37.122  57.440  1.00 84.18           C  
ANISOU 2488  CD  ARG A 390    13068   9156   9761    859    970   -978       C  
ATOM   2489  NE  ARG A 390      -5.195  36.390  58.234  1.00 89.60           N  
ANISOU 2489  NE  ARG A 390    13676   9974  10395    965   1000   -943       N  
ATOM   2490  CZ  ARG A 390      -6.414  36.827  58.563  1.00 92.69           C  
ANISOU 2490  CZ  ARG A 390    14099  10349  10769   1128   1103   -921       C  
ATOM   2491  NH1 ARG A 390      -6.844  38.023  58.166  1.00 96.25           N  
ANISOU 2491  NH1 ARG A 390    14667  10655  11250   1223   1185   -927       N  
ATOM   2492  NH2 ARG A 390      -7.215  36.048  59.290  1.00 87.83           N  
ANISOU 2492  NH2 ARG A 390    13398   9865  10110   1198   1132   -890       N  
ATOM   2493  N   THR A 391      -3.199  31.333  57.400  1.00 60.93           N  
ANISOU 2493  N   THR A 391     9498   6843   6809    635    634   -763       N  
ATOM   2494  CA  THR A 391      -3.317  30.240  58.355  1.00 62.27           C  
ANISOU 2494  CA  THR A 391     9615   7138   6907    635    611   -752       C  
ATOM   2495  C   THR A 391      -3.277  28.890  57.647  1.00 59.09           C  
ANISOU 2495  C   THR A 391     9057   6839   6554    602    551   -658       C  
ATOM   2496  O   THR A 391      -3.915  28.681  56.625  1.00 60.34           O  
ANISOU 2496  O   THR A 391     9129   7007   6790    643    568   -578       O  
ATOM   2497  CB  THR A 391      -4.560  30.417  59.277  1.00 69.10           C  
ANISOU 2497  CB  THR A 391    10521   8024   7711    760    716   -747       C  
ATOM   2498  OG1 THR A 391      -4.754  29.245  60.078  1.00 77.22           O  
ANISOU 2498  OG1 THR A 391    11491   9173   8675    760    706   -716       O  
ATOM   2499  CG2 THR A 391      -5.835  30.695  58.491  1.00 64.79           C  
ANISOU 2499  CG2 THR A 391     9914   7463   7239    878    796   -669       C  
ATOM   2500  N   THR A 392      -2.487  27.976  58.175  1.00 57.75           N  
ANISOU 2500  N   THR A 392     8857   6747   6337    530    477   -672       N  
ATOM   2501  CA  THR A 392      -2.310  26.683  57.517  1.00 54.84           C  
ANISOU 2501  CA  THR A 392     8358   6464   6014    492    419   -591       C  
ATOM   2502  C   THR A 392      -3.612  25.880  57.554  1.00 52.04           C  
ANISOU 2502  C   THR A 392     7923   6183   5668    573    483   -502       C  
ATOM   2503  O   THR A 392      -3.980  25.225  56.588  1.00 50.52           O  
ANISOU 2503  O   THR A 392     7622   6025   5549    571    472   -426       O  
ATOM   2504  CB  THR A 392      -1.185  25.884  58.198  1.00 52.92           C  
ANISOU 2504  CB  THR A 392     8111   6287   5708    415    328   -625       C  
ATOM   2505  OG1 THR A 392      -1.427  25.841  59.620  1.00 51.42           O  
ANISOU 2505  OG1 THR A 392     8002   6132   5402    456    356   -665       O  
ATOM   2506  CG2 THR A 392       0.195  26.522  57.906  1.00 49.65           C  
ANISOU 2506  CG2 THR A 392     7731   5819   5314    315    251   -708       C  
ATOM   2507  N   SER A 393      -4.316  25.973  58.669  1.00 50.51           N  
ANISOU 2507  N   SER A 393     7783   6012   5397    639    555   -518       N  
ATOM   2508  CA  SER A 393      -5.468  25.118  58.922  1.00 52.36           C  
ANISOU 2508  CA  SER A 393     7940   6325   5628    699    624   -443       C  
ATOM   2509  C   SER A 393      -6.735  25.442  58.132  1.00 51.13           C  
ANISOU 2509  C   SER A 393     7705   6165   5556    780    697   -389       C  
ATOM   2510  O   SER A 393      -7.750  24.736  58.294  1.00 48.68           O  
ANISOU 2510  O   SER A 393     7312   5928   5257    822    759   -331       O  
ATOM   2511  CB  SER A 393      -5.775  25.059  60.426  1.00 55.70           C  
ANISOU 2511  CB  SER A 393     8451   6778   5932    741    686   -477       C  
ATOM   2512  OG  SER A 393      -5.801  26.354  60.992  1.00 58.37           O  
ANISOU 2512  OG  SER A 393     8915   7041   6224    786    730   -561       O  
ATOM   2513  N   SER A 394      -6.696  26.497  57.309  1.00 48.14           N  
ANISOU 2513  N   SER A 394     7354   5704   5235    805    693   -407       N  
ATOM   2514  CA  SER A 394      -7.744  26.703  56.299  1.00 48.46           C  
ANISOU 2514  CA  SER A 394     7303   5750   5361    881    731   -345       C  
ATOM   2515  C   SER A 394      -7.621  25.712  55.114  1.00 45.58           C  
ANISOU 2515  C   SER A 394     6807   5440   5072    822    658   -275       C  
ATOM   2516  O   SER A 394      -8.569  25.548  54.334  1.00 47.60           O  
ANISOU 2516  O   SER A 394     6959   5736   5391    876    677   -217       O  
ATOM   2517  CB  SER A 394      -7.728  28.139  55.768  1.00 48.92           C  
ANISOU 2517  CB  SER A 394     7448   5693   5446    937    751   -379       C  
ATOM   2518  OG  SER A 394      -6.584  28.325  54.947  1.00 48.87           O  
ANISOU 2518  OG  SER A 394     7471   5625   5472    846    669   -393       O  
ATOM   2519  N   LEU A 395      -6.471  25.050  54.986  1.00 42.68           N  
ANISOU 2519  N   LEU A 395     6442   5080   4696    716    575   -283       N  
ATOM   2520  CA  LEU A 395      -6.182  24.125  53.859  1.00 39.37           C  
ANISOU 2520  CA  LEU A 395     5918   4700   4340    653    505   -227       C  
ATOM   2521  C   LEU A 395      -6.239  24.829  52.507  1.00 41.23           C  
ANISOU 2521  C   LEU A 395     6139   4880   4645    675    483   -207       C  
ATOM   2522  O   LEU A 395      -6.558  24.216  51.455  1.00 39.60           O  
ANISOU 2522  O   LEU A 395     5834   4716   4497    666    451   -149       O  
ATOM   2523  CB  LEU A 395      -7.051  22.859  53.873  1.00 38.35           C  
ANISOU 2523  CB  LEU A 395     5671   4671   4231    656    527   -162       C  
ATOM   2524  CG  LEU A 395      -7.099  22.020  55.178  1.00 40.43           C  
ANISOU 2524  CG  LEU A 395     5953   4989   4421    638    562   -164       C  
ATOM   2525  CD1 LEU A 395      -7.770  20.651  54.955  1.00 36.33           C  
ANISOU 2525  CD1 LEU A 395     5316   4551   3936    610    577    -96       C  
ATOM   2526  CD2 LEU A 395      -5.699  21.833  55.766  1.00 38.72           C  
ANISOU 2526  CD2 LEU A 395     5823   4750   4140    568    494   -209       C  
ATOM   2527  N   TRP A 396      -5.891  26.122  52.543  1.00 41.57           N  
ANISOU 2527  N   TRP A 396     6295   4824   4678    700    502   -256       N  
ATOM   2528  CA  TRP A 396      -5.820  26.932  51.347  1.00 42.22           C  
ANISOU 2528  CA  TRP A 396     6399   4831   4811    722    491   -239       C  
ATOM   2529  C   TRP A 396      -4.904  26.381  50.296  1.00 42.35           C  
ANISOU 2529  C   TRP A 396     6376   4849   4867    629    415   -216       C  
ATOM   2530  O   TRP A 396      -5.224  26.472  49.115  1.00 42.80           O  
ANISOU 2530  O   TRP A 396     6395   4898   4969    658    400   -166       O  
ATOM   2531  CB  TRP A 396      -5.484  28.383  51.658  1.00 41.56           C  
ANISOU 2531  CB  TRP A 396     6465   4622   4705    749    534   -302       C  
ATOM   2532  CG  TRP A 396      -4.102  28.643  52.181  1.00 41.51           C  
ANISOU 2532  CG  TRP A 396     6548   4559   4666    637    499   -381       C  
ATOM   2533  CD1 TRP A 396      -3.700  28.711  53.518  1.00 41.22           C  
ANISOU 2533  CD1 TRP A 396     6577   4526   4558    607    506   -456       C  
ATOM   2534  CD2 TRP A 396      -2.900  28.965  51.410  1.00 38.84           C  
ANISOU 2534  CD2 TRP A 396     6247   4151   4359    539    453   -405       C  
ATOM   2535  NE1 TRP A 396      -2.372  29.021  53.617  1.00 39.32           N  
ANISOU 2535  NE1 TRP A 396     6398   4235   4308    498    457   -525       N  
ATOM   2536  CE2 TRP A 396      -1.823  29.169  52.395  1.00 39.63           C  
ANISOU 2536  CE2 TRP A 396     6417   4227   4412    447    428   -499       C  
ATOM   2537  CE3 TRP A 396      -2.608  29.075  50.064  1.00 39.43           C  
ANISOU 2537  CE3 TRP A 396     6303   4187   4491    516    431   -360       C  
ATOM   2538  CZ2 TRP A 396      -0.524  29.500  52.016  1.00 38.84           C  
ANISOU 2538  CZ2 TRP A 396     6352   4070   4335    333    387   -550       C  
ATOM   2539  CZ3 TRP A 396      -1.286  29.403  49.685  1.00 39.60           C  
ANISOU 2539  CZ3 TRP A 396     6372   4142   4531    401    401   -405       C  
ATOM   2540  CH2 TRP A 396      -0.277  29.626  50.643  1.00 39.50           C  
ANISOU 2540  CH2 TRP A 396     6414   4110   4485    309    381   -500       C  
ATOM   2541  N   LYS A 397      -3.765  25.811  50.693  1.00 40.61           N  
ANISOU 2541  N   LYS A 397     6163   4642   4625    525    365   -252       N  
ATOM   2542  CA  LYS A 397      -2.869  25.272  49.717  1.00 40.09           C  
ANISOU 2542  CA  LYS A 397     6056   4580   4598    442    300   -233       C  
ATOM   2543  C   LYS A 397      -3.561  24.090  49.051  1.00 41.29           C  
ANISOU 2543  C   LYS A 397     6086   4822   4781    455    278   -160       C  
ATOM   2544  O   LYS A 397      -3.501  23.919  47.817  1.00 41.83           O  
ANISOU 2544  O   LYS A 397     6114   4886   4891    443    248   -120       O  
ATOM   2545  CB  LYS A 397      -1.575  24.841  50.371  1.00 41.89           C  
ANISOU 2545  CB  LYS A 397     6300   4819   4795    343    251   -288       C  
ATOM   2546  CG  LYS A 397      -0.586  25.965  50.582  1.00 45.19           C  
ANISOU 2546  CG  LYS A 397     6822   5145   5205    290    252   -367       C  
ATOM   2547  CD  LYS A 397       0.697  25.411  51.176  1.00 48.82           C  
ANISOU 2547  CD  LYS A 397     7268   5643   5639    195    186   -421       C  
ATOM   2548  CE  LYS A 397       1.681  26.510  51.544  1.00 49.90           C  
ANISOU 2548  CE  LYS A 397     7495   5698   5765    127    184   -516       C  
ATOM   2549  NZ  LYS A 397       3.060  25.943  51.545  1.00 51.29           N  
ANISOU 2549  NZ  LYS A 397     7619   5918   5950     25    108   -556       N  
ATOM   2550  N   ASP A 398      -4.251  23.293  49.865  1.00 41.24           N  
ANISOU 2550  N   ASP A 398     6026   4894   4751    477    297   -144       N  
ATOM   2551  CA  ASP A 398      -4.931  22.087  49.377  1.00 41.41           C  
ANISOU 2551  CA  ASP A 398     5931   5000   4803    473    283    -84       C  
ATOM   2552  C   ASP A 398      -6.052  22.426  48.407  1.00 40.57           C  
ANISOU 2552  C   ASP A 398     5766   4908   4742    548    298    -41       C  
ATOM   2553  O   ASP A 398      -6.153  21.838  47.347  1.00 41.56           O  
ANISOU 2553  O   ASP A 398     5822   5064   4904    526    256     -3       O  
ATOM   2554  CB  ASP A 398      -5.468  21.254  50.551  1.00 42.06           C  
ANISOU 2554  CB  ASP A 398     5982   5150   4847    479    320    -79       C  
ATOM   2555  CG  ASP A 398      -4.453  21.132  51.696  1.00 44.20           C  
ANISOU 2555  CG  ASP A 398     6333   5408   5053    433    306   -126       C  
ATOM   2556  OD1 ASP A 398      -4.100  22.168  52.347  1.00 43.65           O  
ANISOU 2556  OD1 ASP A 398     6358   5284   4943    453    323   -183       O  
ATOM   2557  OD2 ASP A 398      -3.992  19.989  51.920  1.00 44.66           O  
ANISOU 2557  OD2 ASP A 398     6362   5509   5097    380    273   -109       O  
ATOM   2558  N   LYS A 399      -6.893  23.382  48.772  1.00 42.54           N  
ANISOU 2558  N   LYS A 399     6043   5137   4983    644    356    -48       N  
ATOM   2559  CA  LYS A 399      -7.998  23.789  47.909  1.00 44.30           C  
ANISOU 2559  CA  LYS A 399     6207   5382   5244    737    367     -8       C  
ATOM   2560  C   LYS A 399      -7.523  24.330  46.557  1.00 43.15           C  
ANISOU 2560  C   LYS A 399     6099   5176   5121    738    319     12       C  
ATOM   2561  O   LYS A 399      -8.098  24.007  45.501  1.00 41.87           O  
ANISOU 2561  O   LYS A 399     5857   5062   4989    766    283     57       O  
ATOM   2562  CB  LYS A 399      -8.869  24.815  48.638  1.00 45.48           C  
ANISOU 2562  CB  LYS A 399     6395   5508   5376    853    445    -24       C  
ATOM   2563  CG  LYS A 399      -9.582  24.224  49.849  1.00 49.35           C  
ANISOU 2563  CG  LYS A 399     6831   6073   5845    864    505    -32       C  
ATOM   2564  CD  LYS A 399     -10.223  25.274  50.763  1.00 49.22           C  
ANISOU 2564  CD  LYS A 399     6881   6023   5798    972    593    -63       C  
ATOM   2565  CE  LYS A 399     -11.464  24.677  51.410  1.00 51.58           C  
ANISOU 2565  CE  LYS A 399     7066   6426   6105   1019    661    -44       C  
ATOM   2566  NZ  LYS A 399     -12.308  25.684  52.128  1.00 58.40           N  
ANISOU 2566  NZ  LYS A 399     7968   7271   6950   1147    756    -66       N  
ATOM   2567  N   ALA A 400      -6.465  25.135  46.593  1.00 40.74           N  
ANISOU 2567  N   ALA A 400     5915   4767   4798    703    321    -24       N  
ATOM   2568  CA  ALA A 400      -5.953  25.752  45.368  1.00 42.97           C  
ANISOU 2568  CA  ALA A 400     6254   4975   5095    701    296     -5       C  
ATOM   2569  C   ALA A 400      -5.293  24.712  44.471  1.00 40.88           C  
ANISOU 2569  C   ALA A 400     5929   4752   4850    608    230     18       C  
ATOM   2570  O   ALA A 400      -5.521  24.704  43.255  1.00 44.30           O  
ANISOU 2570  O   ALA A 400     6343   5191   5299    634    200     61       O  
ATOM   2571  CB  ALA A 400      -4.991  26.894  45.687  1.00 40.67           C  
ANISOU 2571  CB  ALA A 400     6109   4557   4788    672    329    -56       C  
ATOM   2572  N   ALA A 401      -4.490  23.831  45.059  1.00 38.02           N  
ANISOU 2572  N   ALA A 401     5543   4420   4482    510    208    -10       N  
ATOM   2573  CA  ALA A 401      -3.903  22.712  44.286  1.00 38.34           C  
ANISOU 2573  CA  ALA A 401     5522   4504   4541    430    152     11       C  
ATOM   2574  C   ALA A 401      -4.967  21.862  43.553  1.00 38.12           C  
ANISOU 2574  C   ALA A 401     5386   4564   4533    463    124     61       C  
ATOM   2575  O   ALA A 401      -4.769  21.417  42.383  1.00 36.98           O  
ANISOU 2575  O   ALA A 401     5216   4432   4403    436     81     87       O  
ATOM   2576  CB  ALA A 401      -3.057  21.828  45.191  1.00 35.19           C  
ANISOU 2576  CB  ALA A 401     5108   4134   4127    345    135    -22       C  
ATOM   2577  N   VAL A 402      -6.097  21.631  44.226  1.00 37.57           N  
ANISOU 2577  N   VAL A 402     5251   4558   4465    516    152     69       N  
ATOM   2578  CA  VAL A 402      -7.145  20.824  43.608  1.00 37.57           C  
ANISOU 2578  CA  VAL A 402     5134   4650   4492    535    127    105       C  
ATOM   2579  C   VAL A 402      -7.606  21.525  42.353  1.00 39.32           C  
ANISOU 2579  C   VAL A 402     5359   4862   4720    609     98    136       C  
ATOM   2580  O   VAL A 402      -7.706  20.904  41.297  1.00 39.33           O  
ANISOU 2580  O   VAL A 402     5309   4904   4732    585     44    158       O  
ATOM   2581  CB  VAL A 402      -8.333  20.546  44.542  1.00 40.83           C  
ANISOU 2581  CB  VAL A 402     5465   5135   4911    579    174    107       C  
ATOM   2582  CG1 VAL A 402      -9.463  19.818  43.812  1.00 39.52           C  
ANISOU 2582  CG1 VAL A 402     5166   5069   4783    592    145    136       C  
ATOM   2583  CG2 VAL A 402      -7.863  19.707  45.708  1.00 40.19           C  
ANISOU 2583  CG2 VAL A 402     5392   5066   4812    504    200     87       C  
ATOM   2584  N   GLU A 403      -7.847  22.829  42.455  1.00 42.27           N  
ANISOU 2584  N   GLU A 403     5805   5173   5080    702    134    136       N  
ATOM   2585  CA  GLU A 403      -8.417  23.568  41.352  1.00 42.27           C  
ANISOU 2585  CA  GLU A 403     5818   5164   5078    799    111    173       C  
ATOM   2586  C   GLU A 403      -7.442  23.721  40.215  1.00 40.71           C  
ANISOU 2586  C   GLU A 403     5701   4901   4867    754     76    188       C  
ATOM   2587  O   GLU A 403      -7.840  23.638  39.058  1.00 44.22           O  
ANISOU 2587  O   GLU A 403     6120   5378   5303    794     28    224       O  
ATOM   2588  CB  GLU A 403      -8.954  24.914  41.808  1.00 45.59           C  
ANISOU 2588  CB  GLU A 403     6309   5526   5487    922    169    172       C  
ATOM   2589  CG  GLU A 403     -10.128  24.827  42.782  1.00 51.04           C  
ANISOU 2589  CG  GLU A 403     6908   6294   6192    993    211    163       C  
ATOM   2590  CD  GLU A 403     -11.267  23.886  42.362  1.00 52.21           C  
ANISOU 2590  CD  GLU A 403     6883   6585   6372   1011    170    188       C  
ATOM   2591  OE1 GLU A 403     -11.496  23.648  41.160  1.00 56.24           O  
ANISOU 2591  OE1 GLU A 403     7347   7135   6884   1025    101    218       O  
ATOM   2592  OE2 GLU A 403     -11.961  23.382  43.263  1.00 55.49           O  
ANISOU 2592  OE2 GLU A 403     7205   7072   6805   1008    209    173       O  
ATOM   2593  N   ILE A 404      -6.168  23.926  40.530  1.00 40.27           N  
ANISOU 2593  N   ILE A 404     5737   4759   4803    670     99    157       N  
ATOM   2594  CA  ILE A 404      -5.147  24.018  39.491  1.00 36.98           C  
ANISOU 2594  CA  ILE A 404     5391   4282   4378    613     80    168       C  
ATOM   2595  C   ILE A 404      -5.063  22.685  38.721  1.00 39.34           C  
ANISOU 2595  C   ILE A 404     5600   4663   4683    548     19    182       C  
ATOM   2596  O   ILE A 404      -5.015  22.662  37.481  1.00 39.84           O  
ANISOU 2596  O   ILE A 404     5682   4724   4730    560    -14    213       O  
ATOM   2597  CB  ILE A 404      -3.790  24.397  40.098  1.00 35.78           C  
ANISOU 2597  CB  ILE A 404     5327   4040   4228    521    117    121       C  
ATOM   2598  CG1 ILE A 404      -3.818  25.836  40.653  1.00 36.18           C  
ANISOU 2598  CG1 ILE A 404     5492   3988   4269    579    180    101       C  
ATOM   2599  CG2 ILE A 404      -2.686  24.314  39.063  1.00 35.09           C  
ANISOU 2599  CG2 ILE A 404     5288   3904   4140    447    106    128       C  
ATOM   2600  CD1 ILE A 404      -2.795  26.096  41.738  1.00 34.76           C  
ANISOU 2600  CD1 ILE A 404     5364   3752   4090    492    211     34       C  
ATOM   2601  N   ASN A 405      -5.062  21.575  39.460  1.00 40.94           N  
ANISOU 2601  N   ASN A 405     5719   4933   4905    482      7    160       N  
ATOM   2602  CA  ASN A 405      -5.066  20.243  38.863  1.00 40.69           C  
ANISOU 2602  CA  ASN A 405     5606   4972   4882    420    -42    168       C  
ATOM   2603  C   ASN A 405      -6.267  19.997  37.985  1.00 40.66           C  
ANISOU 2603  C   ASN A 405     5526   5045   4876    481    -88    198       C  
ATOM   2604  O   ASN A 405      -6.120  19.506  36.860  1.00 41.59           O  
ANISOU 2604  O   ASN A 405     5638   5183   4982    457   -134    212       O  
ATOM   2605  CB  ASN A 405      -4.890  19.162  39.934  1.00 43.59           C  
ANISOU 2605  CB  ASN A 405     5915   5382   5267    348    -34    142       C  
ATOM   2606  CG  ASN A 405      -3.415  18.908  40.250  1.00 44.77           C  
ANISOU 2606  CG  ASN A 405     6119   5478   5414    264    -28    115       C  
ATOM   2607  OD1 ASN A 405      -2.741  18.161  39.539  1.00 46.75           O  
ANISOU 2607  OD1 ASN A 405     6362   5731   5668    205    -55    116       O  
ATOM   2608  ND2 ASN A 405      -2.903  19.561  41.289  1.00 44.07           N  
ANISOU 2608  ND2 ASN A 405     6084   5344   5317    261      7     84       N  
ATOM   2609  N   LEU A 406      -7.448  20.401  38.455  1.00 40.73           N  
ANISOU 2609  N   LEU A 406     5479   5102   4895    566    -75    206       N  
ATOM   2610  CA  LEU A 406      -8.648  20.283  37.656  1.00 38.82           C  
ANISOU 2610  CA  LEU A 406     5150   4947   4653    637   -125    230       C  
ATOM   2611  C   LEU A 406      -8.517  21.127  36.404  1.00 42.68           C  
ANISOU 2611  C   LEU A 406     5721   5392   5102    709   -157    263       C  
ATOM   2612  O   LEU A 406      -8.921  20.705  35.299  1.00 45.91           O  
ANISOU 2612  O   LEU A 406     6088   5862   5492    721   -223    279       O  
ATOM   2613  CB  LEU A 406      -9.910  20.677  38.449  1.00 39.63           C  
ANISOU 2613  CB  LEU A 406     5171   5110   4777    727    -95    230       C  
ATOM   2614  CG  LEU A 406     -11.233  20.450  37.685  1.00 41.48           C  
ANISOU 2614  CG  LEU A 406     5278   5461   5021    797   -155    246       C  
ATOM   2615  CD1 LEU A 406     -11.343  19.019  37.152  1.00 39.97           C  
ANISOU 2615  CD1 LEU A 406     4990   5349   4846    689   -212    230       C  
ATOM   2616  CD2 LEU A 406     -12.464  20.785  38.531  1.00 42.00           C  
ANISOU 2616  CD2 LEU A 406     5243   5596   5117    884   -115    243       C  
ATOM   2617  N   ALA A 407      -7.930  22.311  36.538  1.00 40.80           N  
ANISOU 2617  N   ALA A 407     5611   5047   4846    753   -108    272       N  
ATOM   2618  CA  ALA A 407      -7.809  23.168  35.362  1.00 40.67           C  
ANISOU 2618  CA  ALA A 407     5693   4974   4785    826   -124    313       C  
ATOM   2619  C   ALA A 407      -6.901  22.490  34.316  1.00 41.23           C  
ANISOU 2619  C   ALA A 407     5800   5034   4833    736   -158    316       C  
ATOM   2620  O   ALA A 407      -7.188  22.544  33.107  1.00 40.89           O  
ANISOU 2620  O   ALA A 407     5777   5014   4747    786   -208    349       O  
ATOM   2621  CB  ALA A 407      -7.310  24.571  35.724  1.00 38.22           C  
ANISOU 2621  CB  ALA A 407     5528   4531   4463    877    -52    320       C  
ATOM   2622  N   VAL A 408      -5.831  21.834  34.771  1.00 38.37           N  
ANISOU 2622  N   VAL A 408     5445   4641   4494    611   -134    282       N  
ATOM   2623  CA  VAL A 408      -4.965  21.165  33.818  1.00 39.72           C  
ANISOU 2623  CA  VAL A 408     5644   4801   4645    532   -156    282       C  
ATOM   2624  C   VAL A 408      -5.769  20.099  33.069  1.00 40.02           C  
ANISOU 2624  C   VAL A 408     5583   4950   4672    530   -233    285       C  
ATOM   2625  O   VAL A 408      -5.765  20.073  31.833  1.00 41.51           O  
ANISOU 2625  O   VAL A 408     5810   5147   4814    552   -273    308       O  
ATOM   2626  CB  VAL A 408      -3.685  20.561  34.460  1.00 36.78           C  
ANISOU 2626  CB  VAL A 408     5281   4391   4305    408   -121    242       C  
ATOM   2627  CG1 VAL A 408      -2.931  19.767  33.426  1.00 35.30           C  
ANISOU 2627  CG1 VAL A 408     5107   4206   4100    340   -143    242       C  
ATOM   2628  CG2 VAL A 408      -2.779  21.650  35.010  1.00 35.69           C  
ANISOU 2628  CG2 VAL A 408     5243   4144   4174    395    -53    229       C  
ATOM   2629  N   LEU A 409      -6.472  19.239  33.815  1.00 42.44           N  
ANISOU 2629  N   LEU A 409     5768   5340   5018    502   -252    261       N  
ATOM   2630  CA  LEU A 409      -7.279  18.163  33.203  1.00 42.10           C  
ANISOU 2630  CA  LEU A 409     5619   5402   4973    480   -322    251       C  
ATOM   2631  C   LEU A 409      -8.323  18.682  32.254  1.00 43.29           C  
ANISOU 2631  C   LEU A 409     5747   5615   5086    589   -385    279       C  
ATOM   2632  O   LEU A 409      -8.490  18.167  31.150  1.00 45.93           O  
ANISOU 2632  O   LEU A 409     6071   5997   5383    580   -451    278       O  
ATOM   2633  CB  LEU A 409      -7.955  17.296  34.264  1.00 40.80           C  
ANISOU 2633  CB  LEU A 409     5331   5307   4863    433   -314    223       C  
ATOM   2634  CG  LEU A 409      -6.960  16.349  34.919  1.00 41.89           C  
ANISOU 2634  CG  LEU A 409     5484   5406   5026    318   -278    197       C  
ATOM   2635  CD1 LEU A 409      -7.505  15.935  36.269  1.00 43.69           C  
ANISOU 2635  CD1 LEU A 409     5634   5670   5297    296   -238    182       C  
ATOM   2636  CD2 LEU A 409      -6.649  15.127  34.043  1.00 39.79           C  
ANISOU 2636  CD2 LEU A 409     5203   5164   4752    235   -320    180       C  
ATOM   2637  N   HIS A 410      -9.035  19.713  32.679  1.00 45.55           N  
ANISOU 2637  N   HIS A 410     6030   5903   5376    702   -368    301       N  
ATOM   2638  CA  HIS A 410     -10.130  20.239  31.863  1.00 46.26           C  
ANISOU 2638  CA  HIS A 410     6084   6065   5429    829   -434    330       C  
ATOM   2639  C   HIS A 410      -9.577  20.845  30.579  1.00 46.35           C  
ANISOU 2639  C   HIS A 410     6233   6015   5363    879   -457    369       C  
ATOM   2640  O   HIS A 410     -10.130  20.678  29.492  1.00 48.00           O  
ANISOU 2640  O   HIS A 410     6422   6296   5521    929   -540    383       O  
ATOM   2641  CB  HIS A 410     -10.947  21.228  32.696  1.00 45.09           C  
ANISOU 2641  CB  HIS A 410     5907   5921   5305    948   -396    345       C  
ATOM   2642  CG  HIS A 410     -11.770  22.172  31.879  1.00 51.39           C  
ANISOU 2642  CG  HIS A 410     6723   6748   6054   1113   -445    390       C  
ATOM   2643  ND1 HIS A 410     -13.052  21.931  31.565  1.00 50.81           N  
ANISOU 2643  ND1 HIS A 410     6507   6815   5986   1189   -522    387       N  
ATOM   2644  CD2 HIS A 410     -11.449  23.391  31.307  1.00 52.55           C  
ANISOU 2644  CD2 HIS A 410     7025   6797   6144   1222   -426    440       C  
ATOM   2645  CE1 HIS A 410     -13.529  22.939  30.832  1.00 55.53           C  
ANISOU 2645  CE1 HIS A 410     7161   7410   6527   1351   -558    436       C  
ATOM   2646  NE2 HIS A 410     -12.548  23.837  30.674  1.00 56.34           N  
ANISOU 2646  NE2 HIS A 410     7456   7360   6590   1372   -495    472       N  
ATOM   2647  N   SER A 411      -8.444  21.515  30.684  1.00 45.05           N  
ANISOU 2647  N   SER A 411     6212   5719   5187    856   -383    385       N  
ATOM   2648  CA  SER A 411      -7.941  22.264  29.547  1.00 46.15           C  
ANISOU 2648  CA  SER A 411     6498   5783   5252    911   -381    430       C  
ATOM   2649  C   SER A 411      -7.347  21.347  28.496  1.00 42.94           C  
ANISOU 2649  C   SER A 411     6113   5398   4805    826   -421    420       C  
ATOM   2650  O   SER A 411      -7.516  21.606  27.334  1.00 43.33           O  
ANISOU 2650  O   SER A 411     6229   5458   4778    893   -465    454       O  
ATOM   2651  CB  SER A 411      -6.927  23.318  29.988  1.00 42.98           C  
ANISOU 2651  CB  SER A 411     6242   5229   4858    902   -278    445       C  
ATOM   2652  OG  SER A 411      -7.550  24.276  30.837  1.00 43.79           O  
ANISOU 2652  OG  SER A 411     6350   5305   4986    999   -242    456       O  
ATOM   2653  N   PHE A 412      -6.660  20.285  28.912  1.00 42.70           N  
ANISOU 2653  N   PHE A 412     6034   5372   4819    689   -403    373       N  
ATOM   2654  CA  PHE A 412      -6.151  19.281  27.979  1.00 43.27           C  
ANISOU 2654  CA  PHE A 412     6116   5469   4858    608   -438    355       C  
ATOM   2655  C   PHE A 412      -7.288  18.521  27.266  1.00 45.43           C  
ANISOU 2655  C   PHE A 412     6289   5874   5100    635   -547    339       C  
ATOM   2656  O   PHE A 412      -7.239  18.317  26.059  1.00 46.21           O  
ANISOU 2656  O   PHE A 412     6441   5993   5124    649   -596    348       O  
ATOM   2657  CB  PHE A 412      -5.214  18.316  28.708  1.00 41.10           C  
ANISOU 2657  CB  PHE A 412     5806   5166   4643    471   -392    309       C  
ATOM   2658  CG  PHE A 412      -3.799  18.787  28.752  1.00 39.75           C  
ANISOU 2658  CG  PHE A 412     5748   4881   4475    422   -307    315       C  
ATOM   2659  CD1 PHE A 412      -3.460  19.938  29.452  1.00 40.75           C  
ANISOU 2659  CD1 PHE A 412     5936   4923   4623    453   -241    331       C  
ATOM   2660  CD2 PHE A 412      -2.808  18.105  28.058  1.00 41.58           C  
ANISOU 2660  CD2 PHE A 412     6023   5087   4687    344   -291    300       C  
ATOM   2661  CE1 PHE A 412      -2.154  20.397  29.469  1.00 41.55           C  
ANISOU 2661  CE1 PHE A 412     6131   4923   4732    395   -163    329       C  
ATOM   2662  CE2 PHE A 412      -1.486  18.534  28.085  1.00 42.87           C  
ANISOU 2662  CE2 PHE A 412     6272   5154   4861    293   -209    301       C  
ATOM   2663  CZ  PHE A 412      -1.158  19.693  28.783  1.00 45.41           C  
ANISOU 2663  CZ  PHE A 412     6647   5398   5209    314   -146    314       C  
ATOM   2664  N   GLN A 413      -8.315  18.142  28.020  1.00 48.25           N  
ANISOU 2664  N   GLN A 413     6501   6320   5511    641   -581    314       N  
ATOM   2665  CA  GLN A 413      -9.488  17.461  27.474  1.00 52.65           C  
ANISOU 2665  CA  GLN A 413     6937   7013   6054    657   -684    289       C  
ATOM   2666  C   GLN A 413     -10.138  18.305  26.419  1.00 53.16           C  
ANISOU 2666  C   GLN A 413     7046   7119   6035    799   -755    331       C  
ATOM   2667  O   GLN A 413     -10.326  17.849  25.298  1.00 54.71           O  
ANISOU 2667  O   GLN A 413     7252   7374   6163    800   -835    321       O  
ATOM   2668  CB  GLN A 413     -10.477  17.055  28.581  1.00 53.53           C  
ANISOU 2668  CB  GLN A 413     6883   7207   6249    640   -686    259       C  
ATOM   2669  CG  GLN A 413      -9.958  15.846  29.379  1.00 57.35           C  
ANISOU 2669  CG  GLN A 413     7320   7672   6799    488   -639    213       C  
ATOM   2670  CD  GLN A 413     -10.664  15.586  30.724  1.00 61.55           C  
ANISOU 2670  CD  GLN A 413     7726   8247   7413    465   -600    193       C  
ATOM   2671  OE1 GLN A 413     -10.209  14.754  31.510  1.00 58.61           O  
ANISOU 2671  OE1 GLN A 413     7336   7845   7088    360   -549    168       O  
ATOM   2672  NE2 GLN A 413     -11.783  16.283  30.982  1.00 67.45           N  
ANISOU 2672  NE2 GLN A 413     8388   9068   8174    570   -620    207       N  
ATOM   2673  N   LEU A 414     -10.416  19.561  26.755  1.00 58.13           N  
ANISOU 2673  N   LEU A 414     7719   7709   6660    925   -723    380       N  
ATOM   2674  CA  LEU A 414     -11.031  20.499  25.812  1.00 55.96           C  
ANISOU 2674  CA  LEU A 414     7503   7460   6299   1087   -784    433       C  
ATOM   2675  C   LEU A 414     -10.192  20.647  24.535  1.00 53.36           C  
ANISOU 2675  C   LEU A 414     7343   7065   5866   1089   -789    465       C  
ATOM   2676  O   LEU A 414     -10.712  20.679  23.438  1.00 54.94           O  
ANISOU 2676  O   LEU A 414     7561   7335   5977   1169   -881    482       O  
ATOM   2677  CB  LEU A 414     -11.203  21.852  26.497  1.00 61.29           C  
ANISOU 2677  CB  LEU A 414     8236   8060   6992   1210   -717    482       C  
ATOM   2678  CG  LEU A 414     -12.061  22.925  25.825  1.00 68.95           C  
ANISOU 2678  CG  LEU A 414     9247   9059   7890   1411   -772    542       C  
ATOM   2679  CD1 LEU A 414     -13.546  22.698  26.102  1.00 68.53           C  
ANISOU 2679  CD1 LEU A 414     8993   9173   7874   1493   -860    519       C  
ATOM   2680  CD2 LEU A 414     -11.611  24.295  26.313  1.00 69.78           C  
ANISOU 2680  CD2 LEU A 414     9503   9013   7997   1497   -666    596       C  
ATOM   2681  N   ALA A 415      -8.879  20.724  24.689  1.00 51.87           N  
ANISOU 2681  N   ALA A 415     7274   6745   5688   1000   -689    470       N  
ATOM   2682  CA  ALA A 415      -7.984  20.892  23.561  1.00 51.60           C  
ANISOU 2682  CA  ALA A 415     7404   6638   5564    992   -667    500       C  
ATOM   2683  C   ALA A 415      -7.756  19.588  22.752  1.00 52.79           C  
ANISOU 2683  C   ALA A 415     7524   6854   5678    891   -726    451       C  
ATOM   2684  O   ALA A 415      -7.093  19.637  21.716  1.00 51.94           O  
ANISOU 2684  O   ALA A 415     7550   6701   5485    889   -712    473       O  
ATOM   2685  CB  ALA A 415      -6.663  21.447  24.065  1.00 47.00           C  
ANISOU 2685  CB  ALA A 415     6941   5900   5019    925   -532    515       C  
ATOM   2686  N   LYS A 416      -8.303  18.451  23.222  1.00 50.91           N  
ANISOU 2686  N   LYS A 416     7124   6716   5502    808   -781    386       N  
ATOM   2687  CA  LYS A 416      -8.123  17.114  22.590  1.00 51.75           C  
ANISOU 2687  CA  LYS A 416     7199   6877   5588    699   -830    327       C  
ATOM   2688  C   LYS A 416      -6.627  16.714  22.558  1.00 48.62           C  
ANISOU 2688  C   LYS A 416     6905   6367   5202    589   -730    317       C  
ATOM   2689  O   LYS A 416      -6.063  16.311  21.538  1.00 47.43           O  
ANISOU 2689  O   LYS A 416     6845   6200   4977    559   -734    310       O  
ATOM   2690  CB  LYS A 416      -8.745  17.025  21.188  1.00 55.10           C  
ANISOU 2690  CB  LYS A 416     7656   7388   5891    771   -944    330       C  
ATOM   2691  CG  LYS A 416     -10.058  17.785  20.964  1.00 66.91           C  
ANISOU 2691  CG  LYS A 416     9091   8985   7347    926  -1042    361       C  
ATOM   2692  CD  LYS A 416     -11.345  17.012  21.271  1.00 70.04           C  
ANISOU 2692  CD  LYS A 416     9276   9539   7795    905  -1149    298       C  
ATOM   2693  CE  LYS A 416     -11.445  16.622  22.747  1.00 74.72           C  
ANISOU 2693  CE  LYS A 416     9737  10122   8530    816  -1080    266       C  
ATOM   2694  NZ  LYS A 416     -12.701  17.029  23.453  1.00 74.09           N  
ANISOU 2694  NZ  LYS A 416     9499  10141   8509    900  -1120    267       N  
ATOM   2695  N   VAL A 417      -5.989  16.880  23.698  1.00 44.93           N  
ANISOU 2695  N   VAL A 417     6423   5824   4825    536   -638    317       N  
ATOM   2696  CA  VAL A 417      -4.610  16.545  23.872  1.00 43.51           C  
ANISOU 2696  CA  VAL A 417     6309   5549   4672    438   -545    304       C  
ATOM   2697  C   VAL A 417      -4.617  15.537  25.009  1.00 43.47           C  
ANISOU 2697  C   VAL A 417     6179   5569   4767    340   -536    252       C  
ATOM   2698  O   VAL A 417      -5.136  15.812  26.095  1.00 41.72           O  
ANISOU 2698  O   VAL A 417     5878   5365   4611    356   -528    253       O  
ATOM   2699  CB  VAL A 417      -3.775  17.796  24.227  1.00 43.22           C  
ANISOU 2699  CB  VAL A 417     6378   5396   4647    469   -445    351       C  
ATOM   2700  CG1 VAL A 417      -2.314  17.431  24.468  1.00 41.60           C  
ANISOU 2700  CG1 VAL A 417     6216   5108   4483    362   -351    330       C  
ATOM   2701  CG2 VAL A 417      -3.900  18.848  23.129  1.00 46.61           C  
ANISOU 2701  CG2 VAL A 417     6944   5792   4974    578   -448    413       C  
ATOM   2702  N   THR A 418      -4.048  14.369  24.731  1.00 43.09           N  
ANISOU 2702  N   THR A 418     6128   5521   4724    245   -532    209       N  
ATOM   2703  CA  THR A 418      -3.940  13.274  25.663  1.00 41.53           C  
ANISOU 2703  CA  THR A 418     5837   5333   4607    151   -517    164       C  
ATOM   2704  C   THR A 418      -3.291  13.705  26.961  1.00 42.39           C  
ANISOU 2704  C   THR A 418     5935   5380   4791    134   -438    176       C  
ATOM   2705  O   THR A 418      -2.269  14.392  26.977  1.00 45.22           O  
ANISOU 2705  O   THR A 418     6376   5660   5147    138   -371    197       O  
ATOM   2706  CB  THR A 418      -3.081  12.126  25.086  1.00 42.45           C  
ANISOU 2706  CB  THR A 418     5995   5423   4710     67   -498    125       C  
ATOM   2707  OG1 THR A 418      -3.283  12.007  23.674  1.00 43.61           O  
ANISOU 2707  OG1 THR A 418     6209   5601   4762     91   -550    120       O  
ATOM   2708  CG2 THR A 418      -3.422  10.795  25.757  1.00 42.65           C  
ANISOU 2708  CG2 THR A 418     5925   5481   4799    -18   -515     76       C  
ATOM   2709  N   ILE A 419      -3.903  13.286  28.058  1.00 41.29           N  
ANISOU 2709  N   ILE A 419     5693   5278   4716    110   -446    158       N  
ATOM   2710  CA  ILE A 419      -3.376  13.510  29.393  1.00 40.23           C  
ANISOU 2710  CA  ILE A 419     5541   5098   4647     89   -382    161       C  
ATOM   2711  C   ILE A 419      -4.011  12.433  30.242  1.00 41.02           C  
ANISOU 2711  C   ILE A 419     5538   5248   4800     34   -396    131       C  
ATOM   2712  O   ILE A 419      -5.114  11.946  29.916  1.00 39.60           O  
ANISOU 2712  O   ILE A 419     5287   5144   4616     31   -454    115       O  
ATOM   2713  CB  ILE A 419      -3.761  14.896  29.957  1.00 39.24           C  
ANISOU 2713  CB  ILE A 419     5427   4956   4526    172   -362    195       C  
ATOM   2714  CG1 ILE A 419      -2.931  15.192  31.216  1.00 38.48           C  
ANISOU 2714  CG1 ILE A 419     5341   4799   4482    142   -293    189       C  
ATOM   2715  CG2 ILE A 419      -5.277  14.973  30.216  1.00 38.93           C  
ANISOU 2715  CG2 ILE A 419     5289   5006   4497    227   -416    197       C  
ATOM   2716  CD1 ILE A 419      -2.777  16.664  31.547  1.00 38.06           C  
ANISOU 2716  CD1 ILE A 419     5351   4688   4423    206   -252    215       C  
ATOM   2717  N   VAL A 420      -3.346  12.072  31.338  1.00 38.59           N  
ANISOU 2717  N   VAL A 420     5222   4901   4540    -11   -344    123       N  
ATOM   2718  CA  VAL A 420      -3.950  11.129  32.262  1.00 36.69           C  
ANISOU 2718  CA  VAL A 420     4900   4696   4346    -58   -342    104       C  
ATOM   2719  C   VAL A 420      -3.938  11.637  33.699  1.00 35.19           C  
ANISOU 2719  C   VAL A 420     4688   4491   4191    -38   -296    117       C  
ATOM   2720  O   VAL A 420      -2.909  12.150  34.191  1.00 34.54           O  
ANISOU 2720  O   VAL A 420     4661   4351   4112    -31   -256    123       O  
ATOM   2721  CB  VAL A 420      -3.298   9.744  32.100  1.00 37.89           C  
ANISOU 2721  CB  VAL A 420     5068   4822   4509   -138   -332     77       C  
ATOM   2722  CG1 VAL A 420      -1.833   9.770  32.543  1.00 34.98           C  
ANISOU 2722  CG1 VAL A 420     4760   4381   4149   -149   -280     81       C  
ATOM   2723  CG2 VAL A 420      -4.142   8.679  32.807  1.00 36.83           C  
ANISOU 2723  CG2 VAL A 420     4857   4722   4415   -194   -332     59       C  
ATOM   2724  N   ASP A 421      -5.082  11.542  34.368  1.00 34.90           N  
ANISOU 2724  N   ASP A 421     4569   4510   4180    -28   -299    116       N  
ATOM   2725  CA  ASP A 421      -5.153  11.962  35.763  1.00 37.08           C  
ANISOU 2725  CA  ASP A 421     4830   4776   4481     -8   -251    125       C  
ATOM   2726  C   ASP A 421      -4.489  10.930  36.663  1.00 39.98           C  
ANISOU 2726  C   ASP A 421     5209   5112   4870    -73   -213    116       C  
ATOM   2727  O   ASP A 421      -4.332   9.759  36.297  1.00 37.21           O  
ANISOU 2727  O   ASP A 421     4855   4757   4526   -135   -222    103       O  
ATOM   2728  CB  ASP A 421      -6.584  12.245  36.248  1.00 39.96           C  
ANISOU 2728  CB  ASP A 421     5104   5213   4867     31   -251    130       C  
ATOM   2729  CG  ASP A 421      -7.431  10.985  36.380  1.00 42.22           C  
ANISOU 2729  CG  ASP A 421     5301   5554   5185    -40   -256    111       C  
ATOM   2730  OD1 ASP A 421      -7.204  10.160  37.298  1.00 42.49           O  
ANISOU 2730  OD1 ASP A 421     5337   5566   5242    -97   -210    108       O  
ATOM   2731  OD2 ASP A 421      -8.344  10.824  35.548  1.00 46.44           O  
ANISOU 2731  OD2 ASP A 421     5767   6155   5721    -39   -308     98       O  
ATOM   2732  N   HIS A 422      -4.117  11.385  37.851  1.00 41.23           N  
ANISOU 2732  N   HIS A 422     5388   5246   5032    -52   -172    123       N  
ATOM   2733  CA  HIS A 422      -3.401  10.562  38.792  1.00 40.26           C  
ANISOU 2733  CA  HIS A 422     5289   5094   4916    -92   -141    120       C  
ATOM   2734  C   HIS A 422      -4.197   9.399  39.312  1.00 40.07           C  
ANISOU 2734  C   HIS A 422     5216   5096   4911   -139   -120    122       C  
ATOM   2735  O   HIS A 422      -3.599   8.406  39.695  1.00 43.85           O  
ANISOU 2735  O   HIS A 422     5725   5543   5392   -179   -102    124       O  
ATOM   2736  CB  HIS A 422      -2.834  11.409  39.918  1.00 39.51           C  
ANISOU 2736  CB  HIS A 422     5232   4972   4807    -55   -111    120       C  
ATOM   2737  CG  HIS A 422      -3.863  12.255  40.624  1.00 43.30           C  
ANISOU 2737  CG  HIS A 422     5681   5483   5286     -4    -87    127       C  
ATOM   2738  ND1 HIS A 422      -4.387  13.389  40.075  1.00 43.84           N  
ANISOU 2738  ND1 HIS A 422     5745   5560   5351     53    -99    130       N  
ATOM   2739  CD2 HIS A 422      -4.463  12.101  41.871  1.00 43.15           C  
ANISOU 2739  CD2 HIS A 422     5641   5486   5266      5    -44    132       C  
ATOM   2740  CE1 HIS A 422      -5.275  13.923  40.933  1.00 47.57           C  
ANISOU 2740  CE1 HIS A 422     6187   6060   5826     99    -65    134       C  
ATOM   2741  NE2 HIS A 422      -5.319  13.138  42.036  1.00 49.24           N  
ANISOU 2741  NE2 HIS A 422     6388   6282   6038     66    -29    133       N  
ATOM   2742  N   HIS A 423      -5.527   9.467  39.330  1.00 38.22           N  
ANISOU 2742  N   HIS A 423     4907   4920   4696   -136   -117    123       N  
ATOM   2743  CA  HIS A 423      -6.299   8.254  39.671  1.00 38.63           C  
ANISOU 2743  CA  HIS A 423     4908   4994   4775   -203    -90    120       C  
ATOM   2744  C   HIS A 423      -6.229   7.201  38.592  1.00 40.70           C  
ANISOU 2744  C   HIS A 423     5169   5247   5047   -271   -124    100       C  
ATOM   2745  O   HIS A 423      -5.868   6.052  38.858  1.00 43.68           O  
ANISOU 2745  O   HIS A 423     5582   5583   5434   -329    -96    100       O  
ATOM   2746  CB  HIS A 423      -7.729   8.583  39.991  1.00 36.98           C  
ANISOU 2746  CB  HIS A 423     4601   4857   4591   -188    -71    120       C  
ATOM   2747  CG  HIS A 423      -7.858   9.624  41.053  1.00 39.69           C  
ANISOU 2747  CG  HIS A 423     4952   5206   4921   -116    -30    135       C  
ATOM   2748  ND1 HIS A 423      -7.582   9.371  42.354  1.00 38.51           N  
ANISOU 2748  ND1 HIS A 423     4844   5030   4760   -120     32    149       N  
ATOM   2749  CD2 HIS A 423      -8.188  10.984  40.972  1.00 37.93           C  
ANISOU 2749  CD2 HIS A 423     4717   5007   4689    -28    -42    138       C  
ATOM   2750  CE1 HIS A 423      -7.755  10.500  43.073  1.00 36.70           C  
ANISOU 2750  CE1 HIS A 423     4623   4810   4512    -46     57    153       C  
ATOM   2751  NE2 HIS A 423      -8.120  11.488  42.227  1.00 38.51           N  
ANISOU 2751  NE2 HIS A 423     4821   5065   4747     10     15    146       N  
ATOM   2752  N   ALA A 424      -6.549   7.581  37.359  1.00 39.83           N  
ANISOU 2752  N   ALA A 424     5033   5172   4930   -259   -183     84       N  
ATOM   2753  CA  ALA A 424      -6.507   6.630  36.261  1.00 37.76           C  
ANISOU 2753  CA  ALA A 424     4777   4904   4667   -322   -220     56       C  
ATOM   2754  C   ALA A 424      -5.105   6.062  36.105  1.00 37.19           C  
ANISOU 2754  C   ALA A 424     4803   4751   4577   -338   -207     57       C  
ATOM   2755  O   ALA A 424      -4.954   4.856  35.935  1.00 39.50           O  
ANISOU 2755  O   ALA A 424     5120   5009   4880   -404   -195     41       O  
ATOM   2756  CB  ALA A 424      -6.972   7.274  34.970  1.00 34.38           C  
ANISOU 2756  CB  ALA A 424     4319   4528   4214   -289   -292     41       C  
ATOM   2757  N   ALA A 425      -4.088   6.923  36.170  1.00 34.30           N  
ANISOU 2757  N   ALA A 425     4492   4353   4186   -280   -206     74       N  
ATOM   2758  CA  ALA A 425      -2.694   6.473  36.030  1.00 32.51           C  
ANISOU 2758  CA  ALA A 425     4343   4062   3948   -286   -193     72       C  
ATOM   2759  C   ALA A 425      -2.308   5.402  37.066  1.00 36.82           C  
ANISOU 2759  C   ALA A 425     4913   4566   4510   -315   -148     82       C  
ATOM   2760  O   ALA A 425      -1.727   4.347  36.702  1.00 41.40           O  
ANISOU 2760  O   ALA A 425     5537   5101   5091   -348   -140     71       O  
ATOM   2761  CB  ALA A 425      -1.747   7.641  36.142  1.00 29.17           C  
ANISOU 2761  CB  ALA A 425     3956   3620   3507   -228   -190     84       C  
ATOM   2762  N   THR A 426      -2.600   5.664  38.349  1.00 34.41           N  
ANISOU 2762  N   THR A 426     4592   4272   4210   -296   -115    103       N  
ATOM   2763  CA  THR A 426      -2.245   4.696  39.387  1.00 34.48           C  
ANISOU 2763  CA  THR A 426     4639   4242   4222   -311    -71    121       C  
ATOM   2764  C   THR A 426      -3.057   3.397  39.260  1.00 37.85           C  
ANISOU 2764  C   THR A 426     5057   4653   4672   -386    -45    115       C  
ATOM   2765  O   THR A 426      -2.461   2.334  39.406  1.00 37.97           O  
ANISOU 2765  O   THR A 426     5133   4608   4686   -405    -21    122       O  
ATOM   2766  CB  THR A 426      -2.304   5.287  40.810  1.00 32.80           C  
ANISOU 2766  CB  THR A 426     4427   4043   3994   -268    -41    144       C  
ATOM   2767  OG1 THR A 426      -3.583   5.857  41.035  1.00 31.52           O  
ANISOU 2767  OG1 THR A 426     4200   3933   3845   -270    -28    145       O  
ATOM   2768  CG2 THR A 426      -1.243   6.362  41.006  1.00 30.10           C  
ANISOU 2768  CG2 THR A 426     4111   3698   3629   -209    -64    139       C  
ATOM   2769  N   VAL A 427      -4.372   3.459  38.949  1.00 37.42           N  
ANISOU 2769  N   VAL A 427     4928   4650   4642   -428    -50    100       N  
ATOM   2770  CA  VAL A 427      -5.134   2.231  38.702  1.00 39.54           C  
ANISOU 2770  CA  VAL A 427     5181   4903   4939   -518    -26     82       C  
ATOM   2771  C   VAL A 427      -4.378   1.420  37.633  1.00 44.14           C  
ANISOU 2771  C   VAL A 427     5827   5430   5513   -548    -52     56       C  
ATOM   2772  O   VAL A 427      -4.172   0.189  37.758  1.00 41.99           O  
ANISOU 2772  O   VAL A 427     5613   5089   5251   -597    -13     54       O  
ATOM   2773  CB  VAL A 427      -6.596   2.450  38.198  1.00 43.31           C  
ANISOU 2773  CB  VAL A 427     5548   5461   5447   -565    -49     53       C  
ATOM   2774  CG1 VAL A 427      -7.091   1.215  37.441  1.00 39.97           C  
ANISOU 2774  CG1 VAL A 427     5118   5018   5050   -670    -52     12       C  
ATOM   2775  CG2 VAL A 427      -7.605   2.780  39.320  1.00 37.92           C  
ANISOU 2775  CG2 VAL A 427     4794   4827   4788   -564      5     73       C  
ATOM   2776  N   SER A 428      -3.936   2.102  36.582  1.00 43.56           N  
ANISOU 2776  N   SER A 428     5754   5378   5418   -512   -109     37       N  
ATOM   2777  CA  SER A 428      -3.307   1.364  35.495  1.00 42.79           C  
ANISOU 2777  CA  SER A 428     5716   5235   5308   -539   -128      7       C  
ATOM   2778  C   SER A 428      -1.907   0.817  35.914  1.00 41.59           C  
ANISOU 2778  C   SER A 428     5653   5004   5145   -502    -92     28       C  
ATOM   2779  O   SER A 428      -1.436  -0.205  35.395  1.00 43.87           O  
ANISOU 2779  O   SER A 428     6004   5232   5433   -529    -78      9       O  
ATOM   2780  CB  SER A 428      -3.282   2.195  34.205  1.00 41.17           C  
ANISOU 2780  CB  SER A 428     5495   5075   5072   -513   -191    -16       C  
ATOM   2781  OG  SER A 428      -2.054   2.899  34.080  1.00 47.56           O  
ANISOU 2781  OG  SER A 428     6352   5862   5856   -444   -192      2       O  
ATOM   2782  N   PHE A 429      -1.269   1.439  36.895  1.00 38.49           N  
ANISOU 2782  N   PHE A 429     5266   4614   4745   -437    -77     64       N  
ATOM   2783  CA  PHE A 429       0.032   0.935  37.312  1.00 38.61           C  
ANISOU 2783  CA  PHE A 429     5348   4571   4750   -393    -54     80       C  
ATOM   2784  C   PHE A 429      -0.144  -0.347  38.118  1.00 40.57           C  
ANISOU 2784  C   PHE A 429     5647   4758   5008   -420     -2    101       C  
ATOM   2785  O   PHE A 429       0.714  -1.252  38.072  1.00 40.71           O  
ANISOU 2785  O   PHE A 429     5735   4711   5022   -401     19    106       O  
ATOM   2786  CB  PHE A 429       0.832   1.978  38.085  1.00 38.42           C  
ANISOU 2786  CB  PHE A 429     5313   4575   4711   -320    -63    102       C  
ATOM   2787  CG  PHE A 429       2.213   1.521  38.436  1.00 39.18           C  
ANISOU 2787  CG  PHE A 429     5457   4631   4798   -269    -54    112       C  
ATOM   2788  CD1 PHE A 429       3.208   1.462  37.446  1.00 33.92           C  
ANISOU 2788  CD1 PHE A 429     4808   3948   4132   -252    -65     89       C  
ATOM   2789  CD2 PHE A 429       2.527   1.127  39.743  1.00 33.66           C  
ANISOU 2789  CD2 PHE A 429     4787   3916   4087   -231    -32    145       C  
ATOM   2790  CE1 PHE A 429       4.470   1.007  37.742  1.00 32.85           C  
ANISOU 2790  CE1 PHE A 429     4701   3786   3995   -198    -56     96       C  
ATOM   2791  CE2 PHE A 429       3.812   0.690  40.041  1.00 34.77           C  
ANISOU 2791  CE2 PHE A 429     4963   4031   4217   -171    -34    154       C  
ATOM   2792  CZ  PHE A 429       4.784   0.625  39.040  1.00 33.53           C  
ANISOU 2792  CZ  PHE A 429     4807   3863   4070   -154    -46    127       C  
ATOM   2793  N   MET A 430      -1.275  -0.455  38.806  1.00 37.10           N  
ANISOU 2793  N   MET A 430     5176   4337   4583   -464     27    114       N  
ATOM   2794  CA  MET A 430      -1.540  -1.644  39.625  1.00 40.88           C  
ANISOU 2794  CA  MET A 430     5713   4751   5070   -498     91    140       C  
ATOM   2795  C   MET A 430      -1.739  -2.839  38.702  1.00 42.18           C  
ANISOU 2795  C   MET A 430     5922   4850   5255   -573    107    106       C  
ATOM   2796  O   MET A 430      -1.250  -3.959  38.957  1.00 41.57           O  
ANISOU 2796  O   MET A 430     5938   4681   5175   -572    153    122       O  
ATOM   2797  CB  MET A 430      -2.791  -1.476  40.516  1.00 38.18           C  
ANISOU 2797  CB  MET A 430     5321   4445   4741   -540    133    158       C  
ATOM   2798  CG  MET A 430      -2.676  -0.373  41.567  1.00 40.30           C  
ANISOU 2798  CG  MET A 430     5561   4768   4983   -467    130    189       C  
ATOM   2799  SD  MET A 430      -1.340  -0.659  42.755  1.00 42.29           S  
ANISOU 2799  SD  MET A 430     5913   4971   5186   -373    147    238       S  
ATOM   2800  CE  MET A 430      -1.894  -2.200  43.529  1.00 38.42           C  
ANISOU 2800  CE  MET A 430     5508   4393   4696   -426    241    278       C  
ATOM   2801  N   LYS A 431      -2.469  -2.581  37.625  1.00 41.62           N  
ANISOU 2801  N   LYS A 431     5791   4825   5200   -633     67     58       N  
ATOM   2802  CA  LYS A 431      -2.732  -3.575  36.611  1.00 41.75           C  
ANISOU 2802  CA  LYS A 431     5842   4792   5230   -713     68      9       C  
ATOM   2803  C   LYS A 431      -1.378  -3.991  35.995  1.00 39.47           C  
ANISOU 2803  C   LYS A 431     5642   4438   4916   -656     62      2       C  
ATOM   2804  O   LYS A 431      -1.072  -5.183  35.875  1.00 37.19           O  
ANISOU 2804  O   LYS A 431     5443   4055   4633   -681    105     -6       O  
ATOM   2805  CB  LYS A 431      -3.750  -3.020  35.614  1.00 43.38           C  
ANISOU 2805  CB  LYS A 431     5955   5084   5444   -771      7    -43       C  
ATOM   2806  CG  LYS A 431      -4.064  -3.921  34.428  1.00 51.30           C  
ANISOU 2806  CG  LYS A 431     6988   6053   6451   -859    -11   -109       C  
ATOM   2807  CD  LYS A 431      -4.691  -5.232  34.882  1.00 59.41           C  
ANISOU 2807  CD  LYS A 431     8053   7002   7516   -963     59   -121       C  
ATOM   2808  CE  LYS A 431      -4.980  -6.194  33.729  1.00 55.04           C  
ANISOU 2808  CE  LYS A 431     7542   6404   6967  -1062     44   -198       C  
ATOM   2809  NZ  LYS A 431      -5.236  -7.521  34.339  1.00 52.44           N  
ANISOU 2809  NZ  LYS A 431     7291   5961   6673  -1147    134   -196       N  
ATOM   2810  N   HIS A 432      -0.539  -3.012  35.681  1.00 37.83           N  
ANISOU 2810  N   HIS A 432     5413   4277   4685   -576     20      8       N  
ATOM   2811  CA  HIS A 432       0.832  -3.307  35.253  1.00 34.58           C  
ANISOU 2811  CA  HIS A 432     5068   3815   4254   -510     25      7       C  
ATOM   2812  C   HIS A 432       1.600  -4.172  36.231  1.00 35.36           C  
ANISOU 2812  C   HIS A 432     5241   3838   4355   -458     76     48       C  
ATOM   2813  O   HIS A 432       2.244  -5.166  35.832  1.00 35.96           O  
ANISOU 2813  O   HIS A 432     5399   3834   4430   -444    106     37       O  
ATOM   2814  CB  HIS A 432       1.572  -2.016  34.933  1.00 34.86           C  
ANISOU 2814  CB  HIS A 432     5057   3918   4272   -442    -17     10       C  
ATOM   2815  CG  HIS A 432       3.022  -2.221  34.599  1.00 34.53           C  
ANISOU 2815  CG  HIS A 432     5060   3839   4219   -373     -5      9       C  
ATOM   2816  ND1 HIS A 432       3.431  -2.819  33.437  1.00 37.48           N  
ANISOU 2816  ND1 HIS A 432     5486   4173   4582   -384      4    -30       N  
ATOM   2817  CD2 HIS A 432       4.167  -1.940  35.325  1.00 32.20           C  
ANISOU 2817  CD2 HIS A 432     4762   3549   3923   -290      2     38       C  
ATOM   2818  CE1 HIS A 432       4.779  -2.866  33.416  1.00 36.78           C  
ANISOU 2818  CE1 HIS A 432     5418   4066   4492   -307     22    -22       C  
ATOM   2819  NE2 HIS A 432       5.235  -2.318  34.572  1.00 32.93           N  
ANISOU 2819  NE2 HIS A 432     4889   3610   4012   -251     16     18       N  
ATOM   2820  N   LEU A 433       1.509  -3.854  37.524  1.00 36.33           N  
ANISOU 2820  N   LEU A 433     5346   3981   4475   -424     90     96       N  
ATOM   2821  CA  LEU A 433       2.131  -4.682  38.574  1.00 36.28           C  
ANISOU 2821  CA  LEU A 433     5420   3907   4459   -365    135    144       C  
ATOM   2822  C   LEU A 433       1.641  -6.131  38.583  1.00 39.64           C  
ANISOU 2822  C   LEU A 433     5939   4225   4898   -426    199    146       C  
ATOM   2823  O   LEU A 433       2.444  -7.076  38.724  1.00 39.24           O  
ANISOU 2823  O   LEU A 433     5983   4088   4838   -371    234    165       O  
ATOM   2824  CB  LEU A 433       1.936  -4.049  39.976  1.00 38.76           C  
ANISOU 2824  CB  LEU A 433     5704   4268   4754   -326    138    192       C  
ATOM   2825  CG  LEU A 433       2.813  -2.829  40.381  1.00 36.78           C  
ANISOU 2825  CG  LEU A 433     5397   4095   4482   -241     85    200       C  
ATOM   2826  CD1 LEU A 433       2.481  -2.333  41.782  1.00 35.01           C  
ANISOU 2826  CD1 LEU A 433     5162   3908   4231   -212     94    240       C  
ATOM   2827  CD2 LEU A 433       4.286  -3.206  40.376  1.00 36.68           C  
ANISOU 2827  CD2 LEU A 433     5424   4057   4456   -148     74    207       C  
ATOM   2828  N   ASP A 434       0.325  -6.309  38.427  1.00 40.66           N  
ANISOU 2828  N   ASP A 434     6040   4358   5052   -539    218    123       N  
ATOM   2829  CA  ASP A 434      -0.253  -7.639  38.260  1.00 41.82           C  
ANISOU 2829  CA  ASP A 434     6270   4401   5221   -627    282    109       C  
ATOM   2830  C   ASP A 434       0.254  -8.353  36.982  1.00 42.24           C  
ANISOU 2830  C   ASP A 434     6385   4389   5276   -643    275     53       C  
ATOM   2831  O   ASP A 434       0.641  -9.511  37.043  1.00 40.20           O  
ANISOU 2831  O   ASP A 434     6243   4013   5018   -636    332     62       O  
ATOM   2832  CB  ASP A 434      -1.780  -7.594  38.296  1.00 48.16           C  
ANISOU 2832  CB  ASP A 434     7002   5238   6056   -756    298     84       C  
ATOM   2833  CG  ASP A 434      -2.390  -8.984  38.153  1.00 62.88           C  
ANISOU 2833  CG  ASP A 434     8952   6989   7951   -867    372     61       C  
ATOM   2834  OD1 ASP A 434      -1.699  -9.960  38.514  1.00 69.56           O  
ANISOU 2834  OD1 ASP A 434     9928   7717   8784   -825    430     94       O  
ATOM   2835  OD2 ASP A 434      -3.549  -9.130  37.685  1.00 73.27           O  
ANISOU 2835  OD2 ASP A 434    10208   8330   9303   -996    373      9       O  
ATOM   2836  N   ASN A 435       0.273  -7.664  35.838  1.00 39.79           N  
ANISOU 2836  N   ASN A 435     6010   4149   4960   -657    211      0       N  
ATOM   2837  CA  ASN A 435       0.826  -8.255  34.632  1.00 43.04           C  
ANISOU 2837  CA  ASN A 435     6486   4505   5361   -660    207    -53       C  
ATOM   2838  C   ASN A 435       2.232  -8.797  34.860  1.00 43.15           C  
ANISOU 2838  C   ASN A 435     6590   4446   5361   -543    241    -20       C  
ATOM   2839  O   ASN A 435       2.560  -9.899  34.429  1.00 44.25           O  
ANISOU 2839  O   ASN A 435     6835   4478   5501   -548    286    -42       O  
ATOM   2840  CB  ASN A 435       0.881  -7.245  33.470  1.00 40.58           C  
ANISOU 2840  CB  ASN A 435     6099   4290   5028   -658    133    -99       C  
ATOM   2841  CG  ASN A 435      -0.491  -6.811  33.001  1.00 44.47           C  
ANISOU 2841  CG  ASN A 435     6508   4858   5530   -763     88   -141       C  
ATOM   2842  OD1 ASN A 435      -1.514  -7.401  33.385  1.00 45.73           O  
ANISOU 2842  OD1 ASN A 435     6661   4994   5719   -859    115   -152       O  
ATOM   2843  ND2 ASN A 435      -0.526  -5.772  32.157  1.00 40.67           N  
ANISOU 2843  ND2 ASN A 435     5960   4469   5022   -745     20   -165       N  
ATOM   2844  N   GLU A 436       3.056  -7.997  35.530  1.00 41.33           N  
ANISOU 2844  N   GLU A 436     6312   4276   5117   -436    217     27       N  
ATOM   2845  CA  GLU A 436       4.484  -8.252  35.613  1.00 38.66           C  
ANISOU 2845  CA  GLU A 436     6018   3905   4766   -313    229     49       C  
ATOM   2846  C   GLU A 436       4.836  -9.334  36.655  1.00 40.33           C  
ANISOU 2846  C   GLU A 436     6332   4016   4974   -252    287    104       C  
ATOM   2847  O   GLU A 436       5.813 -10.097  36.489  1.00 40.49           O  
ANISOU 2847  O   GLU A 436     6430   3965   4989   -167    317    110       O  
ATOM   2848  CB  GLU A 436       5.190  -6.933  35.874  1.00 39.86           C  
ANISOU 2848  CB  GLU A 436     6068   4169   4908   -238    175     66       C  
ATOM   2849  CG  GLU A 436       5.141  -6.011  34.646  1.00 42.90           C  
ANISOU 2849  CG  GLU A 436     6386   4625   5288   -275    132     15       C  
ATOM   2850  CD  GLU A 436       6.206  -6.372  33.607  1.00 42.51           C  
ANISOU 2850  CD  GLU A 436     6377   4543   5232   -225    150    -19       C  
ATOM   2851  OE1 GLU A 436       7.338  -5.866  33.718  1.00 46.99           O  
ANISOU 2851  OE1 GLU A 436     6904   5150   5799   -138    142     -7       O  
ATOM   2852  OE2 GLU A 436       5.936  -7.196  32.710  1.00 44.58           O  
ANISOU 2852  OE2 GLU A 436     6712   4739   5489   -274    175    -62       O  
ATOM   2853  N   GLN A 437       4.040  -9.396  37.718  1.00 37.33           N  
ANISOU 2853  N   GLN A 437     5958   3631   4595   -289    309    148       N  
ATOM   2854  CA  GLN A 437       4.139 -10.470  38.653  1.00 40.86           C  
ANISOU 2854  CA  GLN A 437     6522   3971   5032   -250    374    203       C  
ATOM   2855  C   GLN A 437       4.037 -11.758  37.833  1.00 43.12           C  
ANISOU 2855  C   GLN A 437     6927   4122   5335   -301    434    166       C  
ATOM   2856  O   GLN A 437       4.959 -12.585  37.855  1.00 40.17           O  
ANISOU 2856  O   GLN A 437     6653   3660   4950   -203    469    186       O  
ATOM   2857  CB  GLN A 437       3.048 -10.395  39.767  1.00 41.47           C  
ANISOU 2857  CB  GLN A 437     6596   4054   5107   -314    407    247       C  
ATOM   2858  CG  GLN A 437       3.367 -11.244  40.988  1.00 40.00           C  
ANISOU 2858  CG  GLN A 437     6531   3778   4890   -236    468    327       C  
ATOM   2859  CD  GLN A 437       4.743 -10.880  41.533  1.00 43.68           C  
ANISOU 2859  CD  GLN A 437     6988   4293   5317    -65    418    367       C  
ATOM   2860  OE1 GLN A 437       5.139  -9.699  41.532  1.00 40.91           O  
ANISOU 2860  OE1 GLN A 437     6518   4067   4960    -28    344    352       O  
ATOM   2861  NE2 GLN A 437       5.497 -11.881  41.962  1.00 40.50           N  
ANISOU 2861  NE2 GLN A 437     6707   3791   4889     41    457    415       N  
ATOM   2862  N   LYS A 438       2.954 -11.905  37.070  1.00 45.06           N  
ANISOU 2862  N   LYS A 438     7159   4357   5606   -448    442    105       N  
ATOM   2863  CA  LYS A 438       2.794 -13.109  36.232  1.00 47.89           C  
ANISOU 2863  CA  LYS A 438     7633   4584   5978   -515    496     54       C  
ATOM   2864  C   LYS A 438       3.947 -13.290  35.253  1.00 46.10           C  
ANISOU 2864  C   LYS A 438     7443   4336   5737   -426    482     18       C  
ATOM   2865  O   LYS A 438       4.550 -14.341  35.238  1.00 47.43           O  
ANISOU 2865  O   LYS A 438     7740   4381   5902   -367    541     27       O  
ATOM   2866  CB  LYS A 438       1.435 -13.157  35.545  1.00 51.41           C  
ANISOU 2866  CB  LYS A 438     8038   5043   6452   -695    490    -18       C  
ATOM   2867  CG  LYS A 438       0.302 -13.404  36.540  1.00 62.84           C  
ANISOU 2867  CG  LYS A 438     9483   6468   7924   -792    542     16       C  
ATOM   2868  CD  LYS A 438      -1.078 -13.482  35.890  1.00 72.97           C  
ANISOU 2868  CD  LYS A 438    10705   7776   9244   -976    534    -61       C  
ATOM   2869  CE  LYS A 438      -1.839 -12.171  36.053  1.00 76.79           C  
ANISOU 2869  CE  LYS A 438    11013   8427   9735  -1005    464    -62       C  
ATOM   2870  NZ  LYS A 438      -2.849 -11.954  34.978  1.00 86.88           N  
ANISOU 2870  NZ  LYS A 438    12201   9775  11033  -1138    410   -155       N  
ATOM   2871  N   ALA A 439       4.315 -12.240  34.523  1.00 45.80           N  
ANISOU 2871  N   ALA A 439     7297   4418   5689   -402    412    -16       N  
ATOM   2872  CA  ALA A 439       5.360 -12.313  33.456  1.00 45.59           C  
ANISOU 2872  CA  ALA A 439     7292   4382   5646   -330    406    -58       C  
ATOM   2873  C   ALA A 439       6.847 -12.467  33.867  1.00 46.00           C  
ANISOU 2873  C   ALA A 439     7367   4420   5690   -156    423    -12       C  
ATOM   2874  O   ALA A 439       7.591 -13.162  33.189  1.00 50.97           O  
ANISOU 2874  O   ALA A 439     8074   4977   6315    -99    461    -40       O  
ATOM   2875  CB  ALA A 439       5.210 -11.131  32.504  1.00 42.14           C  
ANISOU 2875  CB  ALA A 439     6742   4073   5198   -369    336   -106       C  
ATOM   2876  N   ARG A 440       7.283 -11.813  34.942  1.00 44.30           N  
ANISOU 2876  N   ARG A 440     7081   4280   5473    -72    392     53       N  
ATOM   2877  CA  ARG A 440       8.716 -11.766  35.303  1.00 44.83           C  
ANISOU 2877  CA  ARG A 440     7132   4370   5533     92    387     87       C  
ATOM   2878  C   ARG A 440       8.935 -12.000  36.778  1.00 43.25           C  
ANISOU 2878  C   ARG A 440     6957   4157   5319    180    389    168       C  
ATOM   2879  O   ARG A 440      10.080 -11.995  37.224  1.00 42.77           O  
ANISOU 2879  O   ARG A 440     6877   4125   5250    322    374    200       O  
ATOM   2880  CB  ARG A 440       9.348 -10.385  34.980  1.00 45.33           C  
ANISOU 2880  CB  ARG A 440     7046   4579   5597    123    323     69       C  
ATOM   2881  CG  ARG A 440       9.511 -10.086  33.500  1.00 47.42           C  
ANISOU 2881  CG  ARG A 440     7290   4866   5863     79    324     -1       C  
ATOM   2882  CD  ARG A 440      10.660  -9.124  33.226  1.00 48.60           C  
ANISOU 2882  CD  ARG A 440     7330   5119   6016    158    296     -9       C  
ATOM   2883  NE  ARG A 440      10.412  -7.761  33.688  1.00 46.00           N  
ANISOU 2883  NE  ARG A 440     6882   4906   5688    124    235      6       N  
ATOM   2884  CZ  ARG A 440      11.272  -6.752  33.578  1.00 45.35           C  
ANISOU 2884  CZ  ARG A 440     6697   4919   5616    167    209     -1       C  
ATOM   2885  NH1 ARG A 440      12.463  -6.917  32.999  1.00 44.22           N  
ANISOU 2885  NH1 ARG A 440     6537   4781   5484    246    240    -22       N  
ATOM   2886  NH2 ARG A 440      10.926  -5.556  34.035  1.00 43.80           N  
ANISOU 2886  NH2 ARG A 440     6412   4810   5419    128    160     11       N  
ATOM   2887  N   GLY A 441       7.852 -12.131  37.549  1.00 40.50           N  
ANISOU 2887  N   GLY A 441     6642   3780   4966     99    405    201       N  
ATOM   2888  CA  GLY A 441       7.970 -12.403  38.976  1.00 42.28           C  
ANISOU 2888  CA  GLY A 441     6913   3985   5164    179    416    282       C  
ATOM   2889  C   GLY A 441       8.213 -11.183  39.873  1.00 44.06           C  
ANISOU 2889  C   GLY A 441     7017   4353   5370    227    343    314       C  
ATOM   2890  O   GLY A 441       8.626 -11.328  41.036  1.00 43.76           O  
ANISOU 2890  O   GLY A 441     7012   4319   5297    329    336    378       O  
ATOM   2891  N   GLY A 442       7.929  -9.990  39.359  1.00 41.86           N  
ANISOU 2891  N   GLY A 442     6612   4186   5107    156    290    268       N  
ATOM   2892  CA  GLY A 442       8.089  -8.764  40.134  1.00 43.75           C  
ANISOU 2892  CA  GLY A 442     6741   4551   5330    185    226    286       C  
ATOM   2893  C   GLY A 442       8.174  -7.556  39.221  1.00 44.47           C  
ANISOU 2893  C   GLY A 442     6709   4743   5444    135    176    227       C  
ATOM   2894  O   GLY A 442       8.068  -7.677  37.982  1.00 44.36           O  
ANISOU 2894  O   GLY A 442     6697   4707   5451     79    190    177       O  
ATOM   2895  N   CYS A 443       8.369  -6.386  39.820  1.00 42.90           N  
ANISOU 2895  N   CYS A 443     6415   4650   5234    155    121    234       N  
ATOM   2896  CA  CYS A 443       8.509  -5.163  39.042  1.00 42.13           C  
ANISOU 2896  CA  CYS A 443     6211   4640   5155    115     81    186       C  
ATOM   2897  C   CYS A 443       9.208  -4.135  39.906  1.00 41.67           C  
ANISOU 2897  C   CYS A 443     6070   4678   5083    176     27    196       C  
ATOM   2898  O   CYS A 443       8.710  -3.811  40.975  1.00 43.35           O  
ANISOU 2898  O   CYS A 443     6283   4917   5271    175     12    227       O  
ATOM   2899  CB  CYS A 443       7.129  -4.664  38.609  1.00 39.91           C  
ANISOU 2899  CB  CYS A 443     5909   4372   4882     -8     82    165       C  
ATOM   2900  SG  CYS A 443       7.041  -3.021  37.871  1.00 43.30           S  
ANISOU 2900  SG  CYS A 443     6226   4903   5321    -53     34    124       S  
ATOM   2901  N   PRO A 444      10.371  -3.635  39.454  1.00 40.30           N  
ANISOU 2901  N   PRO A 444     5827   4558   4927    226      1    166       N  
ATOM   2902  CA  PRO A 444      11.103  -2.604  40.193  1.00 38.10           C  
ANISOU 2902  CA  PRO A 444     5459   4375   4642    270    -53    161       C  
ATOM   2903  C   PRO A 444      10.341  -1.282  40.216  1.00 36.26           C  
ANISOU 2903  C   PRO A 444     5172   4197   4410    186    -76    142       C  
ATOM   2904  O   PRO A 444       9.868  -0.798  39.183  1.00 36.51           O  
ANISOU 2904  O   PRO A 444     5186   4225   4460    113    -61    114       O  
ATOM   2905  CB  PRO A 444      12.418  -2.467  39.413  1.00 36.24           C  
ANISOU 2905  CB  PRO A 444     5159   4173   4439    317    -55    123       C  
ATOM   2906  CG  PRO A 444      12.100  -2.955  38.042  1.00 37.65           C  
ANISOU 2906  CG  PRO A 444     5382   4287   4636    265     -3     99       C  
ATOM   2907  CD  PRO A 444      11.087  -4.051  38.233  1.00 38.85           C  
ANISOU 2907  CD  PRO A 444     5645   4346   4769    242     30    131       C  
ATOM   2908  N   ALA A 445      10.184  -0.709  41.394  1.00 34.23           N  
ANISOU 2908  N   ALA A 445     4896   3985   4124    202   -110    159       N  
ATOM   2909  CA  ALA A 445       9.329   0.438  41.477  1.00 32.57           C  
ANISOU 2909  CA  ALA A 445     4653   3811   3912    131   -121    146       C  
ATOM   2910  C   ALA A 445       9.716   1.276  42.657  1.00 33.31           C  
ANISOU 2910  C   ALA A 445     4708   3972   3978    166   -168    143       C  
ATOM   2911  O   ALA A 445       9.943   0.756  43.769  1.00 31.92           O  
ANISOU 2911  O   ALA A 445     4567   3800   3761    232   -185    174       O  
ATOM   2912  CB  ALA A 445       7.871   0.031  41.581  1.00 31.80           C  
ANISOU 2912  CB  ALA A 445     4612   3668   3804     72    -86    173       C  
ATOM   2913  N   ASP A 446       9.754   2.587  42.398  1.00 34.59           N  
ANISOU 2913  N   ASP A 446     4808   4179   4155    122   -186    106       N  
ATOM   2914  CA  ASP A 446      10.268   3.560  43.342  1.00 36.65           C  
ANISOU 2914  CA  ASP A 446     5026   4504   4397    141   -233     83       C  
ATOM   2915  C   ASP A 446       9.044   4.276  43.914  1.00 35.78           C  
ANISOU 2915  C   ASP A 446     4941   4395   4261    100   -224     93       C  
ATOM   2916  O   ASP A 446       8.450   5.163  43.279  1.00 34.70           O  
ANISOU 2916  O   ASP A 446     4784   4254   4145     42   -208     75       O  
ATOM   2917  CB  ASP A 446      11.231   4.519  42.618  1.00 38.70           C  
ANISOU 2917  CB  ASP A 446     5206   4800   4698    114   -246     29       C  
ATOM   2918  CG  ASP A 446      11.941   5.480  43.567  1.00 40.15           C  
ANISOU 2918  CG  ASP A 446     5337   5050   4867    125   -298    -10       C  
ATOM   2919  OD1 ASP A 446      11.440   5.652  44.681  1.00 43.00           O  
ANISOU 2919  OD1 ASP A 446     5731   5426   5180    143   -321      4       O  
ATOM   2920  OD2 ASP A 446      13.000   6.057  43.200  1.00 44.16           O  
ANISOU 2920  OD2 ASP A 446     5771   5596   5412    111   -312    -57       O  
ATOM   2921  N   TRP A 447       8.675   3.849  45.109  1.00 34.16           N  
ANISOU 2921  N   TRP A 447     4783   4192   4005    139   -229    126       N  
ATOM   2922  CA  TRP A 447       7.452   4.278  45.777  1.00 36.97           C  
ANISOU 2922  CA  TRP A 447     5170   4545   4330    112   -206    144       C  
ATOM   2923  C   TRP A 447       7.268   5.808  45.850  1.00 36.06           C  
ANISOU 2923  C   TRP A 447     5014   4466   4219     77   -221    102       C  
ATOM   2924  O   TRP A 447       6.195   6.360  45.528  1.00 40.44           O  
ANISOU 2924  O   TRP A 447     5569   5008   4787     34   -190    104       O  
ATOM   2925  CB  TRP A 447       7.418   3.617  47.175  1.00 35.58           C  
ANISOU 2925  CB  TRP A 447     5058   4374   4087    175   -210    184       C  
ATOM   2926  CG  TRP A 447       6.065   3.685  47.857  1.00 37.65           C  
ANISOU 2926  CG  TRP A 447     5365   4622   4317    150   -161    215       C  
ATOM   2927  CD1 TRP A 447       5.067   2.718  47.855  1.00 38.34           C  
ANISOU 2927  CD1 TRP A 447     5504   4657   4406    125    -97    262       C  
ATOM   2928  CD2 TRP A 447       5.503   4.810  48.638  1.00 36.56           C  
ANISOU 2928  CD2 TRP A 447     5223   4522   4146    141   -162    196       C  
ATOM   2929  NE1 TRP A 447       3.962   3.147  48.562  1.00 39.75           N  
ANISOU 2929  NE1 TRP A 447     5698   4846   4558    103    -57    275       N  
ATOM   2930  CE2 TRP A 447       4.162   4.388  49.058  1.00 37.96           C  
ANISOU 2930  CE2 TRP A 447     5443   4673   4308    118    -92    238       C  
ATOM   2931  CE3 TRP A 447       5.953   6.082  48.994  1.00 39.13           C  
ANISOU 2931  CE3 TRP A 447     5516   4894   4457    145   -204    145       C  
ATOM   2932  CZ2 TRP A 447       3.333   5.210  49.814  1.00 38.32           C  
ANISOU 2932  CZ2 TRP A 447     5495   4743   4321    112    -66    233       C  
ATOM   2933  CZ3 TRP A 447       5.108   6.906  49.752  1.00 39.40           C  
ANISOU 2933  CZ3 TRP A 447     5571   4944   4456    138   -181    138       C  
ATOM   2934  CH2 TRP A 447       3.826   6.472  50.162  1.00 38.81           C  
ANISOU 2934  CH2 TRP A 447     5534   4848   4363    128   -112    183       C  
ATOM   2935  N   ALA A 448       8.315   6.503  46.257  1.00 35.07           N  
ANISOU 2935  N   ALA A 448     4855   4385   4086     97   -269     60       N  
ATOM   2936  CA  ALA A 448       8.281   7.955  46.455  1.00 35.36           C  
ANISOU 2936  CA  ALA A 448     4867   4445   4122     64   -282     13       C  
ATOM   2937  C   ALA A 448       8.026   8.700  45.151  1.00 35.90           C  
ANISOU 2937  C   ALA A 448     4907   4485   4247      5   -253     -5       C  
ATOM   2938  O   ALA A 448       7.510   9.826  45.168  1.00 40.56           O  
ANISOU 2938  O   ALA A 448     5503   5070   4839    -22   -241    -25       O  
ATOM   2939  CB  ALA A 448       9.590   8.419  47.082  1.00 31.58           C  
ANISOU 2939  CB  ALA A 448     4351   4019   3630     86   -343    -37       C  
ATOM   2940  N   TRP A 449       8.386   8.071  44.031  1.00 34.35           N  
ANISOU 2940  N   TRP A 449     4692   4268   4091     -6   -240      4       N  
ATOM   2941  CA  TRP A 449       8.092   8.602  42.702  1.00 33.70           C  
ANISOU 2941  CA  TRP A 449     4599   4157   4048    -54   -210     -4       C  
ATOM   2942  C   TRP A 449       6.850   8.058  42.088  1.00 33.67           C  
ANISOU 2942  C   TRP A 449     4623   4124   4047    -69   -180     33       C  
ATOM   2943  O   TRP A 449       6.281   8.710  41.222  1.00 36.82           O  
ANISOU 2943  O   TRP A 449     5021   4509   4461    -99   -164     30       O  
ATOM   2944  CB  TRP A 449       9.234   8.323  41.749  1.00 34.53           C  
ANISOU 2944  CB  TRP A 449     4669   4261   4190    -62   -208    -24       C  
ATOM   2945  CG  TRP A 449      10.430   9.206  41.965  1.00 37.48           C  
ANISOU 2945  CG  TRP A 449     4993   4666   4583    -75   -228    -75       C  
ATOM   2946  CD1 TRP A 449      11.277   9.225  43.055  1.00 34.18           C  
ANISOU 2946  CD1 TRP A 449     4541   4296   4148    -46   -274   -103       C  
ATOM   2947  CD2 TRP A 449      10.976  10.204  41.025  1.00 39.90           C  
ANISOU 2947  CD2 TRP A 449     5274   4959   4928   -128   -200   -109       C  
ATOM   2948  NE1 TRP A 449      12.268  10.155  42.884  1.00 38.76           N  
ANISOU 2948  NE1 TRP A 449     5067   4899   4762    -85   -281   -159       N  
ATOM   2949  CE2 TRP A 449      12.153  10.769  41.676  1.00 40.36           C  
ANISOU 2949  CE2 TRP A 449     5275   5060   5001   -139   -230   -163       C  
ATOM   2950  CE3 TRP A 449      10.607  10.667  39.747  1.00 42.75           C  
ANISOU 2950  CE3 TRP A 449     5659   5278   5306   -166   -155   -100       C  
ATOM   2951  CZ2 TRP A 449      12.914  11.772  41.081  1.00 43.01           C  
ANISOU 2951  CZ2 TRP A 449     5576   5389   5377   -199   -202   -208       C  
ATOM   2952  CZ3 TRP A 449      11.377  11.679  39.145  1.00 44.54           C  
ANISOU 2952  CZ3 TRP A 449     5866   5494   5565   -214   -125   -136       C  
ATOM   2953  CH2 TRP A 449      12.515  12.211  39.798  1.00 46.76           C  
ANISOU 2953  CH2 TRP A 449     6088   5809   5870   -236   -143   -190       C  
ATOM   2954  N   ILE A 450       6.424   6.853  42.473  1.00 33.11           N  
ANISOU 2954  N   ILE A 450     4578   4042   3960    -50   -172     67       N  
ATOM   2955  CA  ILE A 450       5.206   6.280  41.878  1.00 35.05           C  
ANISOU 2955  CA  ILE A 450     4842   4263   4215    -80   -143     93       C  
ATOM   2956  C   ILE A 450       3.969   6.927  42.488  1.00 35.59           C  
ANISOU 2956  C   ILE A 450     4909   4348   4268    -88   -129    104       C  
ATOM   2957  O   ILE A 450       3.029   7.232  41.778  1.00 36.02           O  
ANISOU 2957  O   ILE A 450     4947   4402   4337   -115   -118    106       O  
ATOM   2958  CB  ILE A 450       5.110   4.732  42.042  1.00 35.67           C  
ANISOU 2958  CB  ILE A 450     4956   4308   4287    -71   -125    123       C  
ATOM   2959  CG1 ILE A 450       6.265   4.011  41.318  1.00 33.67           C  
ANISOU 2959  CG1 ILE A 450     4708   4034   4052    -53   -130    112       C  
ATOM   2960  CG2 ILE A 450       3.716   4.217  41.648  1.00 32.18           C  
ANISOU 2960  CG2 ILE A 450     4524   3847   3855   -119    -94    141       C  
ATOM   2961  CD1 ILE A 450       6.212   4.077  39.812  1.00 36.45           C  
ANISOU 2961  CD1 ILE A 450     5050   4368   4431    -93   -120     92       C  
ATOM   2962  N   VAL A 451       3.978   7.134  43.809  1.00 38.87           N  
ANISOU 2962  N   VAL A 451     5339   4781   4649    -58   -131    110       N  
ATOM   2963  CA  VAL A 451       2.869   7.799  44.496  1.00 35.92           C  
ANISOU 2963  CA  VAL A 451     4967   4425   4257    -56   -108    117       C  
ATOM   2964  C   VAL A 451       2.744   9.270  44.082  1.00 35.93           C  
ANISOU 2964  C   VAL A 451     4947   4435   4271    -60   -116     87       C  
ATOM   2965  O   VAL A 451       3.729  10.000  44.085  1.00 35.44           O  
ANISOU 2965  O   VAL A 451     4885   4372   4208    -55   -140     56       O  
ATOM   2966  CB  VAL A 451       3.021   7.675  46.019  1.00 35.71           C  
ANISOU 2966  CB  VAL A 451     4977   4414   4178    -17   -105    127       C  
ATOM   2967  CG1 VAL A 451       2.182   8.704  46.762  1.00 33.99           C  
ANISOU 2967  CG1 VAL A 451     4762   4217   3936     -6    -83    119       C  
ATOM   2968  CG2 VAL A 451       2.619   6.279  46.448  1.00 36.52           C  
ANISOU 2968  CG2 VAL A 451     5114   4496   4264    -15    -72    172       C  
ATOM   2969  N   PRO A 452       1.535   9.703  43.694  1.00 38.11           N  
ANISOU 2969  N   PRO A 452     5203   4717   4559    -68    -95     97       N  
ATOM   2970  CA  PRO A 452       1.426  11.080  43.202  1.00 39.03           C  
ANISOU 2970  CA  PRO A 452     5315   4829   4685    -59    -99     76       C  
ATOM   2971  C   PRO A 452       1.613  12.131  44.311  1.00 39.93           C  
ANISOU 2971  C   PRO A 452     5457   4946   4771    -31    -94     52       C  
ATOM   2972  O   PRO A 452       1.422  11.828  45.483  1.00 38.03           O  
ANISOU 2972  O   PRO A 452     5232   4722   4497    -12    -81     58       O  
ATOM   2973  CB  PRO A 452       0.028  11.132  42.571  1.00 39.15           C  
ANISOU 2973  CB  PRO A 452     5298   4861   4718    -60    -84     96       C  
ATOM   2974  CG  PRO A 452      -0.699   9.939  43.111  1.00 43.52           C  
ANISOU 2974  CG  PRO A 452     5834   5432   5271    -76    -61    120       C  
ATOM   2975  CD  PRO A 452       0.354   8.893  43.343  1.00 41.02           C  
ANISOU 2975  CD  PRO A 452     5548   5093   4945    -91    -71    123       C  
ATOM   2976  N   PRO A 453       2.037  13.355  43.937  1.00 41.84           N  
ANISOU 2976  N   PRO A 453     5713   5163   5020    -30    -98     23       N  
ATOM   2977  CA  PRO A 453       2.355  14.388  44.919  1.00 37.74           C  
ANISOU 2977  CA  PRO A 453     5228   4635   4474    -15    -95    -13       C  
ATOM   2978  C   PRO A 453       1.156  15.090  45.535  1.00 37.53           C  
ANISOU 2978  C   PRO A 453     5218   4612   4429     26    -59     -7       C  
ATOM   2979  O   PRO A 453       1.352  15.921  46.430  1.00 36.98           O  
ANISOU 2979  O   PRO A 453     5190   4532   4331     42    -51    -41       O  
ATOM   2980  CB  PRO A 453       3.177  15.405  44.106  1.00 36.45           C  
ANISOU 2980  CB  PRO A 453     5081   4431   4336    -41    -99    -44       C  
ATOM   2981  CG  PRO A 453       2.744  15.214  42.697  1.00 37.31           C  
ANISOU 2981  CG  PRO A 453     5174   4528   4474    -46    -93    -12       C  
ATOM   2982  CD  PRO A 453       2.541  13.723  42.592  1.00 39.84           C  
ANISOU 2982  CD  PRO A 453     5458   4883   4797    -54   -107     18       C  
ATOM   2983  N   ILE A 454      -0.049  14.809  45.047  1.00 37.91           N  
ANISOU 2983  N   ILE A 454     5233   4678   4494     44    -38     29       N  
ATOM   2984  CA  ILE A 454      -1.281  15.133  45.790  1.00 41.84           C  
ANISOU 2984  CA  ILE A 454     5724   5196   4975     88      4     40       C  
ATOM   2985  C   ILE A 454      -2.123  13.853  45.947  1.00 42.33           C  
ANISOU 2985  C   ILE A 454     5737   5302   5044     76     22     77       C  
ATOM   2986  O   ILE A 454      -1.889  12.879  45.258  1.00 39.37           O  
ANISOU 2986  O   ILE A 454     5337   4930   4691     36      0     93       O  
ATOM   2987  CB  ILE A 454      -2.137  16.242  45.137  1.00 44.32           C  
ANISOU 2987  CB  ILE A 454     6034   5498   5309    133     21     44       C  
ATOM   2988  CG1 ILE A 454      -2.331  15.995  43.634  1.00 45.51           C  
ANISOU 2988  CG1 ILE A 454     6147   5651   5493    120     -7     68       C  
ATOM   2989  CG2 ILE A 454      -1.525  17.603  45.406  1.00 46.89           C  
ANISOU 2989  CG2 ILE A 454     6430   5768   5619    151     29      6       C  
ATOM   2990  CD1 ILE A 454      -3.677  16.461  43.082  1.00 42.11           C  
ANISOU 2990  CD1 ILE A 454     5675   5248   5078    176      4     90       C  
ATOM   2991  N   SER A 455      -3.068  13.855  46.881  1.00 43.00           N  
ANISOU 2991  N   SER A 455     5813   5413   5110    104     70     87       N  
ATOM   2992  CA  SER A 455      -4.029  12.763  47.024  1.00 41.04           C  
ANISOU 2992  CA  SER A 455     5513   5204   4878     83    105    120       C  
ATOM   2993  C   SER A 455      -3.401  11.371  47.183  1.00 38.85           C  
ANISOU 2993  C   SER A 455     5253   4916   4592     34     95    138       C  
ATOM   2994  O   SER A 455      -4.022  10.359  46.909  1.00 38.34           O  
ANISOU 2994  O   SER A 455     5150   4866   4553     -4    115    162       O  
ATOM   2995  CB  SER A 455      -4.965  12.801  45.826  1.00 45.35           C  
ANISOU 2995  CB  SER A 455     5981   5775   5474     79     94    130       C  
ATOM   2996  OG  SER A 455      -5.687  14.034  45.802  1.00 50.26           O  
ANISOU 2996  OG  SER A 455     6588   6409   6100    144    111    121       O  
ATOM   2997  N   GLY A 456      -2.159  11.332  47.635  1.00 38.17           N  
ANISOU 2997  N   GLY A 456     5226   4806   4470     37     63    124       N  
ATOM   2998  CA  GLY A 456      -1.419  10.081  47.766  1.00 34.22           C  
ANISOU 2998  CA  GLY A 456     4751   4293   3959     11     48    143       C  
ATOM   2999  C   GLY A 456      -2.200   8.838  48.163  1.00 35.80           C  
ANISOU 2999  C   GLY A 456     4948   4496   4158    -13    100    184       C  
ATOM   3000  O   GLY A 456      -2.299   7.871  47.392  1.00 34.67           O  
ANISOU 3000  O   GLY A 456     4783   4338   4051    -57     98    199       O  
ATOM   3001  N   SER A 457      -2.731   8.841  49.377  1.00 35.03           N  
ANISOU 3001  N   SER A 457     4882   4413   4016     10    155    199       N  
ATOM   3002  CA  SER A 457      -3.403   7.672  49.912  1.00 34.90           C  
ANISOU 3002  CA  SER A 457     4879   4391   3992    -17    220    241       C  
ATOM   3003  C   SER A 457      -4.828   7.527  49.351  1.00 36.14           C  
ANISOU 3003  C   SER A 457     4949   4573   4210    -61    271    248       C  
ATOM   3004  O   SER A 457      -5.547   6.578  49.680  1.00 35.60           O  
ANISOU 3004  O   SER A 457     4875   4500   4151   -104    338    277       O  
ATOM   3005  CB  SER A 457      -3.451   7.750  51.439  1.00 36.76           C  
ANISOU 3005  CB  SER A 457     5186   4633   4146     27    269    256       C  
ATOM   3006  OG  SER A 457      -4.463   8.685  51.843  1.00 39.08           O  
ANISOU 3006  OG  SER A 457     5447   4962   4439     49    321    242       O  
ATOM   3007  N   LEU A 458      -5.244   8.469  48.522  1.00 35.46           N  
ANISOU 3007  N   LEU A 458     4793   4515   4165    -51    241    220       N  
ATOM   3008  CA  LEU A 458      -6.504   8.309  47.825  1.00 37.93           C  
ANISOU 3008  CA  LEU A 458     5008   4865   4539    -89    266    220       C  
ATOM   3009  C   LEU A 458      -6.311   7.418  46.580  1.00 39.10           C  
ANISOU 3009  C   LEU A 458     5128   4995   4732   -153    221    216       C  
ATOM   3010  O   LEU A 458      -7.277   7.014  45.946  1.00 38.06           O  
ANISOU 3010  O   LEU A 458     4918   4895   4650   -201    232    211       O  
ATOM   3011  CB  LEU A 458      -7.034   9.672  47.438  1.00 39.42           C  
ANISOU 3011  CB  LEU A 458     5142   5092   4744    -34    248    196       C  
ATOM   3012  CG  LEU A 458      -7.894  10.503  48.404  1.00 42.56           C  
ANISOU 3012  CG  LEU A 458     5524   5525   5123     22    314    194       C  
ATOM   3013  CD1 LEU A 458      -7.596  10.350  49.886  1.00 39.47           C  
ANISOU 3013  CD1 LEU A 458     5217   5115   4663     42    374    207       C  
ATOM   3014  CD2 LEU A 458      -7.822  11.956  47.961  1.00 40.96           C  
ANISOU 3014  CD2 LEU A 458     5317   5325   4921     93    275    168       C  
ATOM   3015  N   THR A 459      -5.057   7.125  46.227  1.00 36.28           N  
ANISOU 3015  N   THR A 459     4834   4593   4357   -152    170    214       N  
ATOM   3016  CA  THR A 459      -4.771   6.295  45.053  1.00 34.88           C  
ANISOU 3016  CA  THR A 459     4646   4391   4214   -205    132    206       C  
ATOM   3017  C   THR A 459      -4.317   4.915  45.533  1.00 36.95           C  
ANISOU 3017  C   THR A 459     4977   4601   4463   -239    165    232       C  
ATOM   3018  O   THR A 459      -3.736   4.799  46.620  1.00 37.53           O  
ANISOU 3018  O   THR A 459     5119   4653   4487   -200    187    255       O  
ATOM   3019  CB  THR A 459      -3.678   6.919  44.177  1.00 34.13           C  
ANISOU 3019  CB  THR A 459     4572   4281   4114   -176     60    184       C  
ATOM   3020  OG1 THR A 459      -2.406   6.866  44.866  1.00 30.71           O  
ANISOU 3020  OG1 THR A 459     4212   3815   3641   -143     49    189       O  
ATOM   3021  CG2 THR A 459      -4.048   8.375  43.813  1.00 30.82           C  
ANISOU 3021  CG2 THR A 459     4114   3898   3700   -131     37    166       C  
ATOM   3022  N   PRO A 460      -4.593   3.859  44.750  1.00 38.01           N  
ANISOU 3022  N   PRO A 460     5099   4710   4634   -308    169    229       N  
ATOM   3023  CA  PRO A 460      -4.280   2.520  45.294  1.00 37.38           C  
ANISOU 3023  CA  PRO A 460     5098   4565   4541   -337    217    259       C  
ATOM   3024  C   PRO A 460      -2.751   2.231  45.413  1.00 36.98           C  
ANISOU 3024  C   PRO A 460     5134   4467   4452   -282    179    270       C  
ATOM   3025  O   PRO A 460      -2.344   1.420  46.232  1.00 37.69           O  
ANISOU 3025  O   PRO A 460     5303   4510   4507   -264    215    306       O  
ATOM   3026  CB  PRO A 460      -4.961   1.571  44.291  1.00 37.99           C  
ANISOU 3026  CB  PRO A 460     5139   4623   4671   -430    227    240       C  
ATOM   3027  CG  PRO A 460      -4.948   2.351  42.992  1.00 38.16           C  
ANISOU 3027  CG  PRO A 460     5094   4690   4716   -426    148    198       C  
ATOM   3028  CD  PRO A 460      -5.167   3.790  43.384  1.00 36.23           C  
ANISOU 3028  CD  PRO A 460     4803   4507   4456   -359    131    197       C  
ATOM   3029  N   VAL A 461      -1.904   2.893  44.642  1.00 34.50           N  
ANISOU 3029  N   VAL A 461     4804   4164   4139   -249    111    242       N  
ATOM   3030  CA  VAL A 461      -0.447   2.620  44.794  1.00 33.42           C  
ANISOU 3030  CA  VAL A 461     4730   3995   3974   -196     77    248       C  
ATOM   3031  C   VAL A 461       0.118   2.954  46.164  1.00 35.24           C  
ANISOU 3031  C   VAL A 461     5006   4238   4146   -128     79    269       C  
ATOM   3032  O   VAL A 461       1.109   2.370  46.607  1.00 37.37           O  
ANISOU 3032  O   VAL A 461     5334   4481   4383    -82     65    286       O  
ATOM   3033  CB  VAL A 461       0.373   3.340  43.740  1.00 31.82           C  
ANISOU 3033  CB  VAL A 461     4494   3807   3787   -181     15    212       C  
ATOM   3034  CG1 VAL A 461      -0.003   2.766  42.381  1.00 29.98           C  
ANISOU 3034  CG1 VAL A 461     4242   3554   3595   -239     11    192       C  
ATOM   3035  CG2 VAL A 461       0.170   4.866  43.831  1.00 30.32           C  
ANISOU 3035  CG2 VAL A 461     4258   3670   3593   -157     -9    191       C  
ATOM   3036  N   PHE A 462      -0.523   3.889  46.857  1.00 36.31           N  
ANISOU 3036  N   PHE A 462     5118   4418   4263   -115     94    266       N  
ATOM   3037  CA  PHE A 462      -0.061   4.262  48.171  1.00 36.10           C  
ANISOU 3037  CA  PHE A 462     5139   4406   4169    -54     94    278       C  
ATOM   3038  C   PHE A 462      -0.044   3.024  49.097  1.00 39.52           C  
ANISOU 3038  C   PHE A 462     5658   4799   4558    -39    143    330       C  
ATOM   3039  O   PHE A 462       0.827   2.888  49.949  1.00 41.06           O  
ANISOU 3039  O   PHE A 462     5915   4994   4691     26    118    345       O  
ATOM   3040  CB  PHE A 462      -0.968   5.362  48.681  1.00 35.97           C  
ANISOU 3040  CB  PHE A 462     5089   4434   4143    -49    120    265       C  
ATOM   3041  CG  PHE A 462      -0.593   5.920  50.021  1.00 39.24           C  
ANISOU 3041  CG  PHE A 462     5557   4869   4481     11    119    265       C  
ATOM   3042  CD1 PHE A 462      -0.930   5.239  51.198  1.00 39.11           C  
ANISOU 3042  CD1 PHE A 462     5610   4843   4406     30    177    307       C  
ATOM   3043  CD2 PHE A 462       0.013   7.174  50.120  1.00 36.57           C  
ANISOU 3043  CD2 PHE A 462     5207   4559   4127     44     67    220       C  
ATOM   3044  CE1 PHE A 462      -0.619   5.765  52.449  1.00 40.49           C  
ANISOU 3044  CE1 PHE A 462     5844   5043   4497     90    174    304       C  
ATOM   3045  CE2 PHE A 462       0.325   7.697  51.378  1.00 39.25           C  
ANISOU 3045  CE2 PHE A 462     5601   4921   4391     94     62    210       C  
ATOM   3046  CZ  PHE A 462       0.002   7.003  52.540  1.00 38.51           C  
ANISOU 3046  CZ  PHE A 462     5578   4826   4230    120    112    251       C  
ATOM   3047  N   HIS A 463      -0.989   2.113  48.896  1.00 37.38           N  
ANISOU 3047  N   HIS A 463     5393   4492   4318   -100    210    356       N  
ATOM   3048  CA  HIS A 463      -1.183   1.001  49.805  1.00 38.01           C  
ANISOU 3048  CA  HIS A 463     5564   4521   4357    -96    280    411       C  
ATOM   3049  C   HIS A 463      -0.438  -0.220  49.384  1.00 38.06           C  
ANISOU 3049  C   HIS A 463     5635   4456   4370    -90    273    432       C  
ATOM   3050  O   HIS A 463      -0.502  -1.266  50.050  1.00 41.42           O  
ANISOU 3050  O   HIS A 463     6156   4820   4761    -81    334    484       O  
ATOM   3051  CB  HIS A 463      -2.686   0.739  49.953  1.00 38.36           C  
ANISOU 3051  CB  HIS A 463     5578   4563   4433   -174    374    425       C  
ATOM   3052  CG  HIS A 463      -3.437   1.965  50.381  1.00 37.93           C  
ANISOU 3052  CG  HIS A 463     5458   4582   4373   -164    387    403       C  
ATOM   3053  ND1 HIS A 463      -3.440   2.403  51.662  1.00 39.28           N  
ANISOU 3053  ND1 HIS A 463     5683   4774   4468   -106    417    424       N  
ATOM   3054  CD2 HIS A 463      -4.147   2.904  49.644  1.00 38.87           C  
ANISOU 3054  CD2 HIS A 463     5467   4756   4547   -192    367    361       C  
ATOM   3055  CE1 HIS A 463      -4.155   3.540  51.742  1.00 39.16           C  
ANISOU 3055  CE1 HIS A 463     5595   4819   4466   -102    426    393       C  
ATOM   3056  NE2 HIS A 463      -4.580   3.853  50.509  1.00 39.40           N  
ANISOU 3056  NE2 HIS A 463     5523   4869   4577   -150    393    357       N  
ATOM   3057  N   GLN A 464       0.307  -0.083  48.290  1.00 36.72           N  
ANISOU 3057  N   GLN A 464     5422   4288   4240    -88    206    395       N  
ATOM   3058  CA  GLN A 464       1.107  -1.158  47.719  1.00 36.15           C  
ANISOU 3058  CA  GLN A 464     5403   4150   4181    -74    196    405       C  
ATOM   3059  C   GLN A 464       2.597  -1.024  48.072  1.00 35.38           C  
ANISOU 3059  C   GLN A 464     5332   4070   4039     31    127    407       C  
ATOM   3060  O   GLN A 464       3.223  -0.079  47.665  1.00 35.81           O  
ANISOU 3060  O   GLN A 464     5318   4180   4106     49     61    364       O  
ATOM   3061  CB  GLN A 464       0.947  -1.157  46.185  1.00 34.65           C  
ANISOU 3061  CB  GLN A 464     5148   3955   4064   -142    173    358       C  
ATOM   3062  CG  GLN A 464       1.782  -2.204  45.465  1.00 33.73           C  
ANISOU 3062  CG  GLN A 464     5084   3769   3963   -127    166    358       C  
ATOM   3063  CD  GLN A 464       1.327  -3.609  45.814  1.00 35.43           C  
ANISOU 3063  CD  GLN A 464     5398   3888   4174   -156    246    401       C  
ATOM   3064  OE1 GLN A 464       0.144  -3.927  45.707  1.00 38.56           O  
ANISOU 3064  OE1 GLN A 464     5785   4264   4600   -250    304    399       O  
ATOM   3065  NE2 GLN A 464       2.249  -4.440  46.255  1.00 33.40           N  
ANISOU 3065  NE2 GLN A 464     5236   3574   3881    -76    251    439       N  
ATOM   3066  N   GLU A 465       3.174  -1.976  48.800  1.00 35.98           N  
ANISOU 3066  N   GLU A 465     5507   4100   4066     99    142    455       N  
ATOM   3067  CA  GLU A 465       4.623  -1.992  48.983  1.00 35.44           C  
ANISOU 3067  CA  GLU A 465     5448   4054   3965    203     69    452       C  
ATOM   3068  C   GLU A 465       5.344  -2.281  47.657  1.00 38.29           C  
ANISOU 3068  C   GLU A 465     5766   4394   4389    195     39    416       C  
ATOM   3069  O   GLU A 465       4.802  -2.935  46.761  1.00 41.64           O  
ANISOU 3069  O   GLU A 465     6203   4756   4863    127     85    412       O  
ATOM   3070  CB  GLU A 465       5.017  -3.004  50.041  1.00 36.56           C  
ANISOU 3070  CB  GLU A 465     5711   4149   4032    292     91    519       C  
ATOM   3071  CG  GLU A 465       4.385  -2.710  51.401  1.00 37.87           C  
ANISOU 3071  CG  GLU A 465     5931   4337   4118    309    123    557       C  
ATOM   3072  CD  GLU A 465       4.562  -3.848  52.380  1.00 42.95           C  
ANISOU 3072  CD  GLU A 465     6720   4915   4683    389    167    636       C  
ATOM   3073  OE1 GLU A 465       4.949  -4.964  51.928  1.00 43.84           O  
ANISOU 3073  OE1 GLU A 465     6897   4946   4816    414    190    666       O  
ATOM   3074  OE2 GLU A 465       4.326  -3.622  53.602  1.00 43.31           O  
ANISOU 3074  OE2 GLU A 465     6828   4988   4641    432    182    671       O  
ATOM   3075  N   MET A 466       6.554  -1.757  47.519  1.00 38.95           N  
ANISOU 3075  N   MET A 466     5795   4533   4470    259    -35    385       N  
ATOM   3076  CA  MET A 466       7.301  -1.839  46.277  1.00 37.43           C  
ANISOU 3076  CA  MET A 466     5551   4335   4335    255    -58    345       C  
ATOM   3077  C   MET A 466       8.749  -2.152  46.603  1.00 39.87           C  
ANISOU 3077  C   MET A 466     5858   4671   4622    369   -111    348       C  
ATOM   3078  O   MET A 466       9.263  -1.736  47.646  1.00 42.60           O  
ANISOU 3078  O   MET A 466     6196   5077   4913    437   -162    354       O  
ATOM   3079  CB  MET A 466       7.188  -0.508  45.527  1.00 38.05           C  
ANISOU 3079  CB  MET A 466     5526   4476   4456    190    -89    286       C  
ATOM   3080  CG  MET A 466       5.751  -0.173  45.097  1.00 36.43           C  
ANISOU 3080  CG  MET A 466     5309   4256   4276     90    -46    281       C  
ATOM   3081  SD  MET A 466       5.490   1.423  44.297  1.00 38.14           S  
ANISOU 3081  SD  MET A 466     5426   4536   4528     31    -78    225       S  
ATOM   3082  CE  MET A 466       3.688   1.520  44.375  1.00 35.20           C  
ANISOU 3082  CE  MET A 466     5055   4155   4164    -47    -26    240       C  
ATOM   3083  N   VAL A 467       9.384  -2.925  45.732  1.00 40.58           N  
ANISOU 3083  N   VAL A 467     5955   4715   4747    396    -99    342       N  
ATOM   3084  CA  VAL A 467      10.806  -3.266  45.829  1.00 40.28           C  
ANISOU 3084  CA  VAL A 467     5896   4707   4703    510   -146    339       C  
ATOM   3085  C   VAL A 467      11.509  -2.498  44.717  1.00 40.06           C  
ANISOU 3085  C   VAL A 467     5753   4731   4737    477   -171    272       C  
ATOM   3086  O   VAL A 467      11.013  -2.442  43.569  1.00 38.18           O  
ANISOU 3086  O   VAL A 467     5507   4455   4545    393   -131    247       O  
ATOM   3087  CB  VAL A 467      11.044  -4.786  45.625  1.00 39.24           C  
ANISOU 3087  CB  VAL A 467     5867   4474   4569    578    -98    383       C  
ATOM   3088  CG1 VAL A 467      12.485  -5.182  45.926  1.00 42.08           C  
ANISOU 3088  CG1 VAL A 467     6204   4872   4912    723   -149    389       C  
ATOM   3089  CG2 VAL A 467      10.124  -5.577  46.499  1.00 38.22           C  
ANISOU 3089  CG2 VAL A 467     5867   4266   4389    577    -44    450       C  
ATOM   3090  N   ASN A 468      12.647  -1.901  45.048  1.00 37.49           N  
ANISOU 3090  N   ASN A 468     5342   4495   4409    538   -237    242       N  
ATOM   3091  CA  ASN A 468      13.345  -1.095  44.069  1.00 40.49           C  
ANISOU 3091  CA  ASN A 468     5611   4924   4847    498   -251    179       C  
ATOM   3092  C   ASN A 468      14.743  -1.634  43.792  1.00 41.81           C  
ANISOU 3092  C   ASN A 468     5726   5120   5038    596   -270    164       C  
ATOM   3093  O   ASN A 468      15.496  -1.958  44.726  1.00 42.39           O  
ANISOU 3093  O   ASN A 468     5789   5240   5076    704   -324    180       O  
ATOM   3094  CB  ASN A 468      13.438   0.367  44.505  1.00 40.02           C  
ANISOU 3094  CB  ASN A 468     5469   4952   4786    449   -300    135       C  
ATOM   3095  CG  ASN A 468      13.839   1.292  43.349  1.00 41.67           C  
ANISOU 3095  CG  ASN A 468     5588   5186   5057    375   -288     76       C  
ATOM   3096  OD1 ASN A 468      14.251   2.415  43.557  1.00 39.77           O  
ANISOU 3096  OD1 ASN A 468     5273   5011   4828    342   -323     31       O  
ATOM   3097  ND2 ASN A 468      13.730   0.801  42.133  1.00 41.83           N  
ANISOU 3097  ND2 ASN A 468     5628   5152   5116    347   -233     75       N  
ATOM   3098  N   TYR A 469      15.079  -1.745  42.513  1.00 39.40           N  
ANISOU 3098  N   TYR A 469     5390   4791   4789    567   -227    134       N  
ATOM   3099  CA  TYR A 469      16.366  -2.304  42.104  1.00 41.91           C  
ANISOU 3099  CA  TYR A 469     5653   5131   5138    660   -227    117       C  
ATOM   3100  C   TYR A 469      16.654  -1.955  40.658  1.00 43.60           C  
ANISOU 3100  C   TYR A 469     5815   5338   5411    594   -175     69       C  
ATOM   3101  O   TYR A 469      15.753  -1.609  39.896  1.00 38.65           O  
ANISOU 3101  O   TYR A 469     5227   4666   4792    491   -135     61       O  
ATOM   3102  CB  TYR A 469      16.389  -3.826  42.306  1.00 41.76           C  
ANISOU 3102  CB  TYR A 469     5745   5029   5093    765   -198    172       C  
ATOM   3103  CG  TYR A 469      15.129  -4.549  41.831  1.00 41.64           C  
ANISOU 3103  CG  TYR A 469     5863   4888   5068    695   -127    204       C  
ATOM   3104  CD1 TYR A 469      13.984  -4.627  42.654  1.00 40.88           C  
ANISOU 3104  CD1 TYR A 469     5853   4754   4927    653   -124    247       C  
ATOM   3105  CD2 TYR A 469      15.086  -5.176  40.562  1.00 39.48           C  
ANISOU 3105  CD2 TYR A 469     5631   4539   4831    669    -59    185       C  
ATOM   3106  CE1 TYR A 469      12.826  -5.290  42.218  1.00 42.33           C  
ANISOU 3106  CE1 TYR A 469     6142   4831   5111    576    -58    268       C  
ATOM   3107  CE2 TYR A 469      13.950  -5.862  40.131  1.00 38.06           C  
ANISOU 3107  CE2 TYR A 469     5567   4250   4643    597     -1    203       C  
ATOM   3108  CZ  TYR A 469      12.820  -5.910  40.949  1.00 42.39           C  
ANISOU 3108  CZ  TYR A 469     6183   4766   5156    545     -1    243       C  
ATOM   3109  OH  TYR A 469      11.688  -6.572  40.526  1.00 41.55           O  
ANISOU 3109  OH  TYR A 469     6176   4561   5051    461     57    253       O  
ATOM   3110  N   ILE A 470      17.921  -2.030  40.272  1.00 50.18           N  
ANISOU 3110  N   ILE A 470     6557   6224   6284    657   -175     36       N  
ATOM   3111  CA  ILE A 470      18.274  -1.667  38.907  1.00 50.45           C  
ANISOU 3111  CA  ILE A 470     6544   6255   6369    597   -115     -9       C  
ATOM   3112  C   ILE A 470      18.453  -2.889  38.013  1.00 49.45           C  
ANISOU 3112  C   ILE A 470     6489   6047   6253    654    -46      2       C  
ATOM   3113  O   ILE A 470      19.295  -3.748  38.270  1.00 52.72           O  
ANISOU 3113  O   ILE A 470     6893   6467   6674    778    -48     13       O  
ATOM   3114  CB  ILE A 470      19.533  -0.808  38.862  1.00 54.51           C  
ANISOU 3114  CB  ILE A 470     6900   6879   6931    603   -137    -64       C  
ATOM   3115  CG1 ILE A 470      19.541   0.180  40.037  1.00 55.61           C  
ANISOU 3115  CG1 ILE A 470     6976   7101   7053    577   -220    -77       C  
ATOM   3116  CG2 ILE A 470      19.596  -0.076  37.529  1.00 57.22           C  
ANISOU 3116  CG2 ILE A 470     7212   7214   7316    502    -67   -105       C  
ATOM   3117  CD1 ILE A 470      20.935   0.595  40.482  1.00 57.35           C  
ANISOU 3117  CD1 ILE A 470     7039   7441   7309    627   -272   -126       C  
ATOM   3118  N   LEU A 471      17.625  -2.942  36.980  1.00 45.94           N  
ANISOU 3118  N   LEU A 471     6122   5527   5805    566     12     -4       N  
ATOM   3119  CA  LEU A 471      17.729  -3.896  35.893  1.00 47.05           C  
ANISOU 3119  CA  LEU A 471     6334   5589   5954    590     86    -13       C  
ATOM   3120  C   LEU A 471      18.196  -3.171  34.647  1.00 48.86           C  
ANISOU 3120  C   LEU A 471     6502   5850   6214    530    136    -63       C  
ATOM   3121  O   LEU A 471      17.907  -1.989  34.461  1.00 52.56           O  
ANISOU 3121  O   LEU A 471     6922   6361   6686    436    124    -80       O  
ATOM   3122  CB  LEU A 471      16.377  -4.506  35.581  1.00 42.20           C  
ANISOU 3122  CB  LEU A 471     5860   4868   5305    523    112      9       C  
ATOM   3123  CG  LEU A 471      15.616  -5.257  36.663  1.00 41.77           C  
ANISOU 3123  CG  LEU A 471     5897   4757   5216    549     87     63       C  
ATOM   3124  CD1 LEU A 471      14.377  -5.808  36.020  1.00 43.71           C  
ANISOU 3124  CD1 LEU A 471     6260   4903   5444    459    128     64       C  
ATOM   3125  CD2 LEU A 471      16.430  -6.384  37.248  1.00 40.60           C  
ANISOU 3125  CD2 LEU A 471     5784   4577   5064    694     92     93       C  
ATOM   3126  N   SER A 472      18.886  -3.896  33.781  1.00 48.54           N  
ANISOU 3126  N   SER A 472     6476   5777   6190    587    202    -83       N  
ATOM   3127  CA  SER A 472      19.349  -3.366  32.512  1.00 45.31           C  
ANISOU 3127  CA  SER A 472     6029   5386   5801    538    269   -127       C  
ATOM   3128  C   SER A 472      18.724  -4.195  31.388  1.00 43.35           C  
ANISOU 3128  C   SER A 472     5920   5033   5520    514    334   -136       C  
ATOM   3129  O   SER A 472      18.658  -5.404  31.500  1.00 40.35           O  
ANISOU 3129  O   SER A 472     5626   4578   5127    585    351   -121       O  
ATOM   3130  CB  SER A 472      20.886  -3.452  32.456  1.00 46.62           C  
ANISOU 3130  CB  SER A 472     6072   5623   6019    634    299   -155       C  
ATOM   3131  OG  SER A 472      21.377  -2.958  31.220  1.00 47.98           O  
ANISOU 3131  OG  SER A 472     6210   5810   6210    586    381   -196       O  
ATOM   3132  N   PRO A 473      18.329  -3.566  30.262  1.00 44.40           N  
ANISOU 3132  N   PRO A 473     6080   5157   5632    420    373   -162       N  
ATOM   3133  CA  PRO A 473      18.488  -2.156  29.827  1.00 41.88           C  
ANISOU 3133  CA  PRO A 473     5684   4906   5323    338    381   -180       C  
ATOM   3134  C   PRO A 473      17.894  -1.149  30.761  1.00 41.24           C  
ANISOU 3134  C   PRO A 473     5556   4872   5244    278    305   -159       C  
ATOM   3135  O   PRO A 473      16.934  -1.445  31.456  1.00 44.47           O  
ANISOU 3135  O   PRO A 473     6019   5248   5627    265    250   -129       O  
ATOM   3136  CB  PRO A 473      17.747  -2.120  28.495  1.00 39.99           C  
ANISOU 3136  CB  PRO A 473     5552   4610   5033    265    427   -197       C  
ATOM   3137  CG  PRO A 473      17.996  -3.482  27.949  1.00 40.95           C  
ANISOU 3137  CG  PRO A 473     5759   4659   5141    334    481   -213       C  
ATOM   3138  CD  PRO A 473      17.933  -4.430  29.131  1.00 40.71           C  
ANISOU 3138  CD  PRO A 473     5741   4600   5129    410    434   -183       C  
ATOM   3139  N   ALA A 474      18.451   0.054  30.768  1.00 42.07           N  
ANISOU 3139  N   ALA A 474     5562   5046   5378    235    309   -176       N  
ATOM   3140  CA  ALA A 474      17.998   1.071  31.701  1.00 40.45           C  
ANISOU 3140  CA  ALA A 474     5311   4882   5175    184    241   -162       C  
ATOM   3141  C   ALA A 474      18.190   2.462  31.149  1.00 41.58           C  
ANISOU 3141  C   ALA A 474     5409   5058   5330     99    272   -183       C  
ATOM   3142  O   ALA A 474      19.101   2.735  30.354  1.00 41.92           O  
ANISOU 3142  O   ALA A 474     5408   5121   5401     91    345   -211       O  
ATOM   3143  CB  ALA A 474      18.739   0.937  33.023  1.00 37.61           C  
ANISOU 3143  CB  ALA A 474     4855   4586   4849    254    183   -161       C  
ATOM   3144  N   PHE A 475      17.333   3.352  31.606  1.00 39.81           N  
ANISOU 3144  N   PHE A 475     5202   4835   5088     37    225   -167       N  
ATOM   3145  CA  PHE A 475      17.595   4.759  31.461  1.00 40.36           C  
ANISOU 3145  CA  PHE A 475     5224   4935   5177    -35    244   -184       C  
ATOM   3146  C   PHE A 475      18.348   5.236  32.695  1.00 42.12           C  
ANISOU 3146  C   PHE A 475     5332   5227   5446    -24    195   -206       C  
ATOM   3147  O   PHE A 475      17.898   5.000  33.817  1.00 37.15           O  
ANISOU 3147  O   PHE A 475     4702   4610   4802      6    120   -189       O  
ATOM   3148  CB  PHE A 475      16.279   5.506  31.320  1.00 38.86           C  
ANISOU 3148  CB  PHE A 475     5116   4708   4941    -95    219   -158       C  
ATOM   3149  CG  PHE A 475      15.572   5.246  30.019  1.00 39.16           C  
ANISOU 3149  CG  PHE A 475     5259   4693   4928   -113    259   -145       C  
ATOM   3150  CD1 PHE A 475      16.044   5.819  28.824  1.00 37.85           C  
ANISOU 3150  CD1 PHE A 475     5114   4514   4752   -148    339   -157       C  
ATOM   3151  CD2 PHE A 475      14.417   4.479  29.988  1.00 37.44           C  
ANISOU 3151  CD2 PHE A 475     5119   4438   4666   -103    218   -124       C  
ATOM   3152  CE1 PHE A 475      15.379   5.643  27.627  1.00 38.64           C  
ANISOU 3152  CE1 PHE A 475     5318   4572   4790   -161    367   -147       C  
ATOM   3153  CE2 PHE A 475      13.737   4.287  28.795  1.00 38.19           C  
ANISOU 3153  CE2 PHE A 475     5306   4496   4709   -124    242   -121       C  
ATOM   3154  CZ  PHE A 475      14.224   4.862  27.606  1.00 41.02           C  
ANISOU 3154  CZ  PHE A 475     5692   4847   5047   -148    312   -132       C  
ATOM   3155  N   ARG A 476      19.507   5.870  32.506  1.00 42.18           N  
ANISOU 3155  N   ARG A 476     5239   5283   5506    -51    238   -246       N  
ATOM   3156  CA  ARG A 476      20.181   6.457  33.653  1.00 45.12           C  
ANISOU 3156  CA  ARG A 476     5497   5729   5920    -58    183   -278       C  
ATOM   3157  C   ARG A 476      20.537   7.926  33.519  1.00 44.94           C  
ANISOU 3157  C   ARG A 476     5427   5719   5930   -162    217   -314       C  
ATOM   3158  O   ARG A 476      20.656   8.470  32.423  1.00 47.60           O  
ANISOU 3158  O   ARG A 476     5794   6019   6272   -222    306   -317       O  
ATOM   3159  CB  ARG A 476      21.407   5.631  34.096  1.00 53.58           C  
ANISOU 3159  CB  ARG A 476     6451   6872   7035     29    166   -305       C  
ATOM   3160  CG  ARG A 476      22.320   5.134  32.995  1.00 62.17           C  
ANISOU 3160  CG  ARG A 476     7499   7965   8158     55    261   -324       C  
ATOM   3161  CD  ARG A 476      22.234   3.612  32.855  1.00 73.14           C  
ANISOU 3161  CD  ARG A 476     8944   9323   9522    170    259   -295       C  
ATOM   3162  NE  ARG A 476      22.886   2.943  33.984  1.00 83.49           N  
ANISOU 3162  NE  ARG A 476    10168  10701  10852    274    183   -300       N  
ATOM   3163  CZ  ARG A 476      22.950   1.627  34.175  1.00 83.50           C  
ANISOU 3163  CZ  ARG A 476    10208  10681  10836    393    169   -273       C  
ATOM   3164  NH1 ARG A 476      22.406   0.771  33.319  1.00 86.96           N  
ANISOU 3164  NH1 ARG A 476    10770  11029  11241    416    226   -247       N  
ATOM   3165  NH2 ARG A 476      23.569   1.168  35.243  1.00 83.89           N  
ANISOU 3165  NH2 ARG A 476    10178  10798  10897    491     95   -274       N  
ATOM   3166  N   TYR A 477      20.691   8.577  34.660  1.00 44.90           N  
ANISOU 3166  N   TYR A 477     5360   5761   5941   -186    149   -341       N  
ATOM   3167  CA  TYR A 477      21.192   9.935  34.704  1.00 44.95           C  
ANISOU 3167  CA  TYR A 477     5309   5781   5989   -288    179   -388       C  
ATOM   3168  C   TYR A 477      22.637   9.915  34.235  1.00 45.53           C  
ANISOU 3168  C   TYR A 477     5249   5914   6135   -305    242   -439       C  
ATOM   3169  O   TYR A 477      23.329   8.900  34.395  1.00 43.67           O  
ANISOU 3169  O   TYR A 477     4934   5738   5920   -218    222   -448       O  
ATOM   3170  CB  TYR A 477      21.104  10.479  36.138  1.00 47.39           C  
ANISOU 3170  CB  TYR A 477     5578   6135   6295   -300     81   -416       C  
ATOM   3171  CG  TYR A 477      19.689  10.535  36.691  1.00 51.94           C  
ANISOU 3171  CG  TYR A 477     6274   6658   6801   -281     27   -369       C  
ATOM   3172  CD1 TYR A 477      18.690  11.272  36.042  1.00 49.20           C  
ANISOU 3172  CD1 TYR A 477     6041   6229   6425   -334     73   -337       C  
ATOM   3173  CD2 TYR A 477      19.358   9.864  37.872  1.00 56.05           C  
ANISOU 3173  CD2 TYR A 477     6796   7216   7285   -205    -67   -354       C  
ATOM   3174  CE1 TYR A 477      17.390  11.321  36.531  1.00 53.61           C  
ANISOU 3174  CE1 TYR A 477     6692   6749   6927   -313     27   -296       C  
ATOM   3175  CE2 TYR A 477      18.070   9.919  38.378  1.00 59.19           C  
ANISOU 3175  CE2 TYR A 477     7296   7569   7624   -193   -103   -312       C  
ATOM   3176  CZ  TYR A 477      17.088  10.650  37.698  1.00 57.93           C  
ANISOU 3176  CZ  TYR A 477     7231   7334   7445   -248    -55   -286       C  
ATOM   3177  OH  TYR A 477      15.814  10.705  38.209  1.00 55.44           O  
ANISOU 3177  OH  TYR A 477     7000   6986   7079   -231    -89   -248       O  
ATOM   3178  N   GLN A 478      23.084  11.027  33.653  1.00 44.55           N  
ANISOU 3178  N   GLN A 478     5103   5773   6052   -414    325   -472       N  
ATOM   3179  CA  GLN A 478      24.463  11.183  33.205  1.00 46.76           C  
ANISOU 3179  CA  GLN A 478     5244   6111   6411   -454    401   -528       C  
ATOM   3180  C   GLN A 478      24.827  12.638  33.480  1.00 48.66           C  
ANISOU 3180  C   GLN A 478     5441   6350   6699   -590    427   -582       C  
ATOM   3181  O   GLN A 478      23.928  13.474  33.558  1.00 44.57           O  
ANISOU 3181  O   GLN A 478     5040   5754   6140   -644    423   -559       O  
ATOM   3182  CB  GLN A 478      24.609  10.854  31.697  1.00 48.04           C  
ANISOU 3182  CB  GLN A 478     5463   6223   6568   -453    531   -500       C  
ATOM   3183  CG  GLN A 478      23.686  11.696  30.803  1.00 45.98           C  
ANISOU 3183  CG  GLN A 478     5366   5851   6254   -525    603   -456       C  
ATOM   3184  CD  GLN A 478      23.747  11.375  29.319  1.00 43.85           C  
ANISOU 3184  CD  GLN A 478     5174   5531   5957   -518    724   -425       C  
ATOM   3185  OE1 GLN A 478      24.779  10.976  28.797  1.00 42.96           O  
ANISOU 3185  OE1 GLN A 478     4971   5460   5891   -508    802   -454       O  
ATOM   3186  NE2 GLN A 478      22.619  11.581  28.626  1.00 43.18           N  
ANISOU 3186  NE2 GLN A 478     5258   5358   5791   -520    740   -368       N  
ATOM   3187  N   PRO A 479      26.140  12.941  33.633  1.00 49.68           N  
ANISOU 3187  N   PRO A 479     5398   6563   6915   -645    455   -658       N  
ATOM   3188  CA  PRO A 479      26.519  14.324  33.931  1.00 52.71           C  
ANISOU 3188  CA  PRO A 479     5740   6940   7349   -790    482   -720       C  
ATOM   3189  C   PRO A 479      26.199  15.280  32.780  1.00 54.18           C  
ANISOU 3189  C   PRO A 479     6051   7006   7529   -893    625   -692       C  
ATOM   3190  O   PRO A 479      26.162  14.872  31.615  1.00 52.82           O  
ANISOU 3190  O   PRO A 479     5940   6792   7338   -867    724   -646       O  
ATOM   3191  CB  PRO A 479      28.040  14.243  34.175  1.00 53.02           C  
ANISOU 3191  CB  PRO A 479     5551   7104   7488   -821    490   -808       C  
ATOM   3192  CG  PRO A 479      28.481  12.954  33.535  1.00 54.33           C  
ANISOU 3192  CG  PRO A 479     5666   7316   7659   -701    523   -779       C  
ATOM   3193  CD  PRO A 479      27.303  12.024  33.648  1.00 51.63           C  
ANISOU 3193  CD  PRO A 479     5477   6920   7219   -573    452   -694       C  
ATOM   3194  N   ASP A 480      25.949  16.541  33.126  1.00 56.86           N  
ANISOU 3194  N   ASP A 480     6442   7287   7877  -1004    635   -718       N  
ATOM   3195  CA  ASP A 480      25.693  17.596  32.141  1.00 57.91           C  
ANISOU 3195  CA  ASP A 480     6701   7298   8003  -1106    772   -692       C  
ATOM   3196  C   ASP A 480      26.919  17.764  31.257  1.00 59.95           C  
ANISOU 3196  C   ASP A 480     6857   7579   8341  -1189    915   -730       C  
ATOM   3197  O   ASP A 480      28.045  17.678  31.762  1.00 57.24           O  
ANISOU 3197  O   ASP A 480     6320   7343   8084  -1230    899   -813       O  
ATOM   3198  CB  ASP A 480      25.347  18.903  32.844  1.00 57.92           C  
ANISOU 3198  CB  ASP A 480     6762   7237   8010  -1207    752   -726       C  
ATOM   3199  CG  ASP A 480      23.972  18.861  33.470  1.00 57.56           C  
ANISOU 3199  CG  ASP A 480     6851   7144   7875  -1125    646   -673       C  
ATOM   3200  OD1 ASP A 480      23.077  18.240  32.871  1.00 59.52           O  
ANISOU 3200  OD1 ASP A 480     7210   7352   8052  -1030    645   -590       O  
ATOM   3201  OD2 ASP A 480      23.778  19.430  34.554  1.00 58.78           O  
ANISOU 3201  OD2 ASP A 480     6998   7305   8031  -1156    567   -717       O  
ATOM   3202  N   PRO A 481      26.710  17.967  29.932  1.00 59.32           N  
ANISOU 3202  N   PRO A 481     6904   7408   8229  -1208   1055   -671       N  
ATOM   3203  CA  PRO A 481      27.871  17.947  29.023  1.00 61.67           C  
ANISOU 3203  CA  PRO A 481     7105   7732   8594  -1271   1204   -701       C  
ATOM   3204  C   PRO A 481      28.865  19.079  29.250  1.00 65.54           C  
ANISOU 3204  C   PRO A 481     7487   8228   9189  -1443   1287   -786       C  
ATOM   3205  O   PRO A 481      30.001  18.953  28.813  1.00 71.21           O  
ANISOU 3205  O   PRO A 481     8060   9009   9987  -1497   1387   -834       O  
ATOM   3206  CB  PRO A 481      27.248  18.019  27.621  1.00 59.46           C  
ANISOU 3206  CB  PRO A 481     7022   7337   8231  -1252   1327   -612       C  
ATOM   3207  CG  PRO A 481      25.836  18.440  27.825  1.00 56.73           C  
ANISOU 3207  CG  PRO A 481     6867   6897   7793  -1214   1252   -548       C  
ATOM   3208  CD  PRO A 481      25.428  18.030  29.202  1.00 55.39           C  
ANISOU 3208  CD  PRO A 481     6627   6795   7623  -1152   1073   -575       C  
ATOM   3209  N   TRP A 482      28.462  20.133  29.969  1.00 63.03           N  
ANISOU 3209  N   TRP A 482     7227   7849   8873  -1529   1245   -812       N  
ATOM   3210  CA  TRP A 482      29.321  21.293  30.215  1.00 66.55           C  
ANISOU 3210  CA  TRP A 482     7589   8280   9415  -1711   1324   -900       C  
ATOM   3211  C   TRP A 482      30.064  21.284  31.530  1.00 68.56           C  
ANISOU 3211  C   TRP A 482     7633   8667   9750  -1753   1199  -1013       C  
ATOM   3212  O   TRP A 482      29.736  20.579  32.489  1.00 67.24           O  
ANISOU 3212  O   TRP A 482     7415   8584   9548  -1642   1030  -1020       O  
ATOM   3213  CB  TRP A 482      28.515  22.580  30.095  1.00 65.18           C  
ANISOU 3213  CB  TRP A 482     7625   7941   9199  -1795   1381   -867       C  
ATOM   3214  CG  TRP A 482      27.395  22.683  31.096  1.00 61.98           C  
ANISOU 3214  CG  TRP A 482     7317   7510   8723  -1721   1223   -848       C  
ATOM   3215  CD1 TRP A 482      27.461  23.194  32.388  1.00 61.90           C  
ANISOU 3215  CD1 TRP A 482     7242   7534   8745  -1775   1114   -930       C  
ATOM   3216  CD2 TRP A 482      25.997  22.284  30.913  1.00 60.26           C  
ANISOU 3216  CD2 TRP A 482     7279   7231   8387  -1579   1158   -744       C  
ATOM   3217  NE1 TRP A 482      26.233  23.140  33.003  1.00 61.67           N  
ANISOU 3217  NE1 TRP A 482     7342   7463   8625  -1675    999   -881       N  
ATOM   3218  CE2 TRP A 482      25.307  22.603  32.183  1.00 60.25           C  
ANISOU 3218  CE2 TRP A 482     7303   7229   8358  -1557   1017   -770       C  
ATOM   3219  CE3 TRP A 482      25.268  21.707  29.877  1.00 58.59           C  
ANISOU 3219  CE3 TRP A 482     7201   6972   8091  -1474   1196   -642       C  
ATOM   3220  CZ2 TRP A 482      23.943  22.335  32.382  1.00 58.53           C  
ANISOU 3220  CZ2 TRP A 482     7228   6968   8041  -1434    930   -692       C  
ATOM   3221  CZ3 TRP A 482      23.886  21.446  30.091  1.00 59.26           C  
ANISOU 3221  CZ3 TRP A 482     7424   7016   8076  -1355   1095   -569       C  
ATOM   3222  CH2 TRP A 482      23.243  21.755  31.313  1.00 54.66           C  
ANISOU 3222  CH2 TRP A 482     6854   6437   7478  -1337    970   -593       C  
ATOM   3223  OXT TRP A 482      31.039  22.022  31.676  1.00 65.27           O  
ANISOU 3223  OXT TRP A 482     7090   8276   9433  -1907   1266  -1106       O  
TER    3224      TRP A 482                                                      
ATOM   3225  N   LYS B  69      31.047   5.441  53.870  1.00 91.94           N  
ANISOU 3225  N   LYS B  69     8624  14819  11491   1266   1102    938       N  
ATOM   3226  CA  LYS B  69      30.718   6.745  53.239  1.00 93.80           C  
ANISOU 3226  CA  LYS B  69     8865  15039  11735   1005   1121    970       C  
ATOM   3227  C   LYS B  69      29.482   7.324  53.895  1.00 89.34           C  
ANISOU 3227  C   LYS B  69     8533  14180  11231    780    989    860       C  
ATOM   3228  O   LYS B  69      28.463   6.642  54.067  1.00 91.99           O  
ANISOU 3228  O   LYS B  69     9117  14277  11560    876    955    721       O  
ATOM   3229  CB  LYS B  69      30.496   6.606  51.719  1.00100.75           C  
ANISOU 3229  CB  LYS B  69     9832  15930  12517   1152   1284    945       C  
ATOM   3230  CG  LYS B  69      30.918   7.816  50.875  1.00102.76           C  
ANISOU 3230  CG  LYS B  69     9940  16348  12755    960   1359   1066       C  
ATOM   3231  CD  LYS B  69      32.425   7.796  50.569  1.00110.99           C  
ANISOU 3231  CD  LYS B  69    10634  17769  13767   1046   1463   1247       C  
ATOM   3232  CE  LYS B  69      33.219   8.858  51.329  1.00108.97           C  
ANISOU 3232  CE  LYS B  69    10118  17691  13597    742   1365   1402       C  
ATOM   3233  NZ  LYS B  69      32.909   8.957  52.789  1.00102.77           N  
ANISOU 3233  NZ  LYS B  69     9388  16753  12907    585   1172   1352       N  
ATOM   3234  N   PHE B  70      29.581   8.595  54.258  1.00 80.44           N  
ANISOU 3234  N   PHE B  70     7329  13077  10159    478    914    928       N  
ATOM   3235  CA  PHE B  70      28.472   9.294  54.868  1.00 73.06           C  
ANISOU 3235  CA  PHE B  70     6604  11883   9273    265    797    837       C  
ATOM   3236  C   PHE B  70      27.563   9.869  53.786  1.00 65.04           C  
ANISOU 3236  C   PHE B  70     5764  10727   8220    211    863    781       C  
ATOM   3237  O   PHE B  70      28.007  10.630  52.933  1.00 65.48           O  
ANISOU 3237  O   PHE B  70     5720  10911   8250    119    937    873       O  
ATOM   3238  CB  PHE B  70      28.985  10.364  55.839  1.00 72.47           C  
ANISOU 3238  CB  PHE B  70     6401  11870   9263    -22    669    927       C  
ATOM   3239  CG  PHE B  70      29.862   9.810  56.929  1.00 73.43           C  
ANISOU 3239  CG  PHE B  70     6351  12133   9418     23    588    985       C  
ATOM   3240  CD1 PHE B  70      29.296   9.167  58.047  1.00 71.83           C  
ANISOU 3240  CD1 PHE B  70     6288  11761   9242     77    484    886       C  
ATOM   3241  CD2 PHE B  70      31.257   9.907  56.845  1.00 73.83           C  
ANISOU 3241  CD2 PHE B  70     6089  12496   9469     15    614   1149       C  
ATOM   3242  CE1 PHE B  70      30.106   8.639  59.059  1.00 73.75           C  
ANISOU 3242  CE1 PHE B  70     6380  12133   9510    126    403    943       C  
ATOM   3243  CE2 PHE B  70      32.064   9.386  57.859  1.00 76.54           C  
ANISOU 3243  CE2 PHE B  70     6264  12976   9841     63    530   1209       C  
ATOM   3244  CZ  PHE B  70      31.495   8.748  58.967  1.00 73.71           C  
ANISOU 3244  CZ  PHE B  70     6063  12437   9507    122    422   1104       C  
ATOM   3245  N   PRO B  71      26.290   9.471  53.802  1.00 58.08           N  
ANISOU 3245  N   PRO B  71     5143   9592   7334    270    838    639       N  
ATOM   3246  CA  PRO B  71      25.240   9.923  52.874  1.00 55.07           C  
ANISOU 3246  CA  PRO B  71     4954   9050   6919    230    879    571       C  
ATOM   3247  C   PRO B  71      25.117  11.440  52.802  1.00 53.54           C  
ANISOU 3247  C   PRO B  71     4756   8833   6753    -46    840    628       C  
ATOM   3248  O   PRO B  71      24.951  12.095  53.835  1.00 52.51           O  
ANISOU 3248  O   PRO B  71     4647   8624   6682   -228    723    628       O  
ATOM   3249  CB  PRO B  71      23.949   9.334  53.478  1.00 52.93           C  
ANISOU 3249  CB  PRO B  71     4921   8521   6668    276    801    429       C  
ATOM   3250  CG  PRO B  71      24.316   8.961  54.878  1.00 54.35           C  
ANISOU 3250  CG  PRO B  71     5034   8714   6904    262    700    434       C  
ATOM   3251  CD  PRO B  71      25.765   8.552  54.813  1.00 56.58           C  
ANISOU 3251  CD  PRO B  71     5069   9258   7171    367    753    544       C  
ATOM   3252  N   ARG B  72      25.212  11.967  51.583  1.00 53.52           N  
ANISOU 3252  N   ARG B  72     4741   8895   6699    -66    938    678       N  
ATOM   3253  CA  ARG B  72      24.904  13.344  51.228  1.00 55.00           C  
ANISOU 3253  CA  ARG B  72     4982   9022   6894   -298    916    720       C  
ATOM   3254  C   ARG B  72      23.382  13.505  51.024  1.00 55.87           C  
ANISOU 3254  C   ARG B  72     5364   8866   6999   -300    883    594       C  
ATOM   3255  O   ARG B  72      22.801  12.864  50.139  1.00 57.91           O  
ANISOU 3255  O   ARG B  72     5732   9069   7201   -136    955    528       O  
ATOM   3256  CB  ARG B  72      25.604  13.631  49.925  1.00 58.23           C  
ANISOU 3256  CB  ARG B  72     5273   9616   7234   -277   1049    825       C  
ATOM   3257  CG  ARG B  72      25.544  15.051  49.404  1.00 66.03           C  
ANISOU 3257  CG  ARG B  72     6286  10586   8217   -515   1044    904       C  
ATOM   3258  CD  ARG B  72      26.290  15.092  48.062  1.00 76.69           C  
ANISOU 3258  CD  ARG B  72     7507  12148   9485   -451   1197   1011       C  
ATOM   3259  NE  ARG B  72      26.046  16.289  47.244  1.00 79.52           N  
ANISOU 3259  NE  ARG B  72     7937  12465   9812   -631   1218   1073       N  
ATOM   3260  CZ  ARG B  72      24.995  16.470  46.441  1.00 80.44           C  
ANISOU 3260  CZ  ARG B  72     8272  12410   9882   -592   1244    995       C  
ATOM   3261  NH1 ARG B  72      24.036  15.544  46.338  1.00 72.49           N  
ANISOU 3261  NH1 ARG B  72     7435  11252   8857   -394   1246    849       N  
ATOM   3262  NH2 ARG B  72      24.899  17.597  45.741  1.00 84.67           N  
ANISOU 3262  NH2 ARG B  72     8858  12924  10389   -762   1259   1070       N  
ATOM   3263  N   VAL B  73      22.767  14.379  51.822  1.00 51.13           N  
ANISOU 3263  N   VAL B  73     4868   8109   6450   -483    773    566       N  
ATOM   3264  CA  VAL B  73      21.317  14.580  51.874  1.00 48.87           C  
ANISOU 3264  CA  VAL B  73     4816   7584   6170   -489    727    455       C  
ATOM   3265  C   VAL B  73      20.957  15.980  51.379  1.00 49.08           C  
ANISOU 3265  C   VAL B  73     4929   7533   6188   -669    714    495       C  
ATOM   3266  O   VAL B  73      21.349  17.000  51.994  1.00 52.49           O  
ANISOU 3266  O   VAL B  73     5334   7959   6650   -868    641    556       O  
ATOM   3267  CB  VAL B  73      20.839  14.424  53.331  1.00 48.72           C  
ANISOU 3267  CB  VAL B  73     4863   7440   6209   -525    611    387       C  
ATOM   3268  CG1 VAL B  73      19.320  14.334  53.432  1.00 46.28           C  
ANISOU 3268  CG1 VAL B  73     4767   6914   5902   -483    578    274       C  
ATOM   3269  CG2 VAL B  73      21.494  13.197  53.936  1.00 49.82           C  
ANISOU 3269  CG2 VAL B  73     4886   7684   6361   -382    611    381       C  
ATOM   3270  N   LYS B  74      20.214  16.037  50.277  1.00 45.18           N  
ANISOU 3270  N   LYS B  74     4553   6969   5644   -604    775    463       N  
ATOM   3271  CA  LYS B  74      19.853  17.295  49.671  1.00 45.98           C  
ANISOU 3271  CA  LYS B  74     4747   6996   5726   -748    772    505       C  
ATOM   3272  C   LYS B  74      18.384  17.688  49.918  1.00 45.80           C  
ANISOU 3272  C   LYS B  74     4942   6741   5717   -756    705    409       C  
ATOM   3273  O   LYS B  74      17.498  16.852  49.848  1.00 44.65           O  
ANISOU 3273  O   LYS B  74     4882   6518   5567   -611    708    317       O  
ATOM   3274  CB  LYS B  74      20.138  17.226  48.179  1.00 49.28           C  
ANISOU 3274  CB  LYS B  74     5136   7522   6068   -679    890    558       C  
ATOM   3275  CG  LYS B  74      19.724  18.459  47.385  1.00 53.60           C  
ANISOU 3275  CG  LYS B  74     5794   7990   6581   -810    895    605       C  
ATOM   3276  CD  LYS B  74      20.500  18.572  46.081  1.00 58.95           C  
ANISOU 3276  CD  LYS B  74     6377   8839   7181   -797   1015    708       C  
ATOM   3277  CE  LYS B  74      19.887  19.634  45.173  1.00 61.38           C  
ANISOU 3277  CE  LYS B  74     6833   9044   7443   -890   1022    740       C  
ATOM   3278  NZ  LYS B  74      20.633  19.743  43.892  1.00 58.70           N  
ANISOU 3278  NZ  LYS B  74     6407   8878   7018   -879   1145    845       N  
ATOM   3279  N   ASN B  75      18.144  18.962  50.244  1.00 46.39           N  
ANISOU 3279  N   ASN B  75     5106   6712   5809   -925    639    437       N  
ATOM   3280  CA  ASN B  75      16.822  19.559  50.089  1.00 47.38           C  
ANISOU 3280  CA  ASN B  75     5431   6646   5927   -923    604    377       C  
ATOM   3281  C   ASN B  75      16.660  20.182  48.687  1.00 49.87           C  
ANISOU 3281  C   ASN B  75     5804   6962   6182   -941    666    430       C  
ATOM   3282  O   ASN B  75      17.413  21.091  48.316  1.00 52.17           O  
ANISOU 3282  O   ASN B  75     6060   7308   6455  -1087    677    531       O  
ATOM   3283  CB  ASN B  75      16.595  20.633  51.151  1.00 45.89           C  
ANISOU 3283  CB  ASN B  75     5342   6323   5772  -1071    502    373       C  
ATOM   3284  CG  ASN B  75      15.161  21.147  51.148  1.00 43.74           C  
ANISOU 3284  CG  ASN B  75     5269   5859   5491  -1028    468    304       C  
ATOM   3285  OD1 ASN B  75      14.689  21.730  50.168  1.00 45.00           O  
ANISOU 3285  OD1 ASN B  75     5517   5968   5613  -1028    497    327       O  
ATOM   3286  ND2 ASN B  75      14.461  20.919  52.237  1.00 43.41           N  
ANISOU 3286  ND2 ASN B  75     5292   5721   5481   -982    410    226       N  
ATOM   3287  N   TRP B  76      15.676  19.718  47.922  1.00 48.41           N  
ANISOU 3287  N   TRP B  76     5713   6716   5963   -805    698    369       N  
ATOM   3288  CA  TRP B  76      15.510  20.175  46.515  1.00 49.06           C  
ANISOU 3288  CA  TRP B  76     5855   6811   5976   -801    760    417       C  
ATOM   3289  C   TRP B  76      14.781  21.477  46.357  1.00 48.64           C  
ANISOU 3289  C   TRP B  76     5961   6606   5916   -899    709    437       C  
ATOM   3290  O   TRP B  76      14.851  22.092  45.303  1.00 48.92           O  
ANISOU 3290  O   TRP B  76     6040   6652   5894   -939    750    502       O  
ATOM   3291  CB  TRP B  76      14.842  19.095  45.649  1.00 49.34           C  
ANISOU 3291  CB  TRP B  76     5929   6854   5962   -618    809    351       C  
ATOM   3292  CG  TRP B  76      15.779  17.950  45.429  1.00 50.83           C  
ANISOU 3292  CG  TRP B  76     5979   7207   6127   -514    883    356       C  
ATOM   3293  CD1 TRP B  76      16.002  16.849  46.265  1.00 51.04           C  
ANISOU 3293  CD1 TRP B  76     5932   7268   6192   -423    868    298       C  
ATOM   3294  CD2 TRP B  76      16.720  17.800  44.331  1.00 53.09           C  
ANISOU 3294  CD2 TRP B  76     6178   7658   6337   -480    992    431       C  
ATOM   3295  NE1 TRP B  76      16.994  16.044  45.761  1.00 53.04           N  
ANISOU 3295  NE1 TRP B  76     6066   7686   6400   -324    956    330       N  
ATOM   3296  CE2 TRP B  76      17.475  16.558  44.603  1.00 53.75           C  
ANISOU 3296  CE2 TRP B  76     6135   7869   6418   -348   1039    410       C  
ATOM   3297  CE3 TRP B  76      17.024  18.548  43.192  1.00 55.55           C  
ANISOU 3297  CE3 TRP B  76     6503   8027   6577   -537   1058    519       C  
ATOM   3298  CZ2 TRP B  76      18.462  16.098  43.746  1.00 55.16           C  
ANISOU 3298  CZ2 TRP B  76     6206   8231   6523   -260   1154    470       C  
ATOM   3299  CZ3 TRP B  76      18.028  18.074  42.330  1.00 55.46           C  
ANISOU 3299  CZ3 TRP B  76     6375   8207   6489   -462   1177    583       C  
ATOM   3300  CH2 TRP B  76      18.726  16.874  42.600  1.00 57.48           C  
ANISOU 3300  CH2 TRP B  76     6509   8590   6742   -319   1227    557       C  
ATOM   3301  N   GLU B  77      14.058  21.900  47.388  1.00 47.38           N  
ANISOU 3301  N   GLU B  77     5897   6302   5804   -926    623    383       N  
ATOM   3302  CA  GLU B  77      13.381  23.194  47.360  1.00 52.13           C  
ANISOU 3302  CA  GLU B  77     6667   6747   6395  -1003    571    400       C  
ATOM   3303  C   GLU B  77      14.392  24.338  47.610  1.00 54.46           C  
ANISOU 3303  C   GLU B  77     6962   7042   6690  -1209    541    497       C  
ATOM   3304  O   GLU B  77      14.259  25.428  47.038  1.00 54.57           O  
ANISOU 3304  O   GLU B  77     7095   6972   6667  -1296    528    556       O  
ATOM   3305  CB  GLU B  77      12.209  23.232  48.361  1.00 47.49           C  
ANISOU 3305  CB  GLU B  77     6188   6011   5845   -934    500    309       C  
ATOM   3306  CG  GLU B  77      11.739  24.633  48.757  1.00 48.98           C  
ANISOU 3306  CG  GLU B  77     6551   6032   6027  -1017    434    324       C  
ATOM   3307  CD  GLU B  77      10.716  24.650  49.902  1.00 50.00           C  
ANISOU 3307  CD  GLU B  77     6771   6041   6188   -937    376    238       C  
ATOM   3308  OE1 GLU B  77      10.238  23.576  50.370  1.00 48.03           O  
ANISOU 3308  OE1 GLU B  77     6450   5833   5967   -824    384    170       O  
ATOM   3309  OE2 GLU B  77      10.372  25.759  50.352  1.00 51.75           O  
ANISOU 3309  OE2 GLU B  77     7147   6120   6396   -984    323    242       O  
ATOM   3310  N   LEU B  78      15.403  24.065  48.436  1.00 53.40           N  
ANISOU 3310  N   LEU B  78     6696   7002   6593  -1291    523    519       N  
ATOM   3311  CA  LEU B  78      16.307  25.109  48.909  1.00 51.86           C  
ANISOU 3311  CA  LEU B  78     6504   6795   6404  -1508    464    605       C  
ATOM   3312  C   LEU B  78      17.697  24.966  48.352  1.00 52.10           C  
ANISOU 3312  C   LEU B  78     6340   7036   6421  -1609    524    723       C  
ATOM   3313  O   LEU B  78      18.482  25.895  48.435  1.00 54.80           O  
ANISOU 3313  O   LEU B  78     6675   7389   6756  -1813    483    824       O  
ATOM   3314  CB  LEU B  78      16.374  25.105  50.433  1.00 53.27           C  
ANISOU 3314  CB  LEU B  78     6699   6909   6632  -1553    371    551       C  
ATOM   3315  CG  LEU B  78      15.020  25.261  51.139  1.00 57.23           C  
ANISOU 3315  CG  LEU B  78     7385   7218   7143  -1447    318    439       C  
ATOM   3316  CD1 LEU B  78      15.127  25.069  52.648  1.00 55.65           C  
ANISOU 3316  CD1 LEU B  78     7187   6979   6979  -1469    241    382       C  
ATOM   3317  CD2 LEU B  78      14.413  26.624  50.801  1.00 59.27           C  
ANISOU 3317  CD2 LEU B  78     7863   7295   7361  -1513    278    462       C  
ATOM   3318  N   GLY B  79      18.012  23.806  47.786  1.00 51.22           N  
ANISOU 3318  N   GLY B  79     6071   7093   6298  -1467    619    716       N  
ATOM   3319  CA  GLY B  79      19.371  23.541  47.288  1.00 55.85           C  
ANISOU 3319  CA  GLY B  79     6442   7913   6865  -1526    694    831       C  
ATOM   3320  C   GLY B  79      20.429  23.293  48.367  1.00 57.79           C  
ANISOU 3320  C   GLY B  79     6516   8278   7163  -1618    645    869       C  
ATOM   3321  O   GLY B  79      21.627  23.286  48.081  1.00 63.07           O  
ANISOU 3321  O   GLY B  79     6992   9149   7821  -1704    690    988       O  
ATOM   3322  N   SER B  80      19.999  23.100  49.609  1.00 55.17           N  
ANISOU 3322  N   SER B  80     6245   7834   6883  -1601    552    778       N  
ATOM   3323  CA  SER B  80      20.928  22.857  50.705  1.00 54.78           C  
ANISOU 3323  CA  SER B  80     6050   7886   6880  -1685    490    808       C  
ATOM   3324  C   SER B  80      21.288  21.367  50.844  1.00 55.38           C  
ANISOU 3324  C   SER B  80     5949   8121   6971  -1490    554    769       C  
ATOM   3325  O   SER B  80      20.466  20.461  50.582  1.00 47.29           O  
ANISOU 3325  O   SER B  80     4984   7047   5937  -1285    602    668       O  
ATOM   3326  CB  SER B  80      20.375  23.411  52.017  1.00 50.12           C  
ANISOU 3326  CB  SER B  80     5620   7099   6322  -1768    356    735       C  
ATOM   3327  OG  SER B  80      19.098  22.864  52.256  1.00 53.77           O  
ANISOU 3327  OG  SER B  80     6219   7419   6792  -1584    361    600       O  
ATOM   3328  N   ILE B  81      22.537  21.141  51.251  1.00 57.76           N  
ANISOU 3328  N   ILE B  81     6038   8617   7293  -1562    546    859       N  
ATOM   3329  CA  ILE B  81      23.100  19.823  51.408  1.00 58.83           C  
ANISOU 3329  CA  ILE B  81     5990   8924   7438  -1387    602    847       C  
ATOM   3330  C   ILE B  81      23.566  19.624  52.861  1.00 60.58           C  
ANISOU 3330  C   ILE B  81     6141   9163   7715  -1451    490    839       C  
ATOM   3331  O   ILE B  81      24.151  20.521  53.438  1.00 60.80           O  
ANISOU 3331  O   ILE B  81     6140   9200   7760  -1673    397    915       O  
ATOM   3332  CB  ILE B  81      24.222  19.659  50.372  1.00 68.04           C  
ANISOU 3332  CB  ILE B  81     6940  10348   8563  -1374    720    980       C  
ATOM   3333  CG1 ILE B  81      23.599  19.393  48.986  1.00 68.23           C  
ANISOU 3333  CG1 ILE B  81     7055  10350   8520  -1221    843    948       C  
ATOM   3334  CG2 ILE B  81      25.243  18.596  50.771  1.00 68.80           C  
ANISOU 3334  CG2 ILE B  81     6796  10669   8675  -1256    753   1020       C  
ATOM   3335  CD1 ILE B  81      24.327  20.101  47.853  1.00 76.22           C  
ANISOU 3335  CD1 ILE B  81     7971  11512   9475  -1328    931   1093       C  
ATOM   3336  N   THR B  82      23.233  18.479  53.469  1.00 59.66           N  
ANISOU 3336  N   THR B  82     6021   9027   7619  -1266    487    742       N  
ATOM   3337  CA  THR B  82      23.869  18.038  54.727  1.00 57.49           C  
ANISOU 3337  CA  THR B  82     5636   8822   7385  -1288    401    749       C  
ATOM   3338  C   THR B  82      24.500  16.663  54.550  1.00 55.26           C  
ANISOU 3338  C   THR B  82     5172   8726   7099  -1072    481    759       C  
ATOM   3339  O   THR B  82      24.232  15.982  53.566  1.00 53.07           O  
ANISOU 3339  O   THR B  82     4904   8476   6783   -889    595    729       O  
ATOM   3340  CB  THR B  82      22.892  17.969  55.922  1.00 56.80           C  
ANISOU 3340  CB  THR B  82     5735   8523   7325  -1276    298    626       C  
ATOM   3341  OG1 THR B  82      21.686  17.307  55.519  1.00 59.95           O  
ANISOU 3341  OG1 THR B  82     6280   8788   7709  -1089    357    511       O  
ATOM   3342  CG2 THR B  82      22.559  19.378  56.416  1.00 56.24           C  
ANISOU 3342  CG2 THR B  82     5825   8289   7254  -1501    194    631       C  
ATOM   3343  N   TYR B  83      25.356  16.274  55.491  1.00 53.60           N  
ANISOU 3343  N   TYR B  83     4807   8640   6920  -1089    418    804       N  
ATOM   3344  CA  TYR B  83      25.893  14.919  55.521  1.00 53.49           C  
ANISOU 3344  CA  TYR B  83     4646   8777   6902   -861    477    803       C  
ATOM   3345  C   TYR B  83      25.376  14.247  56.780  1.00 48.57           C  
ANISOU 3345  C   TYR B  83     4120   8025   6310   -792    383    702       C  
ATOM   3346  O   TYR B  83      25.474  14.809  57.854  1.00 47.95           O  
ANISOU 3346  O   TYR B  83     4062   7895   6261   -955    260    709       O  
ATOM   3347  CB  TYR B  83      27.434  14.932  55.457  1.00 58.12           C  
ANISOU 3347  CB  TYR B  83     4933   9660   7491   -910    497    962       C  
ATOM   3348  CG  TYR B  83      27.958  15.444  54.109  1.00 65.81           C  
ANISOU 3348  CG  TYR B  83     5795  10788   8421   -948    617   1072       C  
ATOM   3349  CD1 TYR B  83      27.955  14.612  52.973  1.00 65.12           C  
ANISOU 3349  CD1 TYR B  83     5679  10787   8277   -705    774   1058       C  
ATOM   3350  CD2 TYR B  83      28.445  16.755  53.964  1.00 67.39           C  
ANISOU 3350  CD2 TYR B  83     5937  11041   8627  -1228    572   1191       C  
ATOM   3351  CE1 TYR B  83      28.408  15.062  51.745  1.00 67.14           C  
ANISOU 3351  CE1 TYR B  83     5843  11187   8480   -729    891   1158       C  
ATOM   3352  CE2 TYR B  83      28.901  17.221  52.727  1.00 69.67           C  
ANISOU 3352  CE2 TYR B  83     6128  11472   8870  -1269    687   1300       C  
ATOM   3353  CZ  TYR B  83      28.868  16.365  51.621  1.00 71.49           C  
ANISOU 3353  CZ  TYR B  83     6326  11797   9042  -1012    851   1282       C  
ATOM   3354  OH  TYR B  83      29.308  16.791  50.387  1.00 77.93           O  
ANISOU 3354  OH  TYR B  83     7051  12760   9799  -1038    974   1390       O  
ATOM   3355  N   ASP B  84      24.797  13.065  56.657  1.00 46.26           N  
ANISOU 3355  N   ASP B  84     3904   7669   6004   -561    435    608       N  
ATOM   3356  CA  ASP B  84      24.314  12.370  57.846  1.00 48.50           C  
ANISOU 3356  CA  ASP B  84     4277   7837   6312   -496    350    523       C  
ATOM   3357  C   ASP B  84      25.449  11.506  58.388  1.00 51.14           C  
ANISOU 3357  C   ASP B  84     4411   8362   6656   -392    336    588       C  
ATOM   3358  O   ASP B  84      25.835  10.539  57.749  1.00 56.54           O  
ANISOU 3358  O   ASP B  84     5017   9154   7312   -183    429    598       O  
ATOM   3359  CB  ASP B  84      23.021  11.564  57.563  1.00 44.79           C  
ANISOU 3359  CB  ASP B  84     4012   7181   5825   -330    389    394       C  
ATOM   3360  CG  ASP B  84      22.488  10.851  58.788  1.00 46.38           C  
ANISOU 3360  CG  ASP B  84     4309   7266   6048   -276    305    318       C  
ATOM   3361  OD1 ASP B  84      23.281  10.202  59.506  1.00 52.49           O  
ANISOU 3361  OD1 ASP B  84     4965   8146   6834   -216    267    354       O  
ATOM   3362  OD2 ASP B  84      21.264  10.928  59.065  1.00 50.18           O  
ANISOU 3362  OD2 ASP B  84     4977   7557   6532   -292    277    229       O  
ATOM   3363  N   THR B  85      25.997  11.890  59.544  1.00 50.65           N  
ANISOU 3363  N   THR B  85     4275   8344   6626   -535    216    634       N  
ATOM   3364  CA  THR B  85      27.026  11.114  60.242  1.00 52.99           C  
ANISOU 3364  CA  THR B  85     4385   8814   6934   -447    177    698       C  
ATOM   3365  C   THR B  85      26.463  10.289  61.425  1.00 55.17           C  
ANISOU 3365  C   THR B  85     4789   8952   7221   -357     93    607       C  
ATOM   3366  O   THR B  85      27.156   9.398  61.938  1.00 56.44           O  
ANISOU 3366  O   THR B  85     4831   9229   7384   -226     71    642       O  
ATOM   3367  CB  THR B  85      28.154  12.019  60.812  1.00 54.74           C  
ANISOU 3367  CB  THR B  85     4413   9207   7180   -675     79    830       C  
ATOM   3368  OG1 THR B  85      27.573  13.097  61.560  1.00 52.42           O  
ANISOU 3368  OG1 THR B  85     4284   8737   6897   -913    -39    790       O  
ATOM   3369  CG2 THR B  85      29.007  12.580  59.711  1.00 51.55           C  
ANISOU 3369  CG2 THR B  85     3814   9008   6763   -740    166    957       C  
ATOM   3370  N   LEU B  86      25.238  10.612  61.863  1.00 50.02           N  
ANISOU 3370  N   LEU B  86     4370   8064   6570   -425     49    501       N  
ATOM   3371  CA  LEU B  86      24.567   9.896  62.936  1.00 50.31           C  
ANISOU 3371  CA  LEU B  86     4545   7960   6609   -354    -19    418       C  
ATOM   3372  C   LEU B  86      24.368   8.419  62.583  1.00 53.69           C  
ANISOU 3372  C   LEU B  86     4999   8379   7021    -91     53    372       C  
ATOM   3373  O   LEU B  86      24.523   7.562  63.457  1.00 57.44           O  
ANISOU 3373  O   LEU B  86     5476   8852   7498      3     -2    362       O  
ATOM   3374  CB  LEU B  86      23.200  10.539  63.271  1.00 48.09           C  
ANISOU 3374  CB  LEU B  86     4502   7445   6324   -456    -50    320       C  
ATOM   3375  CG  LEU B  86      22.401   9.991  64.465  1.00 45.05           C  
ANISOU 3375  CG  LEU B  86     4268   6913   5934   -418   -120    241       C  
ATOM   3376  CD1 LEU B  86      23.290   9.823  65.710  1.00 46.88           C  
ANISOU 3376  CD1 LEU B  86     4405   7238   6170   -463   -232    293       C  
ATOM   3377  CD2 LEU B  86      21.197  10.861  64.789  1.00 41.52           C  
ANISOU 3377  CD2 LEU B  86     4022   6277   5477   -533   -145    168       C  
ATOM   3378  N   CYS B  87      24.057   8.111  61.318  1.00 54.55           N  
ANISOU 3378  N   CYS B  87     5141   8478   7108     27    169    348       N  
ATOM   3379  CA  CYS B  87      23.752   6.720  60.922  1.00 54.18           C  
ANISOU 3379  CA  CYS B  87     5170   8383   7033    270    228    292       C  
ATOM   3380  C   CYS B  87      24.891   5.736  61.168  1.00 57.36           C  
ANISOU 3380  C   CYS B  87     5418   8951   7425    447    233    354       C  
ATOM   3381  O   CYS B  87      24.651   4.527  61.176  1.00 55.64           O  
ANISOU 3381  O   CYS B  87     5293   8665   7182    643    250    305       O  
ATOM   3382  CB  CYS B  87      23.318   6.622  59.470  1.00 52.16           C  
ANISOU 3382  CB  CYS B  87     4980   8098   6740    359    344    259       C  
ATOM   3383  SG  CYS B  87      24.622   7.155  58.369  1.00 59.47           S  
ANISOU 3383  SG  CYS B  87     5670   9280   7645    367    444    378       S  
ATOM   3384  N   ALA B  88      26.111   6.252  61.372  1.00 59.90           N  
ANISOU 3384  N   ALA B  88     5509   9488   7764    376    213    467       N  
ATOM   3385  CA  ALA B  88      27.282   5.416  61.692  1.00 64.88           C  
ANISOU 3385  CA  ALA B  88     5956  10309   8388    540    208    546       C  
ATOM   3386  C   ALA B  88      27.116   4.740  63.052  1.00 67.14           C  
ANISOU 3386  C   ALA B  88     6316  10507   8687    573     93    514       C  
ATOM   3387  O   ALA B  88      27.730   3.695  63.286  1.00 69.38           O  
ANISOU 3387  O   ALA B  88     6535  10872   8954    776     95    542       O  
ATOM   3388  CB  ALA B  88      28.581   6.227  61.656  1.00 65.61           C  
ANISOU 3388  CB  ALA B  88     5764  10666   8498    420    198    690       C  
ATOM   3389  N   GLN B  89      26.281   5.331  63.923  1.00 67.61           N  
ANISOU 3389  N   GLN B  89     6520  10400   8767    386     -1    457       N  
ATOM   3390  CA  GLN B  89      25.972   4.775  65.262  1.00 67.77           C  
ANISOU 3390  CA  GLN B  89     6641  10318   8792    395   -110    422       C  
ATOM   3391  C   GLN B  89      24.938   3.653  65.221  1.00 66.00           C  
ANISOU 3391  C   GLN B  89     6636   9896   8543    556    -81    322       C  
ATOM   3392  O   GLN B  89      24.679   3.022  66.257  1.00 63.20           O  
ANISOU 3392  O   GLN B  89     6372   9458   8185    589   -158    299       O  
ATOM   3393  CB  GLN B  89      25.429   5.825  66.260  1.00 69.47           C  
ANISOU 3393  CB  GLN B  89     6946  10428   9022    147   -215    396       C  
ATOM   3394  CG  GLN B  89      26.117   7.176  66.357  1.00 75.73           C  
ANISOU 3394  CG  GLN B  89     7603  11340   9832    -83   -268    473       C  
ATOM   3395  CD  GLN B  89      27.615   7.084  66.434  1.00 81.64           C  
ANISOU 3395  CD  GLN B  89     8080  12348  10590    -64   -299    601       C  
ATOM   3396  OE1 GLN B  89      28.161   6.280  67.182  1.00 88.60           O  
ANISOU 3396  OE1 GLN B  89     8894  13303  11469     45   -358    634       O  
ATOM   3397  NE2 GLN B  89      28.295   7.914  65.650  1.00 87.95           N  
ANISOU 3397  NE2 GLN B  89     8716  13300  11401   -171   -259    684       N  
ATOM   3398  N   SER B  90      24.306   3.432  64.064  1.00 64.72           N  
ANISOU 3398  N   SER B  90     6574   9654   8363    636     20    267       N  
ATOM   3399  CA  SER B  90      23.369   2.311  63.928  1.00 64.19           C  
ANISOU 3399  CA  SER B  90     6716   9405   8270    780     39    182       C  
ATOM   3400  C   SER B  90      24.082   0.960  64.084  1.00 69.56           C  
ANISOU 3400  C   SER B  90     7373  10135   8921   1022     38    207       C  
ATOM   3401  O   SER B  90      25.202   0.768  63.594  1.00 68.50           O  
ANISOU 3401  O   SER B  90     7068  10186   8773   1153     89    275       O  
ATOM   3402  CB  SER B  90      22.632   2.356  62.603  1.00 63.70           C  
ANISOU 3402  CB  SER B  90     6760   9258   8185    813    135    125       C  
ATOM   3403  OG  SER B  90      21.624   1.367  62.599  1.00 67.24           O  
ANISOU 3403  OG  SER B  90     7423   9516   8610    901    126     47       O  
ATOM   3404  N   GLN B  91      23.429   0.039  64.785  1.00 75.10           N  
ANISOU 3404  N   GLN B  91     8249  10676   9610   1082    -19    158       N  
ATOM   3405  CA  GLN B  91      24.026  -1.250  65.151  1.00 81.88           C  
ANISOU 3405  CA  GLN B  91     9123  11549  10439   1302    -43    180       C  
ATOM   3406  C   GLN B  91      23.104  -2.387  64.716  1.00 84.57           C  
ANISOU 3406  C   GLN B  91     9715  11679  10739   1432    -23    100       C  
ATOM   3407  O   GLN B  91      23.497  -3.559  64.731  1.00 92.37           O  
ANISOU 3407  O   GLN B  91    10768  12641  11687   1645    -28    104       O  
ATOM   3408  CB  GLN B  91      24.274  -1.333  66.672  1.00 81.97           C  
ANISOU 3408  CB  GLN B  91     9105  11571  10467   1237   -163    219       C  
ATOM   3409  CG  GLN B  91      25.177  -0.248  67.265  1.00 84.17           C  
ANISOU 3409  CG  GLN B  91     9157  12043  10781   1086   -215    301       C  
ATOM   3410  CD  GLN B  91      26.639  -0.661  67.373  1.00 85.06           C  
ANISOU 3410  CD  GLN B  91     9052  12380  10888   1242   -226    401       C  
ATOM   3411  OE1 GLN B  91      27.340  -0.819  66.365  1.00 80.34           O  
ANISOU 3411  OE1 GLN B  91     8329  11920  10277   1386   -132    439       O  
ATOM   3412  NE2 GLN B  91      27.107  -0.828  68.606  1.00 82.98           N  
ANISOU 3412  NE2 GLN B  91     8735  12163  10628   1219   -339    451       N  
ATOM   3413  N   GLN B  92      21.880  -2.027  64.336  1.00 79.29           N  
ANISOU 3413  N   GLN B  92     9192  10859  10076   1299     -9     31       N  
ATOM   3414  CA  GLN B  92      20.862  -3.000  63.967  1.00 78.90           C  
ANISOU 3414  CA  GLN B  92     9386  10602   9990   1367    -10    -40       C  
ATOM   3415  C   GLN B  92      20.483  -2.838  62.492  1.00 77.00           C  
ANISOU 3415  C   GLN B  92     9202  10333   9722   1398     80    -86       C  
ATOM   3416  O   GLN B  92      20.075  -1.750  62.059  1.00 75.50           O  
ANISOU 3416  O   GLN B  92     8956  10172   9558   1244    113    -95       O  
ATOM   3417  CB  GLN B  92      19.628  -2.858  64.866  1.00 82.32           C  
ANISOU 3417  CB  GLN B  92     9951  10881  10448   1185    -83    -71       C  
ATOM   3418  CG  GLN B  92      19.942  -2.465  66.310  1.00 94.04           C  
ANISOU 3418  CG  GLN B  92    11347  12423  11960   1084   -162    -24       C  
ATOM   3419  CD  GLN B  92      18.713  -2.471  67.210  1.00 96.90           C  
ANISOU 3419  CD  GLN B  92    11853  12636  12327    939   -221    -51       C  
ATOM   3420  OE1 GLN B  92      17.815  -3.312  67.058  1.00106.51           O  
ANISOU 3420  OE1 GLN B  92    13250  13696  13523    963   -231    -86       O  
ATOM   3421  NE2 GLN B  92      18.669  -1.535  68.157  1.00 88.88           N  
ANISOU 3421  NE2 GLN B  92    10764  11671  11334    784   -261    -31       N  
ATOM   3422  N   ASP B  93      20.626  -3.926  61.734  1.00 69.33           N  
ANISOU 3422  N   ASP B  93     8356   9297   8689   1605    114   -116       N  
ATOM   3423  CA  ASP B  93      20.335  -3.949  60.298  1.00 65.56           C  
ANISOU 3423  CA  ASP B  93     7961   8786   8163   1668    195   -164       C  
ATOM   3424  C   ASP B  93      18.841  -3.731  59.956  1.00 62.71           C  
ANISOU 3424  C   ASP B  93     7771   8248   7807   1499    168   -228       C  
ATOM   3425  O   ASP B  93      17.971  -4.358  60.537  1.00 59.10           O  
ANISOU 3425  O   ASP B  93     7476   7627   7353   1445     90   -255       O  
ATOM   3426  CB  ASP B  93      20.888  -5.243  59.671  1.00 66.63           C  
ANISOU 3426  CB  ASP B  93     8220   8883   8215   1950    228   -184       C  
ATOM   3427  CG  ASP B  93      22.436  -5.325  59.745  1.00 77.04           C  
ANISOU 3427  CG  ASP B  93     9327  10425   9520   2143    283   -108       C  
ATOM   3428  OD1 ASP B  93      23.083  -4.289  60.031  1.00 80.38           O  
ANISOU 3428  OD1 ASP B  93     9499  11046   9997   2038    304    -39       O  
ATOM   3429  OD2 ASP B  93      23.020  -6.417  59.511  1.00 77.83           O  
ANISOU 3429  OD2 ASP B  93     9510  10508   9552   2403    303   -112       O  
ATOM   3430  N   GLY B  94      18.570  -2.802  59.035  1.00 61.85           N  
ANISOU 3430  N   GLY B  94     7611   8188   7702   1412    230   -240       N  
ATOM   3431  CA  GLY B  94      17.263  -2.646  58.402  1.00 56.08           C  
ANISOU 3431  CA  GLY B  94     7033   7315   6962   1296    218   -297       C  
ATOM   3432  C   GLY B  94      17.094  -3.644  57.251  1.00 53.86           C  
ANISOU 3432  C   GLY B  94     6945   6928   6591   1457    242   -352       C  
ATOM   3433  O   GLY B  94      17.906  -4.575  57.106  1.00 52.13           O  
ANISOU 3433  O   GLY B  94     6771   6718   6316   1669    261   -353       O  
ATOM   3434  N   PRO B  95      16.039  -3.464  56.423  1.00 52.08           N  
ANISOU 3434  N   PRO B  95     6845   6599   6344   1365    236   -398       N  
ATOM   3435  CA  PRO B  95      15.652  -4.518  55.453  1.00 52.37           C  
ANISOU 3435  CA  PRO B  95     7120   6490   6288   1485    224   -460       C  
ATOM   3436  C   PRO B  95      16.309  -4.419  54.063  1.00 50.83           C  
ANISOU 3436  C   PRO B  95     6926   6378   6011   1640    328   -479       C  
ATOM   3437  O   PRO B  95      16.287  -5.385  53.295  1.00 50.93           O  
ANISOU 3437  O   PRO B  95     7142   6283   5926   1793    327   -531       O  
ATOM   3438  CB  PRO B  95      14.116  -4.361  55.366  1.00 50.02           C  
ANISOU 3438  CB  PRO B  95     6945   6049   6011   1284    148   -489       C  
ATOM   3439  CG  PRO B  95      13.862  -2.909  55.672  1.00 46.78           C  
ANISOU 3439  CG  PRO B  95     6338   5754   5681   1107    176   -451       C  
ATOM   3440  CD  PRO B  95      15.038  -2.375  56.479  1.00 50.86           C  
ANISOU 3440  CD  PRO B  95     6643   6435   6246   1142    219   -396       C  
ATOM   3441  N   CYS B  96      16.877  -3.256  53.754  1.00 50.98           N  
ANISOU 3441  N   CYS B  96     6733   6580   6059   1597    413   -434       N  
ATOM   3442  CA  CYS B  96      17.529  -3.011  52.459  1.00 50.99           C  
ANISOU 3442  CA  CYS B  96     6703   6690   5981   1727    526   -435       C  
ATOM   3443  C   CYS B  96      18.900  -3.697  52.354  1.00 54.49           C  
ANISOU 3443  C   CYS B  96     7087   7252   6365   1990    602   -409       C  
ATOM   3444  O   CYS B  96      19.575  -3.927  53.371  1.00 54.73           O  
ANISOU 3444  O   CYS B  96     7002   7350   6443   2035    581   -364       O  
ATOM   3445  CB  CYS B  96      17.665  -1.508  52.212  1.00 47.48           C  
ANISOU 3445  CB  CYS B  96     6051   6400   5589   1572    586   -382       C  
ATOM   3446  SG  CYS B  96      16.095  -0.606  52.370  1.00 47.79           S  
ANISOU 3446  SG  CYS B  96     6143   6318   5697   1293    505   -403       S  
ATOM   3447  N   THR B  97      19.268  -4.070  51.124  1.00 57.29           N  
ANISOU 3447  N   THR B  97     7533   7628   6605   2173    688   -438       N  
ATOM   3448  CA  THR B  97      20.635  -4.509  50.770  1.00 59.45           C  
ANISOU 3448  CA  THR B  97     7716   8066   6807   2445    798   -401       C  
ATOM   3449  C   THR B  97      21.018  -3.756  49.483  1.00 59.26           C  
ANISOU 3449  C   THR B  97     7607   8195   6716   2479    929   -379       C  
ATOM   3450  O   THR B  97      20.159  -3.129  48.862  1.00 58.63           O  
ANISOU 3450  O   THR B  97     7596   8047   6634   2318    916   -408       O  
ATOM   3451  CB  THR B  97      20.765  -6.048  50.569  1.00 60.34           C  
ANISOU 3451  CB  THR B  97     8090   8028   6811   2711    779   -467       C  
ATOM   3452  OG1 THR B  97      20.175  -6.434  49.320  1.00 62.60           O  
ANISOU 3452  OG1 THR B  97     8629   8180   6977   2777    796   -548       O  
ATOM   3453  CG2 THR B  97      20.122  -6.849  51.726  1.00 57.44           C  
ANISOU 3453  CG2 THR B  97     7869   7459   6498   2644    633   -496       C  
ATOM   3454  N   PRO B  98      22.301  -3.786  49.085  1.00 61.53           N  
ANISOU 3454  N   PRO B  98     7732   8699   6947   2686   1057   -317       N  
ATOM   3455  CA  PRO B  98      22.655  -3.052  47.857  1.00 63.80           C  
ANISOU 3455  CA  PRO B  98     7937   9141   7164   2709   1188   -284       C  
ATOM   3456  C   PRO B  98      21.925  -3.548  46.569  1.00 66.89           C  
ANISOU 3456  C   PRO B  98     8628   9369   7418   2799   1206   -383       C  
ATOM   3457  O   PRO B  98      21.793  -2.781  45.600  1.00 64.59           O  
ANISOU 3457  O   PRO B  98     8311   9148   7083   2732   1277   -369       O  
ATOM   3458  CB  PRO B  98      24.178  -3.302  47.731  1.00 66.00           C  
ANISOU 3458  CB  PRO B  98     8009   9677   7390   2964   1320   -199       C  
ATOM   3459  CG  PRO B  98      24.634  -3.700  49.098  1.00 63.37           C  
ANISOU 3459  CG  PRO B  98     7560   9368   7148   2982   1243   -160       C  
ATOM   3460  CD  PRO B  98      23.479  -4.445  49.693  1.00 62.76           C  
ANISOU 3460  CD  PRO B  98     7763   8988   7097   2909   1093   -262       C  
ATOM   3461  N   ARG B  99      21.495  -4.816  46.554  1.00 66.12           N  
ANISOU 3461  N   ARG B  99     8820   9055   7246   2947   1137   -477       N  
ATOM   3462  CA  ARG B  99      20.755  -5.386  45.427  1.00 66.57           C  
ANISOU 3462  CA  ARG B  99     9198   8929   7168   3019   1123   -577       C  
ATOM   3463  C   ARG B  99      19.292  -4.882  45.335  1.00 62.73           C  
ANISOU 3463  C   ARG B  99     8833   8265   6736   2724   1001   -624       C  
ATOM   3464  O   ARG B  99      18.773  -4.731  44.241  1.00 63.83           O  
ANISOU 3464  O   ARG B  99     9121   8348   6784   2709   1016   -668       O  
ATOM   3465  CB  ARG B  99      20.864  -6.925  45.424  1.00 71.92           C  
ANISOU 3465  CB  ARG B  99    10161   9429   7735   3281   1085   -657       C  
ATOM   3466  CG  ARG B  99      19.587  -7.695  45.088  1.00 74.40           C  
ANISOU 3466  CG  ARG B  99    10852   9429   7987   3209    944   -770       C  
ATOM   3467  CD  ARG B  99      19.843  -9.185  44.887  1.00 77.82           C  
ANISOU 3467  CD  ARG B  99    11598   9690   8280   3496    921   -847       C  
ATOM   3468  NE  ARG B  99      20.442  -9.459  43.573  1.00 81.05           N  
ANISOU 3468  NE  ARG B  99    12132  10159   8504   3768   1055   -884       N  
ATOM   3469  CZ  ARG B  99      21.528 -10.200  43.373  1.00 82.43           C  
ANISOU 3469  CZ  ARG B  99    12343  10410   8566   4119   1163   -883       C  
ATOM   3470  NH1 ARG B  99      22.146 -10.771  44.397  1.00 81.99           N  
ANISOU 3470  NH1 ARG B  99    12210  10374   8568   4244   1144   -847       N  
ATOM   3471  NH2 ARG B  99      21.986 -10.388  42.143  1.00 84.71           N  
ANISOU 3471  NH2 ARG B  99    12754  10756   8677   4360   1290   -917       N  
ATOM   3472  N   ARG B 100      18.637  -4.594  46.458  1.00 58.71           N  
ANISOU 3472  N   ARG B 100     8256   7684   6369   2499    885   -608       N  
ATOM   3473  CA  ARG B 100      17.252  -4.116  46.392  1.00 56.00           C  
ANISOU 3473  CA  ARG B 100     8007   7195   6076   2239    777   -641       C  
ATOM   3474  C   ARG B 100      16.842  -3.296  47.606  1.00 52.03           C  
ANISOU 3474  C   ARG B 100     7310   6723   5738   1994    709   -586       C  
ATOM   3475  O   ARG B 100      17.095  -3.703  48.738  1.00 52.85           O  
ANISOU 3475  O   ARG B 100     7358   6812   5910   2002    661   -567       O  
ATOM   3476  CB  ARG B 100      16.274  -5.286  46.154  1.00 57.19           C  
ANISOU 3476  CB  ARG B 100     8502   7078   6151   2258    653   -736       C  
ATOM   3477  CG  ARG B 100      15.913  -6.126  47.375  1.00 55.73           C  
ANISOU 3477  CG  ARG B 100     8397   6744   6034   2216    530   -748       C  
ATOM   3478  CD  ARG B 100      16.977  -7.137  47.792  1.00 58.55           C  
ANISOU 3478  CD  ARG B 100     8792   7112   6343   2479    566   -749       C  
ATOM   3479  NE  ARG B 100      16.545  -7.902  48.968  1.00 58.14           N  
ANISOU 3479  NE  ARG B 100     8830   6905   6355   2415    439   -755       N  
ATOM   3480  CZ  ARG B 100      16.547  -7.430  50.217  1.00 60.48           C  
ANISOU 3480  CZ  ARG B 100     8923   7269   6788   2271    404   -693       C  
ATOM   3481  NH1 ARG B 100      16.968  -6.201  50.486  1.00 61.23           N  
ANISOU 3481  NH1 ARG B 100     8721   7573   6972   2171    476   -625       N  
ATOM   3482  NH2 ARG B 100      16.118  -8.180  51.216  1.00 61.45           N  
ANISOU 3482  NH2 ARG B 100     9150   7245   6952   2219    290   -697       N  
ATOM   3483  N   CYS B 101      16.226  -2.138  47.367  1.00 48.09           N  
ANISOU 3483  N   CYS B 101     6718   6261   5293   1790    706   -561       N  
ATOM   3484  CA  CYS B 101      15.684  -1.320  48.449  1.00 48.98           C  
ANISOU 3484  CA  CYS B 101     6686   6379   5545   1561    638   -520       C  
ATOM   3485  C   CYS B 101      14.300  -1.839  48.909  1.00 48.58           C  
ANISOU 3485  C   CYS B 101     6812   6119   5526   1428    497   -570       C  
ATOM   3486  O   CYS B 101      13.382  -1.976  48.097  1.00 49.03           O  
ANISOU 3486  O   CYS B 101     7036   6066   5529   1378    450   -614       O  
ATOM   3487  CB  CYS B 101      15.588   0.172  48.047  1.00 45.84           C  
ANISOU 3487  CB  CYS B 101     6128   6101   5190   1406    691   -468       C  
ATOM   3488  SG  CYS B 101      14.675   1.191  49.257  1.00 46.73           S  
ANISOU 3488  SG  CYS B 101     6128   6178   5450   1136    600   -436       S  
ATOM   3489  N   LEU B 102      14.151  -2.076  50.214  1.00 50.33           N  
ANISOU 3489  N   LEU B 102     6986   6302   5836   1358    427   -552       N  
ATOM   3490  CA  LEU B 102      12.860  -2.466  50.813  1.00 49.17           C  
ANISOU 3490  CA  LEU B 102     6963   5990   5731   1209    301   -575       C  
ATOM   3491  C   LEU B 102      12.255  -1.371  51.712  1.00 50.98           C  
ANISOU 3491  C   LEU B 102     7029   6266   6075   1001    273   -529       C  
ATOM   3492  O   LEU B 102      11.390  -1.647  52.557  1.00 50.67           O  
ANISOU 3492  O   LEU B 102     7032   6133   6086    888    185   -526       O  
ATOM   3493  CB  LEU B 102      13.047  -3.769  51.593  1.00 49.73           C  
ANISOU 3493  CB  LEU B 102     7154   5951   5790   1304    236   -594       C  
ATOM   3494  CG  LEU B 102      12.685  -5.118  50.938  1.00 51.17           C  
ANISOU 3494  CG  LEU B 102     7630   5949   5864   1409    172   -660       C  
ATOM   3495  CD1 LEU B 102      12.858  -5.153  49.433  1.00 50.13           C  
ANISOU 3495  CD1 LEU B 102     7614   5819   5615   1524    230   -705       C  
ATOM   3496  CD2 LEU B 102      13.398  -6.294  51.599  1.00 48.87           C  
ANISOU 3496  CD2 LEU B 102     7429   5593   5545   1577    150   -668       C  
ATOM   3497  N   GLY B 103      12.688  -0.124  51.523  1.00 52.58           N  
ANISOU 3497  N   GLY B 103     7055   6610   6312    952    349   -488       N  
ATOM   3498  CA  GLY B 103      12.313   0.952  52.443  1.00 51.05           C  
ANISOU 3498  CA  GLY B 103     6717   6462   6216    783    330   -446       C  
ATOM   3499  C   GLY B 103      10.806   1.186  52.599  1.00 51.10           C  
ANISOU 3499  C   GLY B 103     6795   6365   6255    629    252   -456       C  
ATOM   3500  O   GLY B 103      10.376   1.743  53.603  1.00 51.61           O  
ANISOU 3500  O   GLY B 103     6780   6438   6393    516    222   -429       O  
ATOM   3501  N   SER B 104      10.001   0.767  51.614  1.00 50.18           N  
ANISOU 3501  N   SER B 104     6827   6158   6079    626    216   -491       N  
ATOM   3502  CA  SER B 104       8.555   1.070  51.620  1.00 47.75           C  
ANISOU 3502  CA  SER B 104     6562   5782   5800    479    143   -487       C  
ATOM   3503  C   SER B 104       7.737   0.020  52.354  1.00 51.80           C  
ANISOU 3503  C   SER B 104     7178   6177   6326    426     42   -493       C  
ATOM   3504  O   SER B 104       6.534   0.209  52.535  1.00 50.10           O  
ANISOU 3504  O   SER B 104     6971   5924   6141    299    -20   -474       O  
ATOM   3505  CB  SER B 104       8.000   1.256  50.193  1.00 48.91           C  
ANISOU 3505  CB  SER B 104     6804   5903   5878    473    140   -508       C  
ATOM   3506  OG  SER B 104       7.575   0.040  49.578  1.00 43.64           O  
ANISOU 3506  OG  SER B 104     6336   5114   5133    514     68   -552       O  
ATOM   3507  N   LEU B 105       8.386  -1.082  52.750  1.00 49.71           N  
ANISOU 3507  N   LEU B 105     6992   5860   6035    527     25   -512       N  
ATOM   3508  CA  LEU B 105       7.747  -2.137  53.525  1.00 50.75           C  
ANISOU 3508  CA  LEU B 105     7232   5874   6176    477    -71   -510       C  
ATOM   3509  C   LEU B 105       7.431  -1.665  54.969  1.00 52.15           C  
ANISOU 3509  C   LEU B 105     7274   6096   6443    372    -82   -460       C  
ATOM   3510  O   LEU B 105       8.311  -1.131  55.666  1.00 45.49           O  
ANISOU 3510  O   LEU B 105     6299   5346   5638    413    -24   -443       O  
ATOM   3511  CB  LEU B 105       8.641  -3.390  53.545  1.00 53.53           C  
ANISOU 3511  CB  LEU B 105     7717   6155   6468    637    -80   -543       C  
ATOM   3512  CG  LEU B 105       9.013  -4.271  52.318  1.00 57.84           C  
ANISOU 3512  CG  LEU B 105     8462   6616   6900    783    -82   -601       C  
ATOM   3513  CD1 LEU B 105       8.277  -5.593  52.367  1.00 58.18           C  
ANISOU 3513  CD1 LEU B 105     8743   6468   6895    749   -206   -624       C  
ATOM   3514  CD2 LEU B 105       8.862  -3.629  50.933  1.00 55.59           C  
ANISOU 3514  CD2 LEU B 105     8192   6372   6559    791    -37   -626       C  
ATOM   3515  N   VAL B 106       6.177  -1.878  55.393  1.00 50.40           N  
ANISOU 3515  N   VAL B 106     7088   5815   6246    235   -159   -433       N  
ATOM   3516  CA  VAL B 106       5.686  -1.538  56.729  1.00 52.53           C  
ANISOU 3516  CA  VAL B 106     7256   6120   6583    137   -171   -384       C  
ATOM   3517  C   VAL B 106       6.270  -2.421  57.845  1.00 56.85           C  
ANISOU 3517  C   VAL B 106     7837   6626   7135    182   -196   -373       C  
ATOM   3518  O   VAL B 106       6.553  -1.938  58.931  1.00 59.80           O  
ANISOU 3518  O   VAL B 106     8100   7066   7553    165   -169   -346       O  
ATOM   3519  CB  VAL B 106       4.130  -1.617  56.791  1.00 54.45           C  
ANISOU 3519  CB  VAL B 106     7521   6327   6841    -16   -242   -344       C  
ATOM   3520  CG1 VAL B 106       3.601  -1.286  58.193  1.00 51.84           C  
ANISOU 3520  CG1 VAL B 106     7086   6045   6565   -101   -241   -288       C  
ATOM   3521  CG2 VAL B 106       3.489  -0.690  55.763  1.00 49.33           C  
ANISOU 3521  CG2 VAL B 106     6827   5727   6188    -59   -224   -345       C  
ATOM   3522  N   LEU B 107       6.418  -3.719  57.588  1.00 64.95           N  
ANISOU 3522  N   LEU B 107     9035   7535   8110    239   -256   -395       N  
ATOM   3523  CA  LEU B 107       6.931  -4.657  58.604  1.00 65.55           C  
ANISOU 3523  CA  LEU B 107     9168   7554   8183    291   -291   -380       C  
ATOM   3524  C   LEU B 107       8.279  -5.265  58.225  1.00 67.99           C  
ANISOU 3524  C   LEU B 107     9543   7847   8443    489   -260   -421       C  
ATOM   3525  O   LEU B 107       8.591  -5.397  57.038  1.00 66.18           O  
ANISOU 3525  O   LEU B 107     9389   7598   8158    581   -236   -467       O  
ATOM   3526  CB  LEU B 107       5.922  -5.782  58.900  1.00 58.40           C  
ANISOU 3526  CB  LEU B 107     8425   6507   7257    185   -401   -353       C  
ATOM   3527  CG  LEU B 107       4.572  -5.374  59.507  1.00 58.91           C  
ANISOU 3527  CG  LEU B 107     8412   6603   7368     -7   -434   -290       C  
ATOM   3528  CD1 LEU B 107       3.570  -6.530  59.526  1.00 60.11           C  
ANISOU 3528  CD1 LEU B 107     8729   6620   7491   -129   -551   -254       C  
ATOM   3529  CD2 LEU B 107       4.743  -4.772  60.893  1.00 58.39           C  
ANISOU 3529  CD2 LEU B 107     8196   6634   7355    -30   -388   -247       C  
ATOM   3530  N   PRO B 108       9.088  -5.625  59.245  1.00 76.18           N  
ANISOU 3530  N   PRO B 108    10546   8903   9495    564   -257   -401       N  
ATOM   3531  CA  PRO B 108      10.288  -6.426  58.995  1.00 78.78           C  
ANISOU 3531  CA  PRO B 108    10953   9209   9772    769   -241   -429       C  
ATOM   3532  C   PRO B 108       9.873  -7.841  58.633  1.00 78.57           C  
ANISOU 3532  C   PRO B 108    11192   8987   9675    805   -330   -454       C  
ATOM   3533  O   PRO B 108       8.949  -8.377  59.241  1.00 72.04           O  
ANISOU 3533  O   PRO B 108    10458   8056   8858    670   -416   -423       O  
ATOM   3534  CB  PRO B 108      11.010  -6.433  60.355  1.00 78.99           C  
ANISOU 3534  CB  PRO B 108    10874   9301   9839    803   -240   -385       C  
ATOM   3535  CG  PRO B 108      10.363  -5.340  61.158  1.00 79.64           C  
ANISOU 3535  CG  PRO B 108    10799   9469   9991    627   -229   -347       C  
ATOM   3536  CD  PRO B 108       8.944  -5.297  60.678  1.00 74.82           C  
ANISOU 3536  CD  PRO B 108    10265   8782   9380    477   -268   -349       C  
ATOM   3537  N   ARG B 109      10.537  -8.429  57.640  1.00 84.96           N  
ANISOU 3537  N   ARG B 109    12131   9746  10405    983   -309   -505       N  
ATOM   3538  CA  ARG B 109      10.346  -9.838  57.323  1.00 89.31           C  
ANISOU 3538  CA  ARG B 109    12970  10093  10873   1051   -397   -537       C  
ATOM   3539  C   ARG B 109      10.505 -10.688  58.582  1.00 92.74           C  
ANISOU 3539  C   ARG B 109    13470  10446  11321   1063   -463   -495       C  
ATOM   3540  O   ARG B 109       9.636 -11.510  58.912  1.00 79.53           O  
ANISOU 3540  O   ARG B 109    11976   8609   9631    943   -572   -477       O  
ATOM   3541  CB  ARG B 109      11.350 -10.287  56.250  1.00 93.33           C  
ANISOU 3541  CB  ARG B 109    13588  10588  11285   1303   -339   -598       C  
ATOM   3542  CG  ARG B 109      10.722 -10.747  54.943  1.00 98.34           C  
ANISOU 3542  CG  ARG B 109    14455  11082  11826   1297   -383   -659       C  
ATOM   3543  CD  ARG B 109      10.053 -12.099  55.139  1.00 96.48           C  
ANISOU 3543  CD  ARG B 109    14525  10600  11535   1249   -526   -670       C  
ATOM   3544  NE  ARG B 109       9.894 -12.832  53.886  1.00103.19           N  
ANISOU 3544  NE  ARG B 109    15658  11290  12258   1332   -571   -743       N  
ATOM   3545  CZ  ARG B 109       9.715 -14.148  53.815  1.00103.20           C  
ANISOU 3545  CZ  ARG B 109    15983  11057  12172   1378   -682   -772       C  
ATOM   3546  NH1 ARG B 109       9.675 -14.883  54.919  1.00110.87           N  
ANISOU 3546  NH1 ARG B 109    17025  11929  13171   1347   -757   -728       N  
ATOM   3547  NH2 ARG B 109       9.583 -14.737  52.644  1.00103.25           N  
ANISOU 3547  NH2 ARG B 109    16260  10917  12053   1454   -724   -846       N  
ATOM   3548  N   LYS B 110      11.592 -10.419  59.308  1.00104.48           N  
ANISOU 3548  N   LYS B 110    14797  12060  12840   1188   -402   -470       N  
ATOM   3549  CA  LYS B 110      12.132 -11.334  60.321  1.00117.58           C  
ANISOU 3549  CA  LYS B 110    16534  13652  14488   1285   -451   -439       C  
ATOM   3550  C   LYS B 110      11.480 -11.210  61.717  1.00113.89           C  
ANISOU 3550  C   LYS B 110    15999  13186  14089   1096   -509   -370       C  
ATOM   3551  O   LYS B 110      12.071 -11.612  62.728  1.00110.36           O  
ANISOU 3551  O   LYS B 110    15537  12746  13649   1166   -531   -332       O  
ATOM   3552  CB  LYS B 110      13.681 -11.212  60.389  1.00124.38           C  
ANISOU 3552  CB  LYS B 110    17261  14657  15340   1531   -366   -437       C  
ATOM   3553  CG  LYS B 110      14.391 -10.820  59.076  1.00121.82           C  
ANISOU 3553  CG  LYS B 110    16888  14431  14969   1693   -264   -484       C  
ATOM   3554  CD  LYS B 110      14.504 -11.952  58.047  1.00116.66           C  
ANISOU 3554  CD  LYS B 110    16521  13608  14197   1877   -284   -548       C  
ATOM   3555  CE  LYS B 110      15.943 -12.407  57.820  1.00116.52           C  
ANISOU 3555  CE  LYS B 110    16486  13668  14117   2196   -209   -554       C  
ATOM   3556  NZ  LYS B 110      16.449 -13.360  58.854  1.00113.36           N  
ANISOU 3556  NZ  LYS B 110    16170  13194  13709   2318   -271   -519       N  
ATOM   3557  N   LEU B 111      10.260 -10.670  61.759  1.00108.78           N  
ANISOU 3557  N   LEU B 111    15312  12539  13482    867   -533   -351       N  
ATOM   3558  CA  LEU B 111       9.474 -10.582  62.998  1.00110.44           C  
ANISOU 3558  CA  LEU B 111    15472  12749  13740    683   -580   -283       C  
ATOM   3559  C   LEU B 111       8.948 -11.968  63.426  1.00111.84           C  
ANISOU 3559  C   LEU B 111    15900  12723  13873    637   -696   -252       C  
ATOM   3560  O   LEU B 111       7.831 -12.375  63.080  1.00102.02           O  
ANISOU 3560  O   LEU B 111    14786  11366  12612    479   -768   -240       O  
ATOM   3561  CB  LEU B 111       8.307  -9.591  62.836  1.00103.66           C  
ANISOU 3561  CB  LEU B 111    14491  11965  12932    474   -561   -266       C  
ATOM   3562  CG  LEU B 111       7.783  -8.745  64.008  1.00 93.96           C  
ANISOU 3562  CG  LEU B 111    13084  10851  11765    328   -538   -206       C  
ATOM   3563  CD1 LEU B 111       6.270  -8.595  63.885  1.00 85.08           C  
ANISOU 3563  CD1 LEU B 111    11970   9701  10656    120   -575   -169       C  
ATOM   3564  CD2 LEU B 111       8.171  -9.297  65.377  1.00 89.67           C  
ANISOU 3564  CD2 LEU B 111    12561  10290  11221    348   -573   -156       C  
ATOM   3565  N   PRO B 121      21.929 -14.108  75.154  1.00 97.89           N  
ANISOU 3565  N   PRO B 121    13133  12008  12053   2252   -996    353       N  
ATOM   3566  CA  PRO B 121      23.337 -14.159  75.554  1.00 98.46           C  
ANISOU 3566  CA  PRO B 121    13025  12264  12119   2450  -1028    419       C  
ATOM   3567  C   PRO B 121      23.774 -12.890  76.305  1.00 97.35           C  
ANISOU 3567  C   PRO B 121    12613  12353  12023   2286  -1046    457       C  
ATOM   3568  O   PRO B 121      23.355 -11.777  75.961  1.00 93.89           O  
ANISOU 3568  O   PRO B 121    12057  11988  11631   2096   -989    415       O  
ATOM   3569  CB  PRO B 121      24.091 -14.295  74.215  1.00 99.61           C  
ANISOU 3569  CB  PRO B 121    13093  12488  12265   2681   -938    388       C  
ATOM   3570  CG  PRO B 121      23.045 -14.500  73.159  1.00 97.56           C  
ANISOU 3570  CG  PRO B 121    13029  12041  11998   2617   -875    301       C  
ATOM   3571  CD  PRO B 121      21.777 -13.904  73.705  1.00 98.18           C  
ANISOU 3571  CD  PRO B 121    13163  12037  12106   2298   -897    281       C  
ATOM   3572  N   ALA B 122      24.624 -13.078  77.312  1.00 99.50           N  
ANISOU 3572  N   ALA B 122    12801  12729  12276   2366  -1135    536       N  
ATOM   3573  CA  ALA B 122      25.011 -12.026  78.267  1.00 95.19           C  
ANISOU 3573  CA  ALA B 122    12049  12368  11751   2199  -1190    580       C  
ATOM   3574  C   ALA B 122      25.879 -10.928  77.658  1.00 91.44           C  
ANISOU 3574  C   ALA B 122    11270  12142  11329   2183  -1139    587       C  
ATOM   3575  O   ALA B 122      25.597  -9.741  77.839  1.00 88.64           O  
ANISOU 3575  O   ALA B 122    10806  11866  11007   1954  -1130    567       O  
ATOM   3576  CB  ALA B 122      25.717 -12.646  79.471  1.00 94.11           C  
ANISOU 3576  CB  ALA B 122    11921  12268  11569   2304  -1313    670       C  
ATOM   3577  N   GLU B 123      26.931 -11.344  76.953  1.00 92.13           N  
ANISOU 3577  N   GLU B 123    11233  12352  11419   2431  -1106    622       N  
ATOM   3578  CA  GLU B 123      27.869 -10.452  76.266  1.00 91.85           C  
ANISOU 3578  CA  GLU B 123    10897  12572  11429   2447  -1049    649       C  
ATOM   3579  C   GLU B 123      27.180  -9.408  75.367  1.00 85.01           C  
ANISOU 3579  C   GLU B 123     9993  11700  10608   2251   -948    572       C  
ATOM   3580  O   GLU B 123      27.669  -8.282  75.231  1.00 81.77           O  
ANISOU 3580  O   GLU B 123     9350  11481  10239   2122   -935    596       O  
ATOM   3581  CB  GLU B 123      28.903 -11.276  75.465  1.00100.74           C  
ANISOU 3581  CB  GLU B 123    11944  13796  12535   2786   -997    690       C  
ATOM   3582  CG  GLU B 123      28.502 -11.715  74.042  1.00111.86           C  
ANISOU 3582  CG  GLU B 123    13482  15089  13931   2924   -868    611       C  
ATOM   3583  CD  GLU B 123      27.427 -12.814  73.963  1.00116.43           C  
ANISOU 3583  CD  GLU B 123    14432  15344  14461   2972   -877    540       C  
ATOM   3584  OE1 GLU B 123      27.367 -13.698  74.852  1.00117.02           O  
ANISOU 3584  OE1 GLU B 123    14670  15297  14495   3046   -972    574       O  
ATOM   3585  OE2 GLU B 123      26.643 -12.808  72.982  1.00113.28           O  
ANISOU 3585  OE2 GLU B 123    14167  14813  14061   2931   -795    456       O  
ATOM   3586  N   GLN B 124      26.049  -9.777  74.769  1.00 76.38           N  
ANISOU 3586  N   GLN B 124     9129  10387   9504   2220   -887    487       N  
ATOM   3587  CA  GLN B 124      25.380  -8.884  73.850  1.00 73.38           C  
ANISOU 3587  CA  GLN B 124     8725   9994   9161   2062   -793    418       C  
ATOM   3588  C   GLN B 124      24.446  -7.912  74.571  1.00 68.44           C  
ANISOU 3588  C   GLN B 124     8130   9317   8556   1762   -826    388       C  
ATOM   3589  O   GLN B 124      24.379  -6.732  74.211  1.00 65.21           O  
ANISOU 3589  O   GLN B 124     7588   9003   8185   1603   -784    369       O  
ATOM   3590  CB  GLN B 124      24.645  -9.645  72.751  1.00 76.12           C  
ANISOU 3590  CB  GLN B 124     9284  10154   9486   2166   -714    343       C  
ATOM   3591  CG  GLN B 124      24.565  -8.839  71.456  1.00 80.98           C  
ANISOU 3591  CG  GLN B 124     9795  10843  10131   2122   -600    297       C  
ATOM   3592  CD  GLN B 124      23.290  -9.099  70.668  1.00 86.43           C  
ANISOU 3592  CD  GLN B 124    10714  11317  10810   2057   -549    208       C  
ATOM   3593  OE1 GLN B 124      22.422  -8.220  70.554  1.00 90.27           O  
ANISOU 3593  OE1 GLN B 124    11200  11772  11328   1835   -526    167       O  
ATOM   3594  NE2 GLN B 124      23.161 -10.311  70.126  1.00 85.81           N  
ANISOU 3594  NE2 GLN B 124    10840  11086  10679   2252   -539    179       N  
ATOM   3595  N   LEU B 125      23.722  -8.410  75.576  1.00 64.93           N  
ANISOU 3595  N   LEU B 125     7870   8721   8079   1694   -898    388       N  
ATOM   3596  CA  LEU B 125      22.941  -7.556  76.466  1.00 58.72           C  
ANISOU 3596  CA  LEU B 125     7112   7905   7294   1443   -934    372       C  
ATOM   3597  C   LEU B 125      23.859  -6.541  77.143  1.00 59.76           C  
ANISOU 3597  C   LEU B 125     7026   8242   7439   1351   -995    423       C  
ATOM   3598  O   LEU B 125      23.536  -5.352  77.237  1.00 57.04           O  
ANISOU 3598  O   LEU B 125     6618   7940   7113   1153   -983    396       O  
ATOM   3599  CB  LEU B 125      22.242  -8.394  77.536  1.00 57.75           C  
ANISOU 3599  CB  LEU B 125     7202   7620   7119   1421  -1005    389       C  
ATOM   3600  CG  LEU B 125      21.541  -7.647  78.677  1.00 52.71           C  
ANISOU 3600  CG  LEU B 125     6603   6966   6459   1199  -1048    388       C  
ATOM   3601  CD1 LEU B 125      20.351  -6.846  78.154  1.00 49.80           C  
ANISOU 3601  CD1 LEU B 125     6278   6528   6115   1024   -963    318       C  
ATOM   3602  CD2 LEU B 125      21.093  -8.641  79.727  1.00 52.18           C  
ANISOU 3602  CD2 LEU B 125     6729   6766   6332   1218  -1119    427       C  
ATOM   3603  N   LEU B 126      25.012  -7.029  77.591  1.00 60.07           N  
ANISOU 3603  N   LEU B 126     6957   8403   7463   1499  -1067    499       N  
ATOM   3604  CA  LEU B 126      25.990  -6.199  78.244  1.00 63.23           C  
ANISOU 3604  CA  LEU B 126     7145   9009   7871   1419  -1147    563       C  
ATOM   3605  C   LEU B 126      26.463  -5.047  77.363  1.00 62.91           C  
ANISOU 3605  C   LEU B 126     6890   9129   7883   1328  -1086    558       C  
ATOM   3606  O   LEU B 126      26.557  -3.916  77.837  1.00 61.11           O  
ANISOU 3606  O   LEU B 126     6575   8980   7663   1123  -1135    565       O  
ATOM   3607  CB  LEU B 126      27.184  -7.035  78.669  1.00 67.91           C  
ANISOU 3607  CB  LEU B 126     7639   9722   8443   1629  -1226    655       C  
ATOM   3608  CG  LEU B 126      27.853  -6.453  79.897  1.00 70.44           C  
ANISOU 3608  CG  LEU B 126     7838  10182   8743   1510  -1361    724       C  
ATOM   3609  CD1 LEU B 126      27.337  -7.210  81.103  1.00 73.20           C  
ANISOU 3609  CD1 LEU B 126     8402  10382   9027   1517  -1449    734       C  
ATOM   3610  CD2 LEU B 126      29.368  -6.564  79.768  1.00 75.90           C  
ANISOU 3610  CD2 LEU B 126     8262  11125   9451   1663  -1408    828       C  
ATOM   3611  N   SER B 127      26.768  -5.334  76.097  1.00 62.42           N  
ANISOU 3611  N   SER B 127     6758   9110   7849   1478   -985    550       N  
ATOM   3612  CA  SER B 127      27.234  -4.299  75.178  1.00 63.87           C  
ANISOU 3612  CA  SER B 127     6739   9451   8077   1400   -917    557       C  
ATOM   3613  C   SER B 127      26.182  -3.245  74.851  1.00 61.58           C  
ANISOU 3613  C   SER B 127     6530   9059   7807   1170   -865    477       C  
ATOM   3614  O   SER B 127      26.526  -2.063  74.728  1.00 60.05           O  
ANISOU 3614  O   SER B 127     6189   8986   7641   1006   -871    494       O  
ATOM   3615  CB  SER B 127      27.817  -4.881  73.901  1.00 68.66           C  
ANISOU 3615  CB  SER B 127     7259  10136   8694   1633   -811    570       C  
ATOM   3616  OG  SER B 127      27.226  -6.124  73.602  1.00 80.51           O  
ANISOU 3616  OG  SER B 127     8984  11446  10160   1818   -773    521       O  
ATOM   3617  N   GLN B 128      24.915  -3.666  74.723  1.00 58.91           N  
ANISOU 3617  N   GLN B 128     6426   8503   7455   1156   -820    397       N  
ATOM   3618  CA  GLN B 128      23.811  -2.735  74.520  1.00 55.27           C  
ANISOU 3618  CA  GLN B 128     6053   7939   7007    955   -775    326       C  
ATOM   3619  C   GLN B 128      23.577  -1.925  75.776  1.00 56.46           C  
ANISOU 3619  C   GLN B 128     6229   8087   7137    759   -865    331       C  
ATOM   3620  O   GLN B 128      23.274  -0.735  75.695  1.00 58.17           O  
ANISOU 3620  O   GLN B 128     6419   8317   7367    582   -852    302       O  
ATOM   3621  CB  GLN B 128      22.519  -3.467  74.177  1.00 57.46           C  
ANISOU 3621  CB  GLN B 128     6561   8002   7270    987   -719    257       C  
ATOM   3622  CG  GLN B 128      22.502  -4.198  72.846  1.00 57.66           C  
ANISOU 3622  CG  GLN B 128     6620   7985   7302   1157   -629    230       C  
ATOM   3623  CD  GLN B 128      21.298  -5.116  72.721  1.00 58.68           C  
ANISOU 3623  CD  GLN B 128     6995   7894   7406   1182   -612    178       C  
ATOM   3624  OE1 GLN B 128      21.411  -6.323  72.909  1.00 64.47           O  
ANISOU 3624  OE1 GLN B 128     7844   8545   8108   1335   -644    194       O  
ATOM   3625  NE2 GLN B 128      20.141  -4.547  72.419  1.00 53.11           N  
ANISOU 3625  NE2 GLN B 128     6372   7094   6713   1030   -569    123       N  
ATOM   3626  N   ALA B 129      23.703  -2.580  76.936  1.00 56.30           N  
ANISOU 3626  N   ALA B 129     6278   8039   7074    797   -958    365       N  
ATOM   3627  CA  ALA B 129      23.540  -1.916  78.230  1.00 54.21           C  
ANISOU 3627  CA  ALA B 129     6056   7771   6769    631  -1052    372       C  
ATOM   3628  C   ALA B 129      24.627  -0.858  78.447  1.00 57.10           C  
ANISOU 3628  C   ALA B 129     6223   8323   7147    520  -1125    422       C  
ATOM   3629  O   ALA B 129      24.304   0.310  78.722  1.00 55.88           O  
ANISOU 3629  O   ALA B 129     6088   8159   6983    327  -1143    390       O  
ATOM   3630  CB  ALA B 129      23.534  -2.930  79.368  1.00 53.87           C  
ANISOU 3630  CB  ALA B 129     6128   7669   6671    712  -1137    409       C  
ATOM   3631  N   ARG B 130      25.897  -1.260  78.296  1.00 56.31           N  
ANISOU 3631  N   ARG B 130     5936   8394   7067    641  -1168    503       N  
ATOM   3632  CA  ARG B 130      27.016  -0.332  78.392  1.00 59.19           C  
ANISOU 3632  CA  ARG B 130     6079   8962   7449    532  -1241    571       C  
ATOM   3633  C   ARG B 130      26.762   0.875  77.498  1.00 58.88           C  
ANISOU 3633  C   ARG B 130     5988   8934   7448    375  -1168    532       C  
ATOM   3634  O   ARG B 130      26.814   2.010  77.968  1.00 58.79           O  
ANISOU 3634  O   ARG B 130     5968   8946   7424    166  -1236    529       O  
ATOM   3635  CB  ARG B 130      28.352  -1.012  78.042  1.00 65.52           C  
ANISOU 3635  CB  ARG B 130     6655   9965   8274    720  -1259    671       C  
ATOM   3636  CG  ARG B 130      28.731  -2.136  79.001  1.00 71.51           C  
ANISOU 3636  CG  ARG B 130     7456  10725   8991    877  -1352    723       C  
ATOM   3637  CD  ARG B 130      30.027  -2.841  78.625  1.00 79.87           C  
ANISOU 3637  CD  ARG B 130     8291  11988  10068   1097  -1361    825       C  
ATOM   3638  NE  ARG B 130      31.123  -2.428  79.501  1.00 91.03           N  
ANISOU 3638  NE  ARG B 130     9512  13605  11470   1018  -1511    929       N  
ATOM   3639  CZ  ARG B 130      31.870  -1.336  79.312  1.00 97.30           C  
ANISOU 3639  CZ  ARG B 130    10084  14591  12295    847  -1552    988       C  
ATOM   3640  NH1 ARG B 130      31.645  -0.543  78.258  1.00 94.81           N  
ANISOU 3640  NH1 ARG B 130     9714  14286  12023    749  -1444    951       N  
ATOM   3641  NH2 ARG B 130      32.850  -1.040  80.170  1.00 94.54           N  
ANISOU 3641  NH2 ARG B 130     9569  14422  11929    767  -1708   1089       N  
ATOM   3642  N   ASP B 131      26.445   0.636  76.226  1.00 56.90           N  
ANISOU 3642  N   ASP B 131     5729   8654   7236    474  -1034    498       N  
ATOM   3643  CA  ASP B 131      26.194   1.731  75.318  1.00 58.62           C  
ANISOU 3643  CA  ASP B 131     5906   8880   7487    338   -961    466       C  
ATOM   3644  C   ASP B 131      25.072   2.644  75.821  1.00 58.04           C  
ANISOU 3644  C   ASP B 131     6019   8645   7388    144   -973    387       C  
ATOM   3645  O   ASP B 131      25.159   3.879  75.683  1.00 56.95           O  
ANISOU 3645  O   ASP B 131     5842   8538   7258    -37   -989    384       O  
ATOM   3646  CB  ASP B 131      25.860   1.257  73.903  1.00 59.24           C  
ANISOU 3646  CB  ASP B 131     5988   8924   7595    482   -815    431       C  
ATOM   3647  CG  ASP B 131      25.503   2.440  72.974  1.00 66.72           C  
ANISOU 3647  CG  ASP B 131     6913   9866   8571    332   -741    397       C  
ATOM   3648  OD1 ASP B 131      26.451   3.125  72.515  1.00 71.38           O  
ANISOU 3648  OD1 ASP B 131     7304  10631   9187    268   -743    465       O  
ATOM   3649  OD2 ASP B 131      24.289   2.716  72.732  1.00 61.96           O  
ANISOU 3649  OD2 ASP B 131     6485   9092   7964    271   -685    313       O  
ATOM   3650  N   PHE B 132      24.015   2.053  76.387  1.00 54.27           N  
ANISOU 3650  N   PHE B 132     5748   7997   6876    183   -962    328       N  
ATOM   3651  CA  PHE B 132      22.901   2.884  76.807  1.00 50.94           C  
ANISOU 3651  CA  PHE B 132     5496   7435   6424     30   -954    256       C  
ATOM   3652  C   PHE B 132      23.255   3.668  78.066  1.00 51.52           C  
ANISOU 3652  C   PHE B 132     5591   7539   6445   -125  -1083    275       C  
ATOM   3653  O   PHE B 132      22.824   4.811  78.232  1.00 50.70           O  
ANISOU 3653  O   PHE B 132     5563   7381   6320   -283  -1092    233       O  
ATOM   3654  CB  PHE B 132      21.596   2.118  77.007  1.00 49.64           C  
ANISOU 3654  CB  PHE B 132     5531   7097   6234     98   -896    199       C  
ATOM   3655  CG  PHE B 132      20.593   2.916  77.770  1.00 51.46           C  
ANISOU 3655  CG  PHE B 132     5919   7219   6416    -41   -905    146       C  
ATOM   3656  CD1 PHE B 132      19.908   3.949  77.151  1.00 49.26           C  
ANISOU 3656  CD1 PHE B 132     5678   6887   6151   -139   -837     93       C  
ATOM   3657  CD2 PHE B 132      20.430   2.730  79.132  1.00 53.14           C  
ANISOU 3657  CD2 PHE B 132     6237   7396   6559    -70   -985    154       C  
ATOM   3658  CE1 PHE B 132      19.022   4.741  77.859  1.00 49.56           C  
ANISOU 3658  CE1 PHE B 132     5862   6833   6135   -245   -840     46       C  
ATOM   3659  CE2 PHE B 132      19.540   3.521  79.844  1.00 54.49           C  
ANISOU 3659  CE2 PHE B 132     6555   7477   6670   -182   -984    106       C  
ATOM   3660  CZ  PHE B 132      18.832   4.530  79.199  1.00 48.99           C  
ANISOU 3660  CZ  PHE B 132     5897   6727   5988   -262   -908     50       C  
ATOM   3661  N   ILE B 133      24.038   3.061  78.953  1.00 51.34           N  
ANISOU 3661  N   ILE B 133     5517   7595   6394    -75  -1188    336       N  
ATOM   3662  CA  ILE B 133      24.431   3.750  80.174  1.00 52.98           C  
ANISOU 3662  CA  ILE B 133     5754   7835   6541   -222  -1327    356       C  
ATOM   3663  C   ILE B 133      25.309   4.928  79.744  1.00 56.82           C  
ANISOU 3663  C   ILE B 133     6084   8449   7057   -379  -1376    394       C  
ATOM   3664  O   ILE B 133      25.213   6.028  80.305  1.00 56.93           O  
ANISOU 3664  O   ILE B 133     6181   8425   7026   -564  -1450    370       O  
ATOM   3665  CB  ILE B 133      25.159   2.815  81.187  1.00 54.08           C  
ANISOU 3665  CB  ILE B 133     5858   8047   6641   -131  -1441    425       C  
ATOM   3666  CG1 ILE B 133      24.230   1.698  81.697  1.00 52.56           C  
ANISOU 3666  CG1 ILE B 133     5850   7711   6409     -2  -1400    394       C  
ATOM   3667  CG2 ILE B 133      25.784   3.596  82.342  1.00 53.48           C  
ANISOU 3667  CG2 ILE B 133     5782   8036   6501   -296  -1604    458       C  
ATOM   3668  CD1 ILE B 133      22.941   2.155  82.346  1.00 49.96           C  
ANISOU 3668  CD1 ILE B 133     5748   7219   6015   -100  -1370    317       C  
ATOM   3669  N   ASN B 134      26.137   4.698  78.723  1.00 60.13           N  
ANISOU 3669  N   ASN B 134     6289   9014   7545   -305  -1332    454       N  
ATOM   3670  CA  ASN B 134      27.074   5.726  78.234  1.00 59.90           C  
ANISOU 3670  CA  ASN B 134     6076   9133   7548   -456  -1375    515       C  
ATOM   3671  C   ASN B 134      26.289   6.876  77.657  1.00 56.85           C  
ANISOU 3671  C   ASN B 134     5803   8629   7167   -603  -1310    444       C  
ATOM   3672  O   ASN B 134      26.612   8.027  77.884  1.00 58.78           O  
ANISOU 3672  O   ASN B 134     6047   8892   7394   -806  -1392    458       O  
ATOM   3673  CB  ASN B 134      28.088   5.168  77.211  1.00 59.37           C  
ANISOU 3673  CB  ASN B 134     5747   9264   7547   -320  -1318    604       C  
ATOM   3674  CG  ASN B 134      29.122   4.230  77.845  1.00 62.75           C  
ANISOU 3674  CG  ASN B 134     6024   9850   7966   -189  -1410    699       C  
ATOM   3675  OD1 ASN B 134      29.505   4.374  79.014  1.00 64.26           O  
ANISOU 3675  OD1 ASN B 134     6231  10073   8112   -280  -1559    732       O  
ATOM   3676  ND2 ASN B 134      29.582   3.260  77.064  1.00 64.12           N  
ANISOU 3676  ND2 ASN B 134     6061  10124   8177     36  -1323    742       N  
ATOM   3677  N   GLN B 135      25.222   6.559  76.942  1.00 57.60           N  
ANISOU 3677  N   GLN B 135     6012   8592   7280   -502  -1170    368       N  
ATOM   3678  CA  GLN B 135      24.376   7.598  76.379  1.00 56.81           C  
ANISOU 3678  CA  GLN B 135     6030   8373   7183   -617  -1103    300       C  
ATOM   3679  C   GLN B 135      23.770   8.433  77.507  1.00 56.59           C  
ANISOU 3679  C   GLN B 135     6207   8214   7078   -762  -1185    244       C  
ATOM   3680  O   GLN B 135      23.778   9.654  77.452  1.00 57.40           O  
ANISOU 3680  O   GLN B 135     6360   8284   7165   -931  -1221    230       O  
ATOM   3681  CB  GLN B 135      23.263   6.982  75.556  1.00 58.09           C  
ANISOU 3681  CB  GLN B 135     6286   8417   7368   -474   -954    233       C  
ATOM   3682  CG  GLN B 135      23.616   6.493  74.159  1.00 58.60           C  
ANISOU 3682  CG  GLN B 135     6202   8567   7495   -353   -847    262       C  
ATOM   3683  CD  GLN B 135      22.336   6.170  73.393  1.00 58.67           C  
ANISOU 3683  CD  GLN B 135     6350   8428   7515   -268   -722    182       C  
ATOM   3684  OE1 GLN B 135      21.422   7.001  73.335  1.00 60.20           O  
ANISOU 3684  OE1 GLN B 135     6673   8506   7694   -366   -693    124       O  
ATOM   3685  NE2 GLN B 135      22.244   4.954  72.837  1.00 56.91           N  
ANISOU 3685  NE2 GLN B 135     6111   8202   7308    -83   -655    181       N  
ATOM   3686  N   TYR B 136      23.260   7.763  78.535  1.00 56.00           N  
ANISOU 3686  N   TYR B 136     6264   8064   6949   -692  -1215    215       N  
ATOM   3687  CA  TYR B 136      22.656   8.447  79.676  1.00 54.61           C  
ANISOU 3687  CA  TYR B 136     6297   7769   6683   -799  -1283    160       C  
ATOM   3688  C   TYR B 136      23.606   9.421  80.386  1.00 55.27           C  
ANISOU 3688  C   TYR B 136     6362   7916   6721   -989  -1445    198       C  
ATOM   3689  O   TYR B 136      23.240  10.566  80.666  1.00 53.82           O  
ANISOU 3689  O   TYR B 136     6332   7634   6484  -1130  -1480    149       O  
ATOM   3690  CB  TYR B 136      22.069   7.438  80.684  1.00 52.51           C  
ANISOU 3690  CB  TYR B 136     6153   7439   6360   -684  -1288    142       C  
ATOM   3691  CG  TYR B 136      21.523   8.110  81.929  1.00 53.29           C  
ANISOU 3691  CG  TYR B 136     6466   7434   6348   -780  -1356     92       C  
ATOM   3692  CD1 TYR B 136      20.308   8.812  81.890  1.00 51.39           C  
ANISOU 3692  CD1 TYR B 136     6408   7051   6067   -803  -1270     11       C  
ATOM   3693  CD2 TYR B 136      22.246   8.095  83.141  1.00 54.21           C  
ANISOU 3693  CD2 TYR B 136     6607   7601   6391   -842  -1508    128       C  
ATOM   3694  CE1 TYR B 136      19.818   9.458  83.014  1.00 51.74           C  
ANISOU 3694  CE1 TYR B 136     6659   7003   5995   -870  -1321    -37       C  
ATOM   3695  CE2 TYR B 136      21.757   8.742  84.265  1.00 54.02           C  
ANISOU 3695  CE2 TYR B 136     6799   7478   6249   -923  -1569     77       C  
ATOM   3696  CZ  TYR B 136      20.544   9.409  84.193  1.00 52.33           C  
ANISOU 3696  CZ  TYR B 136     6770   7121   5992   -929  -1469     -7       C  
ATOM   3697  OH  TYR B 136      20.049  10.043  85.296  1.00 53.90           O  
ANISOU 3697  OH  TYR B 136     7194   7225   6062   -984  -1516    -60       O  
ATOM   3698  N   TYR B 137      24.821   8.972  80.669  1.00 56.49           N  
ANISOU 3698  N   TYR B 137     6337   8235   6893   -993  -1550    289       N  
ATOM   3699  CA  TYR B 137      25.735   9.787  81.452  1.00 60.21           C  
ANISOU 3699  CA  TYR B 137     6789   8774   7314  -1184  -1728    336       C  
ATOM   3700  C   TYR B 137      26.297  10.938  80.651  1.00 61.19           C  
ANISOU 3700  C   TYR B 137     6818   8952   7478  -1363  -1752    370       C  
ATOM   3701  O   TYR B 137      26.533  12.015  81.173  1.00 64.44           O  
ANISOU 3701  O   TYR B 137     7329   9323   7833  -1565  -1873    364       O  
ATOM   3702  CB  TYR B 137      26.815   8.925  82.114  1.00 61.91           C  
ANISOU 3702  CB  TYR B 137     6841   9156   7526  -1131  -1846    431       C  
ATOM   3703  CG  TYR B 137      26.336   8.410  83.455  1.00 62.11           C  
ANISOU 3703  CG  TYR B 137     7054   9089   7455  -1079  -1910    394       C  
ATOM   3704  CD1 TYR B 137      26.486   9.179  84.598  1.00 63.25           C  
ANISOU 3704  CD1 TYR B 137     7348   9189   7496  -1244  -2064    379       C  
ATOM   3705  CD2 TYR B 137      25.678   7.182  83.572  1.00 61.00           C  
ANISOU 3705  CD2 TYR B 137     6967   8893   7315   -872  -1816    372       C  
ATOM   3706  CE1 TYR B 137      26.026   8.731  85.820  1.00 63.69           C  
ANISOU 3706  CE1 TYR B 137     7585   9163   7450  -1193  -2114    345       C  
ATOM   3707  CE2 TYR B 137      25.223   6.725  84.804  1.00 60.57           C  
ANISOU 3707  CE2 TYR B 137     7089   8759   7167   -834  -1869    347       C  
ATOM   3708  CZ  TYR B 137      25.401   7.512  85.914  1.00 60.16           C  
ANISOU 3708  CZ  TYR B 137     7170   8677   7010   -990  -2012    334       C  
ATOM   3709  OH  TYR B 137      24.961   7.104  87.135  1.00 61.88           O  
ANISOU 3709  OH  TYR B 137     7569   8821   7120   -953  -2061    312       O  
ATOM   3710  N   SER B 138      26.484  10.705  79.371  1.00 61.73           N  
ANISOU 3710  N   SER B 138     6712   9105   7639  -1290  -1634    404       N  
ATOM   3711  CA  SER B 138      26.853  11.749  78.452  1.00 64.11           C  
ANISOU 3711  CA  SER B 138     6934   9445   7981  -1444  -1623    436       C  
ATOM   3712  C   SER B 138      25.735  12.823  78.367  1.00 66.23           C  
ANISOU 3712  C   SER B 138     7466   9493   8204  -1537  -1579    330       C  
ATOM   3713  O   SER B 138      26.042  14.030  78.343  1.00 64.38           O  
ANISOU 3713  O   SER B 138     7285   9230   7947  -1747  -1662    343       O  
ATOM   3714  CB  SER B 138      27.165  11.117  77.091  1.00 61.97           C  
ANISOU 3714  CB  SER B 138     6438   9303   7803  -1303  -1483    487       C  
ATOM   3715  OG  SER B 138      27.110  12.066  76.056  1.00 64.94           O  
ANISOU 3715  OG  SER B 138     6795   9667   8213  -1416  -1422    492       O  
ATOM   3716  N   SER B 139      24.459  12.394  78.352  1.00 61.70           N  
ANISOU 3716  N   SER B 139     7061   8769   7615  -1386  -1457    234       N  
ATOM   3717  CA  SER B 139      23.320  13.334  78.297  1.00 62.81           C  
ANISOU 3717  CA  SER B 139     7445   8711   7709  -1435  -1403    138       C  
ATOM   3718  C   SER B 139      23.312  14.344  79.460  1.00 65.89           C  
ANISOU 3718  C   SER B 139     8050   8995   7991  -1600  -1546    101       C  
ATOM   3719  O   SER B 139      23.080  15.531  79.260  1.00 69.00           O  
ANISOU 3719  O   SER B 139     8582   9281   8353  -1731  -1566     67       O  
ATOM   3720  CB  SER B 139      21.985  12.600  78.271  1.00 60.39           C  
ANISOU 3720  CB  SER B 139     7261   8290   7395  -1244  -1264     58       C  
ATOM   3721  OG  SER B 139      21.487  12.420  79.591  1.00 63.99           O  
ANISOU 3721  OG  SER B 139     7895   8662   7758  -1221  -1318     12       O  
ATOM   3722  N   ILE B 140      23.571  13.853  80.664  1.00 64.79           N  
ANISOU 3722  N   ILE B 140     7953   8878   7787  -1588  -1648    107       N  
ATOM   3723  CA  ILE B 140      23.618  14.669  81.883  1.00 66.63           C  
ANISOU 3723  CA  ILE B 140     8403   9015   7898  -1730  -1796     71       C  
ATOM   3724  C   ILE B 140      25.004  15.294  82.138  1.00 69.92           C  
ANISOU 3724  C   ILE B 140     8712   9545   8308  -1955  -1990    159       C  
ATOM   3725  O   ILE B 140      25.264  15.848  83.216  1.00 69.07           O  
ANISOU 3725  O   ILE B 140     8765   9382   8096  -2088  -2149    144       O  
ATOM   3726  CB  ILE B 140      23.174  13.827  83.110  1.00 65.04           C  
ANISOU 3726  CB  ILE B 140     8317   8782   7615  -1608  -1815     37       C  
ATOM   3727  CG1 ILE B 140      24.182  12.701  83.392  1.00 62.62           C  
ANISOU 3727  CG1 ILE B 140     7782   8660   7351  -1554  -1887    132       C  
ATOM   3728  CG2 ILE B 140      21.768  13.255  82.883  1.00 63.34           C  
ANISOU 3728  CG2 ILE B 140     8203   8460   7401  -1412  -1630    -37       C  
ATOM   3729  CD1 ILE B 140      24.037  12.045  84.749  1.00 64.15           C  
ANISOU 3729  CD1 ILE B 140     8094   8833   7446  -1489  -1960    120       C  
ATOM   3730  N   LYS B 141      25.884  15.179  81.142  1.00 72.91           N  
ANISOU 3730  N   LYS B 141     8818  10091   8793  -1997  -1978    256       N  
ATOM   3731  CA  LYS B 141      27.230  15.767  81.155  1.00 82.78           C  
ANISOU 3731  CA  LYS B 141     9909  11486  10057  -2222  -2145    365       C  
ATOM   3732  C   LYS B 141      28.230  15.073  82.110  1.00 86.54           C  
ANISOU 3732  C   LYS B 141    10241  12128  10511  -2237  -2300    449       C  
ATOM   3733  O   LYS B 141      29.413  15.432  82.141  1.00 84.59           O  
ANISOU 3733  O   LYS B 141     9818  12040  10282  -2417  -2446    559       O  
ATOM   3734  CB  LYS B 141      27.172  17.289  81.417  1.00 88.21           C  
ANISOU 3734  CB  LYS B 141    10830  12019  10666  -2470  -2262    329       C  
ATOM   3735  CG  LYS B 141      26.260  18.066  80.473  1.00 91.63           C  
ANISOU 3735  CG  LYS B 141    11407  12290  11117  -2461  -2125    258       C  
ATOM   3736  CD  LYS B 141      26.993  18.495  79.207  1.00 98.20           C  
ANISOU 3736  CD  LYS B 141    12016  13248  12047  -2580  -2100    357       C  
ATOM   3737  CE  LYS B 141      26.049  18.564  78.015  1.00102.86           C  
ANISOU 3737  CE  LYS B 141    12638  13750  12694  -2447  -1896    303       C  
ATOM   3738  NZ  LYS B 141      24.815  19.345  78.306  1.00107.64           N  
ANISOU 3738  NZ  LYS B 141    13589  14093  13215  -2427  -1858    174       N  
ATOM   3739  N   ARG B 142      27.763  14.071  82.858  1.00 86.36           N  
ANISOU 3739  N   ARG B 142    10283  12079  10451  -2051  -2270    406       N  
ATOM   3740  CA  ARG B 142      28.603  13.382  83.852  1.00 90.84           C  
ANISOU 3740  CA  ARG B 142    10748  12783  10984  -2045  -2418    479       C  
ATOM   3741  C   ARG B 142      29.443  12.214  83.285  1.00 86.65           C  
ANISOU 3741  C   ARG B 142     9878  12489  10558  -1890  -2373    591       C  
ATOM   3742  O   ARG B 142      29.853  11.317  84.022  1.00 81.86           O  
ANISOU 3742  O   ARG B 142     9201  11973   9929  -1790  -2442    636       O  
ATOM   3743  CB  ARG B 142      27.762  12.941  85.069  1.00 96.96           C  
ANISOU 3743  CB  ARG B 142    11782  13412  11647  -1939  -2430    389       C  
ATOM   3744  CG  ARG B 142      27.216  14.083  85.925  1.00100.91           C  
ANISOU 3744  CG  ARG B 142    12615  13714  12011  -2095  -2522    295       C  
ATOM   3745  CD  ARG B 142      28.339  14.944  86.490  1.00111.98           C  
ANISOU 3745  CD  ARG B 142    14004  15184  13360  -2364  -2764    363       C  
ATOM   3746  NE  ARG B 142      27.895  16.272  86.929  1.00120.21           N  
ANISOU 3746  NE  ARG B 142    15366  16021  14288  -2541  -2844    275       N  
ATOM   3747  CZ  ARG B 142      27.838  17.363  86.158  1.00121.42           C  
ANISOU 3747  CZ  ARG B 142    15574  16093  14466  -2689  -2832    260       C  
ATOM   3748  NH1 ARG B 142      28.181  17.315  84.873  1.00118.73           N  
ANISOU 3748  NH1 ARG B 142    14981  15868  14262  -2690  -2734    330       N  
ATOM   3749  NH2 ARG B 142      27.427  18.514  86.676  1.00120.87           N  
ANISOU 3749  NH2 ARG B 142    15832  15819  14274  -2830  -2916    175       N  
ATOM   3750  N   SER B 143      29.716  12.269  81.981  1.00 85.60           N  
ANISOU 3750  N   SER B 143     9544  12453  10527  -1869  -2261    640       N  
ATOM   3751  CA  SER B 143      30.512  11.265  81.254  1.00 85.97           C  
ANISOU 3751  CA  SER B 143     9270  12726  10668  -1707  -2194    745       C  
ATOM   3752  C   SER B 143      31.938  11.066  81.819  1.00 88.69           C  
ANISOU 3752  C   SER B 143     9369  13315  11014  -1787  -2374    888       C  
ATOM   3753  O   SER B 143      32.702  12.023  81.952  1.00 87.36           O  
ANISOU 3753  O   SER B 143     9127  13231  10833  -2039  -2519    961       O  
ATOM   3754  CB  SER B 143      30.581  11.674  79.774  1.00 86.31           C  
ANISOU 3754  CB  SER B 143     9172  12824  10798  -1721  -2057    771       C  
ATOM   3755  OG  SER B 143      30.580  10.553  78.910  1.00 81.43           O  
ANISOU 3755  OG  SER B 143     8390  12298  10251  -1466  -1897    792       O  
ATOM   3756  N   GLY B 144      32.287   9.821  82.147  1.00 90.14           N  
ANISOU 3756  N   GLY B 144     9428  13612  11210  -1574  -2370    935       N  
ATOM   3757  CA  GLY B 144      33.605   9.494  82.703  1.00 87.60           C  
ANISOU 3757  CA  GLY B 144     8860  13536  10889  -1607  -2535   1078       C  
ATOM   3758  C   GLY B 144      33.695   9.565  84.221  1.00 90.64           C  
ANISOU 3758  C   GLY B 144     9404  13866  11168  -1707  -2737   1067       C  
ATOM   3759  O   GLY B 144      34.608   8.991  84.816  1.00 96.66           O  
ANISOU 3759  O   GLY B 144     9993  14812  11923  -1667  -2864   1173       O  
ATOM   3760  N   SER B 145      32.748  10.259  84.852  1.00 89.34           N  
ANISOU 3760  N   SER B 145     9573  13456  10916  -1823  -2764    942       N  
ATOM   3761  CA  SER B 145      32.720  10.450  86.309  1.00 89.70           C  
ANISOU 3761  CA  SER B 145     9823  13421  10837  -1928  -2949    914       C  
ATOM   3762  C   SER B 145      32.648   9.156  87.109  1.00 90.70           C  
ANISOU 3762  C   SER B 145     9965  13568  10927  -1703  -2958    923       C  
ATOM   3763  O   SER B 145      32.563   8.055  86.552  1.00 90.21           O  
ANISOU 3763  O   SER B 145     9777  13562  10936  -1454  -2819    943       O  
ATOM   3764  CB  SER B 145      31.516  11.302  86.702  1.00 90.02           C  
ANISOU 3764  CB  SER B 145    10242  13177  10786  -2022  -2919    762       C  
ATOM   3765  OG  SER B 145      30.304  10.589  86.482  1.00 88.70           O  
ANISOU 3765  OG  SER B 145    10223  12856  10624  -1791  -2719    659       O  
ATOM   3766  N   GLN B 146      32.650   9.306  88.428  1.00 90.27           N  
ANISOU 3766  N   GLN B 146    10095  13451  10753  -1794  -3126    904       N  
ATOM   3767  CA  GLN B 146      32.556   8.165  89.321  1.00 91.42           C  
ANISOU 3767  CA  GLN B 146    10292  13599  10844  -1606  -3154    914       C  
ATOM   3768  C   GLN B 146      31.183   7.525  89.255  1.00 85.09           C  
ANISOU 3768  C   GLN B 146     9717  12588  10025  -1405  -2956    795       C  
ATOM   3769  O   GLN B 146      31.085   6.310  89.111  1.00 83.22           O  
ANISOU 3769  O   GLN B 146     9408  12385   9829  -1172  -2867    821       O  
ATOM   3770  CB  GLN B 146      32.897   8.555  90.765  1.00 96.86           C  
ANISOU 3770  CB  GLN B 146    11138  14272  11393  -1768  -3390    923       C  
ATOM   3771  CG  GLN B 146      34.382   8.817  90.999  1.00104.66           C  
ANISOU 3771  CG  GLN B 146    11859  15511  12396  -1930  -3615   1074       C  
ATOM   3772  CD  GLN B 146      35.230   7.550  91.044  1.00105.54           C  
ANISOU 3772  CD  GLN B 146    11689  15848  12564  -1720  -3642   1205       C  
ATOM   3773  OE1 GLN B 146      34.793   6.466  90.633  1.00100.53           O  
ANISOU 3773  OE1 GLN B 146    11025  15189  11982  -1446  -3471   1188       O  
ATOM   3774  NE2 GLN B 146      36.458   7.686  91.547  1.00106.62           N  
ANISOU 3774  NE2 GLN B 146    11620  16205  12686  -1849  -3864   1341       N  
ATOM   3775  N   ALA B 147      30.135   8.344  89.351  1.00 80.71           N  
ANISOU 3775  N   ALA B 147     9435  11823   9409  -1496  -2892    671       N  
ATOM   3776  CA  ALA B 147      28.751   7.851  89.315  1.00 76.71           C  
ANISOU 3776  CA  ALA B 147     9142  11125   8880  -1330  -2707    564       C  
ATOM   3777  C   ALA B 147      28.523   6.987  88.069  1.00 75.79           C  
ANISOU 3777  C   ALA B 147     8855  11047   8896  -1130  -2514    579       C  
ATOM   3778  O   ALA B 147      27.846   5.958  88.132  1.00 76.73           O  
ANISOU 3778  O   ALA B 147     9043  11096   9016   -939  -2406    555       O  
ATOM   3779  CB  ALA B 147      27.755   9.003  89.378  1.00 72.12           C  
ANISOU 3779  CB  ALA B 147     8829  10344   8228  -1455  -2655    443       C  
ATOM   3780  N   HIS B 148      29.116   7.413  86.955  1.00 73.40           N  
ANISOU 3780  N   HIS B 148     8337  10856   8697  -1185  -2480    624       N  
ATOM   3781  CA  HIS B 148      29.141   6.657  85.705  1.00 72.12           C  
ANISOU 3781  CA  HIS B 148     7986  10762   8653  -1004  -2318    651       C  
ATOM   3782  C   HIS B 148      29.856   5.339  85.861  1.00 71.42           C  
ANISOU 3782  C   HIS B 148     7727  10817   8594   -805  -2345    744       C  
ATOM   3783  O   HIS B 148      29.357   4.303  85.434  1.00 69.94           O  
ANISOU 3783  O   HIS B 148     7556  10577   8443   -592  -2214    724       O  
ATOM   3784  CB  HIS B 148      29.808   7.514  84.627  1.00 71.53           C  
ANISOU 3784  CB  HIS B 148     7710  10806   8662  -1133  -2306    698       C  
ATOM   3785  CG  HIS B 148      29.744   6.933  83.237  1.00 70.20           C  
ANISOU 3785  CG  HIS B 148     7379  10693   8602   -963  -2124    712       C  
ATOM   3786  ND1 HIS B 148      30.558   7.347  82.250  1.00 71.48           N  
ANISOU 3786  ND1 HIS B 148     7299  11018   8841  -1020  -2105    788       N  
ATOM   3787  CD2 HIS B 148      28.926   5.959  82.683  1.00 67.13           C  
ANISOU 3787  CD2 HIS B 148     7053  10209   8247   -741  -1957    658       C  
ATOM   3788  CE1 HIS B 148      30.275   6.678  81.121  1.00 68.35           C  
ANISOU 3788  CE1 HIS B 148     6823  10629   8516   -829  -1928    776       C  
ATOM   3789  NE2 HIS B 148      29.289   5.819  81.387  1.00 66.76           N  
ANISOU 3789  NE2 HIS B 148     6812  10265   8290   -662  -1846    695       N  
ATOM   3790  N   GLU B 149      31.025   5.367  86.492  1.00 73.82           N  
ANISOU 3790  N   GLU B 149     7875  11297   8877   -874  -2525    849       N  
ATOM   3791  CA  GLU B 149      31.834   4.177  86.645  1.00 75.12           C  
ANISOU 3791  CA  GLU B 149     7856  11620   9067   -677  -2565    952       C  
ATOM   3792  C   GLU B 149      31.098   3.137  87.476  1.00 72.37           C  
ANISOU 3792  C   GLU B 149     7721  11127   8649   -512  -2546    908       C  
ATOM   3793  O   GLU B 149      31.006   1.984  87.075  1.00 72.09           O  
ANISOU 3793  O   GLU B 149     7645  11092   8656   -277  -2449    926       O  
ATOM   3794  CB  GLU B 149      33.190   4.522  87.283  1.00 82.72           C  
ANISOU 3794  CB  GLU B 149     8616  12806  10009   -809  -2784   1078       C  
ATOM   3795  CG  GLU B 149      34.349   3.663  86.794  1.00 87.67           C  
ANISOU 3795  CG  GLU B 149     8910  13688  10711   -628  -2792   1218       C  
ATOM   3796  CD  GLU B 149      34.763   3.991  85.362  1.00 92.82           C  
ANISOU 3796  CD  GLU B 149     9321  14475  11472   -619  -2666   1259       C  
ATOM   3797  OE1 GLU B 149      33.942   3.787  84.427  1.00 92.39           O  
ANISOU 3797  OE1 GLU B 149     9352  14290  11463   -508  -2470   1174       O  
ATOM   3798  OE2 GLU B 149      35.914   4.453  85.165  1.00 94.35           O  
ANISOU 3798  OE2 GLU B 149     9234  14912  11701   -730  -2765   1384       O  
ATOM   3799  N   GLU B 150      30.568   3.557  88.627  1.00 72.73           N  
ANISOU 3799  N   GLU B 150     8007  11045   8581   -636  -2637    852       N  
ATOM   3800  CA  GLU B 150      29.866   2.659  89.561  1.00 72.57           C  
ANISOU 3800  CA  GLU B 150     8203  10894   8477   -510  -2632    821       C  
ATOM   3801  C   GLU B 150      28.565   2.121  88.965  1.00 68.33           C  
ANISOU 3801  C   GLU B 150     7822  10172   7967   -377  -2423    731       C  
ATOM   3802  O   GLU B 150      28.061   1.098  89.403  1.00 68.47           O  
ANISOU 3802  O   GLU B 150     7962  10105   7949   -230  -2387    730       O  
ATOM   3803  CB  GLU B 150      29.556   3.366  90.887  1.00 73.02           C  
ANISOU 3803  CB  GLU B 150     8493  10860   8392   -683  -2765    777       C  
ATOM   3804  CG  GLU B 150      30.727   3.467  91.855  1.00 82.27           C  
ANISOU 3804  CG  GLU B 150     9571  12188   9500   -773  -3001    875       C  
ATOM   3805  CD  GLU B 150      30.632   4.674  92.786  1.00 85.06           C  
ANISOU 3805  CD  GLU B 150    10117  12473   9729  -1021  -3145    823       C  
ATOM   3806  OE1 GLU B 150      29.571   5.339  92.794  1.00 85.73           O  
ANISOU 3806  OE1 GLU B 150    10435  12375   9764  -1090  -3048    707       O  
ATOM   3807  OE2 GLU B 150      31.623   4.970  93.499  1.00 87.53           O  
ANISOU 3807  OE2 GLU B 150    10352  12916   9988  -1145  -3358    901       O  
ATOM   3808  N   ARG B 151      28.018   2.822  87.982  1.00 63.83           N  
ANISOU 3808  N   ARG B 151     7254   9542   7458   -440  -2296    663       N  
ATOM   3809  CA  ARG B 151      26.786   2.388  87.376  1.00 62.75           C  
ANISOU 3809  CA  ARG B 151     7252   9243   7348   -335  -2111    584       C  
ATOM   3810  C   ARG B 151      27.027   1.246  86.394  1.00 64.18           C  
ANISOU 3810  C   ARG B 151     7288   9473   7624   -120  -2012    626       C  
ATOM   3811  O   ARG B 151      26.265   0.274  86.393  1.00 65.94           O  
ANISOU 3811  O   ARG B 151     7638   9578   7839     20  -1926    603       O  
ATOM   3812  CB  ARG B 151      26.060   3.552  86.710  1.00 59.59           C  
ANISOU 3812  CB  ARG B 151     6921   8753   6968   -472  -2016    496       C  
ATOM   3813  CG  ARG B 151      24.697   3.192  86.156  1.00 56.55           C  
ANISOU 3813  CG  ARG B 151     6680   8206   6602   -382  -1836    416       C  
ATOM   3814  CD  ARG B 151      23.746   2.643  87.203  1.00 53.84           C  
ANISOU 3814  CD  ARG B 151     6564   7733   6161   -338  -1824    386       C  
ATOM   3815  NE  ARG B 151      22.498   2.226  86.562  1.00 54.26           N  
ANISOU 3815  NE  ARG B 151     6715   7657   6246   -258  -1654    330       N  
ATOM   3816  CZ  ARG B 151      21.894   1.046  86.742  1.00 54.18           C  
ANISOU 3816  CZ  ARG B 151     6788   7574   6224   -129  -1599    345       C  
ATOM   3817  NH1 ARG B 151      22.399   0.168  87.603  1.00 53.64           N  
ANISOU 3817  NH1 ARG B 151     6737   7537   6107    -54  -1695    410       N  
ATOM   3818  NH2 ARG B 151      20.758   0.760  86.092  1.00 47.79           N  
ANISOU 3818  NH2 ARG B 151     6056   6656   5447    -85  -1455    300       N  
ATOM   3819  N   LEU B 152      28.069   1.369  85.565  1.00 65.01           N  
ANISOU 3819  N   LEU B 152     7140   9751   7811    -96  -2023    691       N  
ATOM   3820  CA  LEU B 152      28.490   0.286  84.655  1.00 64.82           C  
ANISOU 3820  CA  LEU B 152     6969   9797   7862    133  -1939    740       C  
ATOM   3821  C   LEU B 152      28.869  -0.981  85.454  1.00 65.42           C  
ANISOU 3821  C   LEU B 152     7071   9891   7896    312  -2017    806       C  
ATOM   3822  O   LEU B 152      28.523  -2.102  85.065  1.00 66.42           O  
ANISOU 3822  O   LEU B 152     7259   9937   8040    512  -1931    801       O  
ATOM   3823  CB  LEU B 152      29.670   0.725  83.767  1.00 63.73           C  
ANISOU 3823  CB  LEU B 152     6534   9879   7801    122  -1949    816       C  
ATOM   3824  CG  LEU B 152      29.507   1.894  82.789  1.00 62.42           C  
ANISOU 3824  CG  LEU B 152     6305   9725   7688    -36  -1870    775       C  
ATOM   3825  CD1 LEU B 152      30.864   2.530  82.515  1.00 64.37           C  
ANISOU 3825  CD1 LEU B 152     6263  10220   7974   -131  -1959    883       C  
ATOM   3826  CD2 LEU B 152      28.837   1.473  81.490  1.00 59.59           C  
ANISOU 3826  CD2 LEU B 152     5969   9282   7391    102  -1680    718       C  
ATOM   3827  N   GLN B 153      29.573  -0.782  86.566  1.00 65.70           N  
ANISOU 3827  N   GLN B 153     7072  10023   7869    234  -2189    869       N  
ATOM   3828  CA  GLN B 153      29.907  -1.862  87.488  1.00 65.98           C  
ANISOU 3828  CA  GLN B 153     7154  10069   7848    380  -2284    935       C  
ATOM   3829  C   GLN B 153      28.653  -2.565  87.982  1.00 63.04           C  
ANISOU 3829  C   GLN B 153     7072   9466   7415    437  -2216    869       C  
ATOM   3830  O   GLN B 153      28.588  -3.783  87.957  1.00 62.80           O  
ANISOU 3830  O   GLN B 153     7094   9383   7385    636  -2187    899       O  
ATOM   3831  CB  GLN B 153      30.712  -1.333  88.667  1.00 67.89           C  
ANISOU 3831  CB  GLN B 153     7346  10434   8017    240  -2489   1001       C  
ATOM   3832  CG  GLN B 153      32.220  -1.309  88.452  1.00 75.63           C  
ANISOU 3832  CG  GLN B 153     8006  11683   9046    277  -2598   1127       C  
ATOM   3833  CD  GLN B 153      32.964  -0.480  89.516  1.00 79.20           C  
ANISOU 3833  CD  GLN B 153     8404  12259   9429     65  -2815   1185       C  
ATOM   3834  OE1 GLN B 153      32.584  -0.449  90.698  1.00 78.67           O  
ANISOU 3834  OE1 GLN B 153     8544  12092   9255    -12  -2916   1161       O  
ATOM   3835  NE2 GLN B 153      34.021   0.209  89.089  1.00 78.89           N  
ANISOU 3835  NE2 GLN B 153     8090  12440   9445    -40  -2889   1266       N  
ATOM   3836  N   GLU B 154      27.660  -1.785  88.411  1.00 63.69           N  
ANISOU 3836  N   GLU B 154     7342   9415   7441    264  -2188    783       N  
ATOM   3837  CA  GLU B 154      26.371  -2.300  88.887  1.00 64.27           C  
ANISOU 3837  CA  GLU B 154     7679   9288   7453    287  -2112    726       C  
ATOM   3838  C   GLU B 154      25.718  -3.164  87.828  1.00 64.22           C  
ANISOU 3838  C   GLU B 154     7704   9177   7518    438  -1955    698       C  
ATOM   3839  O   GLU B 154      25.289  -4.287  88.114  1.00 66.77           O  
ANISOU 3839  O   GLU B 154     8160   9398   7813    564  -1936    718       O  
ATOM   3840  CB  GLU B 154      25.411  -1.160  89.258  1.00 63.73           C  
ANISOU 3840  CB  GLU B 154     7771   9119   7325     90  -2076    636       C  
ATOM   3841  CG  GLU B 154      25.522  -0.667  90.690  1.00 66.61           C  
ANISOU 3841  CG  GLU B 154     8260   9489   7561    -34  -2216    644       C  
ATOM   3842  CD  GLU B 154      24.635   0.542  90.998  1.00 69.94           C  
ANISOU 3842  CD  GLU B 154     8845   9814   7915   -208  -2176    550       C  
ATOM   3843  OE1 GLU B 154      23.559   0.705  90.366  1.00 66.73           O  
ANISOU 3843  OE1 GLU B 154     8519   9296   7539   -205  -2020    480       O  
ATOM   3844  OE2 GLU B 154      25.012   1.328  91.908  1.00 71.69           O  
ANISOU 3844  OE2 GLU B 154     9127  10070   8043   -343  -2308    547       O  
ATOM   3845  N   VAL B 155      25.651  -2.632  86.606  1.00 63.00           N  
ANISOU 3845  N   VAL B 155     7439   9046   7451    417  -1851    654       N  
ATOM   3846  CA  VAL B 155      25.008  -3.311  85.474  1.00 59.42           C  
ANISOU 3846  CA  VAL B 155     7019   8493   7063    540  -1704    617       C  
ATOM   3847  C   VAL B 155      25.729  -4.606  85.131  1.00 60.91           C  
ANISOU 3847  C   VAL B 155     7141   8721   7281    775  -1717    685       C  
ATOM   3848  O   VAL B 155      25.074  -5.620  84.888  1.00 59.43           O  
ANISOU 3848  O   VAL B 155     7099   8391   7091    894  -1652    671       O  
ATOM   3849  CB  VAL B 155      24.932  -2.402  84.234  1.00 59.31           C  
ANISOU 3849  CB  VAL B 155     6888   8517   7129    469  -1604    564       C  
ATOM   3850  CG1 VAL B 155      24.774  -3.226  82.964  1.00 56.99           C  
ANISOU 3850  CG1 VAL B 155     6568   8182   6905    639  -1484    552       C  
ATOM   3851  CG2 VAL B 155      23.793  -1.407  84.387  1.00 55.25           C  
ANISOU 3851  CG2 VAL B 155     6514   7892   6585    289  -1546    480       C  
ATOM   3852  N   GLU B 156      27.070  -4.569  85.127  1.00 61.12           N  
ANISOU 3852  N   GLU B 156     6953   8940   7329    842  -1805    763       N  
ATOM   3853  CA  GLU B 156      27.858  -5.778  84.943  1.00 61.41           C  
ANISOU 3853  CA  GLU B 156     6923   9032   7379   1091  -1829    838       C  
ATOM   3854  C   GLU B 156      27.597  -6.784  86.045  1.00 59.67           C  
ANISOU 3854  C   GLU B 156     6894   8700   7079   1171  -1909    874       C  
ATOM   3855  O   GLU B 156      27.328  -7.948  85.745  1.00 59.45           O  
ANISOU 3855  O   GLU B 156     6984   8554   7050   1352  -1863    880       O  
ATOM   3856  CB  GLU B 156      29.351  -5.483  84.829  1.00 67.48           C  
ANISOU 3856  CB  GLU B 156     7401  10058   8180   1142  -1914    930       C  
ATOM   3857  CG  GLU B 156      29.851  -5.688  83.413  1.00 74.27           C  
ANISOU 3857  CG  GLU B 156     8089  11011   9118   1300  -1800    939       C  
ATOM   3858  CD  GLU B 156      31.130  -4.934  83.103  1.00 77.55           C  
ANISOU 3858  CD  GLU B 156     8185  11703   9578   1262  -1850   1021       C  
ATOM   3859  OE1 GLU B 156      32.190  -5.369  83.604  1.00 82.17           O  
ANISOU 3859  OE1 GLU B 156     8620  12454  10148   1379  -1958   1127       O  
ATOM   3860  OE2 GLU B 156      31.075  -3.932  82.334  1.00 75.30           O  
ANISOU 3860  OE2 GLU B 156     7796  11475   9341   1118  -1782    987       O  
ATOM   3861  N   ALA B 157      27.651  -6.332  87.302  1.00 56.44           N  
ANISOU 3861  N   ALA B 157     6533   8317   6596   1033  -2029    898       N  
ATOM   3862  CA  ALA B 157      27.384  -7.206  88.460  1.00 56.39           C  
ANISOU 3862  CA  ALA B 157     6718   8209   6499   1087  -2110    939       C  
ATOM   3863  C   ALA B 157      26.036  -7.904  88.299  1.00 54.12           C  
ANISOU 3863  C   ALA B 157     6681   7688   6193   1105  -1999    883       C  
ATOM   3864  O   ALA B 157      25.933  -9.112  88.500  1.00 54.86           O  
ANISOU 3864  O   ALA B 157     6904   7680   6259   1258  -2012    925       O  
ATOM   3865  CB  ALA B 157      27.449  -6.433  89.779  1.00 54.26           C  
ANISOU 3865  CB  ALA B 157     6493   7987   6139    902  -2238    952       C  
ATOM   3866  N   GLU B 158      25.023  -7.151  87.874  1.00 52.13           N  
ANISOU 3866  N   GLU B 158     6492   7355   5961    950  -1891    796       N  
ATOM   3867  CA  GLU B 158      23.678  -7.670  87.792  1.00 52.20           C  
ANISOU 3867  CA  GLU B 158     6719   7165   5950    927  -1793    752       C  
ATOM   3868  C   GLU B 158      23.461  -8.691  86.643  1.00 53.09           C  
ANISOU 3868  C   GLU B 158     6870   7176   6126   1093  -1703    742       C  
ATOM   3869  O   GLU B 158      22.882  -9.773  86.862  1.00 50.71           O  
ANISOU 3869  O   GLU B 158     6757   6720   5788   1163  -1697    765       O  
ATOM   3870  CB  GLU B 158      22.674  -6.526  87.757  1.00 51.56           C  
ANISOU 3870  CB  GLU B 158     6683   7045   5861    723  -1712    671       C  
ATOM   3871  CG  GLU B 158      21.292  -6.956  88.203  1.00 55.30           C  
ANISOU 3871  CG  GLU B 158     7382   7352   6278    663  -1646    654       C  
ATOM   3872  CD  GLU B 158      20.338  -5.803  88.472  1.00 56.57           C  
ANISOU 3872  CD  GLU B 158     7596   7496   6404    478  -1580    589       C  
ATOM   3873  OE1 GLU B 158      20.817  -4.706  88.828  1.00 58.11           O  
ANISOU 3873  OE1 GLU B 158     7711   7790   6577    382  -1632    566       O  
ATOM   3874  OE2 GLU B 158      19.101  -6.013  88.347  1.00 56.66           O  
ANISOU 3874  OE2 GLU B 158     7734   7391   6403    432  -1481    565       O  
ATOM   3875  N   VAL B 159      23.919  -8.363  85.434  1.00 51.56           N  
ANISOU 3875  N   VAL B 159     6515   7060   6017   1151  -1638    711       N  
ATOM   3876  CA  VAL B 159      23.867  -9.330  84.330  1.00 51.78           C  
ANISOU 3876  CA  VAL B 159     6584   7001   6090   1330  -1564    700       C  
ATOM   3877  C   VAL B 159      24.652 -10.602  84.619  1.00 53.26           C  
ANISOU 3877  C   VAL B 159     6814   7176   6248   1562  -1642    778       C  
ATOM   3878  O   VAL B 159      24.115 -11.703  84.452  1.00 52.73           O  
ANISOU 3878  O   VAL B 159     6946   6931   6159   1661  -1622    779       O  
ATOM   3879  CB  VAL B 159      24.431  -8.761  83.021  1.00 53.19           C  
ANISOU 3879  CB  VAL B 159     6562   7298   6350   1378  -1486    666       C  
ATOM   3880  CG1 VAL B 159      24.436  -9.849  81.932  1.00 54.34           C  
ANISOU 3880  CG1 VAL B 159     6778   7346   6521   1591  -1417    654       C  
ATOM   3881  CG2 VAL B 159      23.674  -7.510  82.607  1.00 48.41           C  
ANISOU 3881  CG2 VAL B 159     5922   6695   5778   1166  -1406    590       C  
ATOM   3882  N   ALA B 160      25.912 -10.439  85.051  1.00 53.87           N  
ANISOU 3882  N   ALA B 160     6709   7440   6321   1643  -1738    847       N  
ATOM   3883  CA  ALA B 160      26.821 -11.556  85.285  1.00 57.05           C  
ANISOU 3883  CA  ALA B 160     7111   7868   6697   1892  -1815    930       C  
ATOM   3884  C   ALA B 160      26.184 -12.609  86.154  1.00 59.80           C  
ANISOU 3884  C   ALA B 160     7733   8020   6969   1924  -1870    961       C  
ATOM   3885  O   ALA B 160      26.396 -13.817  85.943  1.00 63.34           O  
ANISOU 3885  O   ALA B 160     8300   8366   7399   2141  -1883    996       O  
ATOM   3886  CB  ALA B 160      28.138 -11.096  85.916  1.00 56.70           C  
ANISOU 3886  CB  ALA B 160     6830   8068   6646   1920  -1934   1013       C  
ATOM   3887  N   SER B 161      25.406 -12.175  87.138  1.00 58.15           N  
ANISOU 3887  N   SER B 161     7635   7752   6705   1714  -1901    952       N  
ATOM   3888  CA  SER B 161      24.910 -13.144  88.094  1.00 59.88           C  
ANISOU 3888  CA  SER B 161     8097   7814   6842   1735  -1964   1003       C  
ATOM   3889  C   SER B 161      23.437 -13.506  87.923  1.00 56.73           C  
ANISOU 3889  C   SER B 161     7933   7195   6428   1618  -1875    957       C  
ATOM   3890  O   SER B 161      23.001 -14.507  88.466  1.00 60.21           O  
ANISOU 3890  O   SER B 161     8589   7480   6807   1656  -1914   1005       O  
ATOM   3891  CB  SER B 161      25.277 -12.762  89.541  1.00 61.50           C  
ANISOU 3891  CB  SER B 161     8285   8115   6965   1643  -2091   1064       C  
ATOM   3892  OG  SER B 161      24.646 -11.546  89.884  1.00 65.17           O  
ANISOU 3892  OG  SER B 161     8724   8620   7417   1398  -2057   1006       O  
ATOM   3893  N   THR B 162      22.692 -12.754  87.130  1.00 53.74           N  
ANISOU 3893  N   THR B 162     7513   6803   6104   1483  -1762    873       N  
ATOM   3894  CA  THR B 162      21.246 -13.006  86.961  1.00 53.70           C  
ANISOU 3894  CA  THR B 162     7702   6615   6087   1352  -1680    838       C  
ATOM   3895  C   THR B 162      20.766 -13.076  85.505  1.00 53.51           C  
ANISOU 3895  C   THR B 162     7677   6515   6139   1375  -1570    767       C  
ATOM   3896  O   THR B 162      19.576 -13.302  85.265  1.00 55.78           O  
ANISOU 3896  O   THR B 162     8110   6661   6424   1263  -1509    743       O  
ATOM   3897  CB  THR B 162      20.373 -11.917  87.663  1.00 52.61           C  
ANISOU 3897  CB  THR B 162     7559   6515   5913   1110  -1644    809       C  
ATOM   3898  OG1 THR B 162      20.317 -10.720  86.850  1.00 48.50           O  
ANISOU 3898  OG1 THR B 162     6871   6094   5463   1023  -1563    729       O  
ATOM   3899  CG2 THR B 162      20.915 -11.587  89.088  1.00 51.98           C  
ANISOU 3899  CG2 THR B 162     7464   6536   5748   1069  -1754    865       C  
ATOM   3900  N   GLY B 163      21.656 -12.836  84.542  1.00 54.05           N  
ANISOU 3900  N   GLY B 163     7576   6689   6272   1507  -1545    737       N  
ATOM   3901  CA  GLY B 163      21.288 -12.791  83.111  1.00 53.25           C  
ANISOU 3901  CA  GLY B 163     7462   6536   6236   1532  -1439    665       C  
ATOM   3902  C   GLY B 163      20.545 -11.544  82.645  1.00 53.36           C  
ANISOU 3902  C   GLY B 163     7379   6601   6294   1331  -1347    593       C  
ATOM   3903  O   GLY B 163      20.124 -11.435  81.477  1.00 53.37           O  
ANISOU 3903  O   GLY B 163     7377   6558   6345   1330  -1260    533       O  
ATOM   3904  N   THR B 164      20.351 -10.599  83.550  1.00 52.27           N  
ANISOU 3904  N   THR B 164     7180   6549   6131   1166  -1367    597       N  
ATOM   3905  CA  THR B 164      19.648  -9.375  83.197  1.00 51.51           C  
ANISOU 3905  CA  THR B 164     7009   6496   6068    987  -1285    531       C  
ATOM   3906  C   THR B 164      19.992  -8.283  84.214  1.00 51.68           C  
ANISOU 3906  C   THR B 164     6933   6651   6054    866  -1337    540       C  
ATOM   3907  O   THR B 164      20.840  -8.486  85.089  1.00 54.10           O  
ANISOU 3907  O   THR B 164     7211   7029   6317    921  -1440    597       O  
ATOM   3908  CB  THR B 164      18.118  -9.609  83.081  1.00 52.66           C  
ANISOU 3908  CB  THR B 164     7323   6485   6200    864  -1215    507       C  
ATOM   3909  OG1 THR B 164      17.481  -8.448  82.512  1.00 52.79           O  
ANISOU 3909  OG1 THR B 164     7255   6546   6257    728  -1126    440       O  
ATOM   3910  CG2 THR B 164      17.490  -9.957  84.457  1.00 53.74           C  
ANISOU 3910  CG2 THR B 164     7608   6560   6250    775  -1263    565       C  
ATOM   3911  N   TYR B 165      19.357  -7.129  84.070  1.00 48.89           N  
ANISOU 3911  N   TYR B 165     6537   6325   5712    708  -1273    483       N  
ATOM   3912  CA  TYR B 165      19.547  -6.004  84.958  1.00 49.42           C  
ANISOU 3912  CA  TYR B 165     6550   6491   5736    580  -1318    476       C  
ATOM   3913  C   TYR B 165      18.282  -5.147  84.949  1.00 50.33           C  
ANISOU 3913  C   TYR B 165     6733   6554   5837    424  -1226    417       C  
ATOM   3914  O   TYR B 165      17.299  -5.457  84.233  1.00 49.42           O  
ANISOU 3914  O   TYR B 165     6683   6342   5754    414  -1133    392       O  
ATOM   3915  CB  TYR B 165      20.789  -5.188  84.573  1.00 50.70           C  
ANISOU 3915  CB  TYR B 165     6502   6817   5945    592  -1361    473       C  
ATOM   3916  CG  TYR B 165      20.642  -4.292  83.340  1.00 50.28           C  
ANISOU 3916  CG  TYR B 165     6338   6799   5969    538  -1267    409       C  
ATOM   3917  CD1 TYR B 165      20.604  -4.844  82.042  1.00 47.02           C  
ANISOU 3917  CD1 TYR B 165     5891   6350   5625    648  -1187    390       C  
ATOM   3918  CD2 TYR B 165      20.583  -2.882  83.471  1.00 48.15           C  
ANISOU 3918  CD2 TYR B 165     6010   6591   5694    381  -1264    368       C  
ATOM   3919  CE1 TYR B 165      20.495  -4.034  80.920  1.00 46.03           C  
ANISOU 3919  CE1 TYR B 165     5668   6260   5561    601  -1103    338       C  
ATOM   3920  CE2 TYR B 165      20.459  -2.063  82.344  1.00 47.10           C  
ANISOU 3920  CE2 TYR B 165     5785   6484   5628    332  -1181    317       C  
ATOM   3921  CZ  TYR B 165      20.427  -2.635  81.074  1.00 48.12           C  
ANISOU 3921  CZ  TYR B 165     5869   6589   5825    441  -1100    305       C  
ATOM   3922  OH  TYR B 165      20.292  -1.821  79.953  1.00 46.82           O  
ANISOU 3922  OH  TYR B 165     5620   6450   5719    391  -1019    258       O  
ATOM   3923  N   HIS B 166      18.292  -4.096  85.762  1.00 49.75           N  
ANISOU 3923  N   HIS B 166     6654   6542   5708    309  -1256    400       N  
ATOM   3924  CA  HIS B 166      17.162  -3.194  85.840  1.00 50.07           C  
ANISOU 3924  CA  HIS B 166     6759   6543   5721    185  -1170    346       C  
ATOM   3925  C   HIS B 166      17.630  -1.787  85.719  1.00 50.22           C  
ANISOU 3925  C   HIS B 166     6684   6648   5749     97  -1185    296       C  
ATOM   3926  O   HIS B 166      18.777  -1.476  86.068  1.00 52.86           O  
ANISOU 3926  O   HIS B 166     6931   7077   6074     94  -1290    318       O  
ATOM   3927  CB  HIS B 166      16.380  -3.443  87.125  1.00 52.78           C  
ANISOU 3927  CB  HIS B 166     7265   6835   5952    137  -1177    377       C  
ATOM   3928  CG  HIS B 166      15.715  -4.800  87.148  1.00 56.89           C  
ANISOU 3928  CG  HIS B 166     7895   7255   6468    193  -1150    432       C  
ATOM   3929  ND1 HIS B 166      16.394  -5.939  87.449  1.00 58.11           N  
ANISOU 3929  ND1 HIS B 166     8081   7386   6613    295  -1235    496       N  
ATOM   3930  CD2 HIS B 166      14.411  -5.192  86.814  1.00 57.14           C  
ANISOU 3930  CD2 HIS B 166     8008   7198   6506    154  -1051    436       C  
ATOM   3931  CE1 HIS B 166      15.560  -7.002  87.347  1.00 59.54           C  
ANISOU 3931  CE1 HIS B 166     8382   7452   6788    312  -1196    537       C  
ATOM   3932  NE2 HIS B 166      14.349  -6.545  86.952  1.00 61.72           N  
ANISOU 3932  NE2 HIS B 166     8680   7695   7076    216  -1085    502       N  
ATOM   3933  N   LEU B 167      16.760  -0.935  85.186  1.00 46.80           N  
ANISOU 3933  N   LEU B 167     6266   6183   5334     23  -1088    236       N  
ATOM   3934  CA  LEU B 167      17.062   0.478  84.964  1.00 46.01           C  
ANISOU 3934  CA  LEU B 167     6105   6137   5241    -70  -1093    184       C  
ATOM   3935  C   LEU B 167      16.587   1.335  86.132  1.00 46.73           C  
ANISOU 3935  C   LEU B 167     6328   6210   5217   -162  -1113    157       C  
ATOM   3936  O   LEU B 167      15.569   1.018  86.758  1.00 47.58           O  
ANISOU 3936  O   LEU B 167     6563   6258   5256   -157  -1057    163       O  
ATOM   3937  CB  LEU B 167      16.343   0.974  83.718  1.00 43.92           C  
ANISOU 3937  CB  LEU B 167     5801   5835   5050    -87   -975    131       C  
ATOM   3938  CG  LEU B 167      16.561   0.386  82.338  1.00 44.30           C  
ANISOU 3938  CG  LEU B 167     5742   5886   5204     -8   -925    134       C  
ATOM   3939  CD1 LEU B 167      15.443   0.956  81.472  1.00 42.45           C  
ANISOU 3939  CD1 LEU B 167     5531   5595   5004    -49   -808     82       C  
ATOM   3940  CD2 LEU B 167      17.925   0.753  81.786  1.00 43.30           C  
ANISOU 3940  CD2 LEU B 167     5452   5868   5133      4   -984    147       C  
ATOM   3941  N   ARG B 168      17.304   2.424  86.402  1.00 46.67           N  
ANISOU 3941  N   ARG B 168     6295   6255   5182   -247  -1190    132       N  
ATOM   3942  CA  ARG B 168      16.890   3.397  87.404  1.00 50.14           C  
ANISOU 3942  CA  ARG B 168     6883   6665   5503   -331  -1211     91       C  
ATOM   3943  C   ARG B 168      15.779   4.239  86.787  1.00 49.09           C  
ANISOU 3943  C   ARG B 168     6803   6469   5382   -357  -1081     25       C  
ATOM   3944  O   ARG B 168      15.795   4.473  85.578  1.00 51.37           O  
ANISOU 3944  O   ARG B 168     6984   6760   5772   -356  -1025      6       O  
ATOM   3945  CB  ARG B 168      18.068   4.296  87.839  1.00 51.53           C  
ANISOU 3945  CB  ARG B 168     7029   6906   5645   -429  -1356     87       C  
ATOM   3946  CG  ARG B 168      19.242   3.616  88.560  1.00 56.64           C  
ANISOU 3946  CG  ARG B 168     7615   7638   6269   -413  -1507    158       C  
ATOM   3947  CD  ARG B 168      18.857   2.305  89.247  1.00 61.53           C  
ANISOU 3947  CD  ARG B 168     8306   8229   6843   -308  -1496    210       C  
ATOM   3948  NE  ARG B 168      19.925   1.685  90.061  1.00 64.35           N  
ANISOU 3948  NE  ARG B 168     8629   8662   7161   -283  -1647    282       N  
ATOM   3949  CZ  ARG B 168      20.075   0.367  90.250  1.00 65.24           C  
ANISOU 3949  CZ  ARG B 168     8727   8776   7284   -167  -1662    349       C  
ATOM   3950  NH1 ARG B 168      19.244  -0.512  89.677  1.00 61.20           N  
ANISOU 3950  NH1 ARG B 168     8241   8189   6823    -79  -1542    355       N  
ATOM   3951  NH2 ARG B 168      21.074  -0.085  91.007  1.00 68.25           N  
ANISOU 3951  NH2 ARG B 168     9075   9232   7624   -141  -1807    416       N  
ATOM   3952  N   GLU B 169      14.824   4.697  87.595  1.00 49.32           N  
ANISOU 3952  N   GLU B 169     6994   6445   5300   -370  -1029     -5       N  
ATOM   3953  CA  GLU B 169      13.756   5.568  87.090  1.00 53.40           C  
ANISOU 3953  CA  GLU B 169     7564   6910   5815   -378   -907    -63       C  
ATOM   3954  C   GLU B 169      14.227   6.631  86.089  1.00 52.23           C  
ANISOU 3954  C   GLU B 169     7343   6761   5742   -439   -918   -111       C  
ATOM   3955  O   GLU B 169      13.703   6.707  84.972  1.00 51.34           O  
ANISOU 3955  O   GLU B 169     7158   6632   5717   -415   -822   -126       O  
ATOM   3956  CB  GLU B 169      12.969   6.243  88.219  1.00 59.08           C  
ANISOU 3956  CB  GLU B 169     8477   7590   6380   -382   -875    -98       C  
ATOM   3957  CG  GLU B 169      11.844   7.142  87.699  1.00 62.38           C  
ANISOU 3957  CG  GLU B 169     8947   7962   6792   -363   -744   -152       C  
ATOM   3958  CD  GLU B 169      10.832   7.553  88.762  1.00 70.91           C  
ANISOU 3958  CD  GLU B 169    10208   9018   7718   -319   -671   -172       C  
ATOM   3959  OE1 GLU B 169      11.167   7.504  89.968  1.00 74.34           O  
ANISOU 3959  OE1 GLU B 169    10762   9455   8027   -330   -745   -165       O  
ATOM   3960  OE2 GLU B 169       9.684   7.919  88.385  1.00 75.88           O  
ANISOU 3960  OE2 GLU B 169    10855   9631   8343   -266   -536   -189       O  
ATOM   3961  N   SER B 170      15.215   7.435  86.481  1.00 50.52           N  
ANISOU 3961  N   SER B 170     7147   6562   5487   -528  -1041   -128       N  
ATOM   3962  CA  SER B 170      15.683   8.519  85.628  1.00 51.69           C  
ANISOU 3962  CA  SER B 170     7243   6705   5691   -609  -1062   -163       C  
ATOM   3963  C   SER B 170      16.253   7.993  84.294  1.00 49.50           C  
ANISOU 3963  C   SER B 170     6752   6491   5565   -589  -1040   -126       C  
ATOM   3964  O   SER B 170      16.076   8.626  83.250  1.00 44.41           O  
ANISOU 3964  O   SER B 170     6059   5828   4985   -612   -980   -153       O  
ATOM   3965  CB  SER B 170      16.699   9.413  86.363  1.00 52.70           C  
ANISOU 3965  CB  SER B 170     7437   6843   5744   -734  -1221   -174       C  
ATOM   3966  OG  SER B 170      17.929   8.728  86.504  1.00 54.88           O  
ANISOU 3966  OG  SER B 170     7567   7222   6062   -756  -1341   -105       O  
ATOM   3967  N   GLU B 171      16.933   6.845  84.330  1.00 47.83           N  
ANISOU 3967  N   GLU B 171     6424   6351   5398   -534  -1086    -64       N  
ATOM   3968  CA  GLU B 171      17.432   6.234  83.089  1.00 45.23           C  
ANISOU 3968  CA  GLU B 171     5909   6081   5195   -482  -1053    -30       C  
ATOM   3969  C   GLU B 171      16.273   5.827  82.163  1.00 44.45           C  
ANISOU 3969  C   GLU B 171     5817   5921   5152   -404   -905    -53       C  
ATOM   3970  O   GLU B 171      16.261   6.126  80.958  1.00 42.25           O  
ANISOU 3970  O   GLU B 171     5452   5648   4953   -404   -845    -67       O  
ATOM   3971  CB  GLU B 171      18.317   5.039  83.414  1.00 45.35           C  
ANISOU 3971  CB  GLU B 171     5829   6174   5228   -409  -1129     40       C  
ATOM   3972  CG  GLU B 171      19.597   5.386  84.183  1.00 44.80           C  
ANISOU 3972  CG  GLU B 171     5708   6195   5119   -486  -1289     80       C  
ATOM   3973  CD  GLU B 171      20.260   4.152  84.806  1.00 46.17           C  
ANISOU 3973  CD  GLU B 171     5830   6432   5282   -393  -1367    151       C  
ATOM   3974  OE1 GLU B 171      19.620   3.084  84.834  1.00 43.80           O  
ANISOU 3974  OE1 GLU B 171     5580   6077   4984   -282  -1301    162       O  
ATOM   3975  OE2 GLU B 171      21.422   4.236  85.285  1.00 49.49           O  
ANISOU 3975  OE2 GLU B 171     6161   6954   5687   -435  -1502    202       O  
ATOM   3976  N   LEU B 172      15.281   5.155  82.730  1.00 46.04           N  
ANISOU 3976  N   LEU B 172     6122   6067   5305   -347   -850    -50       N  
ATOM   3977  CA  LEU B 172      14.056   4.853  81.992  1.00 42.34           C  
ANISOU 3977  CA  LEU B 172     5671   5543   4874   -298   -722    -65       C  
ATOM   3978  C   LEU B 172      13.428   6.114  81.406  1.00 42.53           C  
ANISOU 3978  C   LEU B 172     5726   5532   4904   -345   -652   -122       C  
ATOM   3979  O   LEU B 172      13.067   6.138  80.213  1.00 42.28           O  
ANISOU 3979  O   LEU B 172     5626   5489   4950   -325   -579   -134       O  
ATOM   3980  CB  LEU B 172      13.063   4.133  82.879  1.00 42.66           C  
ANISOU 3980  CB  LEU B 172     5822   5543   4843   -260   -682    -42       C  
ATOM   3981  CG  LEU B 172      11.696   3.840  82.282  1.00 44.05           C  
ANISOU 3981  CG  LEU B 172     6017   5676   5046   -230   -559    -43       C  
ATOM   3982  CD1 LEU B 172      11.706   2.565  81.438  1.00 43.00           C  
ANISOU 3982  CD1 LEU B 172     5812   5529   4996   -175   -546     -5       C  
ATOM   3983  CD2 LEU B 172      10.716   3.745  83.426  1.00 43.61           C  
ANISOU 3983  CD2 LEU B 172     6084   5603   4884   -227   -518    -25       C  
ATOM   3984  N   VAL B 173      13.314   7.170  82.210  1.00 41.78           N  
ANISOU 3984  N   VAL B 173     5746   5411   4719   -402   -679   -159       N  
ATOM   3985  CA  VAL B 173      12.814   8.452  81.673  1.00 43.28           C  
ANISOU 3985  CA  VAL B 173     5985   5554   4905   -440   -625   -213       C  
ATOM   3986  C   VAL B 173      13.650   8.922  80.462  1.00 43.50           C  
ANISOU 3986  C   VAL B 173     5887   5610   5030   -490   -648   -216       C  
ATOM   3987  O   VAL B 173      13.085   9.285  79.410  1.00 42.46           O  
ANISOU 3987  O   VAL B 173     5726   5454   4954   -475   -565   -236       O  
ATOM   3988  CB  VAL B 173      12.685   9.560  82.748  1.00 43.82           C  
ANISOU 3988  CB  VAL B 173     6229   5574   4848   -487   -665   -258       C  
ATOM   3989  CG1 VAL B 173      12.182  10.855  82.123  1.00 42.27           C  
ANISOU 3989  CG1 VAL B 173     6098   5313   4648   -510   -611   -313       C  
ATOM   3990  CG2 VAL B 173      11.711   9.128  83.838  1.00 41.27           C  
ANISOU 3990  CG2 VAL B 173     6026   5233   4420   -420   -612   -252       C  
ATOM   3991  N   PHE B 174      14.974   8.860  80.586  1.00 42.07           N  
ANISOU 3991  N   PHE B 174     5621   5494   4868   -545   -758   -185       N  
ATOM   3992  CA  PHE B 174      15.844   9.252  79.485  1.00 43.34           C  
ANISOU 3992  CA  PHE B 174     5644   5708   5115   -596   -777   -170       C  
ATOM   3993  C   PHE B 174      15.665   8.373  78.253  1.00 42.43           C  
ANISOU 3993  C   PHE B 174     5402   5621   5097   -506   -689   -150       C  
ATOM   3994  O   PHE B 174      15.559   8.886  77.135  1.00 43.65           O  
ANISOU 3994  O   PHE B 174     5507   5772   5307   -521   -633   -163       O  
ATOM   3995  CB  PHE B 174      17.317   9.284  79.907  1.00 46.81           C  
ANISOU 3995  CB  PHE B 174     5991   6240   5554   -671   -913   -123       C  
ATOM   3996  CG  PHE B 174      18.258   9.528  78.755  1.00 48.86           C  
ANISOU 3996  CG  PHE B 174     6074   6586   5903   -713   -921    -86       C  
ATOM   3997  CD1 PHE B 174      18.469  10.829  78.272  1.00 48.90           C  
ANISOU 3997  CD1 PHE B 174     6096   6570   5912   -836   -937   -102       C  
ATOM   3998  CD2 PHE B 174      18.914   8.467  78.134  1.00 48.01           C  
ANISOU 3998  CD2 PHE B 174     5795   6578   5868   -622   -907    -33       C  
ATOM   3999  CE1 PHE B 174      19.313  11.054  77.200  1.00 51.42           C  
ANISOU 3999  CE1 PHE B 174     6248   6980   6308   -880   -935    -57       C  
ATOM   4000  CE2 PHE B 174      19.774   8.697  77.057  1.00 52.31           C  
ANISOU 4000  CE2 PHE B 174     6171   7220   6486   -648   -898      7       C  
ATOM   4001  CZ  PHE B 174      19.972   9.988  76.593  1.00 50.92           C  
ANISOU 4001  CZ  PHE B 174     5997   7035   6314   -783   -911     -1       C  
ATOM   4002  N   GLY B 175      15.614   7.055  78.456  1.00 43.09           N  
ANISOU 4002  N   GLY B 175     5453   5724   5193   -412   -682   -118       N  
ATOM   4003  CA  GLY B 175      15.369   6.085  77.369  1.00 39.47           C  
ANISOU 4003  CA  GLY B 175     4915   5271   4811   -317   -608   -103       C  
ATOM   4004  C   GLY B 175      14.098   6.279  76.553  1.00 39.42           C  
ANISOU 4004  C   GLY B 175     4957   5194   4827   -298   -498   -139       C  
ATOM   4005  O   GLY B 175      14.131   6.218  75.326  1.00 42.14           O  
ANISOU 4005  O   GLY B 175     5227   5548   5234   -272   -448   -143       O  
ATOM   4006  N   ALA B 176      12.977   6.518  77.219  1.00 40.39           N  
ANISOU 4006  N   ALA B 176     5199   5255   4891   -306   -460   -161       N  
ATOM   4007  CA  ALA B 176      11.686   6.696  76.546  1.00 39.35           C  
ANISOU 4007  CA  ALA B 176     5103   5073   4775   -284   -360   -183       C  
ATOM   4008  C   ALA B 176      11.681   7.918  75.623  1.00 42.17           C  
ANISOU 4008  C   ALA B 176     5442   5420   5162   -328   -327   -217       C  
ATOM   4009  O   ALA B 176      11.212   7.842  74.484  1.00 44.00           O  
ANISOU 4009  O   ALA B 176     5630   5642   5447   -302   -265   -223       O  
ATOM   4010  CB  ALA B 176      10.565   6.802  77.578  1.00 40.40           C  
ANISOU 4010  CB  ALA B 176     5353   5169   4829   -278   -324   -187       C  
ATOM   4011  N   LYS B 177      12.224   9.041  76.097  1.00 45.09           N  
ANISOU 4011  N   LYS B 177     5856   5787   5491   -400   -378   -238       N  
ATOM   4012  CA  LYS B 177      12.350  10.255  75.262  1.00 41.38           C  
ANISOU 4012  CA  LYS B 177     5384   5297   5043   -457   -362   -263       C  
ATOM   4013  C   LYS B 177      13.251   9.977  74.064  1.00 39.84           C  
ANISOU 4013  C   LYS B 177     5042   5164   4931   -464   -366   -236       C  
ATOM   4014  O   LYS B 177      12.949  10.364  72.942  1.00 39.88           O  
ANISOU 4014  O   LYS B 177     5019   5157   4977   -461   -307   -245       O  
ATOM   4015  CB  LYS B 177      12.881  11.438  76.079  1.00 40.93           C  
ANISOU 4015  CB  LYS B 177     5423   5212   4917   -551   -440   -285       C  
ATOM   4016  CG  LYS B 177      11.927  11.924  77.167  1.00 42.11           C  
ANISOU 4016  CG  LYS B 177     5745   5290   4966   -527   -421   -322       C  
ATOM   4017  CD  LYS B 177      12.608  12.989  78.040  1.00 45.50           C  
ANISOU 4017  CD  LYS B 177     6294   5679   5313   -624   -522   -347       C  
ATOM   4018  CE  LYS B 177      11.673  13.578  79.089  1.00 46.17           C  
ANISOU 4018  CE  LYS B 177     6578   5686   5279   -582   -496   -393       C  
ATOM   4019  NZ  LYS B 177      12.445  14.145  80.238  1.00 50.05           N  
ANISOU 4019  NZ  LYS B 177     7195   6150   5674   -667   -618   -411       N  
ATOM   4020  N   GLN B 178      14.341   9.275  74.304  1.00 38.51           N  
ANISOU 4020  N   GLN B 178     4781   5072   4781   -460   -430   -198       N  
ATOM   4021  CA  GLN B 178      15.301   8.925  73.251  1.00 39.12           C  
ANISOU 4021  CA  GLN B 178     4706   5232   4925   -444   -427   -163       C  
ATOM   4022  C   GLN B 178      14.680   7.963  72.185  1.00 39.92           C  
ANISOU 4022  C   GLN B 178     4776   5319   5074   -336   -340   -167       C  
ATOM   4023  O   GLN B 178      14.887   8.098  70.954  1.00 36.62           O  
ANISOU 4023  O   GLN B 178     4287   4929   4699   -322   -293   -163       O  
ATOM   4024  CB  GLN B 178      16.484   8.284  73.961  1.00 39.99           C  
ANISOU 4024  CB  GLN B 178     4733   5432   5031   -436   -516   -117       C  
ATOM   4025  CG  GLN B 178      17.834   8.669  73.455  1.00 45.63           C  
ANISOU 4025  CG  GLN B 178     5297   6261   5781   -491   -560    -69       C  
ATOM   4026  CD  GLN B 178      18.047  10.155  73.326  1.00 45.21           C  
ANISOU 4026  CD  GLN B 178     5270   6195   5715   -640   -590    -75       C  
ATOM   4027  OE1 GLN B 178      17.602  10.976  74.149  1.00 49.96           O  
ANISOU 4027  OE1 GLN B 178     6012   6713   6257   -720   -632   -111       O  
ATOM   4028  NE2 GLN B 178      18.757  10.508  72.301  1.00 45.54           N  
ANISOU 4028  NE2 GLN B 178     5185   6315   5802   -675   -570    -38       N  
ATOM   4029  N   ALA B 179      13.868   7.019  72.662  1.00 39.01           N  
ANISOU 4029  N   ALA B 179     4728   5155   4941   -270   -324   -173       N  
ATOM   4030  CA  ALA B 179      13.088   6.144  71.766  1.00 38.61           C  
ANISOU 4030  CA  ALA B 179     4683   5066   4921   -192   -258   -178       C  
ATOM   4031  C   ALA B 179      12.195   6.927  70.820  1.00 37.49           C  
ANISOU 4031  C   ALA B 179     4566   4883   4795   -217   -188   -207       C  
ATOM   4032  O   ALA B 179      12.092   6.609  69.613  1.00 36.68           O  
ANISOU 4032  O   ALA B 179     4426   4782   4729   -177   -145   -210       O  
ATOM   4033  CB  ALA B 179      12.236   5.191  72.578  1.00 37.47           C  
ANISOU 4033  CB  ALA B 179     4623   4868   4746   -156   -261   -170       C  
ATOM   4034  N   TRP B 180      11.546   7.946  71.368  1.00 38.24           N  
ANISOU 4034  N   TRP B 180     4735   4940   4854   -273   -179   -228       N  
ATOM   4035  CA  TRP B 180      10.695   8.853  70.584  1.00 37.65           C  
ANISOU 4035  CA  TRP B 180     4693   4827   4787   -290   -119   -252       C  
ATOM   4036  C   TRP B 180      11.530   9.627  69.602  1.00 37.98           C  
ANISOU 4036  C   TRP B 180     4672   4900   4860   -332   -119   -251       C  
ATOM   4037  O   TRP B 180      11.244   9.648  68.408  1.00 44.19           O  
ANISOU 4037  O   TRP B 180     5429   5684   5678   -309    -69   -254       O  
ATOM   4038  CB  TRP B 180       9.911   9.783  71.525  1.00 38.46           C  
ANISOU 4038  CB  TRP B 180     4902   4882   4829   -317   -112   -274       C  
ATOM   4039  CG  TRP B 180       8.893  10.677  70.838  1.00 37.49           C  
ANISOU 4039  CG  TRP B 180     4823   4716   4705   -309    -48   -293       C  
ATOM   4040  CD1 TRP B 180       8.483  10.647  69.498  1.00 35.61           C  
ANISOU 4040  CD1 TRP B 180     4538   4478   4514   -287     -1   -291       C  
ATOM   4041  CD2 TRP B 180       8.113  11.743  71.461  1.00 36.16           C  
ANISOU 4041  CD2 TRP B 180     4764   4500   4476   -306    -24   -317       C  
ATOM   4042  NE1 TRP B 180       7.528  11.608  69.268  1.00 39.84           N  
ANISOU 4042  NE1 TRP B 180     5135   4974   5028   -275     44   -305       N  
ATOM   4043  CE2 TRP B 180       7.282  12.319  70.404  1.00 38.78           C  
ANISOU 4043  CE2 TRP B 180     5096   4808   4830   -278     36   -322       C  
ATOM   4044  CE3 TRP B 180       8.043  12.288  72.756  1.00 40.53           C  
ANISOU 4044  CE3 TRP B 180     5425   5025   4951   -314    -48   -336       C  
ATOM   4045  CZ2 TRP B 180       6.405  13.374  70.653  1.00 39.01           C  
ANISOU 4045  CZ2 TRP B 180     5223   4790   4809   -246     75   -342       C  
ATOM   4046  CZ3 TRP B 180       7.156  13.354  72.995  1.00 38.55           C  
ANISOU 4046  CZ3 TRP B 180     5285   4721   4643   -279     -4   -362       C  
ATOM   4047  CH2 TRP B 180       6.350  13.871  71.972  1.00 38.58           C  
ANISOU 4047  CH2 TRP B 180     5279   4705   4673   -239     58   -363       C  
ATOM   4048  N   ARG B 181      12.614  10.218  70.089  1.00 37.78           N  
ANISOU 4048  N   ARG B 181     4621   4911   4822   -400   -179   -239       N  
ATOM   4049  CA  ARG B 181      13.560  10.922  69.241  1.00 36.53           C  
ANISOU 4049  CA  ARG B 181     4385   4802   4691   -460   -187   -219       C  
ATOM   4050  C   ARG B 181      14.091  10.074  68.090  1.00 36.10           C  
ANISOU 4050  C   ARG B 181     4213   4819   4685   -393   -148   -194       C  
ATOM   4051  O   ARG B 181      14.280  10.569  66.984  1.00 39.06           O  
ANISOU 4051  O   ARG B 181     4545   5215   5080   -410   -108   -185       O  
ATOM   4052  CB  ARG B 181      14.720  11.436  70.094  1.00 37.45           C  
ANISOU 4052  CB  ARG B 181     4475   4968   4788   -555   -278   -194       C  
ATOM   4053  CG  ARG B 181      15.696  12.380  69.409  1.00 36.91           C  
ANISOU 4053  CG  ARG B 181     4333   4953   4738   -659   -300   -160       C  
ATOM   4054  CD  ARG B 181      16.877  12.591  70.341  1.00 40.72           C  
ANISOU 4054  CD  ARG B 181     4766   5504   5203   -753   -407   -121       C  
ATOM   4055  NE  ARG B 181      17.782  13.614  69.841  1.00 43.43           N  
ANISOU 4055  NE  ARG B 181     5047   5897   5556   -889   -445    -77       N  
ATOM   4056  CZ  ARG B 181      18.877  14.037  70.465  1.00 44.47           C  
ANISOU 4056  CZ  ARG B 181     5124   6098   5675  -1012   -550    -29       C  
ATOM   4057  NH1 ARG B 181      19.243  13.525  71.631  1.00 44.39           N  
ANISOU 4057  NH1 ARG B 181     5112   6117   5636  -1007   -631    -24       N  
ATOM   4058  NH2 ARG B 181      19.608  14.986  69.912  1.00 47.72           N  
ANISOU 4058  NH2 ARG B 181     5482   6552   6097  -1152   -581     21       N  
ATOM   4059  N   ASN B 182      14.380   8.817  68.350  1.00 35.01           N  
ANISOU 4059  N   ASN B 182     4033   4716   4555   -310   -160   -181       N  
ATOM   4060  CA  ASN B 182      14.904   7.961  67.328  1.00 34.84           C  
ANISOU 4060  CA  ASN B 182     3925   4753   4562   -221   -123   -162       C  
ATOM   4061  C   ASN B 182      13.880   7.347  66.376  1.00 37.06           C  
ANISOU 4061  C   ASN B 182     4262   4968   4850   -147    -60   -191       C  
ATOM   4062  O   ASN B 182      14.276   6.633  65.451  1.00 36.93           O  
ANISOU 4062  O   ASN B 182     4201   4986   4845    -64    -28   -184       O  
ATOM   4063  CB  ASN B 182      15.669   6.852  68.002  1.00 38.43           C  
ANISOU 4063  CB  ASN B 182     4329   5259   5013   -148   -170   -135       C  
ATOM   4064  CG  ASN B 182      16.903   7.364  68.736  1.00 40.62           C  
ANISOU 4064  CG  ASN B 182     4513   5634   5287   -217   -242    -92       C  
ATOM   4065  OD1 ASN B 182      17.500   8.390  68.353  1.00 38.34           O  
ANISOU 4065  OD1 ASN B 182     4157   5402   5007   -310   -246    -68       O  
ATOM   4066  ND2 ASN B 182      17.259   6.679  69.820  1.00 36.71           N  
ANISOU 4066  ND2 ASN B 182     4019   5156   4774   -185   -307    -75       N  
ATOM   4067  N   ALA B 183      12.582   7.569  66.625  1.00 35.82           N  
ANISOU 4067  N   ALA B 183     4205   4723   4681   -170    -45   -219       N  
ATOM   4068  CA  ALA B 183      11.489   6.961  65.835  1.00 33.96           C  
ANISOU 4068  CA  ALA B 183     4023   4428   4450   -121     -3   -238       C  
ATOM   4069  C   ALA B 183      11.367   7.540  64.418  1.00 36.23           C  
ANISOU 4069  C   ALA B 183     4293   4722   4749   -123     48   -246       C  
ATOM   4070  O   ALA B 183      10.754   8.604  64.223  1.00 37.87           O  
ANISOU 4070  O   ALA B 183     4532   4902   4954   -178     69   -254       O  
ATOM   4071  CB  ALA B 183      10.162   7.154  66.558  1.00 30.53           C  
ANISOU 4071  CB  ALA B 183     3672   3929   3998   -152     -1   -249       C  
ATOM   4072  N   PRO B 184      11.883   6.818  63.412  1.00 36.23           N  
ANISOU 4072  N   PRO B 184     4259   4753   4754    -51     71   -243       N  
ATOM   4073  CA  PRO B 184      11.924   7.303  62.009  1.00 35.62           C  
ANISOU 4073  CA  PRO B 184     4163   4694   4676    -45    123   -245       C  
ATOM   4074  C   PRO B 184      10.537   7.666  61.393  1.00 33.98           C  
ANISOU 4074  C   PRO B 184     4032   4413   4464    -69    144   -266       C  
ATOM   4075  O   PRO B 184      10.432   8.571  60.571  1.00 32.51           O  
ANISOU 4075  O   PRO B 184     3842   4235   4277   -100    177   -263       O  
ATOM   4076  CB  PRO B 184      12.576   6.128  61.252  1.00 37.25           C  
ANISOU 4076  CB  PRO B 184     4351   4932   4871     69    141   -245       C  
ATOM   4077  CG  PRO B 184      13.228   5.281  62.316  1.00 37.11           C  
ANISOU 4077  CG  PRO B 184     4311   4935   4855    115     96   -231       C  
ATOM   4078  CD  PRO B 184      12.338   5.419  63.528  1.00 36.65           C  
ANISOU 4078  CD  PRO B 184     4314   4810   4802     45     52   -239       C  
ATOM   4079  N   ARG B 185       9.487   6.978  61.790  1.00 34.44           N  
ANISOU 4079  N   ARG B 185     4155   4410   4520    -59    123   -277       N  
ATOM   4080  CA  ARG B 185       8.138   7.239  61.213  1.00 35.42           C  
ANISOU 4080  CA  ARG B 185     4331   4486   4641    -80    135   -283       C  
ATOM   4081  C   ARG B 185       7.347   8.353  61.863  1.00 36.79           C  
ANISOU 4081  C   ARG B 185     4517   4645   4815   -134    143   -277       C  
ATOM   4082  O   ARG B 185       6.168   8.553  61.518  1.00 43.57           O  
ANISOU 4082  O   ARG B 185     5404   5479   5671   -140    152   -273       O  
ATOM   4083  CB  ARG B 185       7.315   5.934  61.172  1.00 35.69           C  
ANISOU 4083  CB  ARG B 185     4423   4469   4668    -55    104   -284       C  
ATOM   4084  CG  ARG B 185       8.050   4.856  60.349  1.00 37.71           C  
ANISOU 4084  CG  ARG B 185     4703   4717   4907     20     98   -299       C  
ATOM   4085  CD  ARG B 185       7.351   3.521  60.183  1.00 36.97           C  
ANISOU 4085  CD  ARG B 185     4700   4549   4796     38     53   -303       C  
ATOM   4086  NE  ARG B 185       7.979   2.744  59.090  1.00 42.99           N  
ANISOU 4086  NE  ARG B 185     5515   5293   5527    124     57   -328       N  
ATOM   4087  CZ  ARG B 185       7.696   1.472  58.765  1.00 43.02           C  
ANISOU 4087  CZ  ARG B 185     5629   5215   5500    160     12   -342       C  
ATOM   4088  NH1 ARG B 185       6.775   0.769  59.409  1.00 41.75           N  
ANISOU 4088  NH1 ARG B 185     5531   4988   5344    100    -47   -323       N  
ATOM   4089  NH2 ARG B 185       8.334   0.892  57.767  1.00 42.38           N  
ANISOU 4089  NH2 ARG B 185     5609   5118   5376    258     25   -370       N  
ATOM   4090  N   CYS B 186       7.961   9.062  62.820  1.00 35.26           N  
ANISOU 4090  N   CYS B 186     4310   4468   4619   -168    134   -276       N  
ATOM   4091  CA  CYS B 186       7.249  10.065  63.605  1.00 34.26           C  
ANISOU 4091  CA  CYS B 186     4225   4316   4478   -200    139   -277       C  
ATOM   4092  C   CYS B 186       7.524  11.503  63.179  1.00 33.26           C  
ANISOU 4092  C   CYS B 186     4115   4179   4344   -239    156   -281       C  
ATOM   4093  O   CYS B 186       8.667  11.983  63.257  1.00 35.07           O  
ANISOU 4093  O   CYS B 186     4320   4431   4574   -284    139   -276       O  
ATOM   4094  CB  CYS B 186       7.512   9.907  65.120  1.00 37.69           C  
ANISOU 4094  CB  CYS B 186     4675   4751   4893   -214    107   -277       C  
ATOM   4095  SG  CYS B 186       6.496  11.051  66.103  1.00 38.41           S  
ANISOU 4095  SG  CYS B 186     4845   4807   4944   -222    125   -285       S  
ATOM   4096  N   VAL B 187       6.457  12.194  62.772  1.00 33.32           N  
ANISOU 4096  N   VAL B 187     4165   4153   4341   -225    183   -281       N  
ATOM   4097  CA  VAL B 187       6.549  13.550  62.260  1.00 31.51           C  
ANISOU 4097  CA  VAL B 187     3978   3894   4101   -253    197   -281       C  
ATOM   4098  C   VAL B 187       6.504  14.552  63.405  1.00 33.98           C  
ANISOU 4098  C   VAL B 187     4370   4161   4380   -275    183   -294       C  
ATOM   4099  O   VAL B 187       6.816  15.727  63.211  1.00 36.78           O  
ANISOU 4099  O   VAL B 187     4785   4473   4717   -315    178   -295       O  
ATOM   4100  CB  VAL B 187       5.468  13.882  61.193  1.00 33.05           C  
ANISOU 4100  CB  VAL B 187     4191   4072   4295   -214    228   -271       C  
ATOM   4101  CG1 VAL B 187       4.041  14.023  61.803  1.00 30.80           C  
ANISOU 4101  CG1 VAL B 187     3938   3772   3993   -160    243   -266       C  
ATOM   4102  CG2 VAL B 187       5.861  15.157  60.449  1.00 31.06           C  
ANISOU 4102  CG2 VAL B 187     3982   3788   4032   -249    238   -264       C  
ATOM   4103  N   GLY B 188       6.134  14.084  64.594  1.00 36.59           N  
ANISOU 4103  N   GLY B 188     4715   4494   4692   -251    173   -302       N  
ATOM   4104  CA  GLY B 188       5.933  14.953  65.758  1.00 33.51           C  
ANISOU 4104  CA  GLY B 188     4423   4058   4251   -251    165   -320       C  
ATOM   4105  C   GLY B 188       7.137  15.030  66.681  1.00 37.45           C  
ANISOU 4105  C   GLY B 188     4940   4556   4733   -321    107   -331       C  
ATOM   4106  O   GLY B 188       7.032  15.461  67.834  1.00 37.41           O  
ANISOU 4106  O   GLY B 188     5022   4516   4675   -321     88   -350       O  
ATOM   4107  N   ARG B 189       8.308  14.658  66.178  1.00 37.64           N  
ANISOU 4107  N   ARG B 189     4881   4626   4794   -379     77   -315       N  
ATOM   4108  CA  ARG B 189       9.489  14.606  67.059  1.00 39.67           C  
ANISOU 4108  CA  ARG B 189     5125   4907   5040   -447     13   -312       C  
ATOM   4109  C   ARG B 189      10.059  15.957  67.547  1.00 40.20           C  
ANISOU 4109  C   ARG B 189     5291   4916   5065   -540    -40   -321       C  
ATOM   4110  O   ARG B 189      11.000  15.961  68.340  1.00 40.00           O  
ANISOU 4110  O   ARG B 189     5260   4913   5025   -611   -108   -315       O  
ATOM   4111  CB  ARG B 189      10.572  13.727  66.440  1.00 35.51           C  
ANISOU 4111  CB  ARG B 189     4463   4467   4561   -462      0   -282       C  
ATOM   4112  CG  ARG B 189      10.241  12.242  66.499  1.00 37.71           C  
ANISOU 4112  CG  ARG B 189     4685   4783   4861   -380     17   -279       C  
ATOM   4113  CD  ARG B 189      11.360  11.421  65.850  1.00 40.32           C  
ANISOU 4113  CD  ARG B 189     4899   5193   5226   -367     10   -253       C  
ATOM   4114  NE  ARG B 189      11.294  11.422  64.384  1.00 36.62           N  
ANISOU 4114  NE  ARG B 189     4394   4740   4781   -342     61   -246       N  
ATOM   4115  CZ  ARG B 189      12.296  11.061  63.585  1.00 39.15           C  
ANISOU 4115  CZ  ARG B 189     4621   5136   5119   -328     73   -221       C  
ATOM   4116  NH1 ARG B 189      13.469  10.663  64.090  1.00 36.37           N  
ANISOU 4116  NH1 ARG B 189     4185   4861   4773   -334     36   -194       N  
ATOM   4117  NH2 ARG B 189      12.126  11.071  62.262  1.00 37.66           N  
ANISOU 4117  NH2 ARG B 189     4417   4955   4936   -298    125   -218       N  
ATOM   4118  N   ILE B 190       9.512  17.091  67.077  1.00 38.05           N  
ANISOU 4118  N   ILE B 190     5119   4567   4771   -544    -18   -333       N  
ATOM   4119  CA  ILE B 190       9.906  18.410  67.625  1.00 39.53           C  
ANISOU 4119  CA  ILE B 190     5450   4667   4905   -630    -76   -347       C  
ATOM   4120  C   ILE B 190       9.610  18.389  69.140  1.00 39.99           C  
ANISOU 4120  C   ILE B 190     5613   4686   4894   -602   -107   -383       C  
ATOM   4121  O   ILE B 190      10.284  19.034  69.911  1.00 40.40           O  
ANISOU 4121  O   ILE B 190     5761   4693   4899   -690   -185   -395       O  
ATOM   4122  CB  ILE B 190       9.206  19.618  66.891  1.00 39.86           C  
ANISOU 4122  CB  ILE B 190     5612   4609   4923   -612    -44   -355       C  
ATOM   4123  CG1 ILE B 190       9.836  20.983  67.252  1.00 41.40           C  
ANISOU 4123  CG1 ILE B 190     5967   4699   5064   -729   -120   -362       C  
ATOM   4124  CG2 ILE B 190       7.688  19.675  67.156  1.00 39.27           C  
ANISOU 4124  CG2 ILE B 190     5617   4491   4812   -464     24   -385       C  
ATOM   4125  CD1 ILE B 190      11.246  21.177  66.739  1.00 41.19           C  
ANISOU 4125  CD1 ILE B 190     5853   4723   5074   -893   -181   -311       C  
ATOM   4126  N   GLN B 191       8.615  17.594  69.531  1.00 40.91           N  
ANISOU 4126  N   GLN B 191     5709   4829   5004   -485    -49   -395       N  
ATOM   4127  CA  GLN B 191       8.089  17.530  70.888  1.00 42.20           C  
ANISOU 4127  CA  GLN B 191     5972   4967   5093   -430    -52   -423       C  
ATOM   4128  C   GLN B 191       8.819  16.557  71.805  1.00 44.65           C  
ANISOU 4128  C   GLN B 191     6220   5343   5403   -466   -105   -413       C  
ATOM   4129  O   GLN B 191       8.455  16.453  73.002  1.00 45.65           O  
ANISOU 4129  O   GLN B 191     6433   5453   5458   -426   -111   -432       O  
ATOM   4130  CB  GLN B 191       6.613  17.095  70.849  1.00 43.72           C  
ANISOU 4130  CB  GLN B 191     6153   5180   5280   -294     43   -421       C  
ATOM   4131  CG  GLN B 191       5.631  18.171  70.426  1.00 41.18           C  
ANISOU 4131  CG  GLN B 191     5935   4788   4922   -216     97   -436       C  
ATOM   4132  CD  GLN B 191       5.546  19.298  71.431  1.00 47.64           C  
ANISOU 4132  CD  GLN B 191     6960   5505   5635   -196     75   -480       C  
ATOM   4133  OE1 GLN B 191       5.336  20.448  71.055  1.00 50.26           O  
ANISOU 4133  OE1 GLN B 191     7418   5744   5934   -179     77   -498       O  
ATOM   4134  NE2 GLN B 191       5.712  18.982  72.721  1.00 45.59           N  
ANISOU 4134  NE2 GLN B 191     6756   5254   5312   -193     49   -498       N  
ATOM   4135  N   TRP B 192       9.862  15.896  71.283  1.00 43.32           N  
ANISOU 4135  N   TRP B 192     5911   5249   5302   -531   -143   -379       N  
ATOM   4136  CA  TRP B 192      10.433  14.719  71.921  1.00 41.06           C  
ANISOU 4136  CA  TRP B 192     5535   5038   5030   -530   -180   -359       C  
ATOM   4137  C   TRP B 192      10.898  14.889  73.342  1.00 44.09           C  
ANISOU 4137  C   TRP B 192     6008   5404   5339   -573   -257   -372       C  
ATOM   4138  O   TRP B 192      10.942  13.915  74.098  1.00 42.87           O  
ANISOU 4138  O   TRP B 192     5820   5294   5173   -538   -271   -360       O  
ATOM   4139  CB  TRP B 192      11.530  14.066  71.079  1.00 39.41           C  
ANISOU 4139  CB  TRP B 192     5162   4915   4896   -570   -203   -318       C  
ATOM   4140  CG  TRP B 192      12.862  14.777  71.089  1.00 40.19           C  
ANISOU 4140  CG  TRP B 192     5235   5039   4996   -696   -287   -296       C  
ATOM   4141  CD1 TRP B 192      13.335  15.692  70.153  1.00 40.87           C  
ANISOU 4141  CD1 TRP B 192     5305   5118   5105   -779   -290   -278       C  
ATOM   4142  CD2 TRP B 192      13.945  14.665  72.077  1.00 41.74           C  
ANISOU 4142  CD2 TRP B 192     5410   5282   5167   -774   -389   -276       C  
ATOM   4143  NE1 TRP B 192      14.585  16.138  70.484  1.00 41.58           N  
ANISOU 4143  NE1 TRP B 192     5360   5251   5190   -908   -385   -244       N  
ATOM   4144  CE2 TRP B 192      15.020  15.559  71.609  1.00 42.28           C  
ANISOU 4144  CE2 TRP B 192     5437   5377   5252   -911   -451   -241       C  
ATOM   4145  CE3 TRP B 192      14.135  13.936  73.247  1.00 44.13           C  
ANISOU 4145  CE3 TRP B 192     5720   5611   5435   -750   -439   -275       C  
ATOM   4146  CZ2 TRP B 192      16.217  15.709  72.304  1.00 45.61           C  
ANISOU 4146  CZ2 TRP B 192     5815   5857   5656  -1025   -564   -205       C  
ATOM   4147  CZ3 TRP B 192      15.352  14.082  73.942  1.00 44.39           C  
ANISOU 4147  CZ3 TRP B 192     5719   5699   5450   -852   -554   -244       C  
ATOM   4148  CH2 TRP B 192      16.362  14.959  73.490  1.00 47.13           C  
ANISOU 4148  CH2 TRP B 192     6017   6078   5814   -990   -618   -210       C  
ATOM   4149  N   GLY B 193      11.257  16.110  73.726  1.00 47.96           N  
ANISOU 4149  N   GLY B 193     6626   5823   5772   -654   -316   -396       N  
ATOM   4150  CA  GLY B 193      11.805  16.349  75.070  1.00 48.84           C  
ANISOU 4150  CA  GLY B 193     6842   5912   5802   -713   -411   -412       C  
ATOM   4151  C   GLY B 193      10.729  16.544  76.127  1.00 50.19           C  
ANISOU 4151  C   GLY B 193     7182   6017   5871   -619   -371   -456       C  
ATOM   4152  O   GLY B 193      11.027  16.564  77.308  1.00 54.20           O  
ANISOU 4152  O   GLY B 193     7785   6510   6298   -644   -436   -471       O  
ATOM   4153  N   LYS B 194       9.482  16.673  75.686  1.00 49.14           N  
ANISOU 4153  N   LYS B 194     7077   5856   5737   -508   -261   -470       N  
ATOM   4154  CA  LYS B 194       8.336  16.987  76.527  1.00 50.68           C  
ANISOU 4154  CA  LYS B 194     7420   6003   5833   -396   -197   -503       C  
ATOM   4155  C   LYS B 194       7.471  15.729  76.583  1.00 47.43           C  
ANISOU 4155  C   LYS B 194     6888   5680   5453   -298   -111   -467       C  
ATOM   4156  O   LYS B 194       6.570  15.515  75.766  1.00 46.11           O  
ANISOU 4156  O   LYS B 194     6645   5539   5335   -227    -24   -448       O  
ATOM   4157  CB  LYS B 194       7.577  18.148  75.892  1.00 53.42           C  
ANISOU 4157  CB  LYS B 194     7875   6264   6158   -341   -140   -532       C  
ATOM   4158  CG  LYS B 194       6.591  18.877  76.773  1.00 61.66           C  
ANISOU 4158  CG  LYS B 194     9116   7236   7075   -222    -87   -575       C  
ATOM   4159  CD  LYS B 194       6.226  20.205  76.104  1.00 75.33           C  
ANISOU 4159  CD  LYS B 194    10981   8856   8783   -192    -68   -605       C  
ATOM   4160  CE  LYS B 194       5.597  21.219  77.059  1.00 84.27           C  
ANISOU 4160  CE  LYS B 194    12373   9881   9765    -87    -48   -662       C  
ATOM   4161  NZ  LYS B 194       4.337  20.697  77.664  1.00 82.10           N  
ANISOU 4161  NZ  LYS B 194    12075   9684   9434     90     74   -650       N  
ATOM   4162  N   LEU B 195       7.786  14.852  77.519  1.00 48.27           N  
ANISOU 4162  N   LEU B 195     6973   5836   5532   -307   -146   -449       N  
ATOM   4163  CA  LEU B 195       7.102  13.559  77.580  1.00 44.90           C  
ANISOU 4163  CA  LEU B 195     6435   5487   5137   -242    -82   -404       C  
ATOM   4164  C   LEU B 195       6.986  13.248  79.050  1.00 45.01           C  
ANISOU 4164  C   LEU B 195     6544   5512   5046   -216    -97   -403       C  
ATOM   4165  O   LEU B 195       8.005  13.220  79.766  1.00 43.14           O  
ANISOU 4165  O   LEU B 195     6351   5268   4774   -286   -197   -412       O  
ATOM   4166  CB  LEU B 195       7.902  12.466  76.818  1.00 37.69           C  
ANISOU 4166  CB  LEU B 195     5352   4632   4335   -294   -123   -364       C  
ATOM   4167  CG  LEU B 195       7.412  10.995  76.914  1.00 38.44           C  
ANISOU 4167  CG  LEU B 195     5356   4788   4463   -250    -88   -315       C  
ATOM   4168  CD1 LEU B 195       6.107  10.724  76.137  1.00 34.57           C  
ANISOU 4168  CD1 LEU B 195     4811   4315   4010   -189     10   -291       C  
ATOM   4169  CD2 LEU B 195       8.485  10.037  76.441  1.00 37.31           C  
ANISOU 4169  CD2 LEU B 195     5097   4682   4398   -290   -153   -288       C  
ATOM   4170  N   GLN B 196       5.750  13.070  79.504  1.00 44.32           N  
ANISOU 4170  N   GLN B 196     6487   5450   4901   -118      1   -387       N  
ATOM   4171  CA  GLN B 196       5.491  12.565  80.862  1.00 47.57           C  
ANISOU 4171  CA  GLN B 196     6971   5893   5211    -83      9   -369       C  
ATOM   4172  C   GLN B 196       5.625  11.027  80.930  1.00 44.82           C  
ANISOU 4172  C   GLN B 196     6493   5615   4922   -110     -6   -303       C  
ATOM   4173  O   GLN B 196       4.922  10.301  80.237  1.00 45.67           O  
ANISOU 4173  O   GLN B 196     6485   5766   5102    -89     55   -257       O  
ATOM   4174  CB  GLN B 196       4.101  12.996  81.343  1.00 48.66           C  
ANISOU 4174  CB  GLN B 196     7185   6050   5254     40    132   -365       C  
ATOM   4175  CG  GLN B 196       3.708  12.435  82.702  1.00 55.95           C  
ANISOU 4175  CG  GLN B 196     8172   7023   6064     85    162   -334       C  
ATOM   4176  CD  GLN B 196       4.449  13.055  83.888  1.00 63.08           C  
ANISOU 4176  CD  GLN B 196     9268   7865   6836     68     83   -389       C  
ATOM   4177  OE1 GLN B 196       4.805  14.239  83.891  1.00 62.80           O  
ANISOU 4177  OE1 GLN B 196     9373   7739   6749     64     42   -459       O  
ATOM   4178  NE2 GLN B 196       4.662  12.246  84.920  1.00 66.23           N  
ANISOU 4178  NE2 GLN B 196     9688   8304   7171     53     54   -355       N  
ATOM   4179  N   VAL B 197       6.505  10.544  81.791  1.00 43.43           N  
ANISOU 4179  N   VAL B 197     6350   5443   4708   -156    -94   -296       N  
ATOM   4180  CA  VAL B 197       6.775   9.126  81.864  1.00 44.02           C  
ANISOU 4180  CA  VAL B 197     6326   5565   4834   -177   -124   -236       C  
ATOM   4181  C   VAL B 197       6.223   8.535  83.148  1.00 45.81           C  
ANISOU 4181  C   VAL B 197     6625   5824   4955   -141    -96   -195       C  
ATOM   4182  O   VAL B 197       6.672   8.884  84.233  1.00 49.36           O  
ANISOU 4182  O   VAL B 197     7194   6260   5300   -148   -148   -217       O  
ATOM   4183  CB  VAL B 197       8.285   8.851  81.772  1.00 43.47           C  
ANISOU 4183  CB  VAL B 197     6211   5491   4813   -249   -251   -241       C  
ATOM   4184  CG1 VAL B 197       8.551   7.368  81.935  1.00 41.38           C  
ANISOU 4184  CG1 VAL B 197     5871   5263   4587   -244   -282   -179       C  
ATOM   4185  CG2 VAL B 197       8.840   9.360  80.429  1.00 43.40           C  
ANISOU 4185  CG2 VAL B 197     6111   5467   4909   -287   -267   -267       C  
ATOM   4186  N   PHE B 198       5.233   7.653  83.035  1.00 44.90           N  
ANISOU 4186  N   PHE B 198     6444   5755   4861   -112    -16   -131       N  
ATOM   4187  CA  PHE B 198       4.749   6.939  84.213  1.00 44.16           C  
ANISOU 4187  CA  PHE B 198     6404   5704   4673    -92     10    -73       C  
ATOM   4188  C   PHE B 198       5.494   5.615  84.343  1.00 45.63           C  
ANISOU 4188  C   PHE B 198     6544   5887   4906   -141    -77    -23       C  
ATOM   4189  O   PHE B 198       5.528   4.819  83.399  1.00 45.61           O  
ANISOU 4189  O   PHE B 198     6439   5878   5013   -163    -88      6       O  
ATOM   4190  CB  PHE B 198       3.242   6.742  84.145  1.00 43.48           C  
ANISOU 4190  CB  PHE B 198     6273   5679   4567    -45    141    -14       C  
ATOM   4191  CG  PHE B 198       2.486   8.032  84.080  1.00 45.82           C  
ANISOU 4191  CG  PHE B 198     6619   5984   4805     34    232    -58       C  
ATOM   4192  CD1 PHE B 198       2.426   8.881  85.196  1.00 45.88           C  
ANISOU 4192  CD1 PHE B 198     6784   5985   4664     97    256    -98       C  
ATOM   4193  CD2 PHE B 198       1.852   8.424  82.900  1.00 44.99           C  
ANISOU 4193  CD2 PHE B 198     6421   5888   4786     54    290    -62       C  
ATOM   4194  CE1 PHE B 198       1.734  10.086  85.142  1.00 46.39           C  
ANISOU 4194  CE1 PHE B 198     6918   6044   4664    192    341   -142       C  
ATOM   4195  CE2 PHE B 198       1.168   9.625  82.835  1.00 45.40           C  
ANISOU 4195  CE2 PHE B 198     6527   5942   4780    144    372   -100       C  
ATOM   4196  CZ  PHE B 198       1.101  10.456  83.960  1.00 49.83           C  
ANISOU 4196  CZ  PHE B 198     7252   6490   5192    220    400   -141       C  
ATOM   4197  N   ASP B 199       6.141   5.428  85.487  1.00 44.31           N  
ANISOU 4197  N   ASP B 199     6467   5719   4651   -149   -147    -18       N  
ATOM   4198  CA  ASP B 199       6.790   4.179  85.818  1.00 46.67           C  
ANISOU 4198  CA  ASP B 199     6746   6016   4970   -175   -229     38       C  
ATOM   4199  C   ASP B 199       5.728   3.223  86.320  1.00 47.78           C  
ANISOU 4199  C   ASP B 199     6897   6190   5068   -168   -157    126       C  
ATOM   4200  O   ASP B 199       5.196   3.426  87.412  1.00 45.69           O  
ANISOU 4200  O   ASP B 199     6723   5959   4676   -146   -109    149       O  
ATOM   4201  CB  ASP B 199       7.792   4.402  86.951  1.00 48.06           C  
ANISOU 4201  CB  ASP B 199     7023   6188   5051   -187   -333     19       C  
ATOM   4202  CG  ASP B 199       8.733   3.225  87.138  1.00 50.34           C  
ANISOU 4202  CG  ASP B 199     7278   6473   5376   -202   -440     69       C  
ATOM   4203  OD1 ASP B 199       8.400   2.116  86.653  1.00 47.48           O  
ANISOU 4203  OD1 ASP B 199     6855   6103   5083   -196   -419    127       O  
ATOM   4204  OD2 ASP B 199       9.811   3.418  87.765  1.00 50.46           O  
ANISOU 4204  OD2 ASP B 199     7333   6492   5348   -219   -553     52       O  
ATOM   4205  N   ALA B 200       5.402   2.187  85.549  1.00 44.98           N  
ANISOU 4205  N   ALA B 200     6458   5825   4808   -192   -148    181       N  
ATOM   4206  CA  ALA B 200       4.430   1.211  86.051  1.00 45.88           C  
ANISOU 4206  CA  ALA B 200     6585   5968   4881   -213    -95    281       C  
ATOM   4207  C   ALA B 200       5.088  -0.138  86.241  1.00 45.91           C  
ANISOU 4207  C   ALA B 200     6611   5923   4909   -239   -191    337       C  
ATOM   4208  O   ALA B 200       4.447  -1.159  86.029  1.00 45.91           O  
ANISOU 4208  O   ALA B 200     6596   5910   4938   -279   -175    416       O  
ATOM   4209  CB  ALA B 200       3.235   1.084  85.115  1.00 43.10           C  
ANISOU 4209  CB  ALA B 200     6138   5641   4595   -234     -4    318       C  
ATOM   4210  N   ARG B 201       6.366  -0.139  86.604  1.00 45.69           N  
ANISOU 4210  N   ARG B 201     6621   5868   4872   -219   -297    301       N  
ATOM   4211  CA  ARG B 201       7.110  -1.386  86.690  1.00 49.04           C  
ANISOU 4211  CA  ARG B 201     7065   6243   5326   -217   -395    350       C  
ATOM   4212  C   ARG B 201       6.735  -2.114  87.961  1.00 53.58           C  
ANISOU 4212  C   ARG B 201     7741   6828   5790   -233   -399    437       C  
ATOM   4213  O   ARG B 201       7.041  -3.293  88.095  1.00 56.72           O  
ANISOU 4213  O   ARG B 201     8176   7175   6200   -237   -465    500       O  
ATOM   4214  CB  ARG B 201       8.624  -1.172  86.581  1.00 46.71           C  
ANISOU 4214  CB  ARG B 201     6747   5938   5065   -180   -509    296       C  
ATOM   4215  CG  ARG B 201       9.086  -0.740  85.188  1.00 48.66           C  
ANISOU 4215  CG  ARG B 201     6882   6173   5432   -167   -510    232       C  
ATOM   4216  CD  ARG B 201      10.576  -0.357  85.167  1.00 47.13           C  
ANISOU 4216  CD  ARG B 201     6645   6002   5261   -141   -613    191       C  
ATOM   4217  NE  ARG B 201      10.806   0.838  85.976  1.00 43.42           N  
ANISOU 4217  NE  ARG B 201     6220   5571   4706   -172   -630    147       N  
ATOM   4218  CZ  ARG B 201      11.999   1.281  86.358  1.00 44.28           C  
ANISOU 4218  CZ  ARG B 201     6317   5713   4797   -180   -735    125       C  
ATOM   4219  NH1 ARG B 201      13.105   0.631  86.010  1.00 40.54           N  
ANISOU 4219  NH1 ARG B 201     5761   5256   4386   -144   -823    149       N  
ATOM   4220  NH2 ARG B 201      12.083   2.388  87.102  1.00 43.79           N  
ANISOU 4220  NH2 ARG B 201     6327   5667   4644   -221   -755     82       N  
ATOM   4221  N   ASP B 202       6.060  -1.414  88.880  1.00 58.86           N  
ANISOU 4221  N   ASP B 202     8464   7557   6342   -236   -325    443       N  
ATOM   4222  CA  ASP B 202       5.502  -2.048  90.082  1.00 61.53           C  
ANISOU 4222  CA  ASP B 202     8896   7923   6560   -255   -300    536       C  
ATOM   4223  C   ASP B 202       4.031  -2.462  89.842  1.00 62.54           C  
ANISOU 4223  C   ASP B 202     8981   8091   6693   -304   -181    622       C  
ATOM   4224  O   ASP B 202       3.086  -2.004  90.491  1.00 69.10           O  
ANISOU 4224  O   ASP B 202     9828   9004   7425   -300    -73    657       O  
ATOM   4225  CB  ASP B 202       5.781  -1.221  91.361  1.00 64.34           C  
ANISOU 4225  CB  ASP B 202     9359   8324   6763   -220   -305    504       C  
ATOM   4226  CG  ASP B 202       4.615  -0.326  91.797  1.00 70.94           C  
ANISOU 4226  CG  ASP B 202    10218   9238   7499   -199   -160    501       C  
ATOM   4227  OD1 ASP B 202       4.220   0.532  90.979  1.00 75.21           O  
ANISOU 4227  OD1 ASP B 202    10687   9791   8097   -179    -94    440       O  
ATOM   4228  OD2 ASP B 202       4.117  -0.470  92.962  1.00 67.66           O  
ANISOU 4228  OD2 ASP B 202     9896   8874   6938   -189   -111    563       O  
ATOM   4229  N   CYS B 203       3.877  -3.350  88.871  1.00 57.90           N  
ANISOU 4229  N   CYS B 203     8336   7445   6219   -349   -208    658       N  
ATOM   4230  CA  CYS B 203       2.582  -3.809  88.390  1.00 56.17           C  
ANISOU 4230  CA  CYS B 203     8056   7254   6031   -420   -125    740       C  
ATOM   4231  C   CYS B 203       2.569  -5.335  88.368  1.00 53.11           C  
ANISOU 4231  C   CYS B 203     7726   6785   5671   -492   -199    840       C  
ATOM   4232  O   CYS B 203       3.433  -5.946  87.757  1.00 54.18           O  
ANISOU 4232  O   CYS B 203     7885   6817   5883   -473   -300    808       O  
ATOM   4233  CB  CYS B 203       2.354  -3.264  86.984  1.00 55.15           C  
ANISOU 4233  CB  CYS B 203     7814   7118   6023   -417    -96    672       C  
ATOM   4234  SG  CYS B 203       0.659  -3.452  86.429  1.00 57.17           S  
ANISOU 4234  SG  CYS B 203     7968   7448   6305   -501     14    767       S  
ATOM   4235  N   SER B 204       1.636  -5.963  89.065  1.00 51.71           N  
ANISOU 4235  N   SER B 204     7579   6649   5419   -568   -150    965       N  
ATOM   4236  CA  SER B 204       1.618  -7.418  89.081  1.00 53.00           C  
ANISOU 4236  CA  SER B 204     7823   6717   5599   -649   -231   1066       C  
ATOM   4237  C   SER B 204       0.297  -8.048  88.638  1.00 54.07           C  
ANISOU 4237  C   SER B 204     7907   6874   5762   -783   -181   1181       C  
ATOM   4238  O   SER B 204       0.079  -9.232  88.886  1.00 54.81           O  
ANISOU 4238  O   SER B 204     8087   6898   5840   -876   -237   1291       O  
ATOM   4239  CB  SER B 204       2.036  -7.952  90.455  1.00 53.95           C  
ANISOU 4239  CB  SER B 204     8074   6828   5597   -640   -273   1133       C  
ATOM   4240  OG  SER B 204       1.150  -7.494  91.455  1.00 55.21           O  
ANISOU 4240  OG  SER B 204     8224   7120   5633   -662   -158   1202       O  
ATOM   4241  N   SER B 205      -0.569  -7.290  87.964  1.00 52.02           N  
ANISOU 4241  N   SER B 205     7511   6708   5546   -800    -86   1164       N  
ATOM   4242  CA  SER B 205      -1.873  -7.834  87.555  1.00 53.24           C  
ANISOU 4242  CA  SER B 205     7593   6910   5726   -940    -43   1287       C  
ATOM   4243  C   SER B 205      -2.604  -6.999  86.489  1.00 52.13           C  
ANISOU 4243  C   SER B 205     7295   6850   5664   -939     29   1244       C  
ATOM   4244  O   SER B 205      -2.429  -5.769  86.414  1.00 50.33           O  
ANISOU 4244  O   SER B 205     7004   6690   5430   -824     98   1142       O  
ATOM   4245  CB  SER B 205      -2.785  -7.982  88.771  1.00 51.38           C  
ANISOU 4245  CB  SER B 205     7351   6806   5364  -1001     50   1429       C  
ATOM   4246  OG  SER B 205      -3.304  -6.704  89.089  1.00 53.53           O  
ANISOU 4246  OG  SER B 205     7519   7240   5579   -912    188   1394       O  
ATOM   4247  N   ALA B 206      -3.427  -7.689  85.682  1.00 53.65           N  
ANISOU 4247  N   ALA B 206     7436   7027   5922  -1073      4   1326       N  
ATOM   4248  CA  ALA B 206      -4.369  -7.060  84.741  1.00 52.97           C  
ANISOU 4248  CA  ALA B 206     7189   7039   5899  -1101     70   1327       C  
ATOM   4249  C   ALA B 206      -5.104  -5.878  85.370  1.00 53.32           C  
ANISOU 4249  C   ALA B 206     7111   7281   5868  -1020    227   1342       C  
ATOM   4250  O   ALA B 206      -5.160  -4.784  84.784  1.00 54.09           O  
ANISOU 4250  O   ALA B 206     7121   7429   6000   -923    284   1248       O  
ATOM   4251  CB  ALA B 206      -5.373  -8.075  84.226  1.00 55.06           C  
ANISOU 4251  CB  ALA B 206     7419   7298   6202  -1292     26   1466       C  
ATOM   4252  N   GLN B 207      -5.659  -6.120  86.554  1.00 55.42           N  
ANISOU 4252  N   GLN B 207     7382   7652   6021  -1055    298   1462       N  
ATOM   4253  CA  GLN B 207      -6.278  -5.103  87.395  1.00 57.40           C  
ANISOU 4253  CA  GLN B 207     7556   8088   6166   -954    455   1483       C  
ATOM   4254  C   GLN B 207      -5.426  -3.848  87.578  1.00 54.07           C  
ANISOU 4254  C   GLN B 207     7186   7644   5713   -766    486   1314       C  
ATOM   4255  O   GLN B 207      -5.893  -2.749  87.357  1.00 51.48           O  
ANISOU 4255  O   GLN B 207     6769   7417   5375   -668    585   1268       O  
ATOM   4256  CB  GLN B 207      -6.611  -5.700  88.765  1.00 61.81           C  
ANISOU 4256  CB  GLN B 207     8172   8722   6592  -1004    502   1619       C  
ATOM   4257  CG  GLN B 207      -8.097  -5.902  89.004  1.00 72.77           C  
ANISOU 4257  CG  GLN B 207     9404  10310   7936  -1103    615   1804       C  
ATOM   4258  CD  GLN B 207      -8.920  -4.646  88.737  1.00 78.09           C  
ANISOU 4258  CD  GLN B 207     9908  11165   8596   -983    762   1782       C  
ATOM   4259  OE1 GLN B 207      -8.489  -3.523  89.029  1.00 81.34           O  
ANISOU 4259  OE1 GLN B 207    10361  11590   8954   -800    827   1654       O  
ATOM   4260  NE2 GLN B 207     -10.119  -4.833  88.187  1.00 78.35           N  
ANISOU 4260  NE2 GLN B 207     9758  11339   8674  -1087    809   1913       N  
ATOM   4261  N   GLU B 208      -4.170  -4.005  87.979  1.00 54.87           N  
ANISOU 4261  N   GLU B 208     7436   7615   5798   -719    393   1226       N  
ATOM   4262  CA  GLU B 208      -3.323  -2.835  88.159  1.00 54.10           C  
ANISOU 4262  CA  GLU B 208     7393   7493   5669   -570    403   1075       C  
ATOM   4263  C   GLU B 208      -2.995  -2.176  86.840  1.00 51.46           C  
ANISOU 4263  C   GLU B 208     6994   7099   5458   -531    371    957       C  
ATOM   4264  O   GLU B 208      -2.921  -0.953  86.765  1.00 55.88           O  
ANISOU 4264  O   GLU B 208     7538   7695   5997   -422    430    864       O  
ATOM   4265  CB  GLU B 208      -2.081  -3.172  88.969  1.00 56.24           C  
ANISOU 4265  CB  GLU B 208     7821   7660   5886   -540    305   1027       C  
ATOM   4266  CG  GLU B 208      -2.450  -3.719  90.352  1.00 61.59           C  
ANISOU 4266  CG  GLU B 208     8574   8406   6421   -569    347   1146       C  
ATOM   4267  CD  GLU B 208      -1.255  -4.239  91.141  1.00 65.99           C  
ANISOU 4267  CD  GLU B 208     9289   8859   6926   -554    233   1120       C  
ATOM   4268  OE1 GLU B 208      -0.190  -4.522  90.543  1.00 69.12           O  
ANISOU 4268  OE1 GLU B 208     9723   9126   7415   -545    107   1041       O  
ATOM   4269  OE2 GLU B 208      -1.376  -4.353  92.375  1.00 68.84           O  
ANISOU 4269  OE2 GLU B 208     9733   9277   7146   -541    270   1183       O  
ATOM   4270  N   MET B 209      -2.831  -2.965  85.787  1.00 48.41           N  
ANISOU 4270  N   MET B 209     6582   6620   5193   -617    280    963       N  
ATOM   4271  CA  MET B 209      -2.652  -2.372  84.460  1.00 47.76           C  
ANISOU 4271  CA  MET B 209     6430   6496   5222   -586    260    866       C  
ATOM   4272  C   MET B 209      -3.811  -1.426  84.137  1.00 46.92           C  
ANISOU 4272  C   MET B 209     6191   6528   5108   -550    384    887       C  
ATOM   4273  O   MET B 209      -3.603  -0.294  83.689  1.00 45.19           O  
ANISOU 4273  O   MET B 209     5949   6314   4907   -452    418    785       O  
ATOM   4274  CB  MET B 209      -2.520  -3.441  83.381  1.00 48.07           C  
ANISOU 4274  CB  MET B 209     6467   6425   5371   -687    156    886       C  
ATOM   4275  CG  MET B 209      -1.264  -4.301  83.482  1.00 50.66           C  
ANISOU 4275  CG  MET B 209     6927   6604   5718   -685     31    847       C  
ATOM   4276  SD  MET B 209      -1.216  -5.643  82.267  1.00 52.79           S  
ANISOU 4276  SD  MET B 209     7234   6731   6091   -789    -87    876       S  
ATOM   4277  CE  MET B 209      -1.167  -4.735  80.720  1.00 50.62           C  
ANISOU 4277  CE  MET B 209     6859   6454   5919   -738    -73    764       C  
ATOM   4278  N   PHE B 210      -5.029  -1.886  84.403  1.00 47.17           N  
ANISOU 4278  N   PHE B 210     6136   6678   5107   -628    451   1028       N  
ATOM   4279  CA  PHE B 210      -6.193  -1.083  84.120  1.00 48.99           C  
ANISOU 4279  CA  PHE B 210     6222   7063   5329   -586    570   1070       C  
ATOM   4280  C   PHE B 210      -6.185   0.273  84.845  1.00 49.64           C  
ANISOU 4280  C   PHE B 210     6331   7223   5308   -412    684    998       C  
ATOM   4281  O   PHE B 210      -6.401   1.314  84.217  1.00 49.87           O  
ANISOU 4281  O   PHE B 210     6305   7280   5365   -318    733    929       O  
ATOM   4282  CB  PHE B 210      -7.465  -1.860  84.407  1.00 48.87           C  
ANISOU 4282  CB  PHE B 210     6096   7185   5286   -707    621   1254       C  
ATOM   4283  CG  PHE B 210      -8.706  -1.105  84.057  1.00 51.30           C  
ANISOU 4283  CG  PHE B 210     6226   7675   5591   -662    741   1315       C  
ATOM   4284  CD1 PHE B 210      -8.912  -0.660  82.761  1.00 50.08           C  
ANISOU 4284  CD1 PHE B 210     5981   7505   5540   -655    714   1264       C  
ATOM   4285  CD2 PHE B 210      -9.672  -0.831  85.024  1.00 54.33           C  
ANISOU 4285  CD2 PHE B 210     6528   8256   5860   -614    884   1430       C  
ATOM   4286  CE1 PHE B 210     -10.064   0.028  82.425  1.00 52.19           C  
ANISOU 4286  CE1 PHE B 210     6078   7947   5805   -603    818   1328       C  
ATOM   4287  CE2 PHE B 210     -10.834  -0.142  84.692  1.00 54.95           C  
ANISOU 4287  CE2 PHE B 210     6426   8520   5934   -553    999   1497       C  
ATOM   4288  CZ  PHE B 210     -11.032   0.283  83.383  1.00 52.20           C  
ANISOU 4288  CZ  PHE B 210     5986   8151   5697   -548    961   1447       C  
ATOM   4289  N   THR B 211      -5.930   0.258  86.154  1.00 50.26           N  
ANISOU 4289  N   THR B 211     6511   7324   5261   -368    719   1013       N  
ATOM   4290  CA  THR B 211      -5.766   1.491  86.917  1.00 51.88           C  
ANISOU 4290  CA  THR B 211     6793   7568   5350   -204    806    930       C  
ATOM   4291  C   THR B 211      -4.715   2.376  86.266  1.00 50.57           C  
ANISOU 4291  C   THR B 211     6702   7268   5243   -133    734    762       C  
ATOM   4292  O   THR B 211      -4.989   3.532  85.950  1.00 50.40           O  
ANISOU 4292  O   THR B 211     6664   7277   5209    -22    801    696       O  
ATOM   4293  CB  THR B 211      -5.394   1.227  88.392  1.00 53.62           C  
ANISOU 4293  CB  THR B 211     7151   7797   5424   -182    818    955       C  
ATOM   4294  OG1 THR B 211      -6.474   0.522  89.013  1.00 54.06           O  
ANISOU 4294  OG1 THR B 211     7127   8000   5412   -242    907   1125       O  
ATOM   4295  CG2 THR B 211      -5.187   2.555  89.140  1.00 53.33           C  
ANISOU 4295  CG2 THR B 211     7227   7780   5257    -10    894    854       C  
ATOM   4296  N   TYR B 212      -3.530   1.821  86.038  1.00 47.78           N  
ANISOU 4296  N   TYR B 212     6427   6773   4955   -197    597    701       N  
ATOM   4297  CA  TYR B 212      -2.486   2.574  85.389  1.00 48.14           C  
ANISOU 4297  CA  TYR B 212     6524   6706   5062   -151    524    560       C  
ATOM   4298  C   TYR B 212      -2.919   3.133  84.038  1.00 46.72           C  
ANISOU 4298  C   TYR B 212     6234   6530   4988   -138    546    526       C  
ATOM   4299  O   TYR B 212      -2.634   4.295  83.726  1.00 46.87           O  
ANISOU 4299  O   TYR B 212     6284   6521   5005    -53    563    428       O  
ATOM   4300  CB  TYR B 212      -1.240   1.719  85.208  1.00 50.40           C  
ANISOU 4300  CB  TYR B 212     6870   6866   5415   -223    380    527       C  
ATOM   4301  CG  TYR B 212      -0.308   1.720  86.387  1.00 49.70           C  
ANISOU 4301  CG  TYR B 212     6919   6739   5227   -196    327    495       C  
ATOM   4302  CD1 TYR B 212       0.367   2.885  86.762  1.00 50.67           C  
ANISOU 4302  CD1 TYR B 212     7130   6834   5289   -116    317    387       C  
ATOM   4303  CD2 TYR B 212      -0.067   0.552  87.100  1.00 50.40           C  
ANISOU 4303  CD2 TYR B 212     7060   6809   5282   -258    272    573       C  
ATOM   4304  CE1 TYR B 212       1.241   2.899  87.833  1.00 51.97           C  
ANISOU 4304  CE1 TYR B 212     7423   6965   5359   -103    252    359       C  
ATOM   4305  CE2 TYR B 212       0.806   0.543  88.173  1.00 54.66           C  
ANISOU 4305  CE2 TYR B 212     7724   7317   5728   -232    212    547       C  
ATOM   4306  CZ  TYR B 212       1.458   1.719  88.528  1.00 55.58           C  
ANISOU 4306  CZ  TYR B 212     7917   7417   5785   -157    200    440       C  
ATOM   4307  OH  TYR B 212       2.318   1.706  89.579  1.00 57.00           O  
ANISOU 4307  OH  TYR B 212     8221   7569   5869   -143    127    418       O  
ATOM   4308  N   ILE B 213      -3.591   2.318  83.230  1.00 45.81           N  
ANISOU 4308  N   ILE B 213     6003   6442   4960   -230    536    608       N  
ATOM   4309  CA  ILE B 213      -4.016   2.777  81.906  1.00 46.54           C  
ANISOU 4309  CA  ILE B 213     5993   6541   5151   -225    545    583       C  
ATOM   4310  C   ILE B 213      -5.020   3.932  82.040  1.00 49.12           C  
ANISOU 4310  C   ILE B 213     6259   6989   5416   -110    677    592       C  
ATOM   4311  O   ILE B 213      -4.998   4.856  81.215  1.00 48.67           O  
ANISOU 4311  O   ILE B 213     6182   6909   5403    -45    688    519       O  
ATOM   4312  CB  ILE B 213      -4.589   1.639  81.024  1.00 46.08           C  
ANISOU 4312  CB  ILE B 213     5836   6485   5187   -358    495    673       C  
ATOM   4313  CG1 ILE B 213      -3.466   0.873  80.338  1.00 43.44           C  
ANISOU 4313  CG1 ILE B 213     5569   5998   4940   -423    362    614       C  
ATOM   4314  CG2 ILE B 213      -5.484   2.201  79.925  1.00 46.96           C  
ANISOU 4314  CG2 ILE B 213     5818   6664   5361   -344    539    686       C  
ATOM   4315  CD1 ILE B 213      -3.908  -0.485  79.860  1.00 41.48           C  
ANISOU 4315  CD1 ILE B 213     5292   5723   4747   -561    295    709       C  
ATOM   4316  N   CYS B 214      -5.867   3.880  83.077  1.00 47.29           N  
ANISOU 4316  N   CYS B 214     6007   6887   5076    -74    779    685       N  
ATOM   4317  CA  CYS B 214      -6.890   4.916  83.283  1.00 51.22           C  
ANISOU 4317  CA  CYS B 214     6445   7518   5498     63    919    708       C  
ATOM   4318  C   CYS B 214      -6.285   6.226  83.728  1.00 49.89           C  
ANISOU 4318  C   CYS B 214     6426   7284   5246    214    948    577       C  
ATOM   4319  O   CYS B 214      -6.781   7.280  83.353  1.00 49.67           O  
ANISOU 4319  O   CYS B 214     6378   7292   5203    335   1020    542       O  
ATOM   4320  CB  CYS B 214      -7.957   4.503  84.311  1.00 51.15           C  
ANISOU 4320  CB  CYS B 214     6368   7685   5381     73   1034    852       C  
ATOM   4321  SG  CYS B 214      -9.112   3.258  83.704  1.00 58.80           S  
ANISOU 4321  SG  CYS B 214     7123   8782   6437   -101   1029   1038       S  
ATOM   4322  N   ASN B 215      -5.243   6.161  84.552  1.00 49.09           N  
ANISOU 4322  N   ASN B 215     6483   7087   5083    207    886    510       N  
ATOM   4323  CA  ASN B 215      -4.595   7.382  85.020  1.00 51.13           C  
ANISOU 4323  CA  ASN B 215     6906   7266   5253    325    890    385       C  
ATOM   4324  C   ASN B 215      -3.878   8.068  83.829  1.00 47.18           C  
ANISOU 4324  C   ASN B 215     6418   6644   4865    315    809    276       C  
ATOM   4325  O   ASN B 215      -3.855   9.301  83.731  1.00 44.84           O  
ANISOU 4325  O   ASN B 215     6205   6310   4524    424    842    195       O  
ATOM   4326  CB  ASN B 215      -3.629   7.122  86.210  1.00 52.69           C  
ANISOU 4326  CB  ASN B 215     7268   7398   5354    303    826    348       C  
ATOM   4327  CG  ASN B 215      -4.354   6.811  87.543  1.00 61.42           C  
ANISOU 4327  CG  ASN B 215     8408   8625   6305    354    930    439       C  
ATOM   4328  OD1 ASN B 215      -5.399   7.397  87.876  1.00 65.12           O  
ANISOU 4328  OD1 ASN B 215     8849   9213   6681    478   1071    480       O  
ATOM   4329  ND2 ASN B 215      -3.765   5.897  88.335  1.00 59.84           N  
ANISOU 4329  ND2 ASN B 215     8271   8399   6068    270    861    474       N  
ATOM   4330  N   HIS B 216      -3.339   7.255  82.919  1.00 44.63           N  
ANISOU 4330  N   HIS B 216     6019   6261   4677    190    708    281       N  
ATOM   4331  CA  HIS B 216      -2.621   7.733  81.728  1.00 45.87           C  
ANISOU 4331  CA  HIS B 216     6170   6315   4942    166    632    194       C  
ATOM   4332  C   HIS B 216      -3.575   8.516  80.866  1.00 46.75           C  
ANISOU 4332  C   HIS B 216     6199   6480   5085    241    711    201       C  
ATOM   4333  O   HIS B 216      -3.313   9.665  80.496  1.00 46.83           O  
ANISOU 4333  O   HIS B 216     6278   6428   5088    314    715    117       O  
ATOM   4334  CB  HIS B 216      -2.047   6.533  80.963  1.00 43.56           C  
ANISOU 4334  CB  HIS B 216     5806   5973   4773     35    529    218       C  
ATOM   4335  CG  HIS B 216      -1.320   6.886  79.678  1.00 42.67           C  
ANISOU 4335  CG  HIS B 216     5673   5772   4770      9    460    142       C  
ATOM   4336  ND1 HIS B 216      -0.049   6.487  79.431  1.00 41.83           N  
ANISOU 4336  ND1 HIS B 216     5602   5575   4716    -51    354     92       N  
ATOM   4337  CD2 HIS B 216      -1.735   7.601  78.542  1.00 42.25           C  
ANISOU 4337  CD2 HIS B 216     5559   5718   4777     41    487    117       C  
ATOM   4338  CE1 HIS B 216       0.333   6.925  78.201  1.00 40.44           C  
ANISOU 4338  CE1 HIS B 216     5388   5350   4627    -59    324     39       C  
ATOM   4339  NE2 HIS B 216      -0.693   7.612  77.664  1.00 39.53           N  
ANISOU 4339  NE2 HIS B 216     5222   5282   4514     -7    402     53       N  
ATOM   4340  N   ILE B 217      -4.701   7.891  80.555  1.00 46.02           N  
ANISOU 4340  N   ILE B 217     5959   6504   5025    218    768    310       N  
ATOM   4341  CA  ILE B 217      -5.734   8.491  79.712  1.00 46.46           C  
ANISOU 4341  CA  ILE B 217     5903   6637   5113    285    839    342       C  
ATOM   4342  C   ILE B 217      -6.210   9.822  80.313  1.00 48.20           C  
ANISOU 4342  C   ILE B 217     6204   6895   5215    468    947    305       C  
ATOM   4343  O   ILE B 217      -6.253  10.861  79.646  1.00 46.19           O  
ANISOU 4343  O   ILE B 217     5978   6595   4975    553    961    244       O  
ATOM   4344  CB  ILE B 217      -6.891   7.485  79.504  1.00 45.11           C  
ANISOU 4344  CB  ILE B 217     5553   6608   4979    210    874    488       C  
ATOM   4345  CG1 ILE B 217      -6.389   6.324  78.638  1.00 43.86           C  
ANISOU 4345  CG1 ILE B 217     5351   6373   4941     42    751    501       C  
ATOM   4346  CG2 ILE B 217      -8.127   8.151  78.913  1.00 45.57           C  
ANISOU 4346  CG2 ILE B 217     5480   6792   5042    303    965    545       C  
ATOM   4347  CD1 ILE B 217      -7.403   5.214  78.412  1.00 43.55           C  
ANISOU 4347  CD1 ILE B 217     5165   6442   4940    -73    751    644       C  
ATOM   4348  N   LYS B 218      -6.531   9.769  81.593  1.00 52.53           N  
ANISOU 4348  N   LYS B 218     6806   7515   5636    531   1023    343       N  
ATOM   4349  CA  LYS B 218      -6.985  10.908  82.353  1.00 56.45           C  
ANISOU 4349  CA  LYS B 218     7408   8047   5992    719   1133    311       C  
ATOM   4350  C   LYS B 218      -5.951  12.043  82.268  1.00 53.06           C  
ANISOU 4350  C   LYS B 218     7182   7441   5537    770   1068    160       C  
ATOM   4351  O   LYS B 218      -6.297  13.177  81.991  1.00 53.40           O  
ANISOU 4351  O   LYS B 218     7286   7462   5541    907   1121    113       O  
ATOM   4352  CB  LYS B 218      -7.281  10.411  83.774  1.00 63.33           C  
ANISOU 4352  CB  LYS B 218     8319   9014   6731    746   1204    376       C  
ATOM   4353  CG  LYS B 218      -7.633  11.426  84.847  1.00 75.51           C  
ANISOU 4353  CG  LYS B 218    10012  10589   8090    946   1319    340       C  
ATOM   4354  CD  LYS B 218      -8.384  10.699  85.966  1.00 81.72           C  
ANISOU 4354  CD  LYS B 218    10740  11544   8766    965   1424    463       C  
ATOM   4355  CE  LYS B 218      -8.147  11.319  87.346  1.00 89.72           C  
ANISOU 4355  CE  LYS B 218    11978  12534   9579   1102   1483    403       C  
ATOM   4356  NZ  LYS B 218      -6.929  10.751  88.009  1.00 91.32           N  
ANISOU 4356  NZ  LYS B 218    12323  12612   9763    970   1356    348       N  
ATOM   4357  N   TYR B 219      -4.675  11.716  82.425  1.00 52.15           N  
ANISOU 4357  N   TYR B 219     7163   7200   5450    652    945     92       N  
ATOM   4358  CA  TYR B 219      -3.614  12.710  82.403  1.00 49.96           C  
ANISOU 4358  CA  TYR B 219     7070   6763   5149    663    867    -36       C  
ATOM   4359  C   TYR B 219      -3.376  13.276  80.998  1.00 48.41           C  
ANISOU 4359  C   TYR B 219     6830   6491   5072    638    819    -81       C  
ATOM   4360  O   TYR B 219      -3.334  14.509  80.782  1.00 46.14           O  
ANISOU 4360  O   TYR B 219     6663   6124   4742    730    831   -152       O  
ATOM   4361  CB  TYR B 219      -2.299  12.098  82.923  1.00 51.05           C  
ANISOU 4361  CB  TYR B 219     7286   6817   5295    531    741    -75       C  
ATOM   4362  CG  TYR B 219      -1.139  13.053  82.787  1.00 52.52           C  
ANISOU 4362  CG  TYR B 219     7630   6851   5474    505    640   -190       C  
ATOM   4363  CD1 TYR B 219      -0.853  13.990  83.799  1.00 55.52           C  
ANISOU 4363  CD1 TYR B 219     8230   7161   5703    580    637   -262       C  
ATOM   4364  CD2 TYR B 219      -0.367  13.069  81.639  1.00 50.99           C  
ANISOU 4364  CD2 TYR B 219     7374   6584   5414    405    549   -223       C  
ATOM   4365  CE1 TYR B 219       0.194  14.892  83.670  1.00 57.04           C  
ANISOU 4365  CE1 TYR B 219     8574   7211   5886    532    531   -359       C  
ATOM   4366  CE2 TYR B 219       0.677  13.968  81.497  1.00 54.59           C  
ANISOU 4366  CE2 TYR B 219     7962   6916   5864    364    457   -313       C  
ATOM   4367  CZ  TYR B 219       0.953  14.875  82.512  1.00 56.94           C  
ANISOU 4367  CZ  TYR B 219     8474   7141   6017    418    443   -378       C  
ATOM   4368  OH  TYR B 219       1.988  15.761  82.367  1.00 56.93           O  
ANISOU 4368  OH  TYR B 219     8608   7014   6010    351    337   -457       O  
ATOM   4369  N   ALA B 220      -3.195  12.360  80.050  1.00 45.02           N  
ANISOU 4369  N   ALA B 220     6246   6077   4782    513    761    -40       N  
ATOM   4370  CA  ALA B 220      -2.856  12.725  78.690  1.00 42.42           C  
ANISOU 4370  CA  ALA B 220     5871   5680   4566    471    707    -77       C  
ATOM   4371  C   ALA B 220      -3.970  13.560  78.061  1.00 43.48           C  
ANISOU 4371  C   ALA B 220     5960   5866   4695    597    798    -56       C  
ATOM   4372  O   ALA B 220      -3.679  14.507  77.326  1.00 44.76           O  
ANISOU 4372  O   ALA B 220     6186   5939   4881    626    773   -117       O  
ATOM   4373  CB  ALA B 220      -2.556  11.483  77.871  1.00 39.93           C  
ANISOU 4373  CB  ALA B 220     5411   5380   4380    332    638    -32       C  
ATOM   4374  N   THR B 221      -5.223  13.219  78.382  1.00 40.61           N  
ANISOU 4374  N   THR B 221     5485   5650   4294    672    901     39       N  
ATOM   4375  CA  THR B 221      -6.398  13.904  77.847  1.00 42.96           C  
ANISOU 4375  CA  THR B 221     5708   6032   4583    806    994     81       C  
ATOM   4376  C   THR B 221      -6.549  15.347  78.369  1.00 45.25           C  
ANISOU 4376  C   THR B 221     6180   6264   4747    994   1061     11       C  
ATOM   4377  O   THR B 221      -6.643  16.307  77.575  1.00 46.80           O  
ANISOU 4377  O   THR B 221     6422   6396   4964   1068   1060    -30       O  
ATOM   4378  CB  THR B 221      -7.677  13.087  78.128  1.00 42.97           C  
ANISOU 4378  CB  THR B 221     5519   6232   4574    825   1084    220       C  
ATOM   4379  OG1 THR B 221      -7.551  11.807  77.502  1.00 42.34           O  
ANISOU 4379  OG1 THR B 221     5298   6177   4612    643   1005    280       O  
ATOM   4380  CG2 THR B 221      -8.892  13.778  77.571  1.00 44.11           C  
ANISOU 4380  CG2 THR B 221     5561   6488   4711    971   1177    276       C  
ATOM   4381  N   ASN B 222      -6.609  15.492  79.692  1.00 45.92           N  
ANISOU 4381  N   ASN B 222     6383   6369   4695   1078   1118      1       N  
ATOM   4382  CA  ASN B 222      -6.501  16.799  80.331  1.00 49.20           C  
ANISOU 4382  CA  ASN B 222     7035   6688   4971   1240   1157    -88       C  
ATOM   4383  C   ASN B 222      -7.542  17.768  79.766  1.00 52.44           C  
ANISOU 4383  C   ASN B 222     7425   7142   5355   1434   1253    -69       C  
ATOM   4384  O   ASN B 222      -7.220  18.902  79.378  1.00 52.66           O  
ANISOU 4384  O   ASN B 222     7621   7028   5361   1506   1224   -154       O  
ATOM   4385  CB  ASN B 222      -5.061  17.303  80.132  1.00 48.17           C  
ANISOU 4385  CB  ASN B 222     7086   6350   4866   1126   1017   -207       C  
ATOM   4386  CG  ASN B 222      -4.774  18.617  80.815  1.00 48.43           C  
ANISOU 4386  CG  ASN B 222     7402   6246   4752   1251   1022   -307       C  
ATOM   4387  OD1 ASN B 222      -4.159  19.497  80.210  1.00 51.56           O  
ANISOU 4387  OD1 ASN B 222     7926   6492   5172   1226    947   -383       O  
ATOM   4388  ND2 ASN B 222      -5.185  18.760  82.056  1.00 45.24           N  
ANISOU 4388  ND2 ASN B 222     7113   5887   4190   1379   1102   -309       N  
ATOM   4389  N   ARG B 223      -8.783  17.281  79.682  1.00 54.07           N  
ANISOU 4389  N   ARG B 223     7420   7552   5572   1509   1360     53       N  
ATOM   4390  CA  ARG B 223      -9.933  18.071  79.239  1.00 58.57           C  
ANISOU 4390  CA  ARG B 223     7928   8214   6111   1715   1467     99       C  
ATOM   4391  C   ARG B 223      -9.780  18.674  77.825  1.00 59.62           C  
ANISOU 4391  C   ARG B 223     8049   8250   6355   1695   1396     65       C  
ATOM   4392  O   ARG B 223     -10.429  19.672  77.479  1.00 57.98           O  
ANISOU 4392  O   ARG B 223     7885   8044   6103   1886   1459     62       O  
ATOM   4393  CB  ARG B 223     -10.260  19.163  80.268  1.00 64.92           C  
ANISOU 4393  CB  ARG B 223     8952   8990   6723   1966   1574     46       C  
ATOM   4394  CG  ARG B 223     -10.323  18.677  81.707  1.00 69.87           C  
ANISOU 4394  CG  ARG B 223     9632   9697   7218   1996   1643     68       C  
ATOM   4395  CD  ARG B 223     -10.407  19.847  82.663  1.00 78.88           C  
ANISOU 4395  CD  ARG B 223    11055  10757   8158   2236   1723    -16       C  
ATOM   4396  NE  ARG B 223     -11.781  20.118  83.100  1.00 92.31           N  
ANISOU 4396  NE  ARG B 223    12664  12663   9745   2496   1910     77       N  
ATOM   4397  CZ  ARG B 223     -12.702  20.806  82.415  1.00 95.96           C  
ANISOU 4397  CZ  ARG B 223    13046  13199  10214   2687   1991    120       C  
ATOM   4398  NH1 ARG B 223     -12.436  21.311  81.208  1.00 91.99           N  
ANISOU 4398  NH1 ARG B 223    12549  12574   9829   2642   1899     77       N  
ATOM   4399  NH2 ARG B 223     -13.910  20.984  82.946  1.00 96.99           N  
ANISOU 4399  NH2 ARG B 223    13082  13541  10229   2932   2168    215       N  
ATOM   4400  N   GLY B 224      -8.934  18.056  77.002  1.00 56.45           N  
ANISOU 4400  N   GLY B 224     7591   7768   6091   1475   1269     43       N  
ATOM   4401  CA  GLY B 224      -8.781  18.513  75.630  1.00 54.34           C  
ANISOU 4401  CA  GLY B 224     7298   7422   5925   1441   1204     21       C  
ATOM   4402  C   GLY B 224      -7.438  19.155  75.396  1.00 55.74           C  
ANISOU 4402  C   GLY B 224     7689   7376   6114   1353   1095   -103       C  
ATOM   4403  O   GLY B 224      -7.016  19.360  74.238  1.00 52.41           O  
ANISOU 4403  O   GLY B 224     7250   6875   5789   1269   1020   -125       O  
ATOM   4404  N   ASN B 225      -6.747  19.455  76.490  1.00 55.59           N  
ANISOU 4404  N   ASN B 225     7869   7261   5994   1359   1081   -177       N  
ATOM   4405  CA  ASN B 225      -5.436  20.067  76.373  1.00 57.24           C  
ANISOU 4405  CA  ASN B 225     8277   7267   6205   1256    967   -284       C  
ATOM   4406  C   ASN B 225      -4.351  18.992  76.421  1.00 54.31           C  
ANISOU 4406  C   ASN B 225     7835   6882   5918   1031    865   -291       C  
ATOM   4407  O   ASN B 225      -3.631  18.832  77.416  1.00 53.45           O  
ANISOU 4407  O   ASN B 225     7840   6725   5745    978    825   -333       O  
ATOM   4408  CB  ASN B 225      -5.263  21.154  77.434  1.00 61.55           C  
ANISOU 4408  CB  ASN B 225     9107   7694   6586   1388    989   -366       C  
ATOM   4409  CG  ASN B 225      -4.072  22.050  77.168  1.00 61.40           C  
ANISOU 4409  CG  ASN B 225     9308   7458   6563   1290    868   -466       C  
ATOM   4410  OD1 ASN B 225      -3.685  22.817  78.032  1.00 67.04           O  
ANISOU 4410  OD1 ASN B 225    10273   8049   7149   1340    847   -541       O  
ATOM   4411  ND2 ASN B 225      -3.481  21.953  75.990  1.00 57.47           N  
ANISOU 4411  ND2 ASN B 225     8724   6915   6198   1145    786   -463       N  
ATOM   4412  N   LEU B 226      -4.253  18.250  75.323  1.00 48.01           N  
ANISOU 4412  N   LEU B 226     6854   6130   5260    911    821   -246       N  
ATOM   4413  CA  LEU B 226      -3.504  17.009  75.321  1.00 48.74           C  
ANISOU 4413  CA  LEU B 226     6839   6247   5432    734    748   -229       C  
ATOM   4414  C   LEU B 226      -2.047  17.161  75.728  1.00 48.35           C  
ANISOU 4414  C   LEU B 226     6930   6070   5372    618    644   -308       C  
ATOM   4415  O   LEU B 226      -1.417  18.184  75.449  1.00 45.60           O  
ANISOU 4415  O   LEU B 226     6724   5595   5006    609    595   -373       O  
ATOM   4416  CB  LEU B 226      -3.628  16.317  73.965  1.00 49.09           C  
ANISOU 4416  CB  LEU B 226     6701   6338   5614    642    715   -180       C  
ATOM   4417  CG  LEU B 226      -4.859  15.433  73.750  1.00 48.42           C  
ANISOU 4417  CG  LEU B 226     6418   6416   5564    666    777    -75       C  
ATOM   4418  CD1 LEU B 226      -6.152  16.054  74.246  1.00 44.70           C  
ANISOU 4418  CD1 LEU B 226     5936   6044   5003    850    896    -27       C  
ATOM   4419  CD2 LEU B 226      -4.984  15.082  72.282  1.00 50.52           C  
ANISOU 4419  CD2 LEU B 226     6555   6695   5946    592    733    -45       C  
ATOM   4420  N   ARG B 227      -1.529  16.145  76.417  1.00 47.91           N  
ANISOU 4420  N   ARG B 227     6833   6050   5321    526    605   -292       N  
ATOM   4421  CA  ARG B 227      -0.151  16.181  76.943  1.00 47.49           C  
ANISOU 4421  CA  ARG B 227     6891   5902   5251    417    501   -353       C  
ATOM   4422  C   ARG B 227       0.483  14.854  76.619  1.00 45.41           C  
ANISOU 4422  C   ARG B 227     6479   5685   5088    285    439   -316       C  
ATOM   4423  O   ARG B 227      -0.078  13.830  76.988  1.00 45.84           O  
ANISOU 4423  O   ARG B 227     6435   5833   5148    289    476   -254       O  
ATOM   4424  CB  ARG B 227      -0.146  16.367  78.473  1.00 46.40           C  
ANISOU 4424  CB  ARG B 227     6904   5756   4971    474    518   -377       C  
ATOM   4425  CG  ARG B 227      -0.514  17.754  78.946  1.00 47.95           C  
ANISOU 4425  CG  ARG B 227     7310   5871   5040    608    560   -435       C  
ATOM   4426  CD  ARG B 227      -0.386  17.904  80.451  1.00 49.74           C  
ANISOU 4426  CD  ARG B 227     7709   6078   5113    657    564   -468       C  
ATOM   4427  NE  ARG B 227      -1.424  17.154  81.158  1.00 50.92           N  
ANISOU 4427  NE  ARG B 227     7767   6373   5207    754    677   -396       N  
ATOM   4428  CZ  ARG B 227      -1.805  17.382  82.412  1.00 53.59           C  
ANISOU 4428  CZ  ARG B 227     8244   6731   5388    864    738   -407       C  
ATOM   4429  NH1 ARG B 227      -1.243  18.349  83.140  1.00 52.14           N  
ANISOU 4429  NH1 ARG B 227     8318   6415   5076    896    688   -497       N  
ATOM   4430  NH2 ARG B 227      -2.755  16.633  82.946  1.00 53.74           N  
ANISOU 4430  NH2 ARG B 227     8148   6903   5368    938    846   -323       N  
ATOM   4431  N   SER B 228       1.620  14.861  75.927  1.00 41.41           N  
ANISOU 4431  N   SER B 228     5959   5118   4659    176    348   -346       N  
ATOM   4432  CA  SER B 228       2.355  13.621  75.636  1.00 43.78           C  
ANISOU 4432  CA  SER B 228     6137   5452   5044     72    286   -318       C  
ATOM   4433  C   SER B 228       2.708  12.759  76.844  1.00 40.26           C  
ANISOU 4433  C   SER B 228     5708   5038   4550     45    256   -300       C  
ATOM   4434  O   SER B 228       3.226  13.249  77.834  1.00 41.38           O  
ANISOU 4434  O   SER B 228     5977   5139   4605     42    219   -337       O  
ATOM   4435  CB  SER B 228       3.621  13.925  74.860  1.00 41.54           C  
ANISOU 4435  CB  SER B 228     5848   5109   4826    -23    201   -353       C  
ATOM   4436  OG  SER B 228       3.241  14.570  73.666  1.00 42.22           O  
ANISOU 4436  OG  SER B 228     5908   5173   4960     -3    232   -357       O  
ATOM   4437  N   ALA B 229       2.414  11.467  76.755  1.00 41.88           N  
ANISOU 4437  N   ALA B 229     5799   5309   4804     22    264   -240       N  
ATOM   4438  CA  ALA B 229       2.682  10.545  77.873  1.00 41.57           C  
ANISOU 4438  CA  ALA B 229     5776   5299   4719     -2    236   -211       C  
ATOM   4439  C   ALA B 229       2.995   9.115  77.422  1.00 42.18           C  
ANISOU 4439  C   ALA B 229     5744   5401   4882    -65    192   -163       C  
ATOM   4440  O   ALA B 229       2.500   8.654  76.393  1.00 41.13           O  
ANISOU 4440  O   ALA B 229     5516   5285   4826    -76    213   -134       O  
ATOM   4441  CB  ALA B 229       1.533  10.564  78.886  1.00 39.39           C  
ANISOU 4441  CB  ALA B 229     5541   5084   4341     77    326   -172       C  
ATOM   4442  N   ILE B 230       3.852   8.442  78.187  1.00 41.36           N  
ANISOU 4442  N   ILE B 230     5668   5289   4758   -103    123   -157       N  
ATOM   4443  CA  ILE B 230       4.027   7.010  78.072  1.00 40.71           C  
ANISOU 4443  CA  ILE B 230     5521   5222   4727   -140     86   -105       C  
ATOM   4444  C   ILE B 230       3.888   6.381  79.487  1.00 44.88           C  
ANISOU 4444  C   ILE B 230     6111   5775   5166   -137     81    -62       C  
ATOM   4445  O   ILE B 230       4.207   7.019  80.501  1.00 45.84           O  
ANISOU 4445  O   ILE B 230     6329   5892   5197   -120     68    -91       O  
ATOM   4446  CB  ILE B 230       5.361   6.700  77.387  1.00 39.66           C  
ANISOU 4446  CB  ILE B 230     5347   5054   4669   -177     -1   -133       C  
ATOM   4447  CG1 ILE B 230       5.452   5.235  76.977  1.00 40.81           C  
ANISOU 4447  CG1 ILE B 230     5438   5197   4872   -192    -32    -86       C  
ATOM   4448  CG2 ILE B 230       6.559   7.105  78.237  1.00 38.85           C  
ANISOU 4448  CG2 ILE B 230     5305   4939   4518   -197    -79   -165       C  
ATOM   4449  CD1 ILE B 230       6.800   4.896  76.353  1.00 35.34           C  
ANISOU 4449  CD1 ILE B 230     4703   4484   4239   -197   -106   -109       C  
ATOM   4450  N   THR B 231       3.330   5.177  79.556  1.00 40.96           N  
ANISOU 4450  N   THR B 231     5575   5303   4687   -159     91     11       N  
ATOM   4451  CA  THR B 231       3.318   4.398  80.775  1.00 41.31           C  
ANISOU 4451  CA  THR B 231     5674   5365   4657   -169     74     63       C  
ATOM   4452  C   THR B 231       4.089   3.112  80.451  1.00 43.48           C  
ANISOU 4452  C   THR B 231     5927   5597   4998   -208    -14     90       C  
ATOM   4453  O   THR B 231       3.807   2.450  79.440  1.00 42.96           O  
ANISOU 4453  O   THR B 231     5801   5510   5012   -232    -18    112       O  
ATOM   4454  CB  THR B 231       1.887   4.036  81.196  1.00 44.52           C  
ANISOU 4454  CB  THR B 231     6060   5841   5016   -167    166    146       C  
ATOM   4455  OG1 THR B 231       1.186   5.214  81.593  1.00 43.18           O  
ANISOU 4455  OG1 THR B 231     5919   5720   4770   -100    256    124       O  
ATOM   4456  CG2 THR B 231       1.887   3.026  82.363  1.00 44.53           C  
ANISOU 4456  CG2 THR B 231     6116   5857   4947   -195    144    218       C  
ATOM   4457  N   VAL B 232       5.065   2.778  81.289  1.00 40.82           N  
ANISOU 4457  N   VAL B 232     5648   5242   4620   -207    -90     87       N  
ATOM   4458  CA  VAL B 232       5.969   1.667  81.019  1.00 40.78           C  
ANISOU 4458  CA  VAL B 232     5632   5194   4669   -214   -178    106       C  
ATOM   4459  C   VAL B 232       5.719   0.560  82.027  1.00 44.33           C  
ANISOU 4459  C   VAL B 232     6146   5638   5059   -229   -200    184       C  
ATOM   4460  O   VAL B 232       5.975   0.738  83.227  1.00 46.92           O  
ANISOU 4460  O   VAL B 232     6543   5988   5294   -221   -219    193       O  
ATOM   4461  CB  VAL B 232       7.435   2.108  81.157  1.00 42.25           C  
ANISOU 4461  CB  VAL B 232     5818   5375   4861   -196   -263     53       C  
ATOM   4462  CG1 VAL B 232       8.398   0.966  80.786  1.00 39.36           C  
ANISOU 4462  CG1 VAL B 232     5426   4979   4552   -172   -345     75       C  
ATOM   4463  CG2 VAL B 232       7.674   3.353  80.318  1.00 40.48           C  
ANISOU 4463  CG2 VAL B 232     5545   5158   4679   -198   -240    -17       C  
ATOM   4464  N   PHE B 233       5.205  -0.572  81.547  1.00 42.99           N  
ANISOU 4464  N   PHE B 233     5967   5433   4932   -258   -204    243       N  
ATOM   4465  CA  PHE B 233       4.962  -1.721  82.385  1.00 41.11           C  
ANISOU 4465  CA  PHE B 233     5800   5174   4644   -287   -233    328       C  
ATOM   4466  C   PHE B 233       6.209  -2.593  82.477  1.00 40.23           C  
ANISOU 4466  C   PHE B 233     5735   5000   4552   -248   -342    328       C  
ATOM   4467  O   PHE B 233       7.201  -2.290  81.836  1.00 39.39           O  
ANISOU 4467  O   PHE B 233     5583   4883   4500   -200   -384    265       O  
ATOM   4468  CB  PHE B 233       3.763  -2.490  81.860  1.00 44.42           C  
ANISOU 4468  CB  PHE B 233     6203   5581   5093   -354   -194    401       C  
ATOM   4469  CG  PHE B 233       2.474  -1.764  82.047  1.00 45.47           C  
ANISOU 4469  CG  PHE B 233     6283   5804   5188   -383    -85    431       C  
ATOM   4470  CD1 PHE B 233       1.853  -1.739  83.289  1.00 46.68           C  
ANISOU 4470  CD1 PHE B 233     6474   6026   5238   -397    -32    498       C  
ATOM   4471  CD2 PHE B 233       1.879  -1.100  80.979  1.00 46.69           C  
ANISOU 4471  CD2 PHE B 233     6351   5986   5405   -385    -32    398       C  
ATOM   4472  CE1 PHE B 233       0.653  -1.068  83.464  1.00 47.98           C  
ANISOU 4472  CE1 PHE B 233     6579   6291   5359   -401     81    533       C  
ATOM   4473  CE2 PHE B 233       0.687  -0.424  81.138  1.00 43.49           C  
ANISOU 4473  CE2 PHE B 233     5887   5676   4963   -391     71    433       C  
ATOM   4474  CZ  PHE B 233       0.069  -0.414  82.378  1.00 48.94           C  
ANISOU 4474  CZ  PHE B 233     6604   6441   5549   -394    131    501       C  
ATOM   4475  N   PRO B 234       6.168  -3.665  83.297  1.00 40.15           N  
ANISOU 4475  N   PRO B 234     5810   4955   4490   -264   -386    405       N  
ATOM   4476  CA  PRO B 234       7.356  -4.448  83.690  1.00 38.89           C  
ANISOU 4476  CA  PRO B 234     5708   4746   4322   -208   -491    415       C  
ATOM   4477  C   PRO B 234       8.007  -5.118  82.479  1.00 41.72           C  
ANISOU 4477  C   PRO B 234     6046   5031   4774   -155   -543    388       C  
ATOM   4478  O   PRO B 234       7.306  -5.630  81.583  1.00 38.89           O  
ANISOU 4478  O   PRO B 234     5694   4616   4465   -190   -520    401       O  
ATOM   4479  CB  PRO B 234       6.781  -5.514  84.624  1.00 38.57           C  
ANISOU 4479  CB  PRO B 234     5775   4670   4211   -254   -508    519       C  
ATOM   4480  CG  PRO B 234       5.494  -4.955  85.116  1.00 38.78           C  
ANISOU 4480  CG  PRO B 234     5785   4770   4178   -326   -404    557       C  
ATOM   4481  CD  PRO B 234       4.945  -4.164  83.954  1.00 39.74           C  
ANISOU 4481  CD  PRO B 234     5803   4921   4377   -338   -333    499       C  
ATOM   4482  N   GLN B 235       9.336  -5.109  82.455  1.00 40.12           N  
ANISOU 4482  N   GLN B 235     5820   4835   4589    -69   -613    353       N  
ATOM   4483  CA  GLN B 235      10.056  -5.559  81.293  1.00 41.17           C  
ANISOU 4483  CA  GLN B 235     5919   4923   4800      9   -645    319       C  
ATOM   4484  C   GLN B 235       9.771  -7.049  81.043  1.00 44.32           C  
ANISOU 4484  C   GLN B 235     6436   5200   5202     25   -687    374       C  
ATOM   4485  O   GLN B 235       9.320  -7.757  81.945  1.00 44.15           O  
ANISOU 4485  O   GLN B 235     6517   5137   5121    -17   -713    447       O  
ATOM   4486  CB  GLN B 235      11.562  -5.328  81.506  1.00 42.26           C  
ANISOU 4486  CB  GLN B 235     5996   5117   4942    103   -715    294       C  
ATOM   4487  CG  GLN B 235      12.161  -6.160  82.632  1.00 44.38           C  
ANISOU 4487  CG  GLN B 235     6346   5368   5148    151   -803    357       C  
ATOM   4488  CD  GLN B 235      13.349  -5.476  83.298  1.00 49.71           C  
ANISOU 4488  CD  GLN B 235     6945   6145   5798    187   -866    343       C  
ATOM   4489  OE1 GLN B 235      13.247  -4.306  83.707  1.00 52.13           O  
ANISOU 4489  OE1 GLN B 235     7208   6524   6077    117   -842    309       O  
ATOM   4490  NE2 GLN B 235      14.488  -6.202  83.419  1.00 45.60           N  
ANISOU 4490  NE2 GLN B 235     6414   5629   5281    300   -954    373       N  
ATOM   4491  N   ARG B 236      10.069  -7.533  79.842  1.00 44.69           N  
ANISOU 4491  N   ARG B 236     6485   5184   5310     89   -698    342       N  
ATOM   4492  CA  ARG B 236      10.123  -8.972  79.609  1.00 51.17           C  
ANISOU 4492  CA  ARG B 236     7446   5871   6124    137   -761    383       C  
ATOM   4493  C   ARG B 236      11.180  -9.645  80.469  1.00 51.60           C  
ANISOU 4493  C   ARG B 236     7558   5910   6136    245   -845    421       C  
ATOM   4494  O   ARG B 236      12.132  -9.018  80.912  1.00 52.69           O  
ANISOU 4494  O   ARG B 236     7599   6151   6269    307   -862    402       O  
ATOM   4495  CB  ARG B 236      10.394  -9.265  78.142  1.00 55.30           C  
ANISOU 4495  CB  ARG B 236     7969   6335   6705    213   -755    327       C  
ATOM   4496  CG  ARG B 236       9.840  -8.167  77.282  1.00 58.60           C  
ANISOU 4496  CG  ARG B 236     8270   6824   7172    146   -673    270       C  
ATOM   4497  CD  ARG B 236       9.075  -8.696  76.120  1.00 61.11           C  
ANISOU 4497  CD  ARG B 236     8657   7043   7517    109   -664    257       C  
ATOM   4498  NE  ARG B 236       9.963  -9.262  75.134  1.00 65.68           N  
ANISOU 4498  NE  ARG B 236     9277   7562   8117    252   -692    212       N  
ATOM   4499  CZ  ARG B 236       9.945 -10.531  74.784  1.00 60.85           C  
ANISOU 4499  CZ  ARG B 236     8835   6801   7483    301   -753    230       C  
ATOM   4500  NH1 ARG B 236       9.076 -11.354  75.344  1.00 62.86           N  
ANISOU 4500  NH1 ARG B 236     9229   6954   7703    193   -800    298       N  
ATOM   4501  NH2 ARG B 236      10.791 -10.954  73.880  1.00 57.93           N  
ANISOU 4501  NH2 ARG B 236     8501   6389   7120    456   -765    182       N  
ATOM   4502  N   ALA B 237      10.984 -10.933  80.716  1.00 54.61           N  
ANISOU 4502  N   ALA B 237     8106   6161   6484    258   -906    483       N  
ATOM   4503  CA  ALA B 237      11.865 -11.709  81.584  1.00 55.30           C  
ANISOU 4503  CA  ALA B 237     8275   6216   6522    363   -993    533       C  
ATOM   4504  C   ALA B 237      11.957 -13.135  81.036  1.00 56.62           C  
ANISOU 4504  C   ALA B 237     8624   6205   6684    447  -1056    558       C  
ATOM   4505  O   ALA B 237      10.922 -13.722  80.694  1.00 52.85           O  
ANISOU 4505  O   ALA B 237     8268   5611   6203    339  -1054    586       O  
ATOM   4506  CB  ALA B 237      11.362 -11.689  83.033  1.00 50.56           C  
ANISOU 4506  CB  ALA B 237     7725   5642   5844    260  -1006    609       C  
ATOM   4507  N   PRO B 238      13.204 -13.666  80.920  1.00 61.89           N  
ANISOU 4507  N   PRO B 238     9309   6856   7349    643  -1116    550       N  
ATOM   4508  CA  PRO B 238      13.607 -14.990  80.418  1.00 63.61           C  
ANISOU 4508  CA  PRO B 238     9709   6908   7551    789  -1182    563       C  
ATOM   4509  C   PRO B 238      12.651 -16.126  80.743  1.00 65.64           C  
ANISOU 4509  C   PRO B 238    10207   6973   7759    685  -1236    635       C  
ATOM   4510  O   PRO B 238      12.327 -16.938  79.870  1.00 68.45           O  
ANISOU 4510  O   PRO B 238    10722   7167   8117    704  -1260    620       O  
ATOM   4511  CB  PRO B 238      14.937 -15.232  81.140  1.00 64.48           C  
ANISOU 4511  CB  PRO B 238     9786   7082   7633    971  -1248    594       C  
ATOM   4512  CG  PRO B 238      15.520 -13.865  81.317  1.00 65.01           C  
ANISOU 4512  CG  PRO B 238     9600   7367   7735    957  -1202    555       C  
ATOM   4513  CD  PRO B 238      14.398 -12.854  81.243  1.00 61.11           C  
ANISOU 4513  CD  PRO B 238     9030   6926   7264    746  -1119    525       C  
ATOM   4514  N   GLY B 239      12.209 -16.196  81.990  1.00 68.16           N  
ANISOU 4514  N   GLY B 239    10565   7305   8026    571  -1260    716       N  
ATOM   4515  CA  GLY B 239      11.335 -17.292  82.411  1.00 74.45           C  
ANISOU 4515  CA  GLY B 239    11589   7930   8769    456  -1316    806       C  
ATOM   4516  C   GLY B 239       9.920 -17.316  81.834  1.00 74.37           C  
ANISOU 4516  C   GLY B 239    11621   7857   8779    245  -1276    818       C  
ATOM   4517  O   GLY B 239       9.366 -18.384  81.583  1.00 73.38           O  
ANISOU 4517  O   GLY B 239    11705   7548   8628    181  -1338    867       O  
ATOM   4518  N   ARG B 240       9.332 -16.143  81.605  1.00 69.29           N  
ANISOU 4518  N   ARG B 240    10785   7365   8177    136  -1180    778       N  
ATOM   4519  CA  ARG B 240       7.878 -16.053  81.637  1.00 61.93           C  
ANISOU 4519  CA  ARG B 240     9856   6432   7242    -92  -1139    834       C  
ATOM   4520  C   ARG B 240       7.245 -15.178  80.573  1.00 57.86           C  
ANISOU 4520  C   ARG B 240     9198   5994   6794   -163  -1059    765       C  
ATOM   4521  O   ARG B 240       7.930 -14.417  79.887  1.00 55.65           O  
ANISOU 4521  O   ARG B 240     8790   5793   6563    -48  -1018    667       O  
ATOM   4522  CB  ARG B 240       7.411 -15.653  83.058  1.00 61.55           C  
ANISOU 4522  CB  ARG B 240     9755   6499   7133   -200  -1104    919       C  
ATOM   4523  CG  ARG B 240       8.011 -14.383  83.647  1.00 60.28           C  
ANISOU 4523  CG  ARG B 240     9405   6529   6971   -131  -1042    865       C  
ATOM   4524  CD  ARG B 240       7.026 -13.231  83.556  1.00 59.65           C  
ANISOU 4524  CD  ARG B 240     9164   6590   6909   -259   -930    848       C  
ATOM   4525  NE  ARG B 240       7.510 -12.007  84.185  1.00 62.79           N  
ANISOU 4525  NE  ARG B 240     9418   7149   7291   -210   -877    799       N  
ATOM   4526  CZ  ARG B 240       7.789 -10.856  83.566  1.00 59.06           C  
ANISOU 4526  CZ  ARG B 240     8792   6777   6872   -168   -819    703       C  
ATOM   4527  NH1 ARG B 240       7.650 -10.706  82.253  1.00 54.49           N  
ANISOU 4527  NH1 ARG B 240     8163   6169   6370   -159   -795    641       N  
ATOM   4528  NH2 ARG B 240       8.210  -9.834  84.291  1.00 60.07           N  
ANISOU 4528  NH2 ARG B 240     8828   7028   6967   -141   -790    671       N  
ATOM   4529  N   GLY B 241       5.922 -15.313  80.446  1.00 55.47           N  
ANISOU 4529  N   GLY B 241     8914   5673   6489   -360  -1040    827       N  
ATOM   4530  CA  GLY B 241       5.138 -14.569  79.479  1.00 52.48           C  
ANISOU 4530  CA  GLY B 241     8409   5364   6167   -448   -973    782       C  
ATOM   4531  C   GLY B 241       5.279 -13.077  79.672  1.00 50.79           C  
ANISOU 4531  C   GLY B 241     7968   5351   5979   -413   -867    722       C  
ATOM   4532  O   GLY B 241       5.792 -12.624  80.682  1.00 52.41           O  
ANISOU 4532  O   GLY B 241     8119   5645   6148   -359   -847    729       O  
ATOM   4533  N   ASP B 242       4.822 -12.316  78.692  1.00 50.41           N  
ANISOU 4533  N   ASP B 242     7803   5364   5986   -445   -809    663       N  
ATOM   4534  CA  ASP B 242       4.923 -10.875  78.724  1.00 48.08           C  
ANISOU 4534  CA  ASP B 242     7315   5237   5716   -412   -714    601       C  
ATOM   4535  C   ASP B 242       3.702 -10.251  79.382  1.00 50.69           C  
ANISOU 4535  C   ASP B 242     7552   5687   6020   -551   -636    669       C  
ATOM   4536  O   ASP B 242       2.599 -10.841  79.369  1.00 53.29           O  
ANISOU 4536  O   ASP B 242     7923   5987   6337   -696   -646    758       O  
ATOM   4537  CB  ASP B 242       5.001 -10.341  77.303  1.00 45.69           C  
ANISOU 4537  CB  ASP B 242     6940   4939   5480   -371   -686    510       C  
ATOM   4538  CG  ASP B 242       6.283 -10.725  76.577  1.00 47.64           C  
ANISOU 4538  CG  ASP B 242     7244   5109   5750   -204   -735    433       C  
ATOM   4539  OD1 ASP B 242       7.343 -10.971  77.192  1.00 48.69           O  
ANISOU 4539  OD1 ASP B 242     7404   5236   5859    -85   -770    429       O  
ATOM   4540  OD2 ASP B 242       6.233 -10.757  75.333  1.00 50.17           O  
ANISOU 4540  OD2 ASP B 242     7573   5382   6108   -182   -734    378       O  
ATOM   4541  N   PHE B 243       3.902  -9.068  79.974  1.00 46.95           N  
ANISOU 4541  N   PHE B 243     6956   5352   5532   -507   -561    633       N  
ATOM   4542  CA  PHE B 243       2.809  -8.127  80.167  1.00 45.46           C  
ANISOU 4542  CA  PHE B 243     6646   5295   5333   -589   -462    658       C  
ATOM   4543  C   PHE B 243       2.438  -7.631  78.748  1.00 45.67           C  
ANISOU 4543  C   PHE B 243     6590   5327   5435   -598   -435    597       C  
ATOM   4544  O   PHE B 243       3.325  -7.278  77.957  1.00 41.98           O  
ANISOU 4544  O   PHE B 243     6103   4833   5015   -499   -450    501       O  
ATOM   4545  CB  PHE B 243       3.253  -6.969  81.067  1.00 45.10           C  
ANISOU 4545  CB  PHE B 243     6527   5365   5242   -517   -401    616       C  
ATOM   4546  CG  PHE B 243       3.310  -7.323  82.540  1.00 45.21           C  
ANISOU 4546  CG  PHE B 243     6614   5402   5163   -530   -411    690       C  
ATOM   4547  CD1 PHE B 243       4.443  -7.916  83.087  1.00 43.25           C  
ANISOU 4547  CD1 PHE B 243     6460   5086   4889   -454   -497    684       C  
ATOM   4548  CD2 PHE B 243       2.222  -7.062  83.377  1.00 45.46           C  
ANISOU 4548  CD2 PHE B 243     6617   5531   5126   -609   -332    771       C  
ATOM   4549  CE1 PHE B 243       4.494  -8.270  84.423  1.00 43.33           C  
ANISOU 4549  CE1 PHE B 243     6547   5112   4806   -467   -513    755       C  
ATOM   4550  CE2 PHE B 243       2.262  -7.409  84.719  1.00 45.43           C  
ANISOU 4550  CE2 PHE B 243     6689   5549   5024   -620   -336    843       C  
ATOM   4551  CZ  PHE B 243       3.401  -8.017  85.241  1.00 46.96           C  
ANISOU 4551  CZ  PHE B 243     6989   5662   5192   -553   -432    834       C  
ATOM   4552  N   ARG B 244       1.149  -7.648  78.402  1.00 45.26           N  
ANISOU 4552  N   ARG B 244     6489   5315   5394   -719   -401    660       N  
ATOM   4553  CA  ARG B 244       0.728  -7.183  77.079  1.00 46.58           C  
ANISOU 4553  CA  ARG B 244     6580   5492   5625   -734   -383    610       C  
ATOM   4554  C   ARG B 244      -0.610  -6.475  77.118  1.00 49.14           C  
ANISOU 4554  C   ARG B 244     6773   5953   5946   -820   -298    669       C  
ATOM   4555  O   ARG B 244      -1.546  -6.869  77.851  1.00 52.95           O  
ANISOU 4555  O   ARG B 244     7243   6490   6384   -925   -278    785       O  
ATOM   4556  CB  ARG B 244       0.619  -8.361  76.081  1.00 47.11           C  
ANISOU 4556  CB  ARG B 244     6764   5413   5724   -794   -481    623       C  
ATOM   4557  CG  ARG B 244       1.915  -9.054  75.669  1.00 46.87           C  
ANISOU 4557  CG  ARG B 244     6864   5240   5703   -677   -560    551       C  
ATOM   4558  CD  ARG B 244       2.843  -8.198  74.821  1.00 45.99           C  
ANISOU 4558  CD  ARG B 244     6681   5156   5636   -539   -528    431       C  
ATOM   4559  NE  ARG B 244       2.137  -7.536  73.725  1.00 47.45           N  
ANISOU 4559  NE  ARG B 244     6777   5387   5863   -584   -489    400       N  
ATOM   4560  CZ  ARG B 244       2.189  -7.922  72.450  1.00 48.67           C  
ANISOU 4560  CZ  ARG B 244     6990   5455   6046   -575   -533    356       C  
ATOM   4561  NH1 ARG B 244       2.923  -8.970  72.105  1.00 44.96           N  
ANISOU 4561  NH1 ARG B 244     6675   4844   5564   -511   -611    332       N  
ATOM   4562  NH2 ARG B 244       1.501  -7.248  71.523  1.00 47.33           N  
ANISOU 4562  NH2 ARG B 244     6733   5341   5911   -619   -498    336       N  
ATOM   4563  N   ILE B 245      -0.720  -5.439  76.312  1.00 47.71           N  
ANISOU 4563  N   ILE B 245     6488   5832   5806   -771   -245    600       N  
ATOM   4564  CA  ILE B 245      -2.032  -4.870  76.041  1.00 48.70           C  
ANISOU 4564  CA  ILE B 245     6489   6076   5939   -842   -179    657       C  
ATOM   4565  C   ILE B 245      -2.391  -5.397  74.672  1.00 48.00           C  
ANISOU 4565  C   ILE B 245     6414   5914   5908   -914   -248    653       C  
ATOM   4566  O   ILE B 245      -1.695  -5.105  73.703  1.00 44.36           O  
ANISOU 4566  O   ILE B 245     5972   5393   5490   -839   -270    553       O  
ATOM   4567  CB  ILE B 245      -2.016  -3.327  75.994  1.00 47.44           C  
ANISOU 4567  CB  ILE B 245     6219   6024   5781   -739    -80    586       C  
ATOM   4568  CG1 ILE B 245      -1.496  -2.755  77.325  1.00 44.77           C  
ANISOU 4568  CG1 ILE B 245     5901   5737   5375   -659    -26    569       C  
ATOM   4569  CG2 ILE B 245      -3.401  -2.786  75.600  1.00 43.73           C  
ANISOU 4569  CG2 ILE B 245     5616   5679   5322   -792    -14    651       C  
ATOM   4570  CD1 ILE B 245      -1.055  -1.308  77.190  1.00 42.62           C  
ANISOU 4570  CD1 ILE B 245     5579   5510   5103   -547     36    470       C  
ATOM   4571  N   TRP B 246      -3.469  -6.170  74.595  1.00 48.27           N  
ANISOU 4571  N   TRP B 246     6443   5958   5938  -1066   -285    766       N  
ATOM   4572  CA  TRP B 246      -3.824  -6.820  73.351  1.00 47.42           C  
ANISOU 4572  CA  TRP B 246     6383   5762   5873  -1156   -375    769       C  
ATOM   4573  C   TRP B 246      -4.317  -5.827  72.334  1.00 47.21           C  
ANISOU 4573  C   TRP B 246     6229   5821   5889  -1131   -332    728       C  
ATOM   4574  O   TRP B 246      -4.090  -5.999  71.136  1.00 46.72           O  
ANISOU 4574  O   TRP B 246     6219   5672   5861  -1128   -393    666       O  
ATOM   4575  CB  TRP B 246      -4.842  -7.924  73.593  1.00 50.12           C  
ANISOU 4575  CB  TRP B 246     6759   6089   6194  -1351   -443    913       C  
ATOM   4576  CG  TRP B 246      -4.244  -9.228  74.096  1.00 52.05           C  
ANISOU 4576  CG  TRP B 246     7203   6170   6406  -1391   -539    939       C  
ATOM   4577  CD1 TRP B 246      -3.148  -9.399  74.939  1.00 48.83           C  
ANISOU 4577  CD1 TRP B 246     6889   5698   5966  -1274   -532    893       C  
ATOM   4578  CD2 TRP B 246      -4.721 -10.598  73.816  1.00 51.43           C  
ANISOU 4578  CD2 TRP B 246     7269   5957   6316  -1565   -667   1027       C  
ATOM   4579  NE1 TRP B 246      -2.912 -10.732  75.167  1.00 50.66           N  
ANISOU 4579  NE1 TRP B 246     7308   5771   6169  -1343   -639    942       N  
ATOM   4580  CE2 TRP B 246      -3.816 -11.501  74.528  1.00 52.98           C  
ANISOU 4580  CE2 TRP B 246     7652   6006   6473  -1519   -724   1021       C  
ATOM   4581  CE3 TRP B 246      -5.754 -11.134  73.066  1.00 52.75           C  
ANISOU 4581  CE3 TRP B 246     7437   6108   6498  -1752   -749   1108       C  
ATOM   4582  CZ2 TRP B 246      -3.968 -12.884  74.485  1.00 55.49           C  
ANISOU 4582  CZ2 TRP B 246     8167   6152   6763  -1651   -853   1092       C  
ATOM   4583  CZ3 TRP B 246      -5.903 -12.520  73.029  1.00 55.49           C  
ANISOU 4583  CZ3 TRP B 246     7981   6284   6818  -1902   -885   1179       C  
ATOM   4584  CH2 TRP B 246      -5.032 -13.375  73.729  1.00 56.77           C  
ANISOU 4584  CH2 TRP B 246     8340   6292   6940  -1850   -934   1170       C  
ATOM   4585  N   ASN B 247      -4.966  -4.759  72.783  1.00 45.48           N  
ANISOU 4585  N   ASN B 247     5852   5769   5659  -1097   -224    758       N  
ATOM   4586  CA  ASN B 247      -5.442  -3.759  71.837  1.00 44.96           C  
ANISOU 4586  CA  ASN B 247     5669   5784   5630  -1058   -182    723       C  
ATOM   4587  C   ASN B 247      -4.281  -3.072  71.156  1.00 43.65           C  
ANISOU 4587  C   ASN B 247     5550   5544   5492   -918   -174    577       C  
ATOM   4588  O   ASN B 247      -3.194  -2.920  71.764  1.00 42.99           O  
ANISOU 4588  O   ASN B 247     5531   5412   5390   -822   -157    510       O  
ATOM   4589  CB  ASN B 247      -6.302  -2.730  72.553  1.00 47.80           C  
ANISOU 4589  CB  ASN B 247     5870   6331   5962  -1018    -60    782       C  
ATOM   4590  CG  ASN B 247      -7.420  -3.373  73.332  1.00 52.97           C  
ANISOU 4590  CG  ASN B 247     6455   7090   6580  -1150    -49    941       C  
ATOM   4591  OD1 ASN B 247      -7.173  -4.159  74.251  1.00 54.45           O  
ANISOU 4591  OD1 ASN B 247     6725   7236   6730  -1199    -69    989       O  
ATOM   4592  ND2 ASN B 247      -8.658  -3.058  72.961  1.00 53.07           N  
ANISOU 4592  ND2 ASN B 247     6311   7247   6605  -1210    -19   1034       N  
ATOM   4593  N   SER B 248      -4.491  -2.617  69.922  1.00 41.79           N  
ANISOU 4593  N   SER B 248     5275   5308   5294   -908   -187    535       N  
ATOM   4594  CA  SER B 248      -3.398  -1.921  69.241  1.00 42.03           C  
ANISOU 4594  CA  SER B 248     5341   5281   5347   -782   -172    408       C  
ATOM   4595  C   SER B 248      -3.299  -0.460  69.682  1.00 39.85           C  
ANISOU 4595  C   SER B 248     4973   5107   5063   -673    -65    369       C  
ATOM   4596  O   SER B 248      -2.211   0.102  69.675  1.00 38.02           O  
ANISOU 4596  O   SER B 248     4778   4834   4833   -577    -46    279       O  
ATOM   4597  CB  SER B 248      -3.491  -2.061  67.729  1.00 40.41           C  
ANISOU 4597  CB  SER B 248     5162   5019   5175   -806   -232    370       C  
ATOM   4598  OG  SER B 248      -4.714  -1.512  67.310  1.00 48.32           O  
ANISOU 4598  OG  SER B 248     6041   6132   6188   -859   -209    432       O  
ATOM   4599  N   GLN B 249      -4.425   0.144  70.069  1.00 38.05           N  
ANISOU 4599  N   GLN B 249     4630   5009   4818   -687      2    441       N  
ATOM   4600  CA  GLN B 249      -4.429   1.448  70.761  1.00 39.50           C  
ANISOU 4600  CA  GLN B 249     4758   5279   4971   -576    106    415       C  
ATOM   4601  C   GLN B 249      -5.381   1.346  71.961  1.00 43.12           C  
ANISOU 4601  C   GLN B 249     5150   5856   5377   -602    168    521       C  
ATOM   4602  O   GLN B 249      -6.258   0.470  71.976  1.00 40.99           O  
ANISOU 4602  O   GLN B 249     4835   5629   5109   -718    135    627       O  
ATOM   4603  CB  GLN B 249      -4.891   2.615  69.839  1.00 39.85           C  
ANISOU 4603  CB  GLN B 249     4725   5379   5039   -513    150    386       C  
ATOM   4604  CG  GLN B 249      -4.157   2.761  68.509  1.00 38.75           C  
ANISOU 4604  CG  GLN B 249     4632   5145   4945   -496     97    299       C  
ATOM   4605  CD  GLN B 249      -4.636   3.946  67.666  1.00 42.66           C  
ANISOU 4605  CD  GLN B 249     5060   5694   5456   -434    140    280       C  
ATOM   4606  OE1 GLN B 249      -5.442   4.777  68.098  1.00 48.01           O  
ANISOU 4606  OE1 GLN B 249     5660   6473   6108   -379    214    320       O  
ATOM   4607  NE2 GLN B 249      -4.148   4.013  66.437  1.00 46.05           N  
ANISOU 4607  NE2 GLN B 249     5525   6055   5918   -432     96    221       N  
ATOM   4608  N   LEU B 250      -5.241   2.251  72.938  1.00 40.77           N  
ANISOU 4608  N   LEU B 250     4851   5614   5024   -499    256    498       N  
ATOM   4609  CA  LEU B 250      -6.074   2.187  74.135  1.00 44.35           C  
ANISOU 4609  CA  LEU B 250     5253   6187   5410   -502    329    595       C  
ATOM   4610  C   LEU B 250      -7.523   2.525  73.795  1.00 45.71           C  
ANISOU 4610  C   LEU B 250     5271   6512   5584   -512    388    694       C  
ATOM   4611  O   LEU B 250      -8.446   1.945  74.352  1.00 48.52           O  
ANISOU 4611  O   LEU B 250     5547   6977   5911   -585    413    820       O  
ATOM   4612  CB  LEU B 250      -5.559   3.109  75.255  1.00 42.08           C  
ANISOU 4612  CB  LEU B 250     5027   5913   5047   -378    407    537       C  
ATOM   4613  CG  LEU B 250      -4.077   2.986  75.640  1.00 43.11           C  
ANISOU 4613  CG  LEU B 250     5293   5915   5171   -357    349    440       C  
ATOM   4614  CD1 LEU B 250      -3.703   4.076  76.645  1.00 44.59           C  
ANISOU 4614  CD1 LEU B 250     5543   6123   5278   -242    417    383       C  
ATOM   4615  CD2 LEU B 250      -3.763   1.598  76.187  1.00 39.49           C  
ANISOU 4615  CD2 LEU B 250     4891   5406   4706   -453    280    494       C  
ATOM   4616  N   VAL B 251      -7.718   3.459  72.877  1.00 44.79           N  
ANISOU 4616  N   VAL B 251     5106   6411   5500   -440    407    648       N  
ATOM   4617  CA  VAL B 251      -9.071   3.801  72.426  1.00 47.82           C  
ANISOU 4617  CA  VAL B 251     5332   6946   5891   -438    452    744       C  
ATOM   4618  C   VAL B 251      -9.160   3.489  70.940  1.00 48.76           C  
ANISOU 4618  C   VAL B 251     5427   7010   6088   -520    354    732       C  
ATOM   4619  O   VAL B 251      -8.365   4.013  70.167  1.00 47.43           O  
ANISOU 4619  O   VAL B 251     5334   6736   5951   -465    326    622       O  
ATOM   4620  CB  VAL B 251      -9.414   5.284  72.633  1.00 46.38           C  
ANISOU 4620  CB  VAL B 251     5113   6845   5664   -257    566    712       C  
ATOM   4621  CG1 VAL B 251     -10.871   5.533  72.274  1.00 48.21           C  
ANISOU 4621  CG1 VAL B 251     5161   7259   5898   -243    615    833       C  
ATOM   4622  CG2 VAL B 251      -9.131   5.707  74.058  1.00 46.69           C  
ANISOU 4622  CG2 VAL B 251     5224   6906   5611   -157    655    692       C  
ATOM   4623  N   ARG B 252     -10.107   2.616  70.577  1.00 49.02           N  
ANISOU 4623  N   ARG B 252     5363   7116   6145   -662    299    851       N  
ATOM   4624  CA  ARG B 252     -10.363   2.174  69.204  1.00 50.17           C  
ANISOU 4624  CA  ARG B 252     5492   7219   6352   -764    192    859       C  
ATOM   4625  C   ARG B 252     -11.823   1.785  69.041  1.00 50.85           C  
ANISOU 4625  C   ARG B 252     5405   7474   6444   -877    176   1021       C  
ATOM   4626  O   ARG B 252     -12.461   1.299  69.981  1.00 52.51           O  
ANISOU 4626  O   ARG B 252     5537   7793   6619   -942    212   1139       O  
ATOM   4627  CB  ARG B 252      -9.559   0.935  68.856  1.00 53.93           C  
ANISOU 4627  CB  ARG B 252     6115   7524   6853   -889     70    819       C  
ATOM   4628  CG  ARG B 252      -8.062   1.104  68.917  1.00 59.78           C  
ANISOU 4628  CG  ARG B 252     7013   8106   7594   -797     66    674       C  
ATOM   4629  CD  ARG B 252      -7.472   0.791  67.566  1.00 61.89           C  
ANISOU 4629  CD  ARG B 252     7368   8244   7903   -825    -29    595       C  
ATOM   4630  NE  ARG B 252      -7.642   1.941  66.702  1.00 64.53           N  
ANISOU 4630  NE  ARG B 252     7642   8621   8255   -735      9    550       N  
ATOM   4631  CZ  ARG B 252      -7.037   2.096  65.533  1.00 71.34           C  
ANISOU 4631  CZ  ARG B 252     8572   9390   9144   -712    -38    465       C  
ATOM   4632  NH1 ARG B 252      -6.208   1.154  65.075  1.00 70.78           N  
ANISOU 4632  NH1 ARG B 252     8632   9180   9080   -760   -121    411       N  
ATOM   4633  NH2 ARG B 252      -7.256   3.212  64.831  1.00 76.64           N  
ANISOU 4633  NH2 ARG B 252     9188  10108   9825   -629      2    437       N  
ATOM   4634  N   TYR B 253     -12.351   1.969  67.838  1.00 49.01           N  
ANISOU 4634  N   TYR B 253     5104   7267   6250   -911    117   1037       N  
ATOM   4635  CA  TYR B 253     -13.734   1.610  67.594  1.00 46.83           C  
ANISOU 4635  CA  TYR B 253     4647   7162   5983  -1032     84   1200       C  
ATOM   4636  C   TYR B 253     -13.902   0.181  67.052  1.00 46.16           C  
ANISOU 4636  C   TYR B 253     4618   6997   5925  -1273    -76   1260       C  
ATOM   4637  O   TYR B 253     -13.115  -0.271  66.226  1.00 42.50           O  
ANISOU 4637  O   TYR B 253     4318   6348   5484  -1315   -177   1158       O  
ATOM   4638  CB  TYR B 253     -14.380   2.616  66.645  1.00 47.84           C  
ANISOU 4638  CB  TYR B 253     4655   7392   6132   -940    101   1207       C  
ATOM   4639  CG  TYR B 253     -14.416   4.056  67.125  1.00 46.13           C  
ANISOU 4639  CG  TYR B 253     4386   7260   5881   -702    252   1166       C  
ATOM   4640  CD1 TYR B 253     -14.867   4.384  68.404  1.00 47.02           C  
ANISOU 4640  CD1 TYR B 253     4414   7515   5938   -611    382   1235       C  
ATOM   4641  CD2 TYR B 253     -14.034   5.093  66.276  1.00 43.72           C  
ANISOU 4641  CD2 TYR B 253     4130   6892   5591   -567    263   1061       C  
ATOM   4642  CE1 TYR B 253     -14.926   5.702  68.827  1.00 48.11           C  
ANISOU 4642  CE1 TYR B 253     4534   7716   6032   -383    515   1193       C  
ATOM   4643  CE2 TYR B 253     -14.080   6.417  66.685  1.00 44.56           C  
ANISOU 4643  CE2 TYR B 253     4217   7054   5660   -352    389   1024       C  
ATOM   4644  CZ  TYR B 253     -14.532   6.721  67.958  1.00 47.54           C  
ANISOU 4644  CZ  TYR B 253     4525   7560   5977   -256    513   1086       C  
ATOM   4645  OH  TYR B 253     -14.592   8.035  68.352  1.00 47.20           O  
ANISOU 4645  OH  TYR B 253     4494   7557   5885    -32    634   1042       O  
ATOM   4646  N   ALA B 254     -14.971  -0.503  67.498  1.00 47.88           N  
ANISOU 4646  N   ALA B 254     4699   7359   6133  -1429    -99   1433       N  
ATOM   4647  CA  ALA B 254     -15.251  -1.900  67.145  1.00 46.52           C  
ANISOU 4647  CA  ALA B 254     4587   7114   5976  -1684   -258   1514       C  
ATOM   4648  C   ALA B 254     -15.471  -2.036  65.664  1.00 45.87           C  
ANISOU 4648  C   ALA B 254     4529   6971   5929  -1770   -394   1491       C  
ATOM   4649  O   ALA B 254     -15.975  -1.110  65.036  1.00 46.59           O  
ANISOU 4649  O   ALA B 254     4488   7179   6035  -1678   -361   1496       O  
ATOM   4650  CB  ALA B 254     -16.502  -2.416  67.888  1.00 50.04           C  
ANISOU 4650  CB  ALA B 254     4840   7771   6403  -1841   -246   1730       C  
ATOM   4651  N   GLY B 255     -15.109  -3.190  65.103  1.00 47.63           N  
ANISOU 4651  N   GLY B 255     4932   7008   6156  -1939   -551   1466       N  
ATOM   4652  CA  GLY B 255     -15.530  -3.546  63.738  1.00 49.66           C  
ANISOU 4652  CA  GLY B 255     5219   7219   6432  -2071   -707   1476       C  
ATOM   4653  C   GLY B 255     -16.350  -4.839  63.781  1.00 55.13           C  
ANISOU 4653  C   GLY B 255     5912   7919   7117  -2363   -856   1632       C  
ATOM   4654  O   GLY B 255     -15.820  -5.881  64.168  1.00 54.85           O  
ANISOU 4654  O   GLY B 255     6066   7714   7062  -2465   -924   1616       O  
ATOM   4655  N   TYR B 256     -17.638  -4.780  63.417  1.00 56.28           N  
ANISOU 4655  N   TYR B 256     5846   8262   7275  -2502   -912   1791       N  
ATOM   4656  CA  TYR B 256     -18.522  -5.991  63.465  1.00 63.66           C  
ANISOU 4656  CA  TYR B 256     6759   9225   8203  -2817  -1068   1966       C  
ATOM   4657  C   TYR B 256     -18.675  -6.617  62.096  1.00 65.24           C  
ANISOU 4657  C   TYR B 256     7099   9287   8401  -2989  -1280   1943       C  
ATOM   4658  O   TYR B 256     -19.274  -6.009  61.208  1.00 68.52           O  
ANISOU 4658  O   TYR B 256     7383   9819   8833  -2978  -1317   1966       O  
ATOM   4659  CB  TYR B 256     -19.951  -5.713  64.031  1.00 62.51           C  
ANISOU 4659  CB  TYR B 256     6271   9413   8066  -2911  -1014   2197       C  
ATOM   4660  CG  TYR B 256     -20.007  -5.035  65.405  1.00 67.23           C  
ANISOU 4660  CG  TYR B 256     6705  10190   8648  -2735   -793   2243       C  
ATOM   4661  CD1 TYR B 256     -19.539  -5.766  66.637  1.00 64.50           C  
ANISOU 4661  CD1 TYR B 256     6472   9766   8270  -2783   -746   2265       C  
ATOM   4662  CD2 TYR B 256     -20.223  -3.629  65.459  1.00 68.31           C  
ANISOU 4662  CD2 TYR B 256     6654  10510   8792  -2476   -629   2216       C  
ATOM   4663  CE1 TYR B 256     -19.494  -5.125  67.879  1.00 65.39           C  
ANISOU 4663  CE1 TYR B 256     6470  10022   8353  -2607   -545   2287       C  
ATOM   4664  CE2 TYR B 256     -20.244  -2.984  66.709  1.00 71.02           C  
ANISOU 4664  CE2 TYR B 256     6881  10999   9104  -2298   -428   2244       C  
ATOM   4665  CZ  TYR B 256     -19.981  -3.726  67.902  1.00 69.77           C  
ANISOU 4665  CZ  TYR B 256     6794  10805   8910  -2374   -387   2293       C  
ATOM   4666  OH  TYR B 256     -19.974  -3.068  69.121  1.00 70.42           O  
ANISOU 4666  OH  TYR B 256     6783  11025   8948  -2189   -190   2312       O  
ATOM   4667  N   ARG B 257     -18.130  -7.815  61.912  1.00 68.38           N  
ANISOU 4667  N   ARG B 257     7779   9432   8773  -3138  -1423   1895       N  
ATOM   4668  CA  ARG B 257     -18.272  -8.498  60.629  1.00 76.31           C  
ANISOU 4668  CA  ARG B 257     8956  10280   9757  -3310  -1638   1869       C  
ATOM   4669  C   ARG B 257     -19.725  -8.934  60.455  1.00 79.70           C  
ANISOU 4669  C   ARG B 257     9195  10894  10193  -3606  -1776   2093       C  
ATOM   4670  O   ARG B 257     -20.208  -9.752  61.217  1.00 75.32           O  
ANISOU 4670  O   ARG B 257     8615  10373   9632  -3815  -1824   2240       O  
ATOM   4671  CB  ARG B 257     -17.313  -9.685  60.512  1.00 80.49           C  
ANISOU 4671  CB  ARG B 257     9859  10480  10243  -3375  -1754   1759       C  
ATOM   4672  CG  ARG B 257     -16.977 -10.057  59.071  1.00 88.72           C  
ANISOU 4672  CG  ARG B 257    11148  11313  11248  -3409  -1919   1639       C  
ATOM   4673  CD  ARG B 257     -15.493 -10.389  58.909  1.00 95.00           C  
ANISOU 4673  CD  ARG B 257    12263  11825  12007  -3224  -1894   1431       C  
ATOM   4674  NE  ARG B 257     -15.115 -11.590  59.660  1.00 99.92           N  
ANISOU 4674  NE  ARG B 257    13100  12265  12600  -3333  -1957   1453       N  
ATOM   4675  CZ  ARG B 257     -13.863 -11.958  59.930  1.00100.18           C  
ANISOU 4675  CZ  ARG B 257    13369  12088  12606  -3168  -1911   1312       C  
ATOM   4676  NH1 ARG B 257     -12.833 -11.217  59.513  1.00 94.18           N  
ANISOU 4676  NH1 ARG B 257    12655  11282  11848  -2894  -1797   1139       N  
ATOM   4677  NH2 ARG B 257     -13.645 -13.071  60.626  1.00 95.68           N  
ANISOU 4677  NH2 ARG B 257    12987  11360  12006  -3280  -1981   1353       N  
ATOM   4678  N   GLN B 258     -20.419  -8.333  59.488  1.00 81.53           N  
ANISOU 4678  N   GLN B 258     9276  11263  10439  -3620  -1832   2127       N  
ATOM   4679  CA  GLN B 258     -21.804  -8.684  59.194  1.00 91.25           C  
ANISOU 4679  CA  GLN B 258    10305  12689  11679  -3901  -1979   2344       C  
ATOM   4680  C   GLN B 258     -21.811  -9.947  58.336  1.00 98.24           C  
ANISOU 4680  C   GLN B 258    11481  13328  12519  -4183  -2248   2336       C  
ATOM   4681  O   GLN B 258     -20.823 -10.234  57.641  1.00 98.32           O  
ANISOU 4681  O   GLN B 258    11813  13053  12491  -4096  -2307   2142       O  
ATOM   4682  CB  GLN B 258     -22.553  -7.548  58.472  1.00 89.03           C  
ANISOU 4682  CB  GLN B 258     9750  12652  11424  -3799  -1947   2390       C  
ATOM   4683  CG  GLN B 258     -22.352  -6.134  59.013  1.00 89.23           C  
ANISOU 4683  CG  GLN B 258     9567  12856  11480  -3460  -1691   2339       C  
ATOM   4684  CD  GLN B 258     -22.982  -5.890  60.381  1.00 91.07           C  
ANISOU 4684  CD  GLN B 258     9523  13350  11731  -3439  -1529   2505       C  
ATOM   4685  OE1 GLN B 258     -24.023  -5.238  60.492  1.00 92.32           O  
ANISOU 4685  OE1 GLN B 258     9355  13813  11908  -3418  -1471   2661       O  
ATOM   4686  NE2 GLN B 258     -22.337  -6.395  61.432  1.00 90.57           N  
ANISOU 4686  NE2 GLN B 258     9587  13173  11652  -3427  -1450   2472       N  
ATOM   4687  N   GLN B 259     -22.918 -10.695  58.395  1.00101.45           N  
ANISOU 4687  N   GLN B 259    11777  13846  12923  -4518  -2410   2550       N  
ATOM   4688  CA  GLN B 259     -23.083 -11.927  57.611  1.00104.91           C  
ANISOU 4688  CA  GLN B 259    12492  14058  13311  -4829  -2691   2568       C  
ATOM   4689  C   GLN B 259     -22.699 -11.733  56.138  1.00102.79           C  
ANISOU 4689  C   GLN B 259    12430  13621  13005  -4757  -2811   2401       C  
ATOM   4690  O   GLN B 259     -21.867 -12.479  55.610  1.00 98.77           O  
ANISOU 4690  O   GLN B 259    12308  12783  12435  -4766  -2922   2246       O  
ATOM   4691  CB  GLN B 259     -24.512 -12.478  57.735  1.00108.30           C  
ANISOU 4691  CB  GLN B 259    12693  14705  13752  -5204  -2851   2847       C  
ATOM   4692  CG  GLN B 259     -25.614 -11.433  57.619  1.00107.78           C  
ANISOU 4692  CG  GLN B 259    12176  15040  13736  -5167  -2778   3006       C  
ATOM   4693  CD  GLN B 259     -27.003 -12.048  57.570  1.00115.19           C  
ANISOU 4693  CD  GLN B 259    12895  16191  14681  -5562  -2968   3287       C  
ATOM   4694  OE1 GLN B 259     -27.316 -12.989  58.310  1.00114.67           O  
ANISOU 4694  OE1 GLN B 259    12854  16110  14605  -5822  -3036   3433       O  
ATOM   4695  NE2 GLN B 259     -27.850 -11.512  56.694  1.00115.72           N  
ANISOU 4695  NE2 GLN B 259    12741  16466  14763  -5614  -3060   3373       N  
ATOM   4696  N   ASP B 260     -23.270 -10.706  55.504  1.00102.56           N  
ANISOU 4696  N   ASP B 260    12147  13817  13003  -4661  -2777   2431       N  
ATOM   4697  CA  ASP B 260     -23.030 -10.410  54.080  1.00101.13           C  
ANISOU 4697  CA  ASP B 260    12124  13519  12783  -4594  -2886   2294       C  
ATOM   4698  C   ASP B 260     -21.645  -9.830  53.723  1.00 95.78           C  
ANISOU 4698  C   ASP B 260    11667  12639  12084  -4246  -2741   2031       C  
ATOM   4699  O   ASP B 260     -21.514  -9.100  52.745  1.00 95.10           O  
ANISOU 4699  O   ASP B 260    11584  12566  11985  -4104  -2739   1938       O  
ATOM   4700  CB  ASP B 260     -24.160  -9.534  53.509  1.00104.21           C  
ANISOU 4700  CB  ASP B 260    12165  14225  13206  -4620  -2913   2433       C  
ATOM   4701  CG  ASP B 260     -24.309  -8.214  54.243  1.00104.66           C  
ANISOU 4701  CG  ASP B 260    11869  14567  13329  -4338  -2645   2469       C  
ATOM   4702  OD1 ASP B 260     -23.565  -7.258  53.915  1.00104.44           O  
ANISOU 4702  OD1 ASP B 260    11882  14496  13305  -4029  -2501   2301       O  
ATOM   4703  OD2 ASP B 260     -25.163  -8.141  55.157  1.00104.63           O  
ANISOU 4703  OD2 ASP B 260    11558  14829  13368  -4425  -2579   2669       O  
ATOM   4704  N   GLY B 261     -20.617 -10.138  54.504  1.00 92.13           N  
ANISOU 4704  N   GLY B 261    11383  12004  11619  -4112  -2621   1920       N  
ATOM   4705  CA  GLY B 261     -19.263  -9.762  54.115  1.00 92.02           C  
ANISOU 4705  CA  GLY B 261    11600  11786  11578  -3819  -2512   1681       C  
ATOM   4706  C   GLY B 261     -18.795  -8.354  54.463  1.00 89.33           C  
ANISOU 4706  C   GLY B 261    11053  11600  11289  -3491  -2259   1605       C  
ATOM   4707  O   GLY B 261     -17.589  -8.124  54.611  1.00 88.15           O  
ANISOU 4707  O   GLY B 261    11061  11301  11130  -3261  -2133   1436       O  
ATOM   4708  N   SER B 262     -19.729  -7.409  54.589  1.00 86.06           N  
ANISOU 4708  N   SER B 262    10292  11481  10924  -3465  -2188   1732       N  
ATOM   4709  CA  SER B 262     -19.395  -6.033  55.000  1.00 79.95           C  
ANISOU 4709  CA  SER B 262     9324  10859  10195  -3161  -1952   1676       C  
ATOM   4710  C   SER B 262     -18.862  -5.918  56.459  1.00 77.39           C  
ANISOU 4710  C   SER B 262     8947  10556   9900  -3035  -1761   1668       C  
ATOM   4711  O   SER B 262     -18.832  -6.907  57.211  1.00 74.73           O  
ANISOU 4711  O   SER B 262     8697  10143   9555  -3187  -1805   1725       O  
ATOM   4712  CB  SER B 262     -20.594  -5.089  54.775  1.00 79.69           C  
ANISOU 4712  CB  SER B 262     8946  11136  10198  -3156  -1931   1823       C  
ATOM   4713  OG  SER B 262     -21.758  -5.539  55.442  1.00 82.64           O  
ANISOU 4713  OG  SER B 262     9087  11717  10595  -3377  -1984   2046       O  
ATOM   4714  N   VAL B 263     -18.419  -4.711  56.829  1.00 68.16           N  
ANISOU 4714  N   VAL B 263     7659   9479   8758  -2759  -1558   1595       N  
ATOM   4715  CA  VAL B 263     -18.030  -4.409  58.195  1.00 64.04           C  
ANISOU 4715  CA  VAL B 263     7060   9014   8258  -2626  -1375   1595       C  
ATOM   4716  C   VAL B 263     -18.800  -3.181  58.716  1.00 63.77           C  
ANISOU 4716  C   VAL B 263     6702   9271   8257  -2482  -1218   1694       C  
ATOM   4717  O   VAL B 263     -18.753  -2.116  58.109  1.00 63.84           O  
ANISOU 4717  O   VAL B 263     6646   9337   8274  -2306  -1157   1633       O  
ATOM   4718  CB  VAL B 263     -16.489  -4.220  58.320  1.00 62.34           C  
ANISOU 4718  CB  VAL B 263     7075   8581   8029  -2412  -1275   1387       C  
ATOM   4719  CG1 VAL B 263     -16.093  -3.864  59.742  1.00 60.30           C  
ANISOU 4719  CG1 VAL B 263     6740   8385   7787  -2279  -1096   1388       C  
ATOM   4720  CG2 VAL B 263     -15.756  -5.485  57.905  1.00 63.04           C  
ANISOU 4720  CG2 VAL B 263     7480   8395   8078  -2530  -1418   1302       C  
ATOM   4721  N   ARG B 264     -19.530  -3.337  59.826  1.00 65.17           N  
ANISOU 4721  N   ARG B 264     6683   9633   8445  -2553  -1153   1852       N  
ATOM   4722  CA  ARG B 264     -20.061  -2.182  60.565  1.00 63.15           C  
ANISOU 4722  CA  ARG B 264     6158   9632   8204  -2363   -965   1923       C  
ATOM   4723  C   ARG B 264     -18.974  -1.674  61.531  1.00 57.31           C  
ANISOU 4723  C   ARG B 264     5522   8798   7454  -2135   -785   1788       C  
ATOM   4724  O   ARG B 264     -18.452  -2.447  62.324  1.00 55.65           O  
ANISOU 4724  O   ARG B 264     5437   8477   7230  -2202   -779   1773       O  
ATOM   4725  CB  ARG B 264     -21.328  -2.550  61.328  1.00 68.95           C  
ANISOU 4725  CB  ARG B 264     6628  10628   8943  -2526   -962   2160       C  
ATOM   4726  CG  ARG B 264     -22.034  -1.381  62.002  1.00 74.32           C  
ANISOU 4726  CG  ARG B 264     7014  11597   9625  -2321   -773   2253       C  
ATOM   4727  CD  ARG B 264     -23.559  -1.541  61.948  1.00 80.78           C  
ANISOU 4727  CD  ARG B 264     7516  12721  10455  -2486   -830   2502       C  
ATOM   4728  NE  ARG B 264     -24.248  -0.370  62.512  1.00 86.76           N  
ANISOU 4728  NE  ARG B 264     7994  13765  11206  -2251   -641   2588       N  
ATOM   4729  CZ  ARG B 264     -24.447   0.802  61.888  1.00 89.83           C  
ANISOU 4729  CZ  ARG B 264     8290  14241  11603  -2030   -584   2547       C  
ATOM   4730  NH1 ARG B 264     -24.027   1.010  60.638  1.00 84.64           N  
ANISOU 4730  NH1 ARG B 264     7779  13419  10960  -2018   -699   2423       N  
ATOM   4731  NH2 ARG B 264     -25.081   1.785  62.523  1.00 91.77           N  
ANISOU 4731  NH2 ARG B 264     8299  14738  11831  -1807   -407   2632       N  
ATOM   4732  N   GLY B 265     -18.649  -0.384  61.465  1.00 49.53           N  
ANISOU 4732  N   GLY B 265     4493   7855   6472  -1876   -648   1696       N  
ATOM   4733  CA  GLY B 265     -17.641   0.182  62.336  1.00 49.74           C  
ANISOU 4733  CA  GLY B 265     4618   7797   6485  -1671   -492   1570       C  
ATOM   4734  C   GLY B 265     -16.265   0.142  61.689  1.00 47.33           C  
ANISOU 4734  C   GLY B 265     4579   7225   6179  -1601   -529   1370       C  
ATOM   4735  O   GLY B 265     -16.147   0.264  60.462  1.00 50.12           O  
ANISOU 4735  O   GLY B 265     5003   7503   6539  -1610   -618   1310       O  
ATOM   4736  N   ASP B 266     -15.217  -0.021  62.484  1.00 46.57           N  
ANISOU 4736  N   ASP B 266     4628   6996   6069  -1527   -460   1272       N  
ATOM   4737  CA  ASP B 266     -13.852   0.166  61.940  1.00 44.34           C  
ANISOU 4737  CA  ASP B 266     4562   6499   5786  -1417   -462   1086       C  
ATOM   4738  C   ASP B 266     -13.254  -1.169  61.515  1.00 44.77           C  
ANISOU 4738  C   ASP B 266     4828   6351   5832  -1568   -603   1040       C  
ATOM   4739  O   ASP B 266     -12.976  -2.013  62.378  1.00 44.38           O  
ANISOU 4739  O   ASP B 266     4852   6240   5770  -1642   -612   1063       O  
ATOM   4740  CB  ASP B 266     -12.962   0.878  62.954  1.00 44.13           C  
ANISOU 4740  CB  ASP B 266     4574   6447   5748  -1232   -313    997       C  
ATOM   4741  CG  ASP B 266     -11.600   1.262  62.387  1.00 44.87           C  
ANISOU 4741  CG  ASP B 266     4845   6362   5843  -1110   -302    824       C  
ATOM   4742  OD1 ASP B 266     -11.149   0.653  61.372  1.00 43.18           O  
ANISOU 4742  OD1 ASP B 266     4767   6010   5631  -1177   -410    763       O  
ATOM   4743  OD2 ASP B 266     -10.988   2.197  62.953  1.00 43.00           O  
ANISOU 4743  OD2 ASP B 266     4612   6127   5598   -947   -186    753       O  
ATOM   4744  N   PRO B 267     -13.074  -1.381  60.189  1.00 45.63           N  
ANISOU 4744  N   PRO B 267     5049   6352   5937  -1610   -715    977       N  
ATOM   4745  CA  PRO B 267     -12.594  -2.671  59.641  1.00 46.62           C  
ANISOU 4745  CA  PRO B 267     5400   6276   6039  -1745   -860    932       C  
ATOM   4746  C   PRO B 267     -11.196  -3.101  60.137  1.00 46.11           C  
ANISOU 4746  C   PRO B 267     5533   6029   5959  -1650   -820    808       C  
ATOM   4747  O   PRO B 267     -10.893  -4.299  60.187  1.00 47.27           O  
ANISOU 4747  O   PRO B 267     5852   6027   6083  -1758   -919    803       O  
ATOM   4748  CB  PRO B 267     -12.586  -2.430  58.125  1.00 44.91           C  
ANISOU 4748  CB  PRO B 267     5253   6003   5809  -1737   -945    868       C  
ATOM   4749  CG  PRO B 267     -13.613  -1.375  57.918  1.00 45.01           C  
ANISOU 4749  CG  PRO B 267     5028   6230   5845  -1701   -900    956       C  
ATOM   4750  CD  PRO B 267     -13.480  -0.461  59.109  1.00 45.49           C  
ANISOU 4750  CD  PRO B 267     4950   6407   5926  -1542   -721    964       C  
ATOM   4751  N   ALA B 268     -10.383  -2.138  60.532  1.00 43.35           N  
ANISOU 4751  N   ALA B 268     5157   5693   5620  -1454   -682    719       N  
ATOM   4752  CA  ALA B 268      -9.031  -2.421  61.033  1.00 45.31           C  
ANISOU 4752  CA  ALA B 268     5559   5799   5857  -1352   -639    610       C  
ATOM   4753  C   ALA B 268      -9.097  -3.145  62.396  1.00 46.71           C  
ANISOU 4753  C   ALA B 268     5738   5981   6028  -1420   -625    683       C  
ATOM   4754  O   ALA B 268      -8.107  -3.664  62.867  1.00 45.29           O  
ANISOU 4754  O   ALA B 268     5695   5679   5835  -1371   -620    618       O  
ATOM   4755  CB  ALA B 268      -8.230  -1.118  61.144  1.00 38.91           C  
ANISOU 4755  CB  ALA B 268     4701   5023   5058  -1150   -504    515       C  
ATOM   4756  N   ASN B 269     -10.274  -3.169  63.017  1.00 48.16           N  
ANISOU 4756  N   ASN B 269     5761   6319   6218  -1528   -616    825       N  
ATOM   4757  CA  ASN B 269     -10.403  -3.677  64.379  1.00 49.72           C  
ANISOU 4757  CA  ASN B 269     5935   6553   6403  -1581   -579    906       C  
ATOM   4758  C   ASN B 269     -11.306  -4.881  64.504  1.00 52.08           C  
ANISOU 4758  C   ASN B 269     6245   6852   6691  -1817   -699   1045       C  
ATOM   4759  O   ASN B 269     -11.674  -5.261  65.610  1.00 57.05           O  
ANISOU 4759  O   ASN B 269     6819   7550   7306  -1887   -667   1146       O  
ATOM   4760  CB  ASN B 269     -10.923  -2.583  65.301  1.00 48.33           C  
ANISOU 4760  CB  ASN B 269     5555   6580   6229  -1480   -430    963       C  
ATOM   4761  CG  ASN B 269      -9.994  -1.399  65.364  1.00 46.89           C  
ANISOU 4761  CG  ASN B 269     5385   6382   6049  -1262   -316    832       C  
ATOM   4762  OD1 ASN B 269      -8.769  -1.560  65.284  1.00 43.02           O  
ANISOU 4762  OD1 ASN B 269     5049   5742   5556  -1188   -324    714       O  
ATOM   4763  ND2 ASN B 269     -10.567  -0.195  65.507  1.00 42.75           N  
ANISOU 4763  ND2 ASN B 269     4702   6016   5527  -1157   -212    856       N  
ATOM   4764  N   VAL B 270     -11.652  -5.475  63.374  1.00 52.97           N  
ANISOU 4764  N   VAL B 270     6439   6885   6803  -1947   -842   1052       N  
ATOM   4765  CA  VAL B 270     -12.467  -6.685  63.323  1.00 58.85           C  
ANISOU 4765  CA  VAL B 270     7230   7598   7533  -2202   -990   1179       C  
ATOM   4766  C   VAL B 270     -11.971  -7.791  64.276  1.00 61.30           C  
ANISOU 4766  C   VAL B 270     7704   7771   7815  -2272  -1023   1200       C  
ATOM   4767  O   VAL B 270     -12.761  -8.365  65.036  1.00 67.27           O  
ANISOU 4767  O   VAL B 270     8388   8607   8563  -2443  -1050   1353       O  
ATOM   4768  CB  VAL B 270     -12.547  -7.199  61.866  1.00 58.33           C  
ANISOU 4768  CB  VAL B 270     7314   7396   7453  -2300  -1154   1133       C  
ATOM   4769  CG1 VAL B 270     -13.094  -8.617  61.795  1.00 62.44           C  
ANISOU 4769  CG1 VAL B 270     7973   7806   7945  -2566  -1334   1234       C  
ATOM   4770  CG2 VAL B 270     -13.416  -6.259  61.039  1.00 59.74           C  
ANISOU 4770  CG2 VAL B 270     7294   7749   7655  -2296  -1148   1173       C  
ATOM   4771  N   GLU B 271     -10.669  -8.060  64.241  1.00 57.33           N  
ANISOU 4771  N   GLU B 271     7410   7076   7296  -2136  -1018   1057       N  
ATOM   4772  CA  GLU B 271     -10.089  -9.205  64.910  1.00 57.63           C  
ANISOU 4772  CA  GLU B 271     7649   6944   7302  -2187  -1076   1060       C  
ATOM   4773  C   GLU B 271     -10.126  -9.001  66.429  1.00 56.96           C  
ANISOU 4773  C   GLU B 271     7447   6978   7215  -2156   -957   1136       C  
ATOM   4774  O   GLU B 271     -10.629  -9.862  67.170  1.00 55.75           O  
ANISOU 4774  O   GLU B 271     7322   6821   7041  -2322  -1009   1262       O  
ATOM   4775  CB  GLU B 271      -8.674  -9.444  64.368  1.00 59.23           C  
ANISOU 4775  CB  GLU B 271     8083   6935   7486  -2017  -1092    885       C  
ATOM   4776  CG  GLU B 271      -7.946 -10.654  64.930  1.00 71.59           C  
ANISOU 4776  CG  GLU B 271     9887   8300   9013  -2032  -1161    872       C  
ATOM   4777  CD  GLU B 271      -6.635 -10.985  64.201  1.00 77.37           C  
ANISOU 4777  CD  GLU B 271    10849   8829   9718  -1860  -1191    710       C  
ATOM   4778  OE1 GLU B 271      -5.836 -10.065  63.881  1.00 71.60           O  
ANISOU 4778  OE1 GLU B 271    10056   8144   9006  -1659  -1088    597       O  
ATOM   4779  OE2 GLU B 271      -6.399 -12.194  63.956  1.00 82.40           O  
ANISOU 4779  OE2 GLU B 271    11739   9259  10310  -1926  -1319    702       O  
ATOM   4780  N   ILE B 272      -9.640  -7.843  66.881  1.00 53.82           N  
ANISOU 4780  N   ILE B 272     6926   6689   6832  -1953   -803   1066       N  
ATOM   4781  CA  ILE B 272      -9.692  -7.464  68.298  1.00 49.86           C  
ANISOU 4781  CA  ILE B 272     6311   6317   6317  -1899   -678   1126       C  
ATOM   4782  C   ILE B 272     -11.133  -7.314  68.797  1.00 50.86           C  
ANISOU 4782  C   ILE B 272     6219   6665   6442  -2041   -644   1307       C  
ATOM   4783  O   ILE B 272     -11.425  -7.700  69.937  1.00 48.99           O  
ANISOU 4783  O   ILE B 272     5949   6491   6174  -2107   -606   1412       O  
ATOM   4784  CB  ILE B 272      -8.834  -6.209  68.618  1.00 49.55           C  
ANISOU 4784  CB  ILE B 272     6212   6331   6285  -1655   -534   1004       C  
ATOM   4785  CG1 ILE B 272      -8.817  -5.916  70.108  1.00 50.01           C  
ANISOU 4785  CG1 ILE B 272     6198   6494   6311  -1601   -422   1057       C  
ATOM   4786  CG2 ILE B 272      -9.281  -4.976  67.844  1.00 50.67           C  
ANISOU 4786  CG2 ILE B 272     6194   6601   6456  -1572   -471    972       C  
ATOM   4787  CD1 ILE B 272      -8.169  -7.040  70.896  1.00 53.50           C  
ANISOU 4787  CD1 ILE B 272     6814   6793   6718  -1648   -479   1071       C  
ATOM   4788  N   THR B 273     -12.032  -6.785  67.959  1.00 48.13           N  
ANISOU 4788  N   THR B 273     5720   6444   6123  -2088   -657   1351       N  
ATOM   4789  CA  THR B 273     -13.445  -6.800  68.317  1.00 52.09           C  
ANISOU 4789  CA  THR B 273     6005   7164   6623  -2242   -645   1542       C  
ATOM   4790  C   THR B 273     -13.865  -8.233  68.676  1.00 57.77           C  
ANISOU 4790  C   THR B 273     6823   7809   7320  -2498   -773   1675       C  
ATOM   4791  O   THR B 273     -14.503  -8.450  69.709  1.00 60.11           O  
ANISOU 4791  O   THR B 273     7003   8244   7590  -2587   -719   1823       O  
ATOM   4792  CB  THR B 273     -14.374  -6.180  67.232  1.00 50.78           C  
ANISOU 4792  CB  THR B 273     5669   7135   6490  -2276   -675   1583       C  
ATOM   4793  OG1 THR B 273     -14.042  -4.794  67.036  1.00 48.50           O  
ANISOU 4793  OG1 THR B 273     5290   6923   6216  -2034   -545   1475       O  
ATOM   4794  CG2 THR B 273     -15.855  -6.252  67.630  1.00 51.03           C  
ANISOU 4794  CG2 THR B 273     5451   7418   6519  -2439   -665   1802       C  
ATOM   4795  N   GLU B 274     -13.486  -9.205  67.844  1.00 62.29           N  
ANISOU 4795  N   GLU B 274     7622   8154   7892  -2612   -941   1623       N  
ATOM   4796  CA  GLU B 274     -13.959 -10.590  68.000  1.00 66.72           C  
ANISOU 4796  CA  GLU B 274     8307   8616   8429  -2882  -1093   1752       C  
ATOM   4797  C   GLU B 274     -13.336 -11.301  69.203  1.00 65.61           C  
ANISOU 4797  C   GLU B 274     8310   8371   8248  -2878  -1068   1769       C  
ATOM   4798  O   GLU B 274     -13.979 -12.122  69.843  1.00 64.88           O  
ANISOU 4798  O   GLU B 274     8215   8304   8131  -3087  -1123   1931       O  
ATOM   4799  CB  GLU B 274     -13.739 -11.385  66.712  1.00 72.28           C  
ANISOU 4799  CB  GLU B 274     9245   9091   9130  -2990  -1286   1680       C  
ATOM   4800  CG  GLU B 274     -14.943 -11.357  65.773  1.00 82.24           C  
ANISOU 4800  CG  GLU B 274    10370  10467  10408  -3186  -1394   1787       C  
ATOM   4801  CD  GLU B 274     -14.577 -11.507  64.298  1.00 87.99           C  
ANISOU 4801  CD  GLU B 274    11283  11015  11133  -3175  -1526   1655       C  
ATOM   4802  OE1 GLU B 274     -13.417 -11.878  63.996  1.00 92.01           O  
ANISOU 4802  OE1 GLU B 274    12057  11285  11619  -3046  -1552   1495       O  
ATOM   4803  OE2 GLU B 274     -15.453 -11.248  63.434  1.00 90.63           O  
ANISOU 4803  OE2 GLU B 274    11496  11457  11483  -3287  -1601   1715       O  
ATOM   4804  N   LEU B 275     -12.087 -10.964  69.508  1.00 63.14           N  
ANISOU 4804  N   LEU B 275     8113   7948   7929  -2645   -989   1611       N  
ATOM   4805  CA  LEU B 275     -11.426 -11.470  70.704  1.00 61.88           C  
ANISOU 4805  CA  LEU B 275     8070   7711   7730  -2602   -950   1619       C  
ATOM   4806  C   LEU B 275     -12.099 -10.972  71.980  1.00 64.15           C  
ANISOU 4806  C   LEU B 275     8137   8241   7995  -2608   -807   1753       C  
ATOM   4807  O   LEU B 275     -12.221 -11.724  72.948  1.00 67.68           O  
ANISOU 4807  O   LEU B 275     8641   8672   8400  -2716   -819   1862       O  
ATOM   4808  CB  LEU B 275      -9.941 -11.128  70.698  1.00 58.00           C  
ANISOU 4808  CB  LEU B 275     7723   7077   7238  -2346   -900   1425       C  
ATOM   4809  CG  LEU B 275      -9.138 -11.869  69.620  1.00 57.53           C  
ANISOU 4809  CG  LEU B 275     7923   6756   7178  -2327  -1037   1302       C  
ATOM   4810  CD1 LEU B 275      -7.783 -11.228  69.418  1.00 51.89           C  
ANISOU 4810  CD1 LEU B 275     7269   5972   6474  -2058   -962   1119       C  
ATOM   4811  CD2 LEU B 275      -8.995 -13.352  69.905  1.00 56.88           C  
ANISOU 4811  CD2 LEU B 275     8093   6464   7054  -2474  -1178   1361       C  
ATOM   4812  N   CYS B 276     -12.571  -9.729  71.976  1.00 61.64           N  
ANISOU 4812  N   CYS B 276     7579   8146   7696  -2491   -673   1753       N  
ATOM   4813  CA  CYS B 276     -13.306  -9.210  73.129  1.00 61.53           C  
ANISOU 4813  CA  CYS B 276     7351   8379   7648  -2479   -527   1884       C  
ATOM   4814  C   CYS B 276     -14.646  -9.933  73.326  1.00 64.86           C  
ANISOU 4814  C   CYS B 276     7644   8941   8057  -2754   -584   2114       C  
ATOM   4815  O   CYS B 276     -14.971 -10.301  74.455  1.00 69.29           O  
ANISOU 4815  O   CYS B 276     8167   9592   8569  -2826   -528   2244       O  
ATOM   4816  CB  CYS B 276     -13.507  -7.693  73.039  1.00 59.75           C  
ANISOU 4816  CB  CYS B 276     6919   8347   7436  -2270   -372   1825       C  
ATOM   4817  SG  CYS B 276     -11.975  -6.742  72.910  1.00 57.88           S  
ANISOU 4817  SG  CYS B 276     6812   7971   7209  -1972   -300   1577       S  
ATOM   4818  N   ILE B 277     -15.409 -10.147  72.245  1.00 62.62           N  
ANISOU 4818  N   ILE B 277     7297   8681   7814  -2915   -699   2172       N  
ATOM   4819  CA  ILE B 277     -16.685 -10.891  72.318  1.00 65.33           C  
ANISOU 4819  CA  ILE B 277     7515   9156   8151  -3212   -781   2403       C  
ATOM   4820  C   ILE B 277     -16.499 -12.315  72.844  1.00 67.21           C  
ANISOU 4820  C   ILE B 277     7975   9210   8352  -3427   -906   2486       C  
ATOM   4821  O   ILE B 277     -17.268 -12.779  73.686  1.00 70.51           O  
ANISOU 4821  O   ILE B 277     8288   9768   8735  -3601   -887   2684       O  
ATOM   4822  CB  ILE B 277     -17.440 -10.929  70.966  1.00 64.71           C  
ANISOU 4822  CB  ILE B 277     7361   9106   8121  -3362   -917   2438       C  
ATOM   4823  CG1 ILE B 277     -17.791  -9.497  70.502  1.00 63.86           C  
ANISOU 4823  CG1 ILE B 277     7008   9210   8046  -3157   -789   2389       C  
ATOM   4824  CG2 ILE B 277     -18.703 -11.795  71.064  1.00 65.51           C  
ANISOU 4824  CG2 ILE B 277     7345   9333   8214  -3702  -1027   2688       C  
ATOM   4825  CD1 ILE B 277     -18.381  -9.402  69.107  1.00 62.25           C  
ANISOU 4825  CD1 ILE B 277     6743   9023   7885  -3260   -919   2395       C  
ATOM   4826  N   GLN B 278     -15.472 -12.991  72.348  1.00 67.32           N  
ANISOU 4826  N   GLN B 278     8298   8913   8367  -3404  -1030   2340       N  
ATOM   4827  CA  GLN B 278     -15.184 -14.361  72.734  1.00 71.72           C  
ANISOU 4827  CA  GLN B 278     9116   9250   8886  -3582  -1165   2397       C  
ATOM   4828  C   GLN B 278     -14.681 -14.435  74.180  1.00 72.20           C  
ANISOU 4828  C   GLN B 278     9210   9329   8894  -3483  -1045   2423       C  
ATOM   4829  O   GLN B 278     -14.984 -15.392  74.891  1.00 77.66           O  
ANISOU 4829  O   GLN B 278     9985   9980   9542  -3678  -1104   2571       O  
ATOM   4830  CB  GLN B 278     -14.213 -14.973  71.727  1.00 74.87           C  
ANISOU 4830  CB  GLN B 278     9835   9319   9292  -3540  -1318   2222       C  
ATOM   4831  CG  GLN B 278     -13.367 -16.130  72.212  1.00 81.82           C  
ANISOU 4831  CG  GLN B 278    11040   9921  10125  -3566  -1412   2194       C  
ATOM   4832  CD  GLN B 278     -11.960 -16.069  71.641  1.00 85.26           C  
ANISOU 4832  CD  GLN B 278    11706  10122  10565  -3312  -1427   1959       C  
ATOM   4833  OE1 GLN B 278     -10.969 -16.150  72.381  1.00 88.21           O  
ANISOU 4833  OE1 GLN B 278    12197  10406  10914  -3140  -1367   1883       O  
ATOM   4834  NE2 GLN B 278     -11.861 -15.897  70.318  1.00 85.73           N  
ANISOU 4834  NE2 GLN B 278    11823  10099  10653  -3282  -1504   1848       N  
ATOM   4835  N   HIS B 279     -13.939 -13.415  74.617  1.00 70.28           N  
ANISOU 4835  N   HIS B 279     8906   9149   8649  -3193   -883   2287       N  
ATOM   4836  CA  HIS B 279     -13.576 -13.252  76.034  1.00 71.09           C  
ANISOU 4836  CA  HIS B 279     8995   9322   8693  -3082   -749   2316       C  
ATOM   4837  C   HIS B 279     -14.722 -12.674  76.876  1.00 71.72           C  
ANISOU 4837  C   HIS B 279     8777   9732   8741  -3130   -599   2496       C  
ATOM   4838  O   HIS B 279     -14.540 -12.353  78.047  1.00 73.53           O  
ANISOU 4838  O   HIS B 279     8966  10061   8911  -3019   -465   2522       O  
ATOM   4839  CB  HIS B 279     -12.253 -12.438  76.211  1.00 69.24           C  
ANISOU 4839  CB  HIS B 279     8840   9007   8459  -2765   -654   2099       C  
ATOM   4840  CG  HIS B 279     -10.969 -13.234  75.929  1.00 69.88           C  
ANISOU 4840  CG  HIS B 279     9234   8778   8541  -2702   -775   1961       C  
ATOM   4841  ND1 HIS B 279     -10.388 -13.291  74.704  1.00 68.84           N  
ANISOU 4841  ND1 HIS B 279     9226   8475   8455  -2641   -869   1817       N  
ATOM   4842  CD2 HIS B 279     -10.156 -14.005  76.775  1.00 73.69           C  
ANISOU 4842  CD2 HIS B 279     9925   9101   8974  -2674   -809   1955       C  
ATOM   4843  CE1 HIS B 279      -9.264 -14.051  74.748  1.00 68.42           C  
ANISOU 4843  CE1 HIS B 279     9440   8175   8382  -2567   -951   1722       C  
ATOM   4844  NE2 HIS B 279      -9.122 -14.492  76.017  1.00 73.62           N  
ANISOU 4844  NE2 HIS B 279    10150   8838   8986  -2588   -919   1808       N  
ATOM   4845  N   GLY B 280     -15.906 -12.509  76.285  1.00 72.80           N  
ANISOU 4845  N   GLY B 280     8698  10051   8910  -3282   -618   2623       N  
ATOM   4846  CA  GLY B 280     -17.145 -12.299  77.057  1.00 72.27           C  
ANISOU 4846  CA  GLY B 280     8352  10301   8805  -3389   -505   2847       C  
ATOM   4847  C   GLY B 280     -17.822 -10.934  77.039  1.00 71.14           C  
ANISOU 4847  C   GLY B 280     7899  10462   8671  -3215   -329   2861       C  
ATOM   4848  O   GLY B 280     -18.701 -10.679  77.859  1.00 70.79           O  
ANISOU 4848  O   GLY B 280     7631  10689   8578  -3241   -200   3032       O  
ATOM   4849  N   TRP B 281     -17.440 -10.056  76.114  1.00 66.91           N  
ANISOU 4849  N   TRP B 281     7349   9886   8189  -3032   -320   2689       N  
ATOM   4850  CA  TRP B 281     -18.005  -8.703  76.082  1.00 65.54           C  
ANISOU 4850  CA  TRP B 281     6911   9973   8017  -2836   -155   2686       C  
ATOM   4851  C   TRP B 281     -19.313  -8.687  75.382  1.00 64.56           C  
ANISOU 4851  C   TRP B 281     6538  10060   7931  -3004   -200   2852       C  
ATOM   4852  O   TRP B 281     -19.432  -9.264  74.315  1.00 64.56           O  
ANISOU 4852  O   TRP B 281     6608   9936   7987  -3179   -377   2848       O  
ATOM   4853  CB  TRP B 281     -17.046  -7.773  75.366  1.00 64.31           C  
ANISOU 4853  CB  TRP B 281     6853   9680   7902  -2584   -134   2442       C  
ATOM   4854  CG  TRP B 281     -17.549  -6.377  75.077  1.00 65.51           C  
ANISOU 4854  CG  TRP B 281     6780  10045   8065  -2381      2   2415       C  
ATOM   4855  CD1 TRP B 281     -18.002  -5.419  75.991  1.00 65.82           C  
ANISOU 4855  CD1 TRP B 281     6641  10323   8043  -2198    203   2465       C  
ATOM   4856  CD2 TRP B 281     -17.583  -5.704  73.767  1.00 64.06           C  
ANISOU 4856  CD2 TRP B 281     6552   9840   7948  -2308    -47   2314       C  
ATOM   4857  NE1 TRP B 281     -18.339  -4.246  75.347  1.00 66.15           N  
ANISOU 4857  NE1 TRP B 281     6537  10486   8113  -2023    275   2410       N  
ATOM   4858  CE2 TRP B 281     -18.098  -4.346  74.011  1.00 64.30           C  
ANISOU 4858  CE2 TRP B 281     6370  10105   7957  -2082    131   2320       C  
ATOM   4859  CE3 TRP B 281     -17.265  -6.081  72.469  1.00 61.09           C  
ANISOU 4859  CE3 TRP B 281     6296   9279   7634  -2398   -213   2227       C  
ATOM   4860  CZ2 TRP B 281     -18.283  -3.434  72.982  1.00 63.24           C  
ANISOU 4860  CZ2 TRP B 281     6148  10011   7869  -1964    132   2247       C  
ATOM   4861  CZ3 TRP B 281     -17.460  -5.154  71.439  1.00 61.42           C  
ANISOU 4861  CZ3 TRP B 281     6241   9374   7720  -2283   -206   2155       C  
ATOM   4862  CH2 TRP B 281     -17.944  -3.857  71.690  1.00 62.00           C  
ANISOU 4862  CH2 TRP B 281     6110   9669   7779  -2073    -39   2165       C  
ATOM   4863  N   THR B 282     -20.305  -8.025  75.969  1.00 65.36           N  
ANISOU 4863  N   THR B 282     6350  10487   7998  -2947    -42   3001       N  
ATOM   4864  CA  THR B 282     -21.537  -7.707  75.238  1.00 69.31           C  
ANISOU 4864  CA  THR B 282     6565  11233   8538  -3038    -59   3146       C  
ATOM   4865  C   THR B 282     -21.213  -6.564  74.241  1.00 69.69           C  
ANISOU 4865  C   THR B 282     6595  11247   8636  -2801    -37   2961       C  
ATOM   4866  O   THR B 282     -20.770  -5.479  74.663  1.00 68.27           O  
ANISOU 4866  O   THR B 282     6408  11105   8426  -2505    127   2838       O  
ATOM   4867  CB  THR B 282     -22.688  -7.293  76.185  1.00 70.69           C  
ANISOU 4867  CB  THR B 282     6419  11790   8651  -3012    122   3367       C  
ATOM   4868  OG1 THR B 282     -22.908  -8.320  77.161  1.00 72.96           O  
ANISOU 4868  OG1 THR B 282     6736  12102   8882  -3224    112   3535       O  
ATOM   4869  CG2 THR B 282     -23.991  -7.059  75.408  1.00 71.62           C  
ANISOU 4869  CG2 THR B 282     6220  12178   8813  -3124     87   3539       C  
ATOM   4870  N   PRO B 283     -21.384  -6.818  72.921  1.00 69.46           N  
ANISOU 4870  N   PRO B 283     6587  11129   8677  -2935   -209   2937       N  
ATOM   4871  CA  PRO B 283     -21.044  -5.799  71.906  1.00 69.89           C  
ANISOU 4871  CA  PRO B 283     6645  11133   8776  -2727   -201   2766       C  
ATOM   4872  C   PRO B 283     -22.243  -4.874  71.651  1.00 73.65           C  
ANISOU 4872  C   PRO B 283     6782  11940   9261  -2647   -109   2895       C  
ATOM   4873  O   PRO B 283     -23.358  -5.214  72.024  1.00 72.27           O  
ANISOU 4873  O   PRO B 283     6372  12018   9071  -2806    -96   3125       O  
ATOM   4874  CB  PRO B 283     -20.793  -6.650  70.661  1.00 69.03           C  
ANISOU 4874  CB  PRO B 283     6715  10793   8721  -2938   -437   2712       C  
ATOM   4875  CG  PRO B 283     -21.735  -7.816  70.826  1.00 68.66           C  
ANISOU 4875  CG  PRO B 283     6588  10832   8668  -3284   -562   2944       C  
ATOM   4876  CD  PRO B 283     -21.769  -8.104  72.300  1.00 67.96           C  
ANISOU 4876  CD  PRO B 283     6469  10836   8518  -3287   -433   3049       C  
ATOM   4877  N   GLY B 284     -22.033  -3.712  71.031  1.00 75.51           N  
ANISOU 4877  N   GLY B 284     6987  12186   9518  -2402    -45   2760       N  
ATOM   4878  CA  GLY B 284     -23.201  -2.928  70.561  1.00 77.32           C  
ANISOU 4878  CA  GLY B 284     6907  12708   9763  -2340      4   2887       C  
ATOM   4879  C   GLY B 284     -23.474  -3.285  69.121  1.00 79.95           C  
ANISOU 4879  C   GLY B 284     7248  12968  10162  -2520   -202   2889       C  
ATOM   4880  O   GLY B 284     -23.202  -4.498  68.727  1.00 77.23           O  
ANISOU 4880  O   GLY B 284     7083  12422   9837  -2793   -393   2893       O  
ATOM   4881  N   ASN B 285     -23.836  -2.203  68.329  1.00 80.89           N  
ANISOU 4881  N   ASN B 285     7230  13201  10306  -2339   -167   2853       N  
ATOM   4882  CA  ASN B 285     -23.983  -2.271  66.855  1.00 81.84           C  
ANISOU 4882  CA  ASN B 285     7374  13241  10479  -2444   -348   2817       C  
ATOM   4883  C   ASN B 285     -23.789  -0.905  66.187  1.00 78.35           C  
ANISOU 4883  C   ASN B 285     6907  12813  10050  -2150   -267   2685       C  
ATOM   4884  O   ASN B 285     -24.307  -0.660  65.100  1.00 85.09           O  
ANISOU 4884  O   ASN B 285     7667  13726  10936  -2188   -370   2715       O  
ATOM   4885  CB  ASN B 285     -25.348  -2.866  66.448  1.00 85.46           C  
ANISOU 4885  CB  ASN B 285     7572  13939  10959  -2718   -476   3068       C  
ATOM   4886  CG  ASN B 285     -26.492  -2.325  67.295  1.00 89.95           C  
ANISOU 4886  CG  ASN B 285     7778  14899  11499  -2631   -307   3281       C  
ATOM   4887  OD1 ASN B 285     -26.337  -2.117  68.502  1.00 90.64           O  
ANISOU 4887  OD1 ASN B 285     7843  15058  11536  -2495   -128   3295       O  
ATOM   4888  ND2 ASN B 285     -27.658  -2.123  66.675  1.00 92.05           N  
ANISOU 4888  ND2 ASN B 285     7755  15431  11790  -2707   -366   3457       N  
ATOM   4889  N   GLY B 286     -23.053  -0.017  66.848  1.00 72.73           N  
ANISOU 4889  N   GLY B 286     6285  12043   9306  -1867    -92   2544       N  
ATOM   4890  CA  GLY B 286     -22.767   1.301  66.304  1.00 68.80           C  
ANISOU 4890  CA  GLY B 286     5801  11527   8812  -1587    -12   2411       C  
ATOM   4891  C   GLY B 286     -21.574   1.274  65.368  1.00 66.68           C  
ANISOU 4891  C   GLY B 286     5821  10942   8574  -1577   -117   2194       C  
ATOM   4892  O   GLY B 286     -20.913   0.233  65.201  1.00 60.28           O  
ANISOU 4892  O   GLY B 286     5209   9919   7774  -1762   -241   2136       O  
ATOM   4893  N   ARG B 287     -21.310   2.423  64.744  1.00 64.82           N  
ANISOU 4893  N   ARG B 287     5608  10677   8343  -1356    -66   2081       N  
ATOM   4894  CA  ARG B 287     -20.163   2.573  63.863  1.00 62.89           C  
ANISOU 4894  CA  ARG B 287     5619  10159   8120  -1314   -139   1879       C  
ATOM   4895  C   ARG B 287     -18.968   3.077  64.684  1.00 59.74           C  
ANISOU 4895  C   ARG B 287     5405   9602   7691  -1127     -9   1715       C  
ATOM   4896  O   ARG B 287     -17.835   3.122  64.190  1.00 53.11           O  
ANISOU 4896  O   ARG B 287     4785   8531   6863  -1093    -50   1547       O  
ATOM   4897  CB  ARG B 287     -20.458   3.564  62.713  1.00 66.71           C  
ANISOU 4897  CB  ARG B 287     6043  10683   8620  -1186   -160   1847       C  
ATOM   4898  CG  ARG B 287     -21.813   3.456  62.011  1.00 70.32           C  
ANISOU 4898  CG  ARG B 287     6255  11367   9097  -1300   -253   2028       C  
ATOM   4899  CD  ARG B 287     -21.955   4.531  60.931  1.00 74.27           C  
ANISOU 4899  CD  ARG B 287     6729  11883   9606  -1137   -263   1977       C  
ATOM   4900  NE  ARG B 287     -20.917   4.395  59.894  1.00 80.83           N  
ANISOU 4900  NE  ARG B 287     7819  12442  10449  -1172   -370   1803       N  
ATOM   4901  CZ  ARG B 287     -20.638   5.305  58.962  1.00 78.09           C  
ANISOU 4901  CZ  ARG B 287     7537  12031  10103  -1026   -373   1710       C  
ATOM   4902  NH1 ARG B 287     -21.305   6.454  58.923  1.00 82.26           N  
ANISOU 4902  NH1 ARG B 287     7903  12730  10623   -824   -281   1767       N  
ATOM   4903  NH2 ARG B 287     -19.683   5.069  58.072  1.00 72.08           N  
ANISOU 4903  NH2 ARG B 287     7008  11035   9345  -1073   -464   1564       N  
ATOM   4904  N   PHE B 288     -19.235   3.468  65.933  1.00 59.26           N  
ANISOU 4904  N   PHE B 288     5251   9678   7587  -1005    147   1771       N  
ATOM   4905  CA  PHE B 288     -18.233   4.122  66.774  1.00 56.88           C  
ANISOU 4905  CA  PHE B 288     5107   9258   7246   -811    274   1629       C  
ATOM   4906  C   PHE B 288     -18.299   3.666  68.222  1.00 58.80           C  
ANISOU 4906  C   PHE B 288     5328   9574   7439   -829    368   1698       C  
ATOM   4907  O   PHE B 288     -18.172   4.482  69.137  1.00 60.52           O  
ANISOU 4907  O   PHE B 288     5552   9844   7599   -629    519   1665       O  
ATOM   4908  CB  PHE B 288     -18.370   5.646  66.689  1.00 55.80           C  
ANISOU 4908  CB  PHE B 288     4927   9190   7084   -536    398   1576       C  
ATOM   4909  CG  PHE B 288     -18.228   6.179  65.297  1.00 55.96           C  
ANISOU 4909  CG  PHE B 288     4987   9128   7146   -503    314   1503       C  
ATOM   4910  CD1 PHE B 288     -16.968   6.310  64.713  1.00 54.17           C  
ANISOU 4910  CD1 PHE B 288     4991   8653   6939   -488    262   1326       C  
ATOM   4911  CD2 PHE B 288     -19.350   6.521  64.553  1.00 56.57           C  
ANISOU 4911  CD2 PHE B 288     4866   9387   7240   -492    285   1621       C  
ATOM   4912  CE1 PHE B 288     -16.826   6.782  63.413  1.00 52.96           C  
ANISOU 4912  CE1 PHE B 288     4880   8427   6815   -463    189   1264       C  
ATOM   4913  CE2 PHE B 288     -19.212   7.002  63.257  1.00 57.93           C  
ANISOU 4913  CE2 PHE B 288     5087   9480   7443   -463    202   1556       C  
ATOM   4914  CZ  PHE B 288     -17.946   7.127  62.686  1.00 54.63           C  
ANISOU 4914  CZ  PHE B 288     4911   8806   7039   -451    157   1376       C  
ATOM   4915  N   ASP B 289     -18.500   2.359  68.416  1.00 57.70           N  
ANISOU 4915  N   ASP B 289     5181   9429   7312  -1073    272   1795       N  
ATOM   4916  CA  ASP B 289     -18.518   1.746  69.748  1.00 55.51           C  
ANISOU 4916  CA  ASP B 289     4903   9203   6985  -1127    340   1870       C  
ATOM   4917  C   ASP B 289     -17.081   1.622  70.262  1.00 54.14           C  
ANISOU 4917  C   ASP B 289     4993   8783   6794  -1070    348   1697       C  
ATOM   4918  O   ASP B 289     -16.241   0.953  69.648  1.00 52.25           O  
ANISOU 4918  O   ASP B 289     4931   8328   6594  -1178    221   1600       O  
ATOM   4919  CB  ASP B 289     -19.193   0.371  69.710  1.00 55.29           C  
ANISOU 4919  CB  ASP B 289     4799   9232   6978  -1426    217   2037       C  
ATOM   4920  CG  ASP B 289     -20.695   0.437  69.300  1.00 60.10           C  
ANISOU 4920  CG  ASP B 289     5109  10124   7602  -1510    203   2242       C  
ATOM   4921  OD1 ASP B 289     -21.347   1.485  69.527  1.00 61.07           O  
ANISOU 4921  OD1 ASP B 289     5050  10456   7697  -1308    342   2291       O  
ATOM   4922  OD2 ASP B 289     -21.225  -0.564  68.742  1.00 58.99           O  
ANISOU 4922  OD2 ASP B 289     4919   9996   7497  -1777     47   2356       O  
ATOM   4923  N   VAL B 290     -16.797   2.281  71.381  1.00 53.89           N  
ANISOU 4923  N   VAL B 290     4990   8791   6696   -891    496   1659       N  
ATOM   4924  CA  VAL B 290     -15.479   2.192  71.972  1.00 52.93           C  
ANISOU 4924  CA  VAL B 290     5097   8464   6552   -839    503   1512       C  
ATOM   4925  C   VAL B 290     -15.274   0.795  72.540  1.00 52.86           C  
ANISOU 4925  C   VAL B 290     5160   8387   6536  -1044    425   1578       C  
ATOM   4926  O   VAL B 290     -16.155   0.242  73.198  1.00 54.09           O  
ANISOU 4926  O   VAL B 290     5185   8706   6660  -1149    456   1745       O  
ATOM   4927  CB  VAL B 290     -15.241   3.246  73.057  1.00 52.45           C  
ANISOU 4927  CB  VAL B 290     5066   8455   6409   -607    667   1456       C  
ATOM   4928  CG1 VAL B 290     -13.827   3.089  73.621  1.00 48.74           C  
ANISOU 4928  CG1 VAL B 290     4831   7771   5919   -580    647   1309       C  
ATOM   4929  CG2 VAL B 290     -15.475   4.642  72.484  1.00 49.71           C  
ANISOU 4929  CG2 VAL B 290     4670   8158   6061   -400    737   1394       C  
ATOM   4930  N   LEU B 291     -14.110   0.233  72.251  1.00 49.54           N  
ANISOU 4930  N   LEU B 291     4948   7729   6145  -1097    325   1454       N  
ATOM   4931  CA  LEU B 291     -13.785  -1.126  72.640  1.00 50.70           C  
ANISOU 4931  CA  LEU B 291     5206   7768   6290  -1281    230   1498       C  
ATOM   4932  C   LEU B 291     -13.334  -1.178  74.086  1.00 51.07           C  
ANISOU 4932  C   LEU B 291     5323   7819   6263  -1213    322   1498       C  
ATOM   4933  O   LEU B 291     -12.791  -0.188  74.593  1.00 52.36           O  
ANISOU 4933  O   LEU B 291     5529   7978   6386  -1017    424   1396       O  
ATOM   4934  CB  LEU B 291     -12.653  -1.654  71.744  1.00 50.21           C  
ANISOU 4934  CB  LEU B 291     5349   7451   6279  -1324     95   1357       C  
ATOM   4935  CG  LEU B 291     -12.976  -2.159  70.336  1.00 48.99           C  
ANISOU 4935  CG  LEU B 291     5196   7234   6184  -1461    -46   1367       C  
ATOM   4936  CD1 LEU B 291     -11.649  -2.385  69.613  1.00 45.46           C  
ANISOU 4936  CD1 LEU B 291     4965   6544   5764  -1418   -129   1197       C  
ATOM   4937  CD2 LEU B 291     -13.829  -3.435  70.378  1.00 47.95           C  
ANISOU 4937  CD2 LEU B 291     5030   7136   6054  -1716   -152   1532       C  
ATOM   4938  N   PRO B 292     -13.531  -2.333  74.753  1.00 50.98           N  
ANISOU 4938  N   PRO B 292     5341   7803   6226  -1382    277   1611       N  
ATOM   4939  CA  PRO B 292     -12.889  -2.588  76.038  1.00 51.23           C  
ANISOU 4939  CA  PRO B 292     5488   7788   6188  -1338    329   1596       C  
ATOM   4940  C   PRO B 292     -11.414  -2.950  75.839  1.00 47.43           C  
ANISOU 4940  C   PRO B 292     5241   7050   5731  -1307    236   1435       C  
ATOM   4941  O   PRO B 292     -10.977  -3.184  74.718  1.00 44.82           O  
ANISOU 4941  O   PRO B 292     4982   6581   5467  -1344    130   1354       O  
ATOM   4942  CB  PRO B 292     -13.627  -3.820  76.556  1.00 53.06           C  
ANISOU 4942  CB  PRO B 292     5680   8082   6396  -1561    282   1783       C  
ATOM   4943  CG  PRO B 292     -13.993  -4.551  75.321  1.00 55.30           C  
ANISOU 4943  CG  PRO B 292     5957   8296   6759  -1748    128   1821       C  
ATOM   4944  CD  PRO B 292     -14.356  -3.478  74.326  1.00 55.34           C  
ANISOU 4944  CD  PRO B 292     5834   8385   6809  -1635    161   1763       C  
ATOM   4945  N   LEU B 293     -10.668  -2.998  76.927  1.00 47.47           N  
ANISOU 4945  N   LEU B 293     5358   7003   5675  -1235    278   1395       N  
ATOM   4946  CA  LEU B 293      -9.288  -3.447  76.865  1.00 48.20           C  
ANISOU 4946  CA  LEU B 293     5653   6875   5784  -1210    189   1267       C  
ATOM   4947  C   LEU B 293      -9.153  -4.902  77.285  1.00 49.46           C  
ANISOU 4947  C   LEU B 293     5930   6932   5930  -1373     90   1351       C  
ATOM   4948  O   LEU B 293      -9.874  -5.369  78.173  1.00 51.17           O  
ANISOU 4948  O   LEU B 293     6095   7256   6091  -1466    128   1495       O  
ATOM   4949  CB  LEU B 293      -8.435  -2.585  77.760  1.00 48.73           C  
ANISOU 4949  CB  LEU B 293     5787   6934   5793  -1029    275   1164       C  
ATOM   4950  CG  LEU B 293      -8.323  -1.128  77.335  1.00 49.53           C  
ANISOU 4950  CG  LEU B 293     5830   7084   5905   -860    355   1056       C  
ATOM   4951  CD1 LEU B 293      -8.136  -0.269  78.566  1.00 46.98           C  
ANISOU 4951  CD1 LEU B 293     5529   6834   5486   -715    471   1029       C  
ATOM   4952  CD2 LEU B 293      -7.137  -0.986  76.397  1.00 50.84           C  
ANISOU 4952  CD2 LEU B 293     6103   7076   6137   -814    269    905       C  
ATOM   4953  N   LEU B 294      -8.241  -5.604  76.618  1.00 47.07           N  
ANISOU 4953  N   LEU B 294     5787   6424   5673  -1401    -35   1265       N  
ATOM   4954  CA  LEU B 294      -7.834  -6.933  76.980  1.00 48.00           C  
ANISOU 4954  CA  LEU B 294     6067   6396   5773  -1513   -139   1310       C  
ATOM   4955  C   LEU B 294      -6.427  -6.782  77.496  1.00 47.81           C  
ANISOU 4955  C   LEU B 294     6181   6257   5728  -1360   -140   1184       C  
ATOM   4956  O   LEU B 294      -5.497  -6.497  76.727  1.00 44.26           O  
ANISOU 4956  O   LEU B 294     5794   5699   5324  -1259   -178   1047       O  
ATOM   4957  CB  LEU B 294      -7.856  -7.887  75.773  1.00 50.82           C  
ANISOU 4957  CB  LEU B 294     6522   6599   6189  -1644   -289   1306       C  
ATOM   4958  CG  LEU B 294      -9.185  -8.521  75.345  1.00 56.23           C  
ANISOU 4958  CG  LEU B 294     7125   7353   6889  -1867   -348   1462       C  
ATOM   4959  CD1 LEU B 294      -8.994  -9.305  74.061  1.00 58.36           C  
ANISOU 4959  CD1 LEU B 294     7532   7438   7206  -1960   -503   1415       C  
ATOM   4960  CD2 LEU B 294      -9.775  -9.422  76.431  1.00 56.87           C  
ANISOU 4960  CD2 LEU B 294     7220   7476   6911  -2027   -357   1633       C  
ATOM   4961  N   LEU B 295      -6.281  -6.984  78.804  1.00 49.50           N  
ANISOU 4961  N   LEU B 295     6435   6504   5867  -1348    -98   1239       N  
ATOM   4962  CA  LEU B 295      -5.003  -6.867  79.463  1.00 49.59           C  
ANISOU 4962  CA  LEU B 295     6567   6427   5846  -1215   -104   1141       C  
ATOM   4963  C   LEU B 295      -4.529  -8.218  79.934  1.00 51.70           C  
ANISOU 4963  C   LEU B 295     7006   6551   6089  -1293   -208   1194       C  
ATOM   4964  O   LEU B 295      -5.306  -9.007  80.491  1.00 51.79           O  
ANISOU 4964  O   LEU B 295     7029   6591   6059  -1438   -221   1339       O  
ATOM   4965  CB  LEU B 295      -5.084  -5.889  80.635  1.00 49.73           C  
ANISOU 4965  CB  LEU B 295     6520   6592   5784  -1110     24   1143       C  
ATOM   4966  CG  LEU B 295      -5.674  -4.547  80.205  1.00 48.63           C  
ANISOU 4966  CG  LEU B 295     6225   6592   5660  -1025    131   1101       C  
ATOM   4967  CD1 LEU B 295      -5.814  -3.642  81.419  1.00 47.85           C  
ANISOU 4967  CD1 LEU B 295     6095   6625   5463   -915    257   1106       C  
ATOM   4968  CD2 LEU B 295      -4.839  -3.909  79.095  1.00 45.23           C  
ANISOU 4968  CD2 LEU B 295     5811   6069   5306   -929     93    948       C  
ATOM   4969  N   GLN B 296      -3.240  -8.467  79.711  1.00 49.43           N  
ANISOU 4969  N   GLN B 296     6849   6112   5821  -1191   -282   1083       N  
ATOM   4970  CA  GLN B 296      -2.638  -9.740  80.017  1.00 49.91           C  
ANISOU 4970  CA  GLN B 296     7092   6011   5861  -1228   -391   1115       C  
ATOM   4971  C   GLN B 296      -1.398  -9.549  80.888  1.00 51.38           C  
ANISOU 4971  C   GLN B 296     7352   6165   6004  -1080   -391   1046       C  
ATOM   4972  O   GLN B 296      -0.414  -8.867  80.513  1.00 44.97           O  
ANISOU 4972  O   GLN B 296     6524   5337   5224   -937   -387    918       O  
ATOM   4973  CB  GLN B 296      -2.338 -10.519  78.733  1.00 51.77           C  
ANISOU 4973  CB  GLN B 296     7435   6074   6161  -1257   -507   1066       C  
ATOM   4974  CG  GLN B 296      -1.635 -11.859  78.892  1.00 53.90           C  
ANISOU 4974  CG  GLN B 296     7925   6146   6409  -1265   -629   1084       C  
ATOM   4975  CD  GLN B 296      -1.201 -12.445  77.545  1.00 57.78           C  
ANISOU 4975  CD  GLN B 296     8534   6467   6952  -1241   -729   1004       C  
ATOM   4976  OE1 GLN B 296      -0.283 -11.950  76.867  1.00 53.30           O  
ANISOU 4976  OE1 GLN B 296     7955   5874   6421  -1085   -720    875       O  
ATOM   4977  NE2 GLN B 296      -1.846 -13.526  77.172  1.00 61.51           N  
ANISOU 4977  NE2 GLN B 296     9132   6821   7418  -1399   -826   1086       N  
ATOM   4978  N   ALA B 297      -1.526 -10.130  82.083  1.00 51.12           N  
ANISOU 4978  N   ALA B 297     7391   6140   5894  -1130   -395   1147       N  
ATOM   4979  CA  ALA B 297      -0.463 -10.363  83.020  1.00 51.62           C  
ANISOU 4979  CA  ALA B 297     7563   6149   5901  -1030   -431   1123       C  
ATOM   4980  C   ALA B 297       0.150 -11.703  82.624  1.00 53.59           C  
ANISOU 4980  C   ALA B 297     7995   6195   6172  -1044   -567   1132       C  
ATOM   4981  O   ALA B 297      -0.554 -12.550  82.071  1.00 55.73           O  
ANISOU 4981  O   ALA B 297     8326   6385   6465  -1179   -623   1204       O  
ATOM   4982  CB  ALA B 297      -1.056 -10.453  84.422  1.00 53.68           C  
ANISOU 4982  CB  ALA B 297     7827   6511   6059  -1094   -372   1244       C  
ATOM   4983  N   PRO B 298       1.441 -11.923  82.943  1.00 52.82           N  
ANISOU 4983  N   PRO B 298     7993   6015   6061   -904   -627   1067       N  
ATOM   4984  CA  PRO B 298       2.232 -13.050  82.447  1.00 52.24           C  
ANISOU 4984  CA  PRO B 298     8092   5748   6009   -853   -750   1048       C  
ATOM   4985  C   PRO B 298       1.622 -14.430  82.630  1.00 54.94           C  
ANISOU 4985  C   PRO B 298     8605   5953   6316   -997   -834   1173       C  
ATOM   4986  O   PRO B 298       1.168 -14.774  83.727  1.00 54.51           O  
ANISOU 4986  O   PRO B 298     8590   5933   6190  -1086   -825   1289       O  
ATOM   4987  CB  PRO B 298       3.511 -12.936  83.265  1.00 52.18           C  
ANISOU 4987  CB  PRO B 298     8122   5741   5962   -695   -776   1003       C  
ATOM   4988  CG  PRO B 298       3.648 -11.467  83.466  1.00 49.72           C  
ANISOU 4988  CG  PRO B 298     7635   5602   5656   -634   -677    928       C  
ATOM   4989  CD  PRO B 298       2.246 -11.078  83.839  1.00 49.87           C  
ANISOU 4989  CD  PRO B 298     7570   5736   5642   -778   -585   1012       C  
ATOM   4990  N   ASP B 299       1.623 -15.206  81.541  1.00 55.86           N  
ANISOU 4990  N   ASP B 299     8836   5909   6477  -1021   -920   1151       N  
ATOM   4991  CA  ASP B 299       1.139 -16.585  81.529  1.00 58.30           C  
ANISOU 4991  CA  ASP B 299     9351   6044   6757  -1159  -1027   1257       C  
ATOM   4992  C   ASP B 299      -0.310 -16.737  82.030  1.00 58.41           C  
ANISOU 4992  C   ASP B 299     9310   6144   6738  -1404   -995   1413       C  
ATOM   4993  O   ASP B 299      -0.701 -17.801  82.485  1.00 57.95           O  
ANISOU 4993  O   ASP B 299     9411   5977   6632  -1538  -1072   1535       O  
ATOM   4994  CB  ASP B 299       2.100 -17.495  82.321  1.00 60.20           C  
ANISOU 4994  CB  ASP B 299     9788   6146   6938  -1055  -1113   1283       C  
ATOM   4995  CG  ASP B 299       3.535 -17.392  81.818  1.00 61.64           C  
ANISOU 4995  CG  ASP B 299    10004   6265   7150   -807  -1144   1145       C  
ATOM   4996  OD1 ASP B 299       3.795 -17.693  80.626  1.00 62.06           O  
ANISOU 4996  OD1 ASP B 299    10128   6203   7249   -748  -1190   1067       O  
ATOM   4997  OD2 ASP B 299       4.401 -16.975  82.609  1.00 61.01           O  
ANISOU 4997  OD2 ASP B 299     9873   6264   7045   -670  -1121   1118       O  
ATOM   4998  N   GLU B 300      -1.091 -15.669  81.944  1.00 58.30           N  
ANISOU 4998  N   GLU B 300     9072   6332   6749  -1456   -880   1415       N  
ATOM   4999  CA  GLU B 300      -2.499 -15.729  82.318  1.00 62.55           C  
ANISOU 4999  CA  GLU B 300     9518   6988   7260  -1674   -835   1567       C  
ATOM   5000  C   GLU B 300      -3.346 -15.392  81.099  1.00 62.13           C  
ANISOU 5000  C   GLU B 300     9348   6979   7278  -1773   -829   1552       C  
ATOM   5001  O   GLU B 300      -2.895 -14.673  80.194  1.00 53.66           O  
ANISOU 5001  O   GLU B 300     8206   5917   6267  -1646   -806   1414       O  
ATOM   5002  CB  GLU B 300      -2.820 -14.768  83.486  1.00 66.86           C  
ANISOU 5002  CB  GLU B 300     9892   7762   7748  -1642   -691   1611       C  
ATOM   5003  CG  GLU B 300      -2.297 -15.192  84.862  1.00 66.97           C  
ANISOU 5003  CG  GLU B 300    10020   7757   7668  -1601   -699   1673       C  
ATOM   5004  CD  GLU B 300      -3.008 -16.426  85.445  1.00 78.72           C  
ANISOU 5004  CD  GLU B 300    11641   9172   9096  -1806   -764   1858       C  
ATOM   5005  OE1 GLU B 300      -4.021 -16.883  84.859  1.00 82.50           O  
ANISOU 5005  OE1 GLU B 300    12100   9642   9604  -2003   -796   1952       O  
ATOM   5006  OE2 GLU B 300      -2.564 -16.953  86.506  1.00 80.02           O  
ANISOU 5006  OE2 GLU B 300    11935   9289   9181  -1783   -791   1918       O  
ATOM   5007  N   ALA B 301      -4.561 -15.948  81.064  1.00 62.90           N  
ANISOU 5007  N   ALA B 301     9429   7104   7365  -2008   -857   1703       N  
ATOM   5008  CA  ALA B 301      -5.562 -15.520  80.097  1.00 60.76           C  
ANISOU 5008  CA  ALA B 301     9003   6932   7152  -2124   -840   1721       C  
ATOM   5009  C   ALA B 301      -5.750 -14.008  80.239  1.00 58.73           C  
ANISOU 5009  C   ALA B 301     8489   6914   6911  -1998   -677   1662       C  
ATOM   5010  O   ALA B 301      -5.725 -13.483  81.347  1.00 61.16           O  
ANISOU 5010  O   ALA B 301     8718   7358   7162  -1932   -571   1694       O  
ATOM   5011  CB  ALA B 301      -6.888 -16.248  80.328  1.00 61.33           C  
ANISOU 5011  CB  ALA B 301     9052   7053   7198  -2408   -879   1925       C  
ATOM   5012  N   PRO B 302      -5.943 -13.301  79.119  1.00 59.55           N  
ANISOU 5012  N   PRO B 302     8481   7063   7084  -1960   -659   1575       N  
ATOM   5013  CA  PRO B 302      -6.189 -11.856  79.203  1.00 58.96           C  
ANISOU 5013  CA  PRO B 302     8180   7202   7021  -1842   -510   1524       C  
ATOM   5014  C   PRO B 302      -7.524 -11.536  79.886  1.00 58.17           C  
ANISOU 5014  C   PRO B 302     7889   7331   6881  -1966   -409   1686       C  
ATOM   5015  O   PRO B 302      -8.389 -12.401  79.975  1.00 59.21           O  
ANISOU 5015  O   PRO B 302     8031   7468   6998  -2177   -466   1841       O  
ATOM   5016  CB  PRO B 302      -6.202 -11.429  77.729  1.00 56.73           C  
ANISOU 5016  CB  PRO B 302     7851   6886   6818  -1813   -543   1420       C  
ATOM   5017  CG  PRO B 302      -6.664 -12.665  77.009  1.00 59.55           C  
ANISOU 5017  CG  PRO B 302     8342   7092   7191  -2008   -692   1493       C  
ATOM   5018  CD  PRO B 302      -5.916 -13.760  77.717  1.00 59.33           C  
ANISOU 5018  CD  PRO B 302     8544   6885   7115  -2011   -775   1514       C  
ATOM   5019  N   GLU B 303      -7.679 -10.306  80.368  1.00 56.08           N  
ANISOU 5019  N   GLU B 303     7460   7255   6593  -1832   -261   1655       N  
ATOM   5020  CA  GLU B 303      -8.905  -9.905  81.042  1.00 58.55           C  
ANISOU 5020  CA  GLU B 303     7583   7807   6858  -1904   -142   1803       C  
ATOM   5021  C   GLU B 303      -9.527  -8.654  80.443  1.00 58.66           C  
ANISOU 5021  C   GLU B 303     7386   7995   6907  -1817    -38   1764       C  
ATOM   5022  O   GLU B 303      -8.837  -7.735  79.971  1.00 55.01           O  
ANISOU 5022  O   GLU B 303     6922   7502   6479  -1643     -9   1604       O  
ATOM   5023  CB  GLU B 303      -8.678  -9.685  82.533  1.00 62.69           C  
ANISOU 5023  CB  GLU B 303     8126   8416   7278  -1821    -41   1841       C  
ATOM   5024  CG  GLU B 303      -7.967 -10.814  83.260  1.00 67.42           C  
ANISOU 5024  CG  GLU B 303     8939   8847   7829  -1874   -135   1875       C  
ATOM   5025  CD  GLU B 303      -7.881 -10.583  84.764  1.00 72.73           C  
ANISOU 5025  CD  GLU B 303     9621   9627   8386  -1805    -32   1931       C  
ATOM   5026  OE1 GLU B 303      -8.631  -9.713  85.284  1.00 72.92           O  
ANISOU 5026  OE1 GLU B 303     9479   9872   8356  -1756    117   1981       O  
ATOM   5027  OE2 GLU B 303      -7.069 -11.283  85.424  1.00 73.16           O  
ANISOU 5027  OE2 GLU B 303     9858   9545   8395  -1793   -101   1926       O  
ATOM   5028  N   LEU B 304     -10.851  -8.621  80.519  1.00 59.70           N  
ANISOU 5028  N   LEU B 304     7336   8322   7026  -1940     19   1924       N  
ATOM   5029  CA  LEU B 304     -11.664  -7.587  79.915  1.00 56.08           C  
ANISOU 5029  CA  LEU B 304     6662   8047   6600  -1881    106   1926       C  
ATOM   5030  C   LEU B 304     -11.962  -6.457  80.901  1.00 53.50           C  
ANISOU 5030  C   LEU B 304     6208   7927   6192  -1705    295   1935       C  
ATOM   5031  O   LEU B 304     -12.311  -6.700  82.047  1.00 54.40           O  
ANISOU 5031  O   LEU B 304     6303   8148   6217  -1733    370   2050       O  
ATOM   5032  CB  LEU B 304     -12.953  -8.242  79.458  1.00 59.51           C  
ANISOU 5032  CB  LEU B 304     6959   8591   7061  -2117     54   2112       C  
ATOM   5033  CG  LEU B 304     -13.792  -7.621  78.355  1.00 61.50           C  
ANISOU 5033  CG  LEU B 304     7019   8969   7379  -2132     59   2126       C  
ATOM   5034  CD1 LEU B 304     -13.017  -7.477  77.043  1.00 59.43           C  
ANISOU 5034  CD1 LEU B 304     6872   8509   7199  -2075    -50   1949       C  
ATOM   5035  CD2 LEU B 304     -15.013  -8.510  78.184  1.00 62.40           C  
ANISOU 5035  CD2 LEU B 304     7016   9192   7502  -2409    -12   2344       C  
ATOM   5036  N   PHE B 305     -11.796  -5.222  80.447  1.00 52.58           N  
ANISOU 5036  N   PHE B 305     6023   7856   6097  -1520    368   1810       N  
ATOM   5037  CA  PHE B 305     -12.098  -4.029  81.233  1.00 52.54           C  
ANISOU 5037  CA  PHE B 305     5920   8030   6012  -1329    542   1800       C  
ATOM   5038  C   PHE B 305     -12.709  -2.954  80.343  1.00 52.29           C  
ANISOU 5038  C   PHE B 305     5725   8115   6028  -1228    602   1765       C  
ATOM   5039  O   PHE B 305     -12.074  -2.525  79.365  1.00 51.37           O  
ANISOU 5039  O   PHE B 305     5666   7867   5985  -1165    538   1622       O  
ATOM   5040  CB  PHE B 305     -10.831  -3.447  81.858  1.00 51.96           C  
ANISOU 5040  CB  PHE B 305     6019   7833   5892  -1149    566   1633       C  
ATOM   5041  CG  PHE B 305     -10.109  -4.383  82.768  1.00 51.17           C  
ANISOU 5041  CG  PHE B 305     6087   7616   5739  -1212    507   1652       C  
ATOM   5042  CD1 PHE B 305     -10.427  -4.435  84.131  1.00 53.26           C  
ANISOU 5042  CD1 PHE B 305     6353   8001   5882  -1192    607   1748       C  
ATOM   5043  CD2 PHE B 305      -9.106  -5.206  82.277  1.00 48.13           C  
ANISOU 5043  CD2 PHE B 305     5865   7005   5417  -1278    355   1575       C  
ATOM   5044  CE1 PHE B 305      -9.751  -5.299  84.981  1.00 54.69           C  
ANISOU 5044  CE1 PHE B 305     6698   8073   6010  -1248    547   1770       C  
ATOM   5045  CE2 PHE B 305      -8.427  -6.066  83.126  1.00 51.37           C  
ANISOU 5045  CE2 PHE B 305     6435   7306   5775  -1320    297   1595       C  
ATOM   5046  CZ  PHE B 305      -8.742  -6.111  84.480  1.00 52.44           C  
ANISOU 5046  CZ  PHE B 305     6574   7557   5794  -1310    389   1693       C  
ATOM   5047  N   VAL B 306     -13.933  -2.536  80.671  1.00 53.47           N  
ANISOU 5047  N   VAL B 306     5670   8514   6131  -1208    725   1904       N  
ATOM   5048  CA  VAL B 306     -14.576  -1.410  80.002  1.00 56.91           C  
ANISOU 5048  CA  VAL B 306     5946   9086   6591  -1073    804   1883       C  
ATOM   5049  C   VAL B 306     -14.009  -0.076  80.503  1.00 59.18           C  
ANISOU 5049  C   VAL B 306     6310   9364   6811   -802    923   1735       C  
ATOM   5050  O   VAL B 306     -13.895   0.168  81.710  1.00 60.46           O  
ANISOU 5050  O   VAL B 306     6528   9582   6862   -702   1027   1743       O  
ATOM   5051  CB  VAL B 306     -16.118  -1.433  80.125  1.00 57.90           C  
ANISOU 5051  CB  VAL B 306     5806   9502   6692  -1134    893   2096       C  
ATOM   5052  CG1 VAL B 306     -16.747  -0.380  79.212  1.00 56.58           C  
ANISOU 5052  CG1 VAL B 306     5478   9453   6568  -1005    941   2075       C  
ATOM   5053  CG2 VAL B 306     -16.663  -2.797  79.744  1.00 57.78           C  
ANISOU 5053  CG2 VAL B 306     5733   9490   6732  -1433    762   2256       C  
ATOM   5054  N   LEU B 307     -13.633   0.779  79.564  1.00 57.92           N  
ANISOU 5054  N   LEU B 307     6172   9123   6713   -692    899   1599       N  
ATOM   5055  CA  LEU B 307     -13.238   2.124  79.918  1.00 58.32           C  
ANISOU 5055  CA  LEU B 307     6291   9168   6702   -448   1003   1470       C  
ATOM   5056  C   LEU B 307     -14.453   2.933  80.371  1.00 62.98           C  
ANISOU 5056  C   LEU B 307     6707  10011   7210   -301   1172   1575       C  
ATOM   5057  O   LEU B 307     -15.523   2.864  79.761  1.00 63.39           O  
ANISOU 5057  O   LEU B 307     6554  10226   7304   -351   1186   1698       O  
ATOM   5058  CB  LEU B 307     -12.532   2.784  78.754  1.00 56.54           C  
ANISOU 5058  CB  LEU B 307     6134   8785   6562   -388    928   1313       C  
ATOM   5059  CG  LEU B 307     -11.170   2.119  78.528  1.00 56.39           C  
ANISOU 5059  CG  LEU B 307     6303   8527   6596   -479    790   1197       C  
ATOM   5060  CD1 LEU B 307     -10.618   2.384  77.136  1.00 54.10           C  
ANISOU 5060  CD1 LEU B 307     6045   8101   6409   -487    693   1085       C  
ATOM   5061  CD2 LEU B 307     -10.176   2.546  79.601  1.00 53.96           C  
ANISOU 5061  CD2 LEU B 307     6166   8132   6202   -365    827   1093       C  
ATOM   5062  N   PRO B 308     -14.311   3.661  81.489  1.00 64.77           N  
ANISOU 5062  N   PRO B 308     7017  10282   7310   -118   1300   1535       N  
ATOM   5063  CA  PRO B 308     -15.424   4.511  81.901  1.00 64.96           C  
ANISOU 5063  CA  PRO B 308     6895  10543   7245     64   1472   1621       C  
ATOM   5064  C   PRO B 308     -15.635   5.607  80.850  1.00 62.01           C  
ANISOU 5064  C   PRO B 308     6471  10163   6927    207   1481   1543       C  
ATOM   5065  O   PRO B 308     -14.707   6.362  80.559  1.00 60.21           O  
ANISOU 5065  O   PRO B 308     6419   9749   6711    307   1441   1368       O  
ATOM   5066  CB  PRO B 308     -14.954   5.083  83.252  1.00 66.07           C  
ANISOU 5066  CB  PRO B 308     7208  10665   7231    238   1581   1550       C  
ATOM   5067  CG  PRO B 308     -13.869   4.145  83.728  1.00 64.34           C  
ANISOU 5067  CG  PRO B 308     7163  10263   7019     81   1465   1500       C  
ATOM   5068  CD  PRO B 308     -13.205   3.661  82.472  1.00 64.84           C  
ANISOU 5068  CD  PRO B 308     7252  10143   7241    -73   1291   1426       C  
ATOM   5069  N   PRO B 309     -16.850   5.686  80.276  1.00 63.61           N  
ANISOU 5069  N   PRO B 309     6432  10575   7163    210   1526   1681       N  
ATOM   5070  CA  PRO B 309     -17.083   6.559  79.112  1.00 62.74           C  
ANISOU 5070  CA  PRO B 309     6262  10453   7122    312   1506   1624       C  
ATOM   5071  C   PRO B 309     -16.606   8.002  79.300  1.00 62.77           C  
ANISOU 5071  C   PRO B 309     6433  10364   7054    585   1587   1463       C  
ATOM   5072  O   PRO B 309     -16.168   8.638  78.334  1.00 57.53           O  
ANISOU 5072  O   PRO B 309     5837   9562   6459    629   1519   1349       O  
ATOM   5073  CB  PRO B 309     -18.605   6.493  78.930  1.00 60.88           C  
ANISOU 5073  CB  PRO B 309     5726  10521   6884    320   1588   1830       C  
ATOM   5074  CG  PRO B 309     -18.937   5.122  79.415  1.00 64.41           C  
ANISOU 5074  CG  PRO B 309     6077  11058   7337     73   1549   1989       C  
ATOM   5075  CD  PRO B 309     -18.067   4.929  80.635  1.00 63.01           C  
ANISOU 5075  CD  PRO B 309     6115  10762   7065    100   1587   1911       C  
ATOM   5076  N   GLU B 310     -16.679   8.500  80.536  1.00 66.07           N  
ANISOU 5076  N   GLU B 310     6932  10846   7326    759   1726   1457       N  
ATOM   5077  CA  GLU B 310     -16.209   9.849  80.853  1.00 67.35           C  
ANISOU 5077  CA  GLU B 310     7293  10900   7397   1013   1797   1303       C  
ATOM   5078  C   GLU B 310     -14.691  10.055  80.665  1.00 62.76           C  
ANISOU 5078  C   GLU B 310     6977  10016   6853    959   1669   1104       C  
ATOM   5079  O   GLU B 310     -14.241  11.184  80.564  1.00 59.36           O  
ANISOU 5079  O   GLU B 310     6708   9464   6383   1122   1684    972       O  
ATOM   5080  CB  GLU B 310     -16.647  10.275  82.263  1.00 72.25           C  
ANISOU 5080  CB  GLU B 310     7961  11658   7834   1212   1973   1342       C  
ATOM   5081  CG  GLU B 310     -16.011   9.483  83.393  1.00 78.39           C  
ANISOU 5081  CG  GLU B 310     8864  12380   8540   1100   1960   1339       C  
ATOM   5082  CD  GLU B 310     -16.849   8.288  83.838  1.00 85.11           C  
ANISOU 5082  CD  GLU B 310     9500  13451   9387    942   2000   1548       C  
ATOM   5083  OE1 GLU B 310     -17.482   7.619  82.976  1.00 86.37           O  
ANISOU 5083  OE1 GLU B 310     9438  13712   9666    778   1940   1671       O  
ATOM   5084  OE2 GLU B 310     -16.866   8.014  85.066  1.00 85.01           O  
ANISOU 5084  OE2 GLU B 310     9549  13507   9245    971   2087   1594       O  
ATOM   5085  N   LEU B 311     -13.911   8.975  80.626  1.00 62.68           N  
ANISOU 5085  N   LEU B 311     7012   9890   6914    733   1543   1091       N  
ATOM   5086  CA  LEU B 311     -12.462   9.083  80.371  1.00 59.44           C  
ANISOU 5086  CA  LEU B 311     6816   9219   6550    671   1417    921       C  
ATOM   5087  C   LEU B 311     -12.176   9.177  78.897  1.00 56.81           C  
ANISOU 5087  C   LEU B 311     6446   8781   6357    595   1305    866       C  
ATOM   5088  O   LEU B 311     -11.060   9.516  78.519  1.00 55.85           O  
ANISOU 5088  O   LEU B 311     6481   8465   6274    578   1218    728       O  
ATOM   5089  CB  LEU B 311     -11.672   7.883  80.926  1.00 59.02           C  
ANISOU 5089  CB  LEU B 311     6834   9079   6510    484   1326    926       C  
ATOM   5090  CG  LEU B 311     -11.430   7.741  82.432  1.00 65.51           C  
ANISOU 5090  CG  LEU B 311     7776   9923   7193    531   1392    933       C  
ATOM   5091  CD1 LEU B 311     -10.383   6.672  82.691  1.00 62.07           C  
ANISOU 5091  CD1 LEU B 311     7440   9346   6797    350   1264    905       C  
ATOM   5092  CD2 LEU B 311     -11.003   9.056  83.079  1.00 68.62           C  
ANISOU 5092  CD2 LEU B 311     8364  10244   7464    743   1459    804       C  
ATOM   5093  N   VAL B 312     -13.155   8.843  78.057  1.00 53.27           N  
ANISOU 5093  N   VAL B 312     5789   8469   5983    538   1302    981       N  
ATOM   5094  CA  VAL B 312     -12.886   8.772  76.629  1.00 51.59           C  
ANISOU 5094  CA  VAL B 312     5545   8157   5898    444   1184    938       C  
ATOM   5095  C   VAL B 312     -13.447   9.996  75.922  1.00 52.43           C  
ANISOU 5095  C   VAL B 312     5608   8309   6004    620   1239    917       C  
ATOM   5096  O   VAL B 312     -14.630  10.048  75.591  1.00 57.05           O  
ANISOU 5096  O   VAL B 312     5997   9082   6597    659   1293   1040       O  
ATOM   5097  CB  VAL B 312     -13.429   7.477  75.993  1.00 51.50           C  
ANISOU 5097  CB  VAL B 312     5367   8220   5979    224   1097   1065       C  
ATOM   5098  CG1 VAL B 312     -13.069   7.409  74.511  1.00 48.56           C  
ANISOU 5098  CG1 VAL B 312     4996   7730   5724    134    972   1005       C  
ATOM   5099  CG2 VAL B 312     -12.889   6.256  76.718  1.00 50.80           C  
ANISOU 5099  CG2 VAL B 312     5344   8074   5885     58   1041   1091       C  
ATOM   5100  N   LEU B 313     -12.591  10.990  75.709  1.00 50.92           N  
ANISOU 5100  N   LEU B 313     5599   7948   5801    724   1223    767       N  
ATOM   5101  CA  LEU B 313     -13.024  12.217  75.068  1.00 50.90           C  
ANISOU 5101  CA  LEU B 313     5595   7955   5788    900   1269    737       C  
ATOM   5102  C   LEU B 313     -13.134  12.010  73.549  1.00 51.65           C  
ANISOU 5102  C   LEU B 313     5590   8025   6009    794   1166    750       C  
ATOM   5103  O   LEU B 313     -12.212  11.498  72.891  1.00 48.43           O  
ANISOU 5103  O   LEU B 313     5250   7467   5682    639   1047    681       O  
ATOM   5104  CB  LEU B 313     -12.102  13.404  75.430  1.00 49.25           C  
ANISOU 5104  CB  LEU B 313     5639   7565   5509   1041   1284    580       C  
ATOM   5105  CG  LEU B 313     -12.460  14.795  74.831  1.00 50.74           C  
ANISOU 5105  CG  LEU B 313     5880   7727   5673   1240   1329    536       C  
ATOM   5106  CD1 LEU B 313     -13.826  15.326  75.297  1.00 49.32           C  
ANISOU 5106  CD1 LEU B 313     5584   7755   5401   1459   1478    640       C  
ATOM   5107  CD2 LEU B 313     -11.370  15.812  75.156  1.00 48.30           C  
ANISOU 5107  CD2 LEU B 313     5848   7201   5302   1316   1308    379       C  
ATOM   5108  N   GLU B 314     -14.272  12.423  73.005  1.00 54.13           N  
ANISOU 5108  N   GLU B 314     5742   8495   6330    890   1215    844       N  
ATOM   5109  CA  GLU B 314     -14.554  12.252  71.606  1.00 52.51           C  
ANISOU 5109  CA  GLU B 314     5429   8295   6228    800   1122    874       C  
ATOM   5110  C   GLU B 314     -15.036  13.548  71.000  1.00 53.53           C  
ANISOU 5110  C   GLU B 314     5559   8443   6337   1004   1171    857       C  
ATOM   5111  O   GLU B 314     -15.658  14.363  71.682  1.00 56.07           O  
ANISOU 5111  O   GLU B 314     5876   8864   6566   1219   1296    885       O  
ATOM   5112  CB  GLU B 314     -15.625  11.195  71.456  1.00 56.11           C  
ANISOU 5112  CB  GLU B 314     5640   8956   6724    665   1104   1046       C  
ATOM   5113  CG  GLU B 314     -15.146   9.806  71.831  1.00 59.81           C  
ANISOU 5113  CG  GLU B 314     6122   9378   7225    434   1027   1068       C  
ATOM   5114  CD  GLU B 314     -16.145   8.743  71.435  1.00 66.73           C  
ANISOU 5114  CD  GLU B 314     6778  10422   8154    258    972   1235       C  
ATOM   5115  OE1 GLU B 314     -16.191   8.395  70.236  1.00 71.37           O  
ANISOU 5115  OE1 GLU B 314     7325  10966   8824    136    854   1240       O  
ATOM   5116  OE2 GLU B 314     -16.902   8.273  72.311  1.00 70.96           O  
ANISOU 5116  OE2 GLU B 314     7184  11136   8642    236   1044   1367       O  
ATOM   5117  N   VAL B 315     -14.779  13.728  69.709  1.00 49.60           N  
ANISOU 5117  N   VAL B 315     5073   7854   5918    947   1074    817       N  
ATOM   5118  CA  VAL B 315     -15.137  14.956  69.022  1.00 48.69           C  
ANISOU 5118  CA  VAL B 315     4982   7730   5789   1130   1103    796       C  
ATOM   5119  C   VAL B 315     -16.148  14.641  67.928  1.00 50.15           C  
ANISOU 5119  C   VAL B 315     4947   8066   6041   1078   1049    918       C  
ATOM   5120  O   VAL B 315     -15.790  13.987  66.957  1.00 49.77           O  
ANISOU 5120  O   VAL B 315     4885   7948   6076    895    927    905       O  
ATOM   5121  CB  VAL B 315     -13.884  15.635  68.400  1.00 48.82           C  
ANISOU 5121  CB  VAL B 315     5228   7493   5828   1119   1033    639       C  
ATOM   5122  CG1 VAL B 315     -14.240  16.955  67.709  1.00 50.37           C  
ANISOU 5122  CG1 VAL B 315     5477   7661   6001   1309   1060    620       C  
ATOM   5123  CG2 VAL B 315     -12.805  15.840  69.460  1.00 45.43           C  
ANISOU 5123  CG2 VAL B 315     5009   6914   5338   1129   1058    525       C  
ATOM   5124  N   PRO B 316     -17.413  15.100  68.082  1.00 49.82           N  
ANISOU 5124  N   PRO B 316     4733   8239   5957   1246   1140   1039       N  
ATOM   5125  CA  PRO B 316     -18.376  15.022  66.989  1.00 50.68           C  
ANISOU 5125  CA  PRO B 316     4639   8495   6123   1224   1083   1154       C  
ATOM   5126  C   PRO B 316     -17.839  15.781  65.799  1.00 50.42           C  
ANISOU 5126  C   PRO B 316     4742   8289   6127   1257   1005   1056       C  
ATOM   5127  O   PRO B 316     -17.240  16.856  65.971  1.00 49.61           O  
ANISOU 5127  O   PRO B 316     4843   8032   5973   1418   1054    943       O  
ATOM   5128  CB  PRO B 316     -19.614  15.765  67.536  1.00 53.57           C  
ANISOU 5128  CB  PRO B 316     4851   9093   6411   1481   1224   1271       C  
ATOM   5129  CG  PRO B 316     -19.509  15.590  69.026  1.00 56.54           C  
ANISOU 5129  CG  PRO B 316     5271   9511   6702   1539   1344   1269       C  
ATOM   5130  CD  PRO B 316     -18.029  15.555  69.343  1.00 52.49           C  
ANISOU 5130  CD  PRO B 316     5040   8717   6187   1450   1297   1091       C  
ATOM   5131  N   LEU B 317     -18.044  15.242  64.602  1.00 48.64           N  
ANISOU 5131  N   LEU B 317     4418   8083   5981   1101    882   1101       N  
ATOM   5132  CA  LEU B 317     -17.510  15.904  63.426  1.00 50.69           C  
ANISOU 5132  CA  LEU B 317     4809   8182   6270   1119    806   1014       C  
ATOM   5133  C   LEU B 317     -18.535  16.759  62.700  1.00 53.70           C  
ANISOU 5133  C   LEU B 317     5073   8690   6640   1292    819   1100       C  
ATOM   5134  O   LEU B 317     -19.601  16.275  62.309  1.00 56.31           O  
ANISOU 5134  O   LEU B 317     5167   9230   6998   1244    782   1244       O  
ATOM   5135  CB  LEU B 317     -16.886  14.888  62.492  1.00 49.68           C  
ANISOU 5135  CB  LEU B 317     4704   7951   6219    860    660    979       C  
ATOM   5136  CG  LEU B 317     -15.668  14.203  63.094  1.00 50.20           C  
ANISOU 5136  CG  LEU B 317     4926   7854   6294    722    644    872       C  
ATOM   5137  CD1 LEU B 317     -15.022  13.358  62.011  1.00 53.02           C  
ANISOU 5137  CD1 LEU B 317     5332   8095   6716    512    505    828       C  
ATOM   5138  CD2 LEU B 317     -14.654  15.210  63.633  1.00 47.97           C  
ANISOU 5138  CD2 LEU B 317     4869   7394   5963    855    713    735       C  
ATOM   5139  N   GLU B 318     -18.219  18.042  62.546  1.00 56.46           N  
ANISOU 5139  N   GLU B 318     5592   8915   6944   1492    866   1018       N  
ATOM   5140  CA  GLU B 318     -19.056  18.952  61.744  1.00 60.24           C  
ANISOU 5140  CA  GLU B 318     6003   9476   7410   1672    867   1085       C  
ATOM   5141  C   GLU B 318     -18.208  19.787  60.772  1.00 57.64           C  
ANISOU 5141  C   GLU B 318     5899   8914   7088   1692    805    970       C  
ATOM   5142  O   GLU B 318     -16.977  19.819  60.870  1.00 52.29           O  
ANISOU 5142  O   GLU B 318     5432   8021   6414   1600    784    837       O  
ATOM   5143  CB  GLU B 318     -19.930  19.852  62.639  1.00 64.62           C  
ANISOU 5143  CB  GLU B 318     6506  10171   7875   1974   1018   1148       C  
ATOM   5144  CG  GLU B 318     -19.194  20.982  63.367  1.00 70.54           C  
ANISOU 5144  CG  GLU B 318     7544  10719   8540   2169   1110   1012       C  
ATOM   5145  CD  GLU B 318     -20.140  21.954  64.085  1.00 77.84           C  
ANISOU 5145  CD  GLU B 318     8440  11775   9362   2505   1255   1074       C  
ATOM   5146  OE1 GLU B 318     -20.952  21.473  64.913  1.00 76.63           O  
ANISOU 5146  OE1 GLU B 318     8087  11850   9177   2558   1344   1182       O  
ATOM   5147  OE2 GLU B 318     -20.068  23.194  63.828  1.00 77.53           O  
ANISOU 5147  OE2 GLU B 318     8583  11608   9266   2721   1282   1018       O  
ATOM   5148  N   HIS B 319     -18.878  20.477  59.852  1.00 57.81           N  
ANISOU 5148  N   HIS B 319     5868   8990   7106   1816    776   1030       N  
ATOM   5149  CA  HIS B 319     -18.196  21.279  58.833  1.00 56.01           C  
ANISOU 5149  CA  HIS B 319     5839   8560   6881   1833    714    944       C  
ATOM   5150  C   HIS B 319     -18.434  22.756  59.042  1.00 55.41           C  
ANISOU 5150  C   HIS B 319     5904   8422   6726   2128    799    925       C  
ATOM   5151  O   HIS B 319     -19.526  23.154  59.421  1.00 54.33           O  
ANISOU 5151  O   HIS B 319     5633   8463   6547   2340    876   1025       O  
ATOM   5152  CB  HIS B 319     -18.636  20.828  57.439  1.00 56.68           C  
ANISOU 5152  CB  HIS B 319     5793   8720   7023   1709    585   1019       C  
ATOM   5153  CG  HIS B 319     -17.746  21.328  56.330  1.00 58.47           C  
ANISOU 5153  CG  HIS B 319     6222   8735   7259   1653    507    926       C  
ATOM   5154  ND1 HIS B 319     -17.998  22.481  55.652  1.00 60.45           N  
ANISOU 5154  ND1 HIS B 319     6560   8935   7475   1829    506    937       N  
ATOM   5155  CD2 HIS B 319     -16.566  20.808  55.805  1.00 54.26           C  
ANISOU 5155  CD2 HIS B 319     5824   8030   6761   1442    434    825       C  
ATOM   5156  CE1 HIS B 319     -17.027  22.676  54.739  1.00 60.04           C  
ANISOU 5156  CE1 HIS B 319     6687   8691   7435   1718    434    852       C  
ATOM   5157  NE2 HIS B 319     -16.146  21.651  54.837  1.00 55.65           N  
ANISOU 5157  NE2 HIS B 319     6154   8069   6921   1485    395    783       N  
ATOM   5158  N   PRO B 320     -17.404  23.599  58.831  1.00 55.52           N  
ANISOU 5158  N   PRO B 320     6199   8182   6715   2149    789    801       N  
ATOM   5159  CA  PRO B 320     -17.596  25.056  58.982  1.00 59.44           C  
ANISOU 5159  CA  PRO B 320     6874   8583   7129   2426    857    778       C  
ATOM   5160  C   PRO B 320     -18.684  25.660  58.094  1.00 61.13           C  
ANISOU 5160  C   PRO B 320     6977   8916   7332   2606    838    889       C  
ATOM   5161  O   PRO B 320     -19.349  26.607  58.524  1.00 62.86           O  
ANISOU 5161  O   PRO B 320     7239   9170   7475   2892    925    922       O  
ATOM   5162  CB  PRO B 320     -16.217  25.648  58.599  1.00 56.97           C  
ANISOU 5162  CB  PRO B 320     6860   7975   6811   2327    805    641       C  
ATOM   5163  CG  PRO B 320     -15.507  24.548  57.888  1.00 54.08           C  
ANISOU 5163  CG  PRO B 320     6424   7592   6533   2029    705    619       C  
ATOM   5164  CD  PRO B 320     -15.999  23.285  58.558  1.00 52.96           C  
ANISOU 5164  CD  PRO B 320     6049   7646   6427   1929    723    679       C  
ATOM   5165  N   THR B 321     -18.859  25.150  56.871  1.00 60.83           N  
ANISOU 5165  N   THR B 321     6815   8938   7361   2455    724    945       N  
ATOM   5166  CA  THR B 321     -19.886  25.729  55.983  1.00 65.98           C  
ANISOU 5166  CA  THR B 321     7360   9709   8001   2622    691   1057       C  
ATOM   5167  C   THR B 321     -20.989  24.775  55.516  1.00 67.46           C  
ANISOU 5167  C   THR B 321     7205  10183   8242   2539    630   1210       C  
ATOM   5168  O   THR B 321     -22.111  25.208  55.261  1.00 73.19           O  
ANISOU 5168  O   THR B 321     7774  11090   8946   2733    642   1333       O  
ATOM   5169  CB  THR B 321     -19.293  26.515  54.790  1.00 67.19           C  
ANISOU 5169  CB  THR B 321     7723   9657   8148   2611    609   1005       C  
ATOM   5170  OG1 THR B 321     -18.569  25.638  53.912  1.00 70.28           O  
ANISOU 5170  OG1 THR B 321     8107   9990   8606   2315    496    968       O  
ATOM   5171  CG2 THR B 321     -18.354  27.620  55.285  1.00 68.68           C  
ANISOU 5171  CG2 THR B 321     8249   9573   8272   2715    667    878       C  
ATOM   5172  N   LEU B 322     -20.692  23.484  55.435  1.00 68.06           N  
ANISOU 5172  N   LEU B 322     7169  10307   8385   2256    561   1208       N  
ATOM   5173  CA  LEU B 322     -21.663  22.515  54.916  1.00 67.08           C  
ANISOU 5173  CA  LEU B 322     6746  10431   8311   2128    474   1350       C  
ATOM   5174  C   LEU B 322     -22.511  21.961  56.050  1.00 66.92           C  
ANISOU 5174  C   LEU B 322     6489  10652   8286   2172    562   1454       C  
ATOM   5175  O   LEU B 322     -22.031  21.154  56.838  1.00 63.68           O  
ANISOU 5175  O   LEU B 322     6083  10219   7894   2020    590   1408       O  
ATOM   5176  CB  LEU B 322     -20.965  21.394  54.124  1.00 63.13           C  
ANISOU 5176  CB  LEU B 322     6265   9846   7874   1800    338   1302       C  
ATOM   5177  CG  LEU B 322     -20.052  21.883  52.985  1.00 61.56           C  
ANISOU 5177  CG  LEU B 322     6300   9419   7672   1746    260   1202       C  
ATOM   5178  CD1 LEU B 322     -19.124  20.789  52.479  1.00 57.15           C  
ANISOU 5178  CD1 LEU B 322     5809   8748   7158   1451    165   1124       C  
ATOM   5179  CD2 LEU B 322     -20.809  22.570  51.841  1.00 57.83           C  
ANISOU 5179  CD2 LEU B 322     5778   9013   7180   1865    189   1291       C  
ATOM   5180  N   GLU B 323     -23.763  22.425  56.128  1.00 71.08           N  
ANISOU 5180  N   GLU B 323     6809  11414   8784   2391    610   1599       N  
ATOM   5181  CA  GLU B 323     -24.680  22.077  57.223  1.00 74.38           C  
ANISOU 5181  CA  GLU B 323     6985  12095   9182   2482    718   1719       C  
ATOM   5182  C   GLU B 323     -24.953  20.580  57.318  1.00 71.67           C  
ANISOU 5182  C   GLU B 323     6413  11914   8906   2177    641   1804       C  
ATOM   5183  O   GLU B 323     -24.951  20.013  58.413  1.00 69.19           O  
ANISOU 5183  O   GLU B 323     6035  11672   8582   2130    725   1817       O  
ATOM   5184  CB  GLU B 323     -26.002  22.844  57.098  1.00 81.95           C  
ANISOU 5184  CB  GLU B 323     7737  13301  10098   2776    771   1876       C  
ATOM   5185  CG  GLU B 323     -25.986  24.237  57.722  1.00 90.56           C  
ANISOU 5185  CG  GLU B 323     9019  14298  11091   3152    921   1818       C  
ATOM   5186  CD  GLU B 323     -26.969  25.210  57.060  1.00101.80           C  
ANISOU 5186  CD  GLU B 323    10348  15853  12478   3442    922   1931       C  
ATOM   5187  OE1 GLU B 323     -26.784  25.542  55.861  1.00105.47           O  
ANISOU 5187  OE1 GLU B 323    10900  16205  12968   3398    799   1914       O  
ATOM   5188  OE2 GLU B 323     -27.926  25.666  57.737  1.00106.25           O  
ANISOU 5188  OE2 GLU B 323    10754  16636  12979   3730   1051   2041       O  
ATOM   5189  N   TRP B 324     -25.171  19.940  56.171  1.00 70.96           N  
ANISOU 5189  N   TRP B 324     6220  11867   8874   1964    475   1862       N  
ATOM   5190  CA  TRP B 324     -25.498  18.509  56.141  1.00 69.10           C  
ANISOU 5190  CA  TRP B 324     5783  11774   8697   1659    374   1953       C  
ATOM   5191  C   TRP B 324     -24.405  17.660  56.735  1.00 64.49           C  
ANISOU 5191  C   TRP B 324     5367  11001   8134   1444    378   1824       C  
ATOM   5192  O   TRP B 324     -24.686  16.609  57.316  1.00 63.74           O  
ANISOU 5192  O   TRP B 324     5124  11030   8064   1266    367   1898       O  
ATOM   5193  CB  TRP B 324     -25.873  18.035  54.722  1.00 68.92           C  
ANISOU 5193  CB  TRP B 324     5668  11799   8719   1470    178   2023       C  
ATOM   5194  CG  TRP B 324     -24.861  18.454  53.698  1.00 66.87           C  
ANISOU 5194  CG  TRP B 324     5695  11255   8459   1437     99   1869       C  
ATOM   5195  CD1 TRP B 324     -24.931  19.545  52.833  1.00 66.70           C  
ANISOU 5195  CD1 TRP B 324     5765  11171   8408   1622     79   1855       C  
ATOM   5196  CD2 TRP B 324     -23.548  17.834  53.435  1.00 63.78           C  
ANISOU 5196  CD2 TRP B 324     5549  10594   8090   1216     39   1706       C  
ATOM   5197  NE1 TRP B 324     -23.790  19.637  52.070  1.00 66.90           N  
ANISOU 5197  NE1 TRP B 324     6065  10920   8435   1519     15   1704       N  
ATOM   5198  CE2 TRP B 324     -22.921  18.639  52.378  1.00 64.10           C  
ANISOU 5198  CE2 TRP B 324     5805  10438   8110   1282     -9   1609       C  
ATOM   5199  CE3 TRP B 324     -22.858  16.733  53.947  1.00 62.40           C  
ANISOU 5199  CE3 TRP B 324     5434  10331   7944    988     23   1639       C  
ATOM   5200  CZ2 TRP B 324     -21.662  18.334  51.875  1.00 63.16           C  
ANISOU 5200  CZ2 TRP B 324     5931  10067   8001   1125    -61   1458       C  
ATOM   5201  CZ3 TRP B 324     -21.585  16.440  53.441  1.00 58.30           C  
ANISOU 5201  CZ3 TRP B 324     5169   9549   7435    847    -33   1481       C  
ATOM   5202  CH2 TRP B 324     -21.003  17.219  52.429  1.00 58.83           C  
ANISOU 5202  CH2 TRP B 324     5423   9449   7482    914    -70   1395       C  
ATOM   5203  N   PHE B 325     -23.151  18.108  56.643  1.00 61.09           N  
ANISOU 5203  N   PHE B 325     5242  10277   7691   1461    394   1640       N  
ATOM   5204  CA  PHE B 325     -22.033  17.245  57.041  1.00 57.24           C  
ANISOU 5204  CA  PHE B 325     4913   9607   7230   1244    374   1518       C  
ATOM   5205  C   PHE B 325     -22.211  16.668  58.428  1.00 58.86           C  
ANISOU 5205  C   PHE B 325     5022   9920   7422   1224    476   1559       C  
ATOM   5206  O   PHE B 325     -22.056  15.465  58.615  1.00 60.51           O  
ANISOU 5206  O   PHE B 325     5181  10142   7669    982    412   1577       O  
ATOM   5207  CB  PHE B 325     -20.695  17.970  56.956  1.00 56.51           C  
ANISOU 5207  CB  PHE B 325     5138   9217   7116   1304    407   1331       C  
ATOM   5208  CG  PHE B 325     -19.499  17.065  57.102  1.00 53.26           C  
ANISOU 5208  CG  PHE B 325     4879   8622   6736   1076    361   1212       C  
ATOM   5209  CD1 PHE B 325     -19.083  16.631  58.342  1.00 51.49           C  
ANISOU 5209  CD1 PHE B 325     4685   8377   6501   1046    443   1173       C  
ATOM   5210  CD2 PHE B 325     -18.760  16.676  55.981  1.00 54.47           C  
ANISOU 5210  CD2 PHE B 325     5155   8621   6920    908    239   1138       C  
ATOM   5211  CE1 PHE B 325     -17.970  15.808  58.466  1.00 51.89           C  
ANISOU 5211  CE1 PHE B 325     4875   8262   6579    853    398   1068       C  
ATOM   5212  CE2 PHE B 325     -17.634  15.859  56.101  1.00 50.33           C  
ANISOU 5212  CE2 PHE B 325     4771   7933   6419    725    204   1030       C  
ATOM   5213  CZ  PHE B 325     -17.243  15.423  57.350  1.00 48.83           C  
ANISOU 5213  CZ  PHE B 325     4600   7728   6225    699    281    997       C  
ATOM   5214  N   ALA B 326     -22.536  17.520  59.402  1.00 61.18           N  
ANISOU 5214  N   ALA B 326     5307  10286   7654   1484    634   1573       N  
ATOM   5215  CA  ALA B 326     -22.735  17.064  60.794  1.00 62.79           C  
ANISOU 5215  CA  ALA B 326     5427  10604   7827   1495    749   1615       C  
ATOM   5216  C   ALA B 326     -23.792  15.954  60.895  1.00 64.09           C  
ANISOU 5216  C   ALA B 326     5277  11045   8027   1322    701   1804       C  
ATOM   5217  O   ALA B 326     -23.687  15.050  61.738  1.00 59.88           O  
ANISOU 5217  O   ALA B 326     4700  10554   7499   1174    725   1829       O  
ATOM   5218  CB  ALA B 326     -23.105  18.233  61.700  1.00 63.84           C  
ANISOU 5218  CB  ALA B 326     5588  10797   7870   1835    925   1618       C  
ATOM   5219  N   ALA B 327     -24.799  16.027  60.018  1.00 66.00           N  
ANISOU 5219  N   ALA B 327     5307  11477   8294   1329    625   1942       N  
ATOM   5220  CA  ALA B 327     -25.856  15.005  59.950  1.00 67.88           C  
ANISOU 5220  CA  ALA B 327     5233  11988   8570   1137    551   2139       C  
ATOM   5221  C   ALA B 327     -25.292  13.618  59.592  1.00 66.51           C  
ANISOU 5221  C   ALA B 327     5121  11693   8458    765    393   2106       C  
ATOM   5222  O   ALA B 327     -25.919  12.606  59.886  1.00 65.50           O  
ANISOU 5222  O   ALA B 327     4795  11738   8353    566    345   2245       O  
ATOM   5223  CB  ALA B 327     -26.959  15.425  58.979  1.00 68.70           C  
ANISOU 5223  CB  ALA B 327     5115  12303   8687   1215    478   2286       C  
ATOM   5224  N   LEU B 328     -24.092  13.561  59.000  1.00 64.71           N  
ANISOU 5224  N   LEU B 328     5173  11165   8249    676    318   1926       N  
ATOM   5225  CA  LEU B 328     -23.428  12.264  58.790  1.00 62.99           C  
ANISOU 5225  CA  LEU B 328     5055  10804   8074    363    191   1874       C  
ATOM   5226  C   LEU B 328     -23.149  11.439  60.067  1.00 62.36           C  
ANISOU 5226  C   LEU B 328     4980  10728   7987    259    260   1878       C  
ATOM   5227  O   LEU B 328     -22.847  10.253  59.966  1.00 66.01           O  
ANISOU 5227  O   LEU B 328     5482  11118   8482     -4    151   1877       O  
ATOM   5228  CB  LEU B 328     -22.142  12.409  57.970  1.00 63.31           C  
ANISOU 5228  CB  LEU B 328     5392  10537   8127    321    120   1681       C  
ATOM   5229  CG  LEU B 328     -22.287  12.955  56.551  1.00 63.91           C  
ANISOU 5229  CG  LEU B 328     5495  10576   8210    353     16   1671       C  
ATOM   5230  CD1 LEU B 328     -20.932  13.030  55.886  1.00 57.14           C  
ANISOU 5230  CD1 LEU B 328     4930   9424   7356    306    -31   1484       C  
ATOM   5231  CD2 LEU B 328     -23.259  12.124  55.721  1.00 66.60           C  
ANISOU 5231  CD2 LEU B 328     5641  11084   8582    148   -150   1820       C  
ATOM   5232  N   GLY B 329     -23.236  12.055  61.249  1.00 62.36           N  
ANISOU 5232  N   GLY B 329     4959  10800   7935    468    438   1881       N  
ATOM   5233  CA  GLY B 329     -22.984  11.358  62.526  1.00 60.10           C  
ANISOU 5233  CA  GLY B 329     4683  10525   7628    392    516   1889       C  
ATOM   5234  C   GLY B 329     -21.551  10.892  62.759  1.00 58.38           C  
ANISOU 5234  C   GLY B 329     4748  10015   7420    281    486   1709       C  
ATOM   5235  O   GLY B 329     -21.279  10.063  63.621  1.00 61.84           O  
ANISOU 5235  O   GLY B 329     5207  10437   7851    157    504   1718       O  
ATOM   5236  N   LEU B 330     -20.622  11.435  62.003  1.00 56.26           N  
ANISOU 5236  N   LEU B 330     4693   9521   7163    329    444   1553       N  
ATOM   5237  CA  LEU B 330     -19.230  11.098  62.174  1.00 53.07           C  
ANISOU 5237  CA  LEU B 330     4541   8856   6766    248    422   1387       C  
ATOM   5238  C   LEU B 330     -18.617  11.678  63.450  1.00 54.13           C  
ANISOU 5238  C   LEU B 330     4798   8925   6844    411    570   1303       C  
ATOM   5239  O   LEU B 330     -18.974  12.783  63.894  1.00 53.65           O  
ANISOU 5239  O   LEU B 330     4722   8933   6730    651    691   1307       O  
ATOM   5240  CB  LEU B 330     -18.438  11.555  60.946  1.00 53.60           C  
ANISOU 5240  CB  LEU B 330     4782   8726   6857    253    338   1260       C  
ATOM   5241  CG  LEU B 330     -18.308  10.604  59.747  1.00 53.26           C  
ANISOU 5241  CG  LEU B 330     4761   8613   6863     23    165   1261       C  
ATOM   5242  CD1 LEU B 330     -19.285   9.440  59.769  1.00 55.92           C  
ANISOU 5242  CD1 LEU B 330     4906   9118   7223   -182     75   1418       C  
ATOM   5243  CD2 LEU B 330     -18.452  11.382  58.459  1.00 52.53           C  
ANISOU 5243  CD2 LEU B 330     4689   8496   6776     99    107   1242       C  
ATOM   5244  N   ARG B 331     -17.665  10.934  64.014  1.00 50.79           N  
ANISOU 5244  N   ARG B 331     4515   8358   6427    285    552   1221       N  
ATOM   5245  CA  ARG B 331     -16.961  11.345  65.212  1.00 51.78           C  
ANISOU 5245  CA  ARG B 331     4776   8401   6496    402    666   1134       C  
ATOM   5246  C   ARG B 331     -15.574  10.654  65.311  1.00 51.08           C  
ANISOU 5246  C   ARG B 331     4889   8088   6431    259    599   1004       C  
ATOM   5247  O   ARG B 331     -15.265   9.693  64.579  1.00 49.74           O  
ANISOU 5247  O   ARG B 331     4739   7844   6315     66    475    997       O  
ATOM   5248  CB  ARG B 331     -17.819  11.016  66.430  1.00 56.56           C  
ANISOU 5248  CB  ARG B 331     5225   9213   7053    432    767   1263       C  
ATOM   5249  CG  ARG B 331     -18.019   9.518  66.578  1.00 60.70           C  
ANISOU 5249  CG  ARG B 331     5659   9789   7615    172    681   1355       C  
ATOM   5250  CD  ARG B 331     -19.304   9.186  67.294  1.00 68.98           C  
ANISOU 5250  CD  ARG B 331     6461  11115   8632    168    752   1547       C  
ATOM   5251  NE  ARG B 331     -19.123   9.288  68.737  1.00 76.54           N  
ANISOU 5251  NE  ARG B 331     7465  12104   9513    267    888   1540       N  
ATOM   5252  CZ  ARG B 331     -19.847  10.071  69.537  1.00 81.91           C  
ANISOU 5252  CZ  ARG B 331     8044  12963  10114    486   1045   1607       C  
ATOM   5253  NH1 ARG B 331     -20.828  10.822  69.044  1.00 80.05           N  
ANISOU 5253  NH1 ARG B 331     7641  12902   9872    638   1089   1694       N  
ATOM   5254  NH2 ARG B 331     -19.596  10.091  70.843  1.00 84.87           N  
ANISOU 5254  NH2 ARG B 331     8491  13347  10408    564   1159   1591       N  
ATOM   5255  N   TRP B 332     -14.723  11.169  66.183  1.00 46.85           N  
ANISOU 5255  N   TRP B 332     4511   7441   5850    361    676    900       N  
ATOM   5256  CA  TRP B 332     -13.454  10.513  66.453  1.00 48.10           C  
ANISOU 5256  CA  TRP B 332     4832   7420   6024    242    624    795       C  
ATOM   5257  C   TRP B 332     -12.999  10.808  67.863  1.00 51.15           C  
ANISOU 5257  C   TRP B 332     5312   7783   6341    335    722    751       C  
ATOM   5258  O   TRP B 332     -13.455  11.802  68.473  1.00 53.21           O  
ANISOU 5258  O   TRP B 332     5569   8115   6535    524    832    760       O  
ATOM   5259  CB  TRP B 332     -12.384  10.879  65.425  1.00 43.06           C  
ANISOU 5259  CB  TRP B 332     4347   6591   5423    226    551    667       C  
ATOM   5260  CG  TRP B 332     -11.383   9.779  65.290  1.00 39.37           C  
ANISOU 5260  CG  TRP B 332     3973   5992   4993     57    461    609       C  
ATOM   5261  CD1 TRP B 332     -10.096   9.719  65.834  1.00 39.00           C  
ANISOU 5261  CD1 TRP B 332     4082   5800   4935     50    464    501       C  
ATOM   5262  CD2 TRP B 332     -11.547   8.528  64.553  1.00 38.94           C  
ANISOU 5262  CD2 TRP B 332     3874   5932   4988   -128    347    656       C  
ATOM   5263  NE1 TRP B 332      -9.482   8.532  65.518  1.00 38.32           N  
ANISOU 5263  NE1 TRP B 332     4040   5632   4889   -103    371    483       N  
ATOM   5264  CE2 TRP B 332     -10.300   7.771  64.738  1.00 38.36           C  
ANISOU 5264  CE2 TRP B 332     3946   5703   4927   -214    297    567       C  
ATOM   5265  CE3 TRP B 332     -12.550   7.981  63.779  1.00 39.89           C  
ANISOU 5265  CE3 TRP B 332     3865   6154   5137   -227    275    759       C  
ATOM   5266  CZ2 TRP B 332     -10.122   6.511  64.187  1.00 35.96           C  
ANISOU 5266  CZ2 TRP B 332     3668   5339   4656   -376    188    579       C  
ATOM   5267  CZ3 TRP B 332     -12.350   6.712  63.223  1.00 39.67           C  
ANISOU 5267  CZ3 TRP B 332     3873   6057   5141   -413    153    768       C  
ATOM   5268  CH2 TRP B 332     -11.163   6.001  63.423  1.00 38.45           C  
ANISOU 5268  CH2 TRP B 332     3876   5741   4993   -477    115    676       C  
ATOM   5269  N   TYR B 333     -12.142   9.933  68.405  1.00 47.74           N  
ANISOU 5269  N   TYR B 333     4970   7253   5915    213    681    707       N  
ATOM   5270  CA  TYR B 333     -11.626  10.091  69.772  1.00 48.36           C  
ANISOU 5270  CA  TYR B 333     5149   7301   5923    279    756    664       C  
ATOM   5271  C   TYR B 333     -10.423  11.002  69.743  1.00 47.05           C  
ANISOU 5271  C   TYR B 333     5176   6958   5742    359    753    515       C  
ATOM   5272  O   TYR B 333      -9.838  11.219  68.690  1.00 44.80           O  
ANISOU 5272  O   TYR B 333     4946   6566   5511    324    684    449       O  
ATOM   5273  CB  TYR B 333     -11.245   8.755  70.402  1.00 46.47           C  
ANISOU 5273  CB  TYR B 333     4922   7041   5694    116    707    693       C  
ATOM   5274  CG  TYR B 333     -10.406   7.843  69.530  1.00 43.50           C  
ANISOU 5274  CG  TYR B 333     4611   6523   5393    -46    576    641       C  
ATOM   5275  CD1 TYR B 333     -11.003   6.948  68.626  1.00 44.18           C  
ANISOU 5275  CD1 TYR B 333     4599   6650   5538   -190    488    720       C  
ATOM   5276  CD2 TYR B 333      -9.016   7.842  69.631  1.00 40.67           C  
ANISOU 5276  CD2 TYR B 333     4416   5996   5041    -55    537    519       C  
ATOM   5277  CE1 TYR B 333     -10.218   6.096  67.835  1.00 44.18           C  
ANISOU 5277  CE1 TYR B 333     4686   6509   5590   -319    371    664       C  
ATOM   5278  CE2 TYR B 333      -8.231   7.000  68.858  1.00 39.19           C  
ANISOU 5278  CE2 TYR B 333     4287   5690   4912   -176    430    474       C  
ATOM   5279  CZ  TYR B 333      -8.832   6.130  67.957  1.00 41.67           C  
ANISOU 5279  CZ  TYR B 333     4526   6031   5274   -299    351    541       C  
ATOM   5280  OH  TYR B 333      -8.033   5.284  67.217  1.00 41.77           O  
ANISOU 5280  OH  TYR B 333     4626   5915   5329   -398    249    489       O  
ATOM   5281  N   ALA B 334     -10.065  11.521  70.906  1.00 45.94           N  
ANISOU 5281  N   ALA B 334     5142   6792   5521    458    825    469       N  
ATOM   5282  CA  ALA B 334      -9.135  12.609  71.011  1.00 43.74           C  
ANISOU 5282  CA  ALA B 334     5043   6367   5208    551    832    346       C  
ATOM   5283  C   ALA B 334      -7.704  12.098  71.134  1.00 43.40           C  
ANISOU 5283  C   ALA B 334     5122   6175   5194    429    748    256       C  
ATOM   5284  O   ALA B 334      -6.765  12.736  70.681  1.00 45.40           O  
ANISOU 5284  O   ALA B 334     5490   6297   5463    431    707    163       O  
ATOM   5285  CB  ALA B 334      -9.505  13.466  72.207  1.00 45.22           C  
ANISOU 5285  CB  ALA B 334     5302   6598   5280    725    944    340       C  
ATOM   5286  N   LEU B 335      -7.548  10.928  71.721  1.00 41.57           N  
ANISOU 5286  N   LEU B 335     4856   5968   4969    320    721    295       N  
ATOM   5287  CA  LEU B 335      -6.252  10.475  72.190  1.00 41.44           C  
ANISOU 5287  CA  LEU B 335     4955   5834   4955    242    660    222       C  
ATOM   5288  C   LEU B 335      -5.717   9.333  71.365  1.00 42.14           C  
ANISOU 5288  C   LEU B 335     5009   5870   5131     94    560    225       C  
ATOM   5289  O   LEU B 335      -6.227   8.234  71.459  1.00 42.49           O  
ANISOU 5289  O   LEU B 335     4975   5975   5195      6    538    304       O  
ATOM   5290  CB  LEU B 335      -6.358  10.008  73.649  1.00 41.63           C  
ANISOU 5290  CB  LEU B 335     5004   5913   4902    248    704    259       C  
ATOM   5291  CG  LEU B 335      -5.058   9.689  74.393  1.00 44.42           C  
ANISOU 5291  CG  LEU B 335     5486   6158   5235    196    648    188       C  
ATOM   5292  CD1 LEU B 335      -4.215  10.954  74.565  1.00 41.59           C  
ANISOU 5292  CD1 LEU B 335     5274   5695   4833    275    647     79       C  
ATOM   5293  CD2 LEU B 335      -5.348   9.040  75.749  1.00 42.27           C  
ANISOU 5293  CD2 LEU B 335     5218   5956   4885    189    688    248       C  
ATOM   5294  N   PRO B 336      -4.681   9.591  70.560  1.00 39.63           N  
ANISOU 5294  N   PRO B 336     4761   5438   4860     68    499    141       N  
ATOM   5295  CA  PRO B 336      -4.044   8.522  69.834  1.00 40.54           C  
ANISOU 5295  CA  PRO B 336     4867   5494   5041    -45    411    132       C  
ATOM   5296  C   PRO B 336      -2.983   7.872  70.721  1.00 36.96           C  
ANISOU 5296  C   PRO B 336     4491   4980   4571    -87    374     99       C  
ATOM   5297  O   PRO B 336      -1.956   8.469  70.944  1.00 36.29           O  
ANISOU 5297  O   PRO B 336     4487   4827   4472    -60    362     25       O  
ATOM   5298  CB  PRO B 336      -3.412   9.258  68.650  1.00 39.64           C  
ANISOU 5298  CB  PRO B 336     4788   5305   4967    -28    384     62       C  
ATOM   5299  CG  PRO B 336      -3.073  10.610  69.185  1.00 38.53           C  
ANISOU 5299  CG  PRO B 336     4732   5133   4776     65    432      6       C  
ATOM   5300  CD  PRO B 336      -4.069  10.899  70.274  1.00 40.92           C  
ANISOU 5300  CD  PRO B 336     5016   5523   5008    144    511     57       C  
ATOM   5301  N   ALA B 337      -3.260   6.669  71.219  1.00 37.75           N  
ANISOU 5301  N   ALA B 337     4565   5108   4669   -158    349    162       N  
ATOM   5302  CA  ALA B 337      -2.468   6.041  72.256  1.00 37.47           C  
ANISOU 5302  CA  ALA B 337     4598   5034   4603   -183    322    151       C  
ATOM   5303  C   ALA B 337      -2.095   4.632  71.841  1.00 42.35           C  
ANISOU 5303  C   ALA B 337     5225   5598   5268   -277    238    173       C  
ATOM   5304  O   ALA B 337      -2.821   3.666  72.141  1.00 45.85           O  
ANISOU 5304  O   ALA B 337     5638   6078   5706   -346    226    256       O  
ATOM   5305  CB  ALA B 337      -3.244   6.031  73.567  1.00 36.97           C  
ANISOU 5305  CB  ALA B 337     4524   5059   4463   -157    389    216       C  
ATOM   5306  N   VAL B 338      -0.973   4.520  71.130  1.00 41.06           N  
ANISOU 5306  N   VAL B 338     5106   5348   5145   -278    182    102       N  
ATOM   5307  CA  VAL B 338      -0.491   3.246  70.599  1.00 39.12           C  
ANISOU 5307  CA  VAL B 338     4893   5034   4937   -336    103    107       C  
ATOM   5308  C   VAL B 338      -0.092   2.319  71.753  1.00 38.22           C  
ANISOU 5308  C   VAL B 338     4835   4897   4788   -360     72    138       C  
ATOM   5309  O   VAL B 338       0.703   2.708  72.611  1.00 39.67           O  
ANISOU 5309  O   VAL B 338     5057   5077   4940   -316     79    103       O  
ATOM   5310  CB  VAL B 338       0.699   3.446  69.600  1.00 39.89           C  
ANISOU 5310  CB  VAL B 338     5020   5063   5074   -301     68     26       C  
ATOM   5311  CG1 VAL B 338       1.124   2.113  69.038  1.00 39.09           C  
ANISOU 5311  CG1 VAL B 338     4968   4889   4997   -334     -5     29       C  
ATOM   5312  CG2 VAL B 338       0.288   4.348  68.422  1.00 39.13           C  
ANISOU 5312  CG2 VAL B 338     4878   4985   5005   -283     96      2       C  
ATOM   5313  N   SER B 339      -0.608   1.087  71.751  1.00 36.52           N  
ANISOU 5313  N   SER B 339     4637   4661   4578   -436     27    205       N  
ATOM   5314  CA  SER B 339      -0.454   0.194  72.884  1.00 37.56           C  
ANISOU 5314  CA  SER B 339     4825   4775   4670   -468      0    255       C  
ATOM   5315  C   SER B 339       0.088  -1.185  72.506  1.00 43.20           C  
ANISOU 5315  C   SER B 339     5629   5381   5406   -507    -93    261       C  
ATOM   5316  O   SER B 339       0.170  -2.090  73.358  1.00 44.92           O  
ANISOU 5316  O   SER B 339     5910   5566   5590   -541   -129    312       O  
ATOM   5317  CB  SER B 339      -1.784   0.080  73.641  1.00 37.63           C  
ANISOU 5317  CB  SER B 339     4779   4880   4638   -528     50    359       C  
ATOM   5318  OG  SER B 339      -2.850  -0.308  72.782  1.00 38.41           O  
ANISOU 5318  OG  SER B 339     4820   5005   4771   -611     33    421       O  
ATOM   5319  N   ASN B 340       0.496  -1.353  71.248  1.00 43.53           N  
ANISOU 5319  N   ASN B 340     5691   5358   5492   -490   -133    208       N  
ATOM   5320  CA  ASN B 340       0.995  -2.666  70.804  1.00 44.00           C  
ANISOU 5320  CA  ASN B 340     5859   5300   5559   -505   -220    206       C  
ATOM   5321  C   ASN B 340       2.479  -2.742  70.438  1.00 41.20           C  
ANISOU 5321  C   ASN B 340     5554   4885   5217   -396   -245    124       C  
ATOM   5322  O   ASN B 340       2.933  -3.779  70.001  1.00 41.45           O  
ANISOU 5322  O   ASN B 340     5684   4818   5248   -377   -310    115       O  
ATOM   5323  CB  ASN B 340       0.144  -3.254  69.665  1.00 43.61           C  
ANISOU 5323  CB  ASN B 340     5833   5206   5531   -588   -268    232       C  
ATOM   5324  CG  ASN B 340       0.232  -2.454  68.350  1.00 47.16           C  
ANISOU 5324  CG  ASN B 340     6234   5669   6013   -543   -246    164       C  
ATOM   5325  OD1 ASN B 340      -0.278  -2.909  67.323  1.00 52.41           O  
ANISOU 5325  OD1 ASN B 340     6935   6289   6690   -597   -294    171       O  
ATOM   5326  ND2 ASN B 340       0.837  -1.273  68.374  1.00 39.85           N  
ANISOU 5326  ND2 ASN B 340     5239   4803   5097   -458   -180    106       N  
ATOM   5327  N   MET B 341       3.219  -1.654  70.594  1.00 39.54           N  
ANISOU 5327  N   MET B 341     5276   4734   5012   -324   -197     70       N  
ATOM   5328  CA  MET B 341       4.631  -1.646  70.176  1.00 40.79           C  
ANISOU 5328  CA  MET B 341     5447   4866   5184   -227   -216      6       C  
ATOM   5329  C   MET B 341       5.536  -1.918  71.357  1.00 40.68           C  
ANISOU 5329  C   MET B 341     5457   4857   5143   -183   -242     15       C  
ATOM   5330  O   MET B 341       5.169  -1.681  72.513  1.00 39.46           O  
ANISOU 5330  O   MET B 341     5296   4742   4955   -220   -227     52       O  
ATOM   5331  CB  MET B 341       5.030  -0.300  69.536  1.00 39.37           C  
ANISOU 5331  CB  MET B 341     5179   4750   5028   -190   -161    -51       C  
ATOM   5332  CG  MET B 341       4.396   0.000  68.184  1.00 43.00           C  
ANISOU 5332  CG  MET B 341     5620   5204   5515   -210   -141    -70       C  
ATOM   5333  SD  MET B 341       5.146   1.434  67.348  1.00 39.77           S  
ANISOU 5333  SD  MET B 341     5131   4850   5129   -159    -88   -133       S  
ATOM   5334  CE  MET B 341       6.741   0.764  66.913  1.00 43.32           C  
ANISOU 5334  CE  MET B 341     5601   5275   5583    -64   -119   -167       C  
ATOM   5335  N   LEU B 342       6.747  -2.364  71.076  1.00 41.43           N  
ANISOU 5335  N   LEU B 342     5574   4923   5245    -94   -277    -16       N  
ATOM   5336  CA  LEU B 342       7.662  -2.729  72.152  1.00 37.99           C  
ANISOU 5336  CA  LEU B 342     5157   4494   4783    -45   -316      1       C  
ATOM   5337  C   LEU B 342       8.671  -1.633  72.337  1.00 38.33           C  
ANISOU 5337  C   LEU B 342     5103   4626   4835     -5   -296    -37       C  
ATOM   5338  O   LEU B 342       9.153  -1.043  71.355  1.00 38.49           O  
ANISOU 5338  O   LEU B 342     5060   4678   4887     28   -269    -78       O  
ATOM   5339  CB  LEU B 342       8.353  -4.032  71.812  1.00 38.65           C  
ANISOU 5339  CB  LEU B 342     5331   4493   4862     40   -376      4       C  
ATOM   5340  CG  LEU B 342       9.389  -4.655  72.741  1.00 39.76           C  
ANISOU 5340  CG  LEU B 342     5502   4629   4976    120   -431     28       C  
ATOM   5341  CD1 LEU B 342       9.319  -6.149  72.508  1.00 38.93           C  
ANISOU 5341  CD1 LEU B 342     5547   4395   4852    164   -490     52       C  
ATOM   5342  CD2 LEU B 342      10.764  -4.092  72.389  1.00 38.83           C  
ANISOU 5342  CD2 LEU B 342     5280   4594   4878    223   -422    -11       C  
ATOM   5343  N   LEU B 343       8.978  -1.330  73.598  1.00 37.65           N  
ANISOU 5343  N   LEU B 343     5010   4581   4713    -19   -314    -17       N  
ATOM   5344  CA  LEU B 343       9.965  -0.290  73.875  1.00 38.49           C  
ANISOU 5344  CA  LEU B 343     5035   4767   4820     -4   -317    -46       C  
ATOM   5345  C   LEU B 343      11.282  -0.964  74.328  1.00 38.26           C  
ANISOU 5345  C   LEU B 343     4998   4757   4784     76   -385    -28       C  
ATOM   5346  O   LEU B 343      11.282  -1.705  75.303  1.00 41.24           O  
ANISOU 5346  O   LEU B 343     5440   5106   5122     85   -431     12       O  
ATOM   5347  CB  LEU B 343       9.407   0.733  74.874  1.00 36.15           C  
ANISOU 5347  CB  LEU B 343     4744   4509   4482    -75   -292    -45       C  
ATOM   5348  CG  LEU B 343      10.392   1.606  75.668  1.00 39.41           C  
ANISOU 5348  CG  LEU B 343     5124   4982   4867    -83   -329    -61       C  
ATOM   5349  CD1 LEU B 343      11.197   2.523  74.757  1.00 38.33           C  
ANISOU 5349  CD1 LEU B 343     4899   4892   4775    -83   -321    -99       C  
ATOM   5350  CD2 LEU B 343       9.662   2.433  76.720  1.00 36.97           C  
ANISOU 5350  CD2 LEU B 343     4869   4684   4493   -139   -304    -63       C  
ATOM   5351  N   GLU B 344      12.359  -0.775  73.572  1.00 37.98           N  
ANISOU 5351  N   GLU B 344     4878   4771   4782    140   -389    -48       N  
ATOM   5352  CA  GLU B 344      13.670  -1.362  73.923  1.00 41.91           C  
ANISOU 5352  CA  GLU B 344     5337   5313   5274    233   -451    -22       C  
ATOM   5353  C   GLU B 344      14.625  -0.285  74.399  1.00 42.46           C  
ANISOU 5353  C   GLU B 344     5295   5494   5342    196   -478    -21       C  
ATOM   5354  O   GLU B 344      14.869   0.672  73.680  1.00 42.80           O  
ANISOU 5354  O   GLU B 344     5255   5591   5415    159   -441    -46       O  
ATOM   5355  CB  GLU B 344      14.268  -2.102  72.732  1.00 42.45           C  
ANISOU 5355  CB  GLU B 344     5385   5372   5371    355   -436    -31       C  
ATOM   5356  CG  GLU B 344      15.638  -2.726  72.966  1.00 50.89           C  
ANISOU 5356  CG  GLU B 344     6398   6503   6434    484   -488      2       C  
ATOM   5357  CD  GLU B 344      16.813  -1.787  72.635  1.00 57.01           C  
ANISOU 5357  CD  GLU B 344     6997   7429   7236    493   -480      6       C  
ATOM   5358  OE1 GLU B 344      16.697  -0.987  71.672  1.00 58.43           O  
ANISOU 5358  OE1 GLU B 344     7115   7641   7445    451   -418    -24       O  
ATOM   5359  OE2 GLU B 344      17.865  -1.851  73.326  1.00 56.57           O  
ANISOU 5359  OE2 GLU B 344     6859   7464   7170    535   -540     49       O  
ATOM   5360  N   ILE B 345      15.130  -0.421  75.624  1.00 43.32           N  
ANISOU 5360  N   ILE B 345     5413   5634   5412    191   -549     12       N  
ATOM   5361  CA  ILE B 345      16.119   0.496  76.177  1.00 44.18           C  
ANISOU 5361  CA  ILE B 345     5427   5847   5511    143   -601     22       C  
ATOM   5362  C   ILE B 345      17.272  -0.343  76.712  1.00 50.34           C  
ANISOU 5362  C   ILE B 345     6159   6686   6280    239   -683     74       C  
ATOM   5363  O   ILE B 345      17.059  -1.241  77.520  1.00 52.67           O  
ANISOU 5363  O   ILE B 345     6548   6927   6536    280   -724    103       O  
ATOM   5364  CB  ILE B 345      15.547   1.357  77.332  1.00 45.72           C  
ANISOU 5364  CB  ILE B 345     5697   6027   5649     27   -623     10       C  
ATOM   5365  CG1 ILE B 345      14.282   2.088  76.898  1.00 43.21           C  
ANISOU 5365  CG1 ILE B 345     5436   5648   5332    -40   -537    -35       C  
ATOM   5366  CG2 ILE B 345      16.587   2.360  77.838  1.00 44.58           C  
ANISOU 5366  CG2 ILE B 345     5473   5976   5488    -43   -694     17       C  
ATOM   5367  CD1 ILE B 345      13.594   2.818  78.020  1.00 44.41           C  
ANISOU 5367  CD1 ILE B 345     5683   5777   5413   -119   -540    -47       C  
ATOM   5368  N   GLY B 346      18.492  -0.077  76.251  1.00 50.07           N  
ANISOU 5368  N   GLY B 346     5975   6772   6278    279   -706     97       N  
ATOM   5369  CA  GLY B 346      19.652  -0.766  76.784  1.00 49.42           C  
ANISOU 5369  CA  GLY B 346     5821   6773   6184    376   -788    157       C  
ATOM   5370  C   GLY B 346      19.562  -2.273  76.784  1.00 50.00           C  
ANISOU 5370  C   GLY B 346     5984   6769   6245    533   -793    178       C  
ATOM   5371  O   GLY B 346      20.176  -2.942  77.608  1.00 52.72           O  
ANISOU 5371  O   GLY B 346     6333   7140   6559    605   -872    228       O  
ATOM   5372  N   GLY B 347      18.808  -2.812  75.840  1.00 51.01           N  
ANISOU 5372  N   GLY B 347     6195   6795   6393    584   -717    142       N  
ATOM   5373  CA  GLY B 347      18.750  -4.248  75.629  1.00 50.55           C  
ANISOU 5373  CA  GLY B 347     6243   6643   6321    735   -724    157       C  
ATOM   5374  C   GLY B 347      17.632  -4.869  76.433  1.00 52.26           C  
ANISOU 5374  C   GLY B 347     6645   6716   6496    676   -746    162       C  
ATOM   5375  O   GLY B 347      17.367  -6.059  76.302  1.00 54.07           O  
ANISOU 5375  O   GLY B 347     7003   6834   6708    767   -758    174       O  
ATOM   5376  N   LEU B 348      16.999  -4.062  77.282  1.00 47.50           N  
ANISOU 5376  N   LEU B 348     6062   6118   5869    525   -752    156       N  
ATOM   5377  CA  LEU B 348      15.835  -4.474  78.022  1.00 47.04           C  
ANISOU 5377  CA  LEU B 348     6156   5949   5767    451   -753    167       C  
ATOM   5378  C   LEU B 348      14.618  -4.180  77.154  1.00 47.13           C  
ANISOU 5378  C   LEU B 348     6209   5892   5806    374   -667    124       C  
ATOM   5379  O   LEU B 348      14.589  -3.172  76.419  1.00 45.14           O  
ANISOU 5379  O   LEU B 348     5865   5695   5591    329   -613     81       O  
ATOM   5380  CB  LEU B 348      15.739  -3.725  79.368  1.00 45.05           C  
ANISOU 5380  CB  LEU B 348     5909   5747   5462    345   -792    182       C  
ATOM   5381  CG  LEU B 348      16.903  -3.888  80.353  1.00 49.01           C  
ANISOU 5381  CG  LEU B 348     6368   6327   5926    395   -894    229       C  
ATOM   5382  CD1 LEU B 348      16.611  -3.087  81.608  1.00 51.49           C  
ANISOU 5382  CD1 LEU B 348     6723   6670   6172    276   -927    232       C  
ATOM   5383  CD2 LEU B 348      17.148  -5.346  80.727  1.00 46.79           C  
ANISOU 5383  CD2 LEU B 348     6183   5977   5619    515   -951    285       C  
ATOM   5384  N   GLU B 349      13.604  -5.031  77.251  1.00 44.10           N  
ANISOU 5384  N   GLU B 349     5961   5393   5402    349   -660    143       N  
ATOM   5385  CA  GLU B 349      12.440  -4.883  76.368  1.00 46.05           C  
ANISOU 5385  CA  GLU B 349     6241   5581   5675    278   -591    115       C  
ATOM   5386  C   GLU B 349      11.189  -4.713  77.184  1.00 43.40           C  
ANISOU 5386  C   GLU B 349     5969   5218   5301    154   -569    143       C  
ATOM   5387  O   GLU B 349      10.939  -5.494  78.094  1.00 42.84           O  
ANISOU 5387  O   GLU B 349     5995   5100   5183    142   -610    198       O  
ATOM   5388  CB  GLU B 349      12.299  -6.094  75.440  1.00 46.46           C  
ANISOU 5388  CB  GLU B 349     6392   5519   5741    354   -603    115       C  
ATOM   5389  CG  GLU B 349      13.556  -6.402  74.630  1.00 49.57           C  
ANISOU 5389  CG  GLU B 349     6735   5942   6159    513   -614     92       C  
ATOM   5390  CD  GLU B 349      13.430  -7.639  73.744  1.00 52.59           C  
ANISOU 5390  CD  GLU B 349     7254   6192   6535    608   -629     85       C  
ATOM   5391  OE1 GLU B 349      12.750  -8.630  74.100  1.00 56.54           O  
ANISOU 5391  OE1 GLU B 349     7916   6564   7003    578   -673    119       O  
ATOM   5392  OE2 GLU B 349      14.052  -7.629  72.680  1.00 57.17           O  
ANISOU 5392  OE2 GLU B 349     7790   6796   7134    716   -599     47       O  
ATOM   5393  N   PHE B 350      10.410  -3.692  76.853  1.00 40.30           N  
ANISOU 5393  N   PHE B 350     5524   4864   4924     71   -500    113       N  
ATOM   5394  CA  PHE B 350       9.199  -3.409  77.582  1.00 39.67           C  
ANISOU 5394  CA  PHE B 350     5482   4786   4803    -29   -462    143       C  
ATOM   5395  C   PHE B 350       8.072  -3.672  76.602  1.00 41.26           C  
ANISOU 5395  C   PHE B 350     5701   4937   5038    -81   -417    146       C  
ATOM   5396  O   PHE B 350       7.805  -2.864  75.712  1.00 43.24           O  
ANISOU 5396  O   PHE B 350     5882   5218   5328    -95   -366    101       O  
ATOM   5397  CB  PHE B 350       9.234  -1.969  78.135  1.00 40.22           C  
ANISOU 5397  CB  PHE B 350     5487   4946   4848    -67   -425    110       C  
ATOM   5398  CG  PHE B 350      10.364  -1.737  79.127  1.00 42.09           C  
ANISOU 5398  CG  PHE B 350     5717   5230   5044    -35   -490    112       C  
ATOM   5399  CD1 PHE B 350      10.189  -1.997  80.487  1.00 41.90           C  
ANISOU 5399  CD1 PHE B 350     5769   5210   4941    -58   -519    157       C  
ATOM   5400  CD2 PHE B 350      11.620  -1.331  78.689  1.00 40.67           C  
ANISOU 5400  CD2 PHE B 350     5452   5100   4901     14   -528     79       C  
ATOM   5401  CE1 PHE B 350      11.236  -1.805  81.382  1.00 47.58           C  
ANISOU 5401  CE1 PHE B 350     6486   5974   5617    -33   -593    161       C  
ATOM   5402  CE2 PHE B 350      12.667  -1.145  79.579  1.00 42.06           C  
ANISOU 5402  CE2 PHE B 350     5609   5332   5042     31   -602     91       C  
ATOM   5403  CZ  PHE B 350      12.485  -1.380  80.926  1.00 41.95           C  
ANISOU 5403  CZ  PHE B 350     5679   5314   4948      8   -641    129       C  
ATOM   5404  N   SER B 351       7.448  -4.839  76.750  1.00 43.88           N  
ANISOU 5404  N   SER B 351     6132   5187   5352   -115   -448    204       N  
ATOM   5405  CA  SER B 351       6.414  -5.323  75.819  1.00 40.96           C  
ANISOU 5405  CA  SER B 351     5796   4756   5011   -179   -434    219       C  
ATOM   5406  C   SER B 351       5.055  -4.608  75.955  1.00 41.79           C  
ANISOU 5406  C   SER B 351     5842   4928   5108   -286   -363    249       C  
ATOM   5407  O   SER B 351       4.166  -4.730  75.063  1.00 38.21           O  
ANISOU 5407  O   SER B 351     5379   4454   4684   -347   -348    259       O  
ATOM   5408  CB  SER B 351       6.255  -6.836  75.991  1.00 41.76           C  
ANISOU 5408  CB  SER B 351     6040   4737   5088   -195   -508    280       C  
ATOM   5409  OG  SER B 351       5.904  -7.151  77.331  1.00 40.72           O  
ANISOU 5409  OG  SER B 351     5956   4619   4899   -250   -519    355       O  
ATOM   5410  N   ALA B 352       4.879  -3.880  77.069  1.00 40.12           N  
ANISOU 5410  N   ALA B 352     5595   4799   4849   -302   -321    266       N  
ATOM   5411  CA  ALA B 352       3.685  -3.061  77.262  1.00 37.61           C  
ANISOU 5411  CA  ALA B 352     5213   4564   4513   -365   -239    291       C  
ATOM   5412  C   ALA B 352       4.100  -1.676  77.726  1.00 39.18           C  
ANISOU 5412  C   ALA B 352     5358   4842   4687   -315   -190    233       C  
ATOM   5413  O   ALA B 352       4.503  -1.490  78.876  1.00 39.20           O  
ANISOU 5413  O   ALA B 352     5396   4871   4627   -296   -199    241       O  
ATOM   5414  CB  ALA B 352       2.730  -3.701  78.248  1.00 35.23           C  
ANISOU 5414  CB  ALA B 352     4953   4280   4152   -444   -227    393       C  
ATOM   5415  N   ALA B 353       3.983  -0.698  76.825  1.00 37.91           N  
ANISOU 5415  N   ALA B 353     5127   4710   4569   -299   -147    176       N  
ATOM   5416  CA  ALA B 353       4.471   0.621  77.081  1.00 36.43           C  
ANISOU 5416  CA  ALA B 353     4909   4570   4363   -258   -116    114       C  
ATOM   5417  C   ALA B 353       3.688   1.597  76.219  1.00 38.74           C  
ANISOU 5417  C   ALA B 353     5138   4896   4684   -262    -47     88       C  
ATOM   5418  O   ALA B 353       4.264   2.241  75.333  1.00 40.55           O  
ANISOU 5418  O   ALA B 353     5333   5115   4960   -237    -51     28       O  
ATOM   5419  CB  ALA B 353       5.968   0.676  76.771  1.00 33.64           C  
ANISOU 5419  CB  ALA B 353     4550   4191   4042   -210   -180     59       C  
ATOM   5420  N   PRO B 354       2.371   1.727  76.473  1.00 38.19           N  
ANISOU 5420  N   PRO B 354     5048   4878   4587   -291     18    141       N  
ATOM   5421  CA  PRO B 354       1.498   2.563  75.646  1.00 38.08           C  
ANISOU 5421  CA  PRO B 354     4967   4904   4599   -285     81    130       C  
ATOM   5422  C   PRO B 354       1.899   4.033  75.687  1.00 39.52           C  
ANISOU 5422  C   PRO B 354     5155   5101   4762   -226    117     58       C  
ATOM   5423  O   PRO B 354       2.231   4.558  76.750  1.00 41.35           O  
ANISOU 5423  O   PRO B 354     5442   5344   4924   -199    126     40       O  
ATOM   5424  CB  PRO B 354       0.130   2.392  76.312  1.00 41.15           C  
ANISOU 5424  CB  PRO B 354     5328   5370   4937   -313    146    218       C  
ATOM   5425  CG  PRO B 354       0.476   2.125  77.748  1.00 39.46           C  
ANISOU 5425  CG  PRO B 354     5184   5166   4643   -304    141    241       C  
ATOM   5426  CD  PRO B 354       1.647   1.186  77.632  1.00 37.87           C  
ANISOU 5426  CD  PRO B 354     5037   4877   4477   -322     41    221       C  
ATOM   5427  N   PHE B 355       1.877   4.688  74.529  1.00 41.81           N  
ANISOU 5427  N   PHE B 355     5403   5380   5104   -213    130     17       N  
ATOM   5428  CA  PHE B 355       2.234   6.105  74.435  1.00 42.11           C  
ANISOU 5428  CA  PHE B 355     5460   5414   5126   -169    156    -47       C  
ATOM   5429  C   PHE B 355       1.210   6.935  73.684  1.00 41.87           C  
ANISOU 5429  C   PHE B 355     5387   5414   5107   -140    222    -45       C  
ATOM   5430  O   PHE B 355       0.495   6.441  72.795  1.00 43.49           O  
ANISOU 5430  O   PHE B 355     5527   5637   5361   -163    228     -7       O  
ATOM   5431  CB  PHE B 355       3.613   6.292  73.805  1.00 40.32           C  
ANISOU 5431  CB  PHE B 355     5237   5138   4946   -178     95   -106       C  
ATOM   5432  CG  PHE B 355       3.739   5.691  72.430  1.00 40.52           C  
ANISOU 5432  CG  PHE B 355     5207   5141   5047   -193     74   -106       C  
ATOM   5433  CD1 PHE B 355       3.327   6.406  71.295  1.00 39.00           C  
ANISOU 5433  CD1 PHE B 355     4980   4950   4890   -185    107   -126       C  
ATOM   5434  CD2 PHE B 355       4.301   4.428  72.260  1.00 38.10           C  
ANISOU 5434  CD2 PHE B 355     4902   4807   4769   -206     18    -90       C  
ATOM   5435  CE1 PHE B 355       3.467   5.852  70.026  1.00 38.53           C  
ANISOU 5435  CE1 PHE B 355     4886   4868   4886   -195     86   -129       C  
ATOM   5436  CE2 PHE B 355       4.447   3.877  70.993  1.00 37.65           C  
ANISOU 5436  CE2 PHE B 355     4820   4720   4765   -206     -1    -98       C  
ATOM   5437  CZ  PHE B 355       4.031   4.585  69.882  1.00 36.96           C  
ANISOU 5437  CZ  PHE B 355     4698   4639   4707   -204     33   -119       C  
ATOM   5438  N   SER B 356       1.136   8.201  74.051  1.00 38.30           N  
ANISOU 5438  N   SER B 356     4984   4963   4606    -86    264    -83       N  
ATOM   5439  CA  SER B 356       0.206   9.077  73.383  1.00 41.08           C  
ANISOU 5439  CA  SER B 356     5307   5340   4962    -36    326    -80       C  
ATOM   5440  C   SER B 356       0.728  10.501  73.269  1.00 42.08           C  
ANISOU 5440  C   SER B 356     5514   5412   5063      6    330   -150       C  
ATOM   5441  O   SER B 356       1.502  10.979  74.123  1.00 43.37           O  
ANISOU 5441  O   SER B 356     5773   5534   5172      6    303   -193       O  
ATOM   5442  CB  SER B 356      -1.164   9.043  74.073  1.00 39.15           C  
ANISOU 5442  CB  SER B 356     5030   5185   4660     14    407    -13       C  
ATOM   5443  OG  SER B 356      -1.029   9.439  75.412  1.00 39.47           O  
ANISOU 5443  OG  SER B 356     5161   5230   4604     61    434    -27       O  
ATOM   5444  N   GLY B 357       0.305  11.152  72.186  1.00 38.99           N  
ANISOU 5444  N   GLY B 357     5093   5013   4708     32    354   -158       N  
ATOM   5445  CA  GLY B 357       0.524  12.563  71.957  1.00 38.95           C  
ANISOU 5445  CA  GLY B 357     5173   4951   4676     76    366   -210       C  
ATOM   5446  C   GLY B 357      -0.818  13.153  71.572  1.00 44.33           C  
ANISOU 5446  C   GLY B 357     5825   5677   5341    168    442   -178       C  
ATOM   5447  O   GLY B 357      -1.819  12.972  72.269  1.00 42.63           O  
ANISOU 5447  O   GLY B 357     5582   5538   5076    232    505   -130       O  
ATOM   5448  N   TRP B 358      -0.835  13.855  70.448  1.00 44.18           N  
ANISOU 5448  N   TRP B 358     5804   5622   5359    180    439   -194       N  
ATOM   5449  CA  TRP B 358      -2.069  14.344  69.875  1.00 42.83           C  
ANISOU 5449  CA  TRP B 358     5586   5501   5185    268    498   -155       C  
ATOM   5450  C   TRP B 358      -2.034  14.010  68.414  1.00 40.48           C  
ANISOU 5450  C   TRP B 358     5206   5204   4972    211    462   -141       C  
ATOM   5451  O   TRP B 358      -0.977  13.733  67.864  1.00 38.71           O  
ANISOU 5451  O   TRP B 358     4991   4926   4792    128    404   -174       O  
ATOM   5452  CB  TRP B 358      -2.264  15.844  70.148  1.00 40.96           C  
ANISOU 5452  CB  TRP B 358     5482   5204   4876    378    539   -195       C  
ATOM   5453  CG  TRP B 358      -1.066  16.730  69.803  1.00 42.72           C  
ANISOU 5453  CG  TRP B 358     5832   5298   5101    324    480   -265       C  
ATOM   5454  CD1 TRP B 358      -0.730  17.234  68.554  1.00 42.59           C  
ANISOU 5454  CD1 TRP B 358     5817   5231   5137    290    450   -276       C  
ATOM   5455  CD2 TRP B 358      -0.029  17.260  70.710  1.00 41.97           C  
ANISOU 5455  CD2 TRP B 358     5884   5114   4950    285    436   -325       C  
ATOM   5456  NE1 TRP B 358       0.397  18.001  68.610  1.00 42.22           N  
ANISOU 5456  NE1 TRP B 358     5891   5078   5073    227    398   -329       N  
ATOM   5457  CE2 TRP B 358       0.869  18.067  69.877  1.00 43.83           C  
ANISOU 5457  CE2 TRP B 358     6188   5253   5214    216    380   -361       C  
ATOM   5458  CE3 TRP B 358       0.230  17.159  72.081  1.00 44.53           C  
ANISOU 5458  CE3 TRP B 358     6290   5431   5197    292    432   -347       C  
ATOM   5459  CZ2 TRP B 358       1.987  18.730  70.408  1.00 42.65           C  
ANISOU 5459  CZ2 TRP B 358     6173   5008   5025    142    315   -411       C  
ATOM   5460  CZ3 TRP B 358       1.340  17.841  72.608  1.00 44.42           C  
ANISOU 5460  CZ3 TRP B 358     6424   5314   5139    228    363   -406       C  
ATOM   5461  CH2 TRP B 358       2.207  18.598  71.782  1.00 45.21           C  
ANISOU 5461  CH2 TRP B 358     6578   5326   5275    147    301   -435       C  
ATOM   5462  N   TYR B 359      -3.200  13.998  67.791  1.00 38.09           N  
ANISOU 5462  N   TYR B 359     4816   4974   4685    260    495    -84       N  
ATOM   5463  CA  TYR B 359      -3.351  13.675  66.400  1.00 38.15           C  
ANISOU 5463  CA  TYR B 359     4749   4989   4757    213    459    -64       C  
ATOM   5464  C   TYR B 359      -2.785  14.751  65.477  1.00 39.83           C  
ANISOU 5464  C   TYR B 359     5039   5116   4977    228    444   -111       C  
ATOM   5465  O   TYR B 359      -2.761  15.943  65.806  1.00 39.47           O  
ANISOU 5465  O   TYR B 359     5095   5018   4884    305    474   -141       O  
ATOM   5466  CB  TYR B 359      -4.834  13.543  66.088  1.00 38.41           C  
ANISOU 5466  CB  TYR B 359     4669   5133   4792    266    494     18       C  
ATOM   5467  CG  TYR B 359      -5.346  12.143  66.178  1.00 40.20           C  
ANISOU 5467  CG  TYR B 359     4783   5442   5049    180    467     84       C  
ATOM   5468  CD1 TYR B 359      -4.978  11.208  65.230  1.00 41.10           C  
ANISOU 5468  CD1 TYR B 359     4869   5527   5219     73    393     83       C  
ATOM   5469  CD2 TYR B 359      -6.203  11.749  67.206  1.00 40.61           C  
ANISOU 5469  CD2 TYR B 359     4769   5596   5064    205    516    151       C  
ATOM   5470  CE1 TYR B 359      -5.442   9.925  65.283  1.00 40.12           C  
ANISOU 5470  CE1 TYR B 359     4671   5455   5117    -16    355    143       C  
ATOM   5471  CE2 TYR B 359      -6.682  10.457  67.260  1.00 43.10           C  
ANISOU 5471  CE2 TYR B 359     4990   5980   5407    104    481    223       C  
ATOM   5472  CZ  TYR B 359      -6.286   9.555  66.287  1.00 42.47           C  
ANISOU 5472  CZ  TYR B 359     4902   5849   5386    -11    394    215       C  
ATOM   5473  OH  TYR B 359      -6.724   8.260  66.294  1.00 48.65           O  
ANISOU 5473  OH  TYR B 359     5622   6672   6191   -122    344    283       O  
ATOM   5474  N   MET B 360      -2.308  14.293  64.329  1.00 43.53           N  
ANISOU 5474  N   MET B 360     5474   5565   5501    154    396   -117       N  
ATOM   5475  CA  MET B 360      -2.191  15.135  63.159  1.00 44.15           C  
ANISOU 5475  CA  MET B 360     5586   5599   5591    169    388   -129       C  
ATOM   5476  C   MET B 360      -3.456  14.859  62.340  1.00 39.93           C  
ANISOU 5476  C   MET B 360     4954   5143   5073    201    390    -66       C  
ATOM   5477  O   MET B 360      -3.803  13.712  62.099  1.00 39.40           O  
ANISOU 5477  O   MET B 360     4801   5132   5037    141    359    -31       O  
ATOM   5478  CB  MET B 360      -0.939  14.813  62.354  1.00 44.53           C  
ANISOU 5478  CB  MET B 360     5651   5595   5674     78    341   -165       C  
ATOM   5479  CG  MET B 360      -0.967  15.475  60.972  1.00 49.03           C  
ANISOU 5479  CG  MET B 360     6238   6138   6255     85    334   -161       C  
ATOM   5480  SD  MET B 360       0.604  15.318  60.160  1.00 57.76           S  
ANISOU 5480  SD  MET B 360     7368   7196   7384     -6    302   -198       S  
ATOM   5481  CE  MET B 360       0.527  13.676  59.429  1.00 47.23           C  
ANISOU 5481  CE  MET B 360     5948   5913   6082    -48    268   -184       C  
ATOM   5482  N   SER B 361      -4.122  15.907  61.892  1.00 38.07           N  
ANISOU 5482  N   SER B 361     4741   4908   4817    290    417    -48       N  
ATOM   5483  CA  SER B 361      -5.475  15.757  61.339  1.00 38.06           C  
ANISOU 5483  CA  SER B 361     4631   5006   4822    339    421     26       C  
ATOM   5484  C   SER B 361      -5.601  14.803  60.141  1.00 39.43           C  
ANISOU 5484  C   SER B 361     4729   5211   5042    245    355     53       C  
ATOM   5485  O   SER B 361      -6.693  14.219  59.923  1.00 38.55           O  
ANISOU 5485  O   SER B 361     4504   5201   4943    237    338    125       O  
ATOM   5486  CB  SER B 361      -6.018  17.131  60.957  1.00 40.29           C  
ANISOU 5486  CB  SER B 361     4968   5268   5071    465    455     37       C  
ATOM   5487  OG  SER B 361      -5.089  17.813  60.127  1.00 38.86           O  
ANISOU 5487  OG  SER B 361     4895   4975   4894    433    428    -12       O  
ATOM   5488  N   THR B 362      -4.526  14.634  59.353  1.00 33.39           N  
ANISOU 5488  N   THR B 362     4025   4367   4296    172    317      2       N  
ATOM   5489  CA  THR B 362      -4.634  13.699  58.236  1.00 35.95           C  
ANISOU 5489  CA  THR B 362     4305   4710   4646     94    255     20       C  
ATOM   5490  C   THR B 362      -4.753  12.251  58.717  1.00 36.37           C  
ANISOU 5490  C   THR B 362     4301   4799   4717     12    219     38       C  
ATOM   5491  O   THR B 362      -5.250  11.407  57.991  1.00 39.43           O  
ANISOU 5491  O   THR B 362     4647   5217   5117    -49    160     71       O  
ATOM   5492  CB  THR B 362      -3.495  13.804  57.209  1.00 36.68           C  
ANISOU 5492  CB  THR B 362     4473   4722   4740     52    232    -33       C  
ATOM   5493  OG1 THR B 362      -2.235  13.571  57.855  1.00 37.53           O  
ANISOU 5493  OG1 THR B 362     4628   4778   4853     15    245    -87       O  
ATOM   5494  CG2 THR B 362      -3.514  15.167  56.513  1.00 36.97           C  
ANISOU 5494  CG2 THR B 362     4568   4723   4756    114    254    -33       C  
ATOM   5495  N   GLU B 363      -4.330  11.964  59.941  1.00 34.65           N  
ANISOU 5495  N   GLU B 363     4095   4574   4497      6    246     20       N  
ATOM   5496  CA  GLU B 363      -4.439  10.598  60.437  1.00 35.76           C  
ANISOU 5496  CA  GLU B 363     4198   4739   4652    -72    210     43       C  
ATOM   5497  C   GLU B 363      -5.923  10.201  60.508  1.00 37.48           C  
ANISOU 5497  C   GLU B 363     4305   5065   4870    -87    197    136       C  
ATOM   5498  O   GLU B 363      -6.281   9.085  60.155  1.00 40.81           O  
ANISOU 5498  O   GLU B 363     4696   5503   5308   -181    131    173       O  
ATOM   5499  CB  GLU B 363      -3.795  10.470  61.808  1.00 36.59           C  
ANISOU 5499  CB  GLU B 363     4335   4824   4744    -65    244     16       C  
ATOM   5500  CG  GLU B 363      -2.286  10.647  61.845  1.00 37.80           C  
ANISOU 5500  CG  GLU B 363     4572   4890   4899    -73    241    -60       C  
ATOM   5501  CD  GLU B 363      -1.761  10.487  63.256  1.00 41.43           C  
ANISOU 5501  CD  GLU B 363     5059   5342   5341    -71    260    -77       C  
ATOM   5502  OE1 GLU B 363      -1.695   9.316  63.699  1.00 44.31           O  
ANISOU 5502  OE1 GLU B 363     5409   5714   5714   -122    230    -59       O  
ATOM   5503  OE2 GLU B 363      -1.445  11.509  63.931  1.00 40.75           O  
ANISOU 5503  OE2 GLU B 363     5022   5236   5227    -22    299   -105       O  
ATOM   5504  N   ILE B 364      -6.773  11.144  60.909  1.00 36.65           N  
ANISOU 5504  N   ILE B 364     4145   5034   4745      6    256    179       N  
ATOM   5505  CA  ILE B 364      -8.224  10.938  61.005  1.00 39.06           C  
ANISOU 5505  CA  ILE B 364     4316   5475   5049     10    257    284       C  
ATOM   5506  C   ILE B 364      -8.923  11.229  59.651  1.00 40.80           C  
ANISOU 5506  C   ILE B 364     4487   5733   5281     12    207    323       C  
ATOM   5507  O   ILE B 364      -9.626  10.382  59.073  1.00 43.94           O  
ANISOU 5507  O   ILE B 364     4808   6190   5695    -84    133    387       O  
ATOM   5508  CB  ILE B 364      -8.847  11.874  62.094  1.00 37.91           C  
ANISOU 5508  CB  ILE B 364     4131   5408   4863    145    357    316       C  
ATOM   5509  CG1 ILE B 364      -8.093  11.787  63.431  1.00 38.82           C  
ANISOU 5509  CG1 ILE B 364     4322   5476   4951    157    405    268       C  
ATOM   5510  CG2 ILE B 364     -10.341  11.630  62.258  1.00 38.58           C  
ANISOU 5510  CG2 ILE B 364     4049   5666   4945    157    370    441       C  
ATOM   5511  CD1 ILE B 364      -8.646  12.685  64.530  1.00 35.46           C  
ANISOU 5511  CD1 ILE B 364     3891   5115   4468    299    505    289       C  
ATOM   5512  N   GLY B 365      -8.736  12.445  59.158  1.00 40.76           N  
ANISOU 5512  N   GLY B 365     4537   5689   5261    116    241    287       N  
ATOM   5513  CA  GLY B 365      -9.436  12.896  57.962  1.00 42.25           C  
ANISOU 5513  CA  GLY B 365     4684   5918   5452    143    202    329       C  
ATOM   5514  C   GLY B 365      -9.089  12.133  56.697  1.00 41.18           C  
ANISOU 5514  C   GLY B 365     4586   5729   5332     28    105    309       C  
ATOM   5515  O   GLY B 365      -9.920  11.955  55.837  1.00 46.29           O  
ANISOU 5515  O   GLY B 365     5166   6441   5980     -3     42    370       O  
ATOM   5516  N   THR B 366      -7.860  11.684  56.573  1.00 38.41           N  
ANISOU 5516  N   THR B 366     4344   5264   4984    -30     92    226       N  
ATOM   5517  CA  THR B 366      -7.468  11.006  55.364  1.00 38.75           C  
ANISOU 5517  CA  THR B 366     4444   5251   5026   -113     13    198       C  
ATOM   5518  C   THR B 366      -7.404   9.472  55.505  1.00 38.00           C  
ANISOU 5518  C   THR B 366     4356   5142   4942   -236    -57    203       C  
ATOM   5519  O   THR B 366      -8.137   8.770  54.852  1.00 42.36           O  
ANISOU 5519  O   THR B 366     4878   5728   5491   -317   -143    252       O  
ATOM   5520  CB  THR B 366      -6.172  11.616  54.850  1.00 37.63           C  
ANISOU 5520  CB  THR B 366     4422   5003   4872    -77     45    113       C  
ATOM   5521  OG1 THR B 366      -6.387  13.029  54.742  1.00 38.88           O  
ANISOU 5521  OG1 THR B 366     4588   5168   5017     25     96    122       O  
ATOM   5522  CG2 THR B 366      -5.834  11.049  53.484  1.00 39.38           C  
ANISOU 5522  CG2 THR B 366     4709   5179   5075   -135    -24     88       C  
ATOM   5523  N   ARG B 367      -6.563   8.962  56.389  1.00 36.10           N  
ANISOU 5523  N   ARG B 367     4160   4846   4708   -253    -29    158       N  
ATOM   5524  CA  ARG B 367      -6.425   7.512  56.570  1.00 36.52           C  
ANISOU 5524  CA  ARG B 367     4246   4864   4765   -358    -95    160       C  
ATOM   5525  C   ARG B 367      -7.660   6.828  57.196  1.00 39.98           C  
ANISOU 5525  C   ARG B 367     4578   5398   5215   -439   -134    261       C  
ATOM   5526  O   ARG B 367      -8.252   5.965  56.551  1.00 44.87           O  
ANISOU 5526  O   ARG B 367     5197   6021   5829   -544   -232    303       O  
ATOM   5527  CB  ARG B 367      -5.133   7.210  57.341  1.00 33.73           C  
ANISOU 5527  CB  ARG B 367     3969   4431   4414   -339    -55     89       C  
ATOM   5528  CG  ARG B 367      -3.908   7.878  56.684  1.00 33.92           C  
ANISOU 5528  CG  ARG B 367     4074   4385   4428   -274    -19      7       C  
ATOM   5529  CD  ARG B 367      -3.664   7.342  55.273  1.00 33.37           C  
ANISOU 5529  CD  ARG B 367     4080   4265   4335   -304    -81    -21       C  
ATOM   5530  NE  ARG B 367      -3.697   5.866  55.212  1.00 37.66           N  
ANISOU 5530  NE  ARG B 367     4681   4761   4869   -382   -160    -20       N  
ATOM   5531  CZ  ARG B 367      -2.685   5.077  55.588  1.00 37.93           C  
ANISOU 5531  CZ  ARG B 367     4789   4725   4897   -375   -158    -69       C  
ATOM   5532  NH1 ARG B 367      -1.566   5.613  56.021  1.00 37.48           N  
ANISOU 5532  NH1 ARG B 367     4737   4656   4848   -305    -87   -116       N  
ATOM   5533  NH2 ARG B 367      -2.783   3.755  55.536  1.00 36.06           N  
ANISOU 5533  NH2 ARG B 367     4627   4430   4645   -440   -236    -66       N  
ATOM   5534  N   ASN B 368      -8.074   7.228  58.399  1.00 34.82           N  
ANISOU 5534  N   ASN B 368     3839   4823   4567   -394    -61    305       N  
ATOM   5535  CA  ASN B 368      -9.078   6.461  59.115  1.00 36.92           C  
ANISOU 5535  CA  ASN B 368     4004   5184   4839   -480    -87    406       C  
ATOM   5536  C   ASN B 368     -10.442   6.558  58.473  1.00 38.89           C  
ANISOU 5536  C   ASN B 368     4125   5559   5092   -521   -137    510       C  
ATOM   5537  O   ASN B 368     -11.187   5.577  58.433  1.00 44.09           O  
ANISOU 5537  O   ASN B 368     4729   6266   5756   -657   -220    593       O  
ATOM   5538  CB  ASN B 368      -9.139   6.923  60.571  1.00 37.54           C  
ANISOU 5538  CB  ASN B 368     4029   5326   4909   -404     17    426       C  
ATOM   5539  CG  ASN B 368      -7.807   6.743  61.291  1.00 35.98           C  
ANISOU 5539  CG  ASN B 368     3951   5014   4705   -380     50    334       C  
ATOM   5540  OD1 ASN B 368      -6.895   6.078  60.774  1.00 35.79           O  
ANISOU 5540  OD1 ASN B 368     4033   4878   4688   -427     -6    269       O  
ATOM   5541  ND2 ASN B 368      -7.681   7.336  62.479  1.00 33.88           N  
ANISOU 5541  ND2 ASN B 368     3671   4781   4420   -298    139    330       N  
ATOM   5542  N   LEU B 369     -10.772   7.735  57.954  1.00 36.95           N  
ANISOU 5542  N   LEU B 369     3833   5364   4842   -409    -96    513       N  
ATOM   5543  CA  LEU B 369     -12.075   7.931  57.356  1.00 38.54           C  
ANISOU 5543  CA  LEU B 369     3897   5702   5046   -427   -142    619       C  
ATOM   5544  C   LEU B 369     -12.126   7.640  55.872  1.00 39.37           C  
ANISOU 5544  C   LEU B 369     4057   5756   5145   -503   -258    606       C  
ATOM   5545  O   LEU B 369     -13.190   7.266  55.344  1.00 40.37           O  
ANISOU 5545  O   LEU B 369     4081   5984   5274   -592   -347    705       O  
ATOM   5546  CB  LEU B 369     -12.610   9.342  57.651  1.00 40.42           C  
ANISOU 5546  CB  LEU B 369     4044   6040   5273   -250    -39    651       C  
ATOM   5547  CG  LEU B 369     -12.862   9.708  59.128  1.00 40.88           C  
ANISOU 5547  CG  LEU B 369     4032   6182   5318   -157     78    684       C  
ATOM   5548  CD1 LEU B 369     -13.300  11.159  59.238  1.00 39.24           C  
ANISOU 5548  CD1 LEU B 369     3783   6041   5086     42    173    697       C  
ATOM   5549  CD2 LEU B 369     -13.883   8.782  59.776  1.00 39.85           C  
ANISOU 5549  CD2 LEU B 369     3745   6202   5194   -265     56    815       C  
ATOM   5550  N   CYS B 370     -10.995   7.815  55.194  1.00 41.12           N  
ANISOU 5550  N   CYS B 370     4436   5833   5353   -469   -259    492       N  
ATOM   5551  CA  CYS B 370     -10.985   7.762  53.726  1.00 43.18           C  
ANISOU 5551  CA  CYS B 370     4767   6047   5593   -506   -349    470       C  
ATOM   5552  C   CYS B 370     -10.308   6.540  53.085  1.00 43.47           C  
ANISOU 5552  C   CYS B 370     4955   5953   5608   -623   -445    408       C  
ATOM   5553  O   CYS B 370     -10.586   6.256  51.920  1.00 42.72           O  
ANISOU 5553  O   CYS B 370     4911   5838   5484   -683   -543    413       O  
ATOM   5554  CB  CYS B 370     -10.381   9.036  53.144  1.00 45.70           C  
ANISOU 5554  CB  CYS B 370     5147   6319   5897   -368   -281    405       C  
ATOM   5555  SG  CYS B 370     -11.410  10.486  53.404  1.00 49.64           S  
ANISOU 5555  SG  CYS B 370     5503   6957   6402   -221   -209    486       S  
ATOM   5556  N   ASP B 371      -9.425   5.841  53.815  1.00 39.74           N  
ANISOU 5556  N   ASP B 371     4567   5391   5142   -643   -418    350       N  
ATOM   5557  CA  ASP B 371      -8.880   4.579  53.315  1.00 39.44           C  
ANISOU 5557  CA  ASP B 371     4679   5230   5076   -740   -510    300       C  
ATOM   5558  C   ASP B 371     -10.010   3.675  52.881  1.00 42.37           C  
ANISOU 5558  C   ASP B 371     5024   5639   5436   -899   -650    388       C  
ATOM   5559  O   ASP B 371     -11.037   3.583  53.548  1.00 43.18           O  
ANISOU 5559  O   ASP B 371     4978   5862   5566   -966   -664    497       O  
ATOM   5560  CB  ASP B 371      -7.973   3.856  54.329  1.00 36.92           C  
ANISOU 5560  CB  ASP B 371     4433   4829   4768   -741   -472    252       C  
ATOM   5561  CG  ASP B 371      -6.558   4.454  54.389  1.00 37.27           C  
ANISOU 5561  CG  ASP B 371     4554   4799   4808   -612   -373    146       C  
ATOM   5562  OD1 ASP B 371      -6.279   5.403  53.633  1.00 37.97           O  
ANISOU 5562  OD1 ASP B 371     4650   4893   4885   -533   -334    113       O  
ATOM   5563  OD2 ASP B 371      -5.705   3.980  55.173  1.00 37.24           O  
ANISOU 5563  OD2 ASP B 371     4603   4736   4810   -594   -339    104       O  
ATOM   5564  N   PRO B 372      -9.834   3.017  51.733  1.00 44.20           N  
ANISOU 5564  N   PRO B 372     5400   5773   5620   -964   -758    347       N  
ATOM   5565  CA  PRO B 372     -10.848   2.106  51.214  1.00 43.86           C  
ANISOU 5565  CA  PRO B 372     5366   5745   5555  -1138   -917    424       C  
ATOM   5566  C   PRO B 372     -11.133   0.940  52.164  1.00 45.65           C  
ANISOU 5566  C   PRO B 372     5597   5949   5798  -1277   -972    480       C  
ATOM   5567  O   PRO B 372     -12.281   0.414  52.190  1.00 50.75           O  
ANISOU 5567  O   PRO B 372     6157   6675   6449  -1439  -1082    597       O  
ATOM   5568  CB  PRO B 372     -10.224   1.588  49.914  1.00 44.36           C  
ANISOU 5568  CB  PRO B 372     5649   5661   5546  -1148  -1002    331       C  
ATOM   5569  CG  PRO B 372      -8.742   1.769  50.111  1.00 45.42           C  
ANISOU 5569  CG  PRO B 372     5895   5691   5672  -1000   -882    210       C  
ATOM   5570  CD  PRO B 372      -8.596   3.014  50.929  1.00 41.73           C  
ANISOU 5570  CD  PRO B 372     5265   5327   5262   -878   -734    224       C  
ATOM   5571  N   HIS B 373     -10.124   0.535  52.931  1.00 40.75           N  
ANISOU 5571  N   HIS B 373     5071   5229   5184  -1222   -904    410       N  
ATOM   5572  CA  HIS B 373     -10.273  -0.588  53.877  1.00 43.29           C  
ANISOU 5572  CA  HIS B 373     5423   5511   5515  -1343   -951    458       C  
ATOM   5573  C   HIS B 373     -10.470  -0.078  55.281  1.00 44.10           C  
ANISOU 5573  C   HIS B 373     5352   5735   5669  -1296   -831    519       C  
ATOM   5574  O   HIS B 373     -10.289  -0.817  56.257  1.00 48.41           O  
ANISOU 5574  O   HIS B 373     5928   6244   6223  -1348   -827    540       O  
ATOM   5575  CB  HIS B 373      -9.060  -1.504  53.825  1.00 40.28           C  
ANISOU 5575  CB  HIS B 373     5274   4934   5096  -1312   -969    349       C  
ATOM   5576  CG  HIS B 373      -7.765  -0.779  54.051  1.00 38.91           C  
ANISOU 5576  CG  HIS B 373     5125   4729   4931  -1116   -826    242       C  
ATOM   5577  ND1 HIS B 373      -7.329   0.185  53.222  1.00 38.69           N  
ANISOU 5577  ND1 HIS B 373     5092   4718   4891   -998   -767    180       N  
ATOM   5578  CD2 HIS B 373      -6.799  -0.913  55.048  1.00 38.11           C  
ANISOU 5578  CD2 HIS B 373     5052   4582   4847  -1033   -740    195       C  
ATOM   5579  CE1 HIS B 373      -6.142   0.656  53.668  1.00 36.66           C  
ANISOU 5579  CE1 HIS B 373     4851   4432   4645   -857   -649    102       C  
ATOM   5580  NE2 HIS B 373      -5.829  -0.012  54.792  1.00 38.12           N  
ANISOU 5580  NE2 HIS B 373     5052   4583   4848   -877   -635    111       N  
ATOM   5581  N   ARG B 374     -10.819   1.199  55.409  1.00 42.43           N  
ANISOU 5581  N   ARG B 374     4976   5663   5484  -1185   -731    544       N  
ATOM   5582  CA  ARG B 374     -11.219   1.734  56.709  1.00 44.87           C  
ANISOU 5582  CA  ARG B 374     5118   6105   5826  -1137   -620    614       C  
ATOM   5583  C   ARG B 374     -12.698   2.125  56.634  1.00 46.53           C  
ANISOU 5583  C   ARG B 374     5119   6509   6051  -1194   -645    755       C  
ATOM   5584  O   ARG B 374     -13.521   1.333  56.152  1.00 48.92           O  
ANISOU 5584  O   ARG B 374     5401   6840   6347  -1365   -778    841       O  
ATOM   5585  CB  ARG B 374     -10.274   2.872  57.170  1.00 41.25           C  
ANISOU 5585  CB  ARG B 374     4664   5634   5377   -941   -471    521       C  
ATOM   5586  CG  ARG B 374      -8.821   2.424  57.325  1.00 36.55           C  
ANISOU 5586  CG  ARG B 374     4244   4875   4770   -893   -451    402       C  
ATOM   5587  CD  ARG B 374      -8.562   1.471  58.487  1.00 37.20           C  
ANISOU 5587  CD  ARG B 374     4363   4917   4854   -954   -452    422       C  
ATOM   5588  NE  ARG B 374      -8.884   2.046  59.804  1.00 39.23           N  
ANISOU 5588  NE  ARG B 374     4490   5288   5126   -902   -348    476       N  
ATOM   5589  CZ  ARG B 374      -8.114   2.892  60.490  1.00 38.92           C  
ANISOU 5589  CZ  ARG B 374     4452   5247   5089   -766   -236    413       C  
ATOM   5590  NH1 ARG B 374      -6.948   3.307  60.008  1.00 36.29           N  
ANISOU 5590  NH1 ARG B 374     4219   4816   4752   -675   -211    302       N  
ATOM   5591  NH2 ARG B 374      -8.524   3.351  61.663  1.00 42.70           N  
ANISOU 5591  NH2 ARG B 374     4830   5828   5566   -724   -151    466       N  
ATOM   5592  N   TYR B 375     -13.053   3.322  57.087  1.00 48.12           N  
ANISOU 5592  N   TYR B 375     5171   6846   6268  -1053   -526    786       N  
ATOM   5593  CA  TYR B 375     -14.467   3.693  57.079  1.00 50.04           C  
ANISOU 5593  CA  TYR B 375     5195   7295   6521  -1082   -537    931       C  
ATOM   5594  C   TYR B 375     -14.908   4.091  55.668  1.00 50.52           C  
ANISOU 5594  C   TYR B 375     5246   7377   6574  -1088   -626    938       C  
ATOM   5595  O   TYR B 375     -16.098   4.231  55.394  1.00 50.91           O  
ANISOU 5595  O   TYR B 375     5122   7591   6629  -1139   -676   1065       O  
ATOM   5596  CB  TYR B 375     -14.722   4.827  58.054  1.00 51.10           C  
ANISOU 5596  CB  TYR B 375     5191   7563   6662   -905   -376    961       C  
ATOM   5597  CG  TYR B 375     -14.856   4.402  59.508  1.00 53.37           C  
ANISOU 5597  CG  TYR B 375     5415   7914   6948   -928   -302   1020       C  
ATOM   5598  CD1 TYR B 375     -13.730   4.187  60.295  1.00 53.05           C  
ANISOU 5598  CD1 TYR B 375     5518   7739   6901   -887   -242    919       C  
ATOM   5599  CD2 TYR B 375     -16.111   4.278  60.109  1.00 55.94           C  
ANISOU 5599  CD2 TYR B 375     5528   8451   7276   -981   -285   1183       C  
ATOM   5600  CE1 TYR B 375     -13.844   3.830  61.634  1.00 53.43           C  
ANISOU 5600  CE1 TYR B 375     5519   7845   6938   -903   -174    973       C  
ATOM   5601  CE2 TYR B 375     -16.236   3.917  61.443  1.00 56.41           C  
ANISOU 5601  CE2 TYR B 375     5532   8577   7324   -997   -207   1243       C  
ATOM   5602  CZ  TYR B 375     -15.092   3.696  62.201  1.00 54.44           C  
ANISOU 5602  CZ  TYR B 375     5448   8175   7062   -957   -154   1133       C  
ATOM   5603  OH  TYR B 375     -15.187   3.327  63.520  1.00 52.11           O  
ANISOU 5603  OH  TYR B 375     5113   7940   6747   -973    -81   1191       O  
ATOM   5604  N   ASN B 376     -13.927   4.300  54.792  1.00 47.98           N  
ANISOU 5604  N   ASN B 376     5102   6897   6232  -1027   -639    807       N  
ATOM   5605  CA  ASN B 376     -14.157   4.435  53.366  1.00 48.27           C  
ANISOU 5605  CA  ASN B 376     5185   6911   6245  -1055   -742    796       C  
ATOM   5606  C   ASN B 376     -15.345   5.374  52.970  1.00 49.30           C  
ANISOU 5606  C   ASN B 376     5117   7232   6383  -1000   -744    906       C  
ATOM   5607  O   ASN B 376     -16.236   4.975  52.214  1.00 47.37           O  
ANISOU 5607  O   ASN B 376     4810   7060   6128  -1126   -879    994       O  
ATOM   5608  CB  ASN B 376     -14.282   3.016  52.802  1.00 47.78           C  
ANISOU 5608  CB  ASN B 376     5240   6757   6158  -1266   -912    808       C  
ATOM   5609  CG  ASN B 376     -14.473   2.978  51.308  1.00 47.75           C  
ANISOU 5609  CG  ASN B 376     5322   6710   6111  -1315  -1038    789       C  
ATOM   5610  OD1 ASN B 376     -15.321   2.233  50.812  1.00 46.59           O  
ANISOU 5610  OD1 ASN B 376     5156   6598   5947  -1492  -1193    874       O  
ATOM   5611  ND2 ASN B 376     -13.699   3.775  50.583  1.00 43.19           N  
ANISOU 5611  ND2 ASN B 376     4843   6058   5510  -1169   -980    685       N  
ATOM   5612  N   ILE B 377     -15.309   6.629  53.448  1.00 49.06           N  
ANISOU 5612  N   ILE B 377     5005   7271   6365   -805   -603    899       N  
ATOM   5613  CA  ILE B 377     -16.466   7.568  53.368  1.00 49.70           C  
ANISOU 5613  CA  ILE B 377     4882   7549   6452   -710   -576   1014       C  
ATOM   5614  C   ILE B 377     -16.455   8.523  52.175  1.00 48.81           C  
ANISOU 5614  C   ILE B 377     4810   7417   6317   -605   -597    982       C  
ATOM   5615  O   ILE B 377     -17.373   9.324  52.014  1.00 48.92           O  
ANISOU 5615  O   ILE B 377     4671   7584   6333   -509   -582   1075       O  
ATOM   5616  CB  ILE B 377     -16.644   8.425  54.653  1.00 49.87           C  
ANISOU 5616  CB  ILE B 377     4787   7674   6486   -539   -408   1044       C  
ATOM   5617  CG1 ILE B 377     -15.484   9.421  54.826  1.00 50.36           C  
ANISOU 5617  CG1 ILE B 377     5006   7592   6535   -362   -289    903       C  
ATOM   5618  CG2 ILE B 377     -16.755   7.551  55.885  1.00 47.70           C  
ANISOU 5618  CG2 ILE B 377     4456   7443   6225   -635   -378   1093       C  
ATOM   5619  CD1 ILE B 377     -15.751  10.525  55.828  1.00 52.03           C  
ANISOU 5619  CD1 ILE B 377     5135   7894   6740   -164   -140    926       C  
ATOM   5620  N   LEU B 378     -15.437   8.425  51.331  1.00 48.98           N  
ANISOU 5620  N   LEU B 378     5037   7260   6313   -616   -631    859       N  
ATOM   5621  CA  LEU B 378     -15.296   9.347  50.204  1.00 49.75           C  
ANISOU 5621  CA  LEU B 378     5197   7323   6381   -516   -642    823       C  
ATOM   5622  C   LEU B 378     -16.563   9.434  49.388  1.00 54.69           C  
ANISOU 5622  C   LEU B 378     5685   8097   6996   -561   -757    946       C  
ATOM   5623  O   LEU B 378     -17.101  10.524  49.207  1.00 58.48           O  
ANISOU 5623  O   LEU B 378     6070   8675   7475   -416   -713    998       O  
ATOM   5624  CB  LEU B 378     -14.160   8.923  49.303  1.00 48.86           C  
ANISOU 5624  CB  LEU B 378     5311   7022   6230   -565   -688    698       C  
ATOM   5625  CG  LEU B 378     -12.841   9.704  49.252  1.00 51.72           C  
ANISOU 5625  CG  LEU B 378     5823   7249   6580   -433   -573    573       C  
ATOM   5626  CD1 LEU B 378     -12.687  10.770  50.322  1.00 52.77           C  
ANISOU 5626  CD1 LEU B 378     5892   7415   6742   -279   -426    570       C  
ATOM   5627  CD2 LEU B 378     -11.629   8.786  49.195  1.00 46.43           C  
ANISOU 5627  CD2 LEU B 378     5326   6421   5893   -503   -581    463       C  
ATOM   5628  N   GLU B 379     -17.043   8.305  48.874  1.00 56.84           N  
ANISOU 5628  N   GLU B 379     5956   8385   7257   -761   -913    996       N  
ATOM   5629  CA  GLU B 379     -18.241   8.343  48.035  1.00 60.83           C  
ANISOU 5629  CA  GLU B 379     6327   9036   7748   -827  -1047   1120       C  
ATOM   5630  C   GLU B 379     -19.416   9.029  48.748  1.00 57.69           C  
ANISOU 5630  C   GLU B 379     5653   8879   7388   -730   -985   1270       C  
ATOM   5631  O   GLU B 379     -20.023   9.948  48.209  1.00 60.09           O  
ANISOU 5631  O   GLU B 379     5862   9287   7681   -610   -988   1331       O  
ATOM   5632  CB  GLU B 379     -18.653   6.947  47.570  1.00 68.60           C  
ANISOU 5632  CB  GLU B 379     7346  10005   8714  -1084  -1235   1165       C  
ATOM   5633  CG  GLU B 379     -18.032   6.494  46.261  1.00 77.16           C  
ANISOU 5633  CG  GLU B 379     8671  10915   9730  -1161  -1354   1064       C  
ATOM   5634  CD  GLU B 379     -18.988   5.632  45.436  1.00 85.87           C  
ANISOU 5634  CD  GLU B 379     9749  12077  10799  -1380  -1576   1160       C  
ATOM   5635  OE1 GLU B 379     -19.695   4.773  46.022  1.00 84.63           O  
ANISOU 5635  OE1 GLU B 379     9479  12005  10670  -1554  -1655   1263       O  
ATOM   5636  OE2 GLU B 379     -19.050   5.824  44.196  1.00 92.54           O  
ANISOU 5636  OE2 GLU B 379    10691  12886  11584  -1387  -1678   1139       O  
ATOM   5637  N   ASP B 380     -19.723   8.590  49.960  1.00 55.48           N  
ANISOU 5637  N   ASP B 380     5248   8689   7145   -770   -924   1332       N  
ATOM   5638  CA  ASP B 380     -20.810   9.186  50.737  1.00 59.09           C  
ANISOU 5638  CA  ASP B 380     5437   9388   7628   -663   -845   1477       C  
ATOM   5639  C   ASP B 380     -20.740  10.716  50.738  1.00 56.26           C  
ANISOU 5639  C   ASP B 380     5067   9051   7257   -381   -711   1449       C  
ATOM   5640  O   ASP B 380     -21.738  11.388  50.481  1.00 59.77           O  
ANISOU 5640  O   ASP B 380     5333   9678   7700   -277   -718   1566       O  
ATOM   5641  CB  ASP B 380     -20.820   8.642  52.170  1.00 60.01           C  
ANISOU 5641  CB  ASP B 380     5474   9556   7771   -702   -751   1511       C  
ATOM   5642  CG  ASP B 380     -21.354   7.217  52.260  1.00 64.91           C  
ANISOU 5642  CG  ASP B 380     6029  10229   8404   -983   -893   1608       C  
ATOM   5643  OD1 ASP B 380     -22.070   6.739  51.343  1.00 66.17           O  
ANISOU 5643  OD1 ASP B 380     6128  10457   8556  -1144  -1064   1695       O  
ATOM   5644  OD2 ASP B 380     -21.057   6.574  53.286  1.00 70.54           O  
ANISOU 5644  OD2 ASP B 380     6758  10913   9132  -1050   -837   1601       O  
ATOM   5645  N   VAL B 381     -19.551  11.251  50.995  1.00 53.35           N  
ANISOU 5645  N   VAL B 381     4898   8494   6880   -261   -599   1297       N  
ATOM   5646  CA  VAL B 381     -19.372  12.683  51.111  1.00 53.25           C  
ANISOU 5646  CA  VAL B 381     4915   8466   6851     -8   -472   1260       C  
ATOM   5647  C   VAL B 381     -19.527  13.354  49.743  1.00 54.61           C  
ANISOU 5647  C   VAL B 381     5139   8616   6994     48   -552   1261       C  
ATOM   5648  O   VAL B 381     -20.166  14.404  49.603  1.00 55.89           O  
ANISOU 5648  O   VAL B 381     5213   8879   7143    232   -511   1327       O  
ATOM   5649  CB  VAL B 381     -18.013  13.038  51.734  1.00 49.52           C  
ANISOU 5649  CB  VAL B 381     4649   7792   6373     71   -350   1103       C  
ATOM   5650  CG1 VAL B 381     -17.859  14.550  51.805  1.00 49.03           C  
ANISOU 5650  CG1 VAL B 381     4642   7698   6287    317   -237   1069       C  
ATOM   5651  CG2 VAL B 381     -17.926  12.456  53.132  1.00 50.31           C  
ANISOU 5651  CG2 VAL B 381     4694   7927   6495     35   -270   1110       C  
ATOM   5652  N   ALA B 382     -18.970  12.713  48.731  1.00 53.15           N  
ANISOU 5652  N   ALA B 382     5104   8301   6791   -104   -670   1194       N  
ATOM   5653  CA  ALA B 382     -18.898  13.318  47.437  1.00 53.78           C  
ANISOU 5653  CA  ALA B 382     5277   8327   6830    -57   -737   1174       C  
ATOM   5654  C   ALA B 382     -20.292  13.452  46.878  1.00 55.36           C  
ANISOU 5654  C   ALA B 382     5270   8736   7026    -57   -843   1333       C  
ATOM   5655  O   ALA B 382     -20.582  14.434  46.200  1.00 58.33           O  
ANISOU 5655  O   ALA B 382     5647   9140   7376     86   -846   1361       O  
ATOM   5656  CB  ALA B 382     -18.012  12.506  46.520  1.00 52.28           C  
ANISOU 5656  CB  ALA B 382     5294   7963   6609   -217   -834   1069       C  
ATOM   5657  N   VAL B 383     -21.134  12.457  47.155  1.00 56.42           N  
ANISOU 5657  N   VAL B 383     5232   9020   7185   -226   -936   1443       N  
ATOM   5658  CA  VAL B 383     -22.533  12.496  46.775  1.00 59.63           C  
ANISOU 5658  CA  VAL B 383     5396   9665   7594   -247  -1040   1619       C  
ATOM   5659  C   VAL B 383     -23.239  13.630  47.512  1.00 61.45           C  
ANISOU 5659  C   VAL B 383     5438  10070   7840      9   -901   1711       C  
ATOM   5660  O   VAL B 383     -24.038  14.339  46.902  1.00 65.84           O  
ANISOU 5660  O   VAL B 383     5877  10759   8380    124   -943   1809       O  
ATOM   5661  CB  VAL B 383     -23.276  11.142  46.968  1.00 62.58           C  
ANISOU 5661  CB  VAL B 383     5621  10166   7991   -513  -1177   1731       C  
ATOM   5662  CG1 VAL B 383     -24.784  11.369  47.084  1.00 65.53           C  
ANISOU 5662  CG1 VAL B 383     5665  10850   8384   -487  -1222   1943       C  
ATOM   5663  CG2 VAL B 383     -23.011  10.198  45.795  1.00 59.49           C  
ANISOU 5663  CG2 VAL B 383     5396   9645   7560   -745  -1375   1684       C  
HETATM 5664  N   CAS B 384     -22.957  13.811  48.801  1.00 58.89           N  
ANISOU 5664  N   CAS B 384     5093   9745   7539    110   -738   1681       N  
HETATM 5665  CA  CAS B 384     -23.562  14.937  49.523  1.00 61.29           C  
ANISOU 5665  CA  CAS B 384     5255  10193   7839    383   -592   1753       C  
HETATM 5666  CB  CAS B 384     -23.168  14.934  50.987  1.00 63.09           C  
ANISOU 5666  CB  CAS B 384     5491  10401   8080    457   -425   1707       C  
HETATM 5667  C   CAS B 384     -23.165  16.275  48.919  1.00 61.24           C  
ANISOU 5667  C   CAS B 384     5406  10068   7796    611   -540   1681       C  
HETATM 5668  O   CAS B 384     -23.998  17.174  48.778  1.00 60.16           O  
ANISOU 5668  O   CAS B 384     5141  10074   7642    812   -514   1780       O  
HETATM 5669  SG  CAS B 384     -23.721  13.496  51.901  1.00 70.69           S  
ANISOU 5669  SG  CAS B 384     6256  11525   9080    222   -458   1815       S  
HETATM 5670 AS   CAS B 384     -26.055  14.247  52.267  1.00 90.22          AS  
HETATM 5671  CE2 CAS B 384     -26.317  14.464  54.237  1.00 96.24           C  
HETATM 5672  CE1 CAS B 384     -26.851  12.639  51.378  1.00 92.70           C  
ATOM   5673  N   MET B 385     -21.883  16.399  48.573  1.00 59.98           N  
ANISOU 5673  N   MET B 385     5522   9646   7620    582   -524   1515       N  
ATOM   5674  CA  MET B 385     -21.351  17.592  47.944  1.00 58.82           C  
ANISOU 5674  CA  MET B 385     5558   9356   7436    755   -484   1440       C  
ATOM   5675  C   MET B 385     -21.799  17.669  46.499  1.00 61.65           C  
ANISOU 5675  C   MET B 385     5911   9748   7767    709   -636   1496       C  
ATOM   5676  O   MET B 385     -21.531  18.652  45.804  1.00 62.95           O  
ANISOU 5676  O   MET B 385     6208   9816   7893    845   -626   1463       O  
ATOM   5677  CB  MET B 385     -19.840  17.553  47.989  1.00 61.54           C  
ANISOU 5677  CB  MET B 385     6172   9437   7773    696   -432   1264       C  
ATOM   5678  CG  MET B 385     -19.256  17.743  49.369  1.00 60.22           C  
ANISOU 5678  CG  MET B 385     6054   9206   7621    774   -280   1193       C  
ATOM   5679  SD  MET B 385     -17.511  17.453  49.211  1.00 62.32           S  
ANISOU 5679  SD  MET B 385     6598   9196   7883    652   -262   1010       S  
ATOM   5680  CE  MET B 385     -17.014  18.851  48.195  1.00 60.89           C  
ANISOU 5680  CE  MET B 385     6610   8873   7654    799   -250    960       C  
ATOM   5681  N   ASP B 386     -22.460  16.609  46.048  1.00 63.50           N  
ANISOU 5681  N   ASP B 386     6004  10108   8013    504   -784   1583       N  
ATOM   5682  CA  ASP B 386     -23.062  16.555  44.725  1.00 67.34           C  
ANISOU 5682  CA  ASP B 386     6456  10662   8469    439   -952   1659       C  
ATOM   5683  C   ASP B 386     -22.076  16.452  43.558  1.00 64.36           C  
ANISOU 5683  C   ASP B 386     6348  10064   8044    344  -1029   1534       C  
ATOM   5684  O   ASP B 386     -22.334  16.958  42.481  1.00 64.71           O  
ANISOU 5684  O   ASP B 386     6433  10112   8043    390  -1113   1566       O  
ATOM   5685  CB  ASP B 386     -24.018  17.735  44.535  1.00 72.61           C  
ANISOU 5685  CB  ASP B 386     6981  11488   9121    685   -929   1779       C  
ATOM   5686  CG  ASP B 386     -25.107  17.418  43.573  1.00 79.98           C  
ANISOU 5686  CG  ASP B 386     7739  12609  10039    594  -1112   1925       C  
ATOM   5687  OD1 ASP B 386     -25.396  16.210  43.414  1.00 83.27           O  
ANISOU 5687  OD1 ASP B 386     8074  13093  10473    337  -1244   1968       O  
ATOM   5688  OD2 ASP B 386     -25.661  18.360  42.965  1.00 86.84           O  
ANISOU 5688  OD2 ASP B 386     8565  13552  10879    773  -1135   1999       O  
ATOM   5689  N   LEU B 387     -20.953  15.779  43.755  1.00 64.06           N  
ANISOU 5689  N   LEU B 387     6491   9841   8008    216   -998   1397       N  
ATOM   5690  CA  LEU B 387     -19.920  15.804  42.728  1.00 64.56           C  
ANISOU 5690  CA  LEU B 387     6811   9700   8017    167  -1034   1276       C  
ATOM   5691  C   LEU B 387     -20.146  14.736  41.683  1.00 68.56           C  
ANISOU 5691  C   LEU B 387     7355  10211   8484    -52  -1224   1291       C  
ATOM   5692  O   LEU B 387     -20.820  13.747  41.954  1.00 72.16           O  
ANISOU 5692  O   LEU B 387     7674  10778   8965   -212  -1320   1364       O  
ATOM   5693  CB  LEU B 387     -18.546  15.647  43.358  1.00 58.12           C  
ANISOU 5693  CB  LEU B 387     6177   8692   7214    154   -910   1125       C  
ATOM   5694  CG  LEU B 387     -18.217  16.643  44.467  1.00 57.41           C  
ANISOU 5694  CG  LEU B 387     6083   8574   7155    347   -731   1095       C  
ATOM   5695  CD1 LEU B 387     -16.901  16.233  45.134  1.00 51.30           C  
ANISOU 5695  CD1 LEU B 387     5462   7633   6398    287   -639    958       C  
ATOM   5696  CD2 LEU B 387     -18.168  18.064  43.906  1.00 52.05           C  
ANISOU 5696  CD2 LEU B 387     5492   7848   6439    542   -687   1100       C  
ATOM   5697  N   ASP B 388     -19.586  14.944  40.490  1.00 72.40           N  
ANISOU 5697  N   ASP B 388     8036  10573   8901    -61  -1280   1226       N  
ATOM   5698  CA  ASP B 388     -19.646  13.941  39.431  1.00 75.69           C  
ANISOU 5698  CA  ASP B 388     8547  10956   9257   -259  -1457   1216       C  
ATOM   5699  C   ASP B 388     -18.776  12.748  39.805  1.00 72.88           C  
ANISOU 5699  C   ASP B 388     8323  10464   8905   -417  -1450   1104       C  
ATOM   5700  O   ASP B 388     -17.561  12.755  39.621  1.00 73.93           O  
ANISOU 5700  O   ASP B 388     8662  10421   9006   -393  -1370    973       O  
ATOM   5701  CB  ASP B 388     -19.224  14.530  38.080  1.00 80.68           C  
ANISOU 5701  CB  ASP B 388     9367  11490   9798   -206  -1501   1172       C  
ATOM   5702  CG  ASP B 388     -19.371  13.534  36.918  1.00 85.92           C  
ANISOU 5702  CG  ASP B 388    10144  12123  10379   -399  -1696   1164       C  
ATOM   5703  OD1 ASP B 388     -19.792  12.376  37.138  1.00 92.14           O  
ANISOU 5703  OD1 ASP B 388    10876  12952  11180   -584  -1808   1190       O  
ATOM   5704  OD2 ASP B 388     -19.064  13.914  35.768  1.00 86.25           O  
ANISOU 5704  OD2 ASP B 388    10346  12092  10332   -368  -1741   1132       O  
ATOM   5705  N   THR B 389     -19.426  11.720  40.326  1.00 74.08           N  
ANISOU 5705  N   THR B 389     8349  10706   9094   -578  -1537   1168       N  
ATOM   5706  CA  THR B 389     -18.748  10.555  40.883  1.00 74.43           C  
ANISOU 5706  CA  THR B 389     8495  10635   9151   -720  -1531   1083       C  
ATOM   5707  C   THR B 389     -18.421   9.507  39.810  1.00 74.05           C  
ANISOU 5707  C   THR B 389     8659  10460   9017   -894  -1690   1018       C  
ATOM   5708  O   THR B 389     -17.781   8.493  40.086  1.00 72.51           O  
ANISOU 5708  O   THR B 389     8595  10141   8813  -1003  -1699    935       O  
ATOM   5709  CB  THR B 389     -19.567   9.965  42.070  1.00 73.38           C  
ANISOU 5709  CB  THR B 389     8137  10649   9096   -809  -1536   1188       C  
ATOM   5710  OG1 THR B 389     -18.677   9.573  43.111  1.00 73.57           O  
ANISOU 5710  OG1 THR B 389     8230  10565   9160   -803  -1409   1095       O  
ATOM   5711  CG2 THR B 389     -20.457   8.796  41.671  1.00 71.46           C  
ANISOU 5711  CG2 THR B 389     7836  10481   8834  -1055  -1749   1280       C  
ATOM   5712  N   ARG B 390     -18.844   9.781  38.584  1.00 76.99           N  
ANISOU 5712  N   ARG B 390     9078  10857   9316   -905  -1813   1052       N  
ATOM   5713  CA  ARG B 390     -18.792   8.798  37.508  1.00 81.52           C  
ANISOU 5713  CA  ARG B 390     9844  11337   9792  -1077  -1993   1012       C  
ATOM   5714  C   ARG B 390     -17.417   8.701  36.849  1.00 76.77           C  
ANISOU 5714  C   ARG B 390     9539  10522   9106  -1020  -1925    847       C  
ATOM   5715  O   ARG B 390     -17.165   7.805  36.049  1.00 76.10           O  
ANISOU 5715  O   ARG B 390     9659  10327   8929  -1139  -2047    785       O  
ATOM   5716  CB  ARG B 390     -19.856   9.116  36.448  1.00 85.05           C  
ANISOU 5716  CB  ARG B 390    10221  11910  10185  -1118  -2168   1125       C  
ATOM   5717  CG  ARG B 390     -21.306   8.912  36.893  1.00 93.76           C  
ANISOU 5717  CG  ARG B 390    11031  13241  11351  -1227  -2288   1305       C  
ATOM   5718  CD  ARG B 390     -22.273   9.564  35.900  1.00 97.77           C  
ANISOU 5718  CD  ARG B 390    11440  13896  11814  -1201  -2424   1424       C  
ATOM   5719  NE  ARG B 390     -21.946  10.983  35.697  1.00100.33           N  
ANISOU 5719  NE  ARG B 390    11764  14222  12136   -943  -2276   1406       N  
ATOM   5720  CZ  ARG B 390     -22.259  11.708  34.622  1.00102.13           C  
ANISOU 5720  CZ  ARG B 390    12026  14485  12294   -867  -2351   1446       C  
ATOM   5721  NH1 ARG B 390     -22.922  11.167  33.606  1.00105.70           N  
ANISOU 5721  NH1 ARG B 390    12511  14984  12668  -1026  -2578   1506       N  
ATOM   5722  NH2 ARG B 390     -21.903  12.988  34.562  1.00 98.48           N  
ANISOU 5722  NH2 ARG B 390    11579  14005  11835   -634  -2205   1429       N  
ATOM   5723  N   THR B 391     -16.529   9.629  37.176  1.00 75.37           N  
ANISOU 5723  N   THR B 391     9390  10293   8956   -837  -1730    780       N  
ATOM   5724  CA  THR B 391     -15.245   9.704  36.483  1.00 73.33           C  
ANISOU 5724  CA  THR B 391     9379   9867   8614   -769  -1653    646       C  
ATOM   5725  C   THR B 391     -14.117  10.251  37.371  1.00 66.51           C  
ANISOU 5725  C   THR B 391     8525   8934   7811   -634  -1436    566       C  
ATOM   5726  O   THR B 391     -14.317  11.188  38.144  1.00 67.71           O  
ANISOU 5726  O   THR B 391     8523   9162   8043   -525  -1330    615       O  
ATOM   5727  CB  THR B 391     -15.375  10.482  35.147  1.00 76.41           C  
ANISOU 5727  CB  THR B 391     9858  10266   8909   -703  -1705    665       C  
ATOM   5728  OG1 THR B 391     -14.079  10.866  34.676  1.00 79.59           O  
ANISOU 5728  OG1 THR B 391    10454  10539   9250   -599  -1576    554       O  
ATOM   5729  CG2 THR B 391     -16.255  11.739  35.304  1.00 76.59           C  
ANISOU 5729  CG2 THR B 391     9675  10439   8988   -588  -1683    786       C  
ATOM   5730  N   THR B 392     -12.940   9.647  37.242  1.00 61.07           N  
ANISOU 5730  N   THR B 392     8025   8103   7076   -640  -1379    446       N  
ATOM   5731  CA  THR B 392     -11.763   9.994  38.048  1.00 58.95           C  
ANISOU 5731  CA  THR B 392     7776   7765   6856   -537  -1191    368       C  
ATOM   5732  C   THR B 392     -11.333  11.462  37.834  1.00 56.52           C  
ANISOU 5732  C   THR B 392     7456   7468   6550   -386  -1065    374       C  
ATOM   5733  O   THR B 392     -10.988  12.158  38.783  1.00 50.21           O  
ANISOU 5733  O   THR B 392     6570   6679   5829   -302   -936    373       O  
ATOM   5734  CB  THR B 392     -10.543   9.059  37.741  1.00 57.84           C  
ANISOU 5734  CB  THR B 392     7848   7482   6647   -557  -1161    244       C  
ATOM   5735  OG1 THR B 392     -10.124   9.214  36.370  1.00 52.41           O  
ANISOU 5735  OG1 THR B 392     7338   6740   5835   -524  -1186    203       O  
ATOM   5736  CG2 THR B 392     -10.854   7.566  38.040  1.00 53.33           C  
ANISOU 5736  CG2 THR B 392     7327   6865   6070   -702  -1282    227       C  
ATOM   5737  N   SER B 393     -11.384  11.918  36.581  1.00 56.03           N  
ANISOU 5737  N   SER B 393     7496   7398   6396   -358  -1114    384       N  
ATOM   5738  CA  SER B 393     -10.884  13.247  36.217  1.00 54.22           C  
ANISOU 5738  CA  SER B 393     7297   7155   6149   -230  -1004    390       C  
ATOM   5739  C   SER B 393     -11.649  14.453  36.769  1.00 52.15           C  
ANISOU 5739  C   SER B 393     6872   6980   5961   -135   -969    483       C  
ATOM   5740  O   SER B 393     -11.104  15.553  36.761  1.00 53.69           O  
ANISOU 5740  O   SER B 393     7103   7140   6157    -31   -860    479       O  
ATOM   5741  CB  SER B 393     -10.683  13.375  34.694  1.00 55.36           C  
ANISOU 5741  CB  SER B 393     7612   7262   6160   -226  -1062    378       C  
ATOM   5742  OG  SER B 393     -11.847  13.017  33.984  1.00 57.16           O  
ANISOU 5742  OG  SER B 393     7821   7556   6340   -299  -1242    445       O  
ATOM   5743  N   SER B 394     -12.877  14.268  37.259  1.00 51.26           N  
ANISOU 5743  N   SER B 394     6589   6983   5906   -166  -1055    570       N  
ATOM   5744  CA  SER B 394     -13.578  15.364  37.967  1.00 50.71           C  
ANISOU 5744  CA  SER B 394     6358   7003   5907    -47  -1000    655       C  
ATOM   5745  C   SER B 394     -12.938  15.694  39.342  1.00 50.50           C  
ANISOU 5745  C   SER B 394     6285   6938   5964     19   -843    610       C  
ATOM   5746  O   SER B 394     -13.284  16.693  39.962  1.00 51.67           O  
ANISOU 5746  O   SER B 394     6348   7126   6157    140   -772    658       O  
ATOM   5747  CB  SER B 394     -15.056  15.034  38.160  1.00 52.29           C  
ANISOU 5747  CB  SER B 394     6364   7363   6142    -91  -1125    772       C  
ATOM   5748  OG  SER B 394     -15.230  14.208  39.299  1.00 54.26           O  
ANISOU 5748  OG  SER B 394     6499   7652   6466   -167  -1110    771       O  
ATOM   5749  N   LEU B 395     -12.017  14.841  39.798  1.00 45.88           N  
ANISOU 5749  N   LEU B 395     5767   6273   5391    -56   -796    519       N  
ATOM   5750  CA  LEU B 395     -11.354  14.953  41.091  1.00 44.85           C  
ANISOU 5750  CA  LEU B 395     5603   6106   5333    -20   -668    472       C  
ATOM   5751  C   LEU B 395     -12.309  15.004  42.286  1.00 46.10           C  
ANISOU 5751  C   LEU B 395     5571   6373   5570      8   -657    543       C  
ATOM   5752  O   LEU B 395     -12.028  15.683  43.288  1.00 49.72           O  
ANISOU 5752  O   LEU B 395     5995   6818   6076     98   -542    531       O  
ATOM   5753  CB  LEU B 395     -10.329  16.126  41.120  1.00 44.54           C  
ANISOU 5753  CB  LEU B 395     5662   5976   5285     84   -538    427       C  
ATOM   5754  CG  LEU B 395      -9.321  16.165  39.952  1.00 44.94           C  
ANISOU 5754  CG  LEU B 395     5886   5937   5251     63   -527    370       C  
ATOM   5755  CD1 LEU B 395      -8.303  17.302  40.062  1.00 41.97           C  
ANISOU 5755  CD1 LEU B 395     5592   5482   4872    137   -402    343       C  
ATOM   5756  CD2 LEU B 395      -8.636  14.805  39.726  1.00 41.60           C  
ANISOU 5756  CD2 LEU B 395     5541   5468   4797    -39   -554    293       C  
ATOM   5757  N   TRP B 396     -13.401  14.249  42.213  1.00 44.85           N  
ANISOU 5757  N   TRP B 396     5296   6324   5421    -78   -775    618       N  
ATOM   5758  CA  TRP B 396     -14.342  14.197  43.321  1.00 45.83           C  
ANISOU 5758  CA  TRP B 396     5222   6577   5613    -61   -762    700       C  
ATOM   5759  C   TRP B 396     -13.700  13.671  44.568  1.00 46.49           C  
ANISOU 5759  C   TRP B 396     5301   6615   5748    -90   -672    640       C  
ATOM   5760  O   TRP B 396     -13.854  14.248  45.657  1.00 47.35           O  
ANISOU 5760  O   TRP B 396     5320   6768   5903      8   -571    661       O  
ATOM   5761  CB  TRP B 396     -15.605  13.426  42.954  1.00 47.98           C  
ANISOU 5761  CB  TRP B 396     5360   6988   5884   -176   -917    806       C  
ATOM   5762  CG  TRP B 396     -15.383  11.977  42.579  1.00 49.20           C  
ANISOU 5762  CG  TRP B 396     5600   7082   6010   -371  -1032    765       C  
ATOM   5763  CD1 TRP B 396     -15.135  11.451  41.306  1.00 48.37           C  
ANISOU 5763  CD1 TRP B 396     5653   6899   5824   -461  -1147    723       C  
ATOM   5764  CD2 TRP B 396     -15.372  10.806  43.489  1.00 46.70           C  
ANISOU 5764  CD2 TRP B 396     5243   6764   5735   -500  -1048    758       C  
ATOM   5765  NE1 TRP B 396     -14.972  10.083  41.368  1.00 48.76           N  
ANISOU 5765  NE1 TRP B 396     5774   6890   5862   -625  -1232    686       N  
ATOM   5766  CE2 TRP B 396     -15.114   9.631  42.644  1.00 47.63           C  
ANISOU 5766  CE2 TRP B 396     5516   6788   5792   -661  -1182    709       C  
ATOM   5767  CE3 TRP B 396     -15.559  10.627  44.852  1.00 45.57           C  
ANISOU 5767  CE3 TRP B 396     4969   6683   5661   -495   -970    789       C  
ATOM   5768  CZ2 TRP B 396     -15.045   8.345  43.171  1.00 47.55           C  
ANISOU 5768  CZ2 TRP B 396     5533   6736   5796   -811  -1239    693       C  
ATOM   5769  CZ3 TRP B 396     -15.491   9.319  45.378  1.00 46.47           C  
ANISOU 5769  CZ3 TRP B 396     5098   6767   5792   -655  -1024    779       C  
ATOM   5770  CH2 TRP B 396     -15.226   8.210  44.556  1.00 47.10           C  
ANISOU 5770  CH2 TRP B 396     5335   6743   5816   -809  -1157    732       C  
ATOM   5771  N   LYS B 397     -12.932  12.599  44.429  1.00 46.31           N  
ANISOU 5771  N   LYS B 397     5390   6496   5709   -210   -703    562       N  
ATOM   5772  CA  LYS B 397     -12.174  12.076  45.554  1.00 45.30           C  
ANISOU 5772  CA  LYS B 397     5279   6310   5624   -233   -621    498       C  
ATOM   5773  C   LYS B 397     -11.351  13.159  46.246  1.00 42.63           C  
ANISOU 5773  C   LYS B 397     4975   5915   5307    -98   -471    446       C  
ATOM   5774  O   LYS B 397     -11.361  13.270  47.481  1.00 39.09           O  
ANISOU 5774  O   LYS B 397     4453   5493   4905    -60   -394    451       O  
ATOM   5775  CB  LYS B 397     -11.249  10.925  45.110  1.00 48.12           C  
ANISOU 5775  CB  LYS B 397     5793   6546   5944   -341   -665    407       C  
ATOM   5776  CG  LYS B 397     -11.967   9.636  44.697  1.00 51.56           C  
ANISOU 5776  CG  LYS B 397     6227   7005   6357   -501   -821    446       C  
ATOM   5777  CD  LYS B 397     -10.997   8.461  44.581  1.00 56.89           C  
ANISOU 5777  CD  LYS B 397     7071   7546   6999   -581   -844    349       C  
ATOM   5778  CE  LYS B 397     -11.674   7.233  43.982  1.00 61.24           C  
ANISOU 5778  CE  LYS B 397     7674   8087   7507   -744  -1017    379       C  
ATOM   5779  NZ  LYS B 397     -10.858   5.993  44.167  1.00 61.16           N  
ANISOU 5779  NZ  LYS B 397     7823   7944   7473   -813  -1038    294       N  
ATOM   5780  N   ASP B 398     -10.616  13.937  45.457  1.00 42.92           N  
ANISOU 5780  N   ASP B 398     5135   5870   5303    -36   -435    399       N  
ATOM   5781  CA  ASP B 398      -9.710  14.960  46.020  1.00 42.79           C  
ANISOU 5781  CA  ASP B 398     5179   5780   5300     64   -308    348       C  
ATOM   5782  C   ASP B 398     -10.519  16.078  46.698  1.00 43.33           C  
ANISOU 5782  C   ASP B 398     5154   5916   5393    193   -256    414       C  
ATOM   5783  O   ASP B 398     -10.166  16.577  47.781  1.00 41.38           O  
ANISOU 5783  O   ASP B 398     4906   5641   5174    257   -163    389       O  
ATOM   5784  CB  ASP B 398      -8.831  15.581  44.935  1.00 43.55           C  
ANISOU 5784  CB  ASP B 398     5420   5786   5340     87   -289    305       C  
ATOM   5785  CG  ASP B 398      -8.254  14.561  43.970  1.00 45.96           C  
ANISOU 5785  CG  ASP B 398     5822   6045   5594     -9   -348    255       C  
ATOM   5786  OD1 ASP B 398      -9.034  13.850  43.281  1.00 46.09           O  
ANISOU 5786  OD1 ASP B 398     5823   6107   5581    -74   -461    290       O  
ATOM   5787  OD2 ASP B 398      -7.006  14.517  43.860  1.00 46.63           O  
ANISOU 5787  OD2 ASP B 398     6006   6050   5660    -15   -284    184       O  
ATOM   5788  N   LYS B 399     -11.631  16.440  46.073  1.00 43.21           N  
ANISOU 5788  N   LYS B 399     5065   5991   5361    237   -321    501       N  
ATOM   5789  CA  LYS B 399     -12.480  17.478  46.628  1.00 43.60           C  
ANISOU 5789  CA  LYS B 399     5026   6115   5424    386   -274    571       C  
ATOM   5790  C   LYS B 399     -13.081  17.027  47.938  1.00 42.33           C  
ANISOU 5790  C   LYS B 399     4718   6054   5310    394   -237    608       C  
ATOM   5791  O   LYS B 399     -13.155  17.794  48.891  1.00 43.52           O  
ANISOU 5791  O   LYS B 399     4855   6210   5471    519   -142    611       O  
ATOM   5792  CB  LYS B 399     -13.551  17.931  45.629  1.00 43.99           C  
ANISOU 5792  CB  LYS B 399     5015   6256   5442    442   -357    666       C  
ATOM   5793  CG  LYS B 399     -12.999  18.767  44.484  1.00 44.48           C  
ANISOU 5793  CG  LYS B 399     5235   6215   5449    484   -366    640       C  
ATOM   5794  CD  LYS B 399     -14.088  19.062  43.467  1.00 50.43           C  
ANISOU 5794  CD  LYS B 399     5926   7067   6169    527   -467    738       C  
ATOM   5795  CE  LYS B 399     -13.757  20.242  42.567  1.00 53.16           C  
ANISOU 5795  CE  LYS B 399     6417   7322   6458    623   -454    738       C  
ATOM   5796  NZ  LYS B 399     -14.991  20.659  41.823  1.00 53.66           N  
ANISOU 5796  NZ  LYS B 399     6390   7503   6495    704   -546    851       N  
ATOM   5797  N   ALA B 400     -13.472  15.767  48.017  1.00 43.18           N  
ANISOU 5797  N   ALA B 400     4734   6234   5438    256   -311    636       N  
ATOM   5798  CA  ALA B 400     -14.138  15.294  49.241  1.00 41.64           C  
ANISOU 5798  CA  ALA B 400     4385   6154   5283    250   -279    692       C  
ATOM   5799  C   ALA B 400     -13.165  15.211  50.363  1.00 40.37           C  
ANISOU 5799  C   ALA B 400     4298   5901   5141    256   -179    606       C  
ATOM   5800  O   ALA B 400     -13.451  15.673  51.480  1.00 41.52           O  
ANISOU 5800  O   ALA B 400     4381   6096   5297    357    -89    627       O  
ATOM   5801  CB  ALA B 400     -14.803  13.971  49.016  1.00 40.99           C  
ANISOU 5801  CB  ALA B 400     4197   6163   5214     80   -396    753       C  
ATOM   5802  N   ALA B 401     -11.983  14.673  50.060  1.00 39.81           N  
ANISOU 5802  N   ALA B 401     4366   5695   5064    161   -190    508       N  
ATOM   5803  CA  ALA B 401     -10.953  14.537  51.065  1.00 37.94           C  
ANISOU 5803  CA  ALA B 401     4201   5370   4844    155   -108    427       C  
ATOM   5804  C   ALA B 401     -10.642  15.878  51.753  1.00 38.84           C  
ANISOU 5804  C   ALA B 401     4367   5441   4950    306      0    401       C  
ATOM   5805  O   ALA B 401     -10.490  15.951  52.976  1.00 43.33           O  
ANISOU 5805  O   ALA B 401     4921   6013   5531    344     72    385       O  
ATOM   5806  CB  ALA B 401      -9.710  13.900  50.467  1.00 37.70           C  
ANISOU 5806  CB  ALA B 401     4307   5215   4801     58   -134    335       C  
ATOM   5807  N   VAL B 402     -10.586  16.945  50.975  1.00 41.02           N  
ANISOU 5807  N   VAL B 402     4716   5671   5197    391      6    401       N  
ATOM   5808  CA  VAL B 402     -10.272  18.256  51.511  1.00 41.50           C  
ANISOU 5808  CA  VAL B 402     4865   5663   5240    525     93    375       C  
ATOM   5809  C   VAL B 402     -11.314  18.693  52.527  1.00 41.12           C  
ANISOU 5809  C   VAL B 402     4714   5719   5192    659    148    438       C  
ATOM   5810  O   VAL B 402     -10.972  19.126  53.633  1.00 40.17           O  
ANISOU 5810  O   VAL B 402     4645   5555   5064    725    227    399       O  
ATOM   5811  CB  VAL B 402     -10.076  19.312  50.375  1.00 45.22           C  
ANISOU 5811  CB  VAL B 402     5449   6059   5675    584     77    375       C  
ATOM   5812  CG1 VAL B 402     -10.114  20.730  50.951  1.00 42.31           C  
ANISOU 5812  CG1 VAL B 402     5168   5627   5280    743    152    372       C  
ATOM   5813  CG2 VAL B 402      -8.745  19.077  49.662  1.00 41.80           C  
ANISOU 5813  CG2 VAL B 402     5141   5510   5232    472     64    300       C  
ATOM   5814  N   GLU B 403     -12.591  18.570  52.170  1.00 43.53           N  
ANISOU 5814  N   GLU B 403     4871   6169   5497    702    106    539       N  
ATOM   5815  CA  GLU B 403     -13.646  18.918  53.114  1.00 42.77           C  
ANISOU 5815  CA  GLU B 403     4649   6205   5396    841    168    614       C  
ATOM   5816  C   GLU B 403     -13.654  18.048  54.392  1.00 42.99           C  
ANISOU 5816  C   GLU B 403     4594   6294   5445    781    212    613       C  
ATOM   5817  O   GLU B 403     -13.975  18.535  55.491  1.00 43.10           O  
ANISOU 5817  O   GLU B 403     4587   6351   5437    911    304    626       O  
ATOM   5818  CB  GLU B 403     -15.005  18.879  52.425  1.00 46.52           C  
ANISOU 5818  CB  GLU B 403     4953   6852   5871    885    106    739       C  
ATOM   5819  CG  GLU B 403     -15.145  19.791  51.207  1.00 49.53           C  
ANISOU 5819  CG  GLU B 403     5408   7188   6223    967     61    756       C  
ATOM   5820  CD  GLU B 403     -14.671  21.235  51.418  1.00 50.76           C  
ANISOU 5820  CD  GLU B 403     5743   7206   6338   1142    143    703       C  
ATOM   5821  OE1 GLU B 403     -14.759  21.785  52.547  1.00 53.61           O  
ANISOU 5821  OE1 GLU B 403     6126   7562   6681   1276    239    691       O  
ATOM   5822  OE2 GLU B 403     -14.204  21.834  50.432  1.00 49.95           O  
ANISOU 5822  OE2 GLU B 403     5774   6992   6212   1143    106    676       O  
ATOM   5823  N   ILE B 404     -13.304  16.765  54.254  1.00 42.41           N  
ANISOU 5823  N   ILE B 404     4490   6221   5405    592    147    598       N  
ATOM   5824  CA  ILE B 404     -13.274  15.857  55.406  1.00 41.56           C  
ANISOU 5824  CA  ILE B 404     4315   6161   5315    518    177    602       C  
ATOM   5825  C   ILE B 404     -12.143  16.262  56.325  1.00 42.97           C  
ANISOU 5825  C   ILE B 404     4644   6204   5480    556    258    497       C  
ATOM   5826  O   ILE B 404     -12.346  16.353  57.544  1.00 44.06           O  
ANISOU 5826  O   ILE B 404     4751   6388   5603    624    336    508       O  
ATOM   5827  CB  ILE B 404     -13.121  14.373  54.994  1.00 42.72           C  
ANISOU 5827  CB  ILE B 404     4426   6312   5495    307     76    607       C  
ATOM   5828  CG1 ILE B 404     -14.377  13.881  54.272  1.00 43.01           C  
ANISOU 5828  CG1 ILE B 404     4299   6503   5541    246    -17    727       C  
ATOM   5829  CG2 ILE B 404     -12.836  13.479  56.205  1.00 39.20           C  
ANISOU 5829  CG2 ILE B 404     3959   5874   5063    229    109    596       C  
ATOM   5830  CD1 ILE B 404     -14.064  12.822  53.234  1.00 41.94           C  
ANISOU 5830  CD1 ILE B 404     4216   6305   5414     61   -146    705       C  
ATOM   5831  N   ASN B 405     -10.959  16.530  55.763  1.00 40.77           N  
ANISOU 5831  N   ASN B 405     4523   5767   5199    514    241    403       N  
ATOM   5832  CA  ASN B 405      -9.864  16.969  56.616  1.00 42.08           C  
ANISOU 5832  CA  ASN B 405     4825   5812   5352    536    305    313       C  
ATOM   5833  C   ASN B 405     -10.214  18.326  57.257  1.00 44.37           C  
ANISOU 5833  C   ASN B 405     5174   6089   5597    722    387    316       C  
ATOM   5834  O   ASN B 405      -9.948  18.571  58.435  1.00 43.79           O  
ANISOU 5834  O   ASN B 405     5151   5988   5498    774    452    282       O  
ATOM   5835  CB  ASN B 405      -8.547  17.061  55.857  1.00 40.98           C  
ANISOU 5835  CB  ASN B 405     4824   5529   5218    455    274    229       C  
ATOM   5836  CG  ASN B 405      -7.938  15.695  55.537  1.00 44.08           C  
ANISOU 5836  CG  ASN B 405     5199   5909   5640    297    214    202       C  
ATOM   5837  OD1 ASN B 405      -8.323  15.035  54.567  1.00 48.43           O  
ANISOU 5837  OD1 ASN B 405     5703   6498   6201    228    142    234       O  
ATOM   5838  ND2 ASN B 405      -6.938  15.303  56.300  1.00 41.92           N  
ANISOU 5838  ND2 ASN B 405     4980   5572   5375    245    236    141       N  
ATOM   5839  N   LEU B 406     -10.830  19.210  56.483  1.00 44.73           N  
ANISOU 5839  N   LEU B 406     5225   6147   5622    830    381    357       N  
ATOM   5840  CA  LEU B 406     -11.182  20.499  57.031  1.00 46.29           C  
ANISOU 5840  CA  LEU B 406     5503   6317   5767   1024    454    359       C  
ATOM   5841  C   LEU B 406     -12.196  20.331  58.164  1.00 47.57           C  
ANISOU 5841  C   LEU B 406     5538   6628   5908   1136    525    422       C  
ATOM   5842  O   LEU B 406     -12.087  20.992  59.200  1.00 46.81           O  
ANISOU 5842  O   LEU B 406     5537   6488   5762   1256    603    387       O  
ATOM   5843  CB  LEU B 406     -11.712  21.437  55.942  1.00 50.92           C  
ANISOU 5843  CB  LEU B 406     6119   6893   6334   1131    429    401       C  
ATOM   5844  CG  LEU B 406     -12.020  22.878  56.361  1.00 51.38           C  
ANISOU 5844  CG  LEU B 406     6306   6888   6329   1350    496    398       C  
ATOM   5845  CD1 LEU B 406     -10.719  23.651  56.536  1.00 50.04           C  
ANISOU 5845  CD1 LEU B 406     6378   6502   6133   1315    505    294       C  
ATOM   5846  CD2 LEU B 406     -12.898  23.532  55.319  1.00 52.24           C  
ANISOU 5846  CD2 LEU B 406     6378   7046   6423   1469    466    475       C  
ATOM   5847  N   ALA B 407     -13.156  19.422  57.988  1.00 47.82           N  
ANISOU 5847  N   ALA B 407     5361   6837   5972   1086    495    519       N  
ATOM   5848  CA  ALA B 407     -14.140  19.160  59.054  1.00 49.26           C  
ANISOU 5848  CA  ALA B 407     5392   7191   6133   1175    567    599       C  
ATOM   5849  C   ALA B 407     -13.486  18.640  60.333  1.00 48.59           C  
ANISOU 5849  C   ALA B 407     5359   7067   6038   1116    618    542       C  
ATOM   5850  O   ALA B 407     -13.920  18.973  61.430  1.00 50.40           O  
ANISOU 5850  O   ALA B 407     5575   7360   6215   1250    712    562       O  
ATOM   5851  CB  ALA B 407     -15.223  18.206  58.587  1.00 48.22           C  
ANISOU 5851  CB  ALA B 407     5020   7260   6043   1089    509    724       C  
ATOM   5852  N   VAL B 408     -12.443  17.832  60.193  1.00 46.19           N  
ANISOU 5852  N   VAL B 408     5118   6659   5773    928    558    472       N  
ATOM   5853  CA  VAL B 408     -11.743  17.313  61.369  1.00 45.88           C  
ANISOU 5853  CA  VAL B 408     5133   6575   5723    867    593    419       C  
ATOM   5854  C   VAL B 408     -11.044  18.445  62.108  1.00 46.17           C  
ANISOU 5854  C   VAL B 408     5366   6477   5700    989    658    329       C  
ATOM   5855  O   VAL B 408     -11.123  18.516  63.328  1.00 48.21           O  
ANISOU 5855  O   VAL B 408     5649   6761   5910   1058    729    322       O  
ATOM   5856  CB  VAL B 408     -10.747  16.200  61.008  1.00 44.69           C  
ANISOU 5856  CB  VAL B 408     5011   6344   5627    657    511    367       C  
ATOM   5857  CG1 VAL B 408      -9.701  15.993  62.113  1.00 41.25           C  
ANISOU 5857  CG1 VAL B 408     4686   5814   5173    617    541    287       C  
ATOM   5858  CG2 VAL B 408     -11.520  14.927  60.703  1.00 42.12           C  
ANISOU 5858  CG2 VAL B 408     4511   6152   5342    532    452    459       C  
ATOM   5859  N   LEU B 409     -10.396  19.345  61.371  1.00 44.52           N  
ANISOU 5859  N   LEU B 409     5305   6125   5486   1011    631    267       N  
ATOM   5860  CA  LEU B 409      -9.701  20.472  62.006  1.00 45.20           C  
ANISOU 5860  CA  LEU B 409     5601   6062   5511   1104    673    185       C  
ATOM   5861  C   LEU B 409     -10.647  21.465  62.696  1.00 47.79           C  
ANISOU 5861  C   LEU B 409     5965   6435   5759   1340    763    216       C  
ATOM   5862  O   LEU B 409     -10.397  21.914  63.812  1.00 50.36           O  
ANISOU 5862  O   LEU B 409     6415   6703   6016   1421    819    167       O  
ATOM   5863  CB  LEU B 409      -8.840  21.192  60.984  1.00 43.99           C  
ANISOU 5863  CB  LEU B 409     5591   5752   5370   1055    617    129       C  
ATOM   5864  CG  LEU B 409      -7.531  20.503  60.613  1.00 42.37           C  
ANISOU 5864  CG  LEU B 409     5419   5464   5217    854    552     70       C  
ATOM   5865  CD1 LEU B 409      -7.069  21.062  59.271  1.00 41.70           C  
ANISOU 5865  CD1 LEU B 409     5405   5290   5149    813    502     58       C  
ATOM   5866  CD2 LEU B 409      -6.495  20.725  61.699  1.00 39.19           C  
ANISOU 5866  CD2 LEU B 409     5153   4955   4782    817    567     -8       C  
ATOM   5867  N   HIS B 410     -11.744  21.778  62.023  1.00 47.63           N  
ANISOU 5867  N   HIS B 410     5836   6522   5739   1458    774    299       N  
ATOM   5868  CA  HIS B 410     -12.785  22.637  62.567  1.00 49.37           C  
ANISOU 5868  CA  HIS B 410     6056   6820   5883   1710    865    348       C  
ATOM   5869  C   HIS B 410     -13.395  22.062  63.812  1.00 50.32           C  
ANISOU 5869  C   HIS B 410     6059   7093   5966   1767    949    394       C  
ATOM   5870  O   HIS B 410     -13.529  22.746  64.835  1.00 50.11           O  
ANISOU 5870  O   HIS B 410     6149   7041   5848   1939   1037    366       O  
ATOM   5871  CB  HIS B 410     -13.857  22.865  61.506  1.00 47.21           C  
ANISOU 5871  CB  HIS B 410     5639   6668   5632   1803    846    449       C  
ATOM   5872  CG  HIS B 410     -15.100  23.508  62.036  1.00 51.74           C  
ANISOU 5872  CG  HIS B 410     6141   7382   6135   2070    945    528       C  
ATOM   5873  ND1 HIS B 410     -15.163  24.819  62.335  1.00 52.09           N  
ANISOU 5873  ND1 HIS B 410     6383   7316   6092   2297   1004    488       N  
ATOM   5874  CD2 HIS B 410     -16.354  22.970  62.341  1.00 52.40           C  
ANISOU 5874  CD2 HIS B 410     5967   7725   6219   2148    998    657       C  
ATOM   5875  CE1 HIS B 410     -16.398  25.115  62.793  1.00 53.73           C  
ANISOU 5875  CE1 HIS B 410     6466   7705   6243   2535   1098    581       C  
ATOM   5876  NE2 HIS B 410     -17.125  23.985  62.797  1.00 55.63           N  
ANISOU 5876  NE2 HIS B 410     6413   8183   6540   2438   1097    690       N  
ATOM   5877  N   SER B 411     -13.773  20.794  63.750  1.00 51.02           N  
ANISOU 5877  N   SER B 411     5930   7338   6117   1621    922    469       N  
ATOM   5878  CA  SER B 411     -14.452  20.173  64.881  1.00 50.13           C  
ANISOU 5878  CA  SER B 411     5679   7396   5970   1660   1003    537       C  
ATOM   5879  C   SER B 411     -13.518  20.125  66.083  1.00 48.31           C  
ANISOU 5879  C   SER B 411     5619   7047   5689   1629   1038    440       C  
ATOM   5880  O   SER B 411     -13.898  20.542  67.167  1.00 45.47           O  
ANISOU 5880  O   SER B 411     5303   6735   5239   1792   1139    445       O  
ATOM   5881  CB  SER B 411     -14.914  18.772  64.509  1.00 51.52           C  
ANISOU 5881  CB  SER B 411     5615   7731   6227   1466    943    635       C  
ATOM   5882  OG  SER B 411     -15.690  18.809  63.330  1.00 51.03           O  
ANISOU 5882  OG  SER B 411     5413   7767   6211   1470    887    719       O  
ATOM   5883  N   PHE B 412     -12.284  19.646  65.878  1.00 45.97           N  
ANISOU 5883  N   PHE B 412     5422   6601   5443   1430    953    354       N  
ATOM   5884  CA  PHE B 412     -11.308  19.635  66.959  1.00 46.91           C  
ANISOU 5884  CA  PHE B 412     5706   6603   5517   1391    968    262       C  
ATOM   5885  C   PHE B 412     -11.025  21.029  67.548  1.00 48.61           C  
ANISOU 5885  C   PHE B 412     6162   6679   5629   1571   1020    181       C  
ATOM   5886  O   PHE B 412     -10.897  21.175  68.762  1.00 50.51           O  
ANISOU 5886  O   PHE B 412     6501   6905   5786   1641   1080    147       O  
ATOM   5887  CB  PHE B 412     -10.007  18.912  66.553  1.00 44.40           C  
ANISOU 5887  CB  PHE B 412     5438   6160   5273   1159    865    192       C  
ATOM   5888  CG  PHE B 412     -10.042  17.408  66.778  1.00 45.32           C  
ANISOU 5888  CG  PHE B 412     5397   6379   5443    994    834    244       C  
ATOM   5889  CD1 PHE B 412     -10.820  16.568  65.963  1.00 46.16           C  
ANISOU 5889  CD1 PHE B 412     5308   6615   5616    914    795    338       C  
ATOM   5890  CD2 PHE B 412      -9.285  16.820  67.786  1.00 44.99           C  
ANISOU 5890  CD2 PHE B 412     5417   6294   5382    911    831    200       C  
ATOM   5891  CE1 PHE B 412     -10.821  15.179  66.147  1.00 45.14           C  
ANISOU 5891  CE1 PHE B 412     5066   6553   5531    750    752    384       C  
ATOM   5892  CE2 PHE B 412      -9.283  15.432  67.973  1.00 44.33           C  
ANISOU 5892  CE2 PHE B 412     5212   6284   5345    761    795    248       C  
ATOM   5893  CZ  PHE B 412     -10.058  14.609  67.157  1.00 41.73           C  
ANISOU 5893  CZ  PHE B 412     4706   6069   5081    678    756    340       C  
ATOM   5894  N   GLN B 413     -10.934  22.047  66.701  1.00 52.50           N  
ANISOU 5894  N   GLN B 413     6767   7060   6119   1645    994    151       N  
ATOM   5895  CA  GLN B 413     -10.681  23.421  67.173  1.00 56.45           C  
ANISOU 5895  CA  GLN B 413     7528   7402   6517   1811   1029     75       C  
ATOM   5896  C   GLN B 413     -11.844  23.963  67.990  1.00 58.03           C  
ANISOU 5896  C   GLN B 413     7722   7715   6611   2082   1152    123       C  
ATOM   5897  O   GLN B 413     -11.631  24.572  69.046  1.00 59.83           O  
ANISOU 5897  O   GLN B 413     8147   7857   6729   2198   1204     60       O  
ATOM   5898  CB  GLN B 413     -10.282  24.353  66.011  1.00 57.41           C  
ANISOU 5898  CB  GLN B 413     7782   7369   6663   1809    963     41       C  
ATOM   5899  CG  GLN B 413      -8.834  24.078  65.562  1.00 59.94           C  
ANISOU 5899  CG  GLN B 413     8186   7539   7048   1564    859    -33       C  
ATOM   5900  CD  GLN B 413      -8.481  24.553  64.153  1.00 61.02           C  
ANISOU 5900  CD  GLN B 413     8361   7584   7239   1499    787    -34       C  
ATOM   5901  OE1 GLN B 413      -9.284  25.190  63.459  1.00 60.76           O  
ANISOU 5901  OE1 GLN B 413     8318   7574   7194   1638    804     14       O  
ATOM   5902  NE2 GLN B 413      -7.260  24.244  63.730  1.00 58.45           N  
ANISOU 5902  NE2 GLN B 413     8077   7162   6968   1292    710    -83       N  
ATOM   5903  N   LEU B 414     -13.062  23.685  67.524  1.00 57.43           N  
ANISOU 5903  N   LEU B 414     7415   7843   6564   2177   1197    241       N  
ATOM   5904  CA  LEU B 414     -14.284  24.084  68.215  1.00 58.52           C  
ANISOU 5904  CA  LEU B 414     7485   8142   6607   2445   1325    315       C  
ATOM   5905  C   LEU B 414     -14.501  23.352  69.550  1.00 60.43           C  
ANISOU 5905  C   LEU B 414     7653   8515   6793   2448   1409    341       C  
ATOM   5906  O   LEU B 414     -15.159  23.875  70.455  1.00 64.35           O  
ANISOU 5906  O   LEU B 414     8195   9084   7170   2684   1529    360       O  
ATOM   5907  CB  LEU B 414     -15.506  23.902  67.310  1.00 59.04           C  
ANISOU 5907  CB  LEU B 414     7287   8418   6727   2520   1338    452       C  
ATOM   5908  CG  LEU B 414     -16.747  24.694  67.750  1.00 67.68           C  
ANISOU 5908  CG  LEU B 414     8340   9657   7718   2854   1468    528       C  
ATOM   5909  CD1 LEU B 414     -16.771  26.074  67.091  1.00 68.11           C  
ANISOU 5909  CD1 LEU B 414     8600   9552   7727   3049   1457    483       C  
ATOM   5910  CD2 LEU B 414     -18.029  23.910  67.472  1.00 66.64           C  
ANISOU 5910  CD2 LEU B 414     7842   9842   7636   2869   1505    701       C  
ATOM   5911  N   ALA B 415     -13.967  22.148  69.681  1.00 56.85           N  
ANISOU 5911  N   ALA B 415     7092   8093   6415   2199   1351    346       N  
ATOM   5912  CA  ALA B 415     -14.115  21.409  70.925  1.00 57.10           C  
ANISOU 5912  CA  ALA B 415     7063   8239   6393   2182   1421    376       C  
ATOM   5913  C   ALA B 415     -12.931  21.680  71.854  1.00 57.12           C  
ANISOU 5913  C   ALA B 415     7336   8040   6326   2137   1401    242       C  
ATOM   5914  O   ALA B 415     -12.891  21.155  72.957  1.00 55.34           O  
ANISOU 5914  O   ALA B 415     7109   7877   6042   2123   1452    249       O  
ATOM   5915  CB  ALA B 415     -14.234  19.919  70.640  1.00 54.87           C  
ANISOU 5915  CB  ALA B 415     6530   8098   6221   1943   1366    463       C  
ATOM   5916  N   LYS B 416     -11.971  22.495  71.393  1.00 58.49           N  
ANISOU 5916  N   LYS B 416     7739   7980   6505   2102   1321    130       N  
ATOM   5917  CA  LYS B 416     -10.770  22.871  72.170  1.00 58.46           C  
ANISOU 5917  CA  LYS B 416     8004   7772   6437   2040   1277      4       C  
ATOM   5918  C   LYS B 416      -9.981  21.619  72.515  1.00 54.07           C  
ANISOU 5918  C   LYS B 416     7362   7235   5948   1795   1212     -2       C  
ATOM   5919  O   LYS B 416      -9.594  21.380  73.664  1.00 50.78           O  
ANISOU 5919  O   LYS B 416     7036   6801   5456   1781   1232    -38       O  
ATOM   5920  CB  LYS B 416     -11.118  23.669  73.452  1.00 64.16           C  
ANISOU 5920  CB  LYS B 416     8921   8472   6986   2275   1382    -34       C  
ATOM   5921  CG  LYS B 416     -11.968  24.928  73.262  1.00 71.08           C  
ANISOU 5921  CG  LYS B 416     9906   9330   7771   2567   1462    -28       C  
ATOM   5922  CD  LYS B 416     -11.141  26.201  73.064  1.00 78.79           C  
ANISOU 5922  CD  LYS B 416    11223  10022   8692   2598   1390   -150       C  
ATOM   5923  CE  LYS B 416     -10.608  26.362  71.637  1.00 80.26           C  
ANISOU 5923  CE  LYS B 416    11385  10103   9007   2440   1274   -157       C  
ATOM   5924  NZ  LYS B 416     -10.265  27.773  71.282  1.00 82.33           N  
ANISOU 5924  NZ  LYS B 416    11947  10131   9204   2540   1233   -234       N  
ATOM   5925  N   VAL B 417      -9.795  20.793  71.499  1.00 51.50           N  
ANISOU 5925  N   VAL B 417     6863   6949   5756   1613   1136     39       N  
ATOM   5926  CA  VAL B 417      -9.031  19.586  71.645  1.00 48.23           C  
ANISOU 5926  CA  VAL B 417     6372   6540   5413   1389   1065     35       C  
ATOM   5927  C   VAL B 417      -7.848  19.673  70.704  1.00 48.20           C  
ANISOU 5927  C   VAL B 417     6444   6376   5493   1225    948    -37       C  
ATOM   5928  O   VAL B 417      -8.011  20.014  69.538  1.00 47.81           O  
ANISOU 5928  O   VAL B 417     6356   6306   5502   1224    917    -23       O  
ATOM   5929  CB  VAL B 417      -9.880  18.348  71.353  1.00 47.42           C  
ANISOU 5929  CB  VAL B 417     5997   6638   5384   1313   1080    155       C  
ATOM   5930  CG1 VAL B 417      -9.007  17.090  71.425  1.00 44.91           C  
ANISOU 5930  CG1 VAL B 417     5632   6294   5138   1084    995    143       C  
ATOM   5931  CG2 VAL B 417     -11.045  18.271  72.342  1.00 47.88           C  
ANISOU 5931  CG2 VAL B 417     5962   6879   5352   1470   1206    242       C  
ATOM   5932  N   THR B 418      -6.666  19.375  71.235  1.00 47.02           N  
ANISOU 5932  N   THR B 418     6398   6125   5344   1094    886   -106       N  
ATOM   5933  CA  THR B 418      -5.405  19.555  70.541  1.00 43.31           C  
ANISOU 5933  CA  THR B 418     6014   5508   4934    947    783   -174       C  
ATOM   5934  C   THR B 418      -5.300  18.746  69.250  1.00 46.33           C  
ANISOU 5934  C   THR B 418     6230   5935   5439    817    727   -133       C  
ATOM   5935  O   THR B 418      -5.447  17.520  69.252  1.00 46.55           O  
ANISOU 5935  O   THR B 418     6107   6060   5520    727    715    -84       O  
ATOM   5936  CB  THR B 418      -4.221  19.178  71.453  1.00 41.90           C  
ANISOU 5936  CB  THR B 418     5931   5257   4734    828    727   -233       C  
ATOM   5937  OG1 THR B 418      -4.340  19.841  72.719  1.00 46.67           O  
ANISOU 5937  OG1 THR B 418     6701   5821   5209    944    774   -272       O  
ATOM   5938  CG2 THR B 418      -2.883  19.606  70.812  1.00 41.06           C  
ANISOU 5938  CG2 THR B 418     5923   5005   4672    694    628   -298       C  
ATOM   5939  N   ILE B 419      -4.975  19.442  68.158  1.00 46.27           N  
ANISOU 5939  N   ILE B 419     6273   5841   5468    801    687   -157       N  
ATOM   5940  CA  ILE B 419      -4.805  18.836  66.831  1.00 43.74           C  
ANISOU 5940  CA  ILE B 419     5830   5544   5247    690    632   -129       C  
ATOM   5941  C   ILE B 419      -3.742  19.669  66.114  1.00 40.66           C  
ANISOU 5941  C   ILE B 419     5572   5008   4870    627    574   -188       C  
ATOM   5942  O   ILE B 419      -3.576  20.849  66.396  1.00 43.09           O  
ANISOU 5942  O   ILE B 419     6049   5211   5115    698    583   -229       O  
ATOM   5943  CB  ILE B 419      -6.167  18.870  66.044  1.00 43.84           C  
ANISOU 5943  CB  ILE B 419     5710   5669   5278    787    670    -48       C  
ATOM   5944  CG1 ILE B 419      -6.174  18.009  64.776  1.00 43.42           C  
ANISOU 5944  CG1 ILE B 419     5520   5662   5315    669    610    -11       C  
ATOM   5945  CG2 ILE B 419      -6.555  20.283  65.686  1.00 43.42           C  
ANISOU 5945  CG2 ILE B 419     5776   5548   5175    935    699    -60       C  
ATOM   5946  CD1 ILE B 419      -6.828  16.658  64.976  1.00 45.19           C  
ANISOU 5946  CD1 ILE B 419     5572   6024   5575    606    608     60       C  
ATOM   5947  N   VAL B 420      -3.025  19.059  65.180  1.00 39.41           N  
ANISOU 5947  N   VAL B 420     5345   4841   4786    493    516   -190       N  
ATOM   5948  CA  VAL B 420      -2.083  19.799  64.355  1.00 37.65           C  
ANISOU 5948  CA  VAL B 420     5217   4508   4578    426    470   -225       C  
ATOM   5949  C   VAL B 420      -2.379  19.401  62.922  1.00 37.33           C  
ANISOU 5949  C   VAL B 420     5068   4515   4599    395    452   -185       C  
ATOM   5950  O   VAL B 420      -2.567  18.199  62.655  1.00 42.42           O  
ANISOU 5950  O   VAL B 420     5578   5248   5292    341    439   -156       O  
ATOM   5951  CB  VAL B 420      -0.609  19.515  64.776  1.00 37.53           C  
ANISOU 5951  CB  VAL B 420     5247   4436   4577    288    415   -272       C  
ATOM   5952  CG1 VAL B 420      -0.208  18.075  64.497  1.00 33.33           C  
ANISOU 5952  CG1 VAL B 420     4568   3985   4111    193    390   -255       C  
ATOM   5953  CG2 VAL B 420       0.355  20.491  64.112  1.00 33.68           C  
ANISOU 5953  CG2 VAL B 420     4870   3839   4089    217    373   -298       C  
ATOM   5954  N   ASP B 421      -2.489  20.386  62.018  1.00 36.36           N  
ANISOU 5954  N   ASP B 421     5016   4331   4467    432    448   -179       N  
ATOM   5955  CA  ASP B 421      -2.671  20.112  60.591  1.00 36.61           C  
ANISOU 5955  CA  ASP B 421     4969   4397   4545    399    424   -145       C  
ATOM   5956  C   ASP B 421      -1.306  19.692  60.008  1.00 38.56           C  
ANISOU 5956  C   ASP B 421     5215   4607   4830    252    380   -173       C  
ATOM   5957  O   ASP B 421      -0.252  19.944  60.626  1.00 38.57           O  
ANISOU 5957  O   ASP B 421     5289   4545   4819    185    365   -212       O  
ATOM   5958  CB  ASP B 421      -3.276  21.313  59.835  1.00 38.64           C  
ANISOU 5958  CB  ASP B 421     5306   4603   4771    497    435   -121       C  
ATOM   5959  CG  ASP B 421      -2.291  22.479  59.672  1.00 43.00           C  
ANISOU 5959  CG  ASP B 421     6035   5008   5293    455    413   -159       C  
ATOM   5960  OD1 ASP B 421      -1.231  22.332  59.024  1.00 45.11           O  
ANISOU 5960  OD1 ASP B 421     6306   5244   5590    326    378   -170       O  
ATOM   5961  OD2 ASP B 421      -2.560  23.572  60.212  1.00 51.29           O  
ANISOU 5961  OD2 ASP B 421     7231   5972   6283    552    431   -174       O  
ATOM   5962  N   HIS B 422      -1.331  19.072  58.830  1.00 37.32           N  
ANISOU 5962  N   HIS B 422     4976   4494   4709    208    359   -149       N  
ATOM   5963  CA  HIS B 422      -0.138  18.531  58.191  1.00 36.47           C  
ANISOU 5963  CA  HIS B 422     4848   4378   4630     96    331   -167       C  
ATOM   5964  C   HIS B 422       0.846  19.557  57.674  1.00 39.07           C  
ANISOU 5964  C   HIS B 422     5276   4625   4943     43    324   -178       C  
ATOM   5965  O   HIS B 422       2.036  19.253  57.499  1.00 38.13           O  
ANISOU 5965  O   HIS B 422     5141   4507   4840    -50    310   -192       O  
ATOM   5966  CB  HIS B 422      -0.522  17.577  57.068  1.00 38.44           C  
ANISOU 5966  CB  HIS B 422     5007   4694   4906     79    312   -142       C  
ATOM   5967  CG  HIS B 422      -1.517  18.141  56.089  1.00 42.08           C  
ANISOU 5967  CG  HIS B 422     5472   5164   5351    142    310   -101       C  
ATOM   5968  ND1 HIS B 422      -2.830  18.293  56.390  1.00 46.55           N  
ANISOU 5968  ND1 HIS B 422     5998   5778   5909    233    320    -64       N  
ATOM   5969  CD2 HIS B 422      -1.371  18.563  54.768  1.00 42.36           C  
ANISOU 5969  CD2 HIS B 422     5541   5178   5376    130    296    -85       C  
ATOM   5970  CE1 HIS B 422      -3.491  18.799  55.315  1.00 42.99           C  
ANISOU 5970  CE1 HIS B 422     5553   5336   5446    279    307    -25       C  
ATOM   5971  NE2 HIS B 422      -2.609  18.965  54.328  1.00 42.46           N  
ANISOU 5971  NE2 HIS B 422     5539   5219   5375    214    291    -41       N  
ATOM   5972  N   HIS B 423       0.385  20.775  57.436  1.00 36.52           N  
ANISOU 5972  N   HIS B 423     5054   4235   4586    101    332   -165       N  
ATOM   5973  CA  HIS B 423       1.304  21.827  57.063  1.00 37.60           C  
ANISOU 5973  CA  HIS B 423     5305   4280   4702     34    317   -167       C  
ATOM   5974  C   HIS B 423       2.102  22.276  58.271  1.00 39.19           C  
ANISOU 5974  C   HIS B 423     5591   4415   4883    -20    301   -202       C  
ATOM   5975  O   HIS B 423       3.356  22.442  58.189  1.00 41.09           O  
ANISOU 5975  O   HIS B 423     5849   4633   5131   -144    275   -205       O  
ATOM   5976  CB  HIS B 423       0.568  23.018  56.430  1.00 37.84           C  
ANISOU 5976  CB  HIS B 423     5445   4238   4695    115    322   -139       C  
ATOM   5977  CG  HIS B 423      -0.211  22.668  55.188  1.00 39.03           C  
ANISOU 5977  CG  HIS B 423     5520   4453   4857    163    325    -99       C  
ATOM   5978  ND1 HIS B 423       0.386  22.384  54.005  1.00 39.94           N  
ANISOU 5978  ND1 HIS B 423     5601   4592   4983     85    314    -80       N  
ATOM   5979  CD2 HIS B 423      -1.588  22.531  54.978  1.00 40.86           C  
ANISOU 5979  CD2 HIS B 423     5697   4742   5085    283    333    -68       C  
ATOM   5980  CE1 HIS B 423      -0.556  22.093  53.082  1.00 41.28           C  
ANISOU 5980  CE1 HIS B 423     5718   4816   5151    148    308    -47       C  
ATOM   5981  NE2 HIS B 423      -1.767  22.193  53.673  1.00 42.84           N  
ANISOU 5981  NE2 HIS B 423     5895   5038   5344    264    315    -35       N  
ATOM   5982  N   ALA B 424       1.413  22.510  59.386  1.00 34.20           N  
ANISOU 5982  N   ALA B 424     5015   3760   4220     69    315   -224       N  
ATOM   5983  CA  ALA B 424       2.106  22.983  60.578  1.00 36.77           C  
ANISOU 5983  CA  ALA B 424     5448   4012   4511     22    291   -263       C  
ATOM   5984  C   ALA B 424       3.030  21.886  61.085  1.00 37.74           C  
ANISOU 5984  C   ALA B 424     5458   4209   4672    -77    270   -277       C  
ATOM   5985  O   ALA B 424       4.180  22.161  61.449  1.00 41.78           O  
ANISOU 5985  O   ALA B 424     6013   4683   5179   -191    228   -289       O  
ATOM   5986  CB  ALA B 424       1.133  23.408  61.658  1.00 35.84           C  
ANISOU 5986  CB  ALA B 424     5420   3861   4336    159    319   -285       C  
ATOM   5987  N   ALA B 425       2.571  20.634  61.013  1.00 37.57           N  
ANISOU 5987  N   ALA B 425     5290   4294   4689    -43    293   -267       N  
ATOM   5988  CA  ALA B 425       3.356  19.510  61.531  1.00 36.02           C  
ANISOU 5988  CA  ALA B 425     4998   4164   4526   -113    274   -279       C  
ATOM   5989  C   ALA B 425       4.657  19.316  60.784  1.00 37.28           C  
ANISOU 5989  C   ALA B 425     5106   4343   4717   -226    248   -268       C  
ATOM   5990  O   ALA B 425       5.704  19.225  61.422  1.00 42.11           O  
ANISOU 5990  O   ALA B 425     5712   4958   5330   -306    215   -278       O  
ATOM   5991  CB  ALA B 425       2.560  18.232  61.545  1.00 32.34           C  
ANISOU 5991  CB  ALA B 425     4411   3789   4088    -60    296   -266       C  
ATOM   5992  N   THR B 426       4.598  19.281  59.445  1.00 37.75           N  
ANISOU 5992  N   THR B 426     5125   4423   4794   -228    264   -242       N  
ATOM   5993  CA  THR B 426       5.780  19.063  58.608  1.00 36.40           C  
ANISOU 5993  CA  THR B 426     4894   4293   4645   -315    257   -222       C  
ATOM   5994  C   THR B 426       6.767  20.246  58.687  1.00 38.43           C  
ANISOU 5994  C   THR B 426     5232   4490   4880   -420    229   -207       C  
ATOM   5995  O   THR B 426       7.977  20.040  58.690  1.00 40.82           O  
ANISOU 5995  O   THR B 426     5471   4840   5197   -513    212   -190       O  
ATOM   5996  CB  THR B 426       5.408  18.784  57.134  1.00 39.34           C  
ANISOU 5996  CB  THR B 426     5224   4699   5023   -284    284   -198       C  
ATOM   5997  OG1 THR B 426       4.614  19.850  56.618  1.00 39.25           O  
ANISOU 5997  OG1 THR B 426     5307   4622   4985   -245    291   -181       O  
ATOM   5998  CG2 THR B 426       4.658  17.491  56.993  1.00 40.54           C  
ANISOU 5998  CG2 THR B 426     5297   4912   5196   -217    292   -207       C  
ATOM   5999  N   VAL B 427       6.242  21.468  58.795  1.00 39.82           N  
ANISOU 5999  N   VAL B 427     5551   4561   5019   -405    220   -209       N  
ATOM   6000  CA  VAL B 427       7.056  22.665  59.062  1.00 43.44           C  
ANISOU 6000  CA  VAL B 427     6128   4932   5447   -516    176   -197       C  
ATOM   6001  C   VAL B 427       7.842  22.514  60.372  1.00 42.30           C  
ANISOU 6001  C   VAL B 427     5987   4788   5296   -589    127   -220       C  
ATOM   6002  O   VAL B 427       9.049  22.802  60.415  1.00 42.58           O  
ANISOU 6002  O   VAL B 427     6006   4837   5336   -729     83   -193       O  
ATOM   6003  CB  VAL B 427       6.185  23.966  59.064  1.00 46.65           C  
ANISOU 6003  CB  VAL B 427     6724   5201   5802   -455    172   -203       C  
ATOM   6004  CG1 VAL B 427       6.874  25.141  59.760  1.00 46.90           C  
ANISOU 6004  CG1 VAL B 427     6926   5108   5787   -561    108   -209       C  
ATOM   6005  CG2 VAL B 427       5.862  24.377  57.641  1.00 46.54           C  
ANISOU 6005  CG2 VAL B 427     6718   5177   5788   -437    198   -161       C  
ATOM   6006  N   SER B 428       7.180  22.045  61.426  1.00 40.06           N  
ANISOU 6006  N   SER B 428     5716   4503   5000   -502    132   -263       N  
ATOM   6007  CA  SER B 428       7.901  21.790  62.667  1.00 40.85           C  
ANISOU 6007  CA  SER B 428     5818   4613   5089   -565     82   -284       C  
ATOM   6008  C   SER B 428       8.899  20.630  62.515  1.00 40.37           C  
ANISOU 6008  C   SER B 428     5574   4683   5082   -624     76   -261       C  
ATOM   6009  O   SER B 428       9.970  20.649  63.126  1.00 39.50           O  
ANISOU 6009  O   SER B 428     5442   4597   4971   -728     19   -251       O  
ATOM   6010  CB  SER B 428       6.970  21.613  63.869  1.00 43.45           C  
ANISOU 6010  CB  SER B 428     6218   4913   5380   -456     94   -330       C  
ATOM   6011  OG  SER B 428       6.284  20.365  63.870  1.00 52.01           O  
ANISOU 6011  OG  SER B 428     7171   6092   6497   -362    143   -331       O  
ATOM   6012  N   PHE B 429       8.596  19.660  61.653  1.00 38.67           N  
ANISOU 6012  N   PHE B 429     5235   4551   4908   -558    127   -248       N  
ATOM   6013  CA  PHE B 429       9.558  18.573  61.435  1.00 37.19           C  
ANISOU 6013  CA  PHE B 429     4893   4478   4760   -588    126   -228       C  
ATOM   6014  C   PHE B 429      10.850  19.044  60.774  1.00 39.51           C  
ANISOU 6014  C   PHE B 429     5130   4817   5063   -707    110   -177       C  
ATOM   6015  O   PHE B 429      11.965  18.618  61.152  1.00 38.69           O  
ANISOU 6015  O   PHE B 429     4929   4796   4976   -770     78   -154       O  
ATOM   6016  CB  PHE B 429       8.951  17.426  60.648  1.00 35.86           C  
ANISOU 6016  CB  PHE B 429     4636   4370   4619   -489    178   -230       C  
ATOM   6017  CG  PHE B 429       9.812  16.223  60.646  1.00 36.39           C  
ANISOU 6017  CG  PHE B 429     4578   4535   4715   -485    176   -221       C  
ATOM   6018  CD1 PHE B 429       9.984  15.489  61.810  1.00 34.67           C  
ANISOU 6018  CD1 PHE B 429     4336   4338   4501   -471    145   -238       C  
ATOM   6019  CD2 PHE B 429      10.502  15.847  59.492  1.00 37.93           C  
ANISOU 6019  CD2 PHE B 429     4686   4804   4923   -487    207   -191       C  
ATOM   6020  CE1 PHE B 429      10.819  14.397  61.840  1.00 33.91           C  
ANISOU 6020  CE1 PHE B 429     4133   4325   4426   -453    139   -226       C  
ATOM   6021  CE2 PHE B 429      11.329  14.746  59.507  1.00 37.48           C  
ANISOU 6021  CE2 PHE B 429     4521   4837   4883   -458    210   -182       C  
ATOM   6022  CZ  PHE B 429      11.474  14.010  60.683  1.00 36.23           C  
ANISOU 6022  CZ  PHE B 429     4343   4690   4734   -438    173   -199       C  
ATOM   6023  N   MET B 430      10.705  19.918  59.776  1.00 39.45           N  
ANISOU 6023  N   MET B 430     5178   4768   5044   -737    130   -151       N  
ATOM   6024  CA  MET B 430      11.854  20.593  59.194  1.00 39.91           C  
ANISOU 6024  CA  MET B 430     5203   4860   5100   -871    113    -90       C  
ATOM   6025  C   MET B 430      12.724  21.245  60.273  1.00 41.43           C  
ANISOU 6025  C   MET B 430     5438   5024   5277  -1008     29    -78       C  
ATOM   6026  O   MET B 430      13.948  21.023  60.330  1.00 42.73           O  
ANISOU 6026  O   MET B 430     5479   5295   5460  -1106      1    -28       O  
ATOM   6027  CB  MET B 430      11.405  21.613  58.142  1.00 39.54           C  
ANISOU 6027  CB  MET B 430     5256   4738   5030   -888    137    -64       C  
ATOM   6028  CG  MET B 430      10.698  20.976  56.952  1.00 42.93           C  
ANISOU 6028  CG  MET B 430     5635   5210   5468   -773    209    -66       C  
ATOM   6029  SD  MET B 430      11.618  19.672  56.063  1.00 41.90           S  
ANISOU 6029  SD  MET B 430     5306   5253   5361   -747    263    -34       S  
ATOM   6030  CE  MET B 430      13.171  20.499  55.645  1.00 37.09           C  
ANISOU 6030  CE  MET B 430     4632   4716   4744   -920    254     57       C  
ATOM   6031  N   LYS B 431      12.095  22.036  61.136  1.00 41.84           N  
ANISOU 6031  N   LYS B 431     5665   4940   5290  -1010    -15   -120       N  
ATOM   6032  CA  LYS B 431      12.814  22.665  62.242  1.00 43.27           C  
ANISOU 6032  CA  LYS B 431     5925   5073   5441  -1139   -110   -120       C  
ATOM   6033  C   LYS B 431      13.545  21.595  63.068  1.00 43.37           C  
ANISOU 6033  C   LYS B 431     5793   5206   5480  -1145   -139   -120       C  
ATOM   6034  O   LYS B 431      14.726  21.754  63.439  1.00 47.44           O  
ANISOU 6034  O   LYS B 431     6244   5781   5999  -1287   -210    -74       O  
ATOM   6035  CB  LYS B 431      11.848  23.510  63.086  1.00 45.78           C  
ANISOU 6035  CB  LYS B 431     6475   5222   5698  -1089   -139   -182       C  
ATOM   6036  CG  LYS B 431      12.449  24.135  64.345  1.00 52.15           C  
ANISOU 6036  CG  LYS B 431     7407   5953   6454  -1207   -245   -198       C  
ATOM   6037  CD  LYS B 431      13.668  25.004  64.036  1.00 58.43           C  
ANISOU 6037  CD  LYS B 431     8215   6739   7245  -1427   -328   -129       C  
ATOM   6038  CE  LYS B 431      14.177  25.722  65.275  1.00 61.22           C  
ANISOU 6038  CE  LYS B 431     8730   6994   7536  -1557   -453   -148       C  
ATOM   6039  NZ  LYS B 431      15.578  26.164  65.042  1.00 62.73           N  
ANISOU 6039  NZ  LYS B 431     8845   7246   7742  -1795   -543    -60       N  
ATOM   6040  N   HIS B 432      12.861  20.491  63.319  1.00 37.87           N  
ANISOU 6040  N   HIS B 432     5038   4549   4801   -998    -89   -162       N  
ATOM   6041  CA  HIS B 432      13.450  19.390  64.049  1.00 39.99           C  
ANISOU 6041  CA  HIS B 432     5181   4921   5091   -981   -112   -161       C  
ATOM   6042  C   HIS B 432      14.676  18.823  63.378  1.00 42.56           C  
ANISOU 6042  C   HIS B 432     5313   5399   5461  -1031   -105    -95       C  
ATOM   6043  O   HIS B 432      15.718  18.649  64.035  1.00 44.72           O  
ANISOU 6043  O   HIS B 432     5504   5750   5739  -1113   -170    -62       O  
ATOM   6044  CB  HIS B 432      12.431  18.307  64.280  1.00 38.01           C  
ANISOU 6044  CB  HIS B 432     4914   4677   4851   -821    -57   -208       C  
ATOM   6045  CG  HIS B 432      12.980  17.111  64.997  1.00 39.90           C  
ANISOU 6045  CG  HIS B 432     5041   5008   5109   -791    -79   -205       C  
ATOM   6046  ND1 HIS B 432      13.338  17.146  66.298  1.00 39.93           N  
ANISOU 6046  ND1 HIS B 432     5087   5000   5084   -836   -152   -218       N  
ATOM   6047  CD2 HIS B 432      13.205  15.806  64.560  1.00 39.49           C  
ANISOU 6047  CD2 HIS B 432     4852   5055   5096   -708    -41   -192       C  
ATOM   6048  CE1 HIS B 432      13.770  15.924  66.674  1.00 40.18           C  
ANISOU 6048  CE1 HIS B 432     5003   5124   5140   -784   -158   -207       C  
ATOM   6049  NE2 HIS B 432      13.700  15.106  65.610  1.00 38.52           N  
ANISOU 6049  NE2 HIS B 432     4688   4978   4972   -703    -90   -192       N  
ATOM   6050  N   LEU B 433      14.573  18.564  62.070  1.00 41.42           N  
ANISOU 6050  N   LEU B 433     5095   5305   5339   -979    -27    -71       N  
ATOM   6051  CA  LEU B 433      15.693  18.047  61.272  1.00 42.43           C  
ANISOU 6051  CA  LEU B 433     5039   5587   5495  -1000      2     -4       C  
ATOM   6052  C   LEU B 433      16.936  18.904  61.445  1.00 44.40           C  
ANISOU 6052  C   LEU B 433     5236   5893   5740  -1183    -65     71       C  
ATOM   6053  O   LEU B 433      18.041  18.378  61.669  1.00 46.42           O  
ANISOU 6053  O   LEU B 433     5329   6293   6016  -1215    -88    124       O  
ATOM   6054  CB  LEU B 433      15.323  17.985  59.786  1.00 41.11           C  
ANISOU 6054  CB  LEU B 433     4852   5438   5330   -935     92     10       C  
ATOM   6055  CG  LEU B 433      14.475  16.785  59.402  1.00 45.00           C  
ANISOU 6055  CG  LEU B 433     5333   5934   5832   -764    153    -41       C  
ATOM   6056  CD1 LEU B 433      14.139  16.872  57.918  1.00 46.22           C  
ANISOU 6056  CD1 LEU B 433     5488   6097   5975   -719    227    -26       C  
ATOM   6057  CD2 LEU B 433      15.202  15.488  59.734  1.00 42.62           C  
ANISOU 6057  CD2 LEU B 433     4896   5747   5550   -691    156    -35       C  
ATOM   6058  N   ASP B 434      16.729  20.222  61.344  1.00 45.28           N  
ANISOU 6058  N   ASP B 434     5489   5891   5823  -1302   -101     80       N  
ATOM   6059  CA  ASP B 434      17.759  21.227  61.595  1.00 48.08           C  
ANISOU 6059  CA  ASP B 434     5844   6260   6165  -1512   -188    151       C  
ATOM   6060  C   ASP B 434      18.322  21.131  63.027  1.00 48.33           C  
ANISOU 6060  C   ASP B 434     5876   6301   6187  -1589   -298    143       C  
ATOM   6061  O   ASP B 434      19.557  21.052  63.204  1.00 50.55           O  
ANISOU 6061  O   ASP B 434     6002   6720   6484  -1707   -352    222       O  
ATOM   6062  CB  ASP B 434      17.243  22.647  61.296  1.00 50.33           C  
ANISOU 6062  CB  ASP B 434     6338   6375   6411  -1610   -214    149       C  
ATOM   6063  CG  ASP B 434      18.362  23.673  61.238  1.00 57.21           C  
ANISOU 6063  CG  ASP B 434     7202   7267   7269  -1851   -299    243       C  
ATOM   6064  OD1 ASP B 434      19.304  23.515  60.429  1.00 60.09           O  
ANISOU 6064  OD1 ASP B 434     7378   7794   7659  -1922   -265    340       O  
ATOM   6065  OD2 ASP B 434      18.322  24.656  62.005  1.00 65.78           O  
ANISOU 6065  OD2 ASP B 434     8473   8207   8312  -1976   -402    227       O  
ATOM   6066  N   ASN B 435      17.454  21.134  64.043  1.00 44.26           N  
ANISOU 6066  N   ASN B 435     5523   5653   5640  -1521   -331     56       N  
ATOM   6067  CA  ASN B 435      17.956  20.982  65.418  1.00 46.60           C  
ANISOU 6067  CA  ASN B 435     5831   5959   5915  -1583   -436     44       C  
ATOM   6068  C   ASN B 435      18.812  19.717  65.515  1.00 47.54           C  
ANISOU 6068  C   ASN B 435     5710   6272   6080  -1529   -425     87       C  
ATOM   6069  O   ASN B 435      19.886  19.736  66.110  1.00 46.95           O  
ANISOU 6069  O   ASN B 435     5540   6292   6007  -1647   -516    144       O  
ATOM   6070  CB  ASN B 435      16.824  20.901  66.462  1.00 45.42           C  
ANISOU 6070  CB  ASN B 435     5869   5669   5721  -1472   -444    -56       C  
ATOM   6071  CG  ASN B 435      15.957  22.146  66.493  1.00 45.93           C  
ANISOU 6071  CG  ASN B 435     6185   5539   5728  -1494   -454   -103       C  
ATOM   6072  OD1 ASN B 435      16.393  23.219  66.112  1.00 46.65           O  
ANISOU 6072  OD1 ASN B 435     6352   5571   5800  -1642   -504    -63       O  
ATOM   6073  ND2 ASN B 435      14.712  21.996  66.917  1.00 45.65           N  
ANISOU 6073  ND2 ASN B 435     6278   5407   5661  -1340   -404   -181       N  
ATOM   6074  N   GLU B 436      18.337  18.625  64.902  1.00 45.77           N  
ANISOU 6074  N   GLU B 436     5395   6105   5888  -1348   -319     65       N  
ATOM   6075  CA  GLU B 436      18.996  17.340  65.069  1.00 45.44           C  
ANISOU 6075  CA  GLU B 436     5167   6218   5880  -1256   -305     91       C  
ATOM   6076  C   GLU B 436      20.307  17.251  64.316  1.00 45.92           C  
ANISOU 6076  C   GLU B 436     5011   6467   5971  -1320   -294    195       C  
ATOM   6077  O   GLU B 436      21.228  16.597  64.782  1.00 44.25           O  
ANISOU 6077  O   GLU B 436     4645   6394   5774  -1313   -333    243       O  
ATOM   6078  CB  GLU B 436      18.058  16.188  64.721  1.00 47.33           C  
ANISOU 6078  CB  GLU B 436     5411   6439   6135  -1051   -211     31       C  
ATOM   6079  CG  GLU B 436      16.941  16.028  65.734  1.00 48.30           C  
ANISOU 6079  CG  GLU B 436     5696   6427   6228   -986   -230    -51       C  
ATOM   6080  CD  GLU B 436      17.466  15.550  67.067  1.00 53.31           C  
ANISOU 6080  CD  GLU B 436     6310   7099   6848  -1002   -316    -50       C  
ATOM   6081  OE1 GLU B 436      17.772  14.348  67.160  1.00 57.17           O  
ANISOU 6081  OE1 GLU B 436     6686   7676   7360   -898   -299    -38       O  
ATOM   6082  OE2 GLU B 436      17.600  16.367  68.014  1.00 57.92           O  
ANISOU 6082  OE2 GLU B 436     6998   7617   7390  -1116   -406    -59       O  
ATOM   6083  N   GLN B 437      20.383  17.915  63.158  1.00 47.32           N  
ANISOU 6083  N   GLN B 437     5173   6655   6151  -1376   -237    238       N  
ATOM   6084  CA  GLN B 437      21.620  18.015  62.401  1.00 49.28           C  
ANISOU 6084  CA  GLN B 437     5216   7090   6417  -1457   -218    352       C  
ATOM   6085  C   GLN B 437      22.736  18.654  63.255  1.00 53.39           C  
ANISOU 6085  C   GLN B 437     5665   7686   6934  -1667   -351    432       C  
ATOM   6086  O   GLN B 437      23.832  18.095  63.377  1.00 55.10           O  
ANISOU 6086  O   GLN B 437     5664   8099   7173  -1671   -368    513       O  
ATOM   6087  CB  GLN B 437      21.389  18.783  61.096  1.00 50.39           C  
ANISOU 6087  CB  GLN B 437     5394   7204   6549  -1504   -143    384       C  
ATOM   6088  CG  GLN B 437      22.530  18.674  60.079  1.00 49.57           C  
ANISOU 6088  CG  GLN B 437     5062   7315   6456  -1536    -80    503       C  
ATOM   6089  CD  GLN B 437      22.724  17.248  59.581  1.00 51.89           C  
ANISOU 6089  CD  GLN B 437     5204   7750   6764  -1310     23    496       C  
ATOM   6090  OE1 GLN B 437      21.750  16.470  59.433  1.00 49.25           O  
ANISOU 6090  OE1 GLN B 437     4968   7320   6425  -1130     78    400       O  
ATOM   6091  NE2 GLN B 437      23.984  16.873  59.356  1.00 48.50           N  
ANISOU 6091  NE2 GLN B 437     4536   7548   6344  -1314     43    601       N  
ATOM   6092  N   LYS B 438      22.437  19.782  63.891  1.00 56.28           N  
ANISOU 6092  N   LYS B 438     6222   7894   7269  -1830   -451    408       N  
ATOM   6093  CA  LYS B 438      23.404  20.458  64.754  1.00 57.59           C  
ANISOU 6093  CA  LYS B 438     6363   8100   7420  -2052   -600    476       C  
ATOM   6094  C   LYS B 438      23.740  19.614  65.981  1.00 57.53           C  
ANISOU 6094  C   LYS B 438     6293   8154   7413  -1996   -676    455       C  
ATOM   6095  O   LYS B 438      24.915  19.522  66.381  1.00 54.75           O  
ANISOU 6095  O   LYS B 438     5762   7967   7072  -2107   -761    549       O  
ATOM   6096  CB  LYS B 438      22.883  21.835  65.178  1.00 61.37           C  
ANISOU 6096  CB  LYS B 438     7116   8356   7847  -2219   -692    435       C  
ATOM   6097  CG  LYS B 438      22.924  22.884  64.074  1.00 66.65           C  
ANISOU 6097  CG  LYS B 438     7833   8982   8510  -2348   -661    495       C  
ATOM   6098  CD  LYS B 438      21.894  23.991  64.291  1.00 71.69           C  
ANISOU 6098  CD  LYS B 438     8797   9349   9094  -2391   -699    412       C  
ATOM   6099  CE  LYS B 438      21.860  24.943  63.095  1.00 78.24           C  
ANISOU 6099  CE  LYS B 438     9681  10129   9917  -2492   -657    473       C  
ATOM   6100  NZ  LYS B 438      20.728  25.916  63.159  1.00 80.78           N  
ANISOU 6100  NZ  LYS B 438    10322  10186  10186  -2475   -670    388       N  
ATOM   6101  N   ALA B 439      22.717  18.999  66.566  1.00 51.01           N  
ANISOU 6101  N   ALA B 439     5605   7206   6572  -1827   -647    342       N  
ATOM   6102  CA  ALA B 439      22.886  18.256  67.825  1.00 54.27           C  
ANISOU 6102  CA  ALA B 439     6004   7644   6972  -1774   -724    314       C  
ATOM   6103  C   ALA B 439      23.567  16.895  67.678  1.00 54.86           C  
ANISOU 6103  C   ALA B 439     5835   7919   7090  -1624   -676    363       C  
ATOM   6104  O   ALA B 439      24.293  16.477  68.578  1.00 58.13           O  
ANISOU 6104  O   ALA B 439     6159   8429   7501  -1648   -769    399       O  
ATOM   6105  CB  ALA B 439      21.549  18.084  68.559  1.00 51.80           C  
ANISOU 6105  CB  ALA B 439     5924   7138   6620  -1653   -707    188       C  
ATOM   6106  N   ARG B 440      23.337  16.200  66.567  1.00 52.91           N  
ANISOU 6106  N   ARG B 440     5497   7731   6876  -1463   -538    362       N  
ATOM   6107  CA  ARG B 440      23.721  14.779  66.466  1.00 51.02           C  
ANISOU 6107  CA  ARG B 440     5091   7632   6663  -1267   -481    379       C  
ATOM   6108  C   ARG B 440      24.344  14.436  65.129  1.00 50.15           C  
ANISOU 6108  C   ARG B 440     4788   7687   6580  -1191   -370    453       C  
ATOM   6109  O   ARG B 440      24.906  13.353  64.969  1.00 51.73           O  
ANISOU 6109  O   ARG B 440     4831   8029   6794  -1034   -326    486       O  
ATOM   6110  CB  ARG B 440      22.501  13.848  66.741  1.00 49.41           C  
ANISOU 6110  CB  ARG B 440     5035   7288   6450  -1074   -424    268       C  
ATOM   6111  CG  ARG B 440      22.285  13.548  68.223  1.00 47.99           C  
ANISOU 6111  CG  ARG B 440     4952   7039   6242  -1075   -524    225       C  
ATOM   6112  CD  ARG B 440      21.617  12.221  68.505  1.00 46.14           C  
ANISOU 6112  CD  ARG B 440     4760   6763   6009   -872   -475    166       C  
ATOM   6113  NE  ARG B 440      20.337  12.045  67.793  1.00 44.38           N  
ANISOU 6113  NE  ARG B 440     4665   6410   5787   -773   -371     92       N  
ATOM   6114  CZ  ARG B 440      19.517  11.001  67.967  1.00 41.42           C  
ANISOU 6114  CZ  ARG B 440     4362   5966   5409   -624   -329     37       C  
ATOM   6115  NH1 ARG B 440      19.817  10.054  68.842  1.00 38.19           N  
ANISOU 6115  NH1 ARG B 440     3926   5591   4992   -550   -377     45       N  
ATOM   6116  NH2 ARG B 440      18.369  10.902  67.284  1.00 43.01           N  
ANISOU 6116  NH2 ARG B 440     4666   6063   5612   -557   -246    -19       N  
ATOM   6117  N   GLY B 441      24.246  15.352  64.171  1.00 47.53           N  
ANISOU 6117  N   GLY B 441     4478   7335   6246  -1292   -322    479       N  
ATOM   6118  CA  GLY B 441      24.823  15.140  62.851  1.00 47.44           C  
ANISOU 6118  CA  GLY B 441     4296   7483   6247  -1230   -208    554       C  
ATOM   6119  C   GLY B 441      23.935  14.319  61.927  1.00 49.79           C  
ANISOU 6119  C   GLY B 441     4666   7715   6539  -1011    -75    476       C  
ATOM   6120  O   GLY B 441      24.430  13.729  60.957  1.00 52.34           O  
ANISOU 6120  O   GLY B 441     4849   8179   6859   -888     27    522       O  
ATOM   6121  N   GLY B 442      22.626  14.282  62.213  1.00 46.51           N  
ANISOU 6121  N   GLY B 442     4469   7090   6113   -962    -76    363       N  
ATOM   6122  CA  GLY B 442      21.681  13.539  61.397  1.00 46.60           C  
ANISOU 6122  CA  GLY B 442     4565   7023   6116   -781     28    290       C  
ATOM   6123  C   GLY B 442      20.356  13.285  62.086  1.00 43.19           C  
ANISOU 6123  C   GLY B 442     4334   6398   5679   -727      2    182       C  
ATOM   6124  O   GLY B 442      20.206  13.534  63.281  1.00 43.93           O  
ANISOU 6124  O   GLY B 442     4497   6424   5769   -799    -88    158       O  
ATOM   6125  N   CYS B 443      19.378  12.799  61.331  1.00 42.41           N  
ANISOU 6125  N   CYS B 443     4327   6215   5573   -604     79    121       N  
ATOM   6126  CA  CYS B 443      18.080  12.390  61.921  1.00 39.33           C  
ANISOU 6126  CA  CYS B 443     4099   5667   5177   -540     64     32       C  
ATOM   6127  C   CYS B 443      17.513  11.228  61.134  1.00 39.08           C  
ANISOU 6127  C   CYS B 443     4090   5617   5140   -369    137     -8       C  
ATOM   6128  O   CYS B 443      17.279  11.360  59.926  1.00 39.52           O  
ANISOU 6128  O   CYS B 443     4156   5676   5184   -337    206     -7       O  
ATOM   6129  CB  CYS B 443      17.062  13.528  61.972  1.00 35.16           C  
ANISOU 6129  CB  CYS B 443     3727   4995   4637   -634     51     -7       C  
ATOM   6130  SG  CYS B 443      15.391  12.984  62.545  1.00 45.76           S  
ANISOU 6130  SG  CYS B 443     5236   6181   5970   -538     54    -98       S  
ATOM   6131  N   PRO B 444      17.313  10.076  61.793  1.00 39.92           N  
ANISOU 6131  N   PRO B 444     4218   5702   5248   -264    115    -40       N  
ATOM   6132  CA  PRO B 444      16.669   8.975  61.069  1.00 39.21           C  
ANISOU 6132  CA  PRO B 444     4187   5566   5146   -119    167    -82       C  
ATOM   6133  C   PRO B 444      15.210   9.311  60.756  1.00 39.81           C  
ANISOU 6133  C   PRO B 444     4405   5505   5216   -143    181   -135       C  
ATOM   6134  O   PRO B 444      14.433   9.684  61.653  1.00 39.78           O  
ANISOU 6134  O   PRO B 444     4481   5417   5217   -202    138   -161       O  
ATOM   6135  CB  PRO B 444      16.788   7.789  62.042  1.00 39.03           C  
ANISOU 6135  CB  PRO B 444     4172   5533   5125    -30    121    -95       C  
ATOM   6136  CG  PRO B 444      17.006   8.394  63.389  1.00 36.97           C  
ANISOU 6136  CG  PRO B 444     3901   5272   4874   -141     43    -80       C  
ATOM   6137  CD  PRO B 444      17.774   9.662  63.134  1.00 38.92           C  
ANISOU 6137  CD  PRO B 444     4062   5599   5128   -270     38    -30       C  
ATOM   6138  N   ALA B 445      14.855   9.207  59.473  1.00 40.70           N  
ANISOU 6138  N   ALA B 445     4544   5607   5312    -92    241   -146       N  
ATOM   6139  CA  ALA B 445      13.524   9.551  59.024  1.00 38.91           C  
ANISOU 6139  CA  ALA B 445     4431   5274   5079   -112    252   -183       C  
ATOM   6140  C   ALA B 445      13.073   8.642  57.870  1.00 40.45           C  
ANISOU 6140  C   ALA B 445     4678   5446   5247     -6    292   -209       C  
ATOM   6141  O   ALA B 445      13.859   8.271  57.007  1.00 37.21           O  
ANISOU 6141  O   ALA B 445     4217   5109   4811     66    339   -193       O  
ATOM   6142  CB  ALA B 445      13.465  11.011  58.626  1.00 38.84           C  
ANISOU 6142  CB  ALA B 445     4428   5260   5069   -219    266   -161       C  
ATOM   6143  N   ASP B 446      11.790   8.278  57.900  1.00 38.46           N  
ANISOU 6143  N   ASP B 446     4526   5093   4992      2    270   -246       N  
ATOM   6144  CA  ASP B 446      11.204   7.366  56.958  1.00 37.90           C  
ANISOU 6144  CA  ASP B 446     4531   4978   4892     79    281   -274       C  
ATOM   6145  C   ASP B 446      10.264   8.215  56.102  1.00 37.38           C  
ANISOU 6145  C   ASP B 446     4513   4873   4816     29    297   -277       C  
ATOM   6146  O   ASP B 446       9.116   8.543  56.501  1.00 35.16           O  
ANISOU 6146  O   ASP B 446     4279   4530   4550    -20    267   -285       O  
ATOM   6147  CB  ASP B 446      10.488   6.232  57.712  1.00 39.41           C  
ANISOU 6147  CB  ASP B 446     4792   5093   5088    107    227   -298       C  
ATOM   6148  CG  ASP B 446      10.015   5.085  56.794  1.00 41.56           C  
ANISOU 6148  CG  ASP B 446     5164   5306   5322    182    218   -327       C  
ATOM   6149  OD1 ASP B 446       9.607   5.327  55.638  1.00 41.91           O  
ANISOU 6149  OD1 ASP B 446     5249   5337   5337    186    240   -337       O  
ATOM   6150  OD2 ASP B 446      10.038   3.916  57.249  1.00 49.25           O  
ANISOU 6150  OD2 ASP B 446     6191   6235   6288    235    180   -339       O  
ATOM   6151  N   TRP B 447      10.778   8.577  54.923  1.00 38.82           N  
ANISOU 6151  N   TRP B 447     4679   5105   4967     51    348   -264       N  
ATOM   6152  CA  TRP B 447      10.139   9.524  54.012  1.00 36.57           C  
ANISOU 6152  CA  TRP B 447     4431   4799   4666      6    368   -255       C  
ATOM   6153  C   TRP B 447       8.697   9.168  53.709  1.00 37.24           C  
ANISOU 6153  C   TRP B 447     4609   4800   4742     10    329   -282       C  
ATOM   6154  O   TRP B 447       7.819  10.003  53.755  1.00 41.10           O  
ANISOU 6154  O   TRP B 447     5118   5253   5244    -43    316   -272       O  
ATOM   6155  CB  TRP B 447      10.966   9.591  52.740  1.00 40.35           C  
ANISOU 6155  CB  TRP B 447     4888   5349   5097     52    431   -237       C  
ATOM   6156  CG  TRP B 447      10.573  10.707  51.786  1.00 41.27           C  
ANISOU 6156  CG  TRP B 447     5033   5458   5190     -1    457   -213       C  
ATOM   6157  CD1 TRP B 447      11.161  11.970  51.650  1.00 41.21           C  
ANISOU 6157  CD1 TRP B 447     4974   5495   5188    -83    488   -163       C  
ATOM   6158  CD2 TRP B 447       9.493  10.691  50.819  1.00 41.21           C  
ANISOU 6158  CD2 TRP B 447     5121   5391   5147     15    445   -231       C  
ATOM   6159  NE1 TRP B 447      10.524  12.712  50.695  1.00 40.49           N  
ANISOU 6159  NE1 TRP B 447     4948   5370   5068   -107    500   -151       N  
ATOM   6160  CE2 TRP B 447       9.526  11.996  50.141  1.00 44.13           C  
ANISOU 6160  CE2 TRP B 447     5490   5774   5501    -46    477   -190       C  
ATOM   6161  CE3 TRP B 447       8.532   9.768  50.455  1.00 41.45           C  
ANISOU 6161  CE3 TRP B 447     5237   5358   5154     60    403   -270       C  
ATOM   6162  CZ2 TRP B 447       8.616  12.329  49.155  1.00 42.98           C  
ANISOU 6162  CZ2 TRP B 447     5424   5587   5319    -43    468   -190       C  
ATOM   6163  CZ3 TRP B 447       7.626  10.108  49.452  1.00 42.29           C  
ANISOU 6163  CZ3 TRP B 447     5415   5428   5224     51    389   -268       C  
ATOM   6164  CH2 TRP B 447       7.673  11.357  48.811  1.00 45.44           C  
ANISOU 6164  CH2 TRP B 447     5808   5848   5608      8    424   -230       C  
ATOM   6165  N   ALA B 448       8.436   7.904  53.418  1.00 39.24           N  
ANISOU 6165  N   ALA B 448     4921   5019   4970     73    304   -310       N  
ATOM   6166  CA  ALA B 448       7.105   7.462  53.024  1.00 38.90           C  
ANISOU 6166  CA  ALA B 448     4962   4905   4913     60    254   -325       C  
ATOM   6167  C   ALA B 448       6.115   7.628  54.150  1.00 39.08           C  
ANISOU 6167  C   ALA B 448     4970   4895   4983     -2    211   -314       C  
ATOM   6168  O   ALA B 448       4.934   7.676  53.886  1.00 42.03           O  
ANISOU 6168  O   ALA B 448     5376   5238   5355    -34    176   -305       O  
ATOM   6169  CB  ALA B 448       7.151   6.010  52.589  1.00 37.87           C  
ANISOU 6169  CB  ALA B 448     4918   4731   4740    129    224   -358       C  
ATOM   6170  N   TRP B 449       6.593   7.704  55.402  1.00 38.53           N  
ANISOU 6170  N   TRP B 449     4849   4842   4949    -16    212   -308       N  
ATOM   6171  CA  TRP B 449       5.706   7.928  56.581  1.00 36.65           C  
ANISOU 6171  CA  TRP B 449     4598   4583   4744    -65    184   -294       C  
ATOM   6172  C   TRP B 449       5.652   9.346  57.026  1.00 35.21           C  
ANISOU 6172  C   TRP B 449     4384   4418   4578   -103    210   -278       C  
ATOM   6173  O   TRP B 449       4.661   9.770  57.603  1.00 35.65           O  
ANISOU 6173  O   TRP B 449     4444   4459   4644   -124    201   -265       O  
ATOM   6174  CB  TRP B 449       6.108   7.074  57.775  1.00 36.46           C  
ANISOU 6174  CB  TRP B 449     4565   4554   4735    -56    159   -297       C  
ATOM   6175  CG  TRP B 449       5.610   5.656  57.681  1.00 39.66           C  
ANISOU 6175  CG  TRP B 449     5034   4910   5127    -40    110   -304       C  
ATOM   6176  CD1 TRP B 449       5.902   4.726  56.696  1.00 39.92           C  
ANISOU 6176  CD1 TRP B 449     5133   4910   5123     12     96   -327       C  
ATOM   6177  CD2 TRP B 449       4.710   4.965  58.607  1.00 38.32           C  
ANISOU 6177  CD2 TRP B 449     4884   4707   4968    -80     64   -284       C  
ATOM   6178  NE1 TRP B 449       5.244   3.554  56.929  1.00 42.37           N  
ANISOU 6178  NE1 TRP B 449     5517   5156   5425     -3     34   -325       N  
ATOM   6179  CE2 TRP B 449       4.511   3.621  58.053  1.00 40.09           C  
ANISOU 6179  CE2 TRP B 449     5197   4870   5167    -65     13   -294       C  
ATOM   6180  CE3 TRP B 449       4.070   5.308  59.793  1.00 40.39           C  
ANISOU 6180  CE3 TRP B 449     5111   4985   5251   -123     62   -256       C  
ATOM   6181  CZ2 TRP B 449       3.714   2.658  58.692  1.00 42.40           C  
ANISOU 6181  CZ2 TRP B 449     5533   5115   5460   -114    -46   -268       C  
ATOM   6182  CZ3 TRP B 449       3.245   4.336  60.427  1.00 45.68           C  
ANISOU 6182  CZ3 TRP B 449     5810   5627   5921   -162     16   -227       C  
ATOM   6183  CH2 TRP B 449       3.081   3.034  59.888  1.00 40.75           C  
ANISOU 6183  CH2 TRP B 449     5264   4940   5277   -167    -41   -229       C  
ATOM   6184  N   ILE B 450       6.714  10.099  56.762  1.00 32.56           N  
ANISOU 6184  N   ILE B 450     4019   4114   4238   -111    244   -275       N  
ATOM   6185  CA  ILE B 450       6.746  11.469  57.197  1.00 33.80           C  
ANISOU 6185  CA  ILE B 450     4174   4266   4403   -159    257   -261       C  
ATOM   6186  C   ILE B 450       5.908  12.347  56.272  1.00 34.06           C  
ANISOU 6186  C   ILE B 450     4246   4274   4421   -161    271   -248       C  
ATOM   6187  O   ILE B 450       5.303  13.293  56.725  1.00 33.94           O  
ANISOU 6187  O   ILE B 450     4261   4229   4408   -175    271   -240       O  
ATOM   6188  CB  ILE B 450       8.212  11.998  57.242  1.00 37.74           C  
ANISOU 6188  CB  ILE B 450     4627   4811   4903   -194    275   -248       C  
ATOM   6189  CG1 ILE B 450       9.024  11.212  58.296  1.00 39.22           C  
ANISOU 6189  CG1 ILE B 450     4766   5031   5106   -186    252   -253       C  
ATOM   6190  CG2 ILE B 450       8.247  13.512  57.473  1.00 32.16           C  
ANISOU 6190  CG2 ILE B 450     3950   4076   4194   -260    278   -232       C  
ATOM   6191  CD1 ILE B 450       8.624  11.457  59.755  1.00 39.63           C  
ANISOU 6191  CD1 ILE B 450     4842   5049   5167   -216    218   -261       C  
ATOM   6192  N   VAL B 451       5.917  12.058  54.967  1.00 33.56           N  
ANISOU 6192  N   VAL B 451     4195   4223   4335   -139    283   -246       N  
ATOM   6193  CA  VAL B 451       5.177  12.849  54.010  1.00 32.00           C  
ANISOU 6193  CA  VAL B 451     4037   4006   4116   -138    291   -229       C  
ATOM   6194  C   VAL B 451       3.695  12.537  54.177  1.00 32.56           C  
ANISOU 6194  C   VAL B 451     4122   4055   4193   -119    255   -225       C  
ATOM   6195  O   VAL B 451       3.313  11.393  54.267  1.00 36.76           O  
ANISOU 6195  O   VAL B 451     4649   4590   4729   -109    224   -234       O  
ATOM   6196  CB  VAL B 451       5.623  12.530  52.569  1.00 33.04           C  
ANISOU 6196  CB  VAL B 451     4184   4162   4208   -116    311   -228       C  
ATOM   6197  CG1 VAL B 451       4.666  13.145  51.559  1.00 30.65           C  
ANISOU 6197  CG1 VAL B 451     3930   3837   3878   -110    303   -208       C  
ATOM   6198  CG2 VAL B 451       7.076  12.955  52.352  1.00 32.26           C  
ANISOU 6198  CG2 VAL B 451     4047   4111   4100   -137    358   -212       C  
ATOM   6199  N   PRO B 452       2.861  13.564  54.273  1.00 34.36           N  
ANISOU 6199  N   PRO B 452     4369   4265   4422   -114    258   -203       N  
ATOM   6200  CA  PRO B 452       1.451  13.270  54.498  1.00 33.97           C  
ANISOU 6200  CA  PRO B 452     4304   4224   4379    -91    229   -184       C  
ATOM   6201  C   PRO B 452       0.731  12.564  53.333  1.00 35.97           C  
ANISOU 6201  C   PRO B 452     4562   4491   4613    -88    189   -171       C  
ATOM   6202  O   PRO B 452       1.148  12.648  52.180  1.00 37.63           O  
ANISOU 6202  O   PRO B 452     4808   4696   4793    -87    193   -176       O  
ATOM   6203  CB  PRO B 452       0.836  14.633  54.805  1.00 32.86           C  
ANISOU 6203  CB  PRO B 452     4187   4064   4233    -60    249   -162       C  
ATOM   6204  CG  PRO B 452       1.879  15.652  54.552  1.00 35.31           C  
ANISOU 6204  CG  PRO B 452     4548   4337   4531    -83    277   -170       C  
ATOM   6205  CD  PRO B 452       3.212  14.985  54.490  1.00 34.60           C  
ANISOU 6205  CD  PRO B 452     4434   4265   4447   -128    284   -193       C  
ATOM   6206  N   PRO B 453      -0.386  11.892  53.640  1.00 37.65           N  
ANISOU 6206  N   PRO B 453     4741   4728   4838    -95    148   -147       N  
ATOM   6207  CA  PRO B 453      -1.187  11.137  52.658  1.00 36.43           C  
ANISOU 6207  CA  PRO B 453     4593   4585   4662   -115     87   -129       C  
ATOM   6208  C   PRO B 453      -2.036  11.982  51.678  1.00 40.25           C  
ANISOU 6208  C   PRO B 453     5080   5089   5125    -93     72    -91       C  
ATOM   6209  O   PRO B 453      -2.642  11.428  50.751  1.00 40.90           O  
ANISOU 6209  O   PRO B 453     5176   5182   5182   -117     11    -74       O  
ATOM   6210  CB  PRO B 453      -2.076  10.261  53.543  1.00 35.97           C  
ANISOU 6210  CB  PRO B 453     4482   4556   4629   -149     47    -99       C  
ATOM   6211  CG  PRO B 453      -2.186  11.003  54.829  1.00 35.40           C  
ANISOU 6211  CG  PRO B 453     4364   4505   4582   -117    100    -87       C  
ATOM   6212  CD  PRO B 453      -0.951  11.829  55.003  1.00 34.71           C  
ANISOU 6212  CD  PRO B 453     4320   4377   4491    -91    155   -130       C  
ATOM   6213  N   ILE B 454      -2.101  13.295  51.884  1.00 39.40           N  
ANISOU 6213  N   ILE B 454     4970   4979   5020    -47    117    -75       N  
ATOM   6214  CA  ILE B 454      -2.619  14.209  50.865  1.00 40.49           C  
ANISOU 6214  CA  ILE B 454     5134   5121   5131    -13    110    -43       C  
ATOM   6215  C   ILE B 454      -1.633  15.359  50.866  1.00 39.25           C  
ANISOU 6215  C   ILE B 454     5037   4912   4963      6    169    -62       C  
ATOM   6216  O   ILE B 454      -1.068  15.628  51.908  1.00 38.04           O  
ANISOU 6216  O   ILE B 454     4883   4737   4832      4    206    -83       O  
ATOM   6217  CB  ILE B 454      -4.026  14.788  51.184  1.00 38.84           C  
ANISOU 6217  CB  ILE B 454     4864   4963   4931     41     96     17       C  
ATOM   6218  CG1 ILE B 454      -4.095  15.371  52.600  1.00 41.27           C  
ANISOU 6218  CG1 ILE B 454     5148   5270   5262     88    151     16       C  
ATOM   6219  CG2 ILE B 454      -5.129  13.755  51.001  1.00 43.19           C  
ANISOU 6219  CG2 ILE B 454     5339   5583   5489      1     23     60       C  
ATOM   6220  CD1 ILE B 454      -5.374  16.137  52.893  1.00 41.24           C  
ANISOU 6220  CD1 ILE B 454     5094   5320   5255    178    160     76       C  
ATOM   6221  N   SER B 455      -1.448  16.011  49.715  1.00 38.22           N  
ANISOU 6221  N   SER B 455     4964   4762   4795     14    171    -49       N  
ATOM   6222  CA  SER B 455      -0.753  17.291  49.585  1.00 38.86           C  
ANISOU 6222  CA  SER B 455     5111   4792   4861     21    216    -44       C  
ATOM   6223  C   SER B 455       0.720  17.136  49.855  1.00 38.84           C  
ANISOU 6223  C   SER B 455     5120   4773   4864    -35    255    -79       C  
ATOM   6224  O   SER B 455       1.365  18.063  50.359  1.00 39.05           O  
ANISOU 6224  O   SER B 455     5184   4758   4896    -54    286    -78       O  
ATOM   6225  CB  SER B 455      -1.311  18.356  50.530  1.00 41.14           C  
ANISOU 6225  CB  SER B 455     5418   5050   5165     76    234    -27       C  
ATOM   6226  OG  SER B 455      -2.680  18.636  50.249  1.00 49.64           O  
ANISOU 6226  OG  SER B 455     6470   6157   6233    149    205     18       O  
ATOM   6227  N   GLY B 456       1.252  15.987  49.484  1.00 33.76           N  
ANISOU 6227  N   GLY B 456     4452   4163   4214    -59    250   -104       N  
ATOM   6228  CA  GLY B 456       2.632  15.668  49.783  1.00 32.91           C  
ANISOU 6228  CA  GLY B 456     4328   4064   4111    -95    288   -130       C  
ATOM   6229  C   GLY B 456       3.564  16.784  49.385  1.00 32.15           C  
ANISOU 6229  C   GLY B 456     4267   3952   3995   -130    330   -106       C  
ATOM   6230  O   GLY B 456       4.204  17.389  50.249  1.00 30.70           O  
ANISOU 6230  O   GLY B 456     4079   3749   3836   -169    347   -105       O  
ATOM   6231  N   SER B 457       3.592  17.080  48.087  1.00 34.20           N  
ANISOU 6231  N   SER B 457     4569   4218   4205   -126    340    -81       N  
ATOM   6232  CA  SER B 457       4.510  18.055  47.529  1.00 36.41           C  
ANISOU 6232  CA  SER B 457     4883   4494   4456   -173    383    -44       C  
ATOM   6233  C   SER B 457       4.182  19.494  47.883  1.00 37.18           C  
ANISOU 6233  C   SER B 457     5048   4518   4561   -195    374    -12       C  
ATOM   6234  O   SER B 457       4.978  20.376  47.681  1.00 40.32           O  
ANISOU 6234  O   SER B 457     5481   4895   4942   -258    398     23       O  
ATOM   6235  CB  SER B 457       4.672  17.870  46.024  1.00 37.79           C  
ANISOU 6235  CB  SER B 457     5092   4704   4563   -158    402    -24       C  
ATOM   6236  OG  SER B 457       3.605  18.472  45.345  1.00 39.65           O  
ANISOU 6236  OG  SER B 457     5394   4901   4770   -129    368      3       O  
ATOM   6237  N   LEU B 458       3.010  19.706  48.444  1.00 40.38           N  
ANISOU 6237  N   LEU B 458     5472   4883   4987   -139    338    -20       N  
ATOM   6238  CA  LEU B 458       2.648  20.982  49.014  1.00 40.05           C  
ANISOU 6238  CA  LEU B 458     5508   4760   4948   -130    330     -1       C  
ATOM   6239  C   LEU B 458       3.279  21.223  50.385  1.00 41.42           C  
ANISOU 6239  C   LEU B 458     5682   4902   5155   -175    334    -27       C  
ATOM   6240  O   LEU B 458       3.114  22.304  50.936  1.00 43.67           O  
ANISOU 6240  O   LEU B 458     6058   5102   5431   -172    325    -20       O  
ATOM   6241  CB  LEU B 458       1.127  21.016  49.176  1.00 41.72           C  
ANISOU 6241  CB  LEU B 458     5722   4965   5165    -30    299      3       C  
ATOM   6242  CG  LEU B 458       0.299  21.385  47.949  1.00 42.22           C  
ANISOU 6242  CG  LEU B 458     5825   5030   5188     21    277     46       C  
ATOM   6243  CD1 LEU B 458       0.989  21.060  46.623  1.00 39.90           C  
ANISOU 6243  CD1 LEU B 458     5540   4768   4851    -29    288     60       C  
ATOM   6244  CD2 LEU B 458      -1.109  20.845  48.047  1.00 37.34           C  
ANISOU 6244  CD2 LEU B 458     5143   4462   4583    104    239     53       C  
ATOM   6245  N   THR B 459       3.944  20.216  50.959  1.00 36.84           N  
ANISOU 6245  N   THR B 459     5014   4381   4604   -207    342    -59       N  
ATOM   6246  CA  THR B 459       4.536  20.374  52.286  1.00 36.61           C  
ANISOU 6246  CA  THR B 459     4982   4328   4601   -250    336    -82       C  
ATOM   6247  C   THR B 459       6.065  20.306  52.144  1.00 36.75           C  
ANISOU 6247  C   THR B 459     4955   4389   4620   -352    352    -66       C  
ATOM   6248  O   THR B 459       6.577  19.741  51.172  1.00 32.75           O  
ANISOU 6248  O   THR B 459     4392   3951   4099   -359    380    -50       O  
ATOM   6249  CB  THR B 459       4.061  19.281  53.263  1.00 38.74           C  
ANISOU 6249  CB  THR B 459     5180   4637   4903   -203    325   -122       C  
ATOM   6250  OG1 THR B 459       4.582  18.017  52.831  1.00 38.69           O  
ANISOU 6250  OG1 THR B 459     5086   4707   4907   -212    333   -134       O  
ATOM   6251  CG2 THR B 459       2.518  19.214  53.361  1.00 34.88           C  
ANISOU 6251  CG2 THR B 459     4699   4142   4413   -107    313   -121       C  
ATOM   6252  N   PRO B 460       6.800  20.899  53.092  1.00 38.31           N  
ANISOU 6252  N   PRO B 460     5178   4552   4828   -429    334    -66       N  
ATOM   6253  CA  PRO B 460       8.247  21.003  52.821  1.00 36.37           C  
ANISOU 6253  CA  PRO B 460     4876   4363   4580   -539    346    -28       C  
ATOM   6254  C   PRO B 460       8.975  19.679  52.880  1.00 37.50           C  
ANISOU 6254  C   PRO B 460     4880   4622   4745   -524    367    -41       C  
ATOM   6255  O   PRO B 460      10.010  19.535  52.243  1.00 36.29           O  
ANISOU 6255  O   PRO B 460     4654   4552   4581   -572    399     -1       O  
ATOM   6256  CB  PRO B 460       8.764  21.935  53.925  1.00 36.58           C  
ANISOU 6256  CB  PRO B 460     4972   4318   4609   -635    300    -25       C  
ATOM   6257  CG  PRO B 460       7.658  22.082  54.917  1.00 36.99           C  
ANISOU 6257  CG  PRO B 460     5109   4286   4661   -552    275    -76       C  
ATOM   6258  CD  PRO B 460       6.366  21.758  54.218  1.00 36.57           C  
ANISOU 6258  CD  PRO B 460     5061   4231   4602   -427    301    -86       C  
ATOM   6259  N   VAL B 461       8.436  18.712  53.632  1.00 37.69           N  
ANISOU 6259  N   VAL B 461     4870   4656   4794   -451    354    -91       N  
ATOM   6260  CA  VAL B 461       9.143  17.450  53.848  1.00 35.33           C  
ANISOU 6260  CA  VAL B 461     4462   4449   4514   -428    365   -105       C  
ATOM   6261  C   VAL B 461       9.294  16.662  52.546  1.00 38.77           C  
ANISOU 6261  C   VAL B 461     4855   4951   4924   -370    409    -97       C  
ATOM   6262  O   VAL B 461      10.305  15.958  52.341  1.00 42.54           O  
ANISOU 6262  O   VAL B 461     5246   5518   5398   -360    438    -86       O  
ATOM   6263  CB  VAL B 461       8.510  16.584  54.939  1.00 34.14           C  
ANISOU 6263  CB  VAL B 461     4301   4282   4390   -370    336   -153       C  
ATOM   6264  CG1 VAL B 461       8.722  17.253  56.304  1.00 35.63           C  
ANISOU 6264  CG1 VAL B 461     4524   4425   4590   -428    298   -161       C  
ATOM   6265  CG2 VAL B 461       7.029  16.297  54.647  1.00 31.33           C  
ANISOU 6265  CG2 VAL B 461     3994   3882   4029   -292    332   -174       C  
ATOM   6266  N   PHE B 462       8.332  16.848  51.650  1.00 35.23           N  
ANISOU 6266  N   PHE B 462     4473   4463   4450   -328    414    -98       N  
ATOM   6267  CA  PHE B 462       8.321  16.155  50.373  1.00 37.60           C  
ANISOU 6267  CA  PHE B 462     4766   4810   4709   -271    447    -97       C  
ATOM   6268  C   PHE B 462       9.631  16.352  49.646  1.00 37.44           C  
ANISOU 6268  C   PHE B 462     4692   4875   4659   -306    502    -51       C  
ATOM   6269  O   PHE B 462      10.146  15.416  49.049  1.00 41.49           O  
ANISOU 6269  O   PHE B 462     5163   5460   5142   -244    540    -58       O  
ATOM   6270  CB  PHE B 462       7.156  16.632  49.505  1.00 33.67           C  
ANISOU 6270  CB  PHE B 462     4354   4257   4183   -243    433    -90       C  
ATOM   6271  CG  PHE B 462       7.022  15.900  48.187  1.00 35.40           C  
ANISOU 6271  CG  PHE B 462     4591   4512   4347   -185    452    -95       C  
ATOM   6272  CD1 PHE B 462       7.683  16.353  47.054  1.00 38.35           C  
ANISOU 6272  CD1 PHE B 462     4978   4928   4666   -200    501    -54       C  
ATOM   6273  CD2 PHE B 462       6.143  14.819  48.056  1.00 33.45           C  
ANISOU 6273  CD2 PHE B 462     4364   4251   4094   -123    413   -135       C  
ATOM   6274  CE1 PHE B 462       7.524  15.705  45.826  1.00 41.01           C  
ANISOU 6274  CE1 PHE B 462     5354   5293   4936   -139    518    -63       C  
ATOM   6275  CE2 PHE B 462       5.960  14.187  46.846  1.00 34.79           C  
ANISOU 6275  CE2 PHE B 462     4579   4437   4201    -76    415   -144       C  
ATOM   6276  CZ  PHE B 462       6.652  14.616  45.720  1.00 38.27           C  
ANISOU 6276  CZ  PHE B 462     5041   4919   4580    -75    470   -113       C  
ATOM   6277  N   HIS B 463      10.153  17.566  49.705  1.00 37.26           N  
ANISOU 6277  N   HIS B 463     4677   4843   4637   -405    507      0       N  
ATOM   6278  CA  HIS B 463      11.334  17.973  48.904  1.00 38.46           C  
ANISOU 6278  CA  HIS B 463     4772   5086   4754   -463    563     68       C  
ATOM   6279  C   HIS B 463      12.621  17.722  49.598  1.00 37.33           C  
ANISOU 6279  C   HIS B 463     4505   5041   4637   -513    574     96       C  
ATOM   6280  O   HIS B 463      13.684  18.042  49.081  1.00 40.87           O  
ANISOU 6280  O   HIS B 463     4876   5590   5063   -572    620    166       O  
ATOM   6281  CB  HIS B 463      11.204  19.448  48.505  1.00 37.83           C  
ANISOU 6281  CB  HIS B 463     4778   4941   4655   -562    554    124       C  
ATOM   6282  CG  HIS B 463       9.873  19.756  47.831  1.00 38.36           C  
ANISOU 6282  CG  HIS B 463     4966   4915   4696   -500    537    104       C  
ATOM   6283  ND1 HIS B 463       9.642  19.492  46.524  1.00 37.24           N  
ANISOU 6283  ND1 HIS B 463     4849   4806   4495   -445    574    117       N  
ATOM   6284  CD2 HIS B 463       8.669  20.258  48.357  1.00 35.09           C  
ANISOU 6284  CD2 HIS B 463     4648   4384   4301   -474    483     72       C  
ATOM   6285  CE1 HIS B 463       8.364  19.835  46.224  1.00 36.32           C  
ANISOU 6285  CE1 HIS B 463     4833   4599   4368   -398    535     99       C  
ATOM   6286  NE2 HIS B 463       7.770  20.295  47.350  1.00 33.81           N  
ANISOU 6286  NE2 HIS B 463     4550   4196   4100   -410    484     75       N  
ATOM   6287  N   GLN B 464      12.521  17.148  50.792  1.00 37.85           N  
ANISOU 6287  N   GLN B 464     4544   5087   4749   -492    529     49       N  
ATOM   6288  CA  GLN B 464      13.652  16.895  51.645  1.00 37.61           C  
ANISOU 6288  CA  GLN B 464     4398   5143   4750   -537    520     73       C  
ATOM   6289  C   GLN B 464      14.033  15.424  51.545  1.00 39.13           C  
ANISOU 6289  C   GLN B 464     4508   5424   4936   -408    554     45       C  
ATOM   6290  O   GLN B 464      13.210  14.561  51.846  1.00 35.81           O  
ANISOU 6290  O   GLN B 464     4142   4941   4525   -318    530    -22       O  
ATOM   6291  CB  GLN B 464      13.298  17.274  53.086  1.00 36.84           C  
ANISOU 6291  CB  GLN B 464     4346   4956   4695   -595    442     41       C  
ATOM   6292  CG  GLN B 464      14.348  16.989  54.135  1.00 35.15           C  
ANISOU 6292  CG  GLN B 464     4025   4819   4512   -645    409     60       C  
ATOM   6293  CD  GLN B 464      15.690  17.678  53.876  1.00 39.15           C  
ANISOU 6293  CD  GLN B 464     4428   5435   5012   -771    420    152       C  
ATOM   6294  OE1 GLN B 464      15.828  18.905  53.973  1.00 39.82           O  
ANISOU 6294  OE1 GLN B 464     4571   5467   5092   -912    383    194       O  
ATOM   6295  NE2 GLN B 464      16.687  16.880  53.547  1.00 38.12           N  
ANISOU 6295  NE2 GLN B 464     4146   5461   4877   -719    469    191       N  
ATOM   6296  N   GLU B 465      15.266  15.138  51.095  1.00 38.82           N  
ANISOU 6296  N   GLU B 465     4343   5530   4876   -394    611    101       N  
ATOM   6297  CA  GLU B 465      15.777  13.771  51.153  1.00 39.34           C  
ANISOU 6297  CA  GLU B 465     4334   5680   4933   -258    641     77       C  
ATOM   6298  C   GLU B 465      15.975  13.385  52.616  1.00 39.92           C  
ANISOU 6298  C   GLU B 465     4363   5741   5062   -273    573     55       C  
ATOM   6299  O   GLU B 465      16.156  14.246  53.472  1.00 40.08           O  
ANISOU 6299  O   GLU B 465     4371   5740   5119   -403    518     81       O  
ATOM   6300  CB  GLU B 465      17.078  13.627  50.373  1.00 43.27           C  
ANISOU 6300  CB  GLU B 465     4695   6356   5390   -224    727    153       C  
ATOM   6301  CG  GLU B 465      16.911  13.768  48.869  1.00 44.28           C  
ANISOU 6301  CG  GLU B 465     4874   6508   5444   -175    807    170       C  
ATOM   6302  CD  GLU B 465      18.229  13.669  48.115  1.00 46.70           C  
ANISOU 6302  CD  GLU B 465     5032   7012   5699   -135    907    256       C  
ATOM   6303  OE1 GLU B 465      19.302  13.578  48.747  1.00 53.23           O  
ANISOU 6303  OE1 GLU B 465     5699   7970   6557   -158    911    314       O  
ATOM   6304  OE2 GLU B 465      18.203  13.689  46.877  1.00 47.57           O  
ANISOU 6304  OE2 GLU B 465     5181   7159   5735    -78    984    273       O  
ATOM   6305  N   MET B 466      15.872  12.092  52.905  1.00 42.28           N  
ANISOU 6305  N   MET B 466     4666   6038   5361   -142    569      5       N  
ATOM   6306  CA  MET B 466      15.905  11.577  54.276  1.00 42.17           C  
ANISOU 6306  CA  MET B 466     4634   5999   5392   -140    502    -21       C  
ATOM   6307  C   MET B 466      16.609  10.221  54.287  1.00 46.65           C  
ANISOU 6307  C   MET B 466     5136   6647   5942     11    529    -27       C  
ATOM   6308  O   MET B 466      16.500   9.438  53.334  1.00 49.03           O  
ANISOU 6308  O   MET B 466     5482   6953   6195    139    581    -52       O  
ATOM   6309  CB  MET B 466      14.497  11.424  54.852  1.00 38.04           C  
ANISOU 6309  CB  MET B 466     4248   5320   4887   -142    445    -91       C  
ATOM   6310  CG  MET B 466      13.732  12.720  54.953  1.00 38.68           C  
ANISOU 6310  CG  MET B 466     4403   5313   4978   -258    419    -89       C  
ATOM   6311  SD  MET B 466      12.068  12.351  55.486  1.00 41.68           S  
ANISOU 6311  SD  MET B 466     4913   5553   5372   -223    373   -157       S  
ATOM   6312  CE  MET B 466      11.203  13.856  55.023  1.00 38.00           C  
ANISOU 6312  CE  MET B 466     4536   5006   4896   -304    373   -146       C  
ATOM   6313  N   VAL B 467      17.306   9.952  55.384  1.00 43.56           N  
ANISOU 6313  N   VAL B 467     4657   6310   5584      2    485     -7       N  
ATOM   6314  CA  VAL B 467      18.074   8.731  55.559  1.00 43.39           C  
ANISOU 6314  CA  VAL B 467     4567   6370   5550    150    501     -3       C  
ATOM   6315  C   VAL B 467      17.325   7.985  56.652  1.00 42.96           C  
ANISOU 6315  C   VAL B 467     4608   6193   5520    176    425    -63       C  
ATOM   6316  O   VAL B 467      16.906   8.577  57.654  1.00 40.30           O  
ANISOU 6316  O   VAL B 467     4297   5795   5221     59    359    -70       O  
ATOM   6317  CB  VAL B 467      19.530   9.067  55.975  1.00 42.23           C  
ANISOU 6317  CB  VAL B 467     4221   6404   5420    110    504     88       C  
ATOM   6318  CG1 VAL B 467      20.413   7.837  55.993  1.00 44.66           C  
ANISOU 6318  CG1 VAL B 467     4441   6821   5705    295    536    104       C  
ATOM   6319  CG2 VAL B 467      20.109  10.089  55.018  1.00 40.07           C  
ANISOU 6319  CG2 VAL B 467     3858   6240   5128     24    567    162       C  
ATOM   6320  N   ASN B 468      17.129   6.696  56.446  1.00 43.36           N  
ANISOU 6320  N   ASN B 468     4730   6203   5544    328    434   -105       N  
ATOM   6321  CA  ASN B 468      16.423   5.899  57.424  1.00 42.73           C  
ANISOU 6321  CA  ASN B 468     4746   6008   5482    348    363   -151       C  
ATOM   6322  C   ASN B 468      17.328   4.846  58.007  1.00 42.24           C  
ANISOU 6322  C   ASN B 468     4628   6007   5414    474    348   -135       C  
ATOM   6323  O   ASN B 468      18.027   4.159  57.264  1.00 43.61           O  
ANISOU 6323  O   ASN B 468     4774   6250   5546    623    404   -125       O  
ATOM   6324  CB  ASN B 468      15.193   5.235  56.811  1.00 41.41           C  
ANISOU 6324  CB  ASN B 468     4746   5701   5286    395    359   -215       C  
ATOM   6325  CG  ASN B 468      14.312   4.611  57.853  1.00 41.59           C  
ANISOU 6325  CG  ASN B 468     4864   5608   5332    371    283   -247       C  
ATOM   6326  OD1 ASN B 468      14.522   4.838  59.052  1.00 44.39           O  
ANISOU 6326  OD1 ASN B 468     5169   5978   5721    313    239   -228       O  
ATOM   6327  ND2 ASN B 468      13.313   3.833  57.422  1.00 37.92           N  
ANISOU 6327  ND2 ASN B 468     4538   5028   4841    406    264   -291       N  
ATOM   6328  N   TYR B 469      17.316   4.716  59.330  1.00 39.68           N  
ANISOU 6328  N   TYR B 469     4295   5657   5123    427    275   -130       N  
ATOM   6329  CA  TYR B 469      18.158   3.716  59.991  1.00 43.39           C  
ANISOU 6329  CA  TYR B 469     4716   6181   5588    548    248   -109       C  
ATOM   6330  C   TYR B 469      17.658   3.479  61.408  1.00 41.65           C  
ANISOU 6330  C   TYR B 469     4554   5875   5393    485    159   -122       C  
ATOM   6331  O   TYR B 469      16.793   4.208  61.883  1.00 41.24           O  
ANISOU 6331  O   TYR B 469     4558   5750   5363    348    129   -141       O  
ATOM   6332  CB  TYR B 469      19.653   4.122  59.962  1.00 44.42           C  
ANISOU 6332  CB  TYR B 469     4640   6513   5725    567    276    -29       C  
ATOM   6333  CG  TYR B 469      19.904   5.571  60.343  1.00 45.66           C  
ANISOU 6333  CG  TYR B 469     4694   6736   5918    368    251     17       C  
ATOM   6334  CD1 TYR B 469      19.869   6.577  59.381  1.00 44.60           C  
ANISOU 6334  CD1 TYR B 469     4529   6638   5779    282    307     35       C  
ATOM   6335  CD2 TYR B 469      20.165   5.934  61.672  1.00 45.01           C  
ANISOU 6335  CD2 TYR B 469     4568   6669   5867    263    162     41       C  
ATOM   6336  CE1 TYR B 469      20.090   7.899  59.723  1.00 46.03           C  
ANISOU 6336  CE1 TYR B 469     4645   6857   5987     94    274     77       C  
ATOM   6337  CE2 TYR B 469      20.378   7.256  62.030  1.00 44.75           C  
ANISOU 6337  CE2 TYR B 469     4474   6673   5855     75    126     77       C  
ATOM   6338  CZ  TYR B 469      20.342   8.230  61.053  1.00 46.16           C  
ANISOU 6338  CZ  TYR B 469     4631   6876   6031    -10    180     96       C  
ATOM   6339  OH  TYR B 469      20.557   9.533  61.384  1.00 46.37           O  
ANISOU 6339  OH  TYR B 469     4624   6921   6073   -199    137    133       O  
ATOM   6340  N   ILE B 470      18.175   2.456  62.085  1.00 43.47           N  
ANISOU 6340  N   ILE B 470     4783   6117   5616    594    121   -109       N  
ATOM   6341  CA  ILE B 470      17.670   2.150  63.445  1.00 43.90           C  
ANISOU 6341  CA  ILE B 470     4908   6087   5684    539     38   -118       C  
ATOM   6342  C   ILE B 470      18.689   2.526  64.506  1.00 45.74           C  
ANISOU 6342  C   ILE B 470     5005   6437   5935    498    -16    -61       C  
ATOM   6343  O   ILE B 470      19.840   2.010  64.504  1.00 45.39           O  
ANISOU 6343  O   ILE B 470     4851   6511   5884    615    -14    -15       O  
ATOM   6344  CB  ILE B 470      17.253   0.665  63.612  1.00 46.27           C  
ANISOU 6344  CB  ILE B 470     5353   6271   5957    666     11   -146       C  
ATOM   6345  CG1 ILE B 470      16.157   0.284  62.617  1.00 43.29           C  
ANISOU 6345  CG1 ILE B 470     5125   5766   5557    679     41   -200       C  
ATOM   6346  CG2 ILE B 470      16.774   0.372  65.027  1.00 44.26           C  
ANISOU 6346  CG2 ILE B 470     5163   5944   5711    602    -69   -141       C  
ATOM   6347  CD1 ILE B 470      16.341  -1.109  62.048  1.00 47.86           C  
ANISOU 6347  CD1 ILE B 470     5817   6279   6089    857     46   -221       C  
ATOM   6348  N   LEU B 471      18.275   3.442  65.393  1.00 43.53           N  
ANISOU 6348  N   LEU B 471     4735   6132   5673    337    -64    -63       N  
ATOM   6349  CA  LEU B 471      19.068   3.787  66.574  1.00 42.34           C  
ANISOU 6349  CA  LEU B 471     4496   6064   5529    273   -141    -17       C  
ATOM   6350  C   LEU B 471      18.339   3.259  67.800  1.00 43.14           C  
ANISOU 6350  C   LEU B 471     4722   6055   5615    258   -205    -40       C  
ATOM   6351  O   LEU B 471      17.103   3.124  67.791  1.00 40.32           O  
ANISOU 6351  O   LEU B 471     4500   5568   5250    231   -188    -86       O  
ATOM   6352  CB  LEU B 471      19.270   5.291  66.702  1.00 40.47           C  
ANISOU 6352  CB  LEU B 471     4192   5878   5306     97   -157      2       C  
ATOM   6353  CG  LEU B 471      20.011   6.070  65.620  1.00 42.86           C  
ANISOU 6353  CG  LEU B 471     4364   6299   5623     61   -102     42       C  
ATOM   6354  CD1 LEU B 471      19.835   7.549  65.956  1.00 40.31           C  
ANISOU 6354  CD1 LEU B 471     4055   5956   5305   -138   -139     46       C  
ATOM   6355  CD2 LEU B 471      21.506   5.701  65.513  1.00 40.20           C  
ANISOU 6355  CD2 LEU B 471     3832   6151   5290    139   -107    123       C  
ATOM   6356  N   SER B 472      19.102   2.979  68.858  1.00 43.73           N  
ANISOU 6356  N   SER B 472     4743   6191   5681    269   -280      1       N  
ATOM   6357  CA  SER B 472      18.537   2.470  70.116  1.00 43.99           C  
ANISOU 6357  CA  SER B 472     4890   6135   5689    255   -345     -9       C  
ATOM   6358  C   SER B 472      18.784   3.519  71.205  1.00 41.95           C  
ANISOU 6358  C   SER B 472     4605   5916   5418    107   -416      7       C  
ATOM   6359  O   SER B 472      19.827   4.147  71.190  1.00 43.63           O  
ANISOU 6359  O   SER B 472     4683   6253   5643     57   -448     50       O  
ATOM   6360  CB  SER B 472      19.245   1.164  70.468  1.00 46.87           C  
ANISOU 6360  CB  SER B 472     5239   6528   6040    410   -383     27       C  
ATOM   6361  OG  SER B 472      18.590   0.543  71.545  1.00 50.72           O  
ANISOU 6361  OG  SER B 472     5858   6914   6499    404   -436     20       O  
ATOM   6362  N   PRO B 473      17.850   3.726  72.155  1.00 41.73           N  
ANISOU 6362  N   PRO B 473     4707   5789   5359     32   -444    -23       N  
ATOM   6363  CA  PRO B 473      16.508   3.165  72.410  1.00 41.78           C  
ANISOU 6363  CA  PRO B 473     4867   5664   5346     49   -414    -59       C  
ATOM   6364  C   PRO B 473      15.556   3.293  71.230  1.00 41.66           C  
ANISOU 6364  C   PRO B 473     4893   5582   5353     53   -328    -98       C  
ATOM   6365  O   PRO B 473      15.659   4.240  70.444  1.00 45.48           O  
ANISOU 6365  O   PRO B 473     5323   6099   5858      1   -289   -110       O  
ATOM   6366  CB  PRO B 473      15.979   4.023  73.573  1.00 39.27           C  
ANISOU 6366  CB  PRO B 473     4626   5310   4983    -68   -451    -73       C  
ATOM   6367  CG  PRO B 473      17.193   4.468  74.280  1.00 40.82           C  
ANISOU 6367  CG  PRO B 473     4740   5603   5166   -115   -538    -38       C  
ATOM   6368  CD  PRO B 473      18.259   4.653  73.231  1.00 39.20           C  
ANISOU 6368  CD  PRO B 473     4376   5507   5009    -92   -523     -8       C  
ATOM   6369  N   ALA B 474      14.617   2.358  71.123  1.00 37.98           N  
ANISOU 6369  N   ALA B 474     4528   5023   4880    103   -306   -110       N  
ATOM   6370  CA  ALA B 474      13.767   2.285  69.962  1.00 36.47           C  
ANISOU 6370  CA  ALA B 474     4376   4774   4708    114   -240   -140       C  
ATOM   6371  C   ALA B 474      12.356   1.804  70.298  1.00 37.10           C  
ANISOU 6371  C   ALA B 474     4574   4753   4770     84   -231   -147       C  
ATOM   6372  O   ALA B 474      12.146   1.026  71.244  1.00 36.34           O  
ANISOU 6372  O   ALA B 474     4542   4620   4647     94   -272   -123       O  
ATOM   6373  CB  ALA B 474      14.407   1.335  68.960  1.00 34.64           C  
ANISOU 6373  CB  ALA B 474     4120   4554   4489    240   -224   -136       C  
ATOM   6374  N   PHE B 475      11.385   2.238  69.512  1.00 37.38           N  
ANISOU 6374  N   PHE B 475     4633   4753   4818     44   -180   -170       N  
ATOM   6375  CA  PHE B 475      10.111   1.517  69.491  1.00 40.95           C  
ANISOU 6375  CA  PHE B 475     5175   5123   5260     27   -173   -163       C  
ATOM   6376  C   PHE B 475      10.169   0.511  68.354  1.00 44.57           C  
ANISOU 6376  C   PHE B 475     5673   5532   5730     97   -173   -172       C  
ATOM   6377  O   PHE B 475      10.591   0.867  67.262  1.00 41.28           O  
ANISOU 6377  O   PHE B 475     5211   5143   5330    132   -140   -197       O  
ATOM   6378  CB  PHE B 475       8.914   2.453  69.329  1.00 37.87           C  
ANISOU 6378  CB  PHE B 475     4791   4728   4872    -49   -126   -173       C  
ATOM   6379  CG  PHE B 475       8.692   3.350  70.513  1.00 38.91           C  
ANISOU 6379  CG  PHE B 475     4923   4888   4972   -101   -123   -168       C  
ATOM   6380  CD1 PHE B 475       7.910   2.925  71.597  1.00 39.89           C  
ANISOU 6380  CD1 PHE B 475     5104   4994   5059   -126   -130   -136       C  
ATOM   6381  CD2 PHE B 475       9.279   4.614  70.564  1.00 36.95           C  
ANISOU 6381  CD2 PHE B 475     4633   4682   4723   -128   -114   -191       C  
ATOM   6382  CE1 PHE B 475       7.701   3.767  72.703  1.00 39.24           C  
ANISOU 6382  CE1 PHE B 475     5040   4937   4931   -158   -121   -136       C  
ATOM   6383  CE2 PHE B 475       9.075   5.453  71.656  1.00 38.16           C  
ANISOU 6383  CE2 PHE B 475     4821   4844   4833   -169   -118   -195       C  
ATOM   6384  CZ  PHE B 475       8.303   5.029  72.730  1.00 39.28           C  
ANISOU 6384  CZ  PHE B 475     5024   4971   4931   -175   -118   -171       C  
ATOM   6385  N   ARG B 476       9.758  -0.737  68.626  1.00 47.10           N  
ANISOU 6385  N   ARG B 476     6090   5774   6033    117   -213   -151       N  
ATOM   6386  CA  ARG B 476       9.720  -1.808  67.623  1.00 47.54           C  
ANISOU 6386  CA  ARG B 476     6229   5751   6083    182   -228   -163       C  
ATOM   6387  C   ARG B 476       8.310  -2.409  67.515  1.00 46.68           C  
ANISOU 6387  C   ARG B 476     6219   5553   5965     98   -249   -144       C  
ATOM   6388  O   ARG B 476       7.491  -2.302  68.433  1.00 42.93           O  
ANISOU 6388  O   ARG B 476     5748   5080   5482     11   -256   -106       O  
ATOM   6389  CB  ARG B 476      10.647  -2.955  68.025  1.00 50.48           C  
ANISOU 6389  CB  ARG B 476     6658   6089   6434    292   -278   -149       C  
ATOM   6390  CG  ARG B 476      12.116  -2.608  68.141  1.00 61.78           C  
ANISOU 6390  CG  ARG B 476     7980   7622   7871    388   -270   -151       C  
ATOM   6391  CD  ARG B 476      12.950  -3.868  67.936  1.00 69.59           C  
ANISOU 6391  CD  ARG B 476     9038   8568   8836    543   -303   -145       C  
ATOM   6392  NE  ARG B 476      13.206  -4.665  69.149  1.00 82.23           N  
ANISOU 6392  NE  ARG B 476    10696  10134  10414    572   -369   -104       N  
ATOM   6393  CZ  ARG B 476      12.609  -5.826  69.472  1.00 85.50           C  
ANISOU 6393  CZ  ARG B 476    11272  10415  10799    575   -422    -85       C  
ATOM   6394  NH1 ARG B 476      11.658  -6.369  68.706  1.00 85.27           N  
ANISOU 6394  NH1 ARG B 476    11369  10270  10759    535   -426   -103       N  
ATOM   6395  NH2 ARG B 476      12.965  -6.451  70.587  1.00 77.25           N  
ANISOU 6395  NH2 ARG B 476    10270   9351   9731    607   -480    -42       N  
ATOM   6396  N   TYR B 477       8.043  -3.080  66.410  1.00 43.58           N  
ANISOU 6396  N   TYR B 477     5909   5085   5564    123   -264   -163       N  
ATOM   6397  CA  TYR B 477       6.876  -3.925  66.346  1.00 43.15           C  
ANISOU 6397  CA  TYR B 477     5966   4935   5495     39   -312   -133       C  
ATOM   6398  C   TYR B 477       7.141  -5.262  67.029  1.00 42.88           C  
ANISOU 6398  C   TYR B 477     6059   4804   5430     72   -381   -103       C  
ATOM   6399  O   TYR B 477       8.298  -5.693  67.172  1.00 39.40           O  
ANISOU 6399  O   TYR B 477     5640   4355   4976    199   -393   -119       O  
ATOM   6400  CB  TYR B 477       6.532  -4.173  64.906  1.00 44.32           C  
ANISOU 6400  CB  TYR B 477     6180   5026   5635     47   -319   -168       C  
ATOM   6401  CG  TYR B 477       6.179  -2.936  64.156  1.00 48.00           C  
ANISOU 6401  CG  TYR B 477     6539   5574   6125     11   -259   -191       C  
ATOM   6402  CD1 TYR B 477       5.002  -2.219  64.443  1.00 47.49           C  
ANISOU 6402  CD1 TYR B 477     6407   5556   6080   -106   -242   -156       C  
ATOM   6403  CD2 TYR B 477       7.000  -2.483  63.142  1.00 52.68           C  
ANISOU 6403  CD2 TYR B 477     7098   6202   6716    103   -216   -240       C  
ATOM   6404  CE1 TYR B 477       4.668  -1.077  63.738  1.00 47.39           C  
ANISOU 6404  CE1 TYR B 477     6310   5610   6086   -125   -191   -175       C  
ATOM   6405  CE2 TYR B 477       6.673  -1.352  62.415  1.00 55.40           C  
ANISOU 6405  CE2 TYR B 477     7360   6612   7079     68   -165   -256       C  
ATOM   6406  CZ  TYR B 477       5.511  -0.656  62.711  1.00 53.98           C  
ANISOU 6406  CZ  TYR B 477     7127   6463   6919    -43   -157   -225       C  
ATOM   6407  OH  TYR B 477       5.223   0.464  61.973  1.00 53.98           O  
ANISOU 6407  OH  TYR B 477     7058   6520   6933    -62   -110   -239       O  
ATOM   6408  N   GLN B 478       6.058  -5.922  67.426  1.00 42.29           N  
ANISOU 6408  N   GLN B 478     6067   4659   5341    -42   -429    -51       N  
ATOM   6409  CA  GLN B 478       6.123  -7.240  68.051  1.00 47.08           C  
ANISOU 6409  CA  GLN B 478     6823   5152   5914    -37   -505    -11       C  
ATOM   6410  C   GLN B 478       4.874  -8.058  67.686  1.00 49.45           C  
ANISOU 6410  C   GLN B 478     7246   5346   6198   -174   -571     33       C  
ATOM   6411  O   GLN B 478       3.838  -7.481  67.303  1.00 48.11           O  
ANISOU 6411  O   GLN B 478     7003   5228   6048   -289   -550     51       O  
ATOM   6412  CB  GLN B 478       6.277  -7.110  69.578  1.00 45.65           C  
ANISOU 6412  CB  GLN B 478     6592   5027   5726    -59   -501     41       C  
ATOM   6413  CG  GLN B 478       5.168  -6.293  70.216  1.00 47.51           C  
ANISOU 6413  CG  GLN B 478     6725   5353   5972   -195   -457     88       C  
ATOM   6414  CD  GLN B 478       5.277  -6.186  71.721  1.00 47.21           C  
ANISOU 6414  CD  GLN B 478     6660   5367   5909   -213   -451    137       C  
ATOM   6415  OE1 GLN B 478       6.008  -6.934  72.361  1.00 47.49           O  
ANISOU 6415  OE1 GLN B 478     6773   5352   5919   -151   -499    153       O  
ATOM   6416  NE2 GLN B 478       4.528  -5.260  72.291  1.00 43.70           N  
ANISOU 6416  NE2 GLN B 478     6115   5025   5465   -288   -392    163       N  
ATOM   6417  N   PRO B 479       4.964  -9.398  67.803  1.00 51.09           N  
ANISOU 6417  N   PRO B 479     7642   5404   6366   -164   -657     55       N  
ATOM   6418  CA  PRO B 479       3.862 -10.261  67.366  1.00 54.17           C  
ANISOU 6418  CA  PRO B 479     8173   5673   6734   -308   -740     98       C  
ATOM   6419  C   PRO B 479       2.618  -9.980  68.173  1.00 53.67           C  
ANISOU 6419  C   PRO B 479     8018   5688   6687   -498   -734    194       C  
ATOM   6420  O   PRO B 479       2.732  -9.598  69.319  1.00 57.05           O  
ANISOU 6420  O   PRO B 479     8354   6204   7120   -498   -690    233       O  
ATOM   6421  CB  PRO B 479       4.359 -11.671  67.700  1.00 50.41           C  
ANISOU 6421  CB  PRO B 479     7920   5024   6208   -252   -831    115       C  
ATOM   6422  CG  PRO B 479       5.842 -11.557  67.777  1.00 49.38           C  
ANISOU 6422  CG  PRO B 479     7769   4919   6072    -29   -789     52       C  
ATOM   6423  CD  PRO B 479       6.093 -10.186  68.336  1.00 51.24           C  
ANISOU 6423  CD  PRO B 479     7760   5352   6355    -21   -690     48       C  
ATOM   6424  N   ASP B 480       1.450 -10.131  67.568  1.00 55.36           N  
ANISOU 6424  N   ASP B 480     8248   5883   6904   -652   -776    233       N  
ATOM   6425  CA  ASP B 480       0.203 -10.155  68.320  1.00 59.03           C  
ANISOU 6425  CA  ASP B 480     8643   6414   7373   -840   -785    347       C  
ATOM   6426  C   ASP B 480       0.247 -11.358  69.274  1.00 59.91           C  
ANISOU 6426  C   ASP B 480     8909   6410   7444   -895   -860    422       C  
ATOM   6427  O   ASP B 480       0.621 -12.445  68.860  1.00 61.32           O  
ANISOU 6427  O   ASP B 480     9301   6410   7589   -872   -954    402       O  
ATOM   6428  CB  ASP B 480      -0.982 -10.238  67.367  1.00 60.49           C  
ANISOU 6428  CB  ASP B 480     8825   6594   7566   -996   -838    383       C  
ATOM   6429  CG  ASP B 480      -1.137  -8.976  66.532  1.00 64.87           C  
ANISOU 6429  CG  ASP B 480     9216   7275   8158   -948   -760    326       C  
ATOM   6430  OD1 ASP B 480      -0.970  -7.867  67.079  1.00 62.46           O  
ANISOU 6430  OD1 ASP B 480     8740   7114   7878   -882   -654    315       O  
ATOM   6431  OD2 ASP B 480      -1.424  -9.080  65.324  1.00 72.19           O  
ANISOU 6431  OD2 ASP B 480    10198   8149   9081   -977   -810    291       O  
ATOM   6432  N   PRO B 481      -0.091 -11.150  70.561  1.00 57.38           N  
ANISOU 6432  N   PRO B 481     8495   6187   7118   -954   -816    505       N  
ATOM   6433  CA  PRO B 481       0.147 -12.183  71.598  1.00 59.71           C  
ANISOU 6433  CA  PRO B 481     8932   6385   7369   -979   -874    573       C  
ATOM   6434  C   PRO B 481      -0.739 -13.423  71.519  1.00 62.90           C  
ANISOU 6434  C   PRO B 481     9503   6654   7743  -1171   -993    673       C  
ATOM   6435  O   PRO B 481      -0.525 -14.340  72.283  1.00 65.22           O  
ANISOU 6435  O   PRO B 481     9941   6842   7996  -1193  -1052    730       O  
ATOM   6436  CB  PRO B 481      -0.131 -11.453  72.913  1.00 55.77           C  
ANISOU 6436  CB  PRO B 481     8271   6055   6866  -1002   -782    638       C  
ATOM   6437  CG  PRO B 481      -0.939 -10.249  72.535  1.00 56.43           C  
ANISOU 6437  CG  PRO B 481     8147   6309   6986  -1047   -694    635       C  
ATOM   6438  CD  PRO B 481      -0.595  -9.883  71.126  1.00 53.62           C  
ANISOU 6438  CD  PRO B 481     7791   5916   6666   -971   -702    530       C  
ATOM   6439  N   TRP B 482      -1.712 -13.453  70.614  1.00 65.56           N  
ANISOU 6439  N   TRP B 482     9825   6989   8095  -1315  -1036    698       N  
ATOM   6440  CA  TRP B 482      -2.612 -14.610  70.487  1.00 70.25           C  
ANISOU 6440  CA  TRP B 482    10577   7456   8659  -1532  -1166    802       C  
ATOM   6441  C   TRP B 482      -2.300 -15.472  69.291  1.00 70.55           C  
ANISOU 6441  C   TRP B 482    10861   7274   8672  -1514  -1288    730       C  
ATOM   6442  O   TRP B 482      -1.673 -15.031  68.321  1.00 66.65           O  
ANISOU 6442  O   TRP B 482    10370   6764   8189  -1361  -1261    606       O  
ATOM   6443  CB  TRP B 482      -4.059 -14.139  70.411  1.00 69.92           C  
ANISOU 6443  CB  TRP B 482    10347   7578   8644  -1742  -1148    911       C  
ATOM   6444  CG  TRP B 482      -4.335 -13.253  69.218  1.00 69.06           C  
ANISOU 6444  CG  TRP B 482    10113   7552   8575  -1710  -1116    837       C  
ATOM   6445  CD1 TRP B 482      -4.708 -13.653  67.936  1.00 70.19           C  
ANISOU 6445  CD1 TRP B 482    10364   7590   8714  -1792  -1222    809       C  
ATOM   6446  CD2 TRP B 482      -4.251 -11.786  69.148  1.00 67.48           C  
ANISOU 6446  CD2 TRP B 482     9672   7550   8418  -1586   -975    779       C  
ATOM   6447  NE1 TRP B 482      -4.865 -12.574  67.109  1.00 71.33           N  
ANISOU 6447  NE1 TRP B 482    10345   7860   8896  -1728  -1154    745       N  
ATOM   6448  CE2 TRP B 482      -4.611 -11.420  67.770  1.00 69.28           C  
ANISOU 6448  CE2 TRP B 482     9875   7781   8668  -1604  -1006    725       C  
ATOM   6449  CE3 TRP B 482      -3.938 -10.777  70.051  1.00 68.53           C  
ANISOU 6449  CE3 TRP B 482     9634   7842   8564  -1470   -839    767       C  
ATOM   6450  CZ2 TRP B 482      -4.642 -10.088  67.338  1.00 67.75           C  
ANISOU 6450  CZ2 TRP B 482     9486   7742   8512  -1505   -900    667       C  
ATOM   6451  CZ3 TRP B 482      -3.972  -9.438  69.605  1.00 66.18           C  
ANISOU 6451  CZ3 TRP B 482     9153   7690   8303  -1374   -738    704       C  
ATOM   6452  CH2 TRP B 482      -4.322  -9.106  68.280  1.00 64.71           C  
ANISOU 6452  CH2 TRP B 482     8941   7503   8142  -1391   -766    658       C  
ATOM   6453  OXT TRP B 482      -2.696 -16.642  69.240  1.00 73.11           O  
ANISOU 6453  OXT TRP B 482    11400   7425   8954  -1658  -1420    795       O  
TER    6454      TRP B 482                                                      
HETATM 6455  N   ARG A 700       8.067  15.634  34.987  1.00 31.92           N  
HETATM 6456  CA  ARG A 700       8.509  16.144  33.715  1.00 38.04           C  
HETATM 6457  C   ARG A 700       7.693  17.354  33.371  1.00 41.85           C  
HETATM 6458  O   ARG A 700       6.786  17.702  34.167  1.00 45.74           O  
HETATM 6459  CB  ARG A 700       8.267  15.064  32.630  1.00 37.94           C  
HETATM 6460  CG  ARG A 700       8.722  13.638  33.017  1.00 39.25           C  
HETATM 6461  CD  ARG A 700       8.368  12.594  31.934  1.00 39.52           C  
HETATM 6462  NE  ARG A 700       6.908  12.512  31.990  1.00 40.35           N  
HETATM 6463  CZ  ARG A 700       6.112  11.803  31.201  1.00 41.34           C  
HETATM 6464  NH1 ARG A 700       4.808  11.861  31.414  1.00 40.77           N  
HETATM 6465  NH2 ARG A 700       6.604  11.044  30.214  1.00 42.91           N  
HETATM 6466  OXT ARG A 700       7.886  17.944  32.271  1.00 41.82           O  
HETATM 6467  N   ARG B 700      -2.512   6.981  63.017  1.00 38.06           N  
HETATM 6468  CA  ARG B 700      -3.009   6.286  64.185  1.00 37.74           C  
HETATM 6469  C   ARG B 700      -4.479   6.592  64.232  1.00 38.03           C  
HETATM 6470  O   ARG B 700      -5.004   7.149  63.238  1.00 39.09           O  
HETATM 6471  CB  ARG B 700      -2.307   6.772  65.455  1.00 34.51           C  
HETATM 6472  CG  ARG B 700      -0.787   6.617  65.366  1.00 37.12           C  
HETATM 6473  CD  ARG B 700      -0.050   7.469  66.404  1.00 37.89           C  
HETATM 6474  NE  ARG B 700      -0.294   8.897  66.181  1.00 42.00           N  
HETATM 6475  CZ  ARG B 700       0.061   9.943  66.962  1.00 44.58           C  
HETATM 6476  NH1 ARG B 700      -0.263  11.173  66.586  1.00 42.91           N  
HETATM 6477  NH2 ARG B 700       0.757   9.797  68.103  1.00 47.15           N  
HETATM 6478  OXT ARG B 700      -5.140   6.288  65.248  1.00 38.93           O  
HETATM 6479  CHA HEM A 500       9.327   9.195  34.827  1.00 33.87           C  
HETATM 6480  CHB HEM A 500       4.526   8.908  33.500  1.00 31.43           C  
HETATM 6481  CHC HEM A 500       5.783   7.412  29.078  1.00 32.55           C  
HETATM 6482  CHD HEM A 500      10.377   6.567  30.993  1.00 30.55           C  
HETATM 6483  C1A HEM A 500       7.901   9.361  34.757  1.00 32.39           C  
HETATM 6484  C2A HEM A 500       7.179  10.096  35.814  1.00 34.36           C  
HETATM 6485  C3A HEM A 500       5.752  10.024  35.432  1.00 29.50           C  
HETATM 6486  C4A HEM A 500       5.749   9.268  34.176  1.00 30.98           C  
HETATM 6487  CMA HEM A 500       4.572  10.593  36.153  1.00 31.46           C  
HETATM 6488  CAA HEM A 500       7.813  10.770  37.016  1.00 37.33           C  
HETATM 6489  CBA HEM A 500       8.144  12.155  36.467  1.00 44.28           C  
HETATM 6490  CGA HEM A 500       8.685  13.195  37.429  1.00 52.29           C  
HETATM 6491  O1A HEM A 500       8.243  13.242  38.605  1.00 47.81           O  
HETATM 6492  O2A HEM A 500       9.552  13.994  36.964  1.00 56.39           O  
HETATM 6493  C1B HEM A 500       4.472   8.494  32.137  1.00 29.60           C  
HETATM 6494  C2B HEM A 500       3.178   8.597  31.430  1.00 31.64           C  
HETATM 6495  C3B HEM A 500       3.557   8.140  30.094  1.00 32.80           C  
HETATM 6496  C4B HEM A 500       4.997   7.827  30.241  1.00 33.30           C  
HETATM 6497  CMB HEM A 500       1.902   9.066  32.019  1.00 30.46           C  
HETATM 6498  CAB HEM A 500       2.704   8.047  28.884  1.00 38.70           C  
HETATM 6499  CBB HEM A 500       2.882   7.083  27.970  1.00 39.89           C  
HETATM 6500  C1C HEM A 500       7.201   7.124  29.176  1.00 29.79           C  
HETATM 6501  C2C HEM A 500       8.028   6.647  28.041  1.00 30.34           C  
HETATM 6502  C3C HEM A 500       9.368   6.399  28.645  1.00 30.78           C  
HETATM 6503  C4C HEM A 500       9.278   6.747  30.069  1.00 32.12           C  
HETATM 6504  CMC HEM A 500       7.611   6.442  26.617  1.00 30.16           C  
HETATM 6505  CAC HEM A 500      10.605   5.891  28.011  1.00 32.27           C  
HETATM 6506  CBC HEM A 500      10.571   5.281  26.840  1.00 33.89           C  
HETATM 6507  C1D HEM A 500      10.486   7.288  32.211  1.00 32.53           C  
HETATM 6508  C2D HEM A 500      11.830   7.454  32.819  1.00 35.17           C  
HETATM 6509  C3D HEM A 500      11.517   8.247  33.991  1.00 35.04           C  
HETATM 6510  C4D HEM A 500      10.045   8.394  33.866  1.00 32.65           C  
HETATM 6511  CMD HEM A 500      13.155   6.946  32.365  1.00 36.46           C  
HETATM 6512  CAD HEM A 500      12.479   8.768  35.016  1.00 39.35           C  
HETATM 6513  CBD HEM A 500      12.835  10.228  34.748  1.00 48.50           C  
HETATM 6514  CGD HEM A 500      13.549  10.765  35.971  1.00 51.70           C  
HETATM 6515  O1D HEM A 500      13.668  12.011  36.096  1.00 56.08           O  
HETATM 6516  O2D HEM A 500      13.980   9.934  36.812  1.00 56.68           O  
HETATM 6517  NA  HEM A 500       7.065   8.913  33.675  1.00 31.23           N  
HETATM 6518  NB  HEM A 500       5.532   8.074  31.480  1.00 29.55           N  
HETATM 6519  NC  HEM A 500       7.969   7.271  30.389  1.00 30.96           N  
HETATM 6520  ND  HEM A 500       9.448   7.872  32.782  1.00 29.65           N  
HETATM 6521 FE   HEM A 500       7.443   7.668  32.208  1.00 35.18          FE  
HETATM 6522  O04 WS7 A 800      10.830  15.012  41.221  1.00 72.60           O  
HETATM 6523  C04 WS7 A 800      10.197  14.035  41.716  1.00 75.16           C  
HETATM 6524  N03 WS7 A 800       9.236  13.369  41.033  1.00 69.44           N  
HETATM 6525  C02 WS7 A 800       8.536  12.328  41.545  1.00 66.08           C  
HETATM 6526  N02 WS7 A 800       7.596  11.712  40.743  1.00 58.07           N  
HETATM 6527  N01 WS7 A 800       8.767  11.896  42.827  1.00 65.01           N  
HETATM 6528  C1A WS7 A 800       9.709  12.473  43.635  1.00 68.55           C  
HETATM 6529  C4A WS7 A 800      10.486  13.608  43.111  1.00 68.86           C  
HETATM 6530  N05 WS7 A 800      11.505  14.118  43.826  1.00 68.87           N  
HETATM 6531  N10 WS7 A 800       9.985  12.071  44.882  1.00 64.63           N  
HETATM 6532  C9A WS7 A 800      10.731  12.922  45.826  1.00 63.67           C  
HETATM 6533  C09 WS7 A 800      11.644  12.081  46.731  1.00 64.13           C  
HETATM 6534  C10 WS7 A 800       9.665  13.652  46.607  1.00 64.32           C  
HETATM 6535  C5A WS7 A 800      11.537  13.994  45.162  1.00 64.63           C  
HETATM 6536  C06 WS7 A 800      12.366  14.965  45.992  1.00 65.81           C  
HETATM 6537  C07 WS7 A 800      12.810  14.347  47.326  1.00 69.69           C  
HETATM 6538  C08 WS7 A 800      12.857  12.813  47.336  1.00 67.39           C  
HETATM 6539  C   ACT A 860      -1.540   5.722  31.306  1.00 49.65           C  
HETATM 6540  O   ACT A 860      -2.433   4.934  31.683  1.00 56.03           O  
HETATM 6541  OXT ACT A 860      -1.802   6.671  30.546  1.00 48.50           O  
HETATM 6542  CH3 ACT A 860      -0.135   5.539  31.774  1.00 45.83           C  
HETATM 6543 ZN    ZN A1483      16.254   1.315  50.954  1.00 49.39          ZN  
HETATM 6544  CHA HEM B 500       4.016   7.586  64.193  1.00 35.69           C  
HETATM 6545  CHB HEM B 500       2.524  12.324  64.854  1.00 38.92           C  
HETATM 6546  CHC HEM B 500       3.664  12.032  69.582  1.00 37.22           C  
HETATM 6547  CHD HEM B 500       6.102   7.745  68.571  1.00 39.55           C  
HETATM 6548  C1A HEM B 500       3.408   8.885  64.023  1.00 37.45           C  
HETATM 6549  C2A HEM B 500       2.689   9.210  62.774  1.00 40.15           C  
HETATM 6550  C3A HEM B 500       2.225  10.581  62.958  1.00 37.82           C  
HETATM 6551  C4A HEM B 500       2.714  10.986  64.300  1.00 37.35           C  
HETATM 6552  CMA HEM B 500       1.452  11.343  61.917  1.00 36.71           C  
HETATM 6553  CAA HEM B 500       2.436   8.320  61.581  1.00 40.05           C  
HETATM 6554  CBA HEM B 500       1.454   7.327  62.185  1.00 44.64           C  
HETATM 6555  CGA HEM B 500       0.562   6.523  61.267  1.00 52.74           C  
HETATM 6556  O1A HEM B 500       0.553   6.744  60.019  1.00 47.21           O  
HETATM 6557  O2A HEM B 500      -0.145   5.649  61.853  1.00 51.58           O  
HETATM 6558  C1B HEM B 500       2.661  12.654  66.256  1.00 38.31           C  
HETATM 6559  C2B HEM B 500       2.009  13.868  66.824  1.00 38.20           C  
HETATM 6560  C3B HEM B 500       2.386  13.758  68.218  1.00 37.60           C  
HETATM 6561  C4B HEM B 500       3.176  12.516  68.283  1.00 37.91           C  
HETATM 6562  CMB HEM B 500       1.201  14.940  66.140  1.00 41.05           C  
HETATM 6563  CAB HEM B 500       2.035  14.692  69.333  1.00 40.46           C  
HETATM 6564  CBB HEM B 500       2.962  15.001  70.233  1.00 36.90           C  
HETATM 6565  C1C HEM B 500       4.384  10.778  69.753  1.00 38.50           C  
HETATM 6566  C2C HEM B 500       4.873  10.286  71.073  1.00 38.87           C  
HETATM 6567  C3C HEM B 500       5.586   9.048  70.741  1.00 37.48           C  
HETATM 6568  C4C HEM B 500       5.476   8.849  69.287  1.00 38.66           C  
HETATM 6569  CMC HEM B 500       4.677  10.891  72.435  1.00 37.56           C  
HETATM 6570  CAC HEM B 500       6.265   8.116  71.673  1.00 39.13           C  
HETATM 6571  CBC HEM B 500       6.553   8.433  72.927  1.00 38.32           C  
HETATM 6572  C1D HEM B 500       5.668   7.314  67.258  1.00 40.97           C  
HETATM 6573  C2D HEM B 500       5.984   5.931  66.848  1.00 39.95           C  
HETATM 6574  C3D HEM B 500       5.367   5.862  65.512  1.00 38.23           C  
HETATM 6575  C4D HEM B 500       4.787   7.228  65.368  1.00 38.33           C  
HETATM 6576  CMD HEM B 500       6.753   4.911  67.640  1.00 36.06           C  
HETATM 6577  CAD HEM B 500       5.287   4.684  64.565  1.00 40.86           C  
HETATM 6578  CBD HEM B 500       3.900   4.070  64.765  1.00 42.18           C  
HETATM 6579  CGD HEM B 500       3.647   2.932  63.808  1.00 49.63           C  
HETATM 6580  O1D HEM B 500       2.457   2.628  63.546  1.00 56.97           O  
HETATM 6581  O2D HEM B 500       4.629   2.332  63.320  1.00 47.91           O  
HETATM 6582  NA  HEM B 500       3.365   9.926  65.038  1.00 38.45           N  
HETATM 6583  NB  HEM B 500       3.306  11.840  67.098  1.00 38.23           N  
HETATM 6584  NC  HEM B 500       4.649   9.858  68.664  1.00 39.07           N  
HETATM 6585  ND  HEM B 500       4.931   8.077  66.421  1.00 38.13           N  
HETATM 6586 FE   HEM B 500       4.431  10.104  66.710  1.00 39.56          FE  
HETATM 6587  O04 WS7 B 800       0.042   3.829  57.647  1.00 84.87           O  
HETATM 6588  C04 WS7 B 800       0.921   4.563  57.135  1.00 74.48           C  
HETATM 6589  N03 WS7 B 800       1.188   5.778  57.659  1.00 77.35           N  
HETATM 6590  C02 WS7 B 800       2.121   6.629  57.153  1.00 71.22           C  
HETATM 6591  N02 WS7 B 800       2.319   7.846  57.755  1.00 64.31           N  
HETATM 6592  N01 WS7 B 800       2.855   6.282  56.057  1.00 66.12           N  
HETATM 6593  C1A WS7 B 800       2.691   5.082  55.426  1.00 68.07           C  
HETATM 6594  C4A WS7 B 800       1.690   4.129  55.931  1.00 72.52           C  
HETATM 6595  N05 WS7 B 800       1.682   2.881  55.418  1.00 67.04           N  
HETATM 6596  N10 WS7 B 800       3.397   4.711  54.361  1.00 66.66           N  
HETATM 6597  C9A WS7 B 800       2.933   3.660  53.458  1.00 64.46           C  
HETATM 6598  C09 WS7 B 800       4.143   2.979  52.773  1.00 60.37           C  
HETATM 6599  C10 WS7 B 800       2.039   4.369  52.472  1.00 62.72           C  
HETATM 6600  C5A WS7 B 800       2.057   2.662  54.151  1.00 60.26           C  
HETATM 6601  C06 WS7 B 800       1.568   1.424  53.414  1.00 58.46           C  
HETATM 6602  C07 WS7 B 800       2.520   1.022  52.272  1.00 59.06           C  
HETATM 6603  C08 WS7 B 800       3.971   1.480  52.483  1.00 55.64           C  
HETATM 6604  C   ACT B 860       3.514  19.258  66.524  1.00 63.44           C  
HETATM 6605  O   ACT B 860       2.304  19.558  66.630  1.00 65.48           O  
HETATM 6606  OXT ACT B 860       4.424  20.087  66.712  1.00 71.44           O  
HETATM 6607  CH3 ACT B 860       3.891  17.864  66.169  1.00 53.74           C  
HETATM 6608  C   ACT B 861      -5.056  16.916  48.057  1.00 35.15           C  
HETATM 6609  O   ACT B 861      -5.083  18.138  47.860  1.00 49.62           O  
HETATM 6610  OXT ACT B 861      -6.093  16.246  48.017  1.00 41.41           O  
HETATM 6611  CH3 ACT B 861      -3.764  16.268  48.308  1.00 34.28           C  
HETATM 6612  C1  GOL B 880      -3.051   0.329  57.385  1.00 64.09           C  
HETATM 6613  O1  GOL B 880      -3.591   0.423  56.054  1.00 62.57           O  
HETATM 6614  C2  GOL B 880      -1.554   0.149  57.151  1.00 64.91           C  
HETATM 6615  O2  GOL B 880      -0.994   1.289  56.479  1.00 61.13           O  
HETATM 6616  C3  GOL B 880      -0.801  -0.021  58.450  1.00 67.23           C  
HETATM 6617  O3  GOL B 880       0.567   0.186  58.071  1.00 69.27           O  
HETATM 6618  O   HOH A2001       5.681  -7.264  53.328  1.00 53.56           O  
HETATM 6619  O   HOH A2002       1.900  -7.250  46.796  1.00 36.12           O  
HETATM 6620  O   HOH A2003      -4.115  -0.803  46.618  1.00 37.12           O  
HETATM 6621  O   HOH A2004      -7.490   2.645  46.311  1.00 48.94           O  
HETATM 6622  O   HOH A2005      -0.581  -7.974  45.911  1.00 40.46           O  
HETATM 6623  O   HOH A2006       7.595  -6.576  43.090  1.00 40.80           O  
HETATM 6624  O   HOH A2007      24.596  -7.737  41.778  1.00 67.85           O  
HETATM 6625  O   HOH A2008      19.651  -2.699  42.412  1.00 45.03           O  
HETATM 6626  O   HOH A2009      19.717  -0.728  47.330  1.00 42.18           O  
HETATM 6627  O   HOH A2010      19.673   0.358  60.700  1.00 46.69           O  
HETATM 6628  O   HOH A2011      11.708  -8.821  18.859  1.00 50.92           O  
HETATM 6629  O   HOH A2012      22.716  -6.680  29.706  1.00 43.39           O  
HETATM 6630  O   HOH A2013      33.339 -16.580  26.336  1.00 70.04           O  
HETATM 6631  O   HOH A2014      13.720 -11.399  28.205  1.00 59.21           O  
HETATM 6632  O   HOH A2015      15.512  -6.529  31.418  1.00 39.88           O  
HETATM 6633  O   HOH A2016      19.899 -10.997  16.831  1.00 53.52           O  
HETATM 6634  O   HOH A2017      11.886  -9.314  21.282  1.00 51.44           O  
HETATM 6635  O   HOH A2018      18.226  14.867   7.176  1.00 48.85           O  
HETATM 6636  O   HOH A2019       6.777  36.410  36.803  1.00 46.76           O  
HETATM 6637  O   HOH A2020       7.788  -0.761  18.138  1.00 48.59           O  
HETATM 6638  O   HOH A2021      15.264   2.104  33.238  1.00 39.78           O  
HETATM 6639  O   HOH A2022       7.726  -3.230  34.698  1.00 38.23           O  
HETATM 6640  O   HOH A2023       8.104 -10.833  29.513  1.00 45.90           O  
HETATM 6641  O   HOH A2024      16.348   0.491  35.089  1.00 36.67           O  
HETATM 6642  O   HOH A2025      15.457  -1.265  37.188  1.00 41.58           O  
HETATM 6643  O   HOH A2026       5.832   8.069  38.449  1.00 42.11           O  
HETATM 6644  O   HOH A2027       0.910   2.364  33.965  1.00 33.90           O  
HETATM 6645  O   HOH A2028       1.000  -3.644  29.336  1.00 45.56           O  
HETATM 6646  O   HOH A2029       1.512  -2.010  26.018  1.00 57.37           O  
HETATM 6647  O   HOH A2030       2.263   4.178  24.377  1.00 38.11           O  
HETATM 6648  O   HOH A2031       5.438  -0.522  19.362  1.00 55.47           O  
HETATM 6649  O   HOH A2032       3.674   4.559  20.203  1.00 38.85           O  
HETATM 6650  O   HOH A2033       9.631   0.425  16.360  1.00 50.33           O  
HETATM 6651  O   HOH A2034      24.272  15.082   8.414  1.00 44.65           O  
HETATM 6652  O   HOH A2035      25.451  20.398  11.880  1.00 52.87           O  
HETATM 6653  O   HOH A2036      16.112  20.397  10.026  1.00 59.40           O  
HETATM 6654  O   HOH A2037      18.019  12.459   8.643  1.00 57.67           O  
HETATM 6655  O   HOH A2038      18.867  16.933   8.305  1.00 48.32           O  
HETATM 6656  O   HOH A2039      13.128  10.858  15.161  1.00 39.93           O  
HETATM 6657  O   HOH A2040       4.653  19.533  20.239  1.00 38.21           O  
HETATM 6658  O   HOH A2041       1.411  17.942  15.624  1.00 54.50           O  
HETATM 6659  O   HOH A2042       4.995  11.197  22.932  1.00 41.38           O  
HETATM 6660  O   HOH A2043       1.695   5.266  21.989  1.00 45.16           O  
HETATM 6661  O   HOH A2044      23.280   8.390  21.494  1.00 37.85           O  
HETATM 6662  O   HOH A2045      27.306   9.367  21.607  1.00 43.42           O  
HETATM 6663  O   HOH A2046      24.890   3.332  17.754  1.00 42.86           O  
HETATM 6664  O   HOH A2047      28.889   2.547  23.812  1.00 42.04           O  
HETATM 6665  O   HOH A2048      14.387  22.671  26.221  1.00 37.16           O  
HETATM 6666  O   HOH A2049       9.519  18.242  26.583  1.00 43.89           O  
HETATM 6667  O   HOH A2050      12.884  23.885  24.363  1.00 47.38           O  
HETATM 6668  O   HOH A2051       9.769  24.428  31.714  1.00 34.07           O  
HETATM 6669  O   HOH A2052       9.293  19.388  35.260  1.00 46.95           O  
HETATM 6670  O   HOH A2053       9.862  31.877  29.697  1.00 47.14           O  
HETATM 6671  O   HOH A2054       8.161  32.027  38.035  1.00 52.66           O  
HETATM 6672  O   HOH A2055       7.538  33.805  36.405  1.00 54.30           O  
HETATM 6673  O   HOH A2056       6.643  38.110  32.405  1.00 57.50           O  
HETATM 6674  O   HOH A2057      18.634  25.724  36.403  1.00 52.35           O  
HETATM 6675  O   HOH A2058      18.793  24.520  33.661  1.00 49.67           O  
HETATM 6676  O   HOH A2059      18.542  34.332  18.469  1.00 56.31           O  
HETATM 6677  O   HOH A2060       4.142  35.674  29.585  1.00 55.67           O  
HETATM 6678  O   HOH A2061       5.594  32.328  38.239  1.00 51.94           O  
HETATM 6679  O   HOH A2062       7.636  30.659  22.837  1.00 52.89           O  
HETATM 6680  O   HOH A2063      24.597  27.955  16.405  1.00 56.33           O  
HETATM 6681  O   HOH A2064       3.672  27.330  20.496  1.00 58.66           O  
HETATM 6682  O   HOH A2065       4.424  20.187  22.911  1.00 40.81           O  
HETATM 6683  O   HOH A2066      -4.327  30.613  32.997  1.00 50.40           O  
HETATM 6684  O   HOH A2067       0.381  15.324  27.599  1.00 36.70           O  
HETATM 6685  O   HOH A2068       9.132  11.740  28.676  1.00 47.45           O  
HETATM 6686  O   HOH A2069      16.501  11.396  27.525  1.00 37.32           O  
HETATM 6687  O   HOH A2070      19.281  11.630  25.802  1.00 37.84           O  
HETATM 6688  O   HOH A2071      20.799  12.404  33.077  1.00 43.80           O  
HETATM 6689  O   HOH A2072      17.378   8.614  27.039  1.00 36.67           O  
HETATM 6690  O   HOH A2073      21.156  -4.565  29.038  1.00 47.08           O  
HETATM 6691  O   HOH A2074      -4.108  15.802  38.723  1.00 40.91           O  
HETATM 6692  O   HOH A2075       3.491  13.906  39.438  1.00 35.96           O  
HETATM 6693  O   HOH A2076       4.076  21.018  44.390  1.00 38.61           O  
HETATM 6694  O   HOH A2077       5.759  14.032  41.832  1.00 35.50           O  
HETATM 6695  O   HOH A2078      10.012  20.412  40.152  1.00 37.60           O  
HETATM 6696  O   HOH A2079      12.619  18.543  42.165  1.00 57.84           O  
HETATM 6697  O   HOH A2080       3.153  27.341  45.106  1.00 36.93           O  
HETATM 6698  O   HOH A2081      14.122  25.229  40.607  1.00 48.30           O  
HETATM 6699  O   HOH A2082       1.992  32.530  44.246  1.00 47.07           O  
HETATM 6700  O   HOH A2083       2.846  30.286  46.241  1.00 42.50           O  
HETATM 6701  O   HOH A2084     -13.532  29.980  46.356  1.00 59.49           O  
HETATM 6702  O   HOH A2085      -9.892  30.269  53.498  1.00 53.45           O  
HETATM 6703  O   HOH A2086      -0.359  29.839  55.932  1.00 45.44           O  
HETATM 6704  O   HOH A2087      -3.531  27.245  62.444  1.00 53.74           O  
HETATM 6705  O   HOH A2088      -2.517  25.393  53.593  1.00 42.73           O  
HETATM 6706  O   HOH A2089     -14.295  23.256  41.175  1.00 53.14           O  
HETATM 6707  O   HOH A2090      -7.957  12.400  30.651  1.00 56.16           O  
HETATM 6708  O   HOH A2091      -7.521  14.651  26.587  1.00 44.78           O  
HETATM 6709  O   HOH A2092      -7.576  10.653  33.067  1.00 38.64           O  
HETATM 6710  O   HOH A2093      -7.788   6.787  43.195  1.00 49.49           O  
HETATM 6711  O   HOH A2094       1.657  -4.473  31.915  1.00 44.63           O  
HETATM 6712  O   HOH A2095       4.800  -7.108  40.508  1.00 37.15           O  
HETATM 6713  O   HOH A2096       1.303 -11.161  32.258  1.00 39.41           O  
HETATM 6714  O   HOH A2097       4.687 -15.031  41.400  1.00 52.83           O  
HETATM 6715  O   HOH A2098      -1.395 -11.198  32.313  1.00 56.29           O  
HETATM 6716  O   HOH A2099       7.870  -3.759  43.504  1.00 30.85           O  
HETATM 6717  O   HOH A2100      10.287   1.699  46.464  1.00 32.98           O  
HETATM 6718  O   HOH A2101       5.705  11.945  43.228  1.00 33.77           O  
HETATM 6719  O   HOH A2102       5.049  10.255  46.630  1.00 53.38           O  
HETATM 6720  O   HOH A2103       3.405   8.828  39.554  1.00 43.27           O  
HETATM 6721  O   HOH A2104       4.342  11.454  40.441  1.00 45.63           O  
HETATM 6722  O   HOH A2105       0.502  12.938  48.629  1.00 60.33           O  
HETATM 6723  O   HOH A2106      -8.749   6.379  49.915  1.00 55.32           O  
HETATM 6724  O   HOH A2107      -6.842   4.558  47.922  1.00 49.86           O  
HETATM 6725  O   HOH A2108      -7.109   7.483  52.368  1.00 45.98           O  
HETATM 6726  O   HOH A2109      -1.651   1.304  53.808  1.00 50.61           O  
HETATM 6727  O   HOH A2110       5.475  -5.263  55.388  1.00 46.70           O  
HETATM 6728  O   HOH A2111      10.787  -0.071  48.976  1.00 51.62           O  
HETATM 6729  O   HOH A2112      20.128  -6.780  34.380  1.00 53.54           O  
HETATM 6730  O   HOH A2113       6.023  14.772  38.550  1.00 38.77           O  
HETATM 6731  O   HOH A2114      10.593  15.742  39.051  1.00 46.88           O  
HETATM 6732  O   HOH A2115      13.125  16.402  42.220  1.00 46.06           O  
HETATM 6733  O   HOH B2001      19.159  18.182  53.411  1.00 37.22           O  
HETATM 6734  O   HOH B2002      16.084  22.120  42.954  1.00 53.50           O  
HETATM 6735  O   HOH B2003      16.758  26.517  44.933  1.00 51.44           O  
HETATM 6736  O   HOH B2004       7.279  23.631  50.808  1.00 39.77           O  
HETATM 6737  O   HOH B2005      19.871  12.772  58.200  1.00 39.39           O  
HETATM 6738  O   HOH B2006      21.908   3.049  68.521  1.00 46.10           O  
HETATM 6739  O   HOH B2007      23.826  -2.007  61.140  1.00 70.94           O  
HETATM 6740  O   HOH B2008      10.990  -1.271  55.273  1.00 46.55           O  
HETATM 6741  O   HOH B2009      14.209  13.086  85.117  1.00 61.47           O  
HETATM 6742  O   HOH B2010      26.840   5.358  92.530  1.00 64.30           O  
HETATM 6743  O   HOH B2011      18.719  -3.711  90.609  1.00 49.02           O  
HETATM 6744  O   HOH B2012      14.492  -8.962  82.433  1.00 37.52           O  
HETATM 6745  O   HOH B2013      16.405  -0.106  89.197  1.00 52.30           O  
HETATM 6746  O   HOH B2014      16.968   0.732  92.234  1.00 51.29           O  
HETATM 6747  O   HOH B2015       9.311   5.169  90.099  1.00 49.68           O  
HETATM 6748  O   HOH B2016       6.111   7.709  87.679  1.00 57.43           O  
HETATM 6749  O   HOH B2017      15.874  11.475  83.370  1.00 49.54           O  
HETATM 6750  O   HOH B2018      15.304  12.705  80.795  1.00 51.13           O  
HETATM 6751  O   HOH B2019      12.339   4.467  67.879  1.00 37.15           O  
HETATM 6752  O   HOH B2020      15.415  12.833  65.892  1.00 45.30           O  
HETATM 6753  O   HOH B2021      16.084   5.032  64.494  1.00 38.00           O  
HETATM 6754  O   HOH B2022      14.602   3.689  66.588  1.00 38.20           O  
HETATM 6755  O   HOH B2023       9.276   4.675  63.803  1.00 52.80           O  
HETATM 6756  O   HOH B2024       4.633  10.566  60.532  1.00 48.78           O  
HETATM 6757  O   HOH B2025       9.912   1.730  62.015  1.00 53.85           O  
HETATM 6758  O   HOH B2026       7.896  17.739  64.553  1.00 35.76           O  
HETATM 6759  O   HOH B2027       4.974  16.779  73.830  1.00 40.48           O  
HETATM 6760  O   HOH B2028      13.002  18.532  72.885  1.00 47.71           O  
HETATM 6761  O   HOH B2029       8.646  12.145  83.499  1.00 46.00           O  
HETATM 6762  O   HOH B2030       8.533  11.485  85.853  1.00 58.49           O  
HETATM 6763  O   HOH B2031      -4.129 -10.798  85.905  1.00 57.88           O  
HETATM 6764  O   HOH B2032      -2.343   0.348  89.676  1.00 68.29           O  
HETATM 6765  O   HOH B2033       0.012   5.517  83.842  1.00 37.52           O  
HETATM 6766  O   HOH B2034      -9.812  10.419  76.375  1.00 48.20           O  
HETATM 6767  O   HOH B2035      -6.325  22.646  73.147  1.00 59.50           O  
HETATM 6768  O   HOH B2036      10.060   5.120  49.879  1.00 60.21           O  
HETATM 6769  O   HOH B2037      11.930   4.150  50.293  1.00 58.01           O  
HETATM 6770  O   HOH B2038      -1.209  12.224  74.983  1.00 44.15           O  
HETATM 6771  O   HOH B2039       0.683  19.914  82.508  1.00 54.46           O  
HETATM 6772  O   HOH B2040       2.891  17.453  75.917  1.00 39.34           O  
HETATM 6773  O   HOH B2041       6.341  -3.850  79.394  1.00 41.51           O  
HETATM 6774  O   HOH B2042       6.759  -7.967  80.055  1.00 33.78           O  
HETATM 6775  O   HOH B2043      10.693  -3.553  84.399  1.00 39.80           O  
HETATM 6776  O   HOH B2044      13.899  -7.118  78.679  1.00 46.25           O  
HETATM 6777  O   HOH B2045       8.325 -11.662  79.614  1.00 39.37           O  
HETATM 6778  O   HOH B2046       3.995 -13.751  76.185  1.00 53.75           O  
HETATM 6779  O   HOH B2047       1.356  -4.646  74.480  1.00 35.77           O  
HETATM 6780  O   HOH B2048      -8.921  -0.480  71.978  1.00 40.74           O  
HETATM 6781  O   HOH B2049      -5.915   5.465  71.358  1.00 41.60           O  
HETATM 6782  O   HOH B2050     -10.966   0.878  73.214  1.00 39.20           O  
HETATM 6783  O   HOH B2051     -11.065   2.956  65.469  1.00 56.62           O  
HETATM 6784  O   HOH B2052     -18.347   0.676  66.392  1.00 51.18           O  
HETATM 6785  O   HOH B2053     -16.855 -10.883  55.806  1.00 70.72           O  
HETATM 6786  O   HOH B2054     -17.202   0.671  57.539  1.00 56.15           O  
HETATM 6787  O   HOH B2055     -19.503  -6.570  78.944  1.00 57.64           O  
HETATM 6788  O   HOH B2056     -21.508   4.141  67.886  1.00 44.13           O  
HETATM 6789  O   HOH B2057     -18.784   6.797  70.834  1.00 56.92           O  
HETATM 6790  O   HOH B2058     -14.382   0.499  76.885  1.00 51.20           O  
HETATM 6791  O   HOH B2059      -4.339 -11.503  82.740  1.00 51.94           O  
HETATM 6792  O   HOH B2060     -12.548 -10.433  82.131  1.00 54.85           O  
HETATM 6793  O   HOH B2061     -15.655   2.628  77.027  1.00 55.76           O  
HETATM 6794  O   HOH B2062      -9.750  10.141  73.301  1.00 52.66           O  
HETATM 6795  O   HOH B2063     -16.371  13.503  74.502  1.00 50.80           O  
HETATM 6796  O   HOH B2064     -20.377  14.176  60.753  1.00 49.11           O  
HETATM 6797  O   HOH B2065     -21.630  20.549  59.709  1.00 42.05           O  
HETATM 6798  O   HOH B2066      -5.525  14.785  69.117  1.00 41.33           O  
HETATM 6799  O   HOH B2067       0.291   7.561  70.022  1.00 44.38           O  
HETATM 6800  O   HOH B2068       2.680   0.841  72.268  1.00 32.15           O  
HETATM 6801  O   HOH B2069       3.043  -1.646  74.289  1.00 44.76           O  
HETATM 6802  O   HOH B2070       5.422   1.066  73.132  1.00 39.24           O  
HETATM 6803  O   HOH B2071      19.360   1.465  74.222  1.00 40.74           O  
HETATM 6804  O   HOH B2072      -1.300  11.148  58.155  1.00 34.97           O  
HETATM 6805  O   HOH B2073      -4.063   6.750  60.527  1.00 43.00           O  
HETATM 6806  O   HOH B2074      -0.542   8.341  56.161  1.00 39.37           O  
HETATM 6807  O   HOH B2075      -5.540   2.674  57.644  1.00 47.19           O  
HETATM 6808  O   HOH B2076     -13.032   6.446  51.062  1.00 45.06           O  
HETATM 6809  O   HOH B2077      -8.201  -2.558  57.497  1.00 56.90           O  
HETATM 6810  O   HOH B2078     -16.188   5.837  49.207  1.00 56.04           O  
HETATM 6811  O   HOH B2079     -18.780   5.954  51.135  1.00 50.57           O  
HETATM 6812  O   HOH B2080     -12.332   4.478  47.772  1.00 51.84           O  
HETATM 6813  O   HOH B2081     -15.404  18.739  39.854  1.00 52.51           O  
HETATM 6814  O   HOH B2082     -10.285   2.939  45.717  1.00 59.73           O  
HETATM 6815  O   HOH B2083      -7.841  22.524  68.494  1.00 51.96           O  
HETATM 6816  O   HOH B2084      -5.197  22.525  68.680  1.00 53.43           O  
HETATM 6817  O   HOH B2085      13.477  24.700  59.210  1.00 53.05           O  
HETATM 6818  O   HOH B2086      14.303  19.075  68.020  1.00 41.38           O  
HETATM 6819  O   HOH B2087      18.650  12.655  65.314  1.00 55.43           O  
HETATM 6820  O   HOH B2088      17.281  11.901  57.392  1.00 32.61           O  
HETATM 6821  O   HOH B2089      13.391   7.655  54.294  1.00 36.95           O  
HETATM 6822  O   HOH B2090      10.579   5.727  52.715  1.00 64.13           O  
HETATM 6823  O   HOH B2091       3.577   9.489  52.155  1.00 49.67           O  
HETATM 6824  O   HOH B2092       1.259  10.969  57.617  1.00 36.20           O  
HETATM 6825  O   HOH B2093       3.420  12.448  58.600  1.00 47.73           O  
HETATM 6826  O   HOH B2094       1.720   9.203  55.144  1.00 46.69           O  
HETATM 6827  O   HOH B2095      10.308   3.521  66.005  1.00 37.96           O  
HETATM 6828  O   HOH B2096       7.540   2.223  63.532  1.00 52.79           O  
HETATM 6829  O   HOH B2097       1.648 -11.183  64.502  1.00 45.89           O  
HETATM 6830  O   HOH B2098      -4.704 -17.336  67.219  1.00 64.29           O  
HETATM 6831  O   HOH B2099      -1.598   8.206  59.379  1.00 44.48           O  
CONECT  233 6543                                                                
CONECT  275 6543                                                                
CONECT  865 6521                                                                
CONECT 2429 2434                                                                
CONECT 2434 2429 2435                                                           
CONECT 2435 2434 2436 2437                                                      
CONECT 2436 2435 2439                                                           
CONECT 2437 2435 2438 2443                                                      
CONECT 2438 2437                                                                
CONECT 2439 2436                                                                
CONECT 2440 2442                                                                
CONECT 2441 2442                                                                
CONECT 2442 2440 2441                                                           
CONECT 2443 2437                                                                
CONECT 3446 6543                                                                
CONECT 3488 6543                                                                
CONECT 4095 6586                                                                
CONECT 5659 5664                                                                
CONECT 5664 5659 5665                                                           
CONECT 5665 5664 5666 5667                                                      
CONECT 5666 5665 5669                                                           
CONECT 5667 5665 5668 5673                                                      
CONECT 5668 5667                                                                
CONECT 5669 5666                                                                
CONECT 5670 5671 5672                                                           
CONECT 5671 5670                                                                
CONECT 5672 5670                                                                
CONECT 5673 5667                                                                
CONECT 6455 6456                                                                
CONECT 6456 6455 6457 6459                                                      
CONECT 6457 6456 6458 6466                                                      
CONECT 6458 6457                                                                
CONECT 6459 6456 6460                                                           
CONECT 6460 6459 6461                                                           
CONECT 6461 6460 6462                                                           
CONECT 6462 6461 6463                                                           
CONECT 6463 6462 6464 6465                                                      
CONECT 6464 6463                                                                
CONECT 6465 6463                                                                
CONECT 6466 6457                                                                
CONECT 6467 6468                                                                
CONECT 6468 6467 6469 6471                                                      
CONECT 6469 6468 6470 6478                                                      
CONECT 6470 6469                                                                
CONECT 6471 6468 6472                                                           
CONECT 6472 6471 6473                                                           
CONECT 6473 6472 6474                                                           
CONECT 6474 6473 6475                                                           
CONECT 6475 6474 6476 6477                                                      
CONECT 6476 6475                                                                
CONECT 6477 6475                                                                
CONECT 6478 6469                                                                
CONECT 6479 6483 6510                                                           
CONECT 6480 6486 6493                                                           
CONECT 6481 6496 6500                                                           
CONECT 6482 6503 6507                                                           
CONECT 6483 6479 6484 6517                                                      
CONECT 6484 6483 6485 6488                                                      
CONECT 6485 6484 6486 6487                                                      
CONECT 6486 6480 6485 6517                                                      
CONECT 6487 6485                                                                
CONECT 6488 6484 6489                                                           
CONECT 6489 6488 6490                                                           
CONECT 6490 6489 6491 6492                                                      
CONECT 6491 6490                                                                
CONECT 6492 6490                                                                
CONECT 6493 6480 6494 6518                                                      
CONECT 6494 6493 6495 6497                                                      
CONECT 6495 6494 6496 6498                                                      
CONECT 6496 6481 6495 6518                                                      
CONECT 6497 6494                                                                
CONECT 6498 6495 6499                                                           
CONECT 6499 6498                                                                
CONECT 6500 6481 6501 6519                                                      
CONECT 6501 6500 6502 6504                                                      
CONECT 6502 6501 6503 6505                                                      
CONECT 6503 6482 6502 6519                                                      
CONECT 6504 6501                                                                
CONECT 6505 6502 6506                                                           
CONECT 6506 6505                                                                
CONECT 6507 6482 6508 6520                                                      
CONECT 6508 6507 6509 6511                                                      
CONECT 6509 6508 6510 6512                                                      
CONECT 6510 6479 6509 6520                                                      
CONECT 6511 6508                                                                
CONECT 6512 6509 6513                                                           
CONECT 6513 6512 6514                                                           
CONECT 6514 6513 6515 6516                                                      
CONECT 6515 6514                                                                
CONECT 6516 6514                                                                
CONECT 6517 6483 6486 6521                                                      
CONECT 6518 6493 6496 6521                                                      
CONECT 6519 6500 6503 6521                                                      
CONECT 6520 6507 6510 6521                                                      
CONECT 6521  865 6517 6518 6519                                                 
CONECT 6521 6520                                                                
CONECT 6522 6523                                                                
CONECT 6523 6522 6524 6529                                                      
CONECT 6524 6523 6525                                                           
CONECT 6525 6524 6526 6527                                                      
CONECT 6526 6525                                                                
CONECT 6527 6525 6528                                                           
CONECT 6528 6527 6529 6531                                                      
CONECT 6529 6523 6528 6530                                                      
CONECT 6530 6529 6535                                                           
CONECT 6531 6528 6532                                                           
CONECT 6532 6531 6533 6534 6535                                                 
CONECT 6533 6532 6538                                                           
CONECT 6534 6532                                                                
CONECT 6535 6530 6532 6536                                                      
CONECT 6536 6535 6537                                                           
CONECT 6537 6536 6538                                                           
CONECT 6538 6533 6537                                                           
CONECT 6539 6540 6541 6542                                                      
CONECT 6540 6539                                                                
CONECT 6541 6539                                                                
CONECT 6542 6539                                                                
CONECT 6543  233  275 3446 3488                                                 
CONECT 6544 6548 6575                                                           
CONECT 6545 6551 6558                                                           
CONECT 6546 6561 6565                                                           
CONECT 6547 6568 6572                                                           
CONECT 6548 6544 6549 6582                                                      
CONECT 6549 6548 6550 6553                                                      
CONECT 6550 6549 6551 6552                                                      
CONECT 6551 6545 6550 6582                                                      
CONECT 6552 6550                                                                
CONECT 6553 6549 6554                                                           
CONECT 6554 6553 6555                                                           
CONECT 6555 6554 6556 6557                                                      
CONECT 6556 6555                                                                
CONECT 6557 6555                                                                
CONECT 6558 6545 6559 6583                                                      
CONECT 6559 6558 6560 6562                                                      
CONECT 6560 6559 6561 6563                                                      
CONECT 6561 6546 6560 6583                                                      
CONECT 6562 6559                                                                
CONECT 6563 6560 6564                                                           
CONECT 6564 6563                                                                
CONECT 6565 6546 6566 6584                                                      
CONECT 6566 6565 6567 6569                                                      
CONECT 6567 6566 6568 6570                                                      
CONECT 6568 6547 6567 6584                                                      
CONECT 6569 6566                                                                
CONECT 6570 6567 6571                                                           
CONECT 6571 6570                                                                
CONECT 6572 6547 6573 6585                                                      
CONECT 6573 6572 6574 6576                                                      
CONECT 6574 6573 6575 6577                                                      
CONECT 6575 6544 6574 6585                                                      
CONECT 6576 6573                                                                
CONECT 6577 6574 6578                                                           
CONECT 6578 6577 6579                                                           
CONECT 6579 6578 6580 6581                                                      
CONECT 6580 6579                                                                
CONECT 6581 6579                                                                
CONECT 6582 6548 6551 6586                                                      
CONECT 6583 6558 6561 6586                                                      
CONECT 6584 6565 6568 6586                                                      
CONECT 6585 6572 6575 6586                                                      
CONECT 6586 4095 6582 6583 6584                                                 
CONECT 6586 6585                                                                
CONECT 6587 6588                                                                
CONECT 6588 6587 6589 6594                                                      
CONECT 6589 6588 6590                                                           
CONECT 6590 6589 6591 6592                                                      
CONECT 6591 6590                                                                
CONECT 6592 6590 6593                                                           
CONECT 6593 6592 6594 6596                                                      
CONECT 6594 6588 6593 6595                                                      
CONECT 6595 6594 6600                                                           
CONECT 6596 6593 6597                                                           
CONECT 6597 6596 6598 6599 6600                                                 
CONECT 6598 6597 6603                                                           
CONECT 6599 6597                                                                
CONECT 6600 6595 6597 6601                                                      
CONECT 6601 6600 6602                                                           
CONECT 6602 6601 6603                                                           
CONECT 6603 6598 6602                                                           
CONECT 6604 6605 6606 6607                                                      
CONECT 6605 6604                                                                
CONECT 6606 6604                                                                
CONECT 6607 6604                                                                
CONECT 6608 6609 6610 6611                                                      
CONECT 6609 6608                                                                
CONECT 6610 6608                                                                
CONECT 6611 6608                                                                
CONECT 6612 6613 6614                                                           
CONECT 6613 6612                                                                
CONECT 6614 6612 6615 6616                                                      
CONECT 6615 6614                                                                
CONECT 6616 6614 6617                                                           
CONECT 6617 6616                                                                
MASTER      536    0   13   38   36    0   26    6 6829    2  193   70          
END