HEADER    HYDROLASE                               16-SEP-97   2HEB              
TITLE     CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE   
TITLE    2 CONFORMATIONAL STABILITY                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSOZYME;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.17;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HUMAN LYSOZYME WITH ILE 23 REP;                                
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: AH22R-;                                    
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PERI8602;                                 
SOURCE  11 EXPRESSION_SYSTEM_GENE: HUMAN LYSOZYME WITH ILE 23 REPLACED BY ALA   
KEYWDS    HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAKANO,J.FUNAHASHI,Y.YAMAGATA,S.FUJII,K.YUTANI                      
REVDAT   3   03-NOV-21 2HEB    1       REMARK SEQADV LINK                       
REVDAT   2   24-FEB-09 2HEB    1       VERSN                                    
REVDAT   1   28-JAN-98 2HEB    0                                                
JRNL        AUTH   K.TAKANO,J.FUNAHASHI,Y.YAMAGATA,S.FUJII,K.YUTANI             
JRNL        TITL   CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN 
JRNL        TITL 2 TO THE CONFORMATIONAL STABILITY.                             
JRNL        REF    J.MOL.BIOL.                   V. 274   132 1997              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9398521                                                      
JRNL        DOI    10.1006/JMBI.1997.1365                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.TAKANO,Y.YAMAGATA,S.FUJII,K.YUTANI                         
REMARK   1  TITL   CONTRIBUTION OF THE HYDROPHOBIC EFFECT TO THE STABILITY OF   
REMARK   1  TITL 2 HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL    
REMARK   1  TITL 3 ANALYSES OF THE NINE VALINE TO ALANINE MUTANTS               
REMARK   1  REF    BIOCHEMISTRY                  V.  36   688 1997              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.TAKANO,K.OGASAHARA,H.KANEDA,Y.YAMAGATA,S.FUJII,E.KANAYA,   
REMARK   1  AUTH 2 M.KIKUCHI,M.OOBATAKE,K.YUTANI                                
REMARK   1  TITL   CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF     
REMARK   1  TITL 2 HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL    
REMARK   1  TITL 3 ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS            
REMARK   1  REF    J.MOL.BIOL.                   V. 254    62 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 66.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 4109                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.124                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1026                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 230                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.520                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2HEB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000178179.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-96                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5702                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 67.7                               
REMARK 200  DATA REDUNDANCY                : 3.870                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.40000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       16.88000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.61000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       16.88000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.40000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.61000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ASP A  18      109.97    -55.01                                   
REMARK 500    PRO A 103      -20.28    -39.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  61   O                                                      
REMARK 620 2 CYS A  65   O    82.9                                              
REMARK 620 3 VAL A  74   O   117.1 109.5                                        
REMARK 620 4 HOH A 140   O    68.4  84.9 164.7                                  
REMARK 620 5 HOH A 283   O   147.7 118.3  80.4  88.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 601                  
DBREF  2HEB A    1   130  UNP    P61626   LYSC_HUMAN      19    148             
SEQADV 2HEB ALA A   23  UNP  P61626    ILE    41 ENGINEERED MUTATION            
SEQRES   1 A  130  LYS VAL PHE GLU ARG CYS GLU LEU ALA ARG THR LEU LYS          
SEQRES   2 A  130  ARG LEU GLY MET ASP GLY TYR ARG GLY ALA SER LEU ALA          
SEQRES   3 A  130  ASN TRP MET CYS LEU ALA LYS TRP GLU SER GLY TYR ASN          
SEQRES   4 A  130  THR ARG ALA THR ASN TYR ASN ALA GLY ASP ARG SER THR          
SEQRES   5 A  130  ASP TYR GLY ILE PHE GLN ILE ASN SER ARG TYR TRP CYS          
SEQRES   6 A  130  ASN ASP GLY LYS THR PRO GLY ALA VAL ASN ALA CYS HIS          
SEQRES   7 A  130  LEU SER CYS SER ALA LEU LEU GLN ASP ASN ILE ALA ASP          
SEQRES   8 A  130  ALA VAL ALA CYS ALA LYS ARG VAL VAL ARG ASP PRO GLN          
SEQRES   9 A  130  GLY ILE ARG ALA TRP VAL ALA TRP ARG ASN ARG CYS GLN          
SEQRES  10 A  130  ASN ARG ASP VAL ARG GLN TYR VAL GLN GLY CYS GLY VAL          
HET     NA  A 601       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   2   NA    NA 1+                                                        
FORMUL   3  HOH   *230(H2 O)                                                    
HELIX    1   1 ARG A    5  ARG A   14  1                                  10    
HELIX    2   2 LEU A   25  SER A   36  1                                  12    
HELIX    3   3 CYS A   81  LEU A   85  5                                   5    
HELIX    4   4 ALA A   90  VAL A  100  1                                  11    
HELIX    5   5 GLY A  105  ALA A  108  5                                   4    
HELIX    6   6 VAL A  110  ARG A  115  1                                   6    
HELIX    7   7 ARG A  122  TYR A  124  5                                   3    
SHEET    1   A 3 THR A  43  ASN A  46  0                                        
SHEET    2   A 3 SER A  51  TYR A  54 -1                                        
SHEET    3   A 3 ILE A  59  ASN A  60 -1                                        
SSBOND   1 CYS A    6    CYS A  128                          1555   1555  2.03  
SSBOND   2 CYS A   30    CYS A  116                          1555   1555  2.02  
SSBOND   3 CYS A   65    CYS A   81                          1555   1555  2.03  
SSBOND   4 CYS A   77    CYS A   95                          1555   1555  2.02  
LINK         O   SER A  61                NA    NA A 601     1554   1555  2.12  
LINK         O   CYS A  65                NA    NA A 601     1554   1555  2.28  
LINK         O   VAL A  74                NA    NA A 601     1554   1555  2.53  
LINK         O   HOH A 140                NA    NA A 601     1555   1555  2.44  
LINK         O   HOH A 283                NA    NA A 601     1555   1555  2.15  
SITE     1 AC1  7 SER A  61  CYS A  65  ASN A  66  ALA A  73                    
SITE     2 AC1  7 VAL A  74  HOH A 140  HOH A 283                               
CRYST1   56.800   61.220   33.760  90.00  90.00  90.00 P 21 21 21    4          
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      0.017606  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029621        0.00000                         
ATOM      1  N   LYS A   1       1.002  19.400  23.148  1.00  6.65           N  
ATOM      2  CA  LYS A   1       1.496  20.420  22.169  1.00  5.07           C  
ATOM      3  C   LYS A   1       2.727  19.863  21.479  1.00  3.18           C  
ATOM      4  O   LYS A   1       3.531  19.191  22.117  1.00  2.58           O  
ATOM      5  CB  LYS A   1       1.897  21.697  22.911  1.00  2.99           C  
ATOM      6  CG  LYS A   1       2.443  22.775  22.028  1.00  5.34           C  
ATOM      7  CD  LYS A   1       3.086  23.840  22.867  1.00  7.46           C  
ATOM      8  CE  LYS A   1       3.852  24.814  22.011  1.00  7.04           C  
ATOM      9  NZ  LYS A   1       4.436  25.854  22.887  1.00 12.51           N  
ATOM     10  N   VAL A   2       2.849  20.082  20.179  1.00  2.01           N  
ATOM     11  CA  VAL A   2       4.032  19.609  19.486  1.00  5.77           C  
ATOM     12  C   VAL A   2       4.888  20.844  19.182  1.00  6.36           C  
ATOM     13  O   VAL A   2       4.505  21.681  18.368  1.00  6.45           O  
ATOM     14  CB  VAL A   2       3.681  18.858  18.185  1.00  4.19           C  
ATOM     15  CG1 VAL A   2       4.936  18.193  17.614  1.00  3.25           C  
ATOM     16  CG2 VAL A   2       2.599  17.822  18.459  1.00  4.73           C  
ATOM     17  N   PHE A   3       6.005  20.991  19.888  1.00  6.03           N  
ATOM     18  CA  PHE A   3       6.896  22.140  19.701  1.00  6.20           C  
ATOM     19  C   PHE A   3       7.658  22.161  18.399  1.00  6.63           C  
ATOM     20  O   PHE A   3       7.974  21.109  17.844  1.00 10.00           O  
ATOM     21  CB  PHE A   3       7.938  22.195  20.811  1.00  4.41           C  
ATOM     22  CG  PHE A   3       7.474  22.882  22.046  1.00  4.56           C  
ATOM     23  CD1 PHE A   3       7.718  24.228  22.226  1.00  2.00           C  
ATOM     24  CD2 PHE A   3       6.873  22.162  23.073  1.00  4.91           C  
ATOM     25  CE1 PHE A   3       7.384  24.855  23.416  1.00  7.23           C  
ATOM     26  CE2 PHE A   3       6.530  22.777  24.270  1.00  7.19           C  
ATOM     27  CZ  PHE A   3       6.788  24.129  24.446  1.00  6.86           C  
ATOM     28  N   GLU A   4       7.927  23.363  17.892  1.00  8.14           N  
ATOM     29  CA  GLU A   4       8.732  23.497  16.689  1.00  7.59           C  
ATOM     30  C   GLU A   4      10.141  23.608  17.275  1.00  5.26           C  
ATOM     31  O   GLU A   4      10.306  24.105  18.393  1.00  2.29           O  
ATOM     32  CB  GLU A   4       8.333  24.725  15.855  1.00 13.68           C  
ATOM     33  CG  GLU A   4       7.007  24.537  15.089  1.00 24.57           C  
ATOM     34  CD  GLU A   4       6.871  25.393  13.814  1.00 30.43           C  
ATOM     35  OE1 GLU A   4       7.667  25.211  12.861  1.00 29.56           O  
ATOM     36  OE2 GLU A   4       5.937  26.226  13.751  1.00 34.60           O  
ATOM     37  N   ARG A   5      11.136  23.106  16.545  1.00  4.84           N  
ATOM     38  CA  ARG A   5      12.529  23.069  17.007  1.00  4.23           C  
ATOM     39  C   ARG A   5      13.090  24.309  17.708  1.00  5.96           C  
ATOM     40  O   ARG A   5      13.344  24.276  18.914  1.00  2.02           O  
ATOM     41  CB  ARG A   5      13.462  22.651  15.868  1.00  6.46           C  
ATOM     42  CG  ARG A   5      14.913  22.416  16.312  1.00  8.06           C  
ATOM     43  CD  ARG A   5      15.779  21.942  15.151  1.00  2.96           C  
ATOM     44  NE  ARG A   5      15.747  22.863  14.012  1.00  5.33           N  
ATOM     45  CZ  ARG A   5      16.708  23.742  13.727  1.00  7.19           C  
ATOM     46  NH1 ARG A   5      16.594  24.529  12.664  1.00  7.00           N  
ATOM     47  NH2 ARG A   5      17.769  23.858  14.516  1.00  4.72           N  
ATOM     48  N   CYS A   6      13.264  25.404  16.969  1.00  4.87           N  
ATOM     49  CA  CYS A   6      13.815  26.627  17.552  1.00  4.82           C  
ATOM     50  C   CYS A   6      12.981  27.211  18.671  1.00  4.62           C  
ATOM     51  O   CYS A   6      13.521  27.830  19.581  1.00  4.87           O  
ATOM     52  CB  CYS A   6      14.085  27.669  16.471  1.00  7.47           C  
ATOM     53  SG  CYS A   6      15.465  27.159  15.409  1.00  8.07           S  
ATOM     54  N   GLU A   7      11.677  26.950  18.632  1.00  6.77           N  
ATOM     55  CA  GLU A   7      10.750  27.426  19.647  1.00  8.76           C  
ATOM     56  C   GLU A   7      11.103  26.734  20.961  1.00  9.89           C  
ATOM     57  O   GLU A   7      11.149  27.366  22.021  1.00  9.81           O  
ATOM     58  CB  GLU A   7       9.313  27.080  19.251  1.00 11.77           C  
ATOM     59  CG  GLU A   7       8.270  27.599  20.231  1.00 16.98           C  
ATOM     60  CD  GLU A   7       6.911  26.889  20.148  1.00 19.41           C  
ATOM     61  OE1 GLU A   7       6.560  26.309  19.087  1.00 17.17           O  
ATOM     62  OE2 GLU A   7       6.194  26.934  21.172  1.00 16.01           O  
ATOM     63  N   LEU A   8      11.362  25.432  20.880  1.00  9.10           N  
ATOM     64  CA  LEU A   8      11.727  24.645  22.055  1.00  4.50           C  
ATOM     65  C   LEU A   8      13.099  25.088  22.570  1.00  3.44           C  
ATOM     66  O   LEU A   8      13.294  25.255  23.778  1.00  3.27           O  
ATOM     67  CB  LEU A   8      11.755  23.150  21.700  1.00  4.77           C  
ATOM     68  CG  LEU A   8      12.020  22.188  22.870  1.00  5.66           C  
ATOM     69  CD1 LEU A   8      11.021  22.449  23.983  1.00  5.99           C  
ATOM     70  CD2 LEU A   8      11.947  20.751  22.413  1.00  3.70           C  
ATOM     71  N   ALA A   9      14.033  25.294  21.643  1.00  3.51           N  
ATOM     72  CA  ALA A   9      15.397  25.712  21.967  1.00  4.86           C  
ATOM     73  C   ALA A   9      15.381  26.975  22.795  1.00  5.49           C  
ATOM     74  O   ALA A   9      15.986  27.034  23.863  1.00  4.78           O  
ATOM     75  CB  ALA A   9      16.190  25.941  20.691  1.00  6.38           C  
ATOM     76  N   ARG A  10      14.650  27.975  22.311  1.00  6.61           N  
ATOM     77  CA  ARG A  10      14.533  29.253  23.008  1.00  5.79           C  
ATOM     78  C   ARG A  10      13.814  29.105  24.317  1.00  2.08           C  
ATOM     79  O   ARG A  10      14.180  29.740  25.307  1.00  2.01           O  
ATOM     80  CB  ARG A  10      13.852  30.314  22.125  1.00  2.56           C  
ATOM     81  CG  ARG A  10      14.795  30.839  21.052  1.00  7.62           C  
ATOM     82  CD  ARG A  10      14.234  32.050  20.323  1.00  5.35           C  
ATOM     83  NE  ARG A  10      12.974  31.756  19.648  1.00  5.35           N  
ATOM     84  CZ  ARG A  10      12.879  31.298  18.407  1.00  6.78           C  
ATOM     85  NH1 ARG A  10      11.687  31.072  17.880  1.00  7.06           N  
ATOM     86  NH2 ARG A  10      13.972  31.046  17.697  1.00 10.32           N  
ATOM     87  N   THR A  11      12.788  28.269  24.336  1.00  2.02           N  
ATOM     88  CA  THR A  11      12.037  28.042  25.570  1.00  3.07           C  
ATOM     89  C   THR A  11      12.898  27.355  26.651  1.00  2.00           C  
ATOM     90  O   THR A  11      12.851  27.739  27.817  1.00  3.95           O  
ATOM     91  CB  THR A  11      10.739  27.248  25.289  1.00  3.48           C  
ATOM     92  OG1 THR A  11       9.974  27.940  24.292  1.00  7.10           O  
ATOM     93  CG2 THR A  11       9.884  27.127  26.546  1.00  2.29           C  
ATOM     94  N   LEU A  12      13.744  26.410  26.257  1.00  2.03           N  
ATOM     95  CA  LEU A  12      14.601  25.693  27.210  1.00  2.01           C  
ATOM     96  C   LEU A  12      15.672  26.595  27.797  1.00  2.56           C  
ATOM     97  O   LEU A  12      16.044  26.480  28.975  1.00  2.03           O  
ATOM     98  CB  LEU A  12      15.256  24.478  26.534  1.00  2.09           C  
ATOM     99  CG  LEU A  12      14.329  23.294  26.255  1.00  2.03           C  
ATOM    100  CD1 LEU A  12      15.114  22.144  25.635  1.00  2.98           C  
ATOM    101  CD2 LEU A  12      13.660  22.850  27.554  1.00  2.04           C  
ATOM    102  N   LYS A  13      16.181  27.484  26.950  1.00  5.42           N  
ATOM    103  CA  LYS A  13      17.209  28.426  27.347  1.00  3.01           C  
ATOM    104  C   LYS A  13      16.661  29.365  28.411  1.00  2.00           C  
ATOM    105  O   LYS A  13      17.328  29.647  29.397  1.00  2.00           O  
ATOM    106  CB  LYS A  13      17.702  29.221  26.127  1.00  5.57           C  
ATOM    107  CG  LYS A  13      18.846  30.148  26.490  1.00 10.90           C  
ATOM    108  CD  LYS A  13      19.603  30.642  25.302  1.00 15.20           C  
ATOM    109  CE  LYS A  13      21.099  30.708  25.629  1.00 17.22           C  
ATOM    110  NZ  LYS A  13      21.353  31.488  26.858  1.00 22.23           N  
ATOM    111  N   ARG A  14      15.422  29.802  28.232  1.00  2.01           N  
ATOM    112  CA  ARG A  14      14.762  30.711  29.175  1.00  5.04           C  
ATOM    113  C   ARG A  14      14.533  30.050  30.538  1.00  3.35           C  
ATOM    114  O   ARG A  14      14.559  30.711  31.569  1.00  2.02           O  
ATOM    115  CB  ARG A  14      13.429  31.184  28.585  1.00  8.79           C  
ATOM    116  CG  ARG A  14      13.258  32.691  28.545  1.00 14.14           C  
ATOM    117  CD  ARG A  14      12.302  33.117  27.421  1.00 19.99           C  
ATOM    118  NE  ARG A  14      11.017  32.409  27.452  1.00 23.30           N  
ATOM    119  CZ  ARG A  14      10.370  31.969  26.372  1.00 24.43           C  
ATOM    120  NH1 ARG A  14       9.215  31.333  26.510  1.00 23.08           N  
ATOM    121  NH2 ARG A  14      10.877  32.155  25.156  1.00 26.60           N  
ATOM    122  N   LEU A  15      14.353  28.733  30.523  1.00  2.86           N  
ATOM    123  CA  LEU A  15      14.125  27.951  31.729  1.00  2.08           C  
ATOM    124  C   LEU A  15      15.421  27.549  32.428  1.00  3.52           C  
ATOM    125  O   LEU A  15      15.384  26.860  33.444  1.00  2.48           O  
ATOM    126  CB  LEU A  15      13.259  26.721  31.413  1.00  5.31           C  
ATOM    127  CG  LEU A  15      11.814  26.976  30.949  1.00  5.18           C  
ATOM    128  CD1 LEU A  15      11.169  25.720  30.387  1.00  3.17           C  
ATOM    129  CD2 LEU A  15      11.007  27.524  32.101  1.00  4.21           C  
ATOM    130  N   GLY A  16      16.562  27.941  31.857  1.00  2.79           N  
ATOM    131  CA  GLY A  16      17.856  27.664  32.474  1.00  4.62           C  
ATOM    132  C   GLY A  16      18.507  26.314  32.248  1.00  7.77           C  
ATOM    133  O   GLY A  16      19.287  25.838  33.090  1.00  7.17           O  
ATOM    134  N   MET A  17      18.271  25.748  31.068  1.00  8.91           N  
ATOM    135  CA  MET A  17      18.801  24.437  30.722  1.00  6.82           C  
ATOM    136  C   MET A  17      20.185  24.436  30.100  1.00  7.63           C  
ATOM    137  O   MET A  17      20.949  23.487  30.277  1.00  9.51           O  
ATOM    138  CB  MET A  17      17.808  23.708  29.811  1.00 11.19           C  
ATOM    139  CG  MET A  17      16.529  23.264  30.533  1.00 11.91           C  
ATOM    140  SD  MET A  17      16.853  21.920  31.689  1.00 20.80           S  
ATOM    141  CE  MET A  17      15.814  20.623  31.003  1.00 19.39           C  
ATOM    142  N   ASP A  18      20.529  25.495  29.383  1.00  7.80           N  
ATOM    143  CA  ASP A  18      21.841  25.555  28.753  1.00  6.49           C  
ATOM    144  C   ASP A  18      22.960  25.349  29.774  1.00  3.57           C  
ATOM    145  O   ASP A  18      23.177  26.183  30.648  1.00  6.00           O  
ATOM    146  CB  ASP A  18      22.029  26.887  28.022  1.00  7.99           C  
ATOM    147  CG  ASP A  18      23.059  26.798  26.898  1.00 12.19           C  
ATOM    148  OD1 ASP A  18      23.785  25.780  26.816  1.00 11.96           O  
ATOM    149  OD2 ASP A  18      23.140  27.744  26.082  1.00 16.91           O  
ATOM    150  N   GLY A  19      23.634  24.211  29.697  1.00  2.60           N  
ATOM    151  CA  GLY A  19      24.723  23.936  30.623  1.00  2.34           C  
ATOM    152  C   GLY A  19      24.302  23.426  31.991  1.00  2.01           C  
ATOM    153  O   GLY A  19      25.138  23.273  32.881  1.00  2.00           O  
ATOM    154  N   TYR A  20      23.017  23.131  32.162  1.00  5.66           N  
ATOM    155  CA  TYR A  20      22.518  22.633  33.447  1.00  6.65           C  
ATOM    156  C   TYR A  20      23.263  21.331  33.795  1.00  7.00           C  
ATOM    157  O   TYR A  20      23.138  20.332  33.087  1.00  5.76           O  
ATOM    158  CB  TYR A  20      20.987  22.420  33.413  1.00  5.03           C  
ATOM    159  CG  TYR A  20      20.441  22.183  34.798  1.00  6.46           C  
ATOM    160  CD1 TYR A  20      20.232  23.249  35.673  1.00  6.79           C  
ATOM    161  CD2 TYR A  20      20.279  20.886  35.289  1.00  4.81           C  
ATOM    162  CE1 TYR A  20      19.895  23.030  37.016  1.00  7.21           C  
ATOM    163  CE2 TYR A  20      19.940  20.651  36.621  1.00  6.67           C  
ATOM    164  CZ  TYR A  20      19.756  21.726  37.483  1.00  7.25           C  
ATOM    165  OH  TYR A  20      19.475  21.492  38.808  1.00  7.82           O  
ATOM    166  N   ARG A  21      24.063  21.383  34.863  1.00  9.59           N  
ATOM    167  CA  ARG A  21      24.898  20.264  35.344  1.00 10.44           C  
ATOM    168  C   ARG A  21      25.934  19.874  34.296  1.00  9.98           C  
ATOM    169  O   ARG A  21      26.307  18.705  34.190  1.00  9.21           O  
ATOM    170  CB  ARG A  21      24.071  19.022  35.737  1.00 13.34           C  
ATOM    171  CG  ARG A  21      23.183  19.181  36.968  1.00 16.97           C  
ATOM    172  CD  ARG A  21      23.984  19.368  38.245  1.00 23.84           C  
ATOM    173  NE  ARG A  21      24.562  18.112  38.724  1.00 29.31           N  
ATOM    174  CZ  ARG A  21      25.441  18.020  39.718  1.00 31.70           C  
ATOM    175  NH1 ARG A  21      25.902  16.832  40.086  1.00 33.33           N  
ATOM    176  NH2 ARG A  21      25.872  19.114  40.335  1.00 33.56           N  
ATOM    177  N   GLY A  22      26.379  20.848  33.507  1.00  7.85           N  
ATOM    178  CA  GLY A  22      27.380  20.572  32.490  1.00  7.91           C  
ATOM    179  C   GLY A  22      26.846  20.081  31.158  1.00  8.09           C  
ATOM    180  O   GLY A  22      27.618  19.897  30.208  1.00 11.06           O  
ATOM    181  N   ALA A  23      25.537  19.873  31.075  1.00  7.28           N  
ATOM    182  CA  ALA A  23      24.902  19.407  29.848  1.00  6.84           C  
ATOM    183  C   ALA A  23      24.455  20.588  28.979  1.00  2.68           C  
ATOM    184  O   ALA A  23      23.615  21.394  29.382  1.00  2.52           O  
ATOM    185  CB  ALA A  23      23.705  18.515  30.189  1.00  6.19           C  
ATOM    186  N   SER A  24      24.979  20.655  27.764  1.00  4.69           N  
ATOM    187  CA  SER A  24      24.637  21.744  26.840  1.00  3.26           C  
ATOM    188  C   SER A  24      23.200  21.699  26.306  1.00  4.21           C  
ATOM    189  O   SER A  24      22.614  20.621  26.131  1.00  2.00           O  
ATOM    190  CB  SER A  24      25.593  21.743  25.654  1.00  2.21           C  
ATOM    191  OG  SER A  24      25.290  20.687  24.749  1.00  6.08           O  
ATOM    192  N   LEU A  25      22.686  22.871  25.935  1.00  2.01           N  
ATOM    193  CA  LEU A  25      21.346  22.989  25.389  1.00  2.44           C  
ATOM    194  C   LEU A  25      21.131  22.018  24.202  1.00  2.31           C  
ATOM    195  O   LEU A  25      20.082  21.358  24.099  1.00  2.88           O  
ATOM    196  CB  LEU A  25      21.113  24.430  24.931  1.00  3.55           C  
ATOM    197  CG  LEU A  25      19.678  24.835  24.611  1.00  7.55           C  
ATOM    198  CD1 LEU A  25      18.822  24.787  25.885  1.00  5.84           C  
ATOM    199  CD2 LEU A  25      19.685  26.239  24.024  1.00  8.27           C  
ATOM    200  N   ALA A  26      22.122  21.913  23.323  1.00  2.00           N  
ATOM    201  CA  ALA A  26      22.014  21.021  22.167  1.00  2.00           C  
ATOM    202  C   ALA A  26      21.773  19.558  22.575  1.00  2.00           C  
ATOM    203  O   ALA A  26      21.116  18.803  21.845  1.00  2.07           O  
ATOM    204  CB  ALA A  26      23.244  21.137  21.302  1.00  2.00           C  
ATOM    205  N   ASN A  27      22.295  19.169  23.740  1.00  2.02           N  
ATOM    206  CA  ASN A  27      22.114  17.803  24.252  1.00  2.01           C  
ATOM    207  C   ASN A  27      20.689  17.599  24.748  1.00  4.49           C  
ATOM    208  O   ASN A  27      20.088  16.535  24.556  1.00  2.01           O  
ATOM    209  CB  ASN A  27      23.137  17.483  25.348  1.00  2.00           C  
ATOM    210  CG  ASN A  27      24.461  16.995  24.775  1.00  3.91           C  
ATOM    211  OD1 ASN A  27      24.504  15.990  24.074  1.00  3.29           O  
ATOM    212  ND2 ASN A  27      25.537  17.714  25.046  1.00  4.62           N  
ATOM    213  N   TRP A  28      20.133  18.637  25.367  1.00  4.52           N  
ATOM    214  CA  TRP A  28      18.762  18.581  25.842  1.00  2.42           C  
ATOM    215  C   TRP A  28      17.813  18.535  24.657  1.00  2.92           C  
ATOM    216  O   TRP A  28      16.736  17.949  24.740  1.00  4.77           O  
ATOM    217  CB  TRP A  28      18.455  19.798  26.703  1.00  3.92           C  
ATOM    218  CG  TRP A  28      19.121  19.729  28.033  1.00  2.03           C  
ATOM    219  CD1 TRP A  28      20.126  20.517  28.476  1.00  2.01           C  
ATOM    220  CD2 TRP A  28      18.796  18.836  29.109  1.00  2.06           C  
ATOM    221  NE1 TRP A  28      20.448  20.188  29.769  1.00  5.24           N  
ATOM    222  CE2 TRP A  28      19.646  19.157  30.183  1.00  2.23           C  
ATOM    223  CE3 TRP A  28      17.861  17.804  29.268  1.00  3.44           C  
ATOM    224  CZ2 TRP A  28      19.593  18.488  31.417  1.00  3.93           C  
ATOM    225  CZ3 TRP A  28      17.803  17.132  30.497  1.00  2.00           C  
ATOM    226  CH2 TRP A  28      18.668  17.481  31.552  1.00  3.06           C  
ATOM    227  N   MET A  29      18.196  19.194  23.568  1.00  2.02           N  
ATOM    228  CA  MET A  29      17.389  19.206  22.355  1.00  2.92           C  
ATOM    229  C   MET A  29      17.394  17.821  21.684  1.00  2.14           C  
ATOM    230  O   MET A  29      16.361  17.338  21.217  1.00  2.08           O  
ATOM    231  CB  MET A  29      17.900  20.278  21.380  1.00  2.02           C  
ATOM    232  CG  MET A  29      17.546  21.704  21.784  1.00  4.22           C  
ATOM    233  SD  MET A  29      15.756  22.009  21.796  1.00  3.18           S  
ATOM    234  CE  MET A  29      15.338  21.536  20.080  1.00  2.19           C  
ATOM    235  N   CYS A  30      18.558  17.180  21.678  1.00  2.00           N  
ATOM    236  CA  CYS A  30      18.708  15.848  21.096  1.00  5.46           C  
ATOM    237  C   CYS A  30      17.855  14.837  21.871  1.00  5.79           C  
ATOM    238  O   CYS A  30      17.166  13.992  21.283  1.00  3.06           O  
ATOM    239  CB  CYS A  30      20.193  15.438  21.101  1.00  5.86           C  
ATOM    240  SG  CYS A  30      20.557  13.837  20.311  1.00  8.33           S  
ATOM    241  N   LEU A  31      17.867  14.972  23.195  1.00  4.26           N  
ATOM    242  CA  LEU A  31      17.096  14.104  24.073  1.00  3.74           C  
ATOM    243  C   LEU A  31      15.583  14.239  23.838  1.00  5.16           C  
ATOM    244  O   LEU A  31      14.898  13.233  23.668  1.00  7.63           O  
ATOM    245  CB  LEU A  31      17.424  14.402  25.550  1.00  4.08           C  
ATOM    246  CG  LEU A  31      16.742  13.510  26.598  1.00  6.10           C  
ATOM    247  CD1 LEU A  31      17.350  12.123  26.540  1.00  4.49           C  
ATOM    248  CD2 LEU A  31      16.857  14.103  28.004  1.00  3.01           C  
ATOM    249  N   ALA A  32      15.054  15.462  23.858  1.00  3.99           N  
ATOM    250  CA  ALA A  32      13.612  15.671  23.647  1.00  3.05           C  
ATOM    251  C   ALA A  32      13.168  15.156  22.294  1.00  2.01           C  
ATOM    252  O   ALA A  32      12.052  14.655  22.142  1.00  2.00           O  
ATOM    253  CB  ALA A  32      13.253  17.141  23.780  1.00  2.00           C  
ATOM    254  N   LYS A  33      14.055  15.304  21.312  1.00  3.42           N  
ATOM    255  CA  LYS A  33      13.816  14.862  19.941  1.00  6.18           C  
ATOM    256  C   LYS A  33      13.578  13.357  19.855  1.00  5.30           C  
ATOM    257  O   LYS A  33      12.566  12.916  19.304  1.00  4.46           O  
ATOM    258  CB  LYS A  33      15.003  15.261  19.053  1.00  5.88           C  
ATOM    259  CG  LYS A  33      15.141  14.492  17.746  1.00 10.64           C  
ATOM    260  CD  LYS A  33      13.968  14.679  16.816  1.00 14.32           C  
ATOM    261  CE  LYS A  33      14.203  13.957  15.481  1.00 15.55           C  
ATOM    262  NZ  LYS A  33      14.296  12.482  15.634  1.00 14.51           N  
ATOM    263  N   TRP A  34      14.507  12.577  20.396  1.00  6.04           N  
ATOM    264  CA  TRP A  34      14.396  11.122  20.362  1.00  6.60           C  
ATOM    265  C   TRP A  34      13.426  10.535  21.382  1.00  6.26           C  
ATOM    266  O   TRP A  34      12.910   9.438  21.181  1.00  7.03           O  
ATOM    267  CB  TRP A  34      15.778  10.477  20.490  1.00  7.59           C  
ATOM    268  CG  TRP A  34      16.649  10.823  19.332  1.00  9.85           C  
ATOM    269  CD1 TRP A  34      17.723  11.668  19.334  1.00  6.29           C  
ATOM    270  CD2 TRP A  34      16.447  10.436  17.969  1.00  9.79           C  
ATOM    271  NE1 TRP A  34      18.185  11.846  18.059  1.00  8.40           N  
ATOM    272  CE2 TRP A  34      17.421  11.101  17.199  1.00  8.53           C  
ATOM    273  CE3 TRP A  34      15.528   9.597  17.321  1.00 12.08           C  
ATOM    274  CZ2 TRP A  34      17.509  10.957  15.815  1.00 12.18           C  
ATOM    275  CZ3 TRP A  34      15.614   9.452  15.936  1.00 15.88           C  
ATOM    276  CH2 TRP A  34      16.599  10.131  15.201  1.00 13.90           C  
ATOM    277  N   GLU A  35      13.146  11.251  22.463  1.00  4.03           N  
ATOM    278  CA  GLU A  35      12.213  10.715  23.440  1.00  4.93           C  
ATOM    279  C   GLU A  35      10.745  10.863  23.023  1.00  5.62           C  
ATOM    280  O   GLU A  35      10.004   9.893  23.066  1.00  4.66           O  
ATOM    281  CB  GLU A  35      12.429  11.334  24.830  1.00  5.74           C  
ATOM    282  CG  GLU A  35      13.758  10.971  25.509  1.00 11.20           C  
ATOM    283  CD  GLU A  35      13.849   9.524  26.022  1.00 11.18           C  
ATOM    284  OE1 GLU A  35      12.864   8.763  25.934  1.00 11.53           O  
ATOM    285  OE2 GLU A  35      14.927   9.153  26.525  1.00 11.35           O  
ATOM    286  N   SER A  36      10.337  12.055  22.586  1.00  5.98           N  
ATOM    287  CA  SER A  36       8.939  12.293  22.218  1.00  5.39           C  
ATOM    288  C   SER A  36       8.695  13.018  20.893  1.00  4.65           C  
ATOM    289  O   SER A  36       7.550  13.143  20.459  1.00  4.56           O  
ATOM    290  CB  SER A  36       8.288  13.135  23.305  1.00  8.44           C  
ATOM    291  OG  SER A  36       8.905  14.416  23.360  1.00  5.75           O  
ATOM    292  N   GLY A  37       9.753  13.506  20.254  1.00  4.85           N  
ATOM    293  CA  GLY A  37       9.570  14.250  19.023  1.00  3.44           C  
ATOM    294  C   GLY A  37       8.941  15.599  19.364  1.00  3.80           C  
ATOM    295  O   GLY A  37       8.068  16.087  18.636  1.00  5.13           O  
ATOM    296  N   TYR A  38       9.359  16.171  20.494  1.00  3.48           N  
ATOM    297  CA  TYR A  38       8.871  17.472  20.993  1.00  4.99           C  
ATOM    298  C   TYR A  38       7.367  17.477  21.274  1.00  5.89           C  
ATOM    299  O   TYR A  38       6.705  18.498  21.088  1.00  4.89           O  
ATOM    300  CB  TYR A  38       9.179  18.616  20.002  1.00  8.95           C  
ATOM    301  CG  TYR A  38      10.595  18.679  19.442  1.00  7.91           C  
ATOM    302  CD1 TYR A  38      10.807  19.075  18.125  1.00  8.11           C  
ATOM    303  CD2 TYR A  38      11.708  18.343  20.219  1.00  5.29           C  
ATOM    304  CE1 TYR A  38      12.090  19.134  17.581  1.00  7.93           C  
ATOM    305  CE2 TYR A  38      13.002  18.402  19.686  1.00  6.41           C  
ATOM    306  CZ  TYR A  38      13.180  18.797  18.360  1.00  7.58           C  
ATOM    307  OH  TYR A  38      14.435  18.832  17.792  1.00  6.27           O  
ATOM    308  N   ASN A  39       6.843  16.363  21.783  1.00  6.95           N  
ATOM    309  CA  ASN A  39       5.413  16.233  22.073  1.00  5.93           C  
ATOM    310  C   ASN A  39       5.180  16.135  23.568  1.00  4.86           C  
ATOM    311  O   ASN A  39       5.550  15.151  24.205  1.00  5.91           O  
ATOM    312  CB  ASN A  39       4.833  14.989  21.382  1.00  6.12           C  
ATOM    313  CG  ASN A  39       3.302  14.912  21.466  1.00  8.08           C  
ATOM    314  OD1 ASN A  39       2.649  15.712  22.149  1.00  9.93           O  
ATOM    315  ND2 ASN A  39       2.727  13.955  20.753  1.00  7.71           N  
ATOM    316  N   THR A  40       4.518  17.141  24.116  1.00  4.63           N  
ATOM    317  CA  THR A  40       4.238  17.190  25.535  1.00  5.55           C  
ATOM    318  C   THR A  40       3.200  16.190  26.018  1.00  5.80           C  
ATOM    319  O   THR A  40       3.106  15.960  27.217  1.00 10.11           O  
ATOM    320  CB  THR A  40       3.776  18.586  25.955  1.00  3.34           C  
ATOM    321  OG1 THR A  40       2.512  18.880  25.343  1.00  4.75           O  
ATOM    322  CG2 THR A  40       4.798  19.622  25.537  1.00  4.17           C  
ATOM    323  N   ARG A  41       2.413  15.603  25.118  1.00  8.30           N  
ATOM    324  CA  ARG A  41       1.396  14.644  25.557  1.00 10.05           C  
ATOM    325  C   ARG A  41       1.752  13.180  25.284  1.00 10.20           C  
ATOM    326  O   ARG A  41       0.928  12.279  25.493  1.00  7.91           O  
ATOM    327  CB  ARG A  41       0.017  14.990  24.982  1.00 11.07           C  
ATOM    328  CG  ARG A  41      -0.072  14.945  23.487  1.00 17.10           C  
ATOM    329  CD  ARG A  41      -1.070  13.893  23.010  1.00 24.83           C  
ATOM    330  NE  ARG A  41      -2.437  14.163  23.450  1.00 31.60           N  
ATOM    331  CZ  ARG A  41      -3.397  13.242  23.517  1.00 35.91           C  
ATOM    332  NH1 ARG A  41      -3.136  11.986  23.166  1.00 37.75           N  
ATOM    333  NH2 ARG A  41      -4.609  13.566  23.964  1.00 36.56           N  
ATOM    334  N   ALA A  42       3.004  12.952  24.894  1.00  8.92           N  
ATOM    335  CA  ALA A  42       3.515  11.620  24.591  1.00  8.41           C  
ATOM    336  C   ALA A  42       3.605  10.724  25.826  1.00  9.45           C  
ATOM    337  O   ALA A  42       4.170  11.117  26.861  1.00  6.00           O  
ATOM    338  CB  ALA A  42       4.867  11.735  23.947  1.00  4.31           C  
ATOM    339  N   THR A  43       3.082   9.507  25.698  1.00 10.52           N  
ATOM    340  CA  THR A  43       3.111   8.524  26.780  1.00 11.76           C  
ATOM    341  C   THR A  43       3.540   7.149  26.281  1.00 11.62           C  
ATOM    342  O   THR A  43       3.181   6.751  25.161  1.00 12.65           O  
ATOM    343  CB  THR A  43       1.729   8.348  27.423  1.00 13.05           C  
ATOM    344  OG1 THR A  43       0.734   8.275  26.398  1.00 16.62           O  
ATOM    345  CG2 THR A  43       1.409   9.492  28.366  1.00 12.98           C  
ATOM    346  N   ASN A  44       4.365   6.454  27.057  1.00  9.45           N  
ATOM    347  CA  ASN A  44       4.758   5.102  26.672  1.00 12.63           C  
ATOM    348  C   ASN A  44       4.608   4.137  27.840  1.00 11.07           C  
ATOM    349  O   ASN A  44       5.354   4.224  28.816  1.00  8.81           O  
ATOM    350  CB  ASN A  44       6.190   5.039  26.154  1.00 17.27           C  
ATOM    351  CG  ASN A  44       6.615   3.609  25.780  1.00 21.55           C  
ATOM    352  OD1 ASN A  44       6.403   3.161  24.648  1.00 25.24           O  
ATOM    353  ND2 ASN A  44       7.195   2.888  26.738  1.00 23.48           N  
ATOM    354  N   TYR A  45       3.631   3.241  27.752  1.00 10.03           N  
ATOM    355  CA  TYR A  45       3.424   2.254  28.802  1.00  9.56           C  
ATOM    356  C   TYR A  45       4.440   1.143  28.591  1.00  9.36           C  
ATOM    357  O   TYR A  45       4.574   0.630  27.483  1.00 10.13           O  
ATOM    358  CB  TYR A  45       2.007   1.673  28.756  1.00 10.33           C  
ATOM    359  CG  TYR A  45       1.786   0.588  29.791  1.00 10.56           C  
ATOM    360  CD1 TYR A  45       1.520  -0.734  29.413  1.00 12.07           C  
ATOM    361  CD2 TYR A  45       1.866   0.879  31.143  1.00 10.69           C  
ATOM    362  CE1 TYR A  45       1.336  -1.734  30.377  1.00 15.30           C  
ATOM    363  CE2 TYR A  45       1.686  -0.100  32.106  1.00 13.66           C  
ATOM    364  CZ  TYR A  45       1.420  -1.400  31.723  1.00 14.73           C  
ATOM    365  OH  TYR A  45       1.214  -2.338  32.702  1.00 21.08           O  
ATOM    366  N   ASN A  46       5.157   0.785  29.656  1.00  9.21           N  
ATOM    367  CA  ASN A  46       6.175  -0.268  29.609  1.00 10.72           C  
ATOM    368  C   ASN A  46       5.550  -1.510  30.205  1.00 11.22           C  
ATOM    369  O   ASN A  46       5.489  -1.659  31.428  1.00  8.19           O  
ATOM    370  CB  ASN A  46       7.424   0.131  30.410  1.00 10.36           C  
ATOM    371  CG  ASN A  46       8.088   1.389  29.867  1.00 15.81           C  
ATOM    372  OD1 ASN A  46       8.761   1.361  28.823  1.00 17.16           O  
ATOM    373  ND2 ASN A  46       7.868   2.511  30.547  1.00 11.76           N  
ATOM    374  N   ALA A  47       5.100  -2.404  29.334  1.00 10.97           N  
ATOM    375  CA  ALA A  47       4.431  -3.623  29.765  1.00 12.72           C  
ATOM    376  C   ALA A  47       5.275  -4.508  30.674  1.00 13.10           C  
ATOM    377  O   ALA A  47       4.764  -5.070  31.638  1.00 13.11           O  
ATOM    378  CB  ALA A  47       3.943  -4.414  28.551  1.00 15.23           C  
ATOM    379  N   GLY A  48       6.570  -4.585  30.390  1.00 13.67           N  
ATOM    380  CA  GLY A  48       7.461  -5.415  31.177  1.00 13.09           C  
ATOM    381  C   GLY A  48       7.511  -5.155  32.669  1.00 14.98           C  
ATOM    382  O   GLY A  48       7.741  -6.080  33.453  1.00 14.19           O  
ATOM    383  N   ASP A  49       7.328  -3.901  33.071  1.00 14.56           N  
ATOM    384  CA  ASP A  49       7.382  -3.569  34.486  1.00 14.05           C  
ATOM    385  C   ASP A  49       6.238  -2.699  35.005  1.00 13.43           C  
ATOM    386  O   ASP A  49       6.320  -2.174  36.103  1.00 11.65           O  
ATOM    387  CB  ASP A  49       8.757  -2.964  34.853  1.00 16.23           C  
ATOM    388  CG  ASP A  49       8.907  -1.502  34.453  1.00 15.56           C  
ATOM    389  OD1 ASP A  49       8.342  -1.085  33.435  1.00 16.50           O  
ATOM    390  OD2 ASP A  49       9.610  -0.759  35.173  1.00 21.77           O  
ATOM    391  N   ARG A  50       5.172  -2.559  34.217  1.00 13.58           N  
ATOM    392  CA  ARG A  50       3.993  -1.768  34.601  1.00 13.72           C  
ATOM    393  C   ARG A  50       4.205  -0.257  34.881  1.00 12.41           C  
ATOM    394  O   ARG A  50       3.370   0.379  35.525  1.00 14.83           O  
ATOM    395  CB  ARG A  50       3.279  -2.442  35.785  1.00 16.05           C  
ATOM    396  CG  ARG A  50       3.141  -3.951  35.621  1.00 20.15           C  
ATOM    397  CD  ARG A  50       2.015  -4.575  36.437  1.00 21.97           C  
ATOM    398  NE  ARG A  50       1.382  -5.639  35.645  1.00 30.59           N  
ATOM    399  CZ  ARG A  50       0.439  -6.476  36.082  1.00 31.49           C  
ATOM    400  NH1 ARG A  50      -0.055  -7.396  35.257  1.00 27.61           N  
ATOM    401  NH2 ARG A  50      -0.007  -6.405  37.337  1.00 33.06           N  
ATOM    402  N   SER A  51       5.278   0.324  34.349  1.00 11.38           N  
ATOM    403  CA  SER A  51       5.574   1.751  34.549  1.00  7.50           C  
ATOM    404  C   SER A  51       5.230   2.530  33.271  1.00  4.90           C  
ATOM    405  O   SER A  51       5.047   1.929  32.226  1.00  2.43           O  
ATOM    406  CB  SER A  51       7.060   1.935  34.892  1.00  2.10           C  
ATOM    407  OG  SER A  51       7.892   1.666  33.765  1.00  3.07           O  
ATOM    408  N   THR A  52       5.159   3.856  33.338  1.00  4.49           N  
ATOM    409  CA  THR A  52       4.843   4.646  32.137  1.00  5.80           C  
ATOM    410  C   THR A  52       5.786   5.836  32.013  1.00  3.60           C  
ATOM    411  O   THR A  52       6.243   6.385  33.015  1.00  6.79           O  
ATOM    412  CB  THR A  52       3.366   5.168  32.147  1.00  6.08           C  
ATOM    413  OG1 THR A  52       2.453   4.070  32.316  1.00  8.57           O  
ATOM    414  CG2 THR A  52       3.024   5.873  30.841  1.00  7.53           C  
ATOM    415  N   ASP A  53       6.132   6.181  30.784  1.00  2.00           N  
ATOM    416  CA  ASP A  53       7.004   7.316  30.512  1.00  2.39           C  
ATOM    417  C   ASP A  53       6.093   8.461  30.100  1.00  2.85           C  
ATOM    418  O   ASP A  53       5.280   8.306  29.186  1.00  2.37           O  
ATOM    419  CB  ASP A  53       7.952   6.967  29.376  1.00  6.08           C  
ATOM    420  CG  ASP A  53       8.822   5.777  29.693  1.00  5.81           C  
ATOM    421  OD1 ASP A  53       9.260   5.671  30.847  1.00 11.81           O  
ATOM    422  OD2 ASP A  53       9.076   4.954  28.796  1.00  8.81           O  
ATOM    423  N   TYR A  54       6.217   9.605  30.764  1.00  3.07           N  
ATOM    424  CA  TYR A  54       5.348  10.744  30.473  1.00  3.11           C  
ATOM    425  C   TYR A  54       6.015  12.026  29.977  1.00  4.52           C  
ATOM    426  O   TYR A  54       7.063  12.430  30.493  1.00  2.01           O  
ATOM    427  CB  TYR A  54       4.567  11.136  31.723  1.00  3.15           C  
ATOM    428  CG  TYR A  54       3.626  10.102  32.297  1.00  3.79           C  
ATOM    429  CD1 TYR A  54       2.270  10.102  31.945  1.00  3.26           C  
ATOM    430  CD2 TYR A  54       4.062   9.199  33.278  1.00  2.05           C  
ATOM    431  CE1 TYR A  54       1.368   9.242  32.560  1.00  2.67           C  
ATOM    432  CE2 TYR A  54       3.170   8.330  33.901  1.00  2.02           C  
ATOM    433  CZ  TYR A  54       1.825   8.359  33.538  1.00  2.32           C  
ATOM    434  OH  TYR A  54       0.929   7.517  34.139  1.00  2.01           O  
ATOM    435  N   GLY A  55       5.383  12.654  28.982  1.00  4.02           N  
ATOM    436  CA  GLY A  55       5.835  13.938  28.472  1.00  5.11           C  
ATOM    437  C   GLY A  55       6.976  14.097  27.503  1.00  3.19           C  
ATOM    438  O   GLY A  55       7.537  13.127  27.000  1.00  7.45           O  
ATOM    439  N   ILE A  56       7.338  15.354  27.264  1.00  3.05           N  
ATOM    440  CA  ILE A  56       8.399  15.696  26.308  1.00  4.37           C  
ATOM    441  C   ILE A  56       9.758  15.020  26.565  1.00  2.42           C  
ATOM    442  O   ILE A  56      10.490  14.730  25.614  1.00  4.88           O  
ATOM    443  CB  ILE A  56       8.531  17.243  26.171  1.00  2.02           C  
ATOM    444  CG1 ILE A  56       9.374  17.614  24.961  1.00  6.87           C  
ATOM    445  CG2 ILE A  56       9.064  17.854  27.441  1.00  2.00           C  
ATOM    446  CD1 ILE A  56       9.221  19.084  24.535  1.00  4.41           C  
ATOM    447  N   PHE A  57      10.069  14.750  27.836  1.00  5.72           N  
ATOM    448  CA  PHE A  57      11.327  14.107  28.246  1.00  2.02           C  
ATOM    449  C   PHE A  57      11.171  12.635  28.616  1.00  2.01           C  
ATOM    450  O   PHE A  57      12.144  11.997  29.001  1.00  2.05           O  
ATOM    451  CB  PHE A  57      11.936  14.838  29.440  1.00  2.01           C  
ATOM    452  CG  PHE A  57      12.468  16.190  29.114  1.00  5.78           C  
ATOM    453  CD1 PHE A  57      12.060  17.303  29.843  1.00  6.56           C  
ATOM    454  CD2 PHE A  57      13.377  16.362  28.071  1.00  4.31           C  
ATOM    455  CE1 PHE A  57      12.549  18.575  29.538  1.00  6.70           C  
ATOM    456  CE2 PHE A  57      13.871  17.628  27.758  1.00  6.32           C  
ATOM    457  CZ  PHE A  57      13.453  18.738  28.499  1.00  4.57           C  
ATOM    458  N   GLN A  58       9.948  12.118  28.512  1.00  3.20           N  
ATOM    459  CA  GLN A  58       9.622  10.723  28.836  1.00  4.17           C  
ATOM    460  C   GLN A  58      10.151  10.312  30.203  1.00  2.11           C  
ATOM    461  O   GLN A  58      11.006   9.432  30.329  1.00  6.13           O  
ATOM    462  CB  GLN A  58      10.123   9.766  27.739  1.00  5.81           C  
ATOM    463  CG  GLN A  58       9.368   9.870  26.416  1.00  5.07           C  
ATOM    464  CD  GLN A  58       7.961   9.314  26.487  1.00  6.25           C  
ATOM    465  OE1 GLN A  58       7.741   8.125  26.269  1.00  7.11           O  
ATOM    466  NE2 GLN A  58       6.999  10.174  26.758  1.00  9.05           N  
ATOM    467  N   ILE A  59       9.610  10.950  31.227  1.00  3.04           N  
ATOM    468  CA  ILE A  59      10.002  10.710  32.598  1.00  2.80           C  
ATOM    469  C   ILE A  59       9.187   9.530  33.167  1.00  3.65           C  
ATOM    470  O   ILE A  59       7.966   9.502  33.095  1.00  2.06           O  
ATOM    471  CB  ILE A  59       9.911  12.059  33.381  1.00  4.47           C  
ATOM    472  CG1 ILE A  59      11.006  13.003  32.850  1.00  5.98           C  
ATOM    473  CG2 ILE A  59      10.093  11.886  34.861  1.00  4.74           C  
ATOM    474  CD1 ILE A  59      11.097  14.347  33.542  1.00  6.63           C  
ATOM    475  N   ASN A  60       9.902   8.546  33.704  1.00  5.50           N  
ATOM    476  CA  ASN A  60       9.324   7.315  34.239  1.00  3.70           C  
ATOM    477  C   ASN A  60       8.611   7.432  35.588  1.00  3.68           C  
ATOM    478  O   ASN A  60       9.145   7.995  36.551  1.00  5.36           O  
ATOM    479  CB  ASN A  60      10.427   6.251  34.295  1.00  8.98           C  
ATOM    480  CG  ASN A  60       9.892   4.845  34.528  1.00  9.43           C  
ATOM    481  OD1 ASN A  60       9.718   4.433  35.667  1.00  8.65           O  
ATOM    482  ND2 ASN A  60       9.687   4.087  33.448  1.00  9.22           N  
ATOM    483  N   SER A  61       7.424   6.832  35.662  1.00  5.04           N  
ATOM    484  CA  SER A  61       6.582   6.850  36.857  1.00  3.59           C  
ATOM    485  C   SER A  61       7.050   5.991  38.030  1.00  7.22           C  
ATOM    486  O   SER A  61       6.438   6.028  39.109  1.00  5.70           O  
ATOM    487  CB  SER A  61       5.155   6.439  36.498  1.00  2.58           C  
ATOM    488  OG  SER A  61       5.137   5.128  35.945  1.00  2.00           O  
ATOM    489  N   ARG A  62       8.126   5.231  37.856  1.00  8.88           N  
ATOM    490  CA  ARG A  62       8.597   4.380  38.946  1.00 10.83           C  
ATOM    491  C   ARG A  62       9.461   5.113  39.947  1.00 11.77           C  
ATOM    492  O   ARG A  62       9.452   4.782  41.139  1.00 12.63           O  
ATOM    493  CB  ARG A  62       9.356   3.168  38.401  1.00 13.69           C  
ATOM    494  CG  ARG A  62       9.813   2.180  39.472  1.00 15.38           C  
ATOM    495  CD  ARG A  62      10.072   0.825  38.854  1.00 18.90           C  
ATOM    496  NE  ARG A  62       8.886   0.328  38.148  1.00 23.56           N  
ATOM    497  CZ  ARG A  62       7.911  -0.368  38.723  1.00 22.20           C  
ATOM    498  NH1 ARG A  62       6.874  -0.766  38.016  1.00 18.79           N  
ATOM    499  NH2 ARG A  62       7.984  -0.691  40.005  1.00 24.23           N  
ATOM    500  N   TYR A  63      10.190   6.122  39.474  1.00 12.49           N  
ATOM    501  CA  TYR A  63      11.089   6.875  40.352  1.00 12.82           C  
ATOM    502  C   TYR A  63      10.870   8.371  40.426  1.00 10.31           C  
ATOM    503  O   TYR A  63      11.159   8.993  41.452  1.00 12.58           O  
ATOM    504  CB  TYR A  63      12.560   6.664  39.946  1.00 18.18           C  
ATOM    505  CG  TYR A  63      12.888   5.324  39.328  1.00 23.16           C  
ATOM    506  CD1 TYR A  63      12.690   5.105  37.965  1.00 26.02           C  
ATOM    507  CD2 TYR A  63      13.410   4.279  40.100  1.00 24.88           C  
ATOM    508  CE1 TYR A  63      13.001   3.887  37.382  1.00 28.45           C  
ATOM    509  CE2 TYR A  63      13.727   3.049  39.523  1.00 26.85           C  
ATOM    510  CZ  TYR A  63      13.518   2.862  38.161  1.00 29.42           C  
ATOM    511  OH  TYR A  63      13.813   1.659  37.560  1.00 33.64           O  
ATOM    512  N   TRP A  64      10.357   8.959  39.351  1.00 11.06           N  
ATOM    513  CA  TRP A  64      10.208  10.409  39.301  1.00  8.75           C  
ATOM    514  C   TRP A  64       8.848  11.051  39.567  1.00  8.16           C  
ATOM    515  O   TRP A  64       8.763  12.040  40.296  1.00  9.38           O  
ATOM    516  CB  TRP A  64      10.809  10.903  37.991  1.00  5.93           C  
ATOM    517  CG  TRP A  64      12.123  10.231  37.707  1.00  3.84           C  
ATOM    518  CD1 TRP A  64      12.365   9.266  36.770  1.00  5.49           C  
ATOM    519  CD2 TRP A  64      13.360  10.424  38.413  1.00  4.24           C  
ATOM    520  NE1 TRP A  64      13.668   8.840  36.855  1.00  6.10           N  
ATOM    521  CE2 TRP A  64      14.302   9.533  37.854  1.00  5.76           C  
ATOM    522  CE3 TRP A  64      13.762  11.263  39.461  1.00  2.37           C  
ATOM    523  CZ2 TRP A  64      15.627   9.457  38.312  1.00  2.00           C  
ATOM    524  CZ3 TRP A  64      15.081  11.184  39.910  1.00  3.35           C  
ATOM    525  CH2 TRP A  64      15.991  10.290  39.336  1.00  2.00           C  
ATOM    526  N   CYS A  65       7.782  10.494  39.015  1.00  8.23           N  
ATOM    527  CA  CYS A  65       6.475  11.085  39.237  1.00  9.12           C  
ATOM    528  C   CYS A  65       5.479  10.023  39.667  1.00  8.48           C  
ATOM    529  O   CYS A  65       5.687   8.835  39.414  1.00  8.05           O  
ATOM    530  CB  CYS A  65       5.989  11.805  37.962  1.00  6.15           C  
ATOM    531  SG  CYS A  65       5.611  10.739  36.530  1.00  5.66           S  
ATOM    532  N   ASN A  66       4.398  10.454  40.306  1.00  5.28           N  
ATOM    533  CA  ASN A  66       3.376   9.533  40.773  1.00  7.94           C  
ATOM    534  C   ASN A  66       2.106   9.509  39.907  1.00 10.70           C  
ATOM    535  O   ASN A  66       1.513  10.564  39.638  1.00 11.11           O  
ATOM    536  CB  ASN A  66       2.991   9.887  42.214  1.00  7.72           C  
ATOM    537  CG  ASN A  66       1.929   8.968  42.774  1.00  8.71           C  
ATOM    538  OD1 ASN A  66       2.011   7.746  42.624  1.00 10.49           O  
ATOM    539  ND2 ASN A  66       0.911   9.544  43.387  1.00  6.25           N  
ATOM    540  N   ASP A  67       1.713   8.320  39.444  1.00  7.88           N  
ATOM    541  CA  ASP A  67       0.478   8.165  38.679  1.00  4.60           C  
ATOM    542  C   ASP A  67      -0.461   7.230  39.452  1.00  5.97           C  
ATOM    543  O   ASP A  67      -1.579   6.940  39.027  1.00  7.10           O  
ATOM    544  CB  ASP A  67       0.723   7.673  37.241  1.00  4.56           C  
ATOM    545  CG  ASP A  67       1.312   6.260  37.158  1.00  3.96           C  
ATOM    546  OD1 ASP A  67       1.570   5.578  38.187  1.00  5.61           O  
ATOM    547  OD2 ASP A  67       1.518   5.834  36.008  1.00  3.52           O  
ATOM    548  N   GLY A  68       0.016   6.761  40.597  1.00  6.42           N  
ATOM    549  CA  GLY A  68      -0.777   5.895  41.449  1.00  6.39           C  
ATOM    550  C   GLY A  68      -0.912   4.431  41.079  1.00  7.24           C  
ATOM    551  O   GLY A  68      -1.272   3.640  41.936  1.00  8.49           O  
ATOM    552  N   LYS A  69      -0.609   4.057  39.839  1.00  9.68           N  
ATOM    553  CA  LYS A  69      -0.739   2.662  39.410  1.00  8.59           C  
ATOM    554  C   LYS A  69       0.566   1.907  39.176  1.00  9.02           C  
ATOM    555  O   LYS A  69       0.542   0.783  38.686  1.00 11.80           O  
ATOM    556  CB  LYS A  69      -1.613   2.570  38.151  1.00  7.36           C  
ATOM    557  CG  LYS A  69      -1.128   3.420  36.991  1.00 10.33           C  
ATOM    558  CD  LYS A  69      -2.021   3.215  35.783  1.00 12.86           C  
ATOM    559  CE  LYS A  69      -1.665   4.156  34.653  1.00 17.39           C  
ATOM    560  NZ  LYS A  69      -0.247   4.016  34.214  1.00 23.83           N  
ATOM    561  N   THR A  70       1.704   2.514  39.488  1.00  7.76           N  
ATOM    562  CA  THR A  70       2.981   1.831  39.282  1.00  9.26           C  
ATOM    563  C   THR A  70       3.408   1.142  40.589  1.00  8.96           C  
ATOM    564  O   THR A  70       3.421   1.767  41.650  1.00  9.72           O  
ATOM    565  CB  THR A  70       4.083   2.814  38.764  1.00  8.70           C  
ATOM    566  OG1 THR A  70       3.661   3.407  37.519  1.00  3.91           O  
ATOM    567  CG2 THR A  70       5.430   2.082  38.565  1.00  2.01           C  
ATOM    568  N   PRO A  71       3.669  -0.175  40.542  1.00  9.90           N  
ATOM    569  CA  PRO A  71       4.081  -0.942  41.722  1.00 12.01           C  
ATOM    570  C   PRO A  71       5.396  -0.445  42.310  1.00 13.56           C  
ATOM    571  O   PRO A  71       6.291  -0.066  41.571  1.00 14.12           O  
ATOM    572  CB  PRO A  71       4.230  -2.360  41.166  1.00 12.06           C  
ATOM    573  CG  PRO A  71       3.259  -2.401  40.055  1.00  9.44           C  
ATOM    574  CD  PRO A  71       3.507  -1.073  39.384  1.00 11.31           C  
ATOM    575  N   GLY A  72       5.485  -0.418  43.640  1.00 16.85           N  
ATOM    576  CA  GLY A  72       6.690   0.028  44.332  1.00 18.81           C  
ATOM    577  C   GLY A  72       7.392   1.263  43.776  1.00 19.93           C  
ATOM    578  O   GLY A  72       8.624   1.292  43.668  1.00 20.60           O  
ATOM    579  N   ALA A  73       6.622   2.312  43.508  1.00 18.74           N  
ATOM    580  CA  ALA A  73       7.161   3.542  42.955  1.00 16.38           C  
ATOM    581  C   ALA A  73       7.536   4.607  43.970  1.00 15.80           C  
ATOM    582  O   ALA A  73       7.065   4.611  45.119  1.00 12.92           O  
ATOM    583  CB  ALA A  73       6.179   4.129  41.955  1.00 17.31           C  
ATOM    584  N   VAL A  74       8.413   5.501  43.529  1.00 12.58           N  
ATOM    585  CA  VAL A  74       8.837   6.634  44.331  1.00 12.67           C  
ATOM    586  C   VAL A  74       8.412   7.835  43.499  1.00 10.59           C  
ATOM    587  O   VAL A  74       8.094   7.702  42.314  1.00 13.22           O  
ATOM    588  CB  VAL A  74      10.387   6.672  44.641  1.00 12.20           C  
ATOM    589  CG1 VAL A  74      10.684   5.953  45.948  1.00 10.94           C  
ATOM    590  CG2 VAL A  74      11.202   6.039  43.523  1.00 10.07           C  
ATOM    591  N   ASN A  75       8.331   8.980  44.145  1.00 10.47           N  
ATOM    592  CA  ASN A  75       7.934  10.215  43.500  1.00  9.57           C  
ATOM    593  C   ASN A  75       9.033  11.229  43.842  1.00  9.02           C  
ATOM    594  O   ASN A  75       8.807  12.160  44.610  1.00 11.38           O  
ATOM    595  CB  ASN A  75       6.576  10.658  44.073  1.00  6.04           C  
ATOM    596  CG  ASN A  75       6.017  11.901  43.400  1.00  2.50           C  
ATOM    597  OD1 ASN A  75       6.583  12.410  42.436  1.00  3.92           O  
ATOM    598  ND2 ASN A  75       4.888  12.384  43.900  1.00  2.00           N  
ATOM    599  N   ALA A  76      10.232  11.016  43.310  1.00  8.56           N  
ATOM    600  CA  ALA A  76      11.351  11.915  43.587  1.00  9.06           C  
ATOM    601  C   ALA A  76      11.098  13.373  43.206  1.00  7.98           C  
ATOM    602  O   ALA A  76      11.498  14.279  43.938  1.00  9.47           O  
ATOM    603  CB  ALA A  76      12.632  11.405  42.940  1.00 11.02           C  
ATOM    604  N   CYS A  77      10.406  13.615  42.100  1.00  4.68           N  
ATOM    605  CA  CYS A  77      10.132  14.994  41.698  1.00  6.56           C  
ATOM    606  C   CYS A  77       8.975  15.627  42.457  1.00  9.81           C  
ATOM    607  O   CYS A  77       8.705  16.817  42.294  1.00 11.60           O  
ATOM    608  CB  CYS A  77       9.833  15.088  40.203  1.00  7.85           C  
ATOM    609  SG  CYS A  77      11.238  14.711  39.122  1.00  6.77           S  
ATOM    610  N   HIS A  78       8.272  14.824  43.250  1.00  9.57           N  
ATOM    611  CA  HIS A  78       7.125  15.283  44.021  1.00 12.26           C  
ATOM    612  C   HIS A  78       6.055  15.959  43.156  1.00 10.90           C  
ATOM    613  O   HIS A  78       5.536  17.036  43.484  1.00 12.18           O  
ATOM    614  CB  HIS A  78       7.574  16.167  45.183  1.00 18.18           C  
ATOM    615  CG  HIS A  78       8.465  15.456  46.148  1.00 26.33           C  
ATOM    616  ND1 HIS A  78       9.833  15.631  46.166  1.00 31.15           N  
ATOM    617  CD2 HIS A  78       8.195  14.513  47.081  1.00 32.17           C  
ATOM    618  CE1 HIS A  78      10.368  14.823  47.063  1.00 34.71           C  
ATOM    619  NE2 HIS A  78       9.395  14.134  47.633  1.00 36.88           N  
ATOM    620  N   LEU A  79       5.680  15.266  42.085  1.00  8.84           N  
ATOM    621  CA  LEU A  79       4.677  15.742  41.143  1.00  8.67           C  
ATOM    622  C   LEU A  79       3.795  14.595  40.684  1.00  8.23           C  
ATOM    623  O   LEU A  79       4.208  13.433  40.675  1.00  8.15           O  
ATOM    624  CB  LEU A  79       5.332  16.325  39.873  1.00  8.88           C  
ATOM    625  CG  LEU A  79       5.938  17.728  39.801  1.00  7.99           C  
ATOM    626  CD1 LEU A  79       6.649  17.850  38.492  1.00  5.52           C  
ATOM    627  CD2 LEU A  79       4.866  18.818  39.950  1.00  5.85           C  
ATOM    628  N   SER A  80       2.573  14.940  40.309  1.00  6.75           N  
ATOM    629  CA  SER A  80       1.632  13.980  39.767  1.00  4.71           C  
ATOM    630  C   SER A  80       2.160  13.824  38.349  1.00  6.07           C  
ATOM    631  O   SER A  80       2.622  14.817  37.758  1.00  8.41           O  
ATOM    632  CB  SER A  80       0.228  14.612  39.735  1.00  6.07           C  
ATOM    633  OG  SER A  80      -0.675  13.909  38.893  1.00  2.00           O  
ATOM    634  N   CYS A  81       2.097  12.624  37.776  1.00  3.93           N  
ATOM    635  CA  CYS A  81       2.581  12.456  36.413  1.00  2.52           C  
ATOM    636  C   CYS A  81       1.749  13.286  35.417  1.00  4.07           C  
ATOM    637  O   CYS A  81       2.209  13.608  34.308  1.00  2.09           O  
ATOM    638  CB  CYS A  81       2.604  10.986  36.011  1.00  5.20           C  
ATOM    639  SG  CYS A  81       3.789   9.939  36.922  1.00  7.38           S  
ATOM    640  N   SER A  82       0.534  13.644  35.829  1.00  2.82           N  
ATOM    641  CA  SER A  82      -0.359  14.462  35.006  1.00  5.84           C  
ATOM    642  C   SER A  82       0.327  15.800  34.697  1.00  4.22           C  
ATOM    643  O   SER A  82       0.185  16.357  33.608  1.00  4.54           O  
ATOM    644  CB  SER A  82      -1.679  14.710  35.753  1.00  5.93           C  
ATOM    645  OG  SER A  82      -2.613  15.426  34.956  1.00  9.92           O  
ATOM    646  N   ALA A  83       1.126  16.274  35.651  1.00  6.17           N  
ATOM    647  CA  ALA A  83       1.848  17.537  35.511  1.00  4.09           C  
ATOM    648  C   ALA A  83       2.783  17.514  34.312  1.00  3.88           C  
ATOM    649  O   ALA A  83       3.017  18.538  33.668  1.00  2.42           O  
ATOM    650  CB  ALA A  83       2.632  17.843  36.793  1.00  2.03           C  
ATOM    651  N   LEU A  84       3.237  16.316  33.967  1.00  4.64           N  
ATOM    652  CA  LEU A  84       4.167  16.124  32.878  1.00  4.36           C  
ATOM    653  C   LEU A  84       3.525  15.970  31.513  1.00  4.64           C  
ATOM    654  O   LEU A  84       4.179  15.518  30.575  1.00  4.92           O  
ATOM    655  CB  LEU A  84       5.065  14.920  33.173  1.00  3.96           C  
ATOM    656  CG  LEU A  84       5.864  14.945  34.468  1.00  2.02           C  
ATOM    657  CD1 LEU A  84       6.653  13.668  34.564  1.00  4.21           C  
ATOM    658  CD2 LEU A  84       6.783  16.139  34.516  1.00  4.81           C  
ATOM    659  N   LEU A  85       2.246  16.318  31.407  1.00  4.11           N  
ATOM    660  CA  LEU A  85       1.536  16.238  30.136  1.00  2.92           C  
ATOM    661  C   LEU A  85       0.952  17.593  29.718  1.00  3.09           C  
ATOM    662  O   LEU A  85       0.235  17.679  28.732  1.00  2.12           O  
ATOM    663  CB  LEU A  85       0.409  15.209  30.225  1.00  4.71           C  
ATOM    664  CG  LEU A  85       0.759  13.754  30.539  1.00  8.50           C  
ATOM    665  CD1 LEU A  85      -0.535  12.955  30.758  1.00  8.59           C  
ATOM    666  CD2 LEU A  85       1.588  13.171  29.397  1.00  7.22           C  
ATOM    667  N   GLN A  86       1.231  18.640  30.486  1.00  5.42           N  
ATOM    668  CA  GLN A  86       0.712  19.981  30.186  1.00  6.91           C  
ATOM    669  C   GLN A  86       1.443  20.611  29.010  1.00  6.19           C  
ATOM    670  O   GLN A  86       2.605  20.266  28.754  1.00  5.94           O  
ATOM    671  CB  GLN A  86       0.931  20.906  31.377  1.00  9.50           C  
ATOM    672  CG  GLN A  86       0.301  20.485  32.662  1.00 10.99           C  
ATOM    673  CD  GLN A  86       0.553  21.504  33.744  1.00 11.75           C  
ATOM    674  OE1 GLN A  86      -0.156  22.500  33.848  1.00 12.11           O  
ATOM    675  NE2 GLN A  86       1.587  21.280  34.536  1.00 10.53           N  
ATOM    676  N   ASP A  87       0.811  21.579  28.338  1.00  4.61           N  
ATOM    677  CA  ASP A  87       1.476  22.257  27.212  1.00  5.03           C  
ATOM    678  C   ASP A  87       2.640  23.102  27.745  1.00  6.64           C  
ATOM    679  O   ASP A  87       3.610  23.365  27.027  1.00  7.92           O  
ATOM    680  CB  ASP A  87       0.513  23.166  26.432  1.00  7.72           C  
ATOM    681  CG  ASP A  87      -0.266  22.426  25.340  1.00  8.97           C  
ATOM    682  OD1 ASP A  87      -0.140  21.189  25.220  1.00  8.65           O  
ATOM    683  OD2 ASP A  87      -1.016  23.090  24.597  1.00  9.88           O  
ATOM    684  N   ASN A  88       2.522  23.550  28.993  1.00  6.69           N  
ATOM    685  CA  ASN A  88       3.551  24.361  29.646  1.00  8.81           C  
ATOM    686  C   ASN A  88       4.555  23.371  30.222  1.00  9.75           C  
ATOM    687  O   ASN A  88       4.228  22.614  31.141  1.00  8.98           O  
ATOM    688  CB  ASN A  88       2.925  25.194  30.773  1.00 12.39           C  
ATOM    689  CG  ASN A  88       3.940  26.068  31.503  1.00 16.00           C  
ATOM    690  OD1 ASN A  88       5.011  25.608  31.906  1.00 14.29           O  
ATOM    691  ND2 ASN A  88       3.589  27.332  31.702  1.00 20.06           N  
ATOM    692  N   ILE A  89       5.784  23.405  29.720  1.00  9.62           N  
ATOM    693  CA  ILE A  89       6.805  22.454  30.149  1.00  6.91           C  
ATOM    694  C   ILE A  89       7.646  22.833  31.360  1.00  5.29           C  
ATOM    695  O   ILE A  89       8.650  22.161  31.657  1.00  4.44           O  
ATOM    696  CB  ILE A  89       7.737  22.090  28.962  1.00  9.89           C  
ATOM    697  CG1 ILE A  89       8.510  23.332  28.491  1.00  8.20           C  
ATOM    698  CG2 ILE A  89       6.917  21.522  27.816  1.00  8.08           C  
ATOM    699  CD1 ILE A  89       9.544  23.048  27.443  1.00  7.88           C  
ATOM    700  N   ALA A  90       7.219  23.848  32.108  1.00  3.58           N  
ATOM    701  CA  ALA A  90       7.974  24.266  33.295  1.00  3.25           C  
ATOM    702  C   ALA A  90       8.156  23.150  34.338  1.00  3.43           C  
ATOM    703  O   ALA A  90       9.243  23.007  34.907  1.00  2.30           O  
ATOM    704  CB  ALA A  90       7.325  25.490  33.945  1.00  3.24           C  
ATOM    705  N   ASP A  91       7.110  22.363  34.594  1.00  4.31           N  
ATOM    706  CA  ASP A  91       7.217  21.286  35.596  1.00  7.31           C  
ATOM    707  C   ASP A  91       8.127  20.158  35.116  1.00  6.81           C  
ATOM    708  O   ASP A  91       8.993  19.689  35.863  1.00  8.69           O  
ATOM    709  CB  ASP A  91       5.841  20.727  35.984  1.00  7.85           C  
ATOM    710  CG  ASP A  91       5.007  21.721  36.778  1.00 13.26           C  
ATOM    711  OD1 ASP A  91       3.841  21.938  36.408  1.00 14.94           O  
ATOM    712  OD2 ASP A  91       5.503  22.274  37.782  1.00 14.99           O  
ATOM    713  N   ALA A  92       7.926  19.727  33.874  1.00  5.15           N  
ATOM    714  CA  ALA A  92       8.739  18.676  33.278  1.00  8.10           C  
ATOM    715  C   ALA A  92      10.217  19.084  33.329  1.00  9.38           C  
ATOM    716  O   ALA A  92      11.088  18.284  33.697  1.00  8.83           O  
ATOM    717  CB  ALA A  92       8.305  18.424  31.829  1.00  4.74           C  
ATOM    718  N   VAL A  93      10.491  20.344  32.993  1.00  9.45           N  
ATOM    719  CA  VAL A  93      11.861  20.852  33.008  1.00  6.90           C  
ATOM    720  C   VAL A  93      12.419  20.751  34.398  1.00  6.61           C  
ATOM    721  O   VAL A  93      13.564  20.350  34.571  1.00 10.55           O  
ATOM    722  CB  VAL A  93      11.942  22.320  32.518  1.00  7.25           C  
ATOM    723  CG1 VAL A  93      13.230  22.994  33.001  1.00  3.26           C  
ATOM    724  CG2 VAL A  93      11.866  22.346  31.005  1.00  2.44           C  
ATOM    725  N   ALA A  94      11.603  21.102  35.385  1.00  5.85           N  
ATOM    726  CA  ALA A  94      12.017  21.053  36.780  1.00  6.45           C  
ATOM    727  C   ALA A  94      12.285  19.616  37.215  1.00  4.25           C  
ATOM    728  O   ALA A  94      13.212  19.355  37.993  1.00  3.72           O  
ATOM    729  CB  ALA A  94      10.961  21.715  37.682  1.00 10.06           C  
ATOM    730  N   CYS A  95      11.492  18.681  36.703  1.00  5.03           N  
ATOM    731  CA  CYS A  95      11.695  17.271  37.040  1.00  4.06           C  
ATOM    732  C   CYS A  95      12.928  16.743  36.283  1.00  5.04           C  
ATOM    733  O   CYS A  95      13.672  15.915  36.803  1.00  8.38           O  
ATOM    734  CB  CYS A  95      10.440  16.450  36.728  1.00  2.12           C  
ATOM    735  SG  CYS A  95      10.451  14.692  37.260  1.00  5.53           S  
ATOM    736  N   ALA A  96      13.184  17.284  35.094  1.00  4.96           N  
ATOM    737  CA  ALA A  96      14.336  16.883  34.278  1.00  6.23           C  
ATOM    738  C   ALA A  96      15.636  17.317  34.949  1.00  4.77           C  
ATOM    739  O   ALA A  96      16.652  16.623  34.870  1.00  5.48           O  
ATOM    740  CB  ALA A  96      14.231  17.486  32.879  1.00  7.92           C  
ATOM    741  N   LYS A  97      15.588  18.462  35.622  1.00  4.91           N  
ATOM    742  CA  LYS A  97      16.727  18.992  36.360  1.00  4.63           C  
ATOM    743  C   LYS A  97      17.057  18.057  37.538  1.00  5.31           C  
ATOM    744  O   LYS A  97      18.228  17.800  37.845  1.00  3.63           O  
ATOM    745  CB  LYS A  97      16.400  20.399  36.868  1.00  5.09           C  
ATOM    746  CG  LYS A  97      16.332  21.452  35.746  1.00  4.64           C  
ATOM    747  CD  LYS A  97      16.326  22.881  36.292  1.00  3.01           C  
ATOM    748  CE  LYS A  97      16.347  23.890  35.156  1.00  4.77           C  
ATOM    749  NZ  LYS A  97      16.312  25.277  35.632  1.00  3.25           N  
ATOM    750  N   ARG A  98      16.014  17.549  38.194  1.00  5.53           N  
ATOM    751  CA  ARG A  98      16.175  16.629  39.310  1.00  3.25           C  
ATOM    752  C   ARG A  98      16.721  15.280  38.823  1.00  3.07           C  
ATOM    753  O   ARG A  98      17.566  14.684  39.471  1.00  4.34           O  
ATOM    754  CB  ARG A  98      14.841  16.440  40.020  1.00  6.17           C  
ATOM    755  CG  ARG A  98      14.831  15.340  41.039  1.00 10.10           C  
ATOM    756  CD  ARG A  98      15.626  15.705  42.278  1.00 14.67           C  
ATOM    757  NE  ARG A  98      15.545  14.635  43.266  1.00 20.13           N  
ATOM    758  CZ  ARG A  98      16.275  13.520  43.226  1.00 24.44           C  
ATOM    759  NH1 ARG A  98      16.115  12.600  44.170  1.00 26.82           N  
ATOM    760  NH2 ARG A  98      17.190  13.336  42.270  1.00 23.79           N  
ATOM    761  N   VAL A  99      16.247  14.792  37.681  1.00  4.65           N  
ATOM    762  CA  VAL A  99      16.750  13.523  37.150  1.00  6.94           C  
ATOM    763  C   VAL A  99      18.263  13.539  36.852  1.00  9.58           C  
ATOM    764  O   VAL A  99      18.976  12.600  37.237  1.00 10.73           O  
ATOM    765  CB  VAL A  99      16.009  13.095  35.884  1.00  3.88           C  
ATOM    766  CG1 VAL A  99      16.589  11.791  35.366  1.00  2.01           C  
ATOM    767  CG2 VAL A  99      14.521  12.957  36.169  1.00  2.74           C  
ATOM    768  N   VAL A 100      18.756  14.575  36.166  1.00  9.13           N  
ATOM    769  CA  VAL A 100      20.191  14.649  35.859  1.00  9.45           C  
ATOM    770  C   VAL A 100      21.079  14.808  37.081  1.00 11.41           C  
ATOM    771  O   VAL A 100      22.245  14.435  37.044  1.00 13.79           O  
ATOM    772  CB  VAL A 100      20.572  15.786  34.881  1.00  8.50           C  
ATOM    773  CG1 VAL A 100      20.008  15.517  33.525  1.00 10.31           C  
ATOM    774  CG2 VAL A 100      20.159  17.150  35.423  1.00  4.61           C  
ATOM    775  N   ARG A 101      20.547  15.397  38.145  1.00 11.66           N  
ATOM    776  CA  ARG A 101      21.321  15.593  39.352  1.00 14.21           C  
ATOM    777  C   ARG A 101      21.758  14.269  40.011  1.00 19.46           C  
ATOM    778  O   ARG A 101      22.539  14.263  40.978  1.00 20.15           O  
ATOM    779  CB  ARG A 101      20.522  16.446  40.335  1.00 13.95           C  
ATOM    780  CG  ARG A 101      20.975  17.901  40.408  1.00 17.59           C  
ATOM    781  CD  ARG A 101      20.247  18.688  41.512  1.00 13.71           C  
ATOM    782  NE  ARG A 101      19.106  19.420  40.972  1.00 18.32           N  
ATOM    783  CZ  ARG A 101      17.895  19.462  41.527  1.00 16.72           C  
ATOM    784  NH1 ARG A 101      16.915  20.157  40.951  1.00 13.61           N  
ATOM    785  NH2 ARG A 101      17.659  18.815  42.652  1.00 15.66           N  
ATOM    786  N   ASP A 102      21.248  13.152  39.499  1.00 21.87           N  
ATOM    787  CA  ASP A 102      21.587  11.835  40.033  1.00 24.11           C  
ATOM    788  C   ASP A 102      22.909  11.307  39.450  1.00 24.52           C  
ATOM    789  O   ASP A 102      23.368  11.792  38.419  1.00 23.12           O  
ATOM    790  CB  ASP A 102      20.421  10.862  39.816  1.00 27.17           C  
ATOM    791  CG  ASP A 102      19.615  10.615  41.099  1.00 31.21           C  
ATOM    792  OD1 ASP A 102      19.214   9.453  41.320  1.00 33.48           O  
ATOM    793  OD2 ASP A 102      19.390  11.564  41.891  1.00 32.20           O  
ATOM    794  N   PRO A 103      23.528  10.296  40.101  1.00 25.27           N  
ATOM    795  CA  PRO A 103      24.803   9.663  39.721  1.00 24.81           C  
ATOM    796  C   PRO A 103      25.190   9.377  38.263  1.00 20.11           C  
ATOM    797  O   PRO A 103      26.374   9.184  37.976  1.00 19.43           O  
ATOM    798  CB  PRO A 103      24.830   8.382  40.585  1.00 26.54           C  
ATOM    799  CG  PRO A 103      23.393   8.150  40.942  1.00 27.30           C  
ATOM    800  CD  PRO A 103      22.932   9.554  41.227  1.00 27.45           C  
ATOM    801  N   GLN A 104      24.226   9.323  37.353  1.00 18.78           N  
ATOM    802  CA  GLN A 104      24.541   9.042  35.950  1.00 17.91           C  
ATOM    803  C   GLN A 104      24.526  10.279  35.074  1.00 13.80           C  
ATOM    804  O   GLN A 104      25.003  10.249  33.932  1.00 12.74           O  
ATOM    805  CB  GLN A 104      23.547   8.047  35.362  1.00 21.37           C  
ATOM    806  CG  GLN A 104      23.436   6.757  36.116  1.00 26.27           C  
ATOM    807  CD  GLN A 104      22.329   5.908  35.564  1.00 29.45           C  
ATOM    808  OE1 GLN A 104      21.198   5.942  36.065  1.00 29.83           O  
ATOM    809  NE2 GLN A 104      22.626   5.170  34.499  1.00 28.64           N  
ATOM    810  N   GLY A 105      23.923  11.344  35.584  1.00  9.81           N  
ATOM    811  CA  GLY A 105      23.836  12.566  34.820  1.00  8.38           C  
ATOM    812  C   GLY A 105      22.818  12.397  33.711  1.00  8.39           C  
ATOM    813  O   GLY A 105      21.779  11.746  33.892  1.00  7.17           O  
ATOM    814  N   ILE A 106      23.130  12.964  32.552  1.00  7.63           N  
ATOM    815  CA  ILE A 106      22.246  12.904  31.397  1.00  8.82           C  
ATOM    816  C   ILE A 106      22.196  11.479  30.790  1.00  9.15           C  
ATOM    817  O   ILE A 106      21.271  11.128  30.057  1.00  5.15           O  
ATOM    818  CB  ILE A 106      22.638  14.003  30.366  1.00  8.49           C  
ATOM    819  CG1 ILE A 106      21.632  14.050  29.216  1.00 10.46           C  
ATOM    820  CG2 ILE A 106      24.064  13.806  29.887  1.00 11.29           C  
ATOM    821  CD1 ILE A 106      21.717  15.315  28.401  1.00 11.98           C  
ATOM    822  N   ARG A 107      23.174  10.653  31.163  1.00  9.87           N  
ATOM    823  CA  ARG A 107      23.243   9.262  30.742  1.00 11.80           C  
ATOM    824  C   ARG A 107      22.079   8.458  31.321  1.00 12.19           C  
ATOM    825  O   ARG A 107      21.897   7.300  30.954  1.00 12.74           O  
ATOM    826  CB  ARG A 107      24.561   8.632  31.211  1.00 16.03           C  
ATOM    827  CG  ARG A 107      25.720   8.935  30.294  1.00 19.58           C  
ATOM    828  CD  ARG A 107      27.077   8.587  30.896  1.00 23.53           C  
ATOM    829  NE  ARG A 107      28.132   8.821  29.909  1.00 25.44           N  
ATOM    830  CZ  ARG A 107      28.454  10.021  29.428  1.00 27.72           C  
ATOM    831  NH1 ARG A 107      29.405  10.137  28.506  1.00 24.45           N  
ATOM    832  NH2 ARG A 107      27.874  11.116  29.918  1.00 27.03           N  
ATOM    833  N   ALA A 108      21.316   9.056  32.245  1.00 10.77           N  
ATOM    834  CA  ALA A 108      20.178   8.374  32.863  1.00 10.02           C  
ATOM    835  C   ALA A 108      19.158   7.906  31.830  1.00  9.68           C  
ATOM    836  O   ALA A 108      18.523   6.864  32.021  1.00 10.73           O  
ATOM    837  CB  ALA A 108      19.524   9.256  33.917  1.00  8.79           C  
ATOM    838  N   TRP A 109      18.985   8.686  30.758  1.00  9.25           N  
ATOM    839  CA  TRP A 109      18.068   8.343  29.663  1.00 10.65           C  
ATOM    840  C   TRP A 109      18.878   7.507  28.676  1.00 13.38           C  
ATOM    841  O   TRP A 109      19.857   7.997  28.103  1.00 14.10           O  
ATOM    842  CB  TRP A 109      17.575   9.597  28.922  1.00  7.96           C  
ATOM    843  CG  TRP A 109      16.592  10.460  29.670  1.00  7.22           C  
ATOM    844  CD1 TRP A 109      15.224  10.399  29.609  1.00  8.83           C  
ATOM    845  CD2 TRP A 109      16.902  11.552  30.550  1.00  7.80           C  
ATOM    846  NE1 TRP A 109      14.662  11.385  30.391  1.00  6.15           N  
ATOM    847  CE2 TRP A 109      15.669  12.109  30.977  1.00  6.96           C  
ATOM    848  CE3 TRP A 109      18.099  12.123  31.008  1.00  7.12           C  
ATOM    849  CZ2 TRP A 109      15.601  13.214  31.841  1.00  6.22           C  
ATOM    850  CZ3 TRP A 109      18.033  13.223  31.866  1.00  7.73           C  
ATOM    851  CH2 TRP A 109      16.792  13.757  32.271  1.00  8.80           C  
ATOM    852  N   VAL A 110      18.450   6.273  28.432  1.00 13.74           N  
ATOM    853  CA  VAL A 110      19.178   5.401  27.519  1.00 12.76           C  
ATOM    854  C   VAL A 110      19.124   5.919  26.090  1.00  9.92           C  
ATOM    855  O   VAL A 110      20.062   5.717  25.318  1.00  9.72           O  
ATOM    856  CB  VAL A 110      18.684   3.927  27.606  1.00 14.02           C  
ATOM    857  CG1 VAL A 110      19.537   3.016  26.736  1.00 12.37           C  
ATOM    858  CG2 VAL A 110      18.762   3.448  29.050  1.00 15.16           C  
ATOM    859  N   ALA A 111      18.050   6.619  25.742  1.00  7.89           N  
ATOM    860  CA  ALA A 111      17.941   7.159  24.392  1.00  7.61           C  
ATOM    861  C   ALA A 111      19.111   8.099  24.120  1.00  5.30           C  
ATOM    862  O   ALA A 111      19.686   8.090  23.035  1.00  7.13           O  
ATOM    863  CB  ALA A 111      16.617   7.889  24.197  1.00  9.58           C  
ATOM    864  N   TRP A 112      19.488   8.878  25.123  1.00  5.45           N  
ATOM    865  CA  TRP A 112      20.591   9.816  24.992  1.00  3.17           C  
ATOM    866  C   TRP A 112      21.880   9.107  24.552  1.00  2.73           C  
ATOM    867  O   TRP A 112      22.543   9.524  23.592  1.00  2.01           O  
ATOM    868  CB  TRP A 112      20.806  10.565  26.310  1.00  2.01           C  
ATOM    869  CG  TRP A 112      21.800  11.639  26.158  1.00  2.00           C  
ATOM    870  CD1 TRP A 112      21.601  12.863  25.591  1.00  2.00           C  
ATOM    871  CD2 TRP A 112      23.198  11.552  26.450  1.00  4.68           C  
ATOM    872  NE1 TRP A 112      22.793  13.538  25.485  1.00  2.02           N  
ATOM    873  CE2 TRP A 112      23.793  12.758  26.004  1.00  3.75           C  
ATOM    874  CE3 TRP A 112      24.008  10.574  27.045  1.00  3.05           C  
ATOM    875  CZ2 TRP A 112      25.163  13.007  26.131  1.00  2.04           C  
ATOM    876  CZ3 TRP A 112      25.365  10.826  27.174  1.00  3.81           C  
ATOM    877  CH2 TRP A 112      25.929  12.037  26.715  1.00  5.29           C  
ATOM    878  N   ARG A 113      22.227   8.036  25.255  1.00  2.24           N  
ATOM    879  CA  ARG A 113      23.422   7.264  24.937  1.00  5.39           C  
ATOM    880  C   ARG A 113      23.412   6.752  23.491  1.00  7.14           C  
ATOM    881  O   ARG A 113      24.413   6.886  22.782  1.00  6.56           O  
ATOM    882  CB  ARG A 113      23.556   6.077  25.890  1.00  7.79           C  
ATOM    883  CG  ARG A 113      23.797   6.454  27.320  1.00 10.65           C  
ATOM    884  CD  ARG A 113      22.776   5.818  28.232  1.00 18.10           C  
ATOM    885  NE  ARG A 113      22.986   4.390  28.438  1.00 19.08           N  
ATOM    886  CZ  ARG A 113      22.953   3.806  29.637  1.00 24.77           C  
ATOM    887  NH1 ARG A 113      23.145   2.501  29.748  1.00 25.18           N  
ATOM    888  NH2 ARG A 113      22.737   4.527  30.733  1.00 24.85           N  
ATOM    889  N   ASN A 114      22.268   6.211  23.062  1.00  8.69           N  
ATOM    890  CA  ASN A 114      22.083   5.655  21.709  1.00 10.48           C  
ATOM    891  C   ASN A 114      22.154   6.663  20.572  1.00  9.88           C  
ATOM    892  O   ASN A 114      22.852   6.434  19.591  1.00  9.14           O  
ATOM    893  CB  ASN A 114      20.718   4.962  21.559  1.00 11.35           C  
ATOM    894  CG  ASN A 114      20.485   3.864  22.567  1.00 14.32           C  
ATOM    895  OD1 ASN A 114      21.390   3.438  23.280  1.00 14.72           O  
ATOM    896  ND2 ASN A 114      19.250   3.391  22.629  1.00 15.46           N  
ATOM    897  N   ARG A 115      21.381   7.745  20.682  1.00  9.39           N  
ATOM    898  CA  ARG A 115      21.305   8.753  19.620  1.00  9.95           C  
ATOM    899  C   ARG A 115      22.020  10.099  19.770  1.00  7.95           C  
ATOM    900  O   ARG A 115      22.031  10.873  18.810  1.00  5.96           O  
ATOM    901  CB  ARG A 115      19.838   9.056  19.259  1.00 12.34           C  
ATOM    902  CG  ARG A 115      18.759   8.272  20.008  1.00 17.74           C  
ATOM    903  CD  ARG A 115      18.372   6.994  19.274  1.00 20.82           C  
ATOM    904  NE  ARG A 115      18.198   7.210  17.836  1.00 23.43           N  
ATOM    905  CZ  ARG A 115      17.497   6.415  17.031  1.00 23.58           C  
ATOM    906  NH1 ARG A 115      17.406   6.704  15.742  1.00 23.18           N  
ATOM    907  NH2 ARG A 115      16.879   5.341  17.510  1.00 25.64           N  
ATOM    908  N   CYS A 116      22.576  10.399  20.945  1.00  6.18           N  
ATOM    909  CA  CYS A 116      23.235  11.692  21.169  1.00  4.94           C  
ATOM    910  C   CYS A 116      24.702  11.670  21.585  1.00  4.50           C  
ATOM    911  O   CYS A 116      25.495  12.484  21.080  1.00  4.01           O  
ATOM    912  CB  CYS A 116      22.460  12.511  22.205  1.00  5.65           C  
ATOM    913  SG  CYS A 116      20.669  12.602  21.903  1.00  5.70           S  
ATOM    914  N   GLN A 117      25.037  10.829  22.566  1.00  3.52           N  
ATOM    915  CA  GLN A 117      26.410  10.708  23.065  1.00  7.52           C  
ATOM    916  C   GLN A 117      27.433  10.487  21.951  1.00 10.97           C  
ATOM    917  O   GLN A 117      27.256   9.635  21.086  1.00  9.36           O  
ATOM    918  CB  GLN A 117      26.519   9.573  24.098  1.00  7.72           C  
ATOM    919  CG  GLN A 117      27.958   9.177  24.440  1.00  6.66           C  
ATOM    920  CD  GLN A 117      28.067   8.249  25.640  1.00  8.67           C  
ATOM    921  OE1 GLN A 117      28.944   8.419  26.484  1.00 10.66           O  
ATOM    922  NE2 GLN A 117      27.189   7.260  25.718  1.00 10.73           N  
ATOM    923  N   ASN A 118      28.505  11.271  21.985  1.00 14.00           N  
ATOM    924  CA  ASN A 118      29.584  11.189  20.988  1.00 15.48           C  
ATOM    925  C   ASN A 118      29.195  11.531  19.547  1.00 13.78           C  
ATOM    926  O   ASN A 118      29.892  11.167  18.598  1.00 16.09           O  
ATOM    927  CB  ASN A 118      30.282   9.824  21.051  1.00 17.69           C  
ATOM    928  CG  ASN A 118      30.886   9.539  22.417  1.00 22.61           C  
ATOM    929  OD1 ASN A 118      31.018   8.383  22.819  1.00 25.77           O  
ATOM    930  ND2 ASN A 118      31.233  10.593  23.148  1.00 21.09           N  
ATOM    931  N   ARG A 119      28.097  12.255  19.380  1.00 12.71           N  
ATOM    932  CA  ARG A 119      27.658  12.645  18.055  1.00 10.05           C  
ATOM    933  C   ARG A 119      27.673  14.154  17.926  1.00  8.27           C  
ATOM    934  O   ARG A 119      27.779  14.875  18.914  1.00 12.28           O  
ATOM    935  CB  ARG A 119      26.248  12.124  17.781  1.00 10.66           C  
ATOM    936  CG  ARG A 119      26.097  10.633  17.982  1.00 14.49           C  
ATOM    937  CD  ARG A 119      24.820  10.146  17.374  1.00 13.70           C  
ATOM    938  NE  ARG A 119      24.528   8.758  17.714  1.00 15.13           N  
ATOM    939  CZ  ARG A 119      24.201   7.832  16.819  1.00 14.31           C  
ATOM    940  NH1 ARG A 119      23.930   6.594  17.211  1.00 12.97           N  
ATOM    941  NH2 ARG A 119      24.201   8.131  15.529  1.00 10.80           N  
ATOM    942  N   ASP A 120      27.523  14.624  16.699  1.00  9.80           N  
ATOM    943  CA  ASP A 120      27.497  16.044  16.390  1.00  9.85           C  
ATOM    944  C   ASP A 120      26.070  16.524  16.640  1.00  9.21           C  
ATOM    945  O   ASP A 120      25.202  16.346  15.791  1.00 12.38           O  
ATOM    946  CB  ASP A 120      27.873  16.225  14.919  1.00  9.68           C  
ATOM    947  CG  ASP A 120      28.086  17.670  14.535  1.00 11.33           C  
ATOM    948  OD1 ASP A 120      28.012  18.556  15.400  1.00  8.83           O  
ATOM    949  OD2 ASP A 120      28.337  17.912  13.344  1.00 16.01           O  
ATOM    950  N   VAL A 121      25.828  17.132  17.797  1.00  8.89           N  
ATOM    951  CA  VAL A 121      24.487  17.604  18.148  1.00  8.73           C  
ATOM    952  C   VAL A 121      24.153  19.062  17.806  1.00  9.68           C  
ATOM    953  O   VAL A 121      23.033  19.517  18.042  1.00  8.75           O  
ATOM    954  CB  VAL A 121      24.148  17.295  19.623  1.00  9.50           C  
ATOM    955  CG1 VAL A 121      23.935  15.795  19.800  1.00  7.54           C  
ATOM    956  CG2 VAL A 121      25.273  17.782  20.558  1.00 12.14           C  
ATOM    957  N   ARG A 122      25.103  19.765  17.192  1.00 11.03           N  
ATOM    958  CA  ARG A 122      24.930  21.166  16.780  1.00 14.24           C  
ATOM    959  C   ARG A 122      23.638  21.410  15.992  1.00 12.51           C  
ATOM    960  O   ARG A 122      22.932  22.398  16.204  1.00 13.01           O  
ATOM    961  CB  ARG A 122      26.095  21.592  15.888  1.00 17.80           C  
ATOM    962  CG  ARG A 122      27.440  21.737  16.578  1.00 24.02           C  
ATOM    963  CD  ARG A 122      28.546  21.884  15.525  1.00 29.14           C  
ATOM    964  NE  ARG A 122      29.887  21.921  16.105  1.00 35.73           N  
ATOM    965  CZ  ARG A 122      30.416  20.958  16.861  1.00 39.26           C  
ATOM    966  NH1 ARG A 122      31.649  21.096  17.345  1.00 39.76           N  
ATOM    967  NH2 ARG A 122      29.721  19.859  17.139  1.00 41.12           N  
ATOM    968  N   GLN A 123      23.357  20.516  15.057  1.00 11.76           N  
ATOM    969  CA  GLN A 123      22.176  20.604  14.205  1.00 13.61           C  
ATOM    970  C   GLN A 123      20.872  20.862  14.950  1.00 12.98           C  
ATOM    971  O   GLN A 123      19.927  21.403  14.383  1.00 14.03           O  
ATOM    972  CB  GLN A 123      22.044  19.322  13.380  1.00 16.40           C  
ATOM    973  CG  GLN A 123      21.891  18.063  14.217  1.00 21.12           C  
ATOM    974  CD  GLN A 123      21.787  16.820  13.364  1.00 27.53           C  
ATOM    975  OE1 GLN A 123      20.760  16.571  12.724  1.00 31.40           O  
ATOM    976  NE2 GLN A 123      22.853  16.032  13.340  1.00 29.91           N  
ATOM    977  N   TYR A 124      20.819  20.479  16.218  1.00 13.77           N  
ATOM    978  CA  TYR A 124      19.615  20.679  16.995  1.00 12.96           C  
ATOM    979  C   TYR A 124      19.355  22.124  17.409  1.00 12.59           C  
ATOM    980  O   TYR A 124      18.196  22.492  17.599  1.00 17.18           O  
ATOM    981  CB  TYR A 124      19.597  19.736  18.201  1.00 10.72           C  
ATOM    982  CG  TYR A 124      19.572  18.269  17.811  1.00 11.34           C  
ATOM    983  CD1 TYR A 124      18.387  17.664  17.389  1.00 10.92           C  
ATOM    984  CD2 TYR A 124      20.738  17.486  17.847  1.00  8.68           C  
ATOM    985  CE1 TYR A 124      18.355  16.325  17.009  1.00  9.86           C  
ATOM    986  CE2 TYR A 124      20.715  16.140  17.467  1.00  8.74           C  
ATOM    987  CZ  TYR A 124      19.519  15.572  17.050  1.00  9.67           C  
ATOM    988  OH  TYR A 124      19.470  14.256  16.663  1.00 10.71           O  
ATOM    989  N   VAL A 125      20.397  22.955  17.485  1.00 10.79           N  
ATOM    990  CA  VAL A 125      20.229  24.366  17.888  1.00  9.91           C  
ATOM    991  C   VAL A 125      20.639  25.433  16.849  1.00 13.08           C  
ATOM    992  O   VAL A 125      20.556  26.638  17.121  1.00 11.32           O  
ATOM    993  CB  VAL A 125      21.012  24.695  19.195  1.00  8.23           C  
ATOM    994  CG1 VAL A 125      20.477  23.896  20.369  1.00  6.89           C  
ATOM    995  CG2 VAL A 125      22.509  24.433  18.997  1.00  6.37           C  
ATOM    996  N   GLN A 126      21.088  25.007  15.675  1.00 15.66           N  
ATOM    997  CA  GLN A 126      21.531  25.945  14.644  1.00 17.82           C  
ATOM    998  C   GLN A 126      20.454  26.837  14.026  1.00 16.71           C  
ATOM    999  O   GLN A 126      19.398  26.367  13.589  1.00 16.95           O  
ATOM   1000  CB  GLN A 126      22.326  25.218  13.554  1.00 22.13           C  
ATOM   1001  CG  GLN A 126      23.622  24.552  14.064  1.00 30.09           C  
ATOM   1002  CD  GLN A 126      24.471  25.448  14.991  1.00 33.23           C  
ATOM   1003  OE1 GLN A 126      25.119  26.400  14.541  1.00 35.94           O  
ATOM   1004  NE2 GLN A 126      24.488  25.120  16.280  1.00 29.75           N  
ATOM   1005  N   GLY A 127      20.727  28.139  14.034  1.00 16.84           N  
ATOM   1006  CA  GLY A 127      19.805  29.120  13.481  1.00 15.69           C  
ATOM   1007  C   GLY A 127      18.654  29.475  14.403  1.00 15.40           C  
ATOM   1008  O   GLY A 127      17.769  30.245  14.022  1.00 15.92           O  
ATOM   1009  N   CYS A 128      18.670  28.951  15.624  1.00 10.92           N  
ATOM   1010  CA  CYS A 128      17.595  29.214  16.561  1.00  9.43           C  
ATOM   1011  C   CYS A 128      17.782  30.494  17.341  1.00 10.30           C  
ATOM   1012  O   CYS A 128      16.865  30.940  18.034  1.00  7.93           O  
ATOM   1013  CB  CYS A 128      17.434  28.047  17.530  1.00  9.76           C  
ATOM   1014  SG  CYS A 128      16.860  26.517  16.737  1.00  8.67           S  
ATOM   1015  N   GLY A 129      18.985  31.055  17.267  1.00 10.51           N  
ATOM   1016  CA  GLY A 129      19.273  32.283  17.978  1.00 13.48           C  
ATOM   1017  C   GLY A 129      19.590  32.101  19.453  1.00 15.79           C  
ATOM   1018  O   GLY A 129      19.624  33.084  20.204  1.00 17.87           O  
ATOM   1019  N   VAL A 130      19.863  30.870  19.878  1.00 15.36           N  
ATOM   1020  CA  VAL A 130      20.193  30.625  21.283  1.00 14.31           C  
ATOM   1021  C   VAL A 130      21.696  30.457  21.480  1.00 13.01           C  
ATOM   1022  O   VAL A 130      22.436  30.455  20.477  1.00 14.90           O  
ATOM   1023  CB  VAL A 130      19.467  29.385  21.843  1.00 13.27           C  
ATOM   1024  CG1 VAL A 130      17.969  29.591  21.780  1.00 13.09           C  
ATOM   1025  CG2 VAL A 130      19.894  28.123  21.086  1.00 15.64           C  
ATOM   1026  OXT VAL A 130      22.121  30.336  22.638  1.00 16.09           O  
TER    1027      VAL A 130                                                      
HETATM 1028 NA    NA A 601       6.082   7.135   7.127  1.00 33.49          NA  
HETATM 1029  O   HOH A 131       0.371  12.741  43.089  1.00  2.00           O  
HETATM 1030  O   HOH A 132       1.294  17.968  40.797  1.00  3.94           O  
HETATM 1031  O   HOH A 133       5.346  20.643  32.657  1.00  5.59           O  
HETATM 1032  O   HOH A 134       8.423  15.138  30.534  1.00  2.00           O  
HETATM 1033  O   HOH A 135      28.951   9.752  15.175  1.00 10.91           O  
HETATM 1034  O   HOH A 136      -4.077   6.344  44.485  1.00  9.45           O  
HETATM 1035  O   HOH A 137       6.089  17.146  29.043  1.00  4.24           O  
HETATM 1036  O   HOH A 138      12.010  25.488  13.857  1.00 15.11           O  
HETATM 1037  O   HOH A 139      27.522  12.568  14.352  1.00  9.16           O  
HETATM 1038  O   HOH A 140       4.024   6.178   6.241  1.00  4.64           O  
HETATM 1039  O   HOH A 141      21.485  29.004  17.586  1.00 14.64           O  
HETATM 1040  O   HOH A 142      10.907  29.895  15.480  1.00  3.62           O  
HETATM 1041  O   HOH A 143       2.225   3.263  34.929  1.00 17.98           O  
HETATM 1042  O   HOH A 144       7.943  20.136  15.207  1.00 16.45           O  
HETATM 1043  O   HOH A 145      -0.072   4.037  31.264  1.00  5.39           O  
HETATM 1044  O   HOH A 146      10.118  21.525  14.281  1.00 10.61           O  
HETATM 1045  O   HOH A 147      -1.023  11.477  40.413  1.00  6.21           O  
HETATM 1046  O   HOH A 148       4.112  25.801  25.810  1.00 20.26           O  
HETATM 1047  O   HOH A 149      15.148  18.235  14.993  1.00 12.40           O  
HETATM 1048  O   HOH A 150       6.426  25.864  28.191  1.00 20.97           O  
HETATM 1049  O   HOH A 151      -1.940  18.830  35.254  1.00 23.00           O  
HETATM 1050  O   HOH A 152       4.786  21.109  14.759  1.00 31.92           O  
HETATM 1051  O   HOH A 153      26.827  14.832  23.051  1.00 17.69           O  
HETATM 1052  O   HOH A 154      18.434  20.591  11.997  1.00 19.21           O  
HETATM 1053  O   HOH A 155      19.768  28.427  29.771  1.00 15.15           O  
HETATM 1054  O   HOH A 156       1.447  -5.468  39.812  1.00 15.18           O  
HETATM 1055  O   HOH A 157      25.459  16.093  34.755  1.00 13.09           O  
HETATM 1056  O   HOH A 158      15.362   6.668  27.131  1.00  8.97           O  
HETATM 1057  O   HOH A 159      11.402  11.188  13.437  1.00 35.82           O  
HETATM 1058  O   HOH A 160      26.284   5.056  14.920  1.00 27.34           O  
HETATM 1059  O   HOH A 161       5.953  27.547  25.256  1.00 29.90           O  
HETATM 1060  O   HOH A 162      27.347   4.539  38.824  1.00 25.03           O  
HETATM 1061  O   HOH A 163      12.042  -5.342  37.749  1.00  8.45           O  
HETATM 1062  O   HOH A 164      18.849  23.634  41.203  1.00 36.63           O  
HETATM 1063  O   HOH A 165       8.382   9.912  47.194  1.00 26.45           O  
HETATM 1064  O   HOH A 166      24.063  23.721  36.970  1.00 30.53           O  
HETATM 1065  O   HOH A 167      17.818  26.356  37.612  1.00 35.68           O  
HETATM 1066  O   HOH A 168      24.802  15.228  38.201  1.00 28.58           O  
HETATM 1067  O   HOH A 169      12.596   9.137  33.335  1.00 25.42           O  
HETATM 1068  O   HOH A 170      10.126  27.213  15.599  1.00 15.68           O  
HETATM 1069  O   HOH A 171      28.759  16.105  21.319  1.00 18.08           O  
HETATM 1070  O   HOH A 172       0.394   0.030  35.842  1.00 14.92           O  
HETATM 1071  O   HOH A 173       3.183  20.817  41.581  1.00 24.18           O  
HETATM 1072  O   HOH A 174      14.360   8.724  41.998  1.00 20.10           O  
HETATM 1073  O   HOH A 175       7.954  23.800  38.834  1.00 40.63           O  
HETATM 1074  O   HOH A 176      -0.410  -4.521  27.024  1.00 26.01           O  
HETATM 1075  O   HOH A 177      -0.010  -0.332  41.653  1.00 34.98           O  
HETATM 1076  O   HOH A 178       1.594   8.678  46.999  1.00 30.49           O  
HETATM 1077  O   HOH A 179       6.065  -2.365  26.460  1.00 25.13           O  
HETATM 1078  O   HOH A 180       0.828  26.733  26.758  1.00 45.64           O  
HETATM 1079  O   HOH A 181      14.204  13.946  12.140  1.00 20.16           O  
HETATM 1080  O   HOH A 182      23.299  29.244  15.164  1.00 37.68           O  
HETATM 1081  O   HOH A 183      23.951  33.544  25.632  1.00 35.76           O  
HETATM 1082  O   HOH A 184      -1.470   9.187  45.525  1.00 19.50           O  
HETATM 1083  O   HOH A 185      25.046   8.424  11.470  1.00 39.56           O  
HETATM 1084  O   HOH A 186      13.630  24.927  36.700  1.00 26.68           O  
HETATM 1085  O   HOH A 187       2.615  -2.134  44.907  1.00 23.22           O  
HETATM 1086  O   HOH A 188      20.889   9.855  15.791  1.00 25.55           O  
HETATM 1087  O   HOH A 189       2.449   3.051  25.156  1.00 28.32           O  
HETATM 1088  O   HOH A 190       4.994  17.758  13.407  1.00 27.24           O  
HETATM 1089  O   HOH A 191       7.082   2.202  46.840  1.00 27.73           O  
HETATM 1090  O   HOH A 192       4.391   3.195  44.967  1.00 30.73           O  
HETATM 1091  O   HOH A 193      26.557  13.105  42.247  1.00 32.73           O  
HETATM 1092  O   HOH A 194      26.168  23.513  19.558  1.00 38.90           O  
HETATM 1093  O   HOH A 195      15.847   5.661  29.885  1.00 18.02           O  
HETATM 1094  O   HOH A 196      -3.761  -6.191  32.262  1.00 42.66           O  
HETATM 1095  O   HOH A 197      26.835  24.265  36.072  1.00 22.71           O  
HETATM 1096  O   HOH A 198       2.165  24.451  34.725  1.00 34.89           O  
HETATM 1097  O   HOH A 199      15.539  32.116  24.675  1.00 13.84           O  
HETATM 1098  O   HOH A 200      15.118   8.758  32.668  1.00 37.94           O  
HETATM 1099  O   HOH A 201       6.719  14.742  16.676  1.00 41.12           O  
HETATM 1100  O   HOH A 202      14.571  21.246  40.040  1.00 24.19           O  
HETATM 1101  O   HOH A 203       7.584  17.395  14.490  1.00 26.14           O  
HETATM 1102  O   HOH A 204       4.136  26.263  16.339  1.00 33.49           O  
HETATM 1103  O   HOH A 205      -0.474   5.827  28.605  1.00 42.67           O  
HETATM 1104  O   HOH A 206      11.338   1.578  35.711  1.00 20.92           O  
HETATM 1105  O   HOH A 207      15.599  26.280  39.388  1.00 21.01           O  
HETATM 1106  O   HOH A 208       3.128  16.782  44.607  1.00 34.27           O  
HETATM 1107  O   HOH A 209      21.158  27.547  10.419  1.00 39.12           O  
HETATM 1108  O   HOH A 211      11.325  25.566  35.282  1.00 34.01           O  
HETATM 1109  O   HOH A 212      33.184  18.502  13.582  1.00 35.06           O  
HETATM 1110  O   HOH A 213       5.133   6.852  11.795  1.00 40.33           O  
HETATM 1111  O   HOH A 214      16.683   1.866  31.717  1.00 39.22           O  
HETATM 1112  O   HOH A 215      -1.902  25.437  36.427  1.00 28.85           O  
HETATM 1113  O   HOH A 216       8.438  12.548  15.799  1.00 40.74           O  
HETATM 1114  O   HOH A 217      -0.814  -4.955  29.940  1.00 39.28           O  
HETATM 1115  O   HOH A 218      14.507   9.271  12.362  1.00 34.72           O  
HETATM 1116  O   HOH A 219      -0.141  -3.492  38.781  1.00 31.67           O  
HETATM 1117  O   HOH A 220       9.013  -4.494  27.604  1.00 37.48           O  
HETATM 1118  O   HOH A 221      17.698  14.398  13.549  1.00 34.54           O  
HETATM 1119  O   HOH A 222      17.918   3.569  41.492  1.00 33.46           O  
HETATM 1120  O   HOH A 223      18.877   3.210  33.539  1.00 41.20           O  
HETATM 1121  O   HOH A 224      10.624  32.165  21.730  1.00 33.06           O  
HETATM 1122  O   HOH A 225      13.534  25.579  11.573  1.00 39.53           O  
HETATM 1123  O   HOH A 226       6.494  19.830  42.622  1.00 34.07           O  
HETATM 1124  O   HOH A 227      20.708  32.896  12.472  1.00 31.88           O  
HETATM 1125  O   HOH A 228       6.937  -0.581  47.883  1.00 40.64           O  
HETATM 1126  O   HOH A 229      12.904   7.190  18.231  1.00 38.62           O  
HETATM 1127  O   HOH A 230      14.996   6.262  13.284  1.00 37.97           O  
HETATM 1128  O   HOH A 231      19.790  33.357  23.305  1.00 37.58           O  
HETATM 1129  O   HOH A 232      14.223   3.920  44.542  1.00 38.97           O  
HETATM 1130  O   HOH A 233      12.441   6.954  31.108  1.00 40.09           O  
HETATM 1131  O   HOH A 234      21.931  10.790  44.249  1.00 34.24           O  
HETATM 1132  O   HOH A 235      16.240  21.501  10.500  1.00 35.52           O  
HETATM 1133  O   HOH A 236      37.838  31.286  10.685  1.00 29.90           O  
HETATM 1134  O   HOH A 237      11.699   6.774  15.855  1.00 29.67           O  
HETATM 1135  O   HOH A 238      18.839  26.156  10.843  1.00 33.83           O  
HETATM 1136  O   HOH A 239      19.958  29.276  36.170  1.00 31.62           O  
HETATM 1137  O   HOH A 240       0.394  17.616  43.351  1.00 13.45           O  
HETATM 1138  O   HOH A 241      11.094  10.887  18.210  1.00 35.62           O  
HETATM 1139  O   HOH A 242       5.023  19.353  30.033  1.00 10.12           O  
HETATM 1140  O   HOH A 243       4.420  23.124  33.870  1.00 10.96           O  
HETATM 1141  O   HOH A 244      14.575  17.842  44.305  1.00 36.65           O  
HETATM 1142  O   HOH A 245      30.158  17.115  18.893  1.00 43.04           O  
HETATM 1143  O   HOH A 246       0.681  -3.954  43.542  1.00 30.08           O  
HETATM 1144  O   HOH A 247      21.235  13.862  10.017  1.00 27.85           O  
HETATM 1145  O   HOH A 248       2.753  15.912  46.985  1.00 35.08           O  
HETATM 1146  O   HOH A 249      21.609  22.058  10.635  1.00 36.50           O  
HETATM 1147  O   HOH A 250      24.037  26.098  35.424  1.00 37.92           O  
HETATM 1148  O   HOH A 251      34.182  22.063  15.868  1.00 38.22           O  
HETATM 1149  O   HOH A 252      -0.573   3.821  44.858  1.00 24.91           O  
HETATM 1150  O   HOH A 253      18.853   8.428  44.473  1.00 34.18           O  
HETATM 1151  O   HOH A 254      36.304  30.305  16.481  1.00 27.89           O  
HETATM 1152  O   HOH A 255      11.466  -0.064  41.746  1.00 28.97           O  
HETATM 1153  O   HOH A 256      10.081  18.777  40.765  1.00 29.62           O  
HETATM 1154  O   HOH A 257      28.369  28.830  11.720  1.00 35.74           O  
HETATM 1155  O   HOH A 258      22.022  12.524  16.775  1.00 36.55           O  
HETATM 1156  O   HOH A 259      33.613  21.444  12.884  1.00 41.79           O  
HETATM 1157  O   HOH A 260      10.601  18.162  45.935  1.00 33.85           O  
HETATM 1158  O   HOH A 261      -0.207   1.529  26.232  1.00 40.30           O  
HETATM 1159  O   HOH A 262      13.561  21.547  11.935  1.00 27.04           O  
HETATM 1160  O   HOH A 263       2.001   8.787  23.127  1.00 29.85           O  
HETATM 1161  O   HOH A 264      23.089   4.712  42.050  1.00 34.06           O  
HETATM 1162  O   HOH A 265      36.358  20.178  16.272  1.00 25.88           O  
HETATM 1163  O   HOH A 266      14.291   5.630  34.371  1.00 34.49           O  
HETATM 1164  O   HOH A 267       1.186   5.906  45.304  1.00 38.21           O  
HETATM 1165  O   HOH A 268      19.375  23.325  12.285  1.00 37.07           O  
HETATM 1166  O   HOH A 269       8.589  21.292  40.184  1.00 39.12           O  
HETATM 1167  O   HOH A 270      24.104  27.191  20.625  1.00 40.16           O  
HETATM 1168  O   HOH A 271       6.261  27.063  38.166  1.00 36.02           O  
HETATM 1169  O   HOH A 272      10.333   0.275  31.850  1.00 38.21           O  
HETATM 1170  O   HOH A 273      11.251   2.359  43.854  1.00 29.87           O  
HETATM 1171  O   HOH A 274      21.197  24.774  40.318  1.00 21.37           O  
HETATM 1172  O   HOH A 275      27.401   7.015  13.082  1.00 32.07           O  
HETATM 1173  O   HOH A 276      -5.477   2.911  34.446  1.00 35.43           O  
HETATM 1174  O   HOH A 277      36.354  26.040  15.194  1.00 26.23           O  
HETATM 1175  O   HOH A 278      15.499   1.053  42.841  1.00 35.33           O  
HETATM 1176  O   HOH A 279       9.512   0.476  46.576  1.00 37.30           O  
HETATM 1177  O   HOH A 280      15.938   2.938  15.095  1.00 33.79           O  
HETATM 1178  O   HOH A 281      -1.223  -7.145  31.757  1.00 31.57           O  
HETATM 1179  O   HOH A 282      23.639   4.521  39.380  1.00 38.76           O  
HETATM 1180  O   HOH A 283       5.143   7.219   9.055  1.00 28.63           O  
HETATM 1181  O   HOH A 284       7.522  31.684  15.528  1.00 21.82           O  
HETATM 1182  O   HOH A 285      13.228   7.463  28.755  1.00 36.47           O  
HETATM 1183  O   HOH A 286      40.183  27.022   9.760  1.00 42.19           O  
HETATM 1184  O   HOH A 287      15.646  -0.151  37.373  1.00 29.00           O  
HETATM 1185  O   HOH A 288       2.869  26.681  36.819  1.00 45.52           O  
HETATM 1186  O   HOH A 289      25.099  11.730  12.515  1.00 43.10           O  
HETATM 1187  O   HOH A 290      21.585   2.111  33.325  1.00 36.67           O  
HETATM 1188  O   HOH A 291      24.322   1.909  33.284  1.00 28.35           O  
HETATM 1189  O   HOH A 292      13.666   4.692  26.068  1.00 31.84           O  
HETATM 1190  O   HOH A 293      11.974   5.013  21.577  1.00 37.05           O  
HETATM 1191  O   HOH A 294      17.263   3.888  36.968  1.00 34.10           O  
HETATM 1192  O   HOH A 295      13.567   4.781  15.116  1.00 39.26           O  
HETATM 1193  O   HOH A 296       3.272  -7.597  37.260  1.00 18.35           O  
HETATM 1194  O   HOH A 297      13.650   4.742  19.583  1.00 32.25           O  
HETATM 1195  O   HOH A 298       2.698   4.309   7.739  1.00 22.69           O  
HETATM 1196  O   HOH A 299      18.869   6.819  37.220  1.00 38.65           O  
HETATM 1197  O   HOH A 300      29.787  20.703  13.098  1.00 32.89           O  
HETATM 1198  O   HOH A 301      28.307  20.646   9.504  1.00 37.53           O  
HETATM 1199  O   HOH A 302      20.817  27.375  38.840  1.00 36.35           O  
HETATM 1200  O   HOH A 303      16.964  18.596  13.154  1.00 38.07           O  
HETATM 1201  O   HOH A 304      12.568  18.106  42.485  1.00 36.05           O  
HETATM 1202  O   HOH A 305      -5.511   0.711  37.047  1.00 41.42           O  
HETATM 1203  O   HOH A 306      26.509  30.439  16.236  1.00 41.44           O  
HETATM 1204  O   HOH A 307      -0.081  28.772  31.522  1.00 25.48           O  
HETATM 1205  O   HOH A 308      13.690  23.972  39.392  1.00 34.81           O  
HETATM 1206  O   HOH A 309      -0.557  -2.656  35.621  1.00 40.57           O  
HETATM 1207  O   HOH A 310      16.872   3.231  10.238  1.00 42.05           O  
HETATM 1208  O   HOH A 311      23.089  22.701  40.313  1.00 38.90           O  
HETATM 1209  O   HOH A 312      22.200   7.608  44.366  1.00 36.28           O  
HETATM 1210  O   HOH A 313      19.012   1.305   3.531  1.00 38.46           O  
HETATM 1211  O   HOH A 314       7.523  31.846  23.934  1.00 38.98           O  
HETATM 1212  O   HOH A 315      30.988  29.402  15.749  1.00 41.68           O  
HETATM 1213  O   HOH A 316       9.036  21.538  11.818  1.00 39.75           O  
HETATM 1214  O   HOH A 317       4.451  28.917  12.752  1.00 44.08           O  
HETATM 1215  O   HOH A 318       7.016  -0.407  21.820  1.00 41.42           O  
HETATM 1216  O   HOH A 319      14.808   0.519  34.616  1.00 31.89           O  
HETATM 1217  O   HOH A 320      10.525   7.051  22.551  1.00 39.97           O  
HETATM 1218  O   HOH A 321       2.232   1.685  44.045  1.00 36.31           O  
HETATM 1219  O   HOH A 322      26.827  20.264  19.183  1.00 48.43           O  
HETATM 1220  O   HOH A 323       5.889  30.156  18.125  1.00 43.18           O  
HETATM 1221  O   HOH A 324       0.657  24.896  38.521  1.00 40.24           O  
HETATM 1222  O   HOH A 325      12.287  -0.150  33.782  1.00 41.68           O  
HETATM 1223  O   HOH A 326      20.709   7.405  39.299  1.00 38.72           O  
HETATM 1224  O   HOH A 327       9.480   9.010  19.969  1.00 39.94           O  
HETATM 1225  O   HOH A 328       8.540  19.101  44.540  1.00 38.41           O  
HETATM 1226  O   HOH A 329      -3.505   1.315  44.789  1.00 39.68           O  
HETATM 1227  O   HOH A 330      14.343  20.561  42.687  1.00 40.99           O  
HETATM 1228  O   HOH A 331      36.769  29.314  13.774  1.00 43.98           O  
HETATM 1229  O   HOH A 332      14.090   6.843  21.977  1.00 38.40           O  
HETATM 1230  O   HOH A 333       6.210  25.491  41.238  1.00 41.01           O  
HETATM 1231  O   HOH A 334      -3.744   0.808  39.476  1.00 36.58           O  
HETATM 1232  O   HOH A 336      27.324  28.590  14.184  1.00 37.38           O  
HETATM 1233  O   HOH A 337      -2.892   1.145  42.148  1.00 45.08           O  
HETATM 1234  O   HOH A 338       4.274   9.315  46.299  1.00 34.53           O  
HETATM 1235  O   HOH A 339      21.672  31.733  15.499  1.00 27.53           O  
HETATM 1236  O   HOH A 340      28.517  11.650  41.091  1.00 32.65           O  
HETATM 1237  O   HOH A 341      29.164  13.192  12.299  1.00 22.71           O  
HETATM 1238  O   HOH A 342       2.267  -3.193  24.918  1.00 47.07           O  
HETATM 1239  O   HOH A 343       1.327  28.580  34.967  1.00 35.42           O  
HETATM 1240  O   HOH A 344      21.078  10.687  36.541  1.00 34.23           O  
HETATM 1241  O   HOH A 345      -3.739   1.960  30.878  1.00 40.89           O  
HETATM 1242  O   HOH A 346      15.808   0.774  40.102  1.00 40.70           O  
HETATM 1243  O   HOH A 347       0.253   6.493  24.024  1.00 42.78           O  
HETATM 1244  O   HOH A 348      12.347  19.938  13.732  1.00 40.66           O  
HETATM 1245  O   HOH A 349      16.131   9.303  43.963  1.00 38.07           O  
HETATM 1246  O   HOH A 350       8.017  25.768   9.744  1.00 34.77           O  
HETATM 1247  O   HOH A 352      15.357   1.986  25.713  1.00 39.99           O  
HETATM 1248  O   HOH A 353      15.894  24.055   9.209  1.00 42.74           O  
HETATM 1249  O   HOH A 354      25.349  28.807  11.673  1.00 36.27           O  
HETATM 1250  O   HOH A 355       4.298  15.889  15.325  1.00 42.60           O  
HETATM 1251  O   HOH A 356      27.449  25.040  17.150  1.00 42.50           O  
HETATM 1252  O   HOH A 357       2.481   0.359  24.485  1.00 46.84           O  
HETATM 1253  O   HOH A 358       7.504   0.101  25.738  1.00 46.34           O  
HETATM 1254  O   HOH A 359      -0.993  -5.699  41.355  1.00 42.24           O  
HETATM 1255  O   HOH A 360      11.871  -0.846  45.590  1.00 34.05           O  
HETATM 1256  O   HOH A 362      27.306   5.122  34.358  1.00 40.03           O  
HETATM 1257  O   HOH A 363       2.512  25.864  11.219  1.00 48.66           O  
HETATM 1258  O   HOH A 364      11.478   0.770  16.405  1.00 40.51           O  
CONECT   53 1014                                                                
CONECT  240  913                                                                
CONECT  531  639                                                                
CONECT  609  735                                                                
CONECT  639  531                                                                
CONECT  735  609                                                                
CONECT  913  240                                                                
CONECT 1014   53                                                                
CONECT 1028 1038 1180                                                           
CONECT 1038 1028                                                                
CONECT 1180 1028                                                                
MASTER      252    0    1    7    3    0    2    6 1257    1   11   10          
END                                                                             
