path: root/plip/test/pdb/2efj.pdb

HEADER    TRANSFERASE                             22-FEB-07   2EFJ              
TITLE     THE STRUCTURE OF 1,7 DIMETHYLXANTHINE METHYLTRANSFERASE               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3,7-DIMETHYLXANTHINE METHYLTRANSFERASE;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.1.1.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: COFFEA CANEPHORA;                               
SOURCE   3 ORGANISM_TAXID: 49390;                                               
SOURCE   4 GENE: DXMT1;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (RIL);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPROEXHTB                                 
KEYWDS    SAM-DEPENDANT METHYLTRANSFERASE, SAH, THEOBROMINE, TRANSFERASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.MCCARTHY,J.G.MCCARTHY                                             
REVDAT   4   13-JUL-11 2EFJ    1       VERSN                                    
REVDAT   3   24-FEB-09 2EFJ    1       VERSN                                    
REVDAT   2   19-JUN-07 2EFJ    1       JRNL   REMARK                            
REVDAT   1   01-MAY-07 2EFJ    0                                                
JRNL        AUTH   A.A.MCCARTHY,J.G.MCCARTHY                                    
JRNL        TITL   THE STRUCTURE OF TWO N-METHYLTRANSFERASES FROM THE CAFFEINE  
JRNL        TITL 2 BIOSYNTHETIC PATHWAY                                         
JRNL        REF    PLANT PHYSIOL.                V. 144   879 2007              
JRNL        REFN                   ISSN 0032-0889                               
JRNL        PMID   17434991                                                     
JRNL        DOI    10.1104/PP.106.094854                                        
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.A.MCCARTHY,L.BIGET,C.LIN,V.PETIARD,S.D.TANKSLEY,           
REMARK   1  AUTH 2 J.G.MCCARTHY                                                 
REMARK   1  TITL   CLONING, EXPRESSION, CRYSTALLIZATION AND PRELIMINARY X-RAY   
REMARK   1  TITL 2 ANALYSIS OF THE XMT AND DXMT N-METHYLTRANSFERASES FROM       
REMARK   1  TITL 3 COFFEA CANEPHORA (ROBUSTA)                                   
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  63   304 2007              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   17401201                                                     
REMARK   1  DOI    10.1107/S1744309107009268                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24209                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1297                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1707                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2719                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 35.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.68000                                             
REMARK   3    B22 (A**2) : 1.42000                                              
REMARK   3    B33 (A**2) : -0.74000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.217         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.196         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.341        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2853 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3873 ; 1.564 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   349 ; 5.634 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;37.532 ;24.331       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   467 ;17.281 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;18.178 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   431 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2160 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1311 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1932 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   157 ; 0.279 ; 0.200       
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):    47 ; 0.149 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.128 ; 0.200       
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):  1802 ; 0.719 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2826 ; 1.171 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1226 ; 1.745 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1044 ; 2.546 ; 4.500       
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  : 3                                          
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     3        A    27                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9340  19.5330  50.2400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0600 T22:  -0.0930                                     
REMARK   3      T33:  -0.0372 T12:   0.0992                                     
REMARK   3      T13:  -0.0018 T23:   0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1675 L22:   4.4754                                     
REMARK   3      L33:   1.9622 L12:  -1.2302                                     
REMARK   3      L13:   4.0267 L23:   0.7737                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3495 S12:   0.9509 S13:  -1.1168                       
REMARK   3      S21:  -0.1063 S22:   0.4389 S23:   0.3908                       
REMARK   3      S31:   0.2223 S32:  -0.0407 S33:  -0.7883                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    28        A   231                          
REMARK   3    RESIDUE RANGE :   A   266        A   302                          
REMARK   3    RESIDUE RANGE :   A   365        A   379                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4310  33.8670  51.9200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1063 T22:  -0.2303                                     
REMARK   3      T33:  -0.1783 T12:   0.0876                                     
REMARK   3      T13:   0.0724 T23:   0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1261 L22:   1.0666                                     
REMARK   3      L33:   2.5178 L12:  -0.7476                                     
REMARK   3      L13:   0.7132 L23:  -0.6932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1552 S12:  -0.2872 S13:   0.0732                       
REMARK   3      S21:   0.3580 S22:   0.2754 S23:   0.0882                       
REMARK   3      S31:  -0.2113 S32:  -0.1757 S33:  -0.1202                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   232        A   265                          
REMARK   3    RESIDUE RANGE :   A   312        A   364                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5130  10.7620  61.7420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0031 T22:  -0.1668                                     
REMARK   3      T33:  -0.2105 T12:   0.1539                                     
REMARK   3      T13:   0.0625 T23:   0.0721                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2790 L22:   3.4891                                     
REMARK   3      L33:   2.4406 L12:  -0.7196                                     
REMARK   3      L13:  -0.7959 L23:   0.1829                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3154 S12:  -0.4022 S13:  -0.7686                       
REMARK   3      S21:   0.4751 S22:   0.2753 S23:   0.1526                       
REMARK   3      S31:   0.2889 S32:   0.0447 S33:   0.0401                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2EFJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB026601.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393                             
REMARK 200  MONOCHROMATOR                  : A DOUBLE CRYSTAL (SI 111) KHOZU    
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25506                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-28% PEG 3350, 200MM LI2SO4, 100MM     
REMARK 280  TRIS-HCL, 2MM DTT, 1MM SAH, 1MM THEOBROMINE, PH 8.5, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.47500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.47500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       25.08000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.81500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       25.08000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.81500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.47500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       25.08000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.81500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.47500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       25.08000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.81500            
REMARK 290   SMTRY3   8  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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY   
REMARK 300 THE SYMMETERY OPERATIONS: -X, Y, -Z+1/2.                             
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       70.47500            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     GLY A    82                                                      
REMARK 465     GLN A    83                                                      
REMARK 465     GLU A    84                                                      
REMARK 465     LYS A    85                                                      
REMARK 465     LYS A    86                                                      
REMARK 465     ASN A    87                                                      
REMARK 465     GLU A    88                                                      
REMARK 465     LEU A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     ARG A    91                                                      
REMARK 465     LEU A   169                                                      
REMARK 465     VAL A   170                                                      
REMARK 465     THR A   171                                                      
REMARK 465     GLU A   172                                                      
REMARK 465     LEU A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     ASP A   303                                                      
REMARK 465     ASP A   304                                                      
REMARK 465     ASP A   305                                                      
REMARK 465     TYR A   306                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     GLY A   308                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     SER A   310                                                      
REMARK 465     HIS A   311                                                      
REMARK 465     GLU A   380                                                      
REMARK 465     LYS A   381                                                      
REMARK 465     ALA A   382                                                      
REMARK 465     ASP A   383                                                      
REMARK 465     MET A   384                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  20    CD   CE   NZ                                        
REMARK 470     LYS A  52    CG   CD   CE   NZ                                   
REMARK 470     LYS A  80    CE   NZ                                             
REMARK 470     LYS A 127    CG   CD   CE   NZ                                   
REMARK 470     ILE A 175    CG1  CG2  CD1                                       
REMARK 470     SER A 176    OG                                                  
REMARK 470     LYS A 179    CD   CE   NZ                                        
REMARK 470     LYS A 186    CG   CD   CE   NZ                                   
REMARK 470     ARG A 218    NE   CZ   NH1  NH2                                  
REMARK 470     ASP A 230    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 231    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 276    NE   CZ   NH1  NH2                                  
REMARK 470     SER A 312    OG                                                  
REMARK 470     LYS A 359    CD   CE   NZ                                        
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    LEU A  26      -62.41    -90.57                                   
REMARK 500    ASN A  49       -3.24     69.44                                   
REMARK 500    LYS A  52      -63.87    -94.67                                   
REMARK 500    ALA A  62     -138.12     56.02                                   
REMARK 500    ARG A 126      100.82    -36.56                                   
REMARK 500    TYR A 157       41.69     72.07                                   
REMARK 500    TYR A 183     -168.78   -160.15                                   
REMARK 500    PHE A 232      -64.45   -102.21                                   
REMARK 500    ASP A 233       46.05     85.51                                   
REMARK 500    PRO A 313     -111.90    -68.14                                   
REMARK 500    VAL A 314      -24.19   -159.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 596        DISTANCE =  5.43 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 37T A 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2EG5   RELATED DB: PDB                                   
REMARK 900 XANTHOSINE METHYLTRANSFERASE                                         
DBREF  2EFJ A    1   384  UNP    A4GE70   A4GE70_COFCA     1    384             
SEQRES   1 A  384  MET GLU LEU GLN GLU VAL LEU HIS MET ASN GLY GLY GLU          
SEQRES   2 A  384  GLY ASP THR SER TYR ALA LYS ASN SER SER TYR ASN LEU          
SEQRES   3 A  384  PHE LEU ILE ARG VAL LYS PRO VAL LEU GLU GLN CYS ILE          
SEQRES   4 A  384  GLN GLU LEU LEU ARG ALA ASN LEU PRO ASN ILE ASN LYS          
SEQRES   5 A  384  CYS PHE LYS VAL GLY ASP LEU GLY CYS ALA SER GLY PRO          
SEQRES   6 A  384  ASN THR PHE SER THR VAL ARG ASP ILE VAL GLN SER ILE          
SEQRES   7 A  384  ASP LYS VAL GLY GLN GLU LYS LYS ASN GLU LEU GLU ARG          
SEQRES   8 A  384  PRO THR ILE GLN ILE PHE LEU ASN ASP LEU PHE GLN ASN          
SEQRES   9 A  384  ASP PHE ASN SER VAL PHE LYS LEU LEU PRO SER PHE TYR          
SEQRES  10 A  384  ARG ASN LEU GLU LYS GLU ASN GLY ARG LYS ILE GLY SER          
SEQRES  11 A  384  CYS LEU ILE GLY ALA MET PRO GLY SER PHE TYR SER ARG          
SEQRES  12 A  384  LEU PHE PRO GLU GLU SER MET HIS PHE LEU HIS SER CYS          
SEQRES  13 A  384  TYR CYS LEU HIS TRP LEU SER GLN VAL PRO SER GLY LEU          
SEQRES  14 A  384  VAL THR GLU LEU GLY ILE SER VAL ASN LYS GLY CYS ILE          
SEQRES  15 A  384  TYR SER SER LYS ALA SER ARG PRO PRO ILE GLN LYS ALA          
SEQRES  16 A  384  TYR LEU ASP GLN PHE THR LYS ASP PHE THR THR PHE LEU          
SEQRES  17 A  384  ARG ILE HIS SER GLU GLU LEU ILE SER ARG GLY ARG MET          
SEQRES  18 A  384  LEU LEU THR PHE ILE CYS LYS GLU ASP GLU PHE ASP HIS          
SEQRES  19 A  384  PRO ASN SER MET ASP LEU LEU GLU MET SER ILE ASN ASP          
SEQRES  20 A  384  LEU VAL ILE GLU GLY HIS LEU GLU GLU GLU LYS LEU ASP          
SEQRES  21 A  384  SER PHE ASN VAL PRO ILE TYR ALA PRO SER THR GLU GLU          
SEQRES  22 A  384  VAL LYS ARG ILE VAL GLU GLU GLU GLY SER PHE GLU ILE          
SEQRES  23 A  384  LEU TYR LEU GLU THR PHE ASN ALA PRO TYR ASP ALA GLY          
SEQRES  24 A  384  PHE SER ILE ASP ASP ASP TYR GLN GLY ARG SER HIS SER          
SEQRES  25 A  384  PRO VAL SER CYS ASP GLU HIS ALA ARG ALA ALA HIS VAL          
SEQRES  26 A  384  ALA SER VAL VAL ARG SER ILE TYR GLU PRO ILE LEU ALA          
SEQRES  27 A  384  SER HIS PHE GLY GLU ALA ILE LEU PRO ASP LEU SER HIS          
SEQRES  28 A  384  ARG ILE ALA LYS ASN ALA ALA LYS VAL LEU ARG SER GLY          
SEQRES  29 A  384  LYS GLY PHE TYR ASP SER VAL ILE ILE SER LEU ALA LYS          
SEQRES  30 A  384  LYS PRO GLU LYS ALA ASP MET                                  
HET    SAH  A 501      26                                                       
HET    37T  A 502      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     37T THEOBROMINE                                                      
HETSYN     37T 3,7-DIMETHYLXANTHINE, 3,7-DIMETHYLPURINE-2,6-DIONE               
FORMUL   2  SAH    C14 H20 N6 O5 S                                              
FORMUL   3  37T    C7 H8 N4 O2                                                  
FORMUL   4  HOH   *146(H2 O)                                                    
HELIX    1   1 SER A   17  SER A   22  1                                   6    
HELIX    2   2 PHE A   27  ALA A   45  1                                  19    
HELIX    3   3 GLY A   64  ASP A   79  1                                  16    
HELIX    4   4 ASP A  105  ASN A  124  1                                  20    
HELIX    5   5 ARG A  189  GLU A  214  1                                  26    
HELIX    6   6 ASN A  236  GLU A  251  1                                  16    
HELIX    7   7 GLU A  255  SER A  261  1                                   7    
HELIX    8   8 SER A  270  GLY A  282  1                                  13    
HELIX    9   9 VAL A  314  GLY A  342  1                                  29    
HELIX   10  10 ILE A  345  GLY A  364  1                                  20    
SHEET    1   A 7 CYS A 131  ALA A 135  0                                        
SHEET    2   A 7 THR A  93  ASN A  99  1  N  ILE A  94   O  LEU A 132           
SHEET    3   A 7 CYS A  53  LEU A  59  1  N  ASP A  58   O  ASN A  99           
SHEET    4   A 7 MET A 150  CYS A 156  1  O  HIS A 154   N  LEU A  59           
SHEET    5   A 7 LEU A 215  ILE A 226  1  O  ILE A 216   N  MET A 150           
SHEET    6   A 7 PHE A 367  LYS A 377 -1  O  LEU A 375   N  MET A 221           
SHEET    7   A 7 PHE A 284  PRO A 295 -1  N  ALA A 294   O  TYR A 368           
SITE     1 AC1 22 LEU A   7  MET A   9  TYR A  18  GLY A  60                    
SITE     2 AC1 22 CYS A  61  ALA A  62  ASN A  66  ASN A  99                    
SITE     3 AC1 22 ASP A 100  GLY A 138  SER A 139  PHE A 140                    
SITE     4 AC1 22 TYR A 141  CYS A 156  TYR A 157  CYS A 158                    
SITE     5 AC1 22 37T A 502  HOH A 510  HOH A 517  HOH A 520                    
SITE     6 AC1 22 HOH A 547  HOH A 647                                          
SITE     1 AC2 13 TYR A  18  LEU A  26  PHE A  27  TYR A 157                    
SITE     2 AC2 13 HIS A 160  TRP A 161  ILE A 226  SER A 237                    
SITE     3 AC2 13 ILE A 332  TYR A 368  SAH A 501  HOH A 509                    
SITE     4 AC2 13 HOH A 587                                                     
CRYST1   50.160  105.630  140.950  90.00  90.00  90.00 C 2 2 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      0.019936  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009467  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007095        0.00000                         
ATOM      1  N   LEU A   3      18.115  22.517  43.440  0.75 46.59           N  
ATOM      2  CA  LEU A   3      16.845  22.051  44.082  0.75 46.24           C  
ATOM      3  C   LEU A   3      15.629  22.658  43.396  0.75 46.25           C  
ATOM      4  O   LEU A   3      14.527  22.116  43.488  0.75 46.60           O  
ATOM      5  CB  LEU A   3      16.793  22.411  45.570  0.75 46.31           C  
ATOM      6  CG  LEU A   3      18.025  22.900  46.312  0.75 46.13           C  
ATOM      7  CD1 LEU A   3      17.539  23.637  47.555  0.75 43.43           C  
ATOM      8  CD2 LEU A   3      18.997  21.770  46.651  0.75 44.91           C  
ATOM      9  N   GLN A   4      15.835  23.800  42.739  0.75 46.12           N  
ATOM     10  CA  GLN A   4      14.815  24.473  41.928  0.75 45.99           C  
ATOM     11  C   GLN A   4      14.005  23.468  41.101  0.75 46.04           C  
ATOM     12  O   GLN A   4      12.792  23.622  40.930  0.75 46.14           O  
ATOM     13  CB  GLN A   4      15.497  25.513  41.015  0.75 46.25           C  
ATOM     14  CG  GLN A   4      14.578  26.262  40.026  0.75 45.73           C  
ATOM     15  CD  GLN A   4      15.394  27.107  39.026  0.75 45.93           C  
ATOM     16  OE1 GLN A   4      15.466  26.773  37.819  0.75 45.09           O  
ATOM     17  NE2 GLN A   4      16.015  28.203  39.525  0.75 45.75           N  
ATOM     18  N   GLU A   5      14.687  22.438  40.598  0.75 46.06           N  
ATOM     19  CA  GLU A   5      14.051  21.407  39.781  0.75 45.82           C  
ATOM     20  C   GLU A   5      13.916  20.036  40.458  0.75 45.77           C  
ATOM     21  O   GLU A   5      13.602  19.040  39.802  0.75 45.93           O  
ATOM     22  CB  GLU A   5      14.740  21.307  38.412  0.75 45.91           C  
ATOM     23  CG  GLU A   5      14.183  22.310  37.408  0.75 45.60           C  
ATOM     24  CD  GLU A   5      12.659  22.299  37.399  0.75 45.75           C  
ATOM     25  OE1 GLU A   5      12.046  23.153  38.091  0.75 47.40           O  
ATOM     26  OE2 GLU A   5      12.074  21.404  36.746  0.75 45.13           O  
ATOM     27  N   VAL A   6      14.122  20.009  41.775  0.75 45.62           N  
ATOM     28  CA  VAL A   6      14.054  18.781  42.571  0.75 45.41           C  
ATOM     29  C   VAL A   6      13.060  18.938  43.729  0.75 44.95           C  
ATOM     30  O   VAL A   6      12.280  18.023  44.006  0.75 44.79           O  
ATOM     31  CB  VAL A   6      15.463  18.372  43.112  0.75 45.64           C  
ATOM     32  CG1 VAL A   6      15.365  17.317  44.224  0.75 46.42           C  
ATOM     33  CG2 VAL A   6      16.361  17.879  41.982  0.75 45.48           C  
ATOM     34  N   LEU A   7      13.089  20.098  44.387  0.75 44.42           N  
ATOM     35  CA  LEU A   7      12.282  20.338  45.580  0.75 44.13           C  
ATOM     36  C   LEU A   7      10.805  20.572  45.271  0.75 44.05           C  
ATOM     37  O   LEU A   7      10.443  21.338  44.373  0.75 43.66           O  
ATOM     38  CB  LEU A   7      12.852  21.490  46.425  0.75 44.05           C  
ATOM     39  CG  LEU A   7      12.352  21.780  47.861  0.75 44.34           C  
ATOM     40  CD1 LEU A   7      11.199  22.748  47.869  0.75 43.47           C  
ATOM     41  CD2 LEU A   7      11.978  20.534  48.655  0.75 43.77           C  
ATOM     42  N   HIS A   8       9.970  19.876  46.036  0.75 43.70           N  
ATOM     43  CA  HIS A   8       8.528  20.020  46.006  0.75 43.56           C  
ATOM     44  C   HIS A   8       7.968  19.170  47.133  0.75 43.46           C  
ATOM     45  O   HIS A   8       8.612  18.214  47.576  0.75 43.19           O  
ATOM     46  CB  HIS A   8       7.943  19.568  44.669  0.75 43.66           C  
ATOM     47  CG  HIS A   8       8.294  18.161  44.302  0.75 44.02           C  
ATOM     48  ND1 HIS A   8       7.578  17.073  44.754  0.75 45.08           N  
ATOM     49  CD2 HIS A   8       9.288  17.663  43.531  0.75 43.65           C  
ATOM     50  CE1 HIS A   8       8.110  15.966  44.266  0.75 44.74           C  
ATOM     51  NE2 HIS A   8       9.153  16.296  43.527  0.75 44.53           N  
ATOM     52  N   MET A   9       6.774  19.532  47.599  0.75 43.22           N  
ATOM     53  CA  MET A   9       6.062  18.718  48.576  0.75 43.47           C  
ATOM     54  C   MET A   9       5.536  17.450  47.887  0.75 43.17           C  
ATOM     55  O   MET A   9       5.432  17.401  46.652  0.75 43.18           O  
ATOM     56  CB  MET A   9       4.923  19.526  49.228  0.75 43.81           C  
ATOM     57  CG  MET A   9       5.353  20.844  49.919  0.75 43.25           C  
ATOM     58  SD  MET A   9       6.548  20.611  51.276  0.75 45.85           S  
ATOM     59  CE  MET A   9       8.131  20.676  50.418  0.75 40.33           C  
ATOM     60  N   ASN A  10       5.229  16.427  48.681  0.75 43.08           N  
ATOM     61  CA  ASN A  10       4.684  15.165  48.166  0.75 42.68           C  
ATOM     62  C   ASN A  10       3.395  15.404  47.370  0.75 42.71           C  
ATOM     63  O   ASN A  10       2.434  15.975  47.893  0.75 43.27           O  
ATOM     64  CB  ASN A  10       4.412  14.209  49.332  0.75 42.62           C  
ATOM     65  CG  ASN A  10       5.066  12.861  49.154  0.75 41.75           C  
ATOM     66  OD1 ASN A  10       5.911  12.673  48.279  0.75 40.63           O  
ATOM     67  ND2 ASN A  10       4.678  11.907  49.994  0.75 41.59           N  
ATOM     68  N   GLY A  11       3.382  14.981  46.107  0.75 42.75           N  
ATOM     69  CA  GLY A  11       2.256  15.236  45.201  0.75 42.56           C  
ATOM     70  C   GLY A  11       0.998  14.462  45.545  0.75 42.37           C  
ATOM     71  O   GLY A  11       0.307  13.963  44.661  0.75 42.05           O  
ATOM     72  N   THR A  16       1.867   9.502  52.059  1.00 50.75           N  
ATOM     73  CA  THR A  16       0.872  10.076  51.152  1.00 50.66           C  
ATOM     74  C   THR A  16       1.101  11.579  50.900  1.00 50.42           C  
ATOM     75  O   THR A  16       2.084  12.163  51.375  1.00 50.17           O  
ATOM     76  CB  THR A  16      -0.601   9.784  51.607  1.00 50.63           C  
ATOM     77  OG1 THR A  16      -0.735   9.991  53.020  1.00 50.45           O  
ATOM     78  CG2 THR A  16      -1.001   8.346  51.275  1.00 51.04           C  
ATOM     79  N   SER A  17       0.182  12.181  50.143  1.00 50.28           N  
ATOM     80  CA  SER A  17       0.349  13.526  49.588  1.00 49.84           C  
ATOM     81  C   SER A  17       0.359  14.649  50.628  1.00 49.84           C  
ATOM     82  O   SER A  17      -0.172  14.496  51.738  1.00 49.55           O  
ATOM     83  CB  SER A  17      -0.728  13.794  48.523  1.00 49.95           C  
ATOM     84  OG  SER A  17      -2.039  13.743  49.065  1.00 49.20           O  
ATOM     85  N   TYR A  18       0.985  15.769  50.255  1.00 49.59           N  
ATOM     86  CA  TYR A  18       0.917  17.004  51.029  1.00 49.60           C  
ATOM     87  C   TYR A  18      -0.533  17.501  51.096  1.00 49.67           C  
ATOM     88  O   TYR A  18      -0.978  17.985  52.144  1.00 49.88           O  
ATOM     89  CB  TYR A  18       1.840  18.087  50.453  1.00 49.41           C  
ATOM     90  CG  TYR A  18       1.825  19.381  51.251  0.50 49.55           C  
ATOM     91  CD1 TYR A  18       2.690  19.563  52.332  0.50 48.73           C  
ATOM     92  CD2 TYR A  18       0.939  20.414  50.933  0.50 48.69           C  
ATOM     93  CE1 TYR A  18       2.672  20.732  53.075  0.50 48.87           C  
ATOM     94  CE2 TYR A  18       0.911  21.594  51.672  0.50 49.37           C  
ATOM     95  CZ  TYR A  18       1.782  21.747  52.744  0.50 49.64           C  
ATOM     96  OH  TYR A  18       1.767  22.907  53.492  0.50 49.02           O  
ATOM     97  N   ALA A  19      -1.261  17.358  49.988  1.00 48.91           N  
ATOM     98  CA  ALA A  19      -2.679  17.712  49.918  1.00 48.42           C  
ATOM     99  C   ALA A  19      -3.536  17.016  50.996  1.00 48.30           C  
ATOM    100  O   ALA A  19      -4.305  17.670  51.704  1.00 47.75           O  
ATOM    101  CB  ALA A  19      -3.222  17.416  48.518  1.00 48.44           C  
ATOM    102  N   LYS A  20      -3.395  15.696  51.126  1.00 48.40           N  
ATOM    103  CA  LYS A  20      -4.221  14.934  52.067  1.00 48.76           C  
ATOM    104  C   LYS A  20      -3.863  15.194  53.542  1.00 48.99           C  
ATOM    105  O   LYS A  20      -4.740  15.126  54.418  1.00 49.29           O  
ATOM    106  CB  LYS A  20      -4.161  13.434  51.744  1.00 48.95           C  
ATOM    107  CG  LYS A  20      -4.854  12.523  52.753  1.00 49.09           C  
ATOM    108  N   ASN A  21      -2.590  15.501  53.803  1.00 48.99           N  
ATOM    109  CA  ASN A  21      -2.070  15.664  55.174  1.00 49.10           C  
ATOM    110  C   ASN A  21      -1.997  17.112  55.697  1.00 48.85           C  
ATOM    111  O   ASN A  21      -1.817  17.328  56.912  1.00 49.30           O  
ATOM    112  CB  ASN A  21      -0.719  14.946  55.315  1.00 49.13           C  
ATOM    113  CG  ASN A  21      -0.848  13.436  55.201  1.00 50.21           C  
ATOM    114  OD1 ASN A  21      -1.380  12.773  56.101  1.00 50.61           O  
ATOM    115  ND2 ASN A  21      -0.364  12.881  54.090  1.00 50.69           N  
ATOM    116  N   SER A  22      -2.176  18.075  54.782  1.00 48.32           N  
ATOM    117  CA ASER A  22      -2.189  19.521  55.079  0.50 48.08           C  
ATOM    118  CA BSER A  22      -2.164  19.506  55.120  0.50 47.94           C  
ATOM    119  C   SER A  22      -3.389  19.921  55.928  1.00 48.07           C  
ATOM    120  O   SER A  22      -4.380  19.181  56.012  1.00 48.39           O  
ATOM    121  CB ASER A  22      -2.220  20.337  53.779  0.50 47.99           C  
ATOM    122  CB BSER A  22      -2.062  20.360  53.855  0.50 47.85           C  
ATOM    123  OG ASER A  22      -0.925  20.526  53.224  0.50 47.85           O  
ATOM    124  OG BSER A  22      -3.031  19.977  52.899  0.50 46.76           O  
ATOM    125  N   SER A  23      -3.316  21.100  56.543  1.00 47.34           N  
ATOM    126  CA  SER A  23      -4.441  21.593  57.314  1.00 46.63           C  
ATOM    127  C   SER A  23      -4.361  23.078  57.495  1.00 46.23           C  
ATOM    128  O   SER A  23      -3.296  23.634  57.772  1.00 46.08           O  
ATOM    129  CB  SER A  23      -4.546  20.923  58.695  1.00 46.71           C  
ATOM    130  OG  SER A  23      -5.743  21.336  59.346  1.00 46.11           O  
ATOM    131  N   TYR A  24      -5.520  23.702  57.344  1.00 45.75           N  
ATOM    132  CA  TYR A  24      -5.690  25.106  57.596  1.00 45.66           C  
ATOM    133  C   TYR A  24      -5.334  25.402  59.054  1.00 45.54           C  
ATOM    134  O   TYR A  24      -4.763  26.456  59.360  1.00 45.67           O  
ATOM    135  CB  TYR A  24      -7.143  25.484  57.307  1.00 45.39           C  
ATOM    136  CG  TYR A  24      -7.379  26.957  57.319  1.00 45.53           C  
ATOM    137  CD1 TYR A  24      -7.924  27.574  58.434  1.00 45.13           C  
ATOM    138  CD2 TYR A  24      -7.046  27.743  56.218  1.00 44.00           C  
ATOM    139  CE1 TYR A  24      -8.139  28.931  58.454  1.00 45.29           C  
ATOM    140  CE2 TYR A  24      -7.240  29.104  56.238  1.00 43.50           C  
ATOM    141  CZ  TYR A  24      -7.794  29.689  57.363  1.00 44.39           C  
ATOM    142  OH  TYR A  24      -8.014  31.038  57.415  1.00 45.00           O  
ATOM    143  N   ASN A  25      -5.651  24.441  59.927  1.00 45.39           N  
ATOM    144  CA  ASN A  25      -5.555  24.578  61.379  1.00 45.42           C  
ATOM    145  C   ASN A  25      -4.137  24.643  61.950  1.00 45.04           C  
ATOM    146  O   ASN A  25      -3.964  24.826  63.161  1.00 45.49           O  
ATOM    147  CB  ASN A  25      -6.301  23.426  62.067  1.00 45.40           C  
ATOM    148  CG  ASN A  25      -7.812  23.508  61.913  1.00 46.52           C  
ATOM    149  OD1 ASN A  25      -8.363  24.479  61.377  1.00 49.85           O  
ATOM    150  ND2 ASN A  25      -8.495  22.477  62.393  1.00 47.77           N  
ATOM    151  N   LEU A  26      -3.125  24.481  61.106  1.00 44.25           N  
ATOM    152  CA  LEU A  26      -1.766  24.424  61.623  1.00 43.44           C  
ATOM    153  C   LEU A  26      -1.161  25.816  61.658  1.00 43.14           C  
ATOM    154  O   LEU A  26      -0.859  26.327  62.736  1.00 42.37           O  
ATOM    155  CB  LEU A  26      -0.910  23.427  60.835  1.00 43.23           C  
ATOM    156  CG  LEU A  26       0.286  22.717  61.479  1.00 43.70           C  
ATOM    157  CD1 LEU A  26      -0.051  21.991  62.779  1.00 41.11           C  
ATOM    158  CD2 LEU A  26       0.920  21.723  60.498  1.00 43.12           C  
ATOM    159  N   PHE A  27      -1.021  26.442  60.493  1.00 42.55           N  
ATOM    160  CA  PHE A  27      -0.425  27.777  60.428  1.00 43.82           C  
ATOM    161  C   PHE A  27      -1.379  28.839  59.869  1.00 44.65           C  
ATOM    162  O   PHE A  27      -1.456  29.959  60.408  1.00 44.40           O  
ATOM    163  CB  PHE A  27       0.907  27.755  59.647  1.00 42.90           C  
ATOM    164  CG  PHE A  27       1.842  26.629  60.058  1.00 42.99           C  
ATOM    165  CD1 PHE A  27       2.421  26.599  61.337  1.00 40.87           C  
ATOM    166  CD2 PHE A  27       2.155  25.613  59.164  1.00 41.70           C  
ATOM    167  CE1 PHE A  27       3.277  25.560  61.726  1.00 41.76           C  
ATOM    168  CE2 PHE A  27       3.008  24.569  59.536  1.00 42.08           C  
ATOM    169  CZ  PHE A  27       3.573  24.537  60.816  1.00 41.19           C  
ATOM    170  N   LEU A  28      -2.135  28.487  58.828  1.00 45.71           N  
ATOM    171  CA  LEU A  28      -2.999  29.480  58.151  1.00 46.69           C  
ATOM    172  C   LEU A  28      -4.016  30.192  59.049  1.00 46.45           C  
ATOM    173  O   LEU A  28      -4.177  31.415  58.924  1.00 46.06           O  
ATOM    174  CB  LEU A  28      -3.652  28.906  56.880  1.00 47.31           C  
ATOM    175  CG  LEU A  28      -2.697  28.554  55.742  1.00 48.96           C  
ATOM    176  CD1 LEU A  28      -3.423  27.920  54.553  1.00 51.07           C  
ATOM    177  CD2 LEU A  28      -1.896  29.774  55.278  1.00 49.20           C  
ATOM    178  N   ILE A  29      -4.662  29.482  59.981  1.00 47.11           N  
ATOM    179  CA  ILE A  29      -5.549  30.173  60.953  1.00 47.17           C  
ATOM    180  C   ILE A  29      -4.844  31.229  61.815  1.00 46.93           C  
ATOM    181  O   ILE A  29      -5.469  32.185  62.260  1.00 47.51           O  
ATOM    182  CB  ILE A  29      -6.322  29.244  61.930  1.00 48.14           C  
ATOM    183  CG1 ILE A  29      -5.633  27.906  62.118  1.00 48.31           C  
ATOM    184  CG2 ILE A  29      -7.829  29.180  61.604  1.00 48.63           C  
ATOM    185  CD1 ILE A  29      -4.731  27.901  63.323  1.00 51.28           C  
ATOM    186  N   ARG A  30      -3.555  31.051  62.067  1.00 46.49           N  
ATOM    187  CA  ARG A  30      -2.793  32.041  62.818  1.00 45.86           C  
ATOM    188  C   ARG A  30      -2.425  33.224  61.916  1.00 45.11           C  
ATOM    189  O   ARG A  30      -2.363  34.366  62.373  1.00 45.72           O  
ATOM    190  CB  ARG A  30      -1.541  31.410  63.430  1.00 45.85           C  
ATOM    191  CG  ARG A  30      -1.779  30.072  64.143  1.00 47.13           C  
ATOM    192  CD  ARG A  30      -2.793  30.159  65.306  1.00 49.33           C  
ATOM    193  NE  ARG A  30      -2.291  30.836  66.505  1.00 48.96           N  
ATOM    194  CZ  ARG A  30      -1.511  30.276  67.426  1.00 47.78           C  
ATOM    195  NH1 ARG A  30      -1.096  29.017  67.291  1.00 45.12           N  
ATOM    196  NH2 ARG A  30      -1.136  30.989  68.486  1.00 45.01           N  
ATOM    197  N   VAL A  31      -2.203  32.932  60.637  1.00 44.02           N  
ATOM    198  CA  VAL A  31      -1.875  33.937  59.617  1.00 42.98           C  
ATOM    199  C   VAL A  31      -3.090  34.817  59.296  1.00 43.21           C  
ATOM    200  O   VAL A  31      -2.961  36.045  59.192  1.00 42.97           O  
ATOM    201  CB  VAL A  31      -1.373  33.262  58.285  1.00 42.93           C  
ATOM    202  CG1 VAL A  31      -1.144  34.301  57.201  1.00 43.05           C  
ATOM    203  CG2 VAL A  31      -0.099  32.455  58.505  1.00 41.17           C  
ATOM    204  N   LYS A  32      -4.252  34.176  59.139  1.00 43.12           N  
ATOM    205  CA  LYS A  32      -5.510  34.829  58.749  1.00 44.48           C  
ATOM    206  C   LYS A  32      -5.779  36.218  59.358  1.00 44.03           C  
ATOM    207  O   LYS A  32      -5.958  37.165  58.608  1.00 45.01           O  
ATOM    208  CB  LYS A  32      -6.716  33.906  58.994  1.00 44.99           C  
ATOM    209  CG  LYS A  32      -8.018  34.466  58.401  1.00 48.63           C  
ATOM    210  CD  LYS A  32      -9.193  33.598  58.762  1.00 54.66           C  
ATOM    211  CE  LYS A  32     -10.246  33.637  57.667  1.00 55.94           C  
ATOM    212  NZ  LYS A  32     -11.158  34.806  57.826  1.00 56.87           N  
ATOM    213  N   PRO A  33      -5.833  36.347  60.711  1.00 43.39           N  
ATOM    214  CA  PRO A  33      -6.094  37.690  61.235  1.00 42.46           C  
ATOM    215  C   PRO A  33      -5.053  38.744  60.815  1.00 41.85           C  
ATOM    216  O   PRO A  33      -5.412  39.922  60.618  1.00 40.72           O  
ATOM    217  CB  PRO A  33      -6.086  37.494  62.763  1.00 42.55           C  
ATOM    218  CG  PRO A  33      -5.325  36.201  62.981  1.00 43.42           C  
ATOM    219  CD  PRO A  33      -5.671  35.357  61.793  1.00 43.07           C  
ATOM    220  N   VAL A  34      -3.788  38.334  60.703  1.00 40.42           N  
ATOM    221  CA  VAL A  34      -2.712  39.245  60.331  1.00 40.67           C  
ATOM    222  C   VAL A  34      -2.817  39.593  58.828  1.00 41.30           C  
ATOM    223  O   VAL A  34      -2.595  40.737  58.446  1.00 40.81           O  
ATOM    224  CB  VAL A  34      -1.324  38.656  60.661  1.00 40.84           C  
ATOM    225  CG1 VAL A  34      -0.192  39.621  60.254  1.00 40.58           C  
ATOM    226  CG2 VAL A  34      -1.229  38.299  62.142  1.00 39.96           C  
ATOM    227  N   LEU A  35      -3.222  38.622  58.042  1.00 41.85           N  
ATOM    228  CA  LEU A  35      -3.473  38.766  56.638  1.00 42.75           C  
ATOM    229  C   LEU A  35      -4.590  39.752  56.431  1.00 43.52           C  
ATOM    230  O   LEU A  35      -4.505  40.620  55.607  1.00 43.02           O  
ATOM    231  CB  LEU A  35      -3.815  37.419  56.018  1.00 42.75           C  
ATOM    232  CG  LEU A  35      -4.262  37.318  54.563  1.00 44.24           C  
ATOM    233  CD1 LEU A  35      -3.240  37.728  53.604  1.00 45.94           C  
ATOM    234  CD2 LEU A  35      -4.768  36.031  54.204  1.00 45.54           C  
ATOM    235  N   GLU A  36      -5.626  39.605  57.225  1.00 44.50           N  
ATOM    236  CA  GLU A  36      -6.820  40.414  57.111  1.00 45.43           C  
ATOM    237  C   GLU A  36      -6.514  41.885  57.377  1.00 45.83           C  
ATOM    238  O   GLU A  36      -6.979  42.769  56.638  1.00 45.55           O  
ATOM    239  CB  GLU A  36      -7.915  39.905  58.048  1.00 46.34           C  
ATOM    240  CG  GLU A  36      -8.521  38.551  57.653  1.00 49.87           C  
ATOM    241  CD  GLU A  36     -10.046  38.539  57.748  1.00 55.20           C  
ATOM    242  OE1 GLU A  36     -10.597  38.788  58.854  1.00 56.26           O  
ATOM    243  OE2 GLU A  36     -10.695  38.299  56.698  1.00 57.22           O  
ATOM    244  N   GLN A  37      -5.716  42.129  58.415  1.00 45.89           N  
ATOM    245  CA  GLN A  37      -5.361  43.475  58.848  1.00 47.01           C  
ATOM    246  C   GLN A  37      -4.442  44.099  57.814  1.00 46.79           C  
ATOM    247  O   GLN A  37      -4.593  45.261  57.460  1.00 46.75           O  
ATOM    248  CB  GLN A  37      -4.684  43.422  60.227  1.00 46.88           C  
ATOM    249  CG  GLN A  37      -4.044  44.720  60.690  1.00 47.98           C  
ATOM    250  CD  GLN A  37      -3.591  44.662  62.140  1.00 48.58           C  
ATOM    251  OE1 GLN A  37      -4.400  44.484  63.047  1.00 50.87           O  
ATOM    252  NE2 GLN A  37      -2.292  44.819  62.363  1.00 51.58           N  
ATOM    253  N   CYS A  38      -3.516  43.294  57.304  1.00 47.47           N  
ATOM    254  CA  CYS A  38      -2.583  43.745  56.282  1.00 46.66           C  
ATOM    255  C   CYS A  38      -3.318  44.230  55.027  1.00 45.46           C  
ATOM    256  O   CYS A  38      -3.105  45.363  54.575  1.00 45.38           O  
ATOM    257  CB  CYS A  38      -1.605  42.631  55.943  1.00 47.34           C  
ATOM    258  SG  CYS A  38      -0.306  43.171  54.872  1.00 50.70           S  
ATOM    259  N   ILE A  39      -4.209  43.392  54.501  1.00 43.29           N  
ATOM    260  CA  ILE A  39      -4.977  43.732  53.315  1.00 42.31           C  
ATOM    261  C   ILE A  39      -5.887  44.968  53.488  1.00 42.08           C  
ATOM    262  O   ILE A  39      -5.891  45.844  52.635  1.00 41.63           O  
ATOM    263  CB  ILE A  39      -5.727  42.508  52.754  1.00 42.40           C  
ATOM    264  CG1 ILE A  39      -4.736  41.619  51.985  1.00 41.89           C  
ATOM    265  CG2 ILE A  39      -6.895  42.934  51.842  1.00 41.36           C  
ATOM    266  CD1 ILE A  39      -5.167  40.185  51.882  1.00 43.33           C  
ATOM    267  N   GLN A  40      -6.621  45.039  54.595  1.00 42.49           N  
ATOM    268  CA  GLN A  40      -7.451  46.217  54.926  1.00 43.43           C  
ATOM    269  C   GLN A  40      -6.646  47.515  55.019  1.00 43.23           C  
ATOM    270  O   GLN A  40      -7.116  48.579  54.605  1.00 43.61           O  
ATOM    271  CB  GLN A  40      -8.229  45.961  56.221  1.00 43.82           C  
ATOM    272  CG  GLN A  40      -9.310  44.884  56.061  1.00 47.62           C  
ATOM    273  CD  GLN A  40     -10.494  45.365  55.227  1.00 51.50           C  
ATOM    274  OE1 GLN A  40     -11.221  46.265  55.639  1.00 54.06           O  
ATOM    275  NE2 GLN A  40     -10.692  44.763  54.056  1.00 51.66           N  
ATOM    276  N   GLU A  41      -5.434  47.424  55.562  1.00 43.45           N  
ATOM    277  CA  GLU A  41      -4.530  48.572  55.666  1.00 43.59           C  
ATOM    278  C   GLU A  41      -4.050  49.005  54.287  1.00 43.05           C  
ATOM    279  O   GLU A  41      -3.914  50.206  54.010  1.00 42.67           O  
ATOM    280  CB  GLU A  41      -3.343  48.265  56.581  1.00 43.78           C  
ATOM    281  CG  GLU A  41      -3.764  47.793  57.973  1.00 46.63           C  
ATOM    282  CD  GLU A  41      -2.696  47.967  59.040  1.00 47.87           C  
ATOM    283  OE1 GLU A  41      -1.498  48.004  58.703  1.00 48.31           O  
ATOM    284  OE2 GLU A  41      -3.068  48.081  60.227  1.00 48.85           O  
ATOM    285  N   LEU A  42      -3.832  48.029  53.415  1.00 42.89           N  
ATOM    286  CA  LEU A  42      -3.452  48.298  52.033  1.00 42.60           C  
ATOM    287  C   LEU A  42      -4.503  49.073  51.235  1.00 42.58           C  
ATOM    288  O   LEU A  42      -4.172  50.013  50.518  1.00 41.27           O  
ATOM    289  CB  LEU A  42      -3.125  46.991  51.324  1.00 43.57           C  
ATOM    290  CG  LEU A  42      -1.683  46.531  51.449  1.00 42.51           C  
ATOM    291  CD1 LEU A  42      -1.563  45.094  51.029  1.00 41.35           C  
ATOM    292  CD2 LEU A  42      -0.853  47.393  50.563  1.00 43.32           C  
ATOM    293  N   LEU A  43      -5.759  48.653  51.339  1.00 43.03           N  
ATOM    294  CA  LEU A  43      -6.859  49.342  50.656  1.00 44.21           C  
ATOM    295  C   LEU A  43      -6.995  50.776  51.154  1.00 44.02           C  
ATOM    296  O   LEU A  43      -7.246  51.679  50.372  1.00 45.24           O  
ATOM    297  CB  LEU A  43      -8.183  48.607  50.865  1.00 44.89           C  
ATOM    298  CG  LEU A  43      -8.333  47.171  50.374  1.00 45.40           C  
ATOM    299  CD1 LEU A  43      -9.484  46.524  51.121  1.00 46.34           C  
ATOM    300  CD2 LEU A  43      -8.553  47.130  48.877  1.00 48.03           C  
ATOM    301  N   ARG A  44      -6.799  50.964  52.456  1.00 43.86           N  
ATOM    302  CA  ARG A  44      -6.894  52.261  53.102  1.00 43.48           C  
ATOM    303  C   ARG A  44      -5.746  53.195  52.732  1.00 43.13           C  
ATOM    304  O   ARG A  44      -5.931  54.405  52.674  1.00 42.88           O  
ATOM    305  CB  ARG A  44      -6.994  52.078  54.611  1.00 43.86           C  
ATOM    306  CG  ARG A  44      -8.397  51.721  55.024  1.00 45.78           C  
ATOM    307  CD  ARG A  44      -8.518  51.053  56.387  1.00 46.50           C  
ATOM    308  NE  ARG A  44      -9.934  50.807  56.668  1.00 49.26           N  
ATOM    309  CZ  ARG A  44     -10.711  49.985  55.957  1.00 51.10           C  
ATOM    310  NH1 ARG A  44     -10.214  49.300  54.923  1.00 51.43           N  
ATOM    311  NH2 ARG A  44     -11.990  49.846  56.276  1.00 52.31           N  
ATOM    312  N   ALA A  45      -4.586  52.611  52.444  1.00 42.28           N  
ATOM    313  CA  ALA A  45      -3.391  53.329  51.982  1.00 42.09           C  
ATOM    314  C   ALA A  45      -3.499  53.869  50.543  1.00 41.86           C  
ATOM    315  O   ALA A  45      -2.666  54.681  50.117  1.00 41.73           O  
ATOM    316  CB  ALA A  45      -2.163  52.423  52.114  1.00 42.29           C  
ATOM    317  N   ASN A  46      -4.517  53.418  49.808  1.00 41.46           N  
ATOM    318  CA  ASN A  46      -4.831  53.926  48.466  1.00 40.97           C  
ATOM    319  C   ASN A  46      -3.641  53.812  47.489  1.00 40.97           C  
ATOM    320  O   ASN A  46      -3.297  54.778  46.794  1.00 40.83           O  
ATOM    321  CB  ASN A  46      -5.379  55.375  48.552  1.00 41.67           C  
ATOM    322  CG  ASN A  46      -6.169  55.785  47.320  1.00 42.86           C  
ATOM    323  OD1 ASN A  46      -6.774  54.950  46.655  1.00 44.30           O  
ATOM    324  ND2 ASN A  46      -6.169  57.080  47.012  1.00 44.61           N  
ATOM    325  N   LEU A  47      -3.005  52.653  47.419  1.00 40.77           N  
ATOM    326  CA  LEU A  47      -1.905  52.455  46.483  1.00 40.79           C  
ATOM    327  C   LEU A  47      -2.370  52.664  45.030  1.00 41.57           C  
ATOM    328  O   LEU A  47      -3.477  52.368  44.740  1.00 40.46           O  
ATOM    329  CB  LEU A  47      -1.318  51.050  46.699  1.00 40.74           C  
ATOM    330  CG  LEU A  47      -0.303  50.748  47.809  1.00 40.43           C  
ATOM    331  CD1 LEU A  47      -0.770  51.025  49.160  1.00 37.72           C  
ATOM    332  CD2 LEU A  47       0.209  49.333  47.731  1.00 38.44           C  
ATOM    333  N   PRO A  48      -1.531  53.134  44.111  1.00 42.92           N  
ATOM    334  CA  PRO A  48      -2.054  53.371  42.765  1.00 44.24           C  
ATOM    335  C   PRO A  48      -2.745  52.151  42.165  1.00 44.49           C  
ATOM    336  O   PRO A  48      -2.231  51.033  42.242  1.00 45.24           O  
ATOM    337  CB  PRO A  48      -0.811  53.773  41.934  1.00 44.32           C  
ATOM    338  CG  PRO A  48       0.367  53.488  42.768  1.00 43.81           C  
ATOM    339  CD  PRO A  48      -0.107  53.503  44.219  1.00 43.48           C  
ATOM    340  N   ASN A  49      -3.932  52.377  41.611  1.00 45.62           N  
ATOM    341  CA  ASN A  49      -4.714  51.336  40.923  1.00 46.72           C  
ATOM    342  C   ASN A  49      -5.325  50.206  41.777  1.00 46.03           C  
ATOM    343  O   ASN A  49      -6.065  49.385  41.262  1.00 46.54           O  
ATOM    344  CB  ASN A  49      -3.919  50.781  39.736  1.00 47.19           C  
ATOM    345  CG  ASN A  49      -3.472  51.885  38.785  1.00 50.47           C  
ATOM    346  OD1 ASN A  49      -4.273  52.746  38.400  1.00 53.20           O  
ATOM    347  ND2 ASN A  49      -2.190  51.879  38.416  1.00 52.23           N  
ATOM    348  N   ILE A  50      -5.060  50.193  43.080  1.00 45.59           N  
ATOM    349  CA  ILE A  50      -5.552  49.122  43.955  1.00 45.12           C  
ATOM    350  C   ILE A  50      -7.094  48.959  43.995  1.00 45.60           C  
ATOM    351  O   ILE A  50      -7.608  47.861  44.206  1.00 45.09           O  
ATOM    352  CB  ILE A  50      -4.950  49.247  45.394  1.00 45.55           C  
ATOM    353  CG1 ILE A  50      -4.887  47.875  46.084  1.00 43.88           C  
ATOM    354  CG2 ILE A  50      -5.695  50.305  46.225  1.00 44.09           C  
ATOM    355  CD1 ILE A  50      -4.086  47.871  47.368  1.00 44.19           C  
ATOM    356  N   ASN A  51      -7.828  50.044  43.789  1.00 45.62           N  
ATOM    357  CA  ASN A  51      -9.280  49.949  43.738  1.00 46.16           C  
ATOM    358  C   ASN A  51      -9.828  49.639  42.339  1.00 45.70           C  
ATOM    359  O   ASN A  51     -11.030  49.497  42.164  1.00 46.94           O  
ATOM    360  CB  ASN A  51      -9.930  51.191  44.365  1.00 46.54           C  
ATOM    361  CG  ASN A  51      -9.513  51.392  45.816  1.00 48.29           C  
ATOM    362  OD1 ASN A  51      -9.475  50.441  46.620  1.00 48.94           O  
ATOM    363  ND2 ASN A  51      -9.184  52.626  46.159  1.00 49.17           N  
ATOM    364  N   LYS A  52      -8.941  49.544  41.352  1.00 45.38           N  
ATOM    365  CA  LYS A  52      -9.285  49.023  40.025  1.00 43.95           C  
ATOM    366  C   LYS A  52      -8.935  47.533  40.017  1.00 42.97           C  
ATOM    367  O   LYS A  52      -9.816  46.684  39.893  1.00 42.33           O  
ATOM    368  CB  LYS A  52      -8.501  49.749  38.925  1.00 43.75           C  
ATOM    369  N   CYS A  53      -7.647  47.237  40.164  1.00 42.33           N  
ATOM    370  CA  CYS A  53      -7.159  45.860  40.216  1.00 41.26           C  
ATOM    371  C   CYS A  53      -6.131  45.643  41.325  1.00 40.89           C  
ATOM    372  O   CYS A  53      -5.045  46.231  41.303  1.00 40.98           O  
ATOM    373  CB  CYS A  53      -6.578  45.429  38.866  1.00 41.51           C  
ATOM    374  SG  CYS A  53      -6.210  43.698  38.825  1.00 44.22           S  
ATOM    375  N   PHE A  54      -6.484  44.772  42.267  1.00 39.91           N  
ATOM    376  CA  PHE A  54      -5.634  44.384  43.404  1.00 40.21           C  
ATOM    377  C   PHE A  54      -4.767  43.204  42.966  1.00 39.98           C  
ATOM    378  O   PHE A  54      -5.264  42.107  42.777  1.00 38.85           O  
ATOM    379  CB  PHE A  54      -6.519  43.999  44.610  1.00 39.86           C  
ATOM    380  CG  PHE A  54      -5.814  44.036  45.959  1.00 40.91           C  
ATOM    381  CD1 PHE A  54      -4.583  43.419  46.155  1.00 42.26           C  
ATOM    382  CD2 PHE A  54      -6.430  44.641  47.058  1.00 43.76           C  
ATOM    383  CE1 PHE A  54      -3.946  43.433  47.405  1.00 42.38           C  
ATOM    384  CE2 PHE A  54      -5.800  44.647  48.324  1.00 44.34           C  
ATOM    385  CZ  PHE A  54      -4.543  44.033  48.474  1.00 43.81           C  
ATOM    386  N   LYS A  55      -3.473  43.446  42.745  1.00 40.20           N  
ATOM    387  CA  LYS A  55      -2.577  42.383  42.244  1.00 40.65           C  
ATOM    388  C   LYS A  55      -1.803  41.726  43.371  1.00 40.94           C  
ATOM    389  O   LYS A  55      -1.113  42.433  44.129  1.00 40.54           O  
ATOM    390  CB  LYS A  55      -1.634  42.952  41.172  1.00 41.63           C  
ATOM    391  CG  LYS A  55      -2.405  43.400  39.932  1.00 43.84           C  
ATOM    392  CD  LYS A  55      -1.541  44.127  38.920  1.00 47.62           C  
ATOM    393  CE  LYS A  55      -0.524  43.145  38.279  1.00 48.29           C  
ATOM    394  NZ  LYS A  55       0.450  43.897  37.423  0.50 47.81           N  
ATOM    395  N   VAL A  56      -1.935  40.385  43.493  1.00 40.51           N  
ATOM    396  CA  VAL A  56      -1.431  39.624  44.624  1.00 40.98           C  
ATOM    397  C   VAL A  56      -0.693  38.376  44.120  1.00 41.70           C  
ATOM    398  O   VAL A  56      -1.134  37.759  43.159  1.00 41.71           O  
ATOM    399  CB  VAL A  56      -2.580  39.085  45.531  1.00 41.36           C  
ATOM    400  CG1 VAL A  56      -1.999  38.386  46.765  1.00 40.81           C  
ATOM    401  CG2 VAL A  56      -3.518  40.197  45.954  1.00 41.00           C  
ATOM    402  N   GLY A  57       0.431  38.043  44.761  1.00 42.15           N  
ATOM    403  CA  GLY A  57       1.191  36.810  44.495  1.00 42.26           C  
ATOM    404  C   GLY A  57       1.232  35.923  45.735  1.00 43.68           C  
ATOM    405  O   GLY A  57       1.427  36.424  46.850  1.00 44.16           O  
ATOM    406  N   ASP A  58       1.021  34.613  45.567  1.00 44.11           N  
ATOM    407  CA  ASP A  58       1.245  33.643  46.664  1.00 45.15           C  
ATOM    408  C   ASP A  58       2.489  32.826  46.315  1.00 45.08           C  
ATOM    409  O   ASP A  58       2.507  32.122  45.324  1.00 43.47           O  
ATOM    410  CB  ASP A  58       0.038  32.717  46.913  1.00 45.49           C  
ATOM    411  CG  ASP A  58       0.220  31.818  48.158  1.00 48.70           C  
ATOM    412  OD1 ASP A  58       0.952  32.186  49.118  1.00 46.97           O  
ATOM    413  OD2 ASP A  58      -0.371  30.713  48.169  1.00 52.65           O  
ATOM    414  N   LEU A  59       3.546  33.017  47.104  1.00 45.48           N  
ATOM    415  CA  LEU A  59       4.884  32.567  46.757  1.00 45.93           C  
ATOM    416  C   LEU A  59       5.127  31.303  47.555  1.00 46.59           C  
ATOM    417  O   LEU A  59       5.309  31.372  48.785  1.00 47.10           O  
ATOM    418  CB  LEU A  59       5.933  33.626  47.127  1.00 45.77           C  
ATOM    419  CG  LEU A  59       5.815  35.046  46.571  1.00 46.99           C  
ATOM    420  CD1 LEU A  59       7.087  35.859  46.861  1.00 45.66           C  
ATOM    421  CD2 LEU A  59       5.503  35.047  45.074  1.00 45.41           C  
ATOM    422  N   GLY A  60       5.074  30.175  46.852  1.00 47.13           N  
ATOM    423  CA  GLY A  60       5.218  28.814  47.418  1.00 48.86           C  
ATOM    424  C   GLY A  60       3.844  28.260  47.770  1.00 49.22           C  
ATOM    425  O   GLY A  60       3.607  27.787  48.896  1.00 49.94           O  
ATOM    426  N   CYS A  61       2.934  28.336  46.807  1.00 49.87           N  
ATOM    427  CA  CYS A  61       1.536  27.973  47.017  1.00 51.67           C  
ATOM    428  C   CYS A  61       1.344  26.476  47.236  1.00 52.17           C  
ATOM    429  O   CYS A  61       0.345  26.069  47.844  1.00 52.23           O  
ATOM    430  CB  CYS A  61       0.670  28.432  45.835  1.00 52.07           C  
ATOM    431  SG  CYS A  61       1.140  27.727  44.236  1.00 53.82           S  
ATOM    432  N   ALA A  62       2.291  25.681  46.743  1.00 52.42           N  
ATOM    433  CA  ALA A  62       2.167  24.206  46.694  1.00 54.12           C  
ATOM    434  C   ALA A  62       0.901  23.789  45.936  1.00 54.90           C  
ATOM    435  O   ALA A  62       0.562  24.369  44.905  1.00 55.65           O  
ATOM    436  CB  ALA A  62       2.201  23.590  48.118  1.00 52.89           C  
ATOM    437  N   SER A  63       0.211  22.789  46.467  1.00 56.84           N  
ATOM    438  CA  SER A  63      -1.097  22.337  45.990  1.00 57.66           C  
ATOM    439  C   SER A  63      -1.916  21.901  47.201  1.00 57.74           C  
ATOM    440  O   SER A  63      -1.415  21.874  48.347  1.00 58.22           O  
ATOM    441  CB  SER A  63      -0.948  21.142  45.045  1.00 58.04           C  
ATOM    442  OG  SER A  63      -0.145  21.476  43.925  1.00 58.84           O  
ATOM    443  N   GLY A  64      -3.163  21.532  46.942  1.00 57.02           N  
ATOM    444  CA  GLY A  64      -4.031  21.005  47.971  1.00 56.54           C  
ATOM    445  C   GLY A  64      -4.973  22.056  48.512  1.00 56.60           C  
ATOM    446  O   GLY A  64      -5.026  23.190  47.989  1.00 56.05           O  
ATOM    447  N   PRO A  65      -5.726  21.700  49.563  1.00 56.03           N  
ATOM    448  CA  PRO A  65      -6.689  22.632  50.137  1.00 55.91           C  
ATOM    449  C   PRO A  65      -6.060  23.964  50.539  1.00 55.36           C  
ATOM    450  O   PRO A  65      -6.674  25.001  50.318  1.00 55.25           O  
ATOM    451  CB  PRO A  65      -7.185  21.885  51.369  1.00 55.73           C  
ATOM    452  CG  PRO A  65      -7.039  20.448  50.975  1.00 56.61           C  
ATOM    453  CD  PRO A  65      -5.739  20.408  50.273  1.00 56.21           C  
ATOM    454  N   ASN A  66      -4.855  23.926  51.118  1.00 54.19           N  
ATOM    455  CA  ASN A  66      -4.176  25.145  51.553  1.00 53.73           C  
ATOM    456  C   ASN A  66      -4.017  26.213  50.467  1.00 52.74           C  
ATOM    457  O   ASN A  66      -4.106  27.404  50.767  1.00 52.99           O  
ATOM    458  CB  ASN A  66      -2.825  24.825  52.191  1.00 53.58           C  
ATOM    459  CG  ASN A  66      -2.964  24.238  53.595  1.00 53.77           C  
ATOM    460  OD1 ASN A  66      -4.062  24.149  54.136  1.00 53.36           O  
ATOM    461  ND2 ASN A  66      -1.839  23.833  54.187  1.00 53.31           N  
ATOM    462  N   THR A  67      -3.770  25.783  49.233  1.00 51.87           N  
ATOM    463  CA  THR A  67      -3.665  26.700  48.069  1.00 52.12           C  
ATOM    464  C   THR A  67      -4.962  27.507  47.921  1.00 51.15           C  
ATOM    465  O   THR A  67      -4.946  28.717  47.951  1.00 51.40           O  
ATOM    466  CB  THR A  67      -3.358  25.939  46.772  1.00 51.26           C  
ATOM    467  OG1 THR A  67      -2.210  25.115  46.982  1.00 54.08           O  
ATOM    468  CG2 THR A  67      -3.057  26.907  45.615  1.00 51.91           C  
ATOM    469  N   PHE A  68      -6.079  26.793  47.821  1.00 51.10           N  
ATOM    470  CA  PHE A  68      -7.406  27.379  47.784  1.00 49.67           C  
ATOM    471  C   PHE A  68      -7.817  28.108  49.053  1.00 48.98           C  
ATOM    472  O   PHE A  68      -8.452  29.167  48.974  1.00 48.47           O  
ATOM    473  CB  PHE A  68      -8.427  26.329  47.369  1.00 49.95           C  
ATOM    474  CG  PHE A  68      -8.325  25.944  45.918  1.00 50.75           C  
ATOM    475  CD1 PHE A  68      -8.827  26.781  44.923  1.00 51.51           C  
ATOM    476  CD2 PHE A  68      -7.720  24.753  45.536  1.00 52.14           C  
ATOM    477  CE1 PHE A  68      -8.727  26.435  43.574  1.00 50.73           C  
ATOM    478  CE2 PHE A  68      -7.623  24.402  44.190  1.00 51.23           C  
ATOM    479  CZ  PHE A  68      -8.128  25.236  43.212  1.00 50.99           C  
ATOM    480  N   SER A  69      -7.425  27.590  50.220  1.00 47.54           N  
ATOM    481  CA  SER A  69      -7.722  28.276  51.474  1.00 47.02           C  
ATOM    482  C   SER A  69      -7.031  29.637  51.557  1.00 46.54           C  
ATOM    483  O   SER A  69      -7.624  30.611  52.014  1.00 45.39           O  
ATOM    484  CB  SER A  69      -7.356  27.402  52.691  1.00 46.83           C  
ATOM    485  OG  SER A  69      -8.039  26.155  52.659  1.00 47.02           O  
ATOM    486  N   THR A  70      -5.782  29.707  51.098  1.00 47.06           N  
ATOM    487  CA  THR A  70      -5.069  30.982  51.072  1.00 47.69           C  
ATOM    488  C   THR A  70      -5.751  31.976  50.111  1.00 47.53           C  
ATOM    489  O   THR A  70      -5.980  33.120  50.482  1.00 47.91           O  
ATOM    490  CB  THR A  70      -3.543  30.802  50.801  1.00 47.77           C  
ATOM    491  OG1 THR A  70      -2.921  30.306  51.994  1.00 49.80           O  
ATOM    492  CG2 THR A  70      -2.858  32.147  50.447  1.00 46.90           C  
ATOM    493  N   VAL A  71      -6.102  31.532  48.907  1.00 48.27           N  
ATOM    494  CA  VAL A  71      -6.848  32.397  47.952  1.00 48.21           C  
ATOM    495  C   VAL A  71      -8.149  32.908  48.558  1.00 48.04           C  
ATOM    496  O   VAL A  71      -8.436  34.122  48.543  1.00 48.39           O  
ATOM    497  CB  VAL A  71      -7.133  31.692  46.596  1.00 47.90           C  
ATOM    498  CG1 VAL A  71      -7.946  32.619  45.664  1.00 48.61           C  
ATOM    499  CG2 VAL A  71      -5.835  31.295  45.900  1.00 48.30           C  
ATOM    500  N   ARG A  72      -8.937  31.986  49.113  1.00 48.59           N  
ATOM    501  CA  ARG A  72     -10.174  32.350  49.819  1.00 48.12           C  
ATOM    502  C   ARG A  72      -9.950  33.410  50.891  1.00 47.77           C  
ATOM    503  O   ARG A  72     -10.635  34.426  50.903  1.00 46.63           O  
ATOM    504  CB  ARG A  72     -10.832  31.123  50.434  1.00 49.05           C  
ATOM    505  CG  ARG A  72     -11.847  30.467  49.528  1.00 51.75           C  
ATOM    506  CD  ARG A  72     -12.709  29.439  50.266  1.00 55.93           C  
ATOM    507  NE  ARG A  72     -12.814  28.242  49.436  1.00 59.20           N  
ATOM    508  CZ  ARG A  72     -12.028  27.172  49.550  1.00 61.91           C  
ATOM    509  NH1 ARG A  72     -11.098  27.112  50.500  1.00 62.45           N  
ATOM    510  NH2 ARG A  72     -12.192  26.140  48.729  1.00 62.90           N  
ATOM    511  N   ASP A  73      -8.993  33.173  51.793  1.00 47.29           N  
ATOM    512  CA  ASP A  73      -8.633  34.183  52.794  1.00 47.13           C  
ATOM    513  C   ASP A  73      -8.292  35.549  52.178  1.00 46.53           C  
ATOM    514  O   ASP A  73      -8.761  36.580  52.659  1.00 47.33           O  
ATOM    515  CB  ASP A  73      -7.489  33.683  53.694  1.00 46.78           C  
ATOM    516  CG  ASP A  73      -7.958  32.680  54.745  1.00 48.80           C  
ATOM    517  OD1 ASP A  73      -9.161  32.310  54.758  0.50 47.88           O  
ATOM    518  OD2 ASP A  73      -7.111  32.256  55.566  0.50 48.21           O  
ATOM    519  N   ILE A  74      -7.492  35.565  51.114  1.00 46.40           N  
ATOM    520  CA  ILE A  74      -7.175  36.823  50.406  1.00 45.09           C  
ATOM    521  C   ILE A  74      -8.437  37.512  49.902  1.00 45.08           C  
ATOM    522  O   ILE A  74      -8.690  38.689  50.200  1.00 44.42           O  
ATOM    523  CB  ILE A  74      -6.152  36.605  49.235  1.00 45.88           C  
ATOM    524  CG1 ILE A  74      -4.812  36.127  49.787  1.00 44.85           C  
ATOM    525  CG2 ILE A  74      -5.950  37.906  48.442  1.00 43.25           C  
ATOM    526  CD1 ILE A  74      -3.841  35.568  48.739  1.00 44.44           C  
ATOM    527  N   VAL A  75      -9.237  36.755  49.159  1.00 45.52           N  
ATOM    528  CA  VAL A  75     -10.452  37.271  48.524  1.00 45.75           C  
ATOM    529  C   VAL A  75     -11.457  37.803  49.559  1.00 46.62           C  
ATOM    530  O   VAL A  75     -11.974  38.911  49.419  1.00 45.96           O  
ATOM    531  CB  VAL A  75     -11.097  36.208  47.576  1.00 45.75           C  
ATOM    532  CG1 VAL A  75     -12.422  36.708  47.033  1.00 45.94           C  
ATOM    533  CG2 VAL A  75     -10.134  35.855  46.414  1.00 44.70           C  
ATOM    534  N   GLN A  76     -11.705  37.026  50.614  1.00 46.93           N  
ATOM    535  CA  GLN A  76     -12.597  37.462  51.680  1.00 47.59           C  
ATOM    536  C   GLN A  76     -12.038  38.695  52.397  1.00 47.36           C  
ATOM    537  O   GLN A  76     -12.797  39.589  52.742  1.00 47.14           O  
ATOM    538  CB  GLN A  76     -12.855  36.325  52.684  1.00 47.70           C  
ATOM    539  CG  GLN A  76     -13.582  35.095  52.109  1.00 48.84           C  
ATOM    540  CD  GLN A  76     -13.541  33.864  53.039  1.00 48.71           C  
ATOM    541  OE1 GLN A  76     -12.537  33.600  53.713  0.50 49.35           O  
ATOM    542  NE2 GLN A  76     -14.631  33.107  53.060  0.50 48.82           N  
ATOM    543  N   SER A  77     -10.721  38.747  52.612  1.00 47.20           N  
ATOM    544  CA  SER A  77     -10.090  39.927  53.223  1.00 48.08           C  
ATOM    545  C   SER A  77     -10.326  41.200  52.394  1.00 48.49           C  
ATOM    546  O   SER A  77     -10.677  42.247  52.935  1.00 48.80           O  
ATOM    547  CB  SER A  77      -8.587  39.731  53.444  1.00 47.49           C  
ATOM    548  OG  SER A  77      -8.286  38.484  54.035  1.00 49.96           O  
ATOM    549  N   ILE A  78     -10.147  41.091  51.083  1.00 49.50           N  
ATOM    550  CA  ILE A  78     -10.367  42.208  50.144  1.00 50.64           C  
ATOM    551  C   ILE A  78     -11.827  42.675  50.159  1.00 51.88           C  
ATOM    552  O   ILE A  78     -12.101  43.883  50.117  1.00 52.14           O  
ATOM    553  CB  ILE A  78      -9.892  41.836  48.689  1.00 49.96           C  
ATOM    554  CG1 ILE A  78      -8.365  41.747  48.633  1.00 49.49           C  
ATOM    555  CG2 ILE A  78     -10.380  42.850  47.663  1.00 50.16           C  
ATOM    556  CD1 ILE A  78      -7.796  41.038  47.392  1.00 50.38           C  
ATOM    557  N   ASP A  79     -12.755  41.723  50.252  1.00 53.36           N  
ATOM    558  CA  ASP A  79     -14.198  42.016  50.195  1.00 55.07           C  
ATOM    559  C   ASP A  79     -14.889  42.278  51.559  1.00 56.13           C  
ATOM    560  O   ASP A  79     -16.118  42.393  51.627  1.00 55.86           O  
ATOM    561  CB  ASP A  79     -14.917  40.882  49.448  1.00 55.44           C  
ATOM    562  CG  ASP A  79     -14.480  40.761  47.985  1.00 57.01           C  
ATOM    563  OD1 ASP A  79     -13.647  41.566  47.512  1.00 59.16           O  
ATOM    564  OD2 ASP A  79     -14.975  39.848  47.298  1.00 58.53           O  
ATOM    565  N   LYS A  80     -14.100  42.394  52.628  1.00 57.21           N  
ATOM    566  CA  LYS A  80     -14.628  42.550  53.994  1.00 58.84           C  
ATOM    567  C   LYS A  80     -15.252  43.931  54.269  1.00 59.49           C  
ATOM    568  O   LYS A  80     -14.597  44.962  54.097  1.00 59.98           O  
ATOM    569  CB  LYS A  80     -13.529  42.234  55.023  1.00 58.77           C  
ATOM    570  CG  LYS A  80     -14.041  41.722  56.371  1.00 60.03           C  
ATOM    571  CD  LYS A  80     -14.096  40.187  56.408  1.00 61.17           C  
ATOM    572  N   VAL A  81     -16.514  43.940  54.705  1.00 60.26           N  
ATOM    573  CA  VAL A  81     -17.252  45.181  54.995  1.00 60.86           C  
ATOM    574  C   VAL A  81     -17.258  45.539  56.489  1.00 61.23           C  
ATOM    575  O   VAL A  81     -17.614  44.722  57.346  1.00 61.73           O  
ATOM    576  CB  VAL A  81     -18.706  45.133  54.427  1.00 60.84           C  
ATOM    577  CG1 VAL A  81     -19.647  46.103  55.168  1.00 61.22           C  
ATOM    578  CG2 VAL A  81     -18.698  45.433  52.933  1.00 60.99           C  
ATOM    579  N   PRO A  92     -13.370  46.108  42.953  1.00 46.09           N  
ATOM    580  CA  PRO A  92     -11.971  45.764  42.624  1.00 45.56           C  
ATOM    581  C   PRO A  92     -11.826  44.394  41.985  1.00 44.52           C  
ATOM    582  O   PRO A  92     -12.291  43.399  42.550  1.00 44.21           O  
ATOM    583  CB  PRO A  92     -11.247  45.783  43.976  1.00 45.53           C  
ATOM    584  CG  PRO A  92     -12.239  46.134  44.987  1.00 46.15           C  
ATOM    585  CD  PRO A  92     -13.620  46.170  44.397  1.00 46.57           C  
ATOM    586  N   THR A  93     -11.197  44.347  40.810  1.00 43.94           N  
ATOM    587  CA  THR A  93     -10.777  43.071  40.228  1.00 43.69           C  
ATOM    588  C   THR A  93      -9.630  42.530  41.065  1.00 42.84           C  
ATOM    589  O   THR A  93      -8.837  43.305  41.596  1.00 42.60           O  
ATOM    590  CB  THR A  93     -10.336  43.232  38.765  1.00 44.15           C  
ATOM    591  OG1 THR A  93     -11.446  43.724  38.008  1.00 46.05           O  
ATOM    592  CG2 THR A  93      -9.877  41.880  38.184  1.00 43.62           C  
ATOM    593  N   ILE A  94      -9.552  41.203  41.199  1.00 42.53           N  
ATOM    594  CA  ILE A  94      -8.463  40.583  41.900  1.00 42.04           C  
ATOM    595  C   ILE A  94      -7.654  39.727  40.910  1.00 42.90           C  
ATOM    596  O   ILE A  94      -8.205  38.829  40.265  1.00 42.73           O  
ATOM    597  CB  ILE A  94      -8.964  39.717  43.087  1.00 42.08           C  
ATOM    598  CG1 ILE A  94      -9.922  40.544  43.978  1.00 41.27           C  
ATOM    599  CG2 ILE A  94      -7.758  39.156  43.861  1.00 42.95           C  
ATOM    600  CD1 ILE A  94     -10.738  39.764  45.054  1.00 41.80           C  
ATOM    601  N   GLN A  95      -6.361  40.013  40.788  1.00 42.10           N  
ATOM    602  CA  GLN A  95      -5.498  39.194  39.959  1.00 44.02           C  
ATOM    603  C   GLN A  95      -4.471  38.478  40.839  1.00 43.68           C  
ATOM    604  O   GLN A  95      -3.586  39.110  41.422  1.00 43.76           O  
ATOM    605  CB  GLN A  95      -4.832  40.011  38.857  1.00 43.65           C  
ATOM    606  CG  GLN A  95      -4.130  39.162  37.788  1.00 45.05           C  
ATOM    607  CD  GLN A  95      -3.395  40.014  36.771  1.00 45.73           C  
ATOM    608  OE1 GLN A  95      -2.940  41.098  37.089  1.00 45.56           O  
ATOM    609  NE2 GLN A  95      -3.258  39.510  35.538  1.00 48.34           N  
ATOM    610  N   ILE A  96      -4.621  37.161  40.941  1.00 43.77           N  
ATOM    611  CA  ILE A  96      -3.776  36.325  41.798  1.00 44.27           C  
ATOM    612  C   ILE A  96      -2.797  35.493  40.965  1.00 44.15           C  
ATOM    613  O   ILE A  96      -3.190  34.783  40.048  1.00 45.47           O  
ATOM    614  CB  ILE A  96      -4.637  35.419  42.714  1.00 44.68           C  
ATOM    615  CG1 ILE A  96      -5.441  36.296  43.695  1.00 44.26           C  
ATOM    616  CG2 ILE A  96      -3.773  34.386  43.485  1.00 46.31           C  
ATOM    617  CD1 ILE A  96      -6.527  35.578  44.420  1.00 45.72           C  
ATOM    618  N   PHE A  97      -1.520  35.601  41.285  1.00 43.50           N  
ATOM    619  CA  PHE A  97      -0.499  34.761  40.667  1.00 43.54           C  
ATOM    620  C   PHE A  97      -0.027  33.732  41.675  1.00 42.74           C  
ATOM    621  O   PHE A  97       0.541  34.075  42.712  1.00 42.46           O  
ATOM    622  CB  PHE A  97       0.696  35.588  40.223  1.00 44.24           C  
ATOM    623  CG  PHE A  97       0.380  36.666  39.230  1.00 47.16           C  
ATOM    624  CD1 PHE A  97      -0.150  37.885  39.645  1.00 47.93           C  
ATOM    625  CD2 PHE A  97       0.673  36.484  37.882  1.00 48.74           C  
ATOM    626  CE1 PHE A  97      -0.398  38.898  38.733  1.00 50.28           C  
ATOM    627  CE2 PHE A  97       0.419  37.505  36.958  1.00 50.78           C  
ATOM    628  CZ  PHE A  97      -0.101  38.703  37.381  1.00 49.17           C  
ATOM    629  N   LEU A  98      -0.267  32.465  41.376  1.00 43.08           N  
ATOM    630  CA  LEU A  98       0.212  31.378  42.225  1.00 42.85           C  
ATOM    631  C   LEU A  98       1.620  30.991  41.786  1.00 44.25           C  
ATOM    632  O   LEU A  98       1.854  30.681  40.597  1.00 44.68           O  
ATOM    633  CB  LEU A  98      -0.724  30.180  42.092  1.00 43.12           C  
ATOM    634  CG  LEU A  98      -2.200  30.415  42.388  1.00 42.40           C  
ATOM    635  CD1 LEU A  98      -3.019  29.158  42.109  1.00 38.08           C  
ATOM    636  CD2 LEU A  98      -2.389  30.900  43.846  1.00 43.37           C  
ATOM    637  N   ASN A  99       2.572  31.029  42.715  1.00 43.79           N  
ATOM    638  CA  ASN A  99       3.945  30.711  42.354  1.00 44.01           C  
ATOM    639  C   ASN A  99       4.404  29.497  43.119  1.00 44.64           C  
ATOM    640  O   ASN A  99       4.190  29.377  44.338  1.00 44.15           O  
ATOM    641  CB  ASN A  99       4.910  31.871  42.635  1.00 43.07           C  
ATOM    642  CG  ASN A  99       6.371  31.408  42.840  1.00 44.06           C  
ATOM    643  OD1 ASN A  99       6.853  31.299  43.979  1.00 42.49           O  
ATOM    644  ND2 ASN A  99       7.076  31.151  41.731  1.00 41.51           N  
ATOM    645  N   ASP A 100       5.073  28.617  42.401  1.00 45.87           N  
ATOM    646  CA  ASP A 100       5.822  27.527  43.042  1.00 47.32           C  
ATOM    647  C   ASP A 100       6.872  27.027  42.052  1.00 48.10           C  
ATOM    648  O   ASP A 100       6.953  27.513  40.938  1.00 47.17           O  
ATOM    649  CB  ASP A 100       4.896  26.423  43.521  1.00 47.61           C  
ATOM    650  CG  ASP A 100       5.488  25.638  44.713  1.00 51.21           C  
ATOM    651  OD1 ASP A 100       6.410  24.830  44.485  1.00 49.78           O  
ATOM    652  OD2 ASP A 100       5.050  25.865  45.874  1.00 53.64           O  
ATOM    653  N   LEU A 101       7.681  26.060  42.471  1.00 51.04           N  
ATOM    654  CA  LEU A 101       8.738  25.499  41.626  1.00 52.73           C  
ATOM    655  C   LEU A 101       8.155  24.870  40.339  1.00 53.32           C  
ATOM    656  O   LEU A 101       6.973  24.522  40.312  1.00 54.21           O  
ATOM    657  CB  LEU A 101       9.624  24.553  42.490  1.00 52.54           C  
ATOM    658  CG  LEU A 101      10.511  25.352  43.463  1.00 53.94           C  
ATOM    659  CD1 LEU A 101      11.135  24.527  44.590  1.00 54.32           C  
ATOM    660  CD2 LEU A 101      11.611  26.114  42.723  1.00 53.83           C  
ATOM    661  N   PHE A 102       8.957  24.775  39.269  1.00 54.07           N  
ATOM    662  CA  PHE A 102       8.500  24.339  37.923  1.00 54.91           C  
ATOM    663  C   PHE A 102       7.856  22.923  37.779  1.00 56.00           C  
ATOM    664  O   PHE A 102       7.217  22.632  36.749  1.00 55.27           O  
ATOM    665  CB  PHE A 102       9.649  24.430  36.894  1.00 55.09           C  
ATOM    666  CG  PHE A 102      10.056  25.826  36.528  1.00 53.72           C  
ATOM    667  CD1 PHE A 102       9.286  26.597  35.657  1.00 53.60           C  
ATOM    668  CD2 PHE A 102      11.229  26.363  37.038  1.00 54.82           C  
ATOM    669  CE1 PHE A 102       9.663  27.876  35.327  1.00 52.40           C  
ATOM    670  CE2 PHE A 102      11.615  27.631  36.720  1.00 52.22           C  
ATOM    671  CZ  PHE A 102      10.835  28.397  35.848  1.00 54.63           C  
ATOM    672  N   GLN A 103       8.046  22.071  38.780  1.00 56.63           N  
ATOM    673  CA  GLN A 103       7.488  20.711  38.828  1.00 59.00           C  
ATOM    674  C   GLN A 103       6.459  20.565  39.962  1.00 59.31           C  
ATOM    675  O   GLN A 103       6.214  19.449  40.484  1.00 60.01           O  
ATOM    676  CB  GLN A 103       8.603  19.673  39.057  1.00 59.25           C  
ATOM    677  CG  GLN A 103       9.485  19.374  37.863  1.00 60.84           C  
ATOM    678  CD  GLN A 103      10.001  17.950  37.871  1.00 64.77           C  
ATOM    679  OE1 GLN A 103      10.036  17.283  38.916  1.00 67.01           O  
ATOM    680  NE2 GLN A 103      10.405  17.464  36.696  1.00 66.56           N  
ATOM    681  N   ASN A 104       5.891  21.696  40.382  1.00 59.36           N  
ATOM    682  CA  ASN A 104       4.761  21.671  41.293  1.00 58.46           C  
ATOM    683  C   ASN A 104       3.581  21.189  40.488  1.00 57.55           C  
ATOM    684  O   ASN A 104       3.559  21.329  39.263  1.00 57.63           O  
ATOM    685  CB  ASN A 104       4.486  23.067  41.884  1.00 58.40           C  
ATOM    686  CG  ASN A 104       3.294  23.083  42.839  1.00 58.06           C  
ATOM    687  OD1 ASN A 104       3.313  22.440  43.885  1.00 56.93           O  
ATOM    688  ND2 ASN A 104       2.265  23.849  42.489  1.00 59.16           N  
ATOM    689  N   ASP A 105       2.598  20.633  41.186  1.00 57.00           N  
ATOM    690  CA  ASP A 105       1.421  20.078  40.561  1.00 56.20           C  
ATOM    691  C   ASP A 105       0.406  21.200  40.310  1.00 55.86           C  
ATOM    692  O   ASP A 105      -0.549  21.367  41.072  1.00 55.52           O  
ATOM    693  CB  ASP A 105       0.837  18.987  41.481  1.00 56.37           C  
ATOM    694  CG  ASP A 105      -0.174  18.096  40.780  1.00 57.18           C  
ATOM    695  OD1 ASP A 105      -0.479  18.340  39.590  1.00 58.24           O  
ATOM    696  OD2 ASP A 105      -0.666  17.143  41.435  1.00 57.21           O  
ATOM    697  N   PHE A 106       0.638  21.980  39.251  1.00 55.64           N  
ATOM    698  CA  PHE A 106      -0.265  23.074  38.848  1.00 54.98           C  
ATOM    699  C   PHE A 106      -1.548  22.561  38.167  1.00 54.80           C  
ATOM    700  O   PHE A 106      -2.638  23.103  38.389  1.00 54.17           O  
ATOM    701  CB  PHE A 106       0.464  24.085  37.937  1.00 54.84           C  
ATOM    702  CG  PHE A 106       1.347  25.053  38.687  1.00 54.09           C  
ATOM    703  CD1 PHE A 106       0.795  26.127  39.381  1.00 53.39           C  
ATOM    704  CD2 PHE A 106       2.730  24.895  38.692  1.00 54.35           C  
ATOM    705  CE1 PHE A 106       1.610  27.024  40.098  1.00 54.12           C  
ATOM    706  CE2 PHE A 106       3.559  25.791  39.386  1.00 54.59           C  
ATOM    707  CZ  PHE A 106       2.992  26.870  40.090  1.00 54.06           C  
ATOM    708  N   ASN A 107      -1.400  21.522  37.346  1.00 54.70           N  
ATOM    709  CA  ASN A 107      -2.500  20.925  36.586  1.00 55.26           C  
ATOM    710  C   ASN A 107      -3.722  20.578  37.448  1.00 55.35           C  
ATOM    711  O   ASN A 107      -4.870  20.698  36.989  1.00 55.86           O  
ATOM    712  CB  ASN A 107      -2.033  19.661  35.838  1.00 54.85           C  
ATOM    713  CG  ASN A 107      -1.585  19.949  34.409  1.00 55.49           C  
ATOM    714  OD1 ASN A 107      -1.339  21.105  34.036  1.00 53.62           O  
ATOM    715  ND2 ASN A 107      -1.484  18.900  33.596  1.00 51.75           N  
ATOM    716  N   SER A 108      -3.462  20.160  38.681  1.00 55.10           N  
ATOM    717  CA  SER A 108      -4.513  19.741  39.588  1.00 55.75           C  
ATOM    718  C   SER A 108      -5.217  20.934  40.236  1.00 54.73           C  
ATOM    719  O   SER A 108      -6.416  20.866  40.521  1.00 54.89           O  
ATOM    720  CB  SER A 108      -3.981  18.761  40.638  1.00 55.99           C  
ATOM    721  OG  SER A 108      -3.202  19.406  41.631  1.00 59.38           O  
ATOM    722  N   VAL A 109      -4.474  22.019  40.460  1.00 53.45           N  
ATOM    723  CA  VAL A 109      -5.052  23.263  40.942  1.00 51.84           C  
ATOM    724  C   VAL A 109      -6.003  23.806  39.890  1.00 51.21           C  
ATOM    725  O   VAL A 109      -7.129  24.184  40.220  1.00 51.33           O  
ATOM    726  CB  VAL A 109      -3.959  24.318  41.298  1.00 51.96           C  
ATOM    727  CG1 VAL A 109      -4.583  25.691  41.633  1.00 51.13           C  
ATOM    728  CG2 VAL A 109      -3.094  23.809  42.443  1.00 51.40           C  
ATOM    729  N   PHE A 110      -5.556  23.818  38.628  1.00 50.24           N  
ATOM    730  CA  PHE A 110      -6.283  24.432  37.517  1.00 49.41           C  
ATOM    731  C   PHE A 110      -7.578  23.689  37.225  1.00 49.28           C  
ATOM    732  O   PHE A 110      -8.560  24.264  36.754  1.00 47.73           O  
ATOM    733  CB  PHE A 110      -5.434  24.445  36.241  1.00 49.35           C  
ATOM    734  CG  PHE A 110      -4.283  25.426  36.264  1.00 49.97           C  
ATOM    735  CD1 PHE A 110      -4.077  26.288  37.348  1.00 51.28           C  
ATOM    736  CD2 PHE A 110      -3.447  25.537  35.159  1.00 51.50           C  
ATOM    737  CE1 PHE A 110      -3.011  27.217  37.352  1.00 49.96           C  
ATOM    738  CE2 PHE A 110      -2.376  26.475  35.140  1.00 51.47           C  
ATOM    739  CZ  PHE A 110      -2.160  27.297  36.254  1.00 50.57           C  
ATOM    740  N   LYS A 111      -7.556  22.390  37.490  1.00 48.94           N  
ATOM    741  CA  LYS A 111      -8.713  21.549  37.230  1.00 49.08           C  
ATOM    742  C   LYS A 111      -9.807  21.779  38.281  1.00 48.46           C  
ATOM    743  O   LYS A 111     -10.979  21.550  38.025  1.00 49.59           O  
ATOM    744  CB  LYS A 111      -8.285  20.085  37.205  1.00 49.46           C  
ATOM    745  CG  LYS A 111      -7.744  19.610  35.862  1.00 51.40           C  
ATOM    746  CD  LYS A 111      -7.376  18.122  35.950  1.00 55.61           C  
ATOM    747  CE  LYS A 111      -6.191  17.755  35.069  1.00 57.13           C  
ATOM    748  NZ  LYS A 111      -5.527  16.561  35.688  1.00 58.78           N  
ATOM    749  N   LEU A 112      -9.403  22.224  39.461  1.00 47.62           N  
ATOM    750  CA  LEU A 112     -10.323  22.602  40.517  1.00 46.54           C  
ATOM    751  C   LEU A 112     -10.795  24.050  40.418  1.00 46.07           C  
ATOM    752  O   LEU A 112     -11.694  24.456  41.140  1.00 45.70           O  
ATOM    753  CB  LEU A 112      -9.697  22.319  41.881  1.00 46.63           C  
ATOM    754  CG  LEU A 112      -9.587  20.825  42.207  1.00 45.91           C  
ATOM    755  CD1 LEU A 112      -8.657  20.578  43.371  1.00 47.24           C  
ATOM    756  CD2 LEU A 112     -10.966  20.234  42.482  1.00 47.24           C  
ATOM    757  N   LEU A 113     -10.202  24.830  39.516  1.00 45.98           N  
ATOM    758  CA  LEU A 113     -10.619  26.217  39.356  1.00 45.61           C  
ATOM    759  C   LEU A 113     -12.079  26.440  38.914  1.00 45.86           C  
ATOM    760  O   LEU A 113     -12.711  27.339  39.425  1.00 46.13           O  
ATOM    761  CB  LEU A 113      -9.622  27.028  38.494  1.00 45.56           C  
ATOM    762  CG  LEU A 113      -8.349  27.515  39.204  1.00 44.54           C  
ATOM    763  CD1 LEU A 113      -7.405  28.233  38.230  1.00 44.73           C  
ATOM    764  CD2 LEU A 113      -8.689  28.444  40.375  1.00 45.22           C  
ATOM    765  N   PRO A 114     -12.616  25.641  37.969  1.00 46.52           N  
ATOM    766  CA  PRO A 114     -14.014  25.889  37.584  1.00 47.45           C  
ATOM    767  C   PRO A 114     -14.995  25.814  38.773  1.00 48.28           C  
ATOM    768  O   PRO A 114     -15.889  26.661  38.882  1.00 48.74           O  
ATOM    769  CB  PRO A 114     -14.307  24.764  36.591  1.00 47.17           C  
ATOM    770  CG  PRO A 114     -12.948  24.372  36.058  1.00 46.70           C  
ATOM    771  CD  PRO A 114     -12.047  24.500  37.222  1.00 46.52           C  
ATOM    772  N   SER A 115     -14.831  24.826  39.644  1.00 48.90           N  
ATOM    773  CA  SER A 115     -15.714  24.704  40.813  1.00 49.63           C  
ATOM    774  C   SER A 115     -15.381  25.749  41.867  1.00 49.44           C  
ATOM    775  O   SER A 115     -16.299  26.364  42.422  1.00 49.46           O  
ATOM    776  CB  SER A 115     -15.718  23.297  41.401  1.00 49.91           C  
ATOM    777  OG  SER A 115     -14.425  22.911  41.802  1.00 52.73           O  
ATOM    778  N   PHE A 116     -14.087  25.982  42.114  1.00 48.86           N  
ATOM    779  CA  PHE A 116     -13.674  27.118  42.944  1.00 49.08           C  
ATOM    780  C   PHE A 116     -14.360  28.433  42.551  1.00 48.64           C  
ATOM    781  O   PHE A 116     -14.862  29.140  43.419  1.00 48.34           O  
ATOM    782  CB  PHE A 116     -12.154  27.338  42.953  1.00 49.86           C  
ATOM    783  CG  PHE A 116     -11.733  28.470  43.847  1.00 51.93           C  
ATOM    784  CD1 PHE A 116     -11.653  28.284  45.234  1.00 52.59           C  
ATOM    785  CD2 PHE A 116     -11.492  29.750  43.317  1.00 53.98           C  
ATOM    786  CE1 PHE A 116     -11.297  29.337  46.077  1.00 54.27           C  
ATOM    787  CE2 PHE A 116     -11.143  30.817  44.151  1.00 54.39           C  
ATOM    788  CZ  PHE A 116     -11.037  30.612  45.531  1.00 53.63           C  
ATOM    789  N   TYR A 117     -14.356  28.764  41.255  1.00 48.11           N  
ATOM    790  CA  TYR A 117     -14.977  30.002  40.758  1.00 47.81           C  
ATOM    791  C   TYR A 117     -16.498  30.071  40.987  1.00 48.22           C  
ATOM    792  O   TYR A 117     -17.027  31.130  41.336  1.00 47.66           O  
ATOM    793  CB  TYR A 117     -14.680  30.216  39.263  1.00 47.27           C  
ATOM    794  CG  TYR A 117     -13.292  30.721  38.919  1.00 46.68           C  
ATOM    795  CD1 TYR A 117     -12.684  31.750  39.643  1.00 47.52           C  
ATOM    796  CD2 TYR A 117     -12.591  30.184  37.833  1.00 45.80           C  
ATOM    797  CE1 TYR A 117     -11.398  32.234  39.283  1.00 44.50           C  
ATOM    798  CE2 TYR A 117     -11.333  30.639  37.490  1.00 43.45           C  
ATOM    799  CZ  TYR A 117     -10.742  31.659  38.213  1.00 45.28           C  
ATOM    800  OH  TYR A 117      -9.490  32.103  37.832  1.00 47.05           O  
ATOM    801  N   ARG A 118     -17.185  28.955  40.751  1.00 49.05           N  
ATOM    802  CA  ARG A 118     -18.625  28.830  41.001  1.00 50.91           C  
ATOM    803  C   ARG A 118     -18.966  28.960  42.482  1.00 51.47           C  
ATOM    804  O   ARG A 118     -19.931  29.622  42.847  1.00 51.15           O  
ATOM    805  CB  ARG A 118     -19.156  27.485  40.501  1.00 51.01           C  
ATOM    806  CG  ARG A 118     -19.126  27.305  38.996  1.00 52.37           C  
ATOM    807  CD  ARG A 118     -19.962  26.119  38.561  1.00 55.51           C  
ATOM    808  NE  ARG A 118     -19.424  24.846  39.051  1.00 57.80           N  
ATOM    809  CZ  ARG A 118     -18.630  24.045  38.342  1.00 58.73           C  
ATOM    810  NH1 ARG A 118     -18.274  24.373  37.101  1.00 58.70           N  
ATOM    811  NH2 ARG A 118     -18.201  22.908  38.869  1.00 59.38           N  
ATOM    812  N   ASN A 119     -18.162  28.313  43.320  1.00 53.10           N  
ATOM    813  CA  ASN A 119     -18.337  28.365  44.765  1.00 54.98           C  
ATOM    814  C   ASN A 119     -18.033  29.756  45.306  1.00 55.85           C  
ATOM    815  O   ASN A 119     -18.635  30.186  46.282  1.00 56.17           O  
ATOM    816  CB  ASN A 119     -17.470  27.306  45.455  1.00 55.49           C  
ATOM    817  CG  ASN A 119     -17.878  25.881  45.098  1.00 56.87           C  
ATOM    818  OD1 ASN A 119     -18.777  25.656  44.280  1.00 59.84           O  
ATOM    819  ND2 ASN A 119     -17.216  24.909  45.716  1.00 57.98           N  
ATOM    820  N   LEU A 120     -17.094  30.446  44.660  1.00 56.87           N  
ATOM    821  CA  LEU A 120     -16.790  31.849  44.954  1.00 57.73           C  
ATOM    822  C   LEU A 120     -17.993  32.748  44.647  1.00 58.03           C  
ATOM    823  O   LEU A 120     -18.252  33.707  45.373  1.00 58.05           O  
ATOM    824  CB  LEU A 120     -15.590  32.315  44.128  1.00 57.77           C  
ATOM    825  CG  LEU A 120     -14.490  33.211  44.713  1.00 58.85           C  
ATOM    826  CD1 LEU A 120     -13.609  33.749  43.585  1.00 58.22           C  
ATOM    827  CD2 LEU A 120     -15.028  34.358  45.547  1.00 59.66           C  
ATOM    828  N   GLU A 121     -18.704  32.442  43.560  1.00 58.73           N  
ATOM    829  CA  GLU A 121     -19.892  33.197  43.158  1.00 59.56           C  
ATOM    830  C   GLU A 121     -21.118  32.837  43.991  1.00 59.89           C  
ATOM    831  O   GLU A 121     -21.983  33.686  44.215  1.00 59.90           O  
ATOM    832  CB  GLU A 121     -20.203  32.993  41.672  1.00 59.67           C  
ATOM    833  CG  GLU A 121     -21.273  33.948  41.121  1.00 59.81           C  
ATOM    834  CD  GLU A 121     -21.697  33.637  39.688  1.00 60.68           C  
ATOM    835  OE1 GLU A 121     -21.200  32.646  39.104  1.00 61.90           O  
ATOM    836  OE2 GLU A 121     -22.541  34.391  39.144  1.00 61.87           O  
ATOM    837  N   LYS A 122     -21.205  31.582  44.432  1.00 60.44           N  
ATOM    838  CA  LYS A 122     -22.302  31.167  45.317  1.00 61.26           C  
ATOM    839  C   LYS A 122     -22.081  31.701  46.734  1.00 61.90           C  
ATOM    840  O   LYS A 122     -23.033  32.130  47.380  1.00 62.08           O  
ATOM    841  CB  LYS A 122     -22.503  29.643  45.313  1.00 61.05           C  
ATOM    842  CG  LYS A 122     -23.428  29.135  44.206  1.00 60.81           C  
ATOM    843  CD  LYS A 122     -23.232  27.644  43.936  1.00 60.81           C  
ATOM    844  CE  LYS A 122     -24.262  27.099  42.933  1.00 61.21           C  
ATOM    845  NZ  LYS A 122     -25.469  26.438  43.551  1.00 61.18           N  
ATOM    846  N   GLU A 123     -20.827  31.696  47.197  1.00 62.67           N  
ATOM    847  CA  GLU A 123     -20.475  32.254  48.512  1.00 63.57           C  
ATOM    848  C   GLU A 123     -20.572  33.785  48.594  1.00 63.92           C  
ATOM    849  O   GLU A 123     -21.382  34.309  49.363  1.00 63.75           O  
ATOM    850  CB  GLU A 123     -19.089  31.785  48.973  1.00 63.55           C  
ATOM    851  CG  GLU A 123     -19.044  30.366  49.544  1.00 65.24           C  
ATOM    852  CD  GLU A 123     -19.339  30.296  51.047  1.00 66.94           C  
ATOM    853  OE1 GLU A 123     -20.273  30.978  51.526  1.00 66.84           O  
ATOM    854  OE2 GLU A 123     -18.632  29.539  51.756  1.00 68.63           O  
ATOM    855  N   ASN A 124     -19.761  34.496  47.806  1.00 64.25           N  
ATOM    856  CA  ASN A 124     -19.617  35.957  47.956  1.00 64.62           C  
ATOM    857  C   ASN A 124     -20.444  36.835  47.000  1.00 64.75           C  
ATOM    858  O   ASN A 124     -20.688  38.018  47.278  1.00 64.98           O  
ATOM    859  CB  ASN A 124     -18.137  36.369  47.877  1.00 64.92           C  
ATOM    860  CG  ASN A 124     -17.232  35.568  48.834  1.00 66.00           C  
ATOM    861  OD1 ASN A 124     -17.705  34.788  49.667  1.00 67.01           O  
ATOM    862  ND2 ASN A 124     -15.917  35.768  48.707  1.00 65.48           N  
ATOM    863  N   GLY A 125     -20.869  36.266  45.877  1.00 64.60           N  
ATOM    864  CA  GLY A 125     -21.459  37.059  44.804  1.00 64.10           C  
ATOM    865  C   GLY A 125     -20.417  37.504  43.789  1.00 63.93           C  
ATOM    866  O   GLY A 125     -20.768  37.896  42.672  1.00 64.34           O  
ATOM    867  N   ARG A 126     -19.138  37.453  44.176  1.00 63.36           N  
ATOM    868  CA  ARG A 126     -18.021  37.676  43.253  1.00 62.38           C  
ATOM    869  C   ARG A 126     -18.342  37.089  41.888  1.00 62.35           C  
ATOM    870  O   ARG A 126     -18.238  35.872  41.683  1.00 62.18           O  
ATOM    871  CB  ARG A 126     -16.731  37.029  43.779  1.00 62.07           C  
ATOM    872  CG  ARG A 126     -15.875  37.909  44.682  1.00 60.52           C  
ATOM    873  CD  ARG A 126     -14.787  38.629  43.909  1.00 57.10           C  
ATOM    874  NE  ARG A 126     -14.343  39.845  44.591  1.00 54.08           N  
ATOM    875  CZ  ARG A 126     -13.692  40.847  44.001  1.00 51.60           C  
ATOM    876  NH1 ARG A 126     -13.391  40.779  42.715  1.00 50.24           N  
ATOM    877  NH2 ARG A 126     -13.341  41.920  44.701  1.00 49.02           N  
ATOM    878  N   LYS A 127     -18.741  37.965  40.964  1.00 62.29           N  
ATOM    879  CA  LYS A 127     -19.029  37.581  39.586  1.00 61.86           C  
ATOM    880  C   LYS A 127     -17.820  36.856  39.003  1.00 61.46           C  
ATOM    881  O   LYS A 127     -16.676  37.102  39.415  1.00 61.87           O  
ATOM    882  CB  LYS A 127     -19.388  38.812  38.750  1.00 61.83           C  
ATOM    883  N   ILE A 128     -18.059  35.940  38.069  1.00 60.62           N  
ATOM    884  CA  ILE A 128     -16.940  35.185  37.497  1.00 59.75           C  
ATOM    885  C   ILE A 128     -16.200  36.061  36.472  1.00 58.84           C  
ATOM    886  O   ILE A 128     -16.821  36.690  35.608  1.00 59.70           O  
ATOM    887  CB  ILE A 128     -17.371  33.760  37.004  1.00 59.93           C  
ATOM    888  CG1 ILE A 128     -17.855  32.932  38.218  1.00 59.86           C  
ATOM    889  CG2 ILE A 128     -16.220  33.063  36.266  1.00 60.44           C  
ATOM    890  CD1 ILE A 128     -18.505  31.570  37.918  1.00 59.61           C  
ATOM    891  N   GLY A 129     -14.882  36.154  36.617  1.00 57.11           N  
ATOM    892  CA  GLY A 129     -14.096  37.106  35.849  1.00 54.72           C  
ATOM    893  C   GLY A 129     -13.640  38.295  36.676  1.00 53.23           C  
ATOM    894  O   GLY A 129     -12.863  39.111  36.204  1.00 52.88           O  
ATOM    895  N   SER A 130     -14.127  38.411  37.910  1.00 51.86           N  
ATOM    896  CA  SER A 130     -13.680  39.492  38.792  1.00 50.42           C  
ATOM    897  C   SER A 130     -12.530  39.041  39.709  1.00 49.70           C  
ATOM    898  O   SER A 130     -11.900  39.869  40.374  1.00 49.71           O  
ATOM    899  CB  SER A 130     -14.841  40.035  39.627  1.00 50.12           C  
ATOM    900  OG  SER A 130     -15.273  39.042  40.512  1.00 48.71           O  
ATOM    901  N   CYS A 131     -12.298  37.727  39.758  1.00 48.38           N  
ATOM    902  CA  CYS A 131     -11.156  37.133  40.429  1.00 46.95           C  
ATOM    903  C   CYS A 131     -10.435  36.252  39.406  1.00 46.08           C  
ATOM    904  O   CYS A 131     -10.970  35.228  38.964  1.00 46.32           O  
ATOM    905  CB  CYS A 131     -11.588  36.303  41.649  1.00 47.21           C  
ATOM    906  SG  CYS A 131     -10.186  35.551  42.513  1.00 49.73           S  
ATOM    907  N   LEU A 132      -9.226  36.664  39.043  1.00 43.66           N  
ATOM    908  CA  LEU A 132      -8.474  36.073  37.939  1.00 42.62           C  
ATOM    909  C   LEU A 132      -7.269  35.326  38.507  1.00 41.95           C  
ATOM    910  O   LEU A 132      -6.322  35.954  38.976  1.00 42.50           O  
ATOM    911  CB  LEU A 132      -8.033  37.183  36.974  1.00 42.17           C  
ATOM    912  CG  LEU A 132      -9.146  38.071  36.411  1.00 43.37           C  
ATOM    913  CD1 LEU A 132      -8.563  39.290  35.713  1.00 43.22           C  
ATOM    914  CD2 LEU A 132     -10.031  37.280  35.461  1.00 43.89           C  
ATOM    915  N   ILE A 133      -7.319  33.991  38.487  1.00 40.38           N  
ATOM    916  CA  ILE A 133      -6.262  33.188  39.080  1.00 40.98           C  
ATOM    917  C   ILE A 133      -5.373  32.558  38.014  1.00 40.77           C  
ATOM    918  O   ILE A 133      -5.828  31.765  37.192  1.00 38.94           O  
ATOM    919  CB  ILE A 133      -6.829  32.107  40.058  1.00 40.50           C  
ATOM    920  CG1 ILE A 133      -7.688  32.788  41.129  1.00 40.62           C  
ATOM    921  CG2 ILE A 133      -5.654  31.295  40.693  1.00 41.17           C  
ATOM    922  CD1 ILE A 133      -8.550  31.822  41.985  1.00 41.56           C  
ATOM    923  N   GLY A 134      -4.105  32.973  37.994  1.00 42.18           N  
ATOM    924  CA  GLY A 134      -3.132  32.330  37.122  1.00 42.60           C  
ATOM    925  C   GLY A 134      -1.921  31.836  37.882  1.00 42.55           C  
ATOM    926  O   GLY A 134      -1.908  31.784  39.110  1.00 43.00           O  
ATOM    927  N   ALA A 135      -0.891  31.471  37.150  1.00 42.52           N  
ATOM    928  CA  ALA A 135       0.305  30.926  37.780  1.00 42.43           C  
ATOM    929  C   ALA A 135       1.547  31.520  37.164  1.00 43.10           C  
ATOM    930  O   ALA A 135       1.590  31.783  35.959  1.00 43.02           O  
ATOM    931  CB  ALA A 135       0.319  29.431  37.638  1.00 42.31           C  
ATOM    932  N   MET A 136       2.561  31.713  38.003  1.00 43.51           N  
ATOM    933  CA  MET A 136       3.859  32.169  37.584  1.00 44.44           C  
ATOM    934  C   MET A 136       4.909  31.222  38.227  1.00 44.50           C  
ATOM    935  O   MET A 136       5.338  31.416  39.376  1.00 43.93           O  
ATOM    936  CB  MET A 136       4.054  33.644  37.973  1.00 45.93           C  
ATOM    937  CG  MET A 136       5.390  34.209  37.574  1.00 46.19           C  
ATOM    938  SD  MET A 136       5.739  33.933  35.840  1.00 54.29           S  
ATOM    939  CE  MET A 136       7.543  34.150  35.822  1.00 48.22           C  
ATOM    940  N   PRO A 137       5.299  30.171  37.487  1.00 44.01           N  
ATOM    941  CA  PRO A 137       6.218  29.198  38.071  1.00 44.25           C  
ATOM    942  C   PRO A 137       7.661  29.698  38.144  1.00 44.20           C  
ATOM    943  O   PRO A 137       8.072  30.523  37.345  1.00 44.25           O  
ATOM    944  CB  PRO A 137       6.087  27.986  37.148  1.00 44.64           C  
ATOM    945  CG  PRO A 137       5.646  28.510  35.851  1.00 44.80           C  
ATOM    946  CD  PRO A 137       4.879  29.799  36.121  1.00 44.81           C  
ATOM    947  N   GLY A 138       8.399  29.228  39.130  1.00 44.22           N  
ATOM    948  CA  GLY A 138       9.799  29.568  39.242  1.00 45.01           C  
ATOM    949  C   GLY A 138      10.226  29.634  40.686  1.00 45.82           C  
ATOM    950  O   GLY A 138       9.410  29.486  41.588  1.00 45.81           O  
ATOM    951  N   SER A 139      11.511  29.891  40.901  1.00 46.22           N  
ATOM    952  CA  SER A 139      12.050  30.088  42.245  1.00 46.67           C  
ATOM    953  C   SER A 139      11.757  31.495  42.751  1.00 46.95           C  
ATOM    954  O   SER A 139      11.975  32.471  42.032  1.00 46.62           O  
ATOM    955  CB  SER A 139      13.565  29.859  42.219  1.00 46.92           C  
ATOM    956  OG  SER A 139      14.124  30.134  43.478  1.00 47.74           O  
ATOM    957  N   PHE A 140      11.284  31.620  43.991  1.00 47.22           N  
ATOM    958  CA  PHE A 140      11.128  32.955  44.543  1.00 47.94           C  
ATOM    959  C   PHE A 140      12.442  33.617  44.916  1.00 47.84           C  
ATOM    960  O   PHE A 140      12.448  34.740  45.373  1.00 48.75           O  
ATOM    961  CB  PHE A 140      10.057  33.069  45.652  1.00 48.74           C  
ATOM    962  CG  PHE A 140      10.177  32.079  46.777  1.00 50.14           C  
ATOM    963  CD1 PHE A 140      11.362  31.932  47.511  1.00 50.74           C  
ATOM    964  CD2 PHE A 140       9.052  31.371  47.182  1.00 51.28           C  
ATOM    965  CE1 PHE A 140      11.435  31.031  48.573  1.00 49.07           C  
ATOM    966  CE2 PHE A 140       9.098  30.478  48.251  1.00 50.75           C  
ATOM    967  CZ  PHE A 140      10.290  30.298  48.951  1.00 52.46           C  
ATOM    968  N   TYR A 141      13.556  32.927  44.681  1.00 47.68           N  
ATOM    969  CA  TYR A 141      14.862  33.547  44.788  1.00 47.36           C  
ATOM    970  C   TYR A 141      15.320  34.206  43.461  1.00 47.34           C  
ATOM    971  O   TYR A 141      16.434  34.715  43.356  1.00 48.14           O  
ATOM    972  CB  TYR A 141      15.891  32.538  45.370  1.00 47.55           C  
ATOM    973  CG  TYR A 141      15.538  32.065  46.789  1.00 46.57           C  
ATOM    974  CD1 TYR A 141      15.367  32.982  47.812  1.00 42.77           C  
ATOM    975  CD2 TYR A 141      15.369  30.701  47.095  1.00 44.95           C  
ATOM    976  CE1 TYR A 141      15.046  32.593  49.086  1.00 44.55           C  
ATOM    977  CE2 TYR A 141      15.053  30.299  48.397  1.00 44.81           C  
ATOM    978  CZ  TYR A 141      14.893  31.254  49.379  1.00 46.73           C  
ATOM    979  OH  TYR A 141      14.566  30.918  50.668  1.00 47.21           O  
ATOM    980  N   SER A 142      14.455  34.192  42.453  1.00 47.23           N  
ATOM    981  CA  SER A 142      14.659  34.971  41.240  1.00 48.09           C  
ATOM    982  C   SER A 142      13.440  35.874  40.948  1.00 47.84           C  
ATOM    983  O   SER A 142      12.390  35.741  41.601  1.00 47.44           O  
ATOM    984  CB  SER A 142      14.989  34.049  40.052  1.00 49.28           C  
ATOM    985  OG  SER A 142      14.229  32.840  40.092  1.00 51.26           O  
ATOM    986  N   ARG A 143      13.594  36.805  40.003  1.00 46.65           N  
ATOM    987  CA  ARG A 143      12.493  37.657  39.582  1.00 46.76           C  
ATOM    988  C   ARG A 143      11.325  36.840  39.043  1.00 45.33           C  
ATOM    989  O   ARG A 143      11.534  35.938  38.257  1.00 43.64           O  
ATOM    990  CB  ARG A 143      12.963  38.640  38.526  1.00 46.98           C  
ATOM    991  CG  ARG A 143      11.854  39.524  37.981  1.00 51.98           C  
ATOM    992  CD  ARG A 143      12.431  40.802  37.367  1.00 56.77           C  
ATOM    993  NE  ARG A 143      11.589  41.938  37.736  1.00 62.40           N  
ATOM    994  CZ  ARG A 143      11.665  42.605  38.886  1.00 63.61           C  
ATOM    995  NH1 ARG A 143      12.568  42.290  39.820  1.00 66.14           N  
ATOM    996  NH2 ARG A 143      10.824  43.590  39.107  1.00 62.44           N  
ATOM    997  N   LEU A 144      10.114  37.182  39.485  1.00 43.59           N  
ATOM    998  CA  LEU A 144       8.850  36.562  39.044  1.00 43.04           C  
ATOM    999  C   LEU A 144       7.901  37.532  38.321  1.00 42.37           C  
ATOM   1000  O   LEU A 144       7.073  37.110  37.514  1.00 42.54           O  
ATOM   1001  CB  LEU A 144       8.108  35.948  40.253  1.00 42.07           C  
ATOM   1002  CG  LEU A 144       8.724  34.724  40.929  1.00 42.80           C  
ATOM   1003  CD1 LEU A 144       8.087  34.415  42.341  1.00 40.25           C  
ATOM   1004  CD2 LEU A 144       8.678  33.504  39.996  1.00 41.09           C  
ATOM   1005  N   PHE A 145       8.043  38.825  38.597  1.00 42.44           N  
ATOM   1006  CA  PHE A 145       7.038  39.837  38.227  1.00 42.62           C  
ATOM   1007  C   PHE A 145       7.704  41.059  37.689  1.00 42.68           C  
ATOM   1008  O   PHE A 145       8.814  41.348  38.081  1.00 42.87           O  
ATOM   1009  CB  PHE A 145       6.150  40.196  39.423  1.00 41.98           C  
ATOM   1010  CG  PHE A 145       5.457  39.016  40.011  1.00 45.56           C  
ATOM   1011  CD1 PHE A 145       4.521  38.310  39.264  1.00 45.23           C  
ATOM   1012  CD2 PHE A 145       5.763  38.583  41.302  1.00 44.56           C  
ATOM   1013  CE1 PHE A 145       3.894  37.199  39.791  1.00 44.53           C  
ATOM   1014  CE2 PHE A 145       5.137  37.497  41.838  1.00 43.94           C  
ATOM   1015  CZ  PHE A 145       4.191  36.788  41.078  1.00 45.55           C  
ATOM   1016  N   PRO A 146       7.045  41.774  36.756  1.00 44.34           N  
ATOM   1017  CA  PRO A 146       7.596  43.053  36.313  1.00 44.52           C  
ATOM   1018  C   PRO A 146       7.791  44.049  37.459  1.00 45.30           C  
ATOM   1019  O   PRO A 146       7.147  43.951  38.525  1.00 45.40           O  
ATOM   1020  CB  PRO A 146       6.559  43.570  35.310  1.00 45.47           C  
ATOM   1021  CG  PRO A 146       5.713  42.394  34.972  1.00 46.05           C  
ATOM   1022  CD  PRO A 146       5.783  41.437  36.081  1.00 43.71           C  
ATOM   1023  N   GLU A 147       8.704  44.988  37.237  1.00 45.03           N  
ATOM   1024  CA  GLU A 147       8.998  46.046  38.211  1.00 45.87           C  
ATOM   1025  C   GLU A 147       7.753  46.861  38.572  1.00 43.94           C  
ATOM   1026  O   GLU A 147       6.944  47.221  37.699  1.00 42.94           O  
ATOM   1027  CB  GLU A 147      10.146  46.948  37.705  1.00 45.59           C  
ATOM   1028  CG  GLU A 147      11.483  46.173  37.531  1.00 47.76           C  
ATOM   1029  CD  GLU A 147      12.732  47.052  37.609  1.00 49.37           C  
ATOM   1030  OE1 GLU A 147      12.659  48.239  37.191  0.50 50.09           O  
ATOM   1031  OE2 GLU A 147      13.792  46.536  38.081  1.00 53.15           O  
ATOM   1032  N   GLU A 148       7.593  47.100  39.869  1.00 42.49           N  
ATOM   1033  CA  GLU A 148       6.515  47.937  40.408  1.00 42.85           C  
ATOM   1034  C   GLU A 148       5.152  47.555  39.852  1.00 42.26           C  
ATOM   1035  O   GLU A 148       4.409  48.414  39.373  1.00 41.47           O  
ATOM   1036  CB  GLU A 148       6.787  49.416  40.131  1.00 42.73           C  
ATOM   1037  CG  GLU A 148       7.753  50.061  41.075  1.00 45.43           C  
ATOM   1038  CD  GLU A 148       7.771  51.567  40.943  1.00 52.25           C  
ATOM   1039  OE1 GLU A 148       6.944  52.249  41.603  1.00 54.04           O  
ATOM   1040  OE2 GLU A 148       8.632  52.074  40.193  1.00 54.64           O  
ATOM   1041  N   SER A 149       4.837  46.267  39.923  1.00 41.30           N  
ATOM   1042  CA  SER A 149       3.606  45.737  39.348  1.00 41.79           C  
ATOM   1043  C   SER A 149       2.671  45.083  40.366  1.00 41.70           C  
ATOM   1044  O   SER A 149       1.516  44.787  40.035  1.00 42.46           O  
ATOM   1045  CB  SER A 149       3.910  44.732  38.230  1.00 41.91           C  
ATOM   1046  OG  SER A 149       4.600  43.606  38.728  1.00 42.51           O  
ATOM   1047  N   MET A 150       3.151  44.835  41.589  1.00 41.10           N  
ATOM   1048  CA  MET A 150       2.374  44.022  42.514  1.00 40.02           C  
ATOM   1049  C   MET A 150       1.996  44.824  43.750  1.00 39.60           C  
ATOM   1050  O   MET A 150       2.775  45.640  44.208  1.00 39.28           O  
ATOM   1051  CB  MET A 150       3.148  42.742  42.907  1.00 40.54           C  
ATOM   1052  CG  MET A 150       3.534  41.850  41.701  1.00 40.72           C  
ATOM   1053  SD  MET A 150       2.058  41.145  40.929  1.00 46.69           S  
ATOM   1054  CE  MET A 150       1.839  39.742  42.033  1.00 41.85           C  
ATOM   1055  N   HIS A 151       0.812  44.576  44.295  1.00 39.91           N  
ATOM   1056  CA  HIS A 151       0.402  45.245  45.552  1.00 40.14           C  
ATOM   1057  C   HIS A 151       0.820  44.470  46.795  1.00 40.19           C  
ATOM   1058  O   HIS A 151       1.144  45.063  47.824  1.00 40.53           O  
ATOM   1059  CB  HIS A 151      -1.101  45.489  45.612  1.00 39.77           C  
ATOM   1060  CG  HIS A 151      -1.607  46.475  44.603  1.00 39.98           C  
ATOM   1061  ND1 HIS A 151      -2.265  46.084  43.455  1.00 39.79           N  
ATOM   1062  CD2 HIS A 151      -1.538  47.827  44.555  1.00 37.34           C  
ATOM   1063  CE1 HIS A 151      -2.583  47.147  42.746  1.00 39.73           C  
ATOM   1064  NE2 HIS A 151      -2.171  48.221  43.399  1.00 39.46           N  
ATOM   1065  N   PHE A 152       0.782  43.139  46.719  1.00 40.31           N  
ATOM   1066  CA  PHE A 152       0.902  42.340  47.917  1.00 40.85           C  
ATOM   1067  C   PHE A 152       1.442  40.949  47.598  1.00 41.06           C  
ATOM   1068  O   PHE A 152       0.999  40.330  46.649  1.00 40.89           O  
ATOM   1069  CB  PHE A 152      -0.469  42.257  48.586  1.00 41.26           C  
ATOM   1070  CG  PHE A 152      -0.497  41.404  49.825  1.00 44.11           C  
ATOM   1071  CD1 PHE A 152       0.179  41.802  50.981  1.00 44.68           C  
ATOM   1072  CD2 PHE A 152      -1.221  40.213  49.842  1.00 44.12           C  
ATOM   1073  CE1 PHE A 152       0.149  41.027  52.119  1.00 44.67           C  
ATOM   1074  CE2 PHE A 152      -1.256  39.437  50.985  1.00 47.60           C  
ATOM   1075  CZ  PHE A 152      -0.566  39.843  52.128  1.00 45.01           C  
ATOM   1076  N   LEU A 153       2.437  40.503  48.366  1.00 40.96           N  
ATOM   1077  CA  LEU A 153       3.035  39.174  48.211  1.00 41.86           C  
ATOM   1078  C   LEU A 153       2.894  38.429  49.526  1.00 41.85           C  
ATOM   1079  O   LEU A 153       3.126  39.000  50.593  1.00 42.87           O  
ATOM   1080  CB  LEU A 153       4.515  39.275  47.811  1.00 41.40           C  
ATOM   1081  CG  LEU A 153       4.798  39.926  46.457  1.00 42.95           C  
ATOM   1082  CD1 LEU A 153       6.265  40.392  46.290  1.00 40.96           C  
ATOM   1083  CD2 LEU A 153       4.353  39.020  45.324  1.00 42.32           C  
ATOM   1084  N   HIS A 154       2.470  37.177  49.451  1.00 41.83           N  
ATOM   1085  CA  HIS A 154       2.206  36.390  50.633  1.00 42.36           C  
ATOM   1086  C   HIS A 154       3.022  35.108  50.464  1.00 42.25           C  
ATOM   1087  O   HIS A 154       3.131  34.600  49.359  1.00 41.50           O  
ATOM   1088  CB  HIS A 154       0.699  36.049  50.750  1.00 42.90           C  
ATOM   1089  CG  HIS A 154       0.402  34.992  51.772  1.00 42.51           C  
ATOM   1090  ND1 HIS A 154       0.278  33.652  51.461  1.00 43.92           N  
ATOM   1091  CD2 HIS A 154       0.257  35.079  53.116  1.00 41.74           C  
ATOM   1092  CE1 HIS A 154       0.076  32.961  52.568  1.00 42.78           C  
ATOM   1093  NE2 HIS A 154       0.047  33.806  53.585  1.00 44.19           N  
ATOM   1094  N   SER A 155       3.623  34.623  51.544  1.00 42.18           N  
ATOM   1095  CA  SER A 155       4.231  33.285  51.532  1.00 42.33           C  
ATOM   1096  C   SER A 155       4.066  32.662  52.898  1.00 42.36           C  
ATOM   1097  O   SER A 155       4.394  33.295  53.883  1.00 42.41           O  
ATOM   1098  CB  SER A 155       5.713  33.354  51.173  1.00 41.75           C  
ATOM   1099  OG  SER A 155       6.311  32.052  51.212  1.00 44.65           O  
ATOM   1100  N   CYS A 156       3.574  31.420  52.964  1.00 43.05           N  
ATOM   1101  CA  CYS A 156       3.450  30.748  54.247  1.00 43.05           C  
ATOM   1102  C   CYS A 156       4.194  29.431  54.209  1.00 43.29           C  
ATOM   1103  O   CYS A 156       3.846  28.547  53.432  1.00 41.52           O  
ATOM   1104  CB  CYS A 156       1.980  30.494  54.622  1.00 43.87           C  
ATOM   1105  SG  CYS A 156       1.753  29.642  56.202  1.00 45.30           S  
ATOM   1106  N   TYR A 157       5.224  29.332  55.041  1.00 43.10           N  
ATOM   1107  CA  TYR A 157       5.947  28.093  55.275  1.00 44.15           C  
ATOM   1108  C   TYR A 157       6.846  27.605  54.141  1.00 44.93           C  
ATOM   1109  O   TYR A 157       6.950  26.387  53.846  1.00 45.42           O  
ATOM   1110  CB  TYR A 157       5.020  27.029  55.862  1.00 44.52           C  
ATOM   1111  CG  TYR A 157       5.319  26.878  57.316  1.00 44.24           C  
ATOM   1112  CD1 TYR A 157       5.065  27.916  58.223  1.00 44.42           C  
ATOM   1113  CD2 TYR A 157       5.945  25.732  57.776  1.00 45.43           C  
ATOM   1114  CE1 TYR A 157       5.396  27.773  59.559  1.00 44.59           C  
ATOM   1115  CE2 TYR A 157       6.280  25.584  59.073  1.00 45.17           C  
ATOM   1116  CZ  TYR A 157       6.008  26.588  59.969  1.00 43.84           C  
ATOM   1117  OH  TYR A 157       6.363  26.373  61.272  1.00 43.13           O  
ATOM   1118  N   CYS A 158       7.542  28.577  53.554  1.00 44.39           N  
ATOM   1119  CA  CYS A 158       8.381  28.333  52.400  1.00 45.73           C  
ATOM   1120  C   CYS A 158       9.791  28.858  52.561  1.00 44.31           C  
ATOM   1121  O   CYS A 158      10.723  28.219  52.116  1.00 43.38           O  
ATOM   1122  CB  CYS A 158       7.749  28.938  51.149  1.00 45.93           C  
ATOM   1123  SG  CYS A 158       6.132  28.283  50.785  1.00 53.25           S  
ATOM   1124  N   LEU A 159       9.928  30.033  53.175  1.00 44.29           N  
ATOM   1125  CA  LEU A 159      11.210  30.744  53.212  1.00 44.16           C  
ATOM   1126  C   LEU A 159      12.321  30.102  54.041  1.00 42.58           C  
ATOM   1127  O   LEU A 159      13.465  30.496  53.928  1.00 41.80           O  
ATOM   1128  CB  LEU A 159      11.036  32.191  53.647  1.00 44.34           C  
ATOM   1129  CG  LEU A 159      10.694  33.059  52.443  1.00 49.07           C  
ATOM   1130  CD1 LEU A 159       9.897  34.229  52.928  1.00 51.01           C  
ATOM   1131  CD2 LEU A 159      11.968  33.496  51.720  1.00 51.10           C  
ATOM   1132  N   HIS A 160      11.989  29.102  54.836  1.00 42.46           N  
ATOM   1133  CA  HIS A 160      13.030  28.305  55.513  1.00 41.68           C  
ATOM   1134  C   HIS A 160      13.758  27.360  54.550  1.00 41.43           C  
ATOM   1135  O   HIS A 160      14.872  26.917  54.839  1.00 40.69           O  
ATOM   1136  CB  HIS A 160      12.420  27.544  56.694  1.00 41.14           C  
ATOM   1137  CG  HIS A 160      11.126  26.864  56.368  1.00 41.66           C  
ATOM   1138  ND1 HIS A 160       9.909  27.325  56.819  1.00 39.37           N  
ATOM   1139  CD2 HIS A 160      10.865  25.736  55.662  1.00 42.04           C  
ATOM   1140  CE1 HIS A 160       8.953  26.524  56.388  1.00 44.05           C  
ATOM   1141  NE2 HIS A 160       9.506  25.549  55.688  1.00 41.01           N  
ATOM   1142  N   TRP A 161      13.126  27.039  53.417  1.00 41.52           N  
ATOM   1143  CA  TRP A 161      13.812  26.301  52.330  1.00 41.69           C  
ATOM   1144  C   TRP A 161      14.850  27.203  51.661  1.00 41.82           C  
ATOM   1145  O   TRP A 161      14.506  28.283  51.175  1.00 42.54           O  
ATOM   1146  CB  TRP A 161      12.807  25.778  51.284  1.00 41.92           C  
ATOM   1147  CG  TRP A 161      11.949  24.662  51.799  1.00 41.02           C  
ATOM   1148  CD1 TRP A 161      10.671  24.763  52.265  1.00 43.20           C  
ATOM   1149  CD2 TRP A 161      12.308  23.293  51.917  1.00 41.59           C  
ATOM   1150  NE1 TRP A 161      10.214  23.542  52.684  1.00 40.90           N  
ATOM   1151  CE2 TRP A 161      11.195  22.615  52.477  1.00 41.49           C  
ATOM   1152  CE3 TRP A 161      13.463  22.571  51.626  1.00 42.19           C  
ATOM   1153  CZ2 TRP A 161      11.198  21.251  52.728  1.00 42.22           C  
ATOM   1154  CZ3 TRP A 161      13.469  21.195  51.863  1.00 42.87           C  
ATOM   1155  CH2 TRP A 161      12.345  20.549  52.413  1.00 43.00           C  
ATOM   1156  N   LEU A 162      16.114  26.777  51.671  1.00 40.69           N  
ATOM   1157  CA  LEU A 162      17.220  27.539  51.055  1.00 40.45           C  
ATOM   1158  C   LEU A 162      17.293  27.306  49.534  1.00 41.00           C  
ATOM   1159  O   LEU A 162      16.741  26.333  49.029  1.00 40.23           O  
ATOM   1160  CB  LEU A 162      18.555  27.155  51.703  1.00 39.68           C  
ATOM   1161  CG  LEU A 162      18.605  27.222  53.250  1.00 38.62           C  
ATOM   1162  CD1 LEU A 162      19.830  26.526  53.791  1.00 35.61           C  
ATOM   1163  CD2 LEU A 162      18.542  28.666  53.738  1.00 36.12           C  
ATOM   1164  N   SER A 163      17.976  28.196  48.816  1.00 42.01           N  
ATOM   1165  CA  SER A 163      18.222  28.006  47.368  1.00 43.45           C  
ATOM   1166  C   SER A 163      19.148  26.818  47.064  1.00 43.88           C  
ATOM   1167  O   SER A 163      19.127  26.247  45.952  1.00 43.06           O  
ATOM   1168  CB  SER A 163      18.808  29.280  46.768  1.00 43.79           C  
ATOM   1169  OG  SER A 163      20.179  29.432  47.123  1.00 44.62           O  
ATOM   1170  N   GLN A 164      19.955  26.433  48.052  1.00 44.05           N  
ATOM   1171  CA  GLN A 164      20.838  25.266  47.914  1.00 45.53           C  
ATOM   1172  C   GLN A 164      21.301  24.740  49.276  1.00 45.41           C  
ATOM   1173  O   GLN A 164      21.110  25.399  50.279  1.00 43.75           O  
ATOM   1174  CB  GLN A 164      22.061  25.615  47.050  1.00 46.04           C  
ATOM   1175  CG  GLN A 164      22.994  26.642  47.679  1.00 46.63           C  
ATOM   1176  CD  GLN A 164      24.285  26.820  46.922  1.00 47.04           C  
ATOM   1177  OE1 GLN A 164      24.330  27.574  45.967  1.00 50.37           O  
ATOM   1178  NE2 GLN A 164      25.355  26.133  47.358  1.00 49.81           N  
ATOM   1179  N   VAL A 165      21.926  23.563  49.305  1.00 45.69           N  
ATOM   1180  CA  VAL A 165      22.625  23.127  50.510  1.00 46.58           C  
ATOM   1181  C   VAL A 165      23.746  24.149  50.744  1.00 47.32           C  
ATOM   1182  O   VAL A 165      24.419  24.576  49.782  1.00 46.71           O  
ATOM   1183  CB  VAL A 165      23.103  21.646  50.410  1.00 47.03           C  
ATOM   1184  CG1 VAL A 165      24.076  21.267  51.526  1.00 46.39           C  
ATOM   1185  CG2 VAL A 165      21.893  20.734  50.465  1.00 48.16           C  
ATOM   1186  N   PRO A 166      23.878  24.639  51.993  1.00 47.88           N  
ATOM   1187  CA  PRO A 166      24.849  25.694  52.291  1.00 48.79           C  
ATOM   1188  C   PRO A 166      26.202  25.528  51.626  1.00 49.79           C  
ATOM   1189  O   PRO A 166      26.813  24.453  51.699  1.00 49.07           O  
ATOM   1190  CB  PRO A 166      24.950  25.636  53.813  1.00 48.30           C  
ATOM   1191  CG  PRO A 166      23.556  25.349  54.186  1.00 48.30           C  
ATOM   1192  CD  PRO A 166      23.082  24.310  53.195  1.00 47.69           C  
ATOM   1193  N   SER A 167      26.652  26.602  50.975  1.00 51.61           N  
ATOM   1194  CA  SER A 167      27.844  26.529  50.131  1.00 53.46           C  
ATOM   1195  C   SER A 167      29.143  26.351  50.920  1.00 54.20           C  
ATOM   1196  O   SER A 167      30.236  26.533  50.379  1.00 54.04           O  
ATOM   1197  CB  SER A 167      27.900  27.668  49.081  1.00 53.57           C  
ATOM   1198  OG  SER A 167      27.851  28.962  49.657  1.00 55.05           O  
ATOM   1199  N   GLY A 168      28.996  25.967  52.195  1.00 55.37           N  
ATOM   1200  CA  GLY A 168      30.092  25.470  53.034  1.00 55.48           C  
ATOM   1201  C   GLY A 168      30.230  23.951  52.963  1.00 56.56           C  
ATOM   1202  O   GLY A 168      30.755  23.382  51.976  1.00 56.81           O  
ATOM   1203  N   ILE A 175      29.656  18.843  50.836  1.00 59.79           N  
ATOM   1204  CA  ILE A 175      30.849  18.006  50.958  1.00 59.71           C  
ATOM   1205  C   ILE A 175      31.385  17.923  52.390  1.00 59.49           C  
ATOM   1206  O   ILE A 175      31.796  16.852  52.821  1.00 60.13           O  
ATOM   1207  CB  ILE A 175      31.979  18.454  50.007  1.00 59.93           C  
ATOM   1208  N   SER A 176      31.379  19.034  53.129  1.00 58.88           N  
ATOM   1209  CA  SER A 176      31.852  19.018  54.523  1.00 58.12           C  
ATOM   1210  C   SER A 176      30.950  18.132  55.398  1.00 57.24           C  
ATOM   1211  O   SER A 176      29.747  18.000  55.122  1.00 56.94           O  
ATOM   1212  CB  SER A 176      31.944  20.438  55.107  1.00 58.56           C  
ATOM   1213  N   VAL A 177      31.534  17.529  56.435  1.00 55.62           N  
ATOM   1214  CA  VAL A 177      30.803  16.581  57.280  1.00 54.21           C  
ATOM   1215  C   VAL A 177      30.043  17.218  58.466  1.00 52.79           C  
ATOM   1216  O   VAL A 177      30.644  17.757  59.415  1.00 52.39           O  
ATOM   1217  CB  VAL A 177      31.713  15.398  57.747  1.00 54.59           C  
ATOM   1218  CG1 VAL A 177      30.953  14.441  58.663  1.00 54.82           C  
ATOM   1219  CG2 VAL A 177      32.250  14.642  56.541  1.00 55.03           C  
ATOM   1220  N   ASN A 178      28.713  17.149  58.372  1.00 50.57           N  
ATOM   1221  CA  ASN A 178      27.794  17.447  59.464  1.00 49.09           C  
ATOM   1222  C   ASN A 178      27.420  16.116  60.160  1.00 48.90           C  
ATOM   1223  O   ASN A 178      26.414  15.487  59.823  1.00 49.09           O  
ATOM   1224  CB  ASN A 178      26.560  18.191  58.902  1.00 48.38           C  
ATOM   1225  CG  ASN A 178      25.635  18.743  59.989  1.00 46.76           C  
ATOM   1226  OD1 ASN A 178      26.031  18.918  61.140  1.00 43.07           O  
ATOM   1227  ND2 ASN A 178      24.390  19.039  59.611  1.00 40.26           N  
ATOM   1228  N   LYS A 179      28.263  15.682  61.110  1.00 48.08           N  
ATOM   1229  CA  LYS A 179      28.129  14.375  61.786  1.00 47.19           C  
ATOM   1230  C   LYS A 179      26.893  14.265  62.663  1.00 45.98           C  
ATOM   1231  O   LYS A 179      26.705  15.074  63.569  1.00 46.29           O  
ATOM   1232  CB  LYS A 179      29.352  14.073  62.677  1.00 46.74           C  
ATOM   1233  CG  LYS A 179      30.563  13.623  61.943  1.00 48.26           C  
ATOM   1234  N   GLY A 180      26.083  13.238  62.406  1.00 45.01           N  
ATOM   1235  CA  GLY A 180      24.888  12.931  63.197  1.00 43.74           C  
ATOM   1236  C   GLY A 180      23.723  13.895  63.047  1.00 43.28           C  
ATOM   1237  O   GLY A 180      22.728  13.789  63.775  1.00 43.36           O  
ATOM   1238  N   CYS A 181      23.845  14.821  62.095  1.00 42.02           N  
ATOM   1239  CA  CYS A 181      22.897  15.910  61.908  1.00 41.50           C  
ATOM   1240  C   CYS A 181      22.493  16.078  60.437  1.00 40.47           C  
ATOM   1241  O   CYS A 181      23.230  15.681  59.537  1.00 39.97           O  
ATOM   1242  CB  CYS A 181      23.509  17.208  62.436  1.00 41.18           C  
ATOM   1243  SG  CYS A 181      23.767  17.229  64.248  1.00 45.11           S  
ATOM   1244  N   ILE A 182      21.338  16.697  60.189  1.00 39.52           N  
ATOM   1245  CA  ILE A 182      20.878  16.888  58.808  1.00 38.64           C  
ATOM   1246  C   ILE A 182      20.777  18.368  58.412  1.00 38.71           C  
ATOM   1247  O   ILE A 182      20.606  18.689  57.240  1.00 36.85           O  
ATOM   1248  CB  ILE A 182      19.564  16.082  58.510  1.00 38.20           C  
ATOM   1249  CG1 ILE A 182      18.382  16.633  59.306  1.00 39.01           C  
ATOM   1250  CG2 ILE A 182      19.766  14.615  58.829  1.00 36.96           C  
ATOM   1251  CD1 ILE A 182      17.021  16.109  58.874  1.00 39.04           C  
ATOM   1252  N   TYR A 183      20.912  19.252  59.406  1.00 38.00           N  
ATOM   1253  CA  TYR A 183      20.898  20.702  59.178  1.00 38.49           C  
ATOM   1254  C   TYR A 183      21.566  21.368  60.405  1.00 38.80           C  
ATOM   1255  O   TYR A 183      22.192  20.680  61.225  1.00 38.67           O  
ATOM   1256  CB  TYR A 183      19.454  21.215  58.874  1.00 38.49           C  
ATOM   1257  CG  TYR A 183      18.612  21.484  60.106  1.00 37.90           C  
ATOM   1258  CD1 TYR A 183      18.300  20.464  61.011  1.00 36.69           C  
ATOM   1259  CD2 TYR A 183      18.162  22.790  60.391  1.00 37.74           C  
ATOM   1260  CE1 TYR A 183      17.537  20.751  62.201  1.00 36.73           C  
ATOM   1261  CE2 TYR A 183      17.422  23.070  61.530  1.00 37.61           C  
ATOM   1262  CZ  TYR A 183      17.112  22.051  62.434  1.00 38.76           C  
ATOM   1263  OH  TYR A 183      16.376  22.363  63.576  1.00 40.49           O  
ATOM   1264  N   SER A 184      21.454  22.683  60.511  1.00 38.35           N  
ATOM   1265  CA  SER A 184      21.983  23.429  61.626  1.00 39.63           C  
ATOM   1266  C   SER A 184      21.126  23.213  62.888  1.00 39.76           C  
ATOM   1267  O   SER A 184      20.557  24.146  63.427  1.00 40.01           O  
ATOM   1268  CB  SER A 184      22.075  24.915  61.270  1.00 39.28           C  
ATOM   1269  OG  SER A 184      20.905  25.351  60.613  1.00 41.52           O  
ATOM   1270  N   SER A 185      21.017  21.969  63.346  1.00 40.34           N  
ATOM   1271  CA  SER A 185      20.244  21.720  64.558  1.00 41.68           C  
ATOM   1272  C   SER A 185      21.024  22.266  65.751  1.00 42.42           C  
ATOM   1273  O   SER A 185      22.200  22.644  65.613  1.00 41.65           O  
ATOM   1274  CB  SER A 185      19.969  20.227  64.746  1.00 41.24           C  
ATOM   1275  OG  SER A 185      21.172  19.498  64.721  1.00 43.10           O  
ATOM   1276  N   LYS A 186      20.371  22.292  66.917  1.00 43.92           N  
ATOM   1277  CA  LYS A 186      21.027  22.708  68.167  1.00 44.89           C  
ATOM   1278  C   LYS A 186      22.263  21.869  68.504  1.00 45.21           C  
ATOM   1279  O   LYS A 186      23.229  22.361  69.107  1.00 46.87           O  
ATOM   1280  CB  LYS A 186      20.026  22.688  69.334  1.00 45.48           C  
ATOM   1281  N   ALA A 187      22.225  20.598  68.133  1.00 44.93           N  
ATOM   1282  CA  ALA A 187      23.357  19.704  68.307  1.00 44.27           C  
ATOM   1283  C   ALA A 187      24.461  19.804  67.235  1.00 43.92           C  
ATOM   1284  O   ALA A 187      25.524  19.205  67.407  1.00 43.67           O  
ATOM   1285  CB  ALA A 187      22.860  18.263  68.420  1.00 45.10           C  
ATOM   1286  N   SER A 188      24.225  20.537  66.136  1.00 43.01           N  
ATOM   1287  CA  SER A 188      25.257  20.687  65.101  1.00 42.38           C  
ATOM   1288  C   SER A 188      26.398  21.624  65.556  1.00 41.81           C  
ATOM   1289  O   SER A 188      26.169  22.586  66.305  1.00 40.89           O  
ATOM   1290  CB  SER A 188      24.650  21.173  63.770  1.00 41.31           C  
ATOM   1291  OG  SER A 188      24.187  22.493  63.918  1.00 42.77           O  
ATOM   1292  N   ARG A 189      27.608  21.362  65.058  1.00 41.17           N  
ATOM   1293  CA  ARG A 189      28.787  22.147  65.445  1.00 40.28           C  
ATOM   1294  C   ARG A 189      28.731  23.574  64.869  1.00 39.44           C  
ATOM   1295  O   ARG A 189      28.059  23.825  63.837  1.00 38.29           O  
ATOM   1296  CB  ARG A 189      30.071  21.428  65.041  1.00 40.76           C  
ATOM   1297  CG  ARG A 189      30.089  19.936  65.381  1.00 41.57           C  
ATOM   1298  CD  ARG A 189      30.829  19.618  66.663  1.00 47.28           C  
ATOM   1299  NE  ARG A 189      30.206  20.171  67.863  1.00 49.08           N  
ATOM   1300  CZ  ARG A 189      30.517  19.791  69.104  1.00 51.58           C  
ATOM   1301  NH1 ARG A 189      31.416  18.844  69.313  1.00 52.43           N  
ATOM   1302  NH2 ARG A 189      29.921  20.355  70.142  1.00 50.97           N  
ATOM   1303  N   PRO A 190      29.387  24.535  65.551  1.00 38.34           N  
ATOM   1304  CA  PRO A 190      29.260  25.922  65.068  1.00 37.91           C  
ATOM   1305  C   PRO A 190      29.680  26.255  63.612  1.00 36.73           C  
ATOM   1306  O   PRO A 190      29.121  27.193  63.076  1.00 37.00           O  
ATOM   1307  CB  PRO A 190      30.094  26.720  66.080  1.00 37.85           C  
ATOM   1308  CG  PRO A 190      30.005  25.881  67.341  1.00 37.97           C  
ATOM   1309  CD  PRO A 190      30.179  24.485  66.801  1.00 37.90           C  
ATOM   1310  N   PRO A 191      30.664  25.544  62.998  1.00 36.92           N  
ATOM   1311  CA  PRO A 191      30.907  25.910  61.586  1.00 36.75           C  
ATOM   1312  C   PRO A 191      29.703  25.587  60.682  1.00 37.20           C  
ATOM   1313  O   PRO A 191      29.505  26.249  59.640  1.00 36.10           O  
ATOM   1314  CB  PRO A 191      32.103  25.041  61.186  1.00 37.08           C  
ATOM   1315  CG  PRO A 191      32.742  24.574  62.505  1.00 36.51           C  
ATOM   1316  CD  PRO A 191      31.564  24.455  63.431  1.00 36.53           C  
ATOM   1317  N   ILE A 192      28.929  24.571  61.078  1.00 37.22           N  
ATOM   1318  CA  ILE A 192      27.702  24.195  60.368  1.00 37.93           C  
ATOM   1319  C   ILE A 192      26.641  25.262  60.546  1.00 38.02           C  
ATOM   1320  O   ILE A 192      26.041  25.726  59.558  1.00 37.09           O  
ATOM   1321  CB  ILE A 192      27.141  22.820  60.825  1.00 38.49           C  
ATOM   1322  CG1 ILE A 192      28.196  21.709  60.624  1.00 38.02           C  
ATOM   1323  CG2 ILE A 192      25.790  22.505  60.095  1.00 38.77           C  
ATOM   1324  CD1 ILE A 192      28.613  21.475  59.169  1.00 42.85           C  
ATOM   1325  N   GLN A 193      26.437  25.660  61.802  1.00 37.68           N  
ATOM   1326  CA  GLN A 193      25.496  26.707  62.154  1.00 38.85           C  
ATOM   1327  C   GLN A 193      25.821  27.976  61.364  1.00 38.05           C  
ATOM   1328  O   GLN A 193      24.931  28.619  60.842  1.00 38.30           O  
ATOM   1329  CB  GLN A 193      25.556  26.993  63.667  1.00 39.02           C  
ATOM   1330  CG  GLN A 193      25.174  25.815  64.591  1.00 40.00           C  
ATOM   1331  CD  GLN A 193      25.156  26.215  66.076  1.00 41.09           C  
ATOM   1332  OE1 GLN A 193      24.601  27.264  66.455  1.00 45.12           O  
ATOM   1333  NE2 GLN A 193      25.760  25.389  66.915  1.00 40.77           N  
ATOM   1334  N   LYS A 194      27.104  28.350  61.299  1.00 38.17           N  
ATOM   1335  CA  LYS A 194      27.493  29.576  60.562  1.00 38.44           C  
ATOM   1336  C   LYS A 194      27.287  29.426  59.048  1.00 36.78           C  
ATOM   1337  O   LYS A 194      26.861  30.355  58.375  1.00 36.96           O  
ATOM   1338  CB  LYS A 194      28.944  29.973  60.872  1.00 37.76           C  
ATOM   1339  CG  LYS A 194      29.406  31.276  60.191  1.00 39.82           C  
ATOM   1340  CD  LYS A 194      30.787  31.738  60.669  1.00 40.68           C  
ATOM   1341  CE  LYS A 194      31.461  32.659  59.654  1.00 45.37           C  
ATOM   1342  NZ  LYS A 194      32.066  31.884  58.517  1.00 48.40           N  
ATOM   1343  N   ALA A 195      27.628  28.259  58.508  1.00 37.00           N  
ATOM   1344  CA  ALA A 195      27.375  27.964  57.091  1.00 36.08           C  
ATOM   1345  C   ALA A 195      25.889  28.066  56.718  1.00 35.81           C  
ATOM   1346  O   ALA A 195      25.529  28.640  55.679  1.00 35.39           O  
ATOM   1347  CB  ALA A 195      27.958  26.553  56.701  1.00 37.13           C  
ATOM   1348  N   TYR A 196      25.022  27.507  57.553  1.00 36.03           N  
ATOM   1349  CA  TYR A 196      23.562  27.597  57.316  1.00 36.26           C  
ATOM   1350  C   TYR A 196      23.014  29.034  57.460  1.00 36.71           C  
ATOM   1351  O   TYR A 196      22.204  29.459  56.633  1.00 36.88           O  
ATOM   1352  CB  TYR A 196      22.794  26.618  58.211  1.00 36.27           C  
ATOM   1353  CG  TYR A 196      22.623  25.206  57.610  1.00 36.31           C  
ATOM   1354  CD1 TYR A 196      23.611  24.241  57.724  1.00 36.64           C  
ATOM   1355  CD2 TYR A 196      21.454  24.859  56.943  1.00 39.10           C  
ATOM   1356  CE1 TYR A 196      23.449  22.951  57.175  1.00 37.58           C  
ATOM   1357  CE2 TYR A 196      21.279  23.581  56.380  1.00 37.86           C  
ATOM   1358  CZ  TYR A 196      22.264  22.647  56.491  1.00 37.17           C  
ATOM   1359  OH  TYR A 196      22.046  21.412  55.935  1.00 34.74           O  
ATOM   1360  N   LEU A 197      23.459  29.771  58.488  1.00 36.81           N  
ATOM   1361  CA  LEU A 197      23.052  31.181  58.667  1.00 37.08           C  
ATOM   1362  C   LEU A 197      23.477  32.034  57.487  1.00 37.13           C  
ATOM   1363  O   LEU A 197      22.661  32.777  56.950  1.00 38.81           O  
ATOM   1364  CB  LEU A 197      23.550  31.800  60.004  1.00 37.08           C  
ATOM   1365  CG  LEU A 197      23.331  33.333  60.143  1.00 36.96           C  
ATOM   1366  CD1 LEU A 197      21.835  33.720  60.033  1.00 36.03           C  
ATOM   1367  CD2 LEU A 197      23.972  33.949  61.412  1.00 37.77           C  
ATOM   1368  N   ASP A 198      24.746  31.934  57.092  1.00 37.70           N  
ATOM   1369  CA  ASP A 198      25.275  32.671  55.940  1.00 38.13           C  
ATOM   1370  C   ASP A 198      24.489  32.374  54.670  1.00 37.81           C  
ATOM   1371  O   ASP A 198      24.258  33.281  53.902  1.00 37.56           O  
ATOM   1372  CB  ASP A 198      26.763  32.393  55.687  1.00 38.62           C  
ATOM   1373  CG  ASP A 198      27.695  33.069  56.702  1.00 40.32           C  
ATOM   1374  OD1 ASP A 198      27.327  34.074  57.366  1.00 43.63           O  
ATOM   1375  OD2 ASP A 198      28.843  32.592  56.795  1.00 43.53           O  
ATOM   1376  N   GLN A 199      24.080  31.118  54.457  1.00 37.46           N  
ATOM   1377  CA  GLN A 199      23.240  30.767  53.299  1.00 38.20           C  
ATOM   1378  C   GLN A 199      21.862  31.443  53.375  1.00 38.97           C  
ATOM   1379  O   GLN A 199      21.449  32.093  52.406  1.00 39.19           O  
ATOM   1380  CB  GLN A 199      23.094  29.237  53.105  1.00 37.64           C  
ATOM   1381  CG  GLN A 199      22.320  28.811  51.831  1.00 37.52           C  
ATOM   1382  CD  GLN A 199      23.039  29.226  50.533  1.00 39.95           C  
ATOM   1383  OE1 GLN A 199      24.217  28.957  50.361  1.00 41.67           O  
ATOM   1384  NE2 GLN A 199      22.332  29.889  49.640  1.00 41.18           N  
ATOM   1385  N   PHE A 200      21.171  31.303  54.517  1.00 38.88           N  
ATOM   1386  CA  PHE A 200      19.894  32.016  54.762  1.00 39.75           C  
ATOM   1387  C   PHE A 200      19.960  33.535  54.533  1.00 39.92           C  
ATOM   1388  O   PHE A 200      19.046  34.135  53.944  1.00 40.12           O  
ATOM   1389  CB  PHE A 200      19.345  31.740  56.189  1.00 39.56           C  
ATOM   1390  CG  PHE A 200      17.946  32.301  56.421  1.00 41.73           C  
ATOM   1391  CD1 PHE A 200      16.847  31.807  55.701  1.00 41.00           C  
ATOM   1392  CD2 PHE A 200      17.735  33.341  57.316  1.00 38.98           C  
ATOM   1393  CE1 PHE A 200      15.551  32.356  55.901  1.00 41.41           C  
ATOM   1394  CE2 PHE A 200      16.445  33.870  57.528  1.00 40.96           C  
ATOM   1395  CZ  PHE A 200      15.364  33.388  56.824  1.00 39.40           C  
ATOM   1396  N   THR A 201      21.036  34.142  55.022  1.00 40.20           N  
ATOM   1397  CA  THR A 201      21.325  35.568  54.853  1.00 40.52           C  
ATOM   1398  C   THR A 201      21.397  35.961  53.391  1.00 41.32           C  
ATOM   1399  O   THR A 201      20.784  36.967  53.007  1.00 41.05           O  
ATOM   1400  CB  THR A 201      22.642  35.973  55.585  1.00 39.93           C  
ATOM   1401  OG1 THR A 201      22.475  35.754  56.985  1.00 40.29           O  
ATOM   1402  CG2 THR A 201      22.993  37.431  55.373  1.00 39.96           C  
ATOM   1403  N   LYS A 202      22.155  35.188  52.604  1.00 40.94           N  
ATOM   1404  CA  LYS A 202      22.283  35.400  51.164  1.00 42.61           C  
ATOM   1405  C   LYS A 202      20.907  35.302  50.520  1.00 42.33           C  
ATOM   1406  O   LYS A 202      20.484  36.214  49.799  1.00 43.16           O  
ATOM   1407  CB  LYS A 202      23.179  34.338  50.489  1.00 41.94           C  
ATOM   1408  CG  LYS A 202      24.574  34.083  51.085  1.00 43.78           C  
ATOM   1409  CD  LYS A 202      25.388  33.067  50.240  1.00 44.01           C  
ATOM   1410  CE  LYS A 202      26.264  32.118  51.096  1.00 47.04           C  
ATOM   1411  NZ  LYS A 202      27.427  32.807  51.751  1.00 46.87           N  
ATOM   1412  N   ASP A 203      20.237  34.180  50.778  1.00 42.33           N  
ATOM   1413  CA  ASP A 203      18.940  33.832  50.193  1.00 42.91           C  
ATOM   1414  C   ASP A 203      17.845  34.851  50.510  1.00 43.10           C  
ATOM   1415  O   ASP A 203      17.209  35.375  49.598  1.00 43.77           O  
ATOM   1416  CB  ASP A 203      18.523  32.414  50.627  1.00 42.66           C  
ATOM   1417  CG  ASP A 203      19.333  31.327  49.914  1.00 43.96           C  
ATOM   1418  OD1 ASP A 203      19.910  31.621  48.846  1.00 45.24           O  
ATOM   1419  OD2 ASP A 203      19.414  30.189  50.415  1.00 44.06           O  
ATOM   1420  N   PHE A 204      17.665  35.132  51.792  1.00 42.37           N  
ATOM   1421  CA  PHE A 204      16.648  36.079  52.286  1.00 42.88           C  
ATOM   1422  C   PHE A 204      16.909  37.526  51.857  1.00 42.46           C  
ATOM   1423  O   PHE A 204      15.983  38.253  51.530  1.00 43.18           O  
ATOM   1424  CB  PHE A 204      16.510  35.946  53.808  1.00 42.62           C  
ATOM   1425  CG  PHE A 204      15.296  36.636  54.386  1.00 44.24           C  
ATOM   1426  CD1 PHE A 204      14.065  36.614  53.717  1.00 45.02           C  
ATOM   1427  CD2 PHE A 204      15.375  37.278  55.619  1.00 43.35           C  
ATOM   1428  CE1 PHE A 204      12.943  37.264  54.252  1.00 45.15           C  
ATOM   1429  CE2 PHE A 204      14.245  37.925  56.171  1.00 43.42           C  
ATOM   1430  CZ  PHE A 204      13.039  37.911  55.494  1.00 43.00           C  
ATOM   1431  N   THR A 205      18.169  37.937  51.842  1.00 42.18           N  
ATOM   1432  CA  THR A 205      18.536  39.246  51.322  1.00 42.11           C  
ATOM   1433  C   THR A 205      18.139  39.367  49.834  1.00 42.03           C  
ATOM   1434  O   THR A 205      17.605  40.401  49.417  1.00 41.52           O  
ATOM   1435  CB  THR A 205      20.046  39.517  51.498  1.00 42.02           C  
ATOM   1436  OG1 THR A 205      20.390  39.395  52.886  1.00 42.89           O  
ATOM   1437  CG2 THR A 205      20.420  40.938  51.009  1.00 42.72           C  
ATOM   1438  N   THR A 206      18.443  38.334  49.051  1.00 40.52           N  
ATOM   1439  CA  THR A 206      18.073  38.270  47.609  1.00 41.38           C  
ATOM   1440  C   THR A 206      16.549  38.316  47.401  1.00 41.36           C  
ATOM   1441  O   THR A 206      16.046  39.096  46.575  1.00 41.98           O  
ATOM   1442  CB  THR A 206      18.608  36.960  46.968  1.00 40.96           C  
ATOM   1443  OG1 THR A 206      20.032  36.957  47.031  1.00 41.86           O  
ATOM   1444  CG2 THR A 206      18.165  36.795  45.517  1.00 42.92           C  
ATOM   1445  N   PHE A 207      15.837  37.477  48.146  1.00 40.35           N  
ATOM   1446  CA  PHE A 207      14.385  37.486  48.201  1.00 40.76           C  
ATOM   1447  C   PHE A 207      13.845  38.919  48.391  1.00 40.06           C  
ATOM   1448  O   PHE A 207      12.977  39.378  47.656  1.00 38.04           O  
ATOM   1449  CB  PHE A 207      13.920  36.596  49.360  1.00 41.98           C  
ATOM   1450  CG  PHE A 207      12.429  36.383  49.410  1.00 45.03           C  
ATOM   1451  CD1 PHE A 207      11.613  37.235  50.150  1.00 46.67           C  
ATOM   1452  CD2 PHE A 207      11.838  35.347  48.696  1.00 46.11           C  
ATOM   1453  CE1 PHE A 207      10.230  37.072  50.176  1.00 45.78           C  
ATOM   1454  CE2 PHE A 207      10.439  35.156  48.743  1.00 46.60           C  
ATOM   1455  CZ  PHE A 207       9.643  36.025  49.491  1.00 46.58           C  
ATOM   1456  N   LEU A 208      14.389  39.616  49.371  1.00 40.20           N  
ATOM   1457  CA  LEU A 208      13.918  40.942  49.726  1.00 40.89           C  
ATOM   1458  C   LEU A 208      14.258  41.977  48.650  1.00 42.14           C  
ATOM   1459  O   LEU A 208      13.411  42.831  48.278  1.00 43.28           O  
ATOM   1460  CB  LEU A 208      14.497  41.337  51.082  1.00 41.05           C  
ATOM   1461  CG  LEU A 208      14.013  40.599  52.338  1.00 39.42           C  
ATOM   1462  CD1 LEU A 208      14.974  40.845  53.483  1.00 35.38           C  
ATOM   1463  CD2 LEU A 208      12.578  41.037  52.747  1.00 40.86           C  
ATOM   1464  N   ARG A 209      15.497  41.928  48.161  1.00 42.26           N  
ATOM   1465  CA  ARG A 209      15.940  42.874  47.143  1.00 42.93           C  
ATOM   1466  C   ARG A 209      15.085  42.731  45.882  1.00 43.32           C  
ATOM   1467  O   ARG A 209      14.582  43.724  45.366  1.00 43.30           O  
ATOM   1468  CB  ARG A 209      17.418  42.700  46.808  1.00 42.94           C  
ATOM   1469  CG  ARG A 209      17.880  43.652  45.702  1.00 45.12           C  
ATOM   1470  CD  ARG A 209      19.298  43.359  45.232  1.00 49.00           C  
ATOM   1471  NE  ARG A 209      19.499  41.956  44.864  1.00 49.28           N  
ATOM   1472  CZ  ARG A 209      19.203  41.443  43.674  1.00 53.45           C  
ATOM   1473  NH1 ARG A 209      18.677  42.204  42.714  1.00 52.95           N  
ATOM   1474  NH2 ARG A 209      19.433  40.153  43.445  1.00 55.71           N  
ATOM   1475  N   ILE A 210      14.901  41.493  45.431  1.00 43.41           N  
ATOM   1476  CA  ILE A 210      14.155  41.196  44.197  1.00 44.41           C  
ATOM   1477  C   ILE A 210      12.672  41.510  44.277  1.00 44.38           C  
ATOM   1478  O   ILE A 210      12.116  42.169  43.376  1.00 45.57           O  
ATOM   1479  CB  ILE A 210      14.365  39.732  43.765  1.00 44.79           C  
ATOM   1480  CG1 ILE A 210      15.773  39.600  43.176  1.00 44.77           C  
ATOM   1481  CG2 ILE A 210      13.268  39.286  42.779  1.00 45.66           C  
ATOM   1482  CD1 ILE A 210      16.160  38.237  42.859  1.00 47.33           C  
ATOM   1483  N   HIS A 211      12.027  41.067  45.345  1.00 43.08           N  
ATOM   1484  CA  HIS A 211      10.599  41.307  45.456  1.00 43.33           C  
ATOM   1485  C   HIS A 211      10.212  42.755  45.813  1.00 42.65           C  
ATOM   1486  O   HIS A 211       9.152  43.217  45.406  1.00 41.95           O  
ATOM   1487  CB  HIS A 211       9.939  40.246  46.337  1.00 43.50           C  
ATOM   1488  CG  HIS A 211      10.155  38.849  45.811  1.00 44.60           C  
ATOM   1489  ND1 HIS A 211       9.680  38.441  44.583  1.00 44.79           N  
ATOM   1490  CD2 HIS A 211      10.853  37.802  46.309  1.00 45.51           C  
ATOM   1491  CE1 HIS A 211      10.067  37.197  44.354  1.00 46.50           C  
ATOM   1492  NE2 HIS A 211      10.777  36.783  45.389  1.00 45.50           N  
ATOM   1493  N   SER A 212      11.059  43.460  46.553  1.00 42.45           N  
ATOM   1494  CA  SER A 212      10.824  44.905  46.747  1.00 43.07           C  
ATOM   1495  C   SER A 212      10.684  45.585  45.399  1.00 42.50           C  
ATOM   1496  O   SER A 212       9.798  46.408  45.233  1.00 43.13           O  
ATOM   1497  CB  SER A 212      11.904  45.574  47.585  1.00 43.09           C  
ATOM   1498  OG  SER A 212      13.129  45.612  46.892  1.00 47.06           O  
ATOM   1499  N   GLU A 213      11.537  45.228  44.434  1.00 42.70           N  
ATOM   1500  CA  GLU A 213      11.492  45.836  43.094  1.00 43.36           C  
ATOM   1501  C   GLU A 213      10.177  45.573  42.355  1.00 42.09           C  
ATOM   1502  O   GLU A 213       9.739  46.408  41.569  1.00 41.45           O  
ATOM   1503  CB  GLU A 213      12.668  45.366  42.228  1.00 43.73           C  
ATOM   1504  CG  GLU A 213      14.048  45.743  42.758  1.00 46.82           C  
ATOM   1505  CD  GLU A 213      15.194  45.283  41.855  0.75 46.16           C  
ATOM   1506  OE1 GLU A 213      14.971  45.059  40.637  0.75 49.75           O  
ATOM   1507  OE2 GLU A 213      16.334  45.169  42.366  0.75 51.07           O  
ATOM   1508  N   GLU A 214       9.586  44.400  42.592  1.00 41.22           N  
ATOM   1509  CA  GLU A 214       8.295  43.996  41.998  1.00 41.05           C  
ATOM   1510  C   GLU A 214       7.071  44.715  42.586  1.00 41.33           C  
ATOM   1511  O   GLU A 214       6.006  44.803  41.949  1.00 41.48           O  
ATOM   1512  CB  GLU A 214       8.106  42.481  42.162  1.00 40.96           C  
ATOM   1513  CG  GLU A 214       9.113  41.667  41.361  1.00 40.10           C  
ATOM   1514  CD  GLU A 214       9.159  40.206  41.770  1.00 42.49           C  
ATOM   1515  OE1 GLU A 214       8.520  39.830  42.768  1.00 44.53           O  
ATOM   1516  OE2 GLU A 214       9.856  39.442  41.091  1.00 42.19           O  
ATOM   1517  N   LEU A 215       7.214  45.219  43.808  1.00 40.67           N  
ATOM   1518  CA  LEU A 215       6.115  45.871  44.495  1.00 40.73           C  
ATOM   1519  C   LEU A 215       5.925  47.323  44.087  1.00 40.88           C  
ATOM   1520  O   LEU A 215       6.890  48.067  43.945  1.00 40.88           O  
ATOM   1521  CB  LEU A 215       6.337  45.810  46.011  1.00 40.78           C  
ATOM   1522  CG  LEU A 215       6.132  44.472  46.694  1.00 39.37           C  
ATOM   1523  CD1 LEU A 215       6.655  44.571  48.113  1.00 38.72           C  
ATOM   1524  CD2 LEU A 215       4.649  44.094  46.682  1.00 40.00           C  
ATOM   1525  N   ILE A 216       4.665  47.703  43.888  1.00 40.60           N  
ATOM   1526  CA  ILE A 216       4.265  49.106  43.782  1.00 40.87           C  
ATOM   1527  C   ILE A 216       4.626  49.806  45.079  1.00 41.34           C  
ATOM   1528  O   ILE A 216       4.698  49.191  46.128  1.00 40.12           O  
ATOM   1529  CB  ILE A 216       2.732  49.209  43.511  1.00 40.88           C  
ATOM   1530  CG1 ILE A 216       2.438  48.775  42.078  1.00 40.02           C  
ATOM   1531  CG2 ILE A 216       2.161  50.630  43.785  1.00 39.78           C  
ATOM   1532  CD1 ILE A 216       1.080  48.088  41.897  1.00 40.52           C  
ATOM   1533  N   SER A 217       4.853  51.111  44.992  1.00 41.75           N  
ATOM   1534  CA  SER A 217       5.223  51.896  46.146  1.00 43.43           C  
ATOM   1535  C   SER A 217       4.294  51.654  47.355  1.00 42.75           C  
ATOM   1536  O   SER A 217       3.053  51.657  47.223  1.00 42.34           O  
ATOM   1537  CB  SER A 217       5.244  53.368  45.762  1.00 42.57           C  
ATOM   1538  OG  SER A 217       5.950  54.084  46.730  1.00 48.54           O  
ATOM   1539  N   ARG A 218       4.923  51.427  48.512  1.00 42.52           N  
ATOM   1540  CA  ARG A 218       4.246  51.111  49.782  1.00 41.54           C  
ATOM   1541  C   ARG A 218       3.499  49.754  49.770  1.00 41.90           C  
ATOM   1542  O   ARG A 218       2.702  49.456  50.673  1.00 41.70           O  
ATOM   1543  CB  ARG A 218       3.371  52.296  50.234  1.00 42.65           C  
ATOM   1544  CG  ARG A 218       4.187  53.559  50.531  1.00 40.05           C  
ATOM   1545  CD  ARG A 218       3.405  54.801  50.162  1.00 46.10           C  
ATOM   1546  N   GLY A 219       3.804  48.922  48.766  1.00 41.18           N  
ATOM   1547  CA  GLY A 219       3.286  47.532  48.682  1.00 40.32           C  
ATOM   1548  C   GLY A 219       3.805  46.679  49.825  1.00 40.75           C  
ATOM   1549  O   GLY A 219       4.804  47.019  50.450  1.00 41.35           O  
ATOM   1550  N   ARG A 220       3.144  45.562  50.125  1.00 40.84           N  
ATOM   1551  CA  ARG A 220       3.528  44.812  51.318  1.00 41.57           C  
ATOM   1552  C   ARG A 220       3.778  43.355  51.044  1.00 41.69           C  
ATOM   1553  O   ARG A 220       3.308  42.822  50.044  1.00 39.56           O  
ATOM   1554  CB  ARG A 220       2.492  44.961  52.431  1.00 41.87           C  
ATOM   1555  CG  ARG A 220       2.313  46.369  52.918  1.00 42.09           C  
ATOM   1556  CD  ARG A 220       1.271  46.397  53.983  1.00 43.96           C  
ATOM   1557  NE  ARG A 220       0.994  47.761  54.432  1.00 42.54           N  
ATOM   1558  CZ  ARG A 220       0.338  48.048  55.548  1.00 42.05           C  
ATOM   1559  NH1 ARG A 220      -0.100  47.069  56.324  1.00 40.15           N  
ATOM   1560  NH2 ARG A 220       0.130  49.309  55.891  1.00 39.96           N  
ATOM   1561  N   MET A 221       4.559  42.738  51.932  1.00 42.61           N  
ATOM   1562  CA  MET A 221       4.737  41.279  51.973  1.00 44.42           C  
ATOM   1563  C   MET A 221       4.324  40.775  53.343  1.00 42.90           C  
ATOM   1564  O   MET A 221       4.534  41.459  54.355  1.00 42.93           O  
ATOM   1565  CB  MET A 221       6.189  40.839  51.689  1.00 44.53           C  
ATOM   1566  CG  MET A 221       6.866  41.506  50.486  1.00 47.30           C  
ATOM   1567  SD  MET A 221       8.163  40.449  49.773  1.00 49.39           S  
ATOM   1568  CE  MET A 221       9.417  40.484  51.034  1.00 49.25           C  
ATOM   1569  N   LEU A 222       3.717  39.591  53.373  1.00 41.61           N  
ATOM   1570  CA  LEU A 222       3.396  38.923  54.620  1.00 40.91           C  
ATOM   1571  C   LEU A 222       4.047  37.548  54.538  1.00 40.29           C  
ATOM   1572  O   LEU A 222       3.669  36.761  53.692  1.00 38.86           O  
ATOM   1573  CB  LEU A 222       1.897  38.701  54.744  1.00 41.26           C  
ATOM   1574  CG  LEU A 222       1.185  38.535  56.102  1.00 44.56           C  
ATOM   1575  CD1 LEU A 222       0.235  37.342  56.062  1.00 45.71           C  
ATOM   1576  CD2 LEU A 222       2.112  38.425  57.287  1.00 43.99           C  
ATOM   1577  N   LEU A 223       4.996  37.273  55.432  1.00 39.52           N  
ATOM   1578  CA  LEU A 223       5.789  36.043  55.367  1.00 39.61           C  
ATOM   1579  C   LEU A 223       5.691  35.279  56.659  1.00 39.45           C  
ATOM   1580  O   LEU A 223       5.814  35.847  57.724  1.00 38.91           O  
ATOM   1581  CB  LEU A 223       7.253  36.351  55.078  1.00 39.37           C  
ATOM   1582  CG  LEU A 223       7.600  37.371  53.986  1.00 39.53           C  
ATOM   1583  CD1 LEU A 223       9.084  37.667  54.047  1.00 41.10           C  
ATOM   1584  CD2 LEU A 223       7.160  36.924  52.596  1.00 36.85           C  
ATOM   1585  N   THR A 224       5.499  33.966  56.548  1.00 40.00           N  
ATOM   1586  CA  THR A 224       5.421  33.081  57.698  1.00 39.94           C  
ATOM   1587  C   THR A 224       6.344  31.882  57.417  1.00 40.07           C  
ATOM   1588  O   THR A 224       6.345  31.371  56.321  1.00 39.93           O  
ATOM   1589  CB  THR A 224       3.957  32.594  57.951  1.00 40.69           C  
ATOM   1590  OG1 THR A 224       3.097  33.718  58.174  1.00 41.83           O  
ATOM   1591  CG2 THR A 224       3.865  31.674  59.178  1.00 39.61           C  
ATOM   1592  N   PHE A 225       7.206  31.528  58.363  1.00 39.94           N  
ATOM   1593  CA  PHE A 225       8.130  30.398  58.162  1.00 40.21           C  
ATOM   1594  C   PHE A 225       8.636  29.919  59.506  1.00 40.16           C  
ATOM   1595  O   PHE A 225       8.318  30.514  60.537  1.00 38.90           O  
ATOM   1596  CB  PHE A 225       9.283  30.749  57.176  1.00 40.79           C  
ATOM   1597  CG  PHE A 225       9.960  32.059  57.469  1.00 41.25           C  
ATOM   1598  CD1 PHE A 225      11.102  32.092  58.258  1.00 41.35           C  
ATOM   1599  CD2 PHE A 225       9.417  33.274  57.003  1.00 42.63           C  
ATOM   1600  CE1 PHE A 225      11.722  33.302  58.562  1.00 43.28           C  
ATOM   1601  CE2 PHE A 225      10.027  34.468  57.266  1.00 43.03           C  
ATOM   1602  CZ  PHE A 225      11.186  34.505  58.064  1.00 43.44           C  
ATOM   1603  N   ILE A 226       9.363  28.805  59.504  1.00 40.58           N  
ATOM   1604  CA  ILE A 226       9.882  28.209  60.727  1.00 42.09           C  
ATOM   1605  C   ILE A 226      10.836  29.171  61.426  1.00 42.81           C  
ATOM   1606  O   ILE A 226      11.658  29.784  60.774  1.00 43.58           O  
ATOM   1607  CB  ILE A 226      10.627  26.871  60.425  1.00 42.12           C  
ATOM   1608  CG1 ILE A 226       9.657  25.803  59.915  1.00 40.89           C  
ATOM   1609  CG2 ILE A 226      11.357  26.348  61.668  1.00 43.17           C  
ATOM   1610  CD1 ILE A 226      10.372  24.552  59.424  1.00 41.75           C  
ATOM   1611  N   CYS A 227      10.730  29.303  62.746  1.00 44.18           N  
ATOM   1612  CA  CYS A 227      11.826  29.923  63.489  1.00 45.03           C  
ATOM   1613  C   CYS A 227      12.375  29.104  64.687  1.00 45.15           C  
ATOM   1614  O   CYS A 227      11.763  28.151  65.163  1.00 43.98           O  
ATOM   1615  CB  CYS A 227      11.513  31.376  63.861  1.00 45.44           C  
ATOM   1616  SG  CYS A 227      10.488  31.550  65.290  1.00 47.77           S  
ATOM   1617  N   LYS A 228      13.578  29.469  65.101  1.00 46.25           N  
ATOM   1618  CA  LYS A 228      14.246  28.865  66.234  1.00 48.56           C  
ATOM   1619  C   LYS A 228      14.212  29.888  67.353  1.00 49.85           C  
ATOM   1620  O   LYS A 228      14.519  31.066  67.152  1.00 50.86           O  
ATOM   1621  CB  LYS A 228      15.660  28.423  65.839  1.00 48.81           C  
ATOM   1622  CG  LYS A 228      16.771  28.646  66.849  1.00 51.88           C  
ATOM   1623  CD  LYS A 228      17.677  29.833  66.460  1.00 52.14           C  
ATOM   1624  CE  LYS A 228      18.469  29.545  65.187  1.00 50.80           C  
ATOM   1625  NZ  LYS A 228      19.596  30.508  64.964  1.00 50.50           N  
ATOM   1626  N   GLU A 229      13.754  29.442  68.509  1.00 50.42           N  
ATOM   1627  CA  GLU A 229      13.669  30.266  69.704  1.00 52.11           C  
ATOM   1628  C   GLU A 229      14.591  29.665  70.752  1.00 52.38           C  
ATOM   1629  O   GLU A 229      14.404  28.516  71.165  1.00 52.12           O  
ATOM   1630  CB  GLU A 229      12.240  30.273  70.251  1.00 52.35           C  
ATOM   1631  CG  GLU A 229      11.132  30.585  69.238  1.00 53.84           C  
ATOM   1632  CD  GLU A 229       9.979  31.307  69.906  1.00 55.40           C  
ATOM   1633  OE1 GLU A 229      10.273  32.134  70.792  1.00 57.36           O  
ATOM   1634  OE2 GLU A 229       8.796  31.062  69.567  1.00 55.07           O  
ATOM   1635  N   ASP A 230      15.603  30.432  71.149  1.00 53.08           N  
ATOM   1636  CA  ASP A 230      16.547  30.020  72.198  1.00 53.58           C  
ATOM   1637  C   ASP A 230      15.846  29.641  73.507  1.00 53.71           C  
ATOM   1638  O   ASP A 230      16.205  28.648  74.140  1.00 53.85           O  
ATOM   1639  N   GLU A 231      14.825  30.411  73.872  1.00 54.01           N  
ATOM   1640  CA  GLU A 231      14.118  30.253  75.146  1.00 54.33           C  
ATOM   1641  C   GLU A 231      13.285  28.977  75.348  1.00 54.26           C  
ATOM   1642  O   GLU A 231      12.924  28.666  76.476  1.00 54.76           O  
ATOM   1643  CB  GLU A 231      13.238  31.482  75.397  1.00 54.54           C  
ATOM   1644  N   PHE A 232      12.987  28.230  74.283  1.00 54.33           N  
ATOM   1645  CA  PHE A 232      11.967  27.163  74.393  1.00 53.64           C  
ATOM   1646  C   PHE A 232      12.412  25.695  74.516  1.00 52.88           C  
ATOM   1647  O   PHE A 232      12.173  25.067  75.558  1.00 53.14           O  
ATOM   1648  CB  PHE A 232      10.892  27.341  73.311  1.00 53.78           C  
ATOM   1649  CG  PHE A 232       9.968  28.492  73.583  1.00 53.46           C  
ATOM   1650  CD1 PHE A 232       9.645  28.829  74.888  1.00 52.45           C  
ATOM   1651  CD2 PHE A 232       9.419  29.227  72.544  1.00 52.97           C  
ATOM   1652  CE1 PHE A 232       8.802  29.896  75.162  1.00 53.25           C  
ATOM   1653  CE2 PHE A 232       8.564  30.299  72.805  1.00 52.81           C  
ATOM   1654  CZ  PHE A 232       8.259  30.631  74.115  1.00 53.86           C  
ATOM   1655  N   ASP A 233      13.059  25.198  73.460  1.00 51.55           N  
ATOM   1656  CA  ASP A 233      13.447  23.786  73.198  1.00 50.72           C  
ATOM   1657  C   ASP A 233      12.368  22.892  72.530  1.00 49.36           C  
ATOM   1658  O   ASP A 233      12.141  21.753  72.953  1.00 49.42           O  
ATOM   1659  CB  ASP A 233      14.097  23.100  74.402  1.00 51.38           C  
ATOM   1660  CG  ASP A 233      15.276  22.205  74.009  1.00 52.80           C  
ATOM   1661  OD1 ASP A 233      15.656  22.176  72.818  1.00 55.22           O  
ATOM   1662  OD2 ASP A 233      15.846  21.537  74.907  1.00 56.35           O  
ATOM   1663  N   HIS A 234      11.724  23.414  71.486  1.00 47.38           N  
ATOM   1664  CA  HIS A 234      10.717  22.655  70.726  1.00 45.96           C  
ATOM   1665  C   HIS A 234      11.240  22.158  69.385  1.00 45.38           C  
ATOM   1666  O   HIS A 234      11.532  22.977  68.490  1.00 46.14           O  
ATOM   1667  CB  HIS A 234       9.465  23.489  70.428  1.00 45.59           C  
ATOM   1668  CG  HIS A 234       8.915  24.218  71.609  1.00 43.30           C  
ATOM   1669  ND1 HIS A 234       8.463  25.517  71.531  1.00 39.99           N  
ATOM   1670  CD2 HIS A 234       8.761  23.840  72.902  1.00 42.80           C  
ATOM   1671  CE1 HIS A 234       8.043  25.903  72.722  1.00 42.87           C  
ATOM   1672  NE2 HIS A 234       8.213  24.905  73.570  1.00 40.89           N  
ATOM   1673  N   PRO A 235      11.274  20.822  69.205  1.00 44.27           N  
ATOM   1674  CA  PRO A 235      11.731  20.195  67.963  1.00 44.10           C  
ATOM   1675  C   PRO A 235      10.813  20.530  66.797  1.00 44.23           C  
ATOM   1676  O   PRO A 235       9.603  20.295  66.859  1.00 44.30           O  
ATOM   1677  CB  PRO A 235      11.644  18.693  68.262  1.00 43.48           C  
ATOM   1678  CG  PRO A 235      11.617  18.598  69.814  1.00 44.15           C  
ATOM   1679  CD  PRO A 235      10.857  19.818  70.207  1.00 44.61           C  
ATOM   1680  N   ASN A 236      11.399  21.075  65.738  1.00 44.10           N  
ATOM   1681  CA  ASN A 236      10.692  21.299  64.498  1.00 43.42           C  
ATOM   1682  C   ASN A 236      10.662  19.997  63.677  1.00 43.82           C  
ATOM   1683  O   ASN A 236      11.215  18.982  64.108  1.00 44.52           O  
ATOM   1684  CB  ASN A 236      11.329  22.485  63.768  1.00 43.67           C  
ATOM   1685  CG  ASN A 236      12.826  22.318  63.549  1.00 43.43           C  
ATOM   1686  OD1 ASN A 236      13.298  21.244  63.176  1.00 40.92           O  
ATOM   1687  ND2 ASN A 236      13.580  23.394  63.766  1.00 41.90           N  
ATOM   1688  N   SER A 237      10.023  20.002  62.508  1.00 44.69           N  
ATOM   1689  CA  SER A 237       9.918  18.788  61.679  1.00 44.30           C  
ATOM   1690  C   SER A 237      11.271  18.207  61.236  1.00 43.77           C  
ATOM   1691  O   SER A 237      11.430  16.968  61.171  1.00 42.95           O  
ATOM   1692  CB  SER A 237       9.021  19.051  60.460  1.00 44.00           C  
ATOM   1693  OG  SER A 237       9.580  20.052  59.638  1.00 45.81           O  
ATOM   1694  N   MET A 238      12.250  19.075  60.965  1.00 44.01           N  
ATOM   1695  CA  MET A 238      13.617  18.599  60.638  1.00 44.12           C  
ATOM   1696  C   MET A 238      14.233  17.946  61.857  1.00 44.22           C  
ATOM   1697  O   MET A 238      14.960  16.960  61.713  1.00 44.78           O  
ATOM   1698  CB  MET A 238      14.567  19.714  60.188  1.00 44.29           C  
ATOM   1699  CG  MET A 238      14.149  20.514  58.975  1.00 46.19           C  
ATOM   1700  SD  MET A 238      13.054  21.878  59.479  1.00 48.79           S  
ATOM   1701  CE  MET A 238      14.143  23.028  60.300  1.00 45.37           C  
ATOM   1702  N   ASP A 239      13.972  18.496  63.058  1.00 44.19           N  
ATOM   1703  CA  ASP A 239      14.520  17.882  64.310  1.00 43.13           C  
ATOM   1704  C   ASP A 239      13.941  16.488  64.536  1.00 43.22           C  
ATOM   1705  O   ASP A 239      14.672  15.549  64.900  1.00 41.72           O  
ATOM   1706  CB  ASP A 239      14.286  18.732  65.569  1.00 43.68           C  
ATOM   1707  CG  ASP A 239      14.967  20.088  65.512  1.00 46.30           C  
ATOM   1708  OD1 ASP A 239      16.135  20.197  65.054  1.00 46.99           O  
ATOM   1709  OD2 ASP A 239      14.315  21.066  65.930  1.00 47.47           O  
ATOM   1710  N   LEU A 240      12.632  16.341  64.325  1.00 43.38           N  
ATOM   1711  CA  LEU A 240      11.968  15.021  64.422  1.00 43.20           C  
ATOM   1712  C   LEU A 240      12.565  14.044  63.419  1.00 43.40           C  
ATOM   1713  O   LEU A 240      12.819  12.850  63.742  1.00 43.71           O  
ATOM   1714  CB  LEU A 240      10.457  15.152  64.174  1.00 43.84           C  
ATOM   1715  CG  LEU A 240       9.621  15.916  65.208  1.00 44.51           C  
ATOM   1716  CD1 LEU A 240       8.177  16.149  64.746  1.00 44.79           C  
ATOM   1717  CD2 LEU A 240       9.686  15.145  66.536  1.00 41.76           C  
ATOM   1718  N   LEU A 241      12.805  14.538  62.203  1.00 43.16           N  
ATOM   1719  CA  LEU A 241      13.431  13.729  61.171  1.00 43.15           C  
ATOM   1720  C   LEU A 241      14.838  13.327  61.603  1.00 43.58           C  
ATOM   1721  O   LEU A 241      15.187  12.166  61.510  1.00 42.53           O  
ATOM   1722  CB  LEU A 241      13.451  14.473  59.822  1.00 43.41           C  
ATOM   1723  CG  LEU A 241      13.972  13.789  58.566  1.00 43.79           C  
ATOM   1724  CD1 LEU A 241      13.312  12.433  58.359  1.00 42.01           C  
ATOM   1725  CD2 LEU A 241      13.814  14.726  57.327  1.00 41.35           C  
ATOM   1726  N   GLU A 242      15.633  14.299  62.055  1.00 44.03           N  
ATOM   1727  CA  GLU A 242      17.039  14.056  62.428  1.00 45.50           C  
ATOM   1728  C   GLU A 242      17.151  12.991  63.522  1.00 46.41           C  
ATOM   1729  O   GLU A 242      17.953  12.056  63.415  1.00 46.05           O  
ATOM   1730  CB  GLU A 242      17.709  15.366  62.861  1.00 45.98           C  
ATOM   1731  CG  GLU A 242      19.235  15.339  63.039  1.00 45.85           C  
ATOM   1732  CD  GLU A 242      19.792  16.725  63.292  1.00 46.93           C  
ATOM   1733  OE1 GLU A 242      19.865  17.517  62.326  1.00 47.36           O  
ATOM   1734  OE2 GLU A 242      20.151  17.042  64.453  1.00 49.59           O  
ATOM   1735  N   MET A 243      16.325  13.116  64.561  1.00 46.81           N  
ATOM   1736  CA  MET A 243      16.372  12.167  65.660  1.00 47.81           C  
ATOM   1737  C   MET A 243      15.933  10.766  65.225  1.00 46.00           C  
ATOM   1738  O   MET A 243      16.426   9.784  65.747  1.00 45.20           O  
ATOM   1739  CB  MET A 243      15.602  12.677  66.891  1.00 47.22           C  
ATOM   1740  CG  MET A 243      14.108  12.880  66.749  1.00 49.65           C  
ATOM   1741  SD  MET A 243      13.357  13.327  68.346  1.00 53.89           S  
ATOM   1742  CE  MET A 243      13.266  15.102  68.223  1.00 52.26           C  
ATOM   1743  N   SER A 244      15.037  10.697  64.241  1.00 44.87           N  
ATOM   1744  CA  SER A 244      14.510   9.428  63.741  1.00 44.18           C  
ATOM   1745  C   SER A 244      15.501   8.692  62.801  1.00 43.74           C  
ATOM   1746  O   SER A 244      15.610   7.466  62.844  1.00 42.85           O  
ATOM   1747  CB  SER A 244      13.171   9.682  63.060  1.00 44.05           C  
ATOM   1748  OG  SER A 244      12.290  10.300  63.993  1.00 45.10           O  
ATOM   1749  N   ILE A 245      16.208   9.451  61.957  1.00 42.77           N  
ATOM   1750  CA  ILE A 245      17.344   8.891  61.204  1.00 42.87           C  
ATOM   1751  C   ILE A 245      18.446   8.400  62.159  1.00 42.92           C  
ATOM   1752  O   ILE A 245      18.993   7.309  61.972  1.00 42.69           O  
ATOM   1753  CB  ILE A 245      17.917   9.895  60.195  1.00 42.50           C  
ATOM   1754  CG1 ILE A 245      16.833  10.307  59.186  1.00 40.85           C  
ATOM   1755  CG2 ILE A 245      19.143   9.285  59.504  1.00 42.86           C  
ATOM   1756  CD1 ILE A 245      17.211  11.445  58.245  1.00 42.04           C  
ATOM   1757  N   ASN A 246      18.748   9.191  63.189  1.00 43.10           N  
ATOM   1758  CA  ASN A 246      19.686   8.742  64.246  1.00 44.20           C  
ATOM   1759  C   ASN A 246      19.303   7.440  64.918  1.00 44.13           C  
ATOM   1760  O   ASN A 246      20.168   6.624  65.176  1.00 44.61           O  
ATOM   1761  CB  ASN A 246      19.898   9.805  65.319  1.00 44.48           C  
ATOM   1762  CG  ASN A 246      21.089  10.680  65.032  1.00 46.03           C  
ATOM   1763  OD1 ASN A 246      22.244  10.251  65.166  1.00 45.67           O  
ATOM   1764  ND2 ASN A 246      20.819  11.926  64.634  1.00 47.18           N  
ATOM   1765  N   ASP A 247      18.020   7.256  65.228  1.00 44.73           N  
ATOM   1766  CA  ASP A 247      17.542   5.994  65.815  1.00 44.98           C  
ATOM   1767  C   ASP A 247      17.971   4.834  64.929  1.00 44.95           C  
ATOM   1768  O   ASP A 247      18.518   3.844  65.415  1.00 44.98           O  
ATOM   1769  CB  ASP A 247      16.002   5.984  65.962  1.00 45.60           C  
ATOM   1770  CG  ASP A 247      15.470   7.068  66.912  1.00 46.11           C  
ATOM   1771  OD1 ASP A 247      16.212   7.517  67.820  1.00 48.39           O  
ATOM   1772  OD2 ASP A 247      14.289   7.460  66.759  1.00 45.43           O  
ATOM   1773  N   LEU A 248      17.746   4.988  63.622  1.00 44.73           N  
ATOM   1774  CA  LEU A 248      17.998   3.935  62.640  1.00 44.07           C  
ATOM   1775  C   LEU A 248      19.469   3.530  62.469  1.00 44.35           C  
ATOM   1776  O   LEU A 248      19.765   2.358  62.187  1.00 43.75           O  
ATOM   1777  CB  LEU A 248      17.358   4.284  61.288  1.00 44.17           C  
ATOM   1778  CG  LEU A 248      15.818   4.309  61.219  1.00 44.10           C  
ATOM   1779  CD1 LEU A 248      15.325   4.704  59.829  1.00 44.64           C  
ATOM   1780  CD2 LEU A 248      15.214   2.950  61.624  1.00 44.68           C  
ATOM   1781  N   VAL A 249      20.386   4.478  62.636  1.00 44.50           N  
ATOM   1782  CA  VAL A 249      21.799   4.137  62.585  1.00 44.94           C  
ATOM   1783  C   VAL A 249      22.198   3.405  63.874  1.00 45.53           C  
ATOM   1784  O   VAL A 249      22.838   2.374  63.809  1.00 45.08           O  
ATOM   1785  CB  VAL A 249      22.756   5.326  62.227  1.00 45.05           C  
ATOM   1786  CG1 VAL A 249      22.115   6.286  61.226  1.00 43.46           C  
ATOM   1787  CG2 VAL A 249      23.263   6.055  63.454  1.00 46.64           C  
ATOM   1788  N   ILE A 250      21.763   3.929  65.021  1.00 46.13           N  
ATOM   1789  CA  ILE A 250      21.968   3.302  66.336  1.00 46.53           C  
ATOM   1790  C   ILE A 250      21.412   1.871  66.363  1.00 47.08           C  
ATOM   1791  O   ILE A 250      22.049   0.952  66.896  1.00 46.88           O  
ATOM   1792  CB  ILE A 250      21.317   4.171  67.452  1.00 46.57           C  
ATOM   1793  CG1 ILE A 250      22.123   5.460  67.670  1.00 46.21           C  
ATOM   1794  CG2 ILE A 250      21.183   3.396  68.748  1.00 47.33           C  
ATOM   1795  CD1 ILE A 250      21.329   6.588  68.308  1.00 48.40           C  
ATOM   1796  N   GLU A 251      20.239   1.689  65.760  1.00 47.70           N  
ATOM   1797  CA  GLU A 251      19.582   0.378  65.687  1.00 48.12           C  
ATOM   1798  C   GLU A 251      20.281  -0.573  64.706  1.00 48.15           C  
ATOM   1799  O   GLU A 251      20.176  -1.800  64.835  1.00 48.63           O  
ATOM   1800  CB  GLU A 251      18.106   0.548  65.310  1.00 48.06           C  
ATOM   1801  CG  GLU A 251      17.193  -0.561  65.838  1.00 48.50           C  
ATOM   1802  CD  GLU A 251      15.703  -0.253  65.678  1.00 48.64           C  
ATOM   1803  OE1 GLU A 251      15.340   0.900  65.333  1.00 47.71           O  
ATOM   1804  OE2 GLU A 251      14.891  -1.184  65.897  1.00 48.12           O  
ATOM   1805  N   GLY A 252      20.989  -0.002  63.732  1.00 48.23           N  
ATOM   1806  CA  GLY A 252      21.770  -0.776  62.765  1.00 48.58           C  
ATOM   1807  C   GLY A 252      21.169  -0.832  61.370  1.00 48.79           C  
ATOM   1808  O   GLY A 252      21.758  -1.433  60.461  1.00 49.04           O  
ATOM   1809  N   HIS A 253      20.002  -0.212  61.201  1.00 48.70           N  
ATOM   1810  CA  HIS A 253      19.250  -0.264  59.940  1.00 49.30           C  
ATOM   1811  C   HIS A 253      19.862   0.581  58.823  1.00 49.20           C  
ATOM   1812  O   HIS A 253      19.577   0.372  57.636  1.00 49.59           O  
ATOM   1813  CB  HIS A 253      17.786   0.146  60.152  1.00 49.18           C  
ATOM   1814  CG  HIS A 253      17.042  -0.731  61.110  1.00 50.84           C  
ATOM   1815  ND1 HIS A 253      16.855  -2.081  60.896  1.00 53.05           N  
ATOM   1816  CD2 HIS A 253      16.430  -0.451  62.284  1.00 52.62           C  
ATOM   1817  CE1 HIS A 253      16.173  -2.597  61.902  1.00 53.40           C  
ATOM   1818  NE2 HIS A 253      15.902  -1.629  62.759  1.00 53.32           N  
ATOM   1819  N   LEU A 254      20.708   1.530  59.213  1.00 48.89           N  
ATOM   1820  CA  LEU A 254      21.277   2.504  58.297  1.00 48.29           C  
ATOM   1821  C   LEU A 254      22.726   2.750  58.693  1.00 48.16           C  
ATOM   1822  O   LEU A 254      23.034   2.845  59.879  1.00 47.60           O  
ATOM   1823  CB  LEU A 254      20.458   3.794  58.383  1.00 48.56           C  
ATOM   1824  CG  LEU A 254      20.271   4.728  57.191  1.00 48.71           C  
ATOM   1825  CD1 LEU A 254      19.974   3.974  55.888  1.00 48.62           C  
ATOM   1826  CD2 LEU A 254      19.154   5.669  57.522  1.00 48.68           C  
ATOM   1827  N   GLU A 255      23.620   2.819  57.709  1.00 48.37           N  
ATOM   1828  CA  GLU A 255      25.030   3.063  57.992  1.00 48.69           C  
ATOM   1829  C   GLU A 255      25.175   4.527  58.366  1.00 48.56           C  
ATOM   1830  O   GLU A 255      24.464   5.380  57.834  1.00 48.40           O  
ATOM   1831  CB  GLU A 255      25.919   2.693  56.797  1.00 49.05           C  
ATOM   1832  CG  GLU A 255      27.307   2.148  57.168  1.00 50.37           C  
ATOM   1833  CD  GLU A 255      28.463   3.078  56.787  0.75 51.39           C  
ATOM   1834  OE1 GLU A 255      29.167   2.760  55.800  0.75 50.44           O  
ATOM   1835  OE2 GLU A 255      28.680   4.110  57.470  0.75 50.06           O  
ATOM   1836  N   GLU A 256      26.061   4.794  59.319  1.00 48.63           N  
ATOM   1837  CA  GLU A 256      26.331   6.141  59.797  1.00 48.93           C  
ATOM   1838  C   GLU A 256      26.725   7.078  58.646  1.00 48.85           C  
ATOM   1839  O   GLU A 256      26.460   8.276  58.714  1.00 48.26           O  
ATOM   1840  CB  GLU A 256      27.402   6.106  60.897  1.00 48.86           C  
ATOM   1841  CG  GLU A 256      27.841   7.466  61.437  1.00 49.62           C  
ATOM   1842  CD  GLU A 256      28.572   7.381  62.774  1.00 50.18           C  
ATOM   1843  OE1 GLU A 256      29.252   6.370  63.029  1.00 50.43           O  
ATOM   1844  OE2 GLU A 256      28.463   8.335  63.577  1.00 53.49           O  
ATOM   1845  N   GLU A 257      27.347   6.534  57.594  1.00 48.62           N  
ATOM   1846  CA  GLU A 257      27.731   7.358  56.445  1.00 48.90           C  
ATOM   1847  C   GLU A 257      26.530   7.977  55.705  1.00 48.75           C  
ATOM   1848  O   GLU A 257      26.628   9.099  55.186  1.00 48.14           O  
ATOM   1849  CB  GLU A 257      28.643   6.610  55.475  1.00 49.09           C  
ATOM   1850  CG  GLU A 257      29.220   7.481  54.342  1.00 50.29           C  
ATOM   1851  CD  GLU A 257      29.838   8.794  54.831  0.50 51.56           C  
ATOM   1852  OE1 GLU A 257      30.554   8.791  55.866  0.50 51.76           O  
ATOM   1853  OE2 GLU A 257      29.608   9.831  54.169  0.50 50.81           O  
ATOM   1854  N   LYS A 258      25.413   7.255  55.657  1.00 48.58           N  
ATOM   1855  CA  LYS A 258      24.198   7.791  55.030  1.00 49.16           C  
ATOM   1856  C   LYS A 258      23.693   9.052  55.736  1.00 48.82           C  
ATOM   1857  O   LYS A 258      23.288  10.014  55.071  1.00 49.68           O  
ATOM   1858  CB  LYS A 258      23.089   6.729  54.935  1.00 49.18           C  
ATOM   1859  CG  LYS A 258      23.205   5.799  53.706  1.00 49.02           C  
ATOM   1860  CD  LYS A 258      23.082   6.596  52.406  1.00 48.65           C  
ATOM   1861  CE  LYS A 258      22.523   5.771  51.223  1.00 49.08           C  
ATOM   1862  NZ  LYS A 258      23.042   4.407  51.111  1.00 44.33           N  
ATOM   1863  N   LEU A 259      23.735   9.041  57.071  1.00 48.25           N  
ATOM   1864  CA  LEU A 259      23.308  10.171  57.894  1.00 48.32           C  
ATOM   1865  C   LEU A 259      24.323  11.309  57.813  1.00 48.06           C  
ATOM   1866  O   LEU A 259      23.942  12.459  57.662  1.00 48.49           O  
ATOM   1867  CB  LEU A 259      23.164   9.739  59.358  1.00 48.28           C  
ATOM   1868  CG  LEU A 259      22.216  10.410  60.355  1.00 48.57           C  
ATOM   1869  CD1 LEU A 259      22.723  10.206  61.796  1.00 47.31           C  
ATOM   1870  CD2 LEU A 259      21.884  11.901  60.086  1.00 49.41           C  
ATOM   1871  N   ASP A 260      25.610  10.970  57.926  1.00 47.66           N  
ATOM   1872  CA  ASP A 260      26.697  11.944  57.815  1.00 47.15           C  
ATOM   1873  C   ASP A 260      26.771  12.666  56.451  1.00 47.10           C  
ATOM   1874  O   ASP A 260      27.261  13.792  56.382  1.00 47.15           O  
ATOM   1875  CB  ASP A 260      28.042  11.280  58.122  1.00 47.64           C  
ATOM   1876  CG  ASP A 260      28.202  10.890  59.593  1.00 47.77           C  
ATOM   1877  OD1 ASP A 260      27.292  11.140  60.420  1.00 48.61           O  
ATOM   1878  OD2 ASP A 260      29.269  10.331  59.917  1.00 47.36           O  
ATOM   1879  N   SER A 261      26.300  12.022  55.380  1.00 46.56           N  
ATOM   1880  CA  SER A 261      26.236  12.654  54.047  1.00 45.94           C  
ATOM   1881  C   SER A 261      24.921  13.413  53.695  1.00 45.11           C  
ATOM   1882  O   SER A 261      24.851  14.107  52.676  1.00 45.34           O  
ATOM   1883  CB  SER A 261      26.572  11.630  52.946  1.00 46.22           C  
ATOM   1884  OG  SER A 261      25.745  10.482  53.023  1.00 47.64           O  
ATOM   1885  N   PHE A 262      23.889  13.252  54.511  1.00 43.61           N  
ATOM   1886  CA  PHE A 262      22.574  13.834  54.240  1.00 42.94           C  
ATOM   1887  C   PHE A 262      22.507  15.235  54.829  1.00 42.74           C  
ATOM   1888  O   PHE A 262      22.635  15.409  56.044  1.00 43.56           O  
ATOM   1889  CB  PHE A 262      21.488  12.934  54.828  1.00 42.88           C  
ATOM   1890  CG  PHE A 262      20.064  13.350  54.509  1.00 42.84           C  
ATOM   1891  CD1 PHE A 262      19.610  13.440  53.190  1.00 43.73           C  
ATOM   1892  CD2 PHE A 262      19.161  13.588  55.546  1.00 44.22           C  
ATOM   1893  CE1 PHE A 262      18.294  13.779  52.901  1.00 43.33           C  
ATOM   1894  CE2 PHE A 262      17.826  13.942  55.278  1.00 44.47           C  
ATOM   1895  CZ  PHE A 262      17.393  14.040  53.946  1.00 43.30           C  
ATOM   1896  N   ASN A 263      22.331  16.234  53.979  1.00 41.37           N  
ATOM   1897  CA  ASN A 263      22.126  17.599  54.456  1.00 41.89           C  
ATOM   1898  C   ASN A 263      20.925  18.248  53.785  1.00 41.84           C  
ATOM   1899  O   ASN A 263      20.839  18.269  52.570  1.00 41.87           O  
ATOM   1900  CB  ASN A 263      23.362  18.452  54.225  1.00 42.22           C  
ATOM   1901  CG  ASN A 263      24.536  18.019  55.088  1.00 41.30           C  
ATOM   1902  OD1 ASN A 263      24.448  18.000  56.320  1.00 49.82           O  
ATOM   1903  ND2 ASN A 263      25.613  17.693  54.463  1.00 42.71           N  
ATOM   1904  N   VAL A 264      20.007  18.767  54.587  1.00 41.10           N  
ATOM   1905  CA  VAL A 264      18.778  19.362  54.051  1.00 41.31           C  
ATOM   1906  C   VAL A 264      18.987  20.868  53.822  1.00 40.46           C  
ATOM   1907  O   VAL A 264      19.584  21.544  54.671  1.00 39.05           O  
ATOM   1908  CB  VAL A 264      17.547  19.042  54.999  1.00 42.07           C  
ATOM   1909  CG1 VAL A 264      16.252  19.608  54.440  1.00 44.60           C  
ATOM   1910  CG2 VAL A 264      17.373  17.535  55.112  1.00 43.57           C  
ATOM   1911  N   PRO A 265      18.520  21.393  52.663  1.00 39.76           N  
ATOM   1912  CA  PRO A 265      18.643  22.818  52.388  1.00 39.30           C  
ATOM   1913  C   PRO A 265      17.569  23.643  53.132  1.00 38.73           C  
ATOM   1914  O   PRO A 265      16.666  24.214  52.515  1.00 38.53           O  
ATOM   1915  CB  PRO A 265      18.490  22.885  50.858  1.00 38.12           C  
ATOM   1916  CG  PRO A 265      17.523  21.775  50.557  1.00 39.07           C  
ATOM   1917  CD  PRO A 265      17.920  20.660  51.516  1.00 40.54           C  
ATOM   1918  N   ILE A 266      17.681  23.699  54.454  1.00 38.65           N  
ATOM   1919  CA AILE A 266      16.656  24.322  55.287  0.50 38.61           C  
ATOM   1920  CA BILE A 266      16.657  24.335  55.303  0.50 38.57           C  
ATOM   1921  C   ILE A 266      17.317  24.993  56.501  1.00 38.88           C  
ATOM   1922  O   ILE A 266      18.195  24.403  57.131  1.00 38.61           O  
ATOM   1923  CB AILE A 266      15.568  23.272  55.706  0.50 38.40           C  
ATOM   1924  CB BILE A 266      15.615  23.335  55.870  0.50 38.44           C  
ATOM   1925  CG1AILE A 266      14.299  23.948  56.252  0.50 38.55           C  
ATOM   1926  CG1BILE A 266      14.654  22.854  54.795  0.50 38.78           C  
ATOM   1927  CG2AILE A 266      16.129  22.245  56.687  0.50 38.27           C  
ATOM   1928  CG2BILE A 266      14.775  24.009  56.975  0.50 37.82           C  
ATOM   1929  CD1AILE A 266      13.077  23.035  56.219  0.50 38.93           C  
ATOM   1930  CD1BILE A 266      13.514  22.019  55.356  0.50 38.77           C  
ATOM   1931  N   TYR A 267      16.913  26.226  56.794  1.00 39.15           N  
ATOM   1932  CA  TYR A 267      17.412  26.900  57.978  1.00 39.40           C  
ATOM   1933  C   TYR A 267      16.264  27.284  58.906  1.00 39.96           C  
ATOM   1934  O   TYR A 267      15.164  27.605  58.454  1.00 40.91           O  
ATOM   1935  CB  TYR A 267      18.298  28.088  57.612  1.00 39.20           C  
ATOM   1936  CG  TYR A 267      18.932  28.764  58.791  1.00 39.78           C  
ATOM   1937  CD1 TYR A 267      19.823  28.092  59.618  1.00 40.55           C  
ATOM   1938  CD2 TYR A 267      18.640  30.092  59.076  1.00 40.76           C  
ATOM   1939  CE1 TYR A 267      20.409  28.742  60.716  1.00 40.69           C  
ATOM   1940  CE2 TYR A 267      19.216  30.746  60.138  1.00 41.51           C  
ATOM   1941  CZ  TYR A 267      20.082  30.070  60.960  1.00 39.92           C  
ATOM   1942  OH  TYR A 267      20.631  30.759  62.012  1.00 38.22           O  
ATOM   1943  N   ALA A 268      16.495  27.209  60.211  1.00 39.88           N  
ATOM   1944  CA  ALA A 268      15.537  27.778  61.167  1.00 39.95           C  
ATOM   1945  C   ALA A 268      16.115  29.055  61.817  1.00 40.21           C  
ATOM   1946  O   ALA A 268      16.934  28.956  62.727  1.00 39.64           O  
ATOM   1947  CB  ALA A 268      15.175  26.742  62.218  1.00 39.68           C  
ATOM   1948  N   PRO A 269      15.716  30.261  61.343  1.00 40.85           N  
ATOM   1949  CA  PRO A 269      16.314  31.462  61.909  1.00 41.06           C  
ATOM   1950  C   PRO A 269      15.686  31.918  63.220  1.00 41.83           C  
ATOM   1951  O   PRO A 269      14.553  31.567  63.524  1.00 42.28           O  
ATOM   1952  CB  PRO A 269      16.006  32.529  60.846  1.00 40.49           C  
ATOM   1953  CG  PRO A 269      14.680  32.117  60.360  1.00 40.63           C  
ATOM   1954  CD  PRO A 269      14.752  30.606  60.277  1.00 40.91           C  
ATOM   1955  N   SER A 270      16.413  32.748  63.958  1.00 41.88           N  
ATOM   1956  CA  SER A 270      15.845  33.435  65.108  1.00 41.97           C  
ATOM   1957  C   SER A 270      15.174  34.706  64.579  1.00 42.02           C  
ATOM   1958  O   SER A 270      15.427  35.123  63.439  1.00 41.75           O  
ATOM   1959  CB  SER A 270      16.938  33.752  66.131  1.00 41.31           C  
ATOM   1960  OG  SER A 270      17.755  34.806  65.656  1.00 40.45           O  
ATOM   1961  N   THR A 271      14.308  35.303  65.392  1.00 43.17           N  
ATOM   1962  CA  THR A 271      13.629  36.548  65.015  1.00 43.71           C  
ATOM   1963  C   THR A 271      14.628  37.688  64.917  1.00 43.64           C  
ATOM   1964  O   THR A 271      14.471  38.572  64.081  1.00 44.32           O  
ATOM   1965  CB  THR A 271      12.487  36.933  65.996  1.00 44.30           C  
ATOM   1966  OG1 THR A 271      13.036  37.265  67.272  1.00 46.02           O  
ATOM   1967  CG2 THR A 271      11.495  35.787  66.164  1.00 43.73           C  
ATOM   1968  N   GLU A 272      15.660  37.662  65.764  1.00 43.12           N  
ATOM   1969  CA  GLU A 272      16.718  38.674  65.724  1.00 42.60           C  
ATOM   1970  C   GLU A 272      17.520  38.613  64.419  1.00 41.48           C  
ATOM   1971  O   GLU A 272      17.881  39.654  63.845  1.00 40.67           O  
ATOM   1972  CB  GLU A 272      17.642  38.540  66.937  1.00 43.25           C  
ATOM   1973  CG  GLU A 272      17.526  37.195  67.676  1.00 46.61           C  
ATOM   1974  CD  GLU A 272      16.301  37.106  68.606  1.00 49.78           C  
ATOM   1975  OE1 GLU A 272      16.001  38.095  69.320  0.50 49.23           O  
ATOM   1976  OE2 GLU A 272      15.644  36.039  68.619  1.00 51.04           O  
ATOM   1977  N   GLU A 273      17.788  37.391  63.964  1.00 40.51           N  
ATOM   1978  CA  GLU A 273      18.419  37.127  62.663  1.00 40.44           C  
ATOM   1979  C   GLU A 273      17.535  37.590  61.507  1.00 40.31           C  
ATOM   1980  O   GLU A 273      18.023  38.206  60.560  1.00 40.84           O  
ATOM   1981  CB  GLU A 273      18.733  35.633  62.495  1.00 39.90           C  
ATOM   1982  CG  GLU A 273      19.972  35.156  63.288  1.00 40.56           C  
ATOM   1983  CD  GLU A 273      20.010  33.647  63.507  1.00 41.06           C  
ATOM   1984  OE1 GLU A 273      19.320  32.923  62.787  1.00 43.77           O  
ATOM   1985  OE2 GLU A 273      20.732  33.177  64.417  1.00 45.82           O  
ATOM   1986  N   VAL A 274      16.242  37.291  61.580  1.00 39.91           N  
ATOM   1987  CA  VAL A 274      15.300  37.780  60.582  1.00 40.35           C  
ATOM   1988  C   VAL A 274      15.328  39.302  60.558  1.00 40.42           C  
ATOM   1989  O   VAL A 274      15.481  39.897  59.499  1.00 40.69           O  
ATOM   1990  CB  VAL A 274      13.872  37.201  60.787  1.00 40.54           C  
ATOM   1991  CG1 VAL A 274      12.854  37.861  59.851  1.00 40.67           C  
ATOM   1992  CG2 VAL A 274      13.890  35.676  60.516  1.00 40.97           C  
ATOM   1993  N   LYS A 275      15.240  39.914  61.738  1.00 41.30           N  
ATOM   1994  CA  LYS A 275      15.189  41.379  61.891  1.00 41.88           C  
ATOM   1995  C   LYS A 275      16.444  42.063  61.334  1.00 41.65           C  
ATOM   1996  O   LYS A 275      16.344  43.041  60.585  1.00 42.10           O  
ATOM   1997  CB  LYS A 275      14.980  41.720  63.379  1.00 41.70           C  
ATOM   1998  CG  LYS A 275      14.508  43.131  63.687  1.00 42.93           C  
ATOM   1999  CD  LYS A 275      14.263  43.270  65.212  1.00 43.63           C  
ATOM   2000  CE  LYS A 275      13.324  44.421  65.523  1.00 46.09           C  
ATOM   2001  NZ  LYS A 275      13.472  44.914  66.921  1.00 48.29           N  
ATOM   2002  N   ARG A 276      17.625  41.562  61.704  1.00 41.77           N  
ATOM   2003  CA  ARG A 276      18.897  42.115  61.210  1.00 41.65           C  
ATOM   2004  C   ARG A 276      18.993  42.078  59.679  1.00 41.90           C  
ATOM   2005  O   ARG A 276      19.398  43.065  59.046  1.00 41.51           O  
ATOM   2006  CB  ARG A 276      20.078  41.370  61.845  1.00 41.90           C  
ATOM   2007  CG  ARG A 276      21.441  41.633  61.217  1.00 42.04           C  
ATOM   2008  CD  ARG A 276      22.580  41.170  62.134  1.00 42.24           C  
ATOM   2009  N   ILE A 277      18.618  40.943  59.092  1.00 42.23           N  
ATOM   2010  CA  ILE A 277      18.655  40.756  57.623  1.00 42.04           C  
ATOM   2011  C   ILE A 277      17.796  41.812  56.907  1.00 42.22           C  
ATOM   2012  O   ILE A 277      18.256  42.469  55.970  1.00 42.60           O  
ATOM   2013  CB  ILE A 277      18.269  39.295  57.207  1.00 42.05           C  
ATOM   2014  CG1 ILE A 277      19.306  38.304  57.741  1.00 40.92           C  
ATOM   2015  CG2 ILE A 277      18.167  39.154  55.675  1.00 41.41           C  
ATOM   2016  CD1 ILE A 277      18.867  36.860  57.697  1.00 41.32           C  
ATOM   2017  N   VAL A 278      16.559  41.973  57.368  1.00 43.03           N  
ATOM   2018  CA  VAL A 278      15.600  42.946  56.796  1.00 42.96           C  
ATOM   2019  C   VAL A 278      16.130  44.375  56.888  1.00 43.77           C  
ATOM   2020  O   VAL A 278      16.096  45.121  55.904  1.00 43.61           O  
ATOM   2021  CB  VAL A 278      14.203  42.851  57.471  1.00 42.43           C  
ATOM   2022  CG1 VAL A 278      13.286  44.018  57.056  1.00 41.88           C  
ATOM   2023  CG2 VAL A 278      13.537  41.518  57.155  1.00 41.75           C  
ATOM   2024  N   GLU A 279      16.642  44.738  58.064  1.00 44.66           N  
ATOM   2025  CA  GLU A 279      17.141  46.095  58.307  1.00 45.91           C  
ATOM   2026  C   GLU A 279      18.398  46.384  57.491  1.00 46.26           C  
ATOM   2027  O   GLU A 279      18.602  47.509  57.027  1.00 46.48           O  
ATOM   2028  CB  GLU A 279      17.398  46.310  59.789  1.00 46.00           C  
ATOM   2029  CG  GLU A 279      16.122  46.348  60.622  1.00 47.49           C  
ATOM   2030  CD  GLU A 279      16.365  46.753  62.074  1.00 47.59           C  
ATOM   2031  OE1 GLU A 279      17.028  47.794  62.325  1.00 50.44           O  
ATOM   2032  OE2 GLU A 279      15.876  46.026  62.968  1.00 48.89           O  
ATOM   2033  N   GLU A 280      19.222  45.352  57.313  1.00 46.60           N  
ATOM   2034  CA  GLU A 280      20.432  45.400  56.491  1.00 47.33           C  
ATOM   2035  C   GLU A 280      20.112  45.634  55.006  1.00 46.81           C  
ATOM   2036  O   GLU A 280      20.702  46.520  54.370  1.00 47.18           O  
ATOM   2037  CB  GLU A 280      21.176  44.072  56.632  1.00 48.12           C  
ATOM   2038  CG  GLU A 280      22.675  44.166  56.600  1.00 50.34           C  
ATOM   2039  CD  GLU A 280      23.268  44.038  57.983  1.00 53.40           C  
ATOM   2040  OE1 GLU A 280      23.104  44.993  58.776  1.00 54.54           O  
ATOM   2041  OE2 GLU A 280      23.895  42.983  58.267  1.00 53.44           O  
ATOM   2042  N   GLU A 281      19.188  44.831  54.472  1.00 46.26           N  
ATOM   2043  CA  GLU A 281      18.687  44.940  53.087  1.00 45.41           C  
ATOM   2044  C   GLU A 281      18.226  46.359  52.790  1.00 44.96           C  
ATOM   2045  O   GLU A 281      18.540  46.916  51.738  1.00 44.93           O  
ATOM   2046  CB  GLU A 281      17.524  43.957  52.856  1.00 45.84           C  
ATOM   2047  CG  GLU A 281      16.448  44.437  51.800  1.00 45.40           C  
ATOM   2048  CD  GLU A 281      16.968  44.334  50.403  1.00 45.99           C  
ATOM   2049  OE1 GLU A 281      17.859  43.480  50.193  0.50 48.10           O  
ATOM   2050  OE2 GLU A 281      16.513  45.075  49.507  1.00 45.17           O  
ATOM   2051  N   GLY A 282      17.459  46.924  53.716  1.00 44.81           N  
ATOM   2052  CA  GLY A 282      17.076  48.335  53.665  1.00 44.58           C  
ATOM   2053  C   GLY A 282      15.806  48.632  52.881  1.00 44.38           C  
ATOM   2054  O   GLY A 282      15.265  49.715  53.014  1.00 44.93           O  
ATOM   2055  N   SER A 283      15.328  47.674  52.081  1.00 43.99           N  
ATOM   2056  CA  SER A 283      14.155  47.873  51.200  1.00 43.11           C  
ATOM   2057  C   SER A 283      12.821  48.009  51.921  1.00 42.99           C  
ATOM   2058  O   SER A 283      11.952  48.771  51.465  1.00 43.72           O  
ATOM   2059  CB  SER A 283      14.057  46.767  50.168  1.00 42.95           C  
ATOM   2060  OG  SER A 283      15.126  46.870  49.257  1.00 42.72           O  
ATOM   2061  N   PHE A 284      12.702  47.341  53.072  1.00 41.20           N  
ATOM   2062  CA  PHE A 284      11.450  47.226  53.806  1.00 40.43           C  
ATOM   2063  C   PHE A 284      11.483  47.733  55.244  1.00 40.31           C  
ATOM   2064  O   PHE A 284      12.429  47.464  55.994  1.00 40.02           O  
ATOM   2065  CB  PHE A 284      11.018  45.752  53.869  1.00 39.54           C  
ATOM   2066  CG  PHE A 284      10.585  45.198  52.566  1.00 39.00           C  
ATOM   2067  CD1 PHE A 284       9.305  45.436  52.095  1.00 39.06           C  
ATOM   2068  CD2 PHE A 284      11.459  44.429  51.788  1.00 40.04           C  
ATOM   2069  CE1 PHE A 284       8.883  44.930  50.881  1.00 37.38           C  
ATOM   2070  CE2 PHE A 284      11.041  43.893  50.572  1.00 39.54           C  
ATOM   2071  CZ  PHE A 284       9.749  44.157  50.108  1.00 39.83           C  
ATOM   2072  N   GLU A 285      10.405  48.407  55.627  1.00 40.13           N  
ATOM   2073  CA  GLU A 285      10.101  48.682  57.024  1.00 40.29           C  
ATOM   2074  C   GLU A 285       9.335  47.493  57.619  1.00 39.75           C  
ATOM   2075  O   GLU A 285       8.468  46.939  56.971  1.00 37.79           O  
ATOM   2076  CB  GLU A 285       9.229  49.923  57.121  1.00 40.23           C  
ATOM   2077  CG  GLU A 285       8.747  50.202  58.510  1.00 42.09           C  
ATOM   2078  CD  GLU A 285       7.571  51.153  58.552  1.00 44.35           C  
ATOM   2079  OE1 GLU A 285       7.120  51.602  57.467  1.00 45.39           O  
ATOM   2080  OE2 GLU A 285       7.106  51.442  59.680  1.00 46.51           O  
ATOM   2081  N   ILE A 286       9.616  47.145  58.873  1.00 40.58           N  
ATOM   2082  CA  ILE A 286       8.891  46.037  59.523  1.00 41.34           C  
ATOM   2083  C   ILE A 286       7.668  46.642  60.200  1.00 41.35           C  
ATOM   2084  O   ILE A 286       7.811  47.500  61.053  1.00 41.25           O  
ATOM   2085  CB  ILE A 286       9.777  45.327  60.587  1.00 41.65           C  
ATOM   2086  CG1 ILE A 286      11.040  44.759  59.935  1.00 41.78           C  
ATOM   2087  CG2 ILE A 286       8.978  44.284  61.386  1.00 42.04           C  
ATOM   2088  CD1 ILE A 286      12.025  44.083  60.921  1.00 41.73           C  
ATOM   2089  N   LEU A 287       6.471  46.216  59.799  1.00 41.56           N  
ATOM   2090  CA  LEU A 287       5.219  46.683  60.440  1.00 41.38           C  
ATOM   2091  C   LEU A 287       4.842  45.823  61.626  1.00 41.72           C  
ATOM   2092  O   LEU A 287       4.277  46.314  62.598  1.00 41.79           O  
ATOM   2093  CB  LEU A 287       4.044  46.636  59.452  1.00 41.22           C  
ATOM   2094  CG  LEU A 287       4.342  47.070  58.016  1.00 41.99           C  
ATOM   2095  CD1 LEU A 287       3.365  46.500  56.988  1.00 44.17           C  
ATOM   2096  CD2 LEU A 287       4.367  48.555  57.966  1.00 36.16           C  
ATOM   2097  N   TYR A 288       5.153  44.534  61.518  1.00 42.22           N  
ATOM   2098  CA  TYR A 288       4.681  43.494  62.425  1.00 42.58           C  
ATOM   2099  C   TYR A 288       5.720  42.364  62.451  1.00 41.93           C  
ATOM   2100  O   TYR A 288       6.243  41.995  61.413  1.00 41.28           O  
ATOM   2101  CB  TYR A 288       3.329  42.960  61.925  1.00 44.08           C  
ATOM   2102  CG  TYR A 288       2.609  41.978  62.843  1.00 45.27           C  
ATOM   2103  CD1 TYR A 288       1.750  42.426  63.848  1.00 46.82           C  
ATOM   2104  CD2 TYR A 288       2.765  40.606  62.677  1.00 46.43           C  
ATOM   2105  CE1 TYR A 288       1.078  41.512  64.693  1.00 48.33           C  
ATOM   2106  CE2 TYR A 288       2.115  39.691  63.502  1.00 47.26           C  
ATOM   2107  CZ  TYR A 288       1.279  40.136  64.501  1.00 48.62           C  
ATOM   2108  OH  TYR A 288       0.638  39.201  65.307  1.00 48.62           O  
ATOM   2109  N   LEU A 289       6.030  41.833  63.623  1.00 41.62           N  
ATOM   2110  CA  LEU A 289       6.901  40.682  63.779  1.00 41.88           C  
ATOM   2111  C   LEU A 289       6.629  39.934  65.043  1.00 41.75           C  
ATOM   2112  O   LEU A 289       6.934  40.396  66.079  1.00 42.00           O  
ATOM   2113  CB  LEU A 289       8.364  41.090  63.700  1.00 42.05           C  
ATOM   2114  CG  LEU A 289       9.543  40.180  64.029  1.00 42.26           C  
ATOM   2115  CD1 LEU A 289       9.536  38.935  63.282  1.00 42.14           C  
ATOM   2116  CD2 LEU A 289      10.841  40.848  63.886  1.00 42.43           C  
ATOM   2117  N   GLU A 290       6.067  38.757  64.932  1.00 41.66           N  
ATOM   2118  CA AGLU A 290       5.731  37.921  66.090  0.50 41.78           C  
ATOM   2119  CA BGLU A 290       5.734  37.923  66.089  0.50 41.94           C  
ATOM   2120  C   GLU A 290       6.128  36.471  65.826  1.00 42.09           C  
ATOM   2121  O   GLU A 290       6.358  36.076  64.679  1.00 41.55           O  
ATOM   2122  CB AGLU A 290       4.234  38.006  66.426  0.50 41.89           C  
ATOM   2123  CB BGLU A 290       4.237  38.006  66.400  0.50 42.27           C  
ATOM   2124  CG AGLU A 290       3.346  37.030  65.645  0.50 41.63           C  
ATOM   2125  CG BGLU A 290       3.758  39.341  66.958  0.50 43.20           C  
ATOM   2126  CD AGLU A 290       2.028  36.692  66.340  0.50 42.21           C  
ATOM   2127  CD BGLU A 290       3.898  39.445  68.468  0.50 45.79           C  
ATOM   2128  OE1AGLU A 290       2.025  36.526  67.584  0.50 40.84           O  
ATOM   2129  OE1BGLU A 290       2.913  39.137  69.176  0.50 45.77           O  
ATOM   2130  OE2AGLU A 290       0.996  36.574  65.632  0.50 41.98           O  
ATOM   2131  OE2BGLU A 290       4.995  39.820  68.950  0.50 47.26           O  
ATOM   2132  N   THR A 291       6.226  35.685  66.893  1.00 41.71           N  
ATOM   2133  CA  THR A 291       6.398  34.243  66.750  1.00 42.08           C  
ATOM   2134  C   THR A 291       5.118  33.652  67.320  1.00 41.51           C  
ATOM   2135  O   THR A 291       4.366  34.349  67.978  1.00 41.20           O  
ATOM   2136  CB  THR A 291       7.619  33.707  67.513  1.00 41.49           C  
ATOM   2137  OG1 THR A 291       7.499  34.028  68.897  1.00 43.29           O  
ATOM   2138  CG2 THR A 291       8.880  34.325  66.993  1.00 42.36           C  
ATOM   2139  N   PHE A 292       4.839  32.403  66.991  1.00 41.29           N  
ATOM   2140  CA  PHE A 292       3.737  31.670  67.576  1.00 41.28           C  
ATOM   2141  C   PHE A 292       4.122  30.212  67.533  1.00 41.34           C  
ATOM   2142  O   PHE A 292       4.962  29.804  66.722  1.00 40.37           O  
ATOM   2143  CB  PHE A 292       2.409  31.920  66.849  1.00 42.20           C  
ATOM   2144  CG  PHE A 292       2.371  31.459  65.393  1.00 43.76           C  
ATOM   2145  CD1 PHE A 292       1.997  30.151  65.055  1.00 44.52           C  
ATOM   2146  CD2 PHE A 292       2.632  32.359  64.362  1.00 45.48           C  
ATOM   2147  CE1 PHE A 292       1.924  29.749  63.716  1.00 42.97           C  
ATOM   2148  CE2 PHE A 292       2.565  31.957  63.025  1.00 43.86           C  
ATOM   2149  CZ  PHE A 292       2.211  30.646  62.712  1.00 44.55           C  
ATOM   2150  N   ASN A 293       3.509  29.421  68.398  1.00 40.30           N  
ATOM   2151  CA  ASN A 293       3.883  28.026  68.499  1.00 40.70           C  
ATOM   2152  C   ASN A 293       2.671  27.172  68.160  1.00 40.37           C  
ATOM   2153  O   ASN A 293       1.645  27.271  68.814  1.00 39.82           O  
ATOM   2154  CB  ASN A 293       4.425  27.730  69.899  1.00 40.65           C  
ATOM   2155  CG  ASN A 293       5.311  28.859  70.433  1.00 40.43           C  
ATOM   2156  OD1 ASN A 293       4.832  29.757  71.125  1.00 38.68           O  
ATOM   2157  ND2 ASN A 293       6.596  28.826  70.088  1.00 37.19           N  
ATOM   2158  N   ALA A 294       2.793  26.352  67.115  1.00 39.00           N  
ATOM   2159  CA  ALA A 294       1.680  25.545  66.635  1.00 38.13           C  
ATOM   2160  C   ALA A 294       1.860  24.112  67.096  1.00 38.11           C  
ATOM   2161  O   ALA A 294       2.878  23.488  66.752  1.00 38.40           O  
ATOM   2162  CB  ALA A 294       1.623  25.615  65.084  1.00 37.75           C  
ATOM   2163  N   PRO A 295       0.878  23.555  67.830  1.00 38.30           N  
ATOM   2164  CA  PRO A 295       0.957  22.141  68.267  1.00 38.24           C  
ATOM   2165  C   PRO A 295       1.103  21.201  67.060  1.00 38.32           C  
ATOM   2166  O   PRO A 295       0.564  21.526  66.023  1.00 38.09           O  
ATOM   2167  CB  PRO A 295      -0.384  21.898  68.980  1.00 38.18           C  
ATOM   2168  CG  PRO A 295      -1.001  23.241  69.188  1.00 37.98           C  
ATOM   2169  CD  PRO A 295      -0.365  24.220  68.272  1.00 38.46           C  
ATOM   2170  N   TYR A 296       1.815  20.061  67.189  1.00 39.34           N  
ATOM   2171  CA  TYR A 296       2.086  19.170  66.029  1.00 39.54           C  
ATOM   2172  C   TYR A 296       0.812  18.671  65.364  1.00 40.50           C  
ATOM   2173  O   TYR A 296       0.742  18.561  64.147  1.00 40.11           O  
ATOM   2174  CB  TYR A 296       2.906  17.915  66.389  1.00 39.48           C  
ATOM   2175  CG  TYR A 296       4.337  18.094  66.824  1.00 38.22           C  
ATOM   2176  CD1 TYR A 296       5.038  19.259  66.545  1.00 36.66           C  
ATOM   2177  CD2 TYR A 296       5.011  17.052  67.484  1.00 37.39           C  
ATOM   2178  CE1 TYR A 296       6.357  19.407  66.941  1.00 37.85           C  
ATOM   2179  CE2 TYR A 296       6.338  17.190  67.876  1.00 36.12           C  
ATOM   2180  CZ  TYR A 296       6.996  18.378  67.588  1.00 37.24           C  
ATOM   2181  OH  TYR A 296       8.293  18.541  67.972  1.00 40.04           O  
ATOM   2182  N   ASP A 297      -0.179  18.334  66.176  1.00 41.76           N  
ATOM   2183  CA  ASP A 297      -1.394  17.681  65.692  1.00 43.59           C  
ATOM   2184  C   ASP A 297      -2.636  18.602  65.579  1.00 44.52           C  
ATOM   2185  O   ASP A 297      -3.762  18.117  65.633  1.00 44.76           O  
ATOM   2186  CB  ASP A 297      -1.706  16.490  66.590  1.00 43.54           C  
ATOM   2187  CG  ASP A 297      -1.786  16.878  68.070  1.00 45.45           C  
ATOM   2188  OD1 ASP A 297      -1.334  17.991  68.435  1.00 47.04           O  
ATOM   2189  OD2 ASP A 297      -2.301  16.074  68.867  1.00 45.26           O  
ATOM   2190  N   ALA A 298      -2.418  19.910  65.405  1.00 45.96           N  
ATOM   2191  CA  ALA A 298      -3.500  20.912  65.273  1.00 47.57           C  
ATOM   2192  C   ALA A 298      -4.409  20.631  64.075  1.00 49.06           C  
ATOM   2193  O   ALA A 298      -5.604  20.950  64.089  1.00 49.48           O  
ATOM   2194  CB  ALA A 298      -2.917  22.336  65.196  1.00 46.60           C  
ATOM   2195  N   GLY A 299      -3.836  20.025  63.041  1.00 50.97           N  
ATOM   2196  CA  GLY A 299      -4.613  19.575  61.889  1.00 53.09           C  
ATOM   2197  C   GLY A 299      -5.248  18.186  61.976  1.00 54.10           C  
ATOM   2198  O   GLY A 299      -5.694  17.656  60.957  1.00 54.37           O  
ATOM   2199  N   PHE A 300      -5.311  17.598  63.172  1.00 55.21           N  
ATOM   2200  CA  PHE A 300      -5.781  16.213  63.326  1.00 56.20           C  
ATOM   2201  C   PHE A 300      -7.198  16.117  63.913  1.00 57.41           C  
ATOM   2202  O   PHE A 300      -7.492  16.742  64.937  1.00 57.69           O  
ATOM   2203  CB  PHE A 300      -4.799  15.415  64.197  1.00 56.11           C  
ATOM   2204  CG  PHE A 300      -5.326  14.071  64.636  1.00 56.13           C  
ATOM   2205  CD1 PHE A 300      -6.126  13.953  65.774  1.00 56.83           C  
ATOM   2206  CD2 PHE A 300      -5.038  12.928  63.906  1.00 55.88           C  
ATOM   2207  CE1 PHE A 300      -6.628  12.716  66.175  1.00 56.47           C  
ATOM   2208  CE2 PHE A 300      -5.524  11.691  64.292  1.00 55.56           C  
ATOM   2209  CZ  PHE A 300      -6.322  11.579  65.436  1.00 56.64           C  
ATOM   2210  N   SER A 301      -8.057  15.304  63.295  1.00 58.50           N  
ATOM   2211  CA  SER A 301      -9.415  15.075  63.827  1.00 59.60           C  
ATOM   2212  C   SER A 301      -9.718  13.614  64.194  1.00 60.38           C  
ATOM   2213  O   SER A 301      -9.182  12.678  63.592  1.00 60.56           O  
ATOM   2214  CB  SER A 301     -10.486  15.641  62.877  1.00 59.86           C  
ATOM   2215  OG  SER A 301     -10.459  17.067  62.849  1.00 59.51           O  
ATOM   2216  N   ILE A 302     -10.574  13.435  65.201  1.00 61.31           N  
ATOM   2217  CA  ILE A 302     -10.969  12.108  65.694  1.00 61.85           C  
ATOM   2218  C   ILE A 302     -12.152  11.523  64.914  1.00 62.29           C  
ATOM   2219  O   ILE A 302     -12.212  11.621  63.682  1.00 62.76           O  
ATOM   2220  CB  ILE A 302     -11.317  12.129  67.208  1.00 61.98           C  
ATOM   2221  CG1 ILE A 302     -11.947  13.481  67.600  1.00 61.94           C  
ATOM   2222  CG2 ILE A 302     -10.073  11.789  68.044  1.00 61.97           C  
ATOM   2223  CD1 ILE A 302     -12.540  13.543  68.997  1.00 61.86           C  
ATOM   2224  N   SER A 312     -13.090   4.403  71.787  1.00 57.62           N  
ATOM   2225  CA  SER A 312     -11.633   4.368  71.884  1.00 57.48           C  
ATOM   2226  C   SER A 312     -11.156   4.476  73.339  1.00 57.41           C  
ATOM   2227  O   SER A 312     -11.810   5.137  74.156  1.00 57.47           O  
ATOM   2228  CB  SER A 312     -11.021   5.491  71.041  1.00 57.70           C  
ATOM   2229  N   PRO A 313     -10.041   3.790  73.682  1.00 57.19           N  
ATOM   2230  CA  PRO A 313      -9.335   4.046  74.944  1.00 56.86           C  
ATOM   2231  C   PRO A 313      -8.683   5.440  74.920  1.00 56.50           C  
ATOM   2232  O   PRO A 313      -9.405   6.442  74.922  1.00 56.56           O  
ATOM   2233  CB  PRO A 313      -8.286   2.921  75.002  1.00 56.86           C  
ATOM   2234  CG  PRO A 313      -8.752   1.895  74.012  1.00 56.94           C  
ATOM   2235  CD  PRO A 313      -9.410   2.690  72.932  1.00 57.16           C  
ATOM   2236  N   VAL A 314      -7.351   5.510  74.894  1.00 55.87           N  
ATOM   2237  CA  VAL A 314      -6.638   6.792  74.799  1.00 55.28           C  
ATOM   2238  C   VAL A 314      -5.220   6.588  74.279  1.00 54.74           C  
ATOM   2239  O   VAL A 314      -4.627   7.507  73.708  1.00 54.42           O  
ATOM   2240  CB  VAL A 314      -6.663   7.620  76.138  1.00 55.46           C  
ATOM   2241  CG1 VAL A 314      -5.697   7.053  77.187  1.00 55.97           C  
ATOM   2242  CG2 VAL A 314      -6.396   9.110  75.880  1.00 55.60           C  
ATOM   2243  N   SER A 315      -4.690   5.380  74.471  1.00 54.07           N  
ATOM   2244  CA  SER A 315      -3.425   4.983  73.852  1.00 53.40           C  
ATOM   2245  C   SER A 315      -3.610   4.874  72.342  1.00 52.96           C  
ATOM   2246  O   SER A 315      -2.659   5.059  71.577  1.00 52.65           O  
ATOM   2247  CB  SER A 315      -2.941   3.650  74.413  1.00 53.47           C  
ATOM   2248  OG  SER A 315      -3.017   3.642  75.826  1.00 53.99           O  
ATOM   2249  N   CYS A 316      -4.843   4.569  71.932  1.00 52.41           N  
ATOM   2250  CA  CYS A 316      -5.246   4.579  70.528  1.00 52.28           C  
ATOM   2251  C   CYS A 316      -5.259   6.008  69.998  1.00 52.00           C  
ATOM   2252  O   CYS A 316      -4.687   6.289  68.939  1.00 51.98           O  
ATOM   2253  CB  CYS A 316      -6.627   3.942  70.353  1.00 52.07           C  
ATOM   2254  SG  CYS A 316      -6.728   2.224  70.919  1.00 53.52           S  
ATOM   2255  N   ASP A 317      -5.906   6.900  70.750  1.00 51.79           N  
ATOM   2256  CA  ASP A 317      -5.990   8.324  70.410  1.00 51.80           C  
ATOM   2257  C   ASP A 317      -4.607   8.922  70.159  1.00 51.47           C  
ATOM   2258  O   ASP A 317      -4.371   9.548  69.113  1.00 51.40           O  
ATOM   2259  CB  ASP A 317      -6.706   9.112  71.521  1.00 52.04           C  
ATOM   2260  CG  ASP A 317      -8.185   8.752  71.655  1.00 52.97           C  
ATOM   2261  OD1 ASP A 317      -8.674   7.881  70.899  1.00 54.12           O  
ATOM   2262  OD2 ASP A 317      -8.862   9.350  72.526  1.00 53.41           O  
ATOM   2263  N   GLU A 318      -3.696   8.711  71.111  1.00 51.12           N  
ATOM   2264  CA  GLU A 318      -2.331   9.245  71.016  1.00 50.80           C  
ATOM   2265  C   GLU A 318      -1.457   8.534  69.968  1.00 50.37           C  
ATOM   2266  O   GLU A 318      -0.569   9.158  69.383  1.00 49.98           O  
ATOM   2267  CB  GLU A 318      -1.658   9.315  72.398  1.00 50.99           C  
ATOM   2268  CG  GLU A 318      -0.865   8.093  72.840  1.00 51.02           C  
ATOM   2269  CD  GLU A 318      -0.602   8.089  74.344  0.50 51.05           C  
ATOM   2270  OE1 GLU A 318      -0.590   9.183  74.956  0.50 50.72           O  
ATOM   2271  OE2 GLU A 318      -0.416   6.989  74.917  0.50 51.43           O  
ATOM   2272  N   HIS A 319      -1.718   7.243  69.730  1.00 49.93           N  
ATOM   2273  CA  HIS A 319      -1.061   6.512  68.640  1.00 49.38           C  
ATOM   2274  C   HIS A 319      -1.375   7.176  67.301  1.00 48.36           C  
ATOM   2275  O   HIS A 319      -0.468   7.534  66.547  1.00 48.37           O  
ATOM   2276  CB  HIS A 319      -1.464   5.021  68.619  1.00 49.77           C  
ATOM   2277  CG  HIS A 319      -0.697   4.202  67.617  1.00 51.52           C  
ATOM   2278  ND1 HIS A 319      -1.089   4.074  66.300  1.00 53.13           N  
ATOM   2279  CD2 HIS A 319       0.452   3.493  67.735  1.00 53.21           C  
ATOM   2280  CE1 HIS A 319      -0.220   3.315  65.654  1.00 53.86           C  
ATOM   2281  NE2 HIS A 319       0.724   2.948  66.502  1.00 53.90           N  
ATOM   2282  N   ALA A 320      -2.669   7.348  67.035  1.00 47.34           N  
ATOM   2283  CA  ALA A 320      -3.174   7.959  65.804  1.00 46.13           C  
ATOM   2284  C   ALA A 320      -2.685   9.393  65.619  1.00 45.49           C  
ATOM   2285  O   ALA A 320      -2.336   9.782  64.507  1.00 45.54           O  
ATOM   2286  CB  ALA A 320      -4.697   7.911  65.782  1.00 46.40           C  
ATOM   2287  N   ARG A 321      -2.662  10.175  66.702  1.00 44.35           N  
ATOM   2288  CA  ARG A 321      -2.114  11.536  66.652  0.50 43.21           C  
ATOM   2289  C   ARG A 321      -0.637  11.540  66.260  1.00 43.24           C  
ATOM   2290  O   ARG A 321      -0.230  12.366  65.437  1.00 43.92           O  
ATOM   2291  CB  ARG A 321      -2.335  12.287  67.965  0.50 42.76           C  
ATOM   2292  CG  ARG A 321      -3.776  12.667  68.191  0.50 40.66           C  
ATOM   2293  CD  ARG A 321      -4.019  13.306  69.555  0.50 37.72           C  
ATOM   2294  NE  ARG A 321      -5.409  13.723  69.676  0.50 34.23           N  
ATOM   2295  CZ  ARG A 321      -5.874  14.922  69.337  0.50 34.41           C  
ATOM   2296  NH1 ARG A 321      -5.060  15.859  68.866  0.50 31.91           N  
ATOM   2297  NH2 ARG A 321      -7.165  15.195  69.484  0.50 34.69           N  
ATOM   2298  N   ALA A 322       0.140  10.605  66.814  1.00 42.90           N  
ATOM   2299  CA  ALA A 322       1.570  10.457  66.501  1.00 42.79           C  
ATOM   2300  C   ALA A 322       1.796   9.986  65.059  1.00 43.02           C  
ATOM   2301  O   ALA A 322       2.755  10.404  64.406  1.00 42.20           O  
ATOM   2302  CB  ALA A 322       2.240   9.484  67.484  1.00 42.92           C  
ATOM   2303  N   ALA A 323       0.918   9.101  64.589  1.00 43.64           N  
ATOM   2304  CA  ALA A 323       0.970   8.558  63.231  1.00 44.29           C  
ATOM   2305  C   ALA A 323       0.665   9.649  62.210  1.00 44.51           C  
ATOM   2306  O   ALA A 323       1.290   9.711  61.158  1.00 44.85           O  
ATOM   2307  CB  ALA A 323      -0.007   7.415  63.088  1.00 44.23           C  
ATOM   2308  N   HIS A 324      -0.302  10.503  62.534  1.00 44.78           N  
ATOM   2309  CA  HIS A 324      -0.611  11.679  61.738  1.00 44.54           C  
ATOM   2310  C   HIS A 324       0.607  12.593  61.605  1.00 44.50           C  
ATOM   2311  O   HIS A 324       0.912  13.060  60.515  1.00 44.41           O  
ATOM   2312  CB  HIS A 324      -1.818  12.425  62.335  1.00 44.45           C  
ATOM   2313  CG  HIS A 324      -1.959  13.837  61.853  1.00 44.79           C  
ATOM   2314  ND1 HIS A 324      -2.571  14.157  60.663  1.00 45.37           N  
ATOM   2315  CD2 HIS A 324      -1.558  15.011  62.397  1.00 45.96           C  
ATOM   2316  CE1 HIS A 324      -2.550  15.469  60.498  1.00 47.42           C  
ATOM   2317  NE2 HIS A 324      -1.942  16.011  61.537  1.00 46.10           N  
ATOM   2318  N   VAL A 325       1.304  12.836  62.713  1.00 44.53           N  
ATOM   2319  CA  VAL A 325       2.457  13.728  62.712  1.00 44.08           C  
ATOM   2320  C   VAL A 325       3.487  13.161  61.769  1.00 45.08           C  
ATOM   2321  O   VAL A 325       4.010  13.897  60.925  1.00 44.54           O  
ATOM   2322  CB  VAL A 325       3.066  13.951  64.122  1.00 44.85           C  
ATOM   2323  CG1 VAL A 325       4.328  14.798  64.054  1.00 42.03           C  
ATOM   2324  CG2 VAL A 325       2.041  14.574  65.063  1.00 43.30           C  
ATOM   2325  N   ALA A 326       3.750  11.851  61.890  1.00 44.90           N  
ATOM   2326  CA  ALA A 326       4.709  11.159  61.028  1.00 45.46           C  
ATOM   2327  C   ALA A 326       4.347  11.243  59.541  1.00 45.45           C  
ATOM   2328  O   ALA A 326       5.234  11.386  58.682  1.00 45.81           O  
ATOM   2329  CB  ALA A 326       4.854   9.714  61.447  1.00 44.66           C  
ATOM   2330  N   SER A 327       3.059  11.123  59.228  1.00 45.96           N  
ATOM   2331  CA  SER A 327       2.595  11.316  57.840  1.00 46.75           C  
ATOM   2332  C   SER A 327       2.869  12.719  57.322  1.00 46.61           C  
ATOM   2333  O   SER A 327       3.303  12.885  56.184  1.00 47.12           O  
ATOM   2334  CB  SER A 327       1.108  10.987  57.696  1.00 46.83           C  
ATOM   2335  OG  SER A 327       0.920   9.586  57.791  1.00 47.73           O  
ATOM   2336  N   VAL A 328       2.594  13.724  58.140  1.00 46.96           N  
ATOM   2337  CA  VAL A 328       2.846  15.114  57.763  1.00 47.59           C  
ATOM   2338  C   VAL A 328       4.351  15.285  57.501  1.00 48.05           C  
ATOM   2339  O   VAL A 328       4.743  15.787  56.453  1.00 49.13           O  
ATOM   2340  CB  VAL A 328       2.332  16.113  58.831  1.00 47.65           C  
ATOM   2341  CG1 VAL A 328       2.868  17.524  58.591  1.00 48.61           C  
ATOM   2342  CG2 VAL A 328       0.801  16.133  58.879  1.00 48.13           C  
ATOM   2343  N   VAL A 329       5.187  14.826  58.430  1.00 48.68           N  
ATOM   2344  CA  VAL A 329       6.650  14.907  58.271  1.00 48.56           C  
ATOM   2345  C   VAL A 329       7.160  14.132  57.024  1.00 48.89           C  
ATOM   2346  O   VAL A 329       8.024  14.625  56.275  1.00 48.86           O  
ATOM   2347  CB  VAL A 329       7.385  14.460  59.573  1.00 48.40           C  
ATOM   2348  CG1 VAL A 329       8.907  14.438  59.365  1.00 46.77           C  
ATOM   2349  CG2 VAL A 329       7.012  15.398  60.745  1.00 47.28           C  
ATOM   2350  N   ARG A 330       6.637  12.933  56.790  1.00 48.83           N  
ATOM   2351  CA  ARG A 330       7.003  12.205  55.568  1.00 49.46           C  
ATOM   2352  C   ARG A 330       6.570  12.978  54.307  1.00 49.39           C  
ATOM   2353  O   ARG A 330       7.296  12.988  53.281  1.00 49.58           O  
ATOM   2354  CB  ARG A 330       6.411  10.787  55.575  1.00 49.50           C  
ATOM   2355  CG  ARG A 330       7.129   9.781  54.692  1.00 52.62           C  
ATOM   2356  CD  ARG A 330       6.362   8.463  54.686  1.00 57.36           C  
ATOM   2357  NE  ARG A 330       6.990   7.432  53.860  1.00 60.12           N  
ATOM   2358  CZ  ARG A 330       6.368   6.735  52.909  1.00 61.54           C  
ATOM   2359  NH1 ARG A 330       5.086   6.947  52.642  1.00 63.28           N  
ATOM   2360  NH2 ARG A 330       7.028   5.818  52.217  1.00 62.48           N  
ATOM   2361  N   SER A 331       5.412  13.639  54.371  1.00 48.70           N  
ATOM   2362  CA  SER A 331       4.906  14.348  53.185  1.00 49.07           C  
ATOM   2363  C   SER A 331       5.739  15.579  52.783  1.00 48.17           C  
ATOM   2364  O   SER A 331       5.724  15.959  51.619  1.00 50.09           O  
ATOM   2365  CB  SER A 331       3.427  14.703  53.304  1.00 48.78           C  
ATOM   2366  OG  SER A 331       3.233  15.753  54.228  1.00 52.09           O  
ATOM   2367  N   ILE A 332       6.432  16.187  53.748  1.00 47.26           N  
ATOM   2368  CA  ILE A 332       7.335  17.320  53.526  1.00 45.45           C  
ATOM   2369  C   ILE A 332       8.653  16.856  52.928  1.00 45.03           C  
ATOM   2370  O   ILE A 332       9.175  17.469  51.983  1.00 44.07           O  
ATOM   2371  CB  ILE A 332       7.632  18.064  54.863  1.00 45.40           C  
ATOM   2372  CG1 ILE A 332       6.343  18.610  55.478  1.00 44.25           C  
ATOM   2373  CG2 ILE A 332       8.613  19.204  54.651  1.00 44.84           C  
ATOM   2374  CD1 ILE A 332       6.443  18.689  56.958  1.00 42.13           C  
ATOM   2375  N   TYR A 333       9.166  15.738  53.430  1.00 44.11           N  
ATOM   2376  CA  TYR A 333      10.529  15.327  53.091  1.00 44.53           C  
ATOM   2377  C   TYR A 333      10.705  14.127  52.157  1.00 44.57           C  
ATOM   2378  O   TYR A 333      11.840  13.838  51.777  1.00 44.32           O  
ATOM   2379  CB  TYR A 333      11.370  15.136  54.380  1.00 44.15           C  
ATOM   2380  CG  TYR A 333      11.391  16.379  55.263  1.00 44.56           C  
ATOM   2381  CD1 TYR A 333      12.192  17.474  54.939  1.00 43.28           C  
ATOM   2382  CD2 TYR A 333      10.619  16.445  56.445  1.00 42.24           C  
ATOM   2383  CE1 TYR A 333      12.205  18.627  55.747  1.00 43.55           C  
ATOM   2384  CE2 TYR A 333      10.631  17.574  57.255  1.00 41.17           C  
ATOM   2385  CZ  TYR A 333      11.426  18.663  56.896  1.00 43.41           C  
ATOM   2386  OH  TYR A 333      11.452  19.789  57.680  1.00 45.46           O  
ATOM   2387  N   GLU A 334       9.626  13.440  51.759  1.00 44.71           N  
ATOM   2388  CA  GLU A 334       9.803  12.184  51.009  1.00 45.30           C  
ATOM   2389  C   GLU A 334      10.659  12.329  49.736  1.00 44.90           C  
ATOM   2390  O   GLU A 334      11.586  11.554  49.544  1.00 43.82           O  
ATOM   2391  CB  GLU A 334       8.478  11.477  50.678  1.00 46.30           C  
ATOM   2392  CG  GLU A 334       8.709  10.075  50.098  1.00 48.05           C  
ATOM   2393  CD  GLU A 334       7.476   9.194  50.091  1.00 51.73           C  
ATOM   2394  OE1 GLU A 334       6.609   9.368  50.970  1.00 54.33           O  
ATOM   2395  OE2 GLU A 334       7.397   8.297  49.214  1.00 53.60           O  
ATOM   2396  N   PRO A 335      10.381  13.344  48.890  1.00 45.32           N  
ATOM   2397  CA  PRO A 335      11.207  13.491  47.693  1.00 45.59           C  
ATOM   2398  C   PRO A 335      12.718  13.505  47.992  1.00 45.92           C  
ATOM   2399  O   PRO A 335      13.479  12.774  47.361  1.00 45.60           O  
ATOM   2400  CB  PRO A 335      10.735  14.839  47.128  1.00 46.07           C  
ATOM   2401  CG  PRO A 335       9.301  14.869  47.486  1.00 46.00           C  
ATOM   2402  CD  PRO A 335       9.323  14.378  48.927  1.00 44.97           C  
ATOM   2403  N   ILE A 336      13.142  14.305  48.966  1.00 47.08           N  
ATOM   2404  CA  ILE A 336      14.563  14.407  49.294  1.00 47.49           C  
ATOM   2405  C   ILE A 336      15.071  13.140  49.993  1.00 47.07           C  
ATOM   2406  O   ILE A 336      16.144  12.638  49.662  1.00 47.93           O  
ATOM   2407  CB  ILE A 336      14.943  15.741  50.014  1.00 48.37           C  
ATOM   2408  CG1 ILE A 336      14.537  15.754  51.476  1.00 48.93           C  
ATOM   2409  CG2 ILE A 336      14.372  16.959  49.247  1.00 50.12           C  
ATOM   2410  CD1 ILE A 336      15.231  16.818  52.249  1.00 53.95           C  
ATOM   2411  N   LEU A 337      14.263  12.580  50.889  1.00 46.19           N  
ATOM   2412  CA  LEU A 337      14.603  11.310  51.532  1.00 45.77           C  
ATOM   2413  C   LEU A 337      14.782  10.160  50.526  1.00 45.82           C  
ATOM   2414  O   LEU A 337      15.741   9.374  50.647  1.00 45.85           O  
ATOM   2415  CB  LEU A 337      13.560  10.941  52.599  1.00 45.71           C  
ATOM   2416  CG  LEU A 337      13.480  11.800  53.862  1.00 44.59           C  
ATOM   2417  CD1 LEU A 337      12.171  11.530  54.667  1.00 42.99           C  
ATOM   2418  CD2 LEU A 337      14.714  11.574  54.725  1.00 44.35           C  
ATOM   2419  N   ALA A 338      13.879  10.053  49.551  1.00 45.11           N  
ATOM   2420  CA  ALA A 338      13.968   8.991  48.540  1.00 45.11           C  
ATOM   2421  C   ALA A 338      15.209   9.156  47.677  1.00 45.38           C  
ATOM   2422  O   ALA A 338      15.864   8.175  47.377  1.00 45.05           O  
ATOM   2423  CB  ALA A 338      12.738   8.933  47.682  1.00 44.83           C  
ATOM   2424  N   SER A 339      15.559  10.390  47.306  1.00 45.57           N  
ATOM   2425  CA  SER A 339      16.732  10.552  46.454  1.00 47.44           C  
ATOM   2426  C   SER A 339      18.031  10.200  47.172  1.00 47.21           C  
ATOM   2427  O   SER A 339      18.917   9.618  46.557  1.00 46.53           O  
ATOM   2428  CB  SER A 339      16.793  11.885  45.693  1.00 46.95           C  
ATOM   2429  OG  SER A 339      16.765  12.990  46.551  1.00 52.86           O  
ATOM   2430  N   HIS A 340      18.118  10.508  48.469  1.00 46.87           N  
ATOM   2431  CA  HIS A 340      19.324  10.213  49.227  1.00 47.10           C  
ATOM   2432  C   HIS A 340      19.397   8.765  49.734  1.00 47.47           C  
ATOM   2433  O   HIS A 340      20.405   8.078  49.538  1.00 46.62           O  
ATOM   2434  CB  HIS A 340      19.544  11.223  50.366  1.00 47.19           C  
ATOM   2435  CG  HIS A 340      20.872  11.068  51.044  1.00 47.74           C  
ATOM   2436  ND1 HIS A 340      22.040  11.573  50.514  1.00 47.88           N  
ATOM   2437  CD2 HIS A 340      21.219  10.448  52.198  1.00 47.02           C  
ATOM   2438  CE1 HIS A 340      23.051  11.262  51.307  1.00 48.59           C  
ATOM   2439  NE2 HIS A 340      22.578  10.582  52.338  1.00 47.96           N  
ATOM   2440  N   PHE A 341      18.320   8.294  50.353  1.00 47.41           N  
ATOM   2441  CA  PHE A 341      18.357   7.027  51.069  1.00 47.14           C  
ATOM   2442  C   PHE A 341      17.816   5.824  50.296  1.00 47.39           C  
ATOM   2443  O   PHE A 341      18.102   4.683  50.661  1.00 47.42           O  
ATOM   2444  CB  PHE A 341      17.593   7.157  52.389  1.00 46.23           C  
ATOM   2445  CG  PHE A 341      18.244   8.073  53.385  1.00 46.28           C  
ATOM   2446  CD1 PHE A 341      17.807   9.388  53.518  1.00 44.75           C  
ATOM   2447  CD2 PHE A 341      19.294   7.622  54.207  1.00 45.47           C  
ATOM   2448  CE1 PHE A 341      18.396  10.237  54.440  1.00 45.36           C  
ATOM   2449  CE2 PHE A 341      19.888   8.488  55.130  1.00 42.28           C  
ATOM   2450  CZ  PHE A 341      19.439   9.791  55.235  1.00 44.20           C  
ATOM   2451  N   GLY A 342      17.027   6.085  49.254  1.00 47.79           N  
ATOM   2452  CA  GLY A 342      16.232   5.049  48.589  1.00 48.27           C  
ATOM   2453  C   GLY A 342      14.919   4.830  49.324  1.00 48.90           C  
ATOM   2454  O   GLY A 342      14.732   5.341  50.429  1.00 49.16           O  
ATOM   2455  N   GLU A 343      14.019   4.056  48.720  1.00 49.53           N  
ATOM   2456  CA  GLU A 343      12.662   3.849  49.256  1.00 50.27           C  
ATOM   2457  C   GLU A 343      12.499   2.807  50.385  1.00 50.10           C  
ATOM   2458  O   GLU A 343      11.484   2.816  51.096  1.00 50.14           O  
ATOM   2459  CB  GLU A 343      11.683   3.530  48.113  1.00 50.52           C  
ATOM   2460  CG  GLU A 343      10.778   4.695  47.704  1.00 51.44           C  
ATOM   2461  CD  GLU A 343      11.276   5.476  46.498  0.50 52.71           C  
ATOM   2462  OE1 GLU A 343      12.256   5.053  45.836  0.50 53.04           O  
ATOM   2463  OE2 GLU A 343      10.657   6.521  46.199  0.50 53.48           O  
ATOM   2464  N   ALA A 344      13.484   1.926  50.551  1.00 49.78           N  
ATOM   2465  CA  ALA A 344      13.359   0.803  51.479  1.00 49.81           C  
ATOM   2466  C   ALA A 344      13.284   1.167  52.976  1.00 49.85           C  
ATOM   2467  O   ALA A 344      12.679   0.435  53.753  1.00 50.12           O  
ATOM   2468  CB  ALA A 344      14.453  -0.243  51.212  1.00 49.48           C  
ATOM   2469  N   ILE A 345      13.868   2.298  53.371  1.00 49.99           N  
ATOM   2470  CA  ILE A 345      13.883   2.702  54.790  1.00 50.25           C  
ATOM   2471  C   ILE A 345      12.697   3.568  55.232  1.00 49.83           C  
ATOM   2472  O   ILE A 345      12.477   3.740  56.434  1.00 50.03           O  
ATOM   2473  CB  ILE A 345      15.188   3.442  55.196  1.00 50.45           C  
ATOM   2474  CG1 ILE A 345      15.518   4.560  54.201  1.00 49.84           C  
ATOM   2475  CG2 ILE A 345      16.351   2.467  55.334  1.00 51.96           C  
ATOM   2476  CD1 ILE A 345      15.082   5.907  54.648  1.00 51.82           C  
ATOM   2477  N   LEU A 346      11.946   4.107  54.274  1.00 49.26           N  
ATOM   2478  CA  LEU A 346      10.838   5.037  54.572  1.00 48.63           C  
ATOM   2479  C   LEU A 346       9.735   4.546  55.545  1.00 48.25           C  
ATOM   2480  O   LEU A 346       9.259   5.334  56.368  1.00 48.62           O  
ATOM   2481  CB  LEU A 346      10.230   5.603  53.283  1.00 48.85           C  
ATOM   2482  CG  LEU A 346      11.151   6.380  52.323  1.00 49.85           C  
ATOM   2483  CD1 LEU A 346      10.409   6.826  51.070  1.00 49.27           C  
ATOM   2484  CD2 LEU A 346      11.801   7.573  53.009  1.00 50.93           C  
ATOM   2485  N   PRO A 347       9.299   3.270  55.446  1.00 48.08           N  
ATOM   2486  CA  PRO A 347       8.383   2.769  56.486  1.00 47.87           C  
ATOM   2487  C   PRO A 347       9.020   2.667  57.883  1.00 47.72           C  
ATOM   2488  O   PRO A 347       8.351   2.929  58.885  1.00 47.22           O  
ATOM   2489  CB  PRO A 347       7.997   1.372  55.981  1.00 47.20           C  
ATOM   2490  CG  PRO A 347       8.350   1.357  54.553  1.00 47.68           C  
ATOM   2491  CD  PRO A 347       9.529   2.252  54.405  1.00 48.28           C  
ATOM   2492  N   ASP A 348      10.289   2.264  57.946  1.00 47.71           N  
ATOM   2493  CA  ASP A 348      11.024   2.284  59.207  1.00 47.85           C  
ATOM   2494  C   ASP A 348      11.171   3.717  59.700  1.00 47.16           C  
ATOM   2495  O   ASP A 348      11.051   3.981  60.898  1.00 46.68           O  
ATOM   2496  CB  ASP A 348      12.407   1.678  59.044  1.00 47.85           C  
ATOM   2497  CG  ASP A 348      12.347   0.267  58.576  1.00 49.53           C  
ATOM   2498  OD1 ASP A 348      11.907  -0.595  59.372  1.00 50.29           O  
ATOM   2499  OD2 ASP A 348      12.720   0.028  57.407  1.00 53.00           O  
ATOM   2500  N   LEU A 349      11.462   4.620  58.776  1.00 47.11           N  
ATOM   2501  CA  LEU A 349      11.565   6.036  59.135  1.00 48.22           C  
ATOM   2502  C   LEU A 349      10.242   6.541  59.696  1.00 48.23           C  
ATOM   2503  O   LEU A 349      10.223   7.110  60.781  1.00 49.31           O  
ATOM   2504  CB  LEU A 349      12.010   6.907  57.961  1.00 48.18           C  
ATOM   2505  CG  LEU A 349      13.246   7.789  58.176  1.00 49.08           C  
ATOM   2506  CD1 LEU A 349      13.328   8.803  57.058  1.00 50.06           C  
ATOM   2507  CD2 LEU A 349      13.333   8.466  59.542  1.00 45.21           C  
ATOM   2508  N   SER A 350       9.138   6.328  58.980  1.00 48.54           N  
ATOM   2509  CA  SER A 350       7.816   6.756  59.492  1.00 48.98           C  
ATOM   2510  C   SER A 350       7.527   6.194  60.884  1.00 48.60           C  
ATOM   2511  O   SER A 350       6.909   6.860  61.710  1.00 48.96           O  
ATOM   2512  CB  SER A 350       6.696   6.334  58.554  1.00 49.20           C  
ATOM   2513  OG  SER A 350       6.842   6.955  57.304  1.00 51.58           O  
ATOM   2514  N   HIS A 351       7.974   4.969  61.145  1.00 48.04           N  
ATOM   2515  CA  HIS A 351       7.761   4.378  62.461  1.00 47.40           C  
ATOM   2516  C   HIS A 351       8.553   5.068  63.582  1.00 46.57           C  
ATOM   2517  O   HIS A 351       8.023   5.277  64.676  1.00 46.19           O  
ATOM   2518  CB  HIS A 351       8.046   2.883  62.465  1.00 47.86           C  
ATOM   2519  CG  HIS A 351       7.750   2.234  63.780  1.00 49.44           C  
ATOM   2520  ND1 HIS A 351       8.705   2.071  64.761  1.00 52.30           N  
ATOM   2521  CD2 HIS A 351       6.598   1.741  64.292  1.00 51.26           C  
ATOM   2522  CE1 HIS A 351       8.161   1.481  65.810  1.00 51.95           C  
ATOM   2523  NE2 HIS A 351       6.883   1.266  65.549  1.00 52.26           N  
ATOM   2524  N   ARG A 352       9.812   5.406  63.320  1.00 45.17           N  
ATOM   2525  CA  ARG A 352      10.594   6.162  64.295  1.00 44.86           C  
ATOM   2526  C   ARG A 352      10.099   7.608  64.507  1.00 44.45           C  
ATOM   2527  O   ARG A 352      10.163   8.127  65.626  1.00 44.36           O  
ATOM   2528  CB  ARG A 352      12.089   6.160  63.938  1.00 45.12           C  
ATOM   2529  CG  ARG A 352      12.835   4.833  64.132  1.00 44.63           C  
ATOM   2530  CD  ARG A 352      12.661   4.207  65.537  1.00 47.34           C  
ATOM   2531  NE  ARG A 352      12.667   5.205  66.615  1.00 48.38           N  
ATOM   2532  CZ  ARG A 352      12.205   4.996  67.848  1.00 47.56           C  
ATOM   2533  NH1 ARG A 352      11.686   3.824  68.187  1.00 48.44           N  
ATOM   2534  NH2 ARG A 352      12.252   5.969  68.747  1.00 48.55           N  
ATOM   2535  N   ILE A 353       9.637   8.266  63.443  1.00 43.78           N  
ATOM   2536  CA  ILE A 353       9.119   9.634  63.584  1.00 43.40           C  
ATOM   2537  C   ILE A 353       7.898   9.661  64.522  1.00 43.27           C  
ATOM   2538  O   ILE A 353       7.748  10.609  65.316  1.00 43.54           O  
ATOM   2539  CB  ILE A 353       8.769  10.321  62.226  1.00 42.82           C  
ATOM   2540  CG1 ILE A 353       9.983  10.409  61.283  1.00 42.11           C  
ATOM   2541  CG2 ILE A 353       8.229  11.725  62.457  1.00 42.40           C  
ATOM   2542  CD1 ILE A 353       9.620  10.491  59.824  1.00 41.63           C  
ATOM   2543  N   ALA A 354       7.030   8.651  64.410  1.00 42.59           N  
ATOM   2544  CA  ALA A 354       5.823   8.556  65.240  1.00 42.64           C  
ATOM   2545  C   ALA A 354       6.199   8.342  66.697  1.00 42.66           C  
ATOM   2546  O   ALA A 354       5.683   9.010  67.581  1.00 42.80           O  
ATOM   2547  CB  ALA A 354       4.884   7.427  64.741  1.00 42.18           C  
ATOM   2548  N   LYS A 355       7.118   7.416  66.943  1.00 42.97           N  
ATOM   2549  CA  LYS A 355       7.577   7.149  68.309  1.00 43.14           C  
ATOM   2550  C   LYS A 355       8.178   8.400  68.946  1.00 43.35           C  
ATOM   2551  O   LYS A 355       7.826   8.759  70.073  1.00 42.74           O  
ATOM   2552  CB  LYS A 355       8.568   5.990  68.323  1.00 43.24           C  
ATOM   2553  CG  LYS A 355       7.943   4.668  67.954  1.00 44.16           C  
ATOM   2554  CD  LYS A 355       6.915   4.244  68.989  1.00 46.45           C  
ATOM   2555  CE  LYS A 355       6.507   2.785  68.826  1.00 46.72           C  
ATOM   2556  NZ  LYS A 355       7.353   1.831  69.621  1.00 48.32           N  
ATOM   2557  N   ASN A 356       9.071   9.061  68.211  1.00 43.13           N  
ATOM   2558  CA  ASN A 356       9.641  10.341  68.633  1.00 43.98           C  
ATOM   2559  C   ASN A 356       8.613  11.464  68.844  1.00 43.98           C  
ATOM   2560  O   ASN A 356       8.697  12.197  69.829  1.00 43.76           O  
ATOM   2561  CB  ASN A 356      10.749  10.787  67.676  1.00 43.70           C  
ATOM   2562  CG  ASN A 356      12.016   9.941  67.816  1.00 45.13           C  
ATOM   2563  OD1 ASN A 356      12.445   9.629  68.922  1.00 43.37           O  
ATOM   2564  ND2 ASN A 356      12.609   9.570  66.694  1.00 45.51           N  
ATOM   2565  N   ALA A 357       7.659  11.579  67.917  1.00 44.08           N  
ATOM   2566  CA  ALA A 357       6.551  12.547  68.001  1.00 43.92           C  
ATOM   2567  C   ALA A 357       5.734  12.423  69.290  1.00 44.06           C  
ATOM   2568  O   ALA A 357       5.423  13.419  69.942  1.00 44.24           O  
ATOM   2569  CB  ALA A 357       5.639  12.391  66.792  1.00 43.88           C  
ATOM   2570  N   ALA A 358       5.388  11.189  69.639  1.00 43.93           N  
ATOM   2571  CA  ALA A 358       4.637  10.898  70.848  1.00 43.97           C  
ATOM   2572  C   ALA A 358       5.388  11.265  72.125  1.00 43.81           C  
ATOM   2573  O   ALA A 358       4.778  11.722  73.072  1.00 44.13           O  
ATOM   2574  CB  ALA A 358       4.219   9.438  70.865  1.00 43.49           C  
ATOM   2575  N   LYS A 359       6.705  11.067  72.152  1.00 43.93           N  
ATOM   2576  CA  LYS A 359       7.494  11.350  73.367  1.00 43.41           C  
ATOM   2577  C   LYS A 359       7.550  12.871  73.560  1.00 43.22           C  
ATOM   2578  O   LYS A 359       7.449  13.367  74.675  1.00 42.14           O  
ATOM   2579  CB  LYS A 359       8.915  10.772  73.247  1.00 43.02           C  
ATOM   2580  CG  LYS A 359       9.775  10.932  74.513  1.00 44.11           C  
ATOM   2581  N   VAL A 360       7.698  13.594  72.447  1.00 42.50           N  
ATOM   2582  CA  VAL A 360       7.780  15.051  72.464  1.00 42.97           C  
ATOM   2583  C   VAL A 360       6.475  15.683  72.967  1.00 42.51           C  
ATOM   2584  O   VAL A 360       6.490  16.540  73.859  1.00 42.84           O  
ATOM   2585  CB  VAL A 360       8.184  15.610  71.069  1.00 42.79           C  
ATOM   2586  CG1 VAL A 360       8.335  17.117  71.134  1.00 43.68           C  
ATOM   2587  CG2 VAL A 360       9.502  14.983  70.632  1.00 44.41           C  
ATOM   2588  N   LEU A 361       5.352  15.228  72.419  1.00 42.81           N  
ATOM   2589  CA  LEU A 361       4.018  15.744  72.786  1.00 42.79           C  
ATOM   2590  C   LEU A 361       3.718  15.522  74.265  1.00 42.90           C  
ATOM   2591  O   LEU A 361       3.189  16.405  74.954  1.00 42.38           O  
ATOM   2592  CB  LEU A 361       2.924  15.105  71.904  1.00 42.76           C  
ATOM   2593  CG  LEU A 361       2.749  15.531  70.436  1.00 42.65           C  
ATOM   2594  CD1 LEU A 361       2.104  14.403  69.629  1.00 41.35           C  
ATOM   2595  CD2 LEU A 361       1.931  16.816  70.333  1.00 42.51           C  
ATOM   2596  N   ARG A 362       4.080  14.336  74.747  1.00 43.29           N  
ATOM   2597  CA  ARG A 362       3.963  13.999  76.153  1.00 43.56           C  
ATOM   2598  C   ARG A 362       4.762  14.895  77.111  1.00 43.04           C  
ATOM   2599  O   ARG A 362       4.277  15.203  78.207  1.00 43.12           O  
ATOM   2600  CB  ARG A 362       4.270  12.513  76.377  1.00 44.22           C  
ATOM   2601  CG  ARG A 362       3.090  11.616  76.016  1.00 46.12           C  
ATOM   2602  CD  ARG A 362       3.188  10.212  76.588  1.00 50.23           C  
ATOM   2603  NE  ARG A 362       1.848   9.694  76.898  1.00 52.87           N  
ATOM   2604  CZ  ARG A 362       1.407   9.345  78.109  1.00 54.47           C  
ATOM   2605  NH1 ARG A 362       2.193   9.408  79.183  1.00 54.61           N  
ATOM   2606  NH2 ARG A 362       0.162   8.903  78.243  1.00 54.96           N  
ATOM   2607  N   SER A 363       5.953  15.332  76.695  1.00 42.48           N  
ATOM   2608  CA  SER A 363       6.737  16.297  77.477  1.00 42.10           C  
ATOM   2609  C   SER A 363       6.187  17.741  77.421  1.00 41.93           C  
ATOM   2610  O   SER A 363       6.614  18.591  78.262  1.00 41.98           O  
ATOM   2611  CB  SER A 363       8.214  16.291  77.037  1.00 42.11           C  
ATOM   2612  OG  SER A 363       8.390  16.981  75.790  1.00 42.73           O  
ATOM   2613  N   GLY A 364       5.254  18.013  76.453  1.00 41.03           N  
ATOM   2614  CA  GLY A 364       4.635  19.346  76.339  1.00 40.74           C  
ATOM   2615  C   GLY A 364       5.484  20.362  75.586  1.00 40.63           C  
ATOM   2616  O   GLY A 364       5.372  21.582  75.818  1.00 40.13           O  
ATOM   2617  N   LYS A 365       6.333  19.844  74.694  1.00 40.60           N  
ATOM   2618  CA  LYS A 365       7.223  20.641  73.839  1.00 41.08           C  
ATOM   2619  C   LYS A 365       6.981  20.347  72.351  1.00 40.64           C  
ATOM   2620  O   LYS A 365       7.793  20.703  71.503  1.00 40.90           O  
ATOM   2621  CB  LYS A 365       8.700  20.421  74.223  1.00 41.10           C  
ATOM   2622  CG  LYS A 365       9.071  21.005  75.601  1.00 41.89           C  
ATOM   2623  CD  LYS A 365      10.502  20.666  76.027  1.00 41.76           C  
ATOM   2624  CE  LYS A 365      10.726  20.982  77.525  1.00 44.11           C  
ATOM   2625  NZ  LYS A 365      10.906  22.454  77.787  1.00 47.32           N  
ATOM   2626  N   GLY A 366       5.829  19.736  72.056  1.00 40.56           N  
ATOM   2627  CA  GLY A 366       5.411  19.395  70.688  1.00 40.48           C  
ATOM   2628  C   GLY A 366       4.758  20.497  69.890  1.00 39.44           C  
ATOM   2629  O   GLY A 366       3.573  20.433  69.547  1.00 40.13           O  
ATOM   2630  N   PHE A 367       5.550  21.515  69.589  1.00 38.89           N  
ATOM   2631  CA  PHE A 367       5.103  22.670  68.849  1.00 38.87           C  
ATOM   2632  C   PHE A 367       6.057  22.946  67.729  1.00 38.74           C  
ATOM   2633  O   PHE A 367       7.268  22.856  67.915  1.00 38.64           O  
ATOM   2634  CB  PHE A 367       5.075  23.913  69.742  1.00 38.50           C  
ATOM   2635  CG  PHE A 367       4.214  23.769  70.928  1.00 38.11           C  
ATOM   2636  CD1 PHE A 367       2.899  24.207  70.898  1.00 38.78           C  
ATOM   2637  CD2 PHE A 367       4.706  23.187  72.092  1.00 39.30           C  
ATOM   2638  CE1 PHE A 367       2.089  24.068  72.008  1.00 38.35           C  
ATOM   2639  CE2 PHE A 367       3.892  23.055  73.202  1.00 39.33           C  
ATOM   2640  CZ  PHE A 367       2.584  23.493  73.150  1.00 38.60           C  
ATOM   2641  N   TYR A 368       5.503  23.288  66.570  1.00 39.28           N  
ATOM   2642  CA  TYR A 368       6.281  23.899  65.507  1.00 39.89           C  
ATOM   2643  C   TYR A 368       6.329  25.412  65.741  1.00 40.48           C  
ATOM   2644  O   TYR A 368       5.308  26.084  65.669  1.00 40.96           O  
ATOM   2645  CB  TYR A 368       5.635  23.642  64.151  1.00 40.17           C  
ATOM   2646  CG  TYR A 368       5.495  22.206  63.762  1.00 39.23           C  
ATOM   2647  CD1 TYR A 368       6.616  21.360  63.707  1.00 38.19           C  
ATOM   2648  CD2 TYR A 368       4.248  21.689  63.413  1.00 38.46           C  
ATOM   2649  CE1 TYR A 368       6.503  20.037  63.328  1.00 37.72           C  
ATOM   2650  CE2 TYR A 368       4.118  20.358  63.025  1.00 38.63           C  
ATOM   2651  CZ  TYR A 368       5.258  19.539  62.974  1.00 39.93           C  
ATOM   2652  OH  TYR A 368       5.144  18.215  62.608  1.00 40.43           O  
ATOM   2653  N   ASP A 369       7.521  25.940  66.005  1.00 41.06           N  
ATOM   2654  CA  ASP A 369       7.711  27.366  66.265  1.00 40.83           C  
ATOM   2655  C   ASP A 369       7.791  28.091  64.933  1.00 41.45           C  
ATOM   2656  O   ASP A 369       8.541  27.663  64.038  1.00 39.00           O  
ATOM   2657  CB  ASP A 369       9.015  27.600  67.044  1.00 41.33           C  
ATOM   2658  CG  ASP A 369       8.984  27.030  68.466  1.00 42.81           C  
ATOM   2659  OD1 ASP A 369       7.892  26.863  69.047  1.00 42.08           O  
ATOM   2660  OD2 ASP A 369      10.078  26.757  69.011  1.00 45.85           O  
ATOM   2661  N   SER A 370       7.033  29.194  64.811  1.00 40.93           N  
ATOM   2662  CA  SER A 370       6.918  29.930  63.559  1.00 42.29           C  
ATOM   2663  C   SER A 370       6.984  31.441  63.814  1.00 42.35           C  
ATOM   2664  O   SER A 370       6.623  31.903  64.879  1.00 40.97           O  
ATOM   2665  CB  SER A 370       5.586  29.592  62.903  1.00 43.25           C  
ATOM   2666  OG  SER A 370       5.421  28.177  62.834  1.00 43.86           O  
ATOM   2667  N   VAL A 371       7.514  32.176  62.847  1.00 42.93           N  
ATOM   2668  CA  VAL A 371       7.550  33.622  62.883  1.00 43.35           C  
ATOM   2669  C   VAL A 371       6.658  34.144  61.746  1.00 44.03           C  
ATOM   2670  O   VAL A 371       6.530  33.516  60.675  1.00 44.49           O  
ATOM   2671  CB  VAL A 371       9.011  34.163  62.753  1.00 43.11           C  
ATOM   2672  CG1 VAL A 371       9.668  33.714  61.464  1.00 42.74           C  
ATOM   2673  CG2 VAL A 371       9.053  35.693  62.880  1.00 44.36           C  
ATOM   2674  N   ILE A 372       6.043  35.289  61.988  1.00 43.56           N  
ATOM   2675  CA  ILE A 372       5.243  35.949  60.991  1.00 43.85           C  
ATOM   2676  C   ILE A 372       5.725  37.416  60.965  1.00 43.18           C  
ATOM   2677  O   ILE A 372       5.904  38.037  62.013  1.00 43.09           O  
ATOM   2678  CB  ILE A 372       3.733  35.763  61.317  1.00 44.48           C  
ATOM   2679  CG1 ILE A 372       2.833  36.502  60.324  1.00 44.43           C  
ATOM   2680  CG2 ILE A 372       3.425  36.210  62.745  1.00 44.99           C  
ATOM   2681  CD1 ILE A 372       1.380  36.139  60.484  1.00 43.67           C  
ATOM   2682  N   ILE A 373       6.015  37.917  59.767  1.00 42.94           N  
ATOM   2683  CA  ILE A 373       6.568  39.269  59.584  1.00 41.31           C  
ATOM   2684  C   ILE A 373       5.891  40.016  58.429  1.00 41.28           C  
ATOM   2685  O   ILE A 373       5.838  39.529  57.287  1.00 39.80           O  
ATOM   2686  CB  ILE A 373       8.118  39.251  59.397  1.00 41.84           C  
ATOM   2687  CG1 ILE A 373       8.690  40.675  59.404  1.00 41.53           C  
ATOM   2688  CG2 ILE A 373       8.522  38.447  58.133  1.00 39.08           C  
ATOM   2689  CD1 ILE A 373      10.234  40.759  59.388  1.00 41.37           C  
ATOM   2690  N   SER A 374       5.375  41.202  58.758  1.00 40.75           N  
ATOM   2691  CA  SER A 374       4.717  42.051  57.811  1.00 40.92           C  
ATOM   2692  C   SER A 374       5.653  43.199  57.403  1.00 40.90           C  
ATOM   2693  O   SER A 374       6.143  43.945  58.245  1.00 40.51           O  
ATOM   2694  CB  SER A 374       3.437  42.602  58.445  1.00 41.10           C  
ATOM   2695  OG  SER A 374       2.612  43.167  57.464  1.00 43.28           O  
ATOM   2696  N   LEU A 375       5.877  43.332  56.101  1.00 40.74           N  
ATOM   2697  CA  LEU A 375       6.825  44.287  55.541  1.00 40.20           C  
ATOM   2698  C   LEU A 375       6.158  45.267  54.589  1.00 40.28           C  
ATOM   2699  O   LEU A 375       5.379  44.847  53.759  1.00 41.33           O  
ATOM   2700  CB  LEU A 375       7.887  43.500  54.756  1.00 39.15           C  
ATOM   2701  CG  LEU A 375       8.635  42.426  55.558  1.00 39.10           C  
ATOM   2702  CD1 LEU A 375       9.455  41.522  54.641  1.00 38.41           C  
ATOM   2703  CD2 LEU A 375       9.505  43.103  56.683  1.00 39.13           C  
ATOM   2704  N   ALA A 376       6.472  46.556  54.711  1.00 40.46           N  
ATOM   2705  CA  ALA A 376       6.079  47.575  53.734  1.00 39.64           C  
ATOM   2706  C   ALA A 376       7.295  48.133  52.997  1.00 39.53           C  
ATOM   2707  O   ALA A 376       8.306  48.460  53.633  1.00 38.94           O  
ATOM   2708  CB  ALA A 376       5.327  48.722  54.422  1.00 39.90           C  
ATOM   2709  N   LYS A 377       7.178  48.271  51.676  1.00 39.76           N  
ATOM   2710  CA  LYS A 377       8.217  48.891  50.827  1.00 40.69           C  
ATOM   2711  C   LYS A 377       8.435  50.368  51.179  1.00 41.93           C  
ATOM   2712  O   LYS A 377       7.488  51.165  51.156  1.00 41.62           O  
ATOM   2713  CB  LYS A 377       7.861  48.740  49.334  1.00 40.75           C  
ATOM   2714  CG  LYS A 377       8.960  49.165  48.352  1.00 40.45           C  
ATOM   2715  CD  LYS A 377       8.552  49.004  46.870  1.00 41.42           C  
ATOM   2716  CE  LYS A 377       9.578  49.661  45.933  1.00 41.84           C  
ATOM   2717  NZ  LYS A 377       9.309  49.422  44.471  1.00 43.63           N  
ATOM   2718  N   LYS A 378       9.676  50.718  51.516  1.00 42.70           N  
ATOM   2719  CA  LYS A 378      10.025  52.093  51.915  1.00 44.33           C  
ATOM   2720  C   LYS A 378       9.939  53.029  50.713  1.00 45.41           C  
ATOM   2721  O   LYS A 378      10.229  52.612  49.581  1.00 46.36           O  
ATOM   2722  CB  LYS A 378      11.449  52.149  52.471  1.00 43.39           C  
ATOM   2723  CG  LYS A 378      11.655  51.558  53.847  1.00 44.56           C  
ATOM   2724  CD  LYS A 378      13.149  51.356  54.065  1.00 45.39           C  
ATOM   2725  CE  LYS A 378      13.515  50.958  55.487  1.00 46.24           C  
ATOM   2726  NZ  LYS A 378      15.001  51.016  55.688  1.00 45.55           N  
ATOM   2727  N   PRO A 379       9.552  54.298  50.939  1.00 47.29           N  
ATOM   2728  CA  PRO A 379       9.619  55.223  49.799  1.00 48.12           C  
ATOM   2729  C   PRO A 379      11.070  55.420  49.326  1.00 48.97           C  
ATOM   2730  O   PRO A 379      12.031  55.003  50.001  1.00 48.80           O  
ATOM   2731  CB  PRO A 379       9.061  56.526  50.370  1.00 48.06           C  
ATOM   2732  CG  PRO A 379       9.250  56.415  51.854  1.00 47.92           C  
ATOM   2733  CD  PRO A 379       9.060  54.961  52.164  1.00 46.71           C  
TER    2734      PRO A 379                                                      
HETATM 2735  N   SAH A 501       2.188  28.012  51.378  1.00 37.24           N  
HETATM 2736  CA  SAH A 501       1.648  26.623  51.249  1.00 37.27           C  
HETATM 2737  CB  SAH A 501       2.766  25.622  50.946  1.00 37.87           C  
HETATM 2738  CG  SAH A 501       3.891  25.509  51.965  1.00 37.26           C  
HETATM 2739  SD  SAH A 501       4.821  23.957  51.734  1.00 41.41           S  
HETATM 2740  C   SAH A 501       0.881  26.161  52.486  1.00 37.42           C  
HETATM 2741  O   SAH A 501       0.557  26.950  53.390  1.00 37.75           O  
HETATM 2742  OXT SAH A 501       0.571  24.975  52.587  1.00 36.75           O  
HETATM 2743  C5' SAH A 501       6.343  24.751  51.173  1.00 38.01           C  
HETATM 2744  C4' SAH A 501       6.348  25.039  49.683  1.00 35.18           C  
HETATM 2745  O4' SAH A 501       7.458  25.848  49.470  1.00 33.47           O  
HETATM 2746  C3' SAH A 501       6.527  23.846  48.735  1.00 33.89           C  
HETATM 2747  O3' SAH A 501       5.438  23.722  47.839  1.00 31.17           O  
HETATM 2748  C2' SAH A 501       7.818  24.165  47.982  1.00 35.34           C  
HETATM 2749  O2' SAH A 501       7.885  23.701  46.641  1.00 38.30           O  
HETATM 2750  C1' SAH A 501       7.845  25.676  48.115  1.00 33.04           C  
HETATM 2751  N9  SAH A 501       9.173  26.272  47.853  1.00 33.43           N  
HETATM 2752  C8  SAH A 501      10.351  26.058  48.525  1.00 34.11           C  
HETATM 2753  N7  SAH A 501      11.343  26.800  47.957  1.00 34.36           N  
HETATM 2754  C5  SAH A 501      10.803  27.503  46.930  1.00 34.55           C  
HETATM 2755  C6  SAH A 501      11.339  28.429  46.023  1.00 32.75           C  
HETATM 2756  N6  SAH A 501      12.627  28.758  46.067  1.00 32.47           N  
HETATM 2757  N1  SAH A 501      10.519  28.999  45.076  1.00 31.96           N  
HETATM 2758  C2  SAH A 501       9.175  28.670  45.010  1.00 34.77           C  
HETATM 2759  N3  SAH A 501       8.639  27.748  45.908  1.00 34.00           N  
HETATM 2760  C4  SAH A 501       9.437  27.183  46.859  1.00 34.77           C  
HETATM 2761  O6 A37T A 502       7.984  21.918  59.473  0.33 24.90           O  
HETATM 2762  O6 B37T A 502       3.836  22.513  55.693  0.33 21.99           O  
HETATM 2763  C6 A37T A 502       7.454  22.194  58.379  0.33 26.32           C  
HETATM 2764  C6 B37T A 502       5.049  22.531  55.971  0.33 21.97           C  
HETATM 2765  N1 A37T A 502       8.193  22.637  57.328  0.33 25.65           N  
HETATM 2766  N1 B37T A 502       5.955  22.950  55.047  0.33 21.58           N  
HETATM 2767  C5 A37T A 502       5.991  22.076  58.137  0.33 26.36           C  
HETATM 2768  C5 B37T A 502       5.601  22.119  57.300  0.33 21.77           C  
HETATM 2769  N7 A37T A 502       4.948  21.690  58.877  0.33 25.73           N  
HETATM 2770  N7 B37T A 502       5.072  21.645  58.448  0.33 22.13           N  
HETATM 2771  C13A37T A 502       5.007  21.245  60.270  0.33 25.46           C  
HETATM 2772  C13B37T A 502       3.643  21.396  58.730  0.33 21.07           C  
HETATM 2773  C8 A37T A 502       3.838  21.782  58.105  0.33 25.33           C  
HETATM 2774  C8 B37T A 502       6.100  21.432  59.316  0.33 21.17           C  
HETATM 2775  N9 A37T A 502       4.140  22.230  56.852  0.33 25.42           N  
HETATM 2776  N9 B37T A 502       7.305  21.746  58.749  0.33 21.40           N  
HETATM 2777  C4 A37T A 502       5.478  22.430  56.830  0.33 26.10           C  
HETATM 2778  C4 B37T A 502       7.042  22.178  57.483  0.33 20.97           C  
HETATM 2779  N3 A37T A 502       6.310  22.847  55.872  0.33 26.21           N  
HETATM 2780  N3 B37T A 502       7.839  22.614  56.496  0.33 20.89           N  
HETATM 2781  C12A37T A 502       5.767  23.191  54.561  0.33 25.77           C  
HETATM 2782  C12B37T A 502       9.291  22.660  56.710  0.33 21.30           C  
HETATM 2783  C2 A37T A 502       7.635  22.946  56.120  0.33 25.33           C  
HETATM 2784  C2 B37T A 502       7.298  22.992  55.303  0.33 20.88           C  
HETATM 2785  O2 A37T A 502       8.393  23.335  55.205  0.33 25.21           O  
HETATM 2786  O2 B37T A 502       8.039  23.392  54.381  0.33 21.11           O  
HETATM 2787  O   HOH A 503       7.268  31.348  53.588  1.00 24.96           O  
HETATM 2788  O   HOH A 504       2.769  41.274  37.573  1.00 32.52           O  
HETATM 2789  O   HOH A 505      27.198  29.136  53.541  1.00 29.72           O  
HETATM 2790  O   HOH A 506       2.190  34.100  55.577  1.00 26.50           O  
HETATM 2791  O   HOH A 507      20.048   4.295  52.538  1.00 40.72           O  
HETATM 2792  O   HOH A 508       1.390  20.148  55.958  1.00 59.56           O  
HETATM 2793  O   HOH A 509       8.748  22.482  61.604  0.50 13.72           O  
HETATM 2794  O   HOH A 510       5.125  21.717  46.482  1.00 43.82           O  
HETATM 2795  O   HOH A 511      25.860  35.597  53.635  1.00 39.09           O  
HETATM 2796  O   HOH A 512       3.028  18.862  73.485  1.00 43.98           O  
HETATM 2797  O   HOH A 513      -4.874  37.394  34.684  1.00 31.50           O  
HETATM 2798  O   HOH A 514       8.477  25.026  63.159  1.00 50.48           O  
HETATM 2799  O   HOH A 515      13.573  33.808  67.660  1.00 40.08           O  
HETATM 2800  O   HOH A 516      15.194  46.425  45.802  1.00 54.33           O  
HETATM 2801  O   HOH A 517       2.632  30.481  50.446  1.00 28.88           O  
HETATM 2802  O   HOH A 518      -4.636  21.149  33.890  1.00 46.67           O  
HETATM 2803  O   HOH A 519      13.108  30.608  38.518  1.00 41.43           O  
HETATM 2804  O   HOH A 520      14.110  26.852  47.630  1.00 29.54           O  
HETATM 2805  O   HOH A 521      15.043  25.654  45.353  1.00 48.67           O  
HETATM 2806  O   HOH A 522       1.208  17.472  54.453  1.00 71.78           O  
HETATM 2807  O   HOH A 523       9.759  23.895  66.516  1.00 36.75           O  
HETATM 2808  O   HOH A 524      14.409  44.907  53.906  1.00 42.71           O  
HETATM 2809  O   HOH A 525       6.143  37.664  69.520  1.00 42.51           O  
HETATM 2810  O   HOH A 526      24.719  15.412  57.558  1.00 34.73           O  
HETATM 2811  O   HOH A 527      14.851   2.651  67.749  1.00 53.99           O  
HETATM 2812  O   HOH A 528      16.641   2.611  51.589  1.00 38.82           O  
HETATM 2813  O   HOH A 529      -1.626  25.668  57.582  1.00 33.85           O  
HETATM 2814  O   HOH A 530       9.551  45.440  34.396  1.00 33.61           O  
HETATM 2815  O   HOH A 531      -0.391  22.174  56.844  1.00 44.15           O  
HETATM 2816  O   HOH A 532      10.677  21.077  41.573  1.00 62.99           O  
HETATM 2817  O   HOH A 533      21.810  11.667  47.497  1.00 54.10           O  
HETATM 2818  O   HOH A 534      -7.342  52.546  42.342  1.00 40.74           O  
HETATM 2819  O   HOH A 535      18.452  26.629  62.342  1.00 39.05           O  
HETATM 2820  O   HOH A 536      10.632  31.679  36.485  1.00 33.85           O  
HETATM 2821  O   HOH A 537      -4.176  58.464  48.362  1.00 50.40           O  
HETATM 2822  O   HOH A 538      14.400   1.247  48.097  1.00 73.00           O  
HETATM 2823  O   HOH A 539      -9.536  54.547  42.130  1.00 44.49           O  
HETATM 2824  O   HOH A 540       0.722  44.811  58.240  1.00 47.62           O  
HETATM 2825  O   HOH A 541       3.204  23.030  76.563  1.00 33.51           O  
HETATM 2826  O   HOH A 542      22.557  15.125  51.096  1.00 43.56           O  
HETATM 2827  O   HOH A 543      -4.630  32.653  55.860  1.00 39.95           O  
HETATM 2828  O   HOH A 544       6.980  23.894  77.482  1.00 40.93           O  
HETATM 2829  O   HOH A 545      -2.796  21.930  50.881  1.00 38.23           O  
HETATM 2830  O   HOH A 546      -6.719  16.459  49.954  1.00 64.50           O  
HETATM 2831  O   HOH A 547      -0.633  29.095  51.245  1.00 50.16           O  
HETATM 2832  O   HOH A 548      12.758  25.729  65.148  1.00 37.46           O  
HETATM 2833  O   HOH A 549       0.285  10.693  47.485  1.00 50.26           O  
HETATM 2834  O   HOH A 550      -3.054  32.733  54.051  1.00 37.34           O  
HETATM 2835  O   HOH A 551       0.622  46.450  37.352  1.00 39.35           O  
HETATM 2836  O   HOH A 552      11.409   1.664  67.344  1.00 49.27           O  
HETATM 2837  O   HOH A 553     -16.135  21.580  36.966  1.00 54.67           O  
HETATM 2838  O   HOH A 554      -0.826  43.164  59.562  1.00 43.39           O  
HETATM 2839  O   HOH A 555      25.953   8.637  50.906  1.00 53.67           O  
HETATM 2840  O   HOH A 556       1.127  19.869  71.418  1.00 38.54           O  
HETATM 2841  O   HOH A 557      11.110  16.679  50.001  1.00 38.11           O  
HETATM 2842  O   HOH A 558       5.869  52.291  53.758  1.00 53.70           O  
HETATM 2843  O   HOH A 559       5.345  49.891  36.728  1.00 45.68           O  
HETATM 2844  O   HOH A 560      14.136  56.364  47.566  1.00 56.03           O  
HETATM 2845  O   HOH A 561      27.718  19.199  63.104  1.00 35.94           O  
HETATM 2846  O   HOH A 562      -7.583  18.178  39.962  1.00 48.17           O  
HETATM 2847  O   HOH A 563      19.849  33.315  46.751  1.00 58.38           O  
HETATM 2848  O   HOH A 564       1.776  11.336  72.587  1.00 54.65           O  
HETATM 2849  O   HOH A 565      24.631  17.371  50.427  1.00 44.14           O  
HETATM 2850  O   HOH A 566      26.449   9.613  63.331  1.00 63.40           O  
HETATM 2851  O   HOH A 567      -1.115  47.952  38.814  1.00 46.11           O  
HETATM 2852  O   HOH A 568      20.783  40.710  46.959  1.00 50.00           O  
HETATM 2853  O   HOH A 569       5.312  43.608  65.994  1.00 45.28           O  
HETATM 2854  O   HOH A 570      22.512  27.932  63.474  1.00 49.25           O  
HETATM 2855  O   HOH A 571      18.177  35.983  41.694  1.00 47.05           O  
HETATM 2856  O   HOH A 572      23.245  28.442  68.180  1.00 57.13           O  
HETATM 2857  O   HOH A 573      11.717  48.786  60.086  1.00 44.62           O  
HETATM 2858  O   HOH A 574      -2.315  44.160  35.598  1.00 45.69           O  
HETATM 2859  O   HOH A 575      -9.440  24.764  50.435  1.00 51.14           O  
HETATM 2860  O   HOH A 576      -7.427  14.069  49.599  1.00 52.56           O  
HETATM 2861  O   HOH A 577       7.496  47.251  34.762  1.00 49.08           O  
HETATM 2862  O   HOH A 578      27.942   2.830  60.830  1.00 55.69           O  
HETATM 2863  O   HOH A 579      -7.467  40.922  61.955  1.00 44.94           O  
HETATM 2864  O   HOH A 580      15.184  32.899  52.553  1.00 42.85           O  
HETATM 2865  O   HOH A 581      12.801  11.468  45.222  1.00 45.06           O  
HETATM 2866  O   HOH A 582      -0.995  34.164  68.459  1.00 60.10           O  
HETATM 2867  O   HOH A 583      21.342  46.144  50.132  1.00 62.79           O  
HETATM 2868  O   HOH A 584       0.325  46.707  60.175  1.00 46.19           O  
HETATM 2869  O   HOH A 585     -11.151  35.188  55.304  1.00 45.71           O  
HETATM 2870  O   HOH A 586      -5.601  48.322  60.995  1.00 53.03           O  
HETATM 2871  O   HOH A 587       1.485  23.557  56.059  1.00 44.62           O  
HETATM 2872  O   HOH A 588      -8.436  44.159  60.160  1.00 63.34           O  
HETATM 2873  O   HOH A 589      23.701  31.255  47.232  1.00 47.01           O  
HETATM 2874  O   HOH A 590      20.417  27.036  64.308  1.00 52.45           O  
HETATM 2875  O   HOH A 591      22.187  22.451  46.676  1.00 48.63           O  
HETATM 2876  O   HOH A 592      12.405  50.329  49.228  1.00 45.54           O  
HETATM 2877  O   HOH A 593      21.447  42.995  48.272  1.00 41.78           O  
HETATM 2878  O   HOH A 594      18.302   6.590  45.593  1.00 60.20           O  
HETATM 2879  O   HOH A 595      -0.999  45.111  64.584  1.00 58.08           O  
HETATM 2880  O   HOH A 596      -1.100   8.667  46.213  1.00 62.47           O  
HETATM 2881  O   HOH A 597       5.674  -1.073  67.682  1.00 55.61           O  
HETATM 2882  O   HOH A 598      13.360  26.305  71.470  1.00 47.17           O  
HETATM 2883  O   HOH A 599       9.111  56.055  46.503  1.00 49.20           O  
HETATM 2884  O   HOH A 600       4.917  42.292  68.116  1.00 52.54           O  
HETATM 2885  O   HOH A 601      33.684  31.653  56.541  1.00 55.75           O  
HETATM 2886  O   HOH A 602     -13.016  32.767  60.276  1.00 57.25           O  
HETATM 2887  O   HOH A 603      -4.443  11.965  72.549  1.00 55.37           O  
HETATM 2888  O   HOH A 604      22.489  20.135  46.117  1.00 50.10           O  
HETATM 2889  O   HOH A 605      12.137  18.761  73.488  1.00 56.72           O  
HETATM 2890  O   HOH A 606      20.654  41.836  54.427  1.00 41.60           O  
HETATM 2891  O   HOH A 607      16.315  29.181  43.827  1.00 38.02           O  
HETATM 2892  O   HOH A 608      17.569  24.739  64.800  1.00 53.19           O  
HETATM 2893  O   HOH A 609      16.352  37.075  38.567  1.00 47.41           O  
HETATM 2894  O   HOH A 610      -8.028  30.995  36.075  1.00 27.92           O  
HETATM 2895  O   HOH A 611      12.172  33.160  39.153  1.00 38.03           O  
HETATM 2896  O   HOH A 612      30.984  19.099  61.732  1.00 50.37           O  
HETATM 2897  O   HOH A 613      22.410  40.955  56.130  1.00 48.60           O  
HETATM 2898  O   HOH A 614      -1.684  26.441  65.614  1.00 45.98           O  
HETATM 2899  O   HOH A 615      19.348  33.156  44.258  1.00 49.45           O  
HETATM 2900  O   HOH A 616       4.399   8.381  48.787  1.00 56.54           O  
HETATM 2901  O   HOH A 617      13.037  58.107  49.218  1.00 67.97           O  
HETATM 2902  O   HOH A 618      13.015  27.401  68.974  1.00 40.69           O  
HETATM 2903  O   HOH A 619      23.096  37.783  59.051  1.00 39.88           O  
HETATM 2904  O   HOH A 620      -7.167  49.139  58.970  1.00 56.26           O  
HETATM 2905  O   HOH A 621      24.148  45.913  52.882  1.00 52.42           O  
HETATM 2906  O   HOH A 622       2.496  17.764  62.092  1.00 52.10           O  
HETATM 2907  O   HOH A 623     -15.072  44.624  41.078  1.00 54.55           O  
HETATM 2908  O   HOH A 624      -1.262  48.771  62.741  1.00 47.91           O  
HETATM 2909  O   HOH A 625      19.150  10.828  68.529  1.00 45.76           O  
HETATM 2910  O   HOH A 626      16.975   3.727  68.790  1.00 53.48           O  
HETATM 2911  O   HOH A 627      22.990   9.019  48.307  1.00 51.62           O  
HETATM 2912  O   HOH A 628     -16.168  33.805  40.846  1.00 53.56           O  
HETATM 2913  O   HOH A 629      33.205  16.096  60.989  1.00 50.30           O  
HETATM 2914  O   HOH A 630      28.188  25.643  46.554  1.00 56.78           O  
HETATM 2915  O   HOH A 631      29.551  30.439  54.767  1.00 59.56           O  
HETATM 2916  O   HOH A 632       1.490  53.717  47.104  1.00 44.54           O  
HETATM 2917  O   HOH A 633       2.204  20.111  44.646  1.00 43.36           O  
HETATM 2918  O   HOH A 634      -1.878  16.499  36.764  1.00 43.53           O  
HETATM 2919  O   HOH A 635     -17.837  43.996  50.213  1.00 65.29           O  
HETATM 2920  O   HOH A 636     -13.839  45.504  48.010  1.00 49.61           O  
HETATM 2921  O   HOH A 637      17.665  20.978  66.935  1.00 50.28           O  
HETATM 2922  O   HOH A 638      -9.225  10.891  61.566  1.00 63.86           O  
HETATM 2923  O   HOH A 639       1.399  42.062  35.662  1.00 46.66           O  
HETATM 2924  O   HOH A 640      -3.775  47.107  38.929  1.00 32.64           O  
HETATM 2925  O   HOH A 641      15.194  42.350  40.068  1.00 48.87           O  
HETATM 2926  O   HOH A 642       8.854  54.839  43.889  1.00 61.84           O  
HETATM 2927  O   HOH A 643      18.498  40.041  39.644  1.00 50.05           O  
HETATM 2928  O   HOH A 644     -16.810  28.302  36.978  1.00 47.76           O  
HETATM 2929  O   HOH A 645     -11.620  24.904  46.388  1.00 49.14           O  
HETATM 2930  O   HOH A 646     -13.966  35.078  39.234  1.00 70.83           O  
HETATM 2931  O   HOH A 647       0.401  25.878  56.086  1.00 39.48           O  
HETATM 2932  O   HOH A 648      14.959   9.024  69.817  1.00 48.58           O  
CONECT 2735 2736                                                                
CONECT 2736 2735 2737 2740                                                      
CONECT 2737 2736 2738                                                           
CONECT 2738 2737 2739                                                           
CONECT 2739 2738 2743                                                           
CONECT 2740 2736 2741 2742                                                      
CONECT 2741 2740                                                                
CONECT 2742 2740                                                                
CONECT 2743 2739 2744                                                           
CONECT 2744 2743 2745 2746                                                      
CONECT 2745 2744 2750                                                           
CONECT 2746 2744 2747 2748                                                      
CONECT 2747 2746                                                                
CONECT 2748 2746 2749 2750                                                      
CONECT 2749 2748                                                                
CONECT 2750 2745 2748 2751                                                      
CONECT 2751 2750 2752 2760                                                      
CONECT 2752 2751 2753                                                           
CONECT 2753 2752 2754                                                           
CONECT 2754 2753 2755 2760                                                      
CONECT 2755 2754 2756 2757                                                      
CONECT 2756 2755                                                                
CONECT 2757 2755 2758                                                           
CONECT 2758 2757 2759                                                           
CONECT 2759 2758 2760                                                           
CONECT 2760 2751 2754 2759                                                      
CONECT 2761 2763                                                                
CONECT 2762 2764                                                                
CONECT 2763 2761 2765 2767                                                      
CONECT 2764 2762 2766 2768                                                      
CONECT 2765 2763 2783                                                           
CONECT 2766 2764 2784                                                           
CONECT 2767 2763 2769 2777                                                      
CONECT 2768 2764 2770 2778                                                      
CONECT 2769 2767 2771 2773                                                      
CONECT 2770 2768 2772 2774                                                      
CONECT 2771 2769                                                                
CONECT 2772 2770                                                                
CONECT 2773 2769 2775                                                           
CONECT 2774 2770 2776                                                           
CONECT 2775 2773 2777                                                           
CONECT 2776 2774 2778                                                           
CONECT 2777 2767 2775 2779                                                      
CONECT 2778 2768 2776 2780                                                      
CONECT 2779 2777 2781 2783                                                      
CONECT 2780 2778 2782 2784                                                      
CONECT 2781 2779                                                                
CONECT 2782 2780                                                                
CONECT 2783 2765 2779 2785                                                      
CONECT 2784 2766 2780 2786                                                      
CONECT 2785 2783                                                                
CONECT 2786 2784                                                                
MASTER      436    0    2   10    7    0   10    6 2904    1   52   30          
END