HEADER    HYDROLASE                               11-JAN-99   1B5Y              
TITLE     CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF     
TITLE    2 HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA       
TITLE    3 MUTANTS                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (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 STRAIN: AH22R-;                                                      
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: PGEL125                                   
KEYWDS    HYDROGEN BOND, STABILITY, HYDROLASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAKANO,Y.YAMAGATA,M.KUBOTA,J.FUNAHASHI,S.FUJII,K.YUTANI             
REVDAT   6   03-APR-24 1B5Y    1       REMARK                                   
REVDAT   5   03-NOV-21 1B5Y    1       REMARK SEQADV LINK                       
REVDAT   4   24-FEB-09 1B5Y    1       VERSN                                    
REVDAT   3   01-APR-03 1B5Y    1       JRNL                                     
REVDAT   2   29-DEC-99 1B5Y    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   20-JAN-99 1B5Y    0                                                
JRNL        AUTH   K.TAKANO,Y.YAMAGATA,M.KUBOTA,J.FUNAHASHI,S.FUJII,K.YUTANI    
JRNL        TITL   CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL         
JRNL        TITL 2 STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS  
JRNL        TITL 3 OF SIX SER --> ALA MUTANTS.                                  
JRNL        REF    BIOCHEMISTRY                  V.  38  6623 1999              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10350481                                                     
JRNL        DOI    10.1021/BI9901228                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.TAKANO,Y.YAMAGATA,K.YUTANI                                 
REMARK   1  TITL   A GENERAL RULE FOR THE RELATIONSHIP BETWEEN HYDROPHOBIC      
REMARK   1  TITL 2 EFFECT AND CONFORMATIONAL STABILITY OF A PROTEIN: STABILITY  
REMARK   1  TITL 3 AND STRUCTURE OF A SERIES OF HYDROPHOBIC MUTANTS OF HUMAN    
REMARK   1  TITL 4 LYSOZYME                                                     
REMARK   1  REF    J.MOL.BIOL.                   V. 280   749 1998              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.YAMAGATA,M.KUBOTA,Y.SUMIKAWA,J.FUNAHASHI,K.TAKANO,S.FUJII, 
REMARK   1  AUTH 2 K.YUTANI                                                     
REMARK   1  TITL   CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL         
REMARK   1  TITL 2 STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS  
REMARK   1  TITL 3 OF SIX TYR->PHE MUTANTS                                      
REMARK   1  REF    BIOCHEMISTRY                  V.  37  9355 1998              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.TAKANO,Y.YAMAGATA,S.FUJII,K.YUTANI                         
REMARK   1  TITL   CONTRIBUTION OF HYDROPHOBIC EFFECT VALINE MUTANTS TO THE     
REMARK   1  TITL 2 STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY  
REMARK   1  TITL 3 STRUCTURAL 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 4                                                          
REMARK   1  AUTH   K.TAKANO,J.F.FUNAHASIHI,Y.YAMAGATA,S.FUJII,K.YUTANI          
REMARK   1  TITL   CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN 
REMARK   1  TITL 2 TO THE CONFORMATIONAL STABILITY                              
REMARK   1  REF    J.MOL.BIOL.                   V. 274   132 1997              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   J.FUNAHASHI,K.TAKANO,K.OGASAHARA,Y.YAMAGATA,K.YUTANI         
REMARK   1  TITL   THE STRUCTURE, STABILITY, AND FOLDING PROCESS OF             
REMARK   1  TITL 2 AMYLOIDOGENIC MUTANT HUMAN LYSOZYME                          
REMARK   1  REF    J.BIOCHEM.(TOKYO)             V. 120  1216 1996              
REMARK   1  REFN                   ISSN 0021-924X                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   K.TAKANO,K.OGASAWAHA,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)   (%) : 92.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 5866                           
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) : 0.148                           
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            : 1028                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 168                                     
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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.530                           
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 1B5Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE DEPOSITION ID IS D_1000008312.                                   
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) : 283                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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                  : DIFFRACTOMETER                     
REMARK 200  DETECTOR MANUFACTURER          : WEISSENBERG                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6155                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: WILD-TYPE OF HUMAN LYSOZYME                          
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: 1.5M TO 1.8M NACL, 20MM ACETATE, PH      
REMARK 280  4.5                                                                 
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       28.49000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       16.97500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.59500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       16.97500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.49000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.59500            
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 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 272  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  61   O                                                      
REMARK 620 2 CYS A  65   O    82.1                                              
REMARK 620 3 VAL A  74   O   128.2 117.2                                        
REMARK 620 4 HOH A 137   O    69.0  79.4 155.5                                  
REMARK 620 5 HOH A 159   O   132.2 106.0  90.6  66.7                            
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 272                  
DBREF  1B5Y A    1   130  UNP    P61626   LYSC_HUMAN      19    148             
SEQADV 1B5Y ALA A   36  UNP  P61626    SER    54 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 ILE SER LEU ALA          
SEQRES   3 A  130  ASN TRP MET CYS LEU ALA LYS TRP GLU ALA 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 272       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   2   NA    NA 1+                                                        
FORMUL   3  HOH   *168(H2 O)                                                    
HELIX    1   1 ARG A    5  ARG A   14  1                                  10    
HELIX    2   2 TYR A   20  GLY A   22  5                                   3    
HELIX    3   3 LEU A   25  GLU A   35  1                                  11    
HELIX    4   4 CYS A   81  LEU A   85  5                                   5    
HELIX    5   5 ALA A   90  ARG A  101  1                                  12    
HELIX    6   6 GLY A  105  ALA A  108  5                                   4    
HELIX    7   7 VAL A  110  ARG A  115  1                                   6    
HELIX    8   8 ARG A  122  TYR A  124  5                                   3    
SHEET    1   A 2 THR A  43  ASN A  46  0                                        
SHEET    2   A 2 SER A  51  TYR A  54 -1  N  ASP A  53   O  ASN A  44           
SSBOND   1 CYS A    6    CYS A  128                          1555   1555  2.03  
SSBOND   2 CYS A   30    CYS A  116                          1555   1555  2.03  
SSBOND   3 CYS A   65    CYS A   81                          1555   1555  2.04  
SSBOND   4 CYS A   77    CYS A   95                          1555   1555  2.03  
LINK         O   SER A  61                NA    NA A 272     1554   1555  2.04  
LINK         O   CYS A  65                NA    NA A 272     1554   1555  2.22  
LINK         O   VAL A  74                NA    NA A 272     1554   1555  2.18  
LINK         O   HOH A 137                NA    NA A 272     1555   1555  2.79  
LINK         O   HOH A 159                NA    NA A 272     1555   1555  2.15  
SITE     1 AC1  6 SER A  61  CYS A  65  ALA A  73  VAL A  74                    
SITE     2 AC1  6 HOH A 137  HOH A 159                                          
CRYST1   56.980   61.190   33.950  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      0.017550  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016342  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029455        0.00000                         
ATOM      1  N   LYS A   1       1.009  19.533  23.095  1.00  2.00           N  
ATOM      2  CA  LYS A   1       1.626  20.504  22.145  1.00  6.81           C  
ATOM      3  C   LYS A   1       2.871  19.903  21.479  1.00  7.21           C  
ATOM      4  O   LYS A   1       3.680  19.244  22.140  1.00 13.23           O  
ATOM      5  CB  LYS A   1       2.015  21.789  22.898  1.00  5.89           C  
ATOM      6  CG  LYS A   1       2.900  22.744  22.115  1.00 11.63           C  
ATOM      7  CD  LYS A   1       3.329  23.908  22.969  1.00 11.59           C  
ATOM      8  CE  LYS A   1       3.924  24.997  22.126  1.00  4.95           C  
ATOM      9  NZ  LYS A   1       4.249  26.166  22.977  1.00 29.90           N  
ATOM     10  N   VAL A   2       2.986  20.089  20.166  1.00  6.53           N  
ATOM     11  CA  VAL A   2       4.149  19.622  19.411  1.00  8.54           C  
ATOM     12  C   VAL A   2       4.976  20.882  19.098  1.00  7.52           C  
ATOM     13  O   VAL A   2       4.546  21.751  18.331  1.00  7.65           O  
ATOM     14  CB  VAL A   2       3.748  18.877  18.093  1.00  7.17           C  
ATOM     15  CG1 VAL A   2       4.990  18.425  17.325  1.00  8.98           C  
ATOM     16  CG2 VAL A   2       2.915  17.657  18.408  1.00  7.58           C  
ATOM     17  N   PHE A   3       6.106  21.021  19.784  1.00  3.68           N  
ATOM     18  CA  PHE A   3       6.999  22.159  19.611  1.00  5.42           C  
ATOM     19  C   PHE A   3       7.754  22.136  18.296  1.00  4.06           C  
ATOM     20  O   PHE A   3       8.067  21.078  17.763  1.00  3.77           O  
ATOM     21  CB  PHE A   3       8.055  22.166  20.725  1.00  4.48           C  
ATOM     22  CG  PHE A   3       7.612  22.822  21.996  1.00  5.56           C  
ATOM     23  CD1 PHE A   3       6.915  22.101  22.962  1.00  7.11           C  
ATOM     24  CD2 PHE A   3       7.923  24.159  22.249  1.00  2.76           C  
ATOM     25  CE1 PHE A   3       6.544  22.694  24.159  1.00  5.24           C  
ATOM     26  CE2 PHE A   3       7.558  24.757  23.442  1.00  2.00           C  
ATOM     27  CZ  PHE A   3       6.863  24.024  24.400  1.00  3.37           C  
ATOM     28  N   GLU A   4       8.070  23.316  17.786  1.00  2.99           N  
ATOM     29  CA  GLU A   4       8.881  23.413  16.579  1.00  6.39           C  
ATOM     30  C   GLU A   4      10.297  23.400  17.155  1.00  8.97           C  
ATOM     31  O   GLU A   4      10.512  23.857  18.293  1.00  7.80           O  
ATOM     32  CB  GLU A   4       8.640  24.745  15.871  1.00  6.71           C  
ATOM     33  CG  GLU A   4       7.166  25.091  15.653  1.00 43.87           C  
ATOM     34  CD  GLU A   4       6.546  24.501  14.382  1.00 55.39           C  
ATOM     35  OE1 GLU A   4       7.023  23.458  13.876  1.00 55.50           O  
ATOM     36  OE2 GLU A   4       5.553  25.093  13.898  1.00 55.64           O  
ATOM     37  N   ARG A   5      11.263  22.895  16.396  1.00  6.47           N  
ATOM     38  CA  ARG A   5      12.642  22.821  16.884  1.00  5.55           C  
ATOM     39  C   ARG A   5      13.173  24.095  17.571  1.00 10.08           C  
ATOM     40  O   ARG A   5      13.450  24.080  18.764  1.00  7.53           O  
ATOM     41  CB  ARG A   5      13.597  22.419  15.754  1.00  2.00           C  
ATOM     42  CG  ARG A   5      15.033  22.210  16.222  1.00  2.00           C  
ATOM     43  CD  ARG A   5      15.928  21.673  15.111  1.00 10.59           C  
ATOM     44  NE  ARG A   5      16.009  22.601  13.983  1.00  4.64           N  
ATOM     45  CZ  ARG A   5      16.935  23.545  13.852  1.00 17.90           C  
ATOM     46  NH1 ARG A   5      17.868  23.705  14.786  1.00 20.77           N  
ATOM     47  NH2 ARG A   5      16.925  24.338  12.789  1.00  2.97           N  
ATOM     48  N   CYS A   6      13.314  25.186  16.815  1.00  7.54           N  
ATOM     49  CA  CYS A   6      13.842  26.433  17.361  1.00  6.70           C  
ATOM     50  C   CYS A   6      12.970  27.081  18.435  1.00  4.93           C  
ATOM     51  O   CYS A   6      13.487  27.792  19.290  1.00  7.83           O  
ATOM     52  CB  CYS A   6      14.176  27.420  16.249  1.00  9.15           C  
ATOM     53  SG  CYS A   6      15.572  26.866  15.208  1.00  7.34           S  
ATOM     54  N   GLU A   7      11.665  26.810  18.420  1.00  2.17           N  
ATOM     55  CA  GLU A   7      10.772  27.347  19.434  1.00  4.17           C  
ATOM     56  C   GLU A   7      11.153  26.725  20.784  1.00  3.06           C  
ATOM     57  O   GLU A   7      11.269  27.429  21.780  1.00  3.11           O  
ATOM     58  CB  GLU A   7       9.314  27.022  19.116  1.00 11.15           C  
ATOM     59  CG  GLU A   7       8.359  27.566  20.167  1.00 12.14           C  
ATOM     60  CD  GLU A   7       6.941  27.004  20.075  1.00 36.65           C  
ATOM     61  OE1 GLU A   7       6.652  26.135  19.206  1.00  9.17           O  
ATOM     62  OE2 GLU A   7       6.113  27.442  20.909  1.00 21.05           O  
ATOM     63  N   LEU A   8      11.376  25.414  20.800  1.00  2.00           N  
ATOM     64  CA  LEU A   8      11.768  24.689  22.011  1.00  3.53           C  
ATOM     65  C   LEU A   8      13.163  25.106  22.531  1.00  5.50           C  
ATOM     66  O   LEU A   8      13.370  25.257  23.732  1.00  5.49           O  
ATOM     67  CB  LEU A   8      11.730  23.167  21.745  1.00  2.00           C  
ATOM     68  CG  LEU A   8      12.092  22.232  22.916  1.00  2.00           C  
ATOM     69  CD1 LEU A   8      11.100  22.421  24.055  1.00  2.00           C  
ATOM     70  CD2 LEU A   8      12.084  20.795  22.462  1.00  2.00           C  
ATOM     71  N   ALA A   9      14.109  25.311  21.620  1.00  2.95           N  
ATOM     72  CA  ALA A   9      15.457  25.695  21.993  1.00  2.00           C  
ATOM     73  C   ALA A   9      15.461  26.982  22.791  1.00  2.74           C  
ATOM     74  O   ALA A   9      16.095  27.075  23.842  1.00  4.15           O  
ATOM     75  CB  ALA A   9      16.324  25.838  20.736  1.00  2.49           C  
ATOM     76  N   ARG A  10      14.728  27.980  22.308  1.00  5.72           N  
ATOM     77  CA  ARG A  10      14.651  29.260  23.008  1.00  2.97           C  
ATOM     78  C   ARG A  10      13.948  29.119  24.350  1.00  2.00           C  
ATOM     79  O   ARG A  10      14.400  29.680  25.349  1.00  2.00           O  
ATOM     80  CB  ARG A  10      13.986  30.313  22.120  1.00  8.96           C  
ATOM     81  CG  ARG A  10      14.852  30.650  20.932  1.00  5.20           C  
ATOM     82  CD  ARG A  10      14.312  31.855  20.172  1.00 16.62           C  
ATOM     83  NE  ARG A  10      13.070  31.541  19.478  1.00  7.44           N  
ATOM     84  CZ  ARG A  10      13.007  31.051  18.246  1.00  7.13           C  
ATOM     85  NH1 ARG A  10      14.111  30.841  17.539  1.00  4.89           N  
ATOM     86  NH2 ARG A  10      11.828  30.793  17.707  1.00  4.84           N  
ATOM     87  N   THR A  11      12.912  28.280  24.387  1.00  2.00           N  
ATOM     88  CA  THR A  11      12.157  28.035  25.617  1.00  5.96           C  
ATOM     89  C   THR A  11      13.039  27.371  26.678  1.00  4.52           C  
ATOM     90  O   THR A  11      13.070  27.820  27.827  1.00  5.75           O  
ATOM     91  CB  THR A  11      10.872  27.175  25.351  1.00  3.25           C  
ATOM     92  OG1 THR A  11      10.070  27.831  24.360  1.00  5.35           O  
ATOM     93  CG2 THR A  11      10.023  27.030  26.605  1.00  2.00           C  
ATOM     94  N   LEU A  12      13.811  26.360  26.282  1.00  3.23           N  
ATOM     95  CA  LEU A  12      14.663  25.658  27.222  1.00  2.00           C  
ATOM     96  C   LEU A  12      15.765  26.564  27.758  1.00  2.90           C  
ATOM     97  O   LEU A  12      16.132  26.502  28.933  1.00  4.70           O  
ATOM     98  CB  LEU A  12      15.229  24.376  26.593  1.00  2.81           C  
ATOM     99  CG  LEU A  12      14.282  23.177  26.393  1.00  5.54           C  
ATOM    100  CD1 LEU A  12      15.071  22.000  25.863  1.00  2.30           C  
ATOM    101  CD2 LEU A  12      13.598  22.782  27.699  1.00  2.00           C  
ATOM    102  N   LYS A  13      16.263  27.448  26.907  1.00  3.24           N  
ATOM    103  CA  LYS A  13      17.307  28.371  27.312  1.00  2.00           C  
ATOM    104  C   LYS A  13      16.788  29.345  28.364  1.00  2.00           C  
ATOM    105  O   LYS A  13      17.491  29.689  29.309  1.00  7.56           O  
ATOM    106  CB  LYS A  13      17.825  29.157  26.101  1.00  5.02           C  
ATOM    107  CG  LYS A  13      19.004  30.057  26.453  1.00 16.50           C  
ATOM    108  CD  LYS A  13      19.848  30.423  25.259  1.00 25.46           C  
ATOM    109  CE  LYS A  13      21.314  30.606  25.679  1.00 30.75           C  
ATOM    110  NZ  LYS A  13      21.484  31.693  26.673  1.00 27.25           N  
ATOM    111  N   ARG A  14      15.548  29.778  28.213  1.00  2.00           N  
ATOM    112  CA  ARG A  14      14.963  30.736  29.143  1.00  5.69           C  
ATOM    113  C   ARG A  14      14.687  30.085  30.480  1.00  2.42           C  
ATOM    114  O   ARG A  14      14.620  30.753  31.506  1.00  2.00           O  
ATOM    115  CB  ARG A  14      13.684  31.309  28.548  1.00  2.46           C  
ATOM    116  CG  ARG A  14      13.302  32.684  29.016  1.00 14.38           C  
ATOM    117  CD  ARG A  14      12.314  33.291  28.021  1.00 24.39           C  
ATOM    118  NE  ARG A  14      11.252  32.346  27.679  1.00 32.96           N  
ATOM    119  CZ  ARG A  14      10.897  32.010  26.437  1.00 39.02           C  
ATOM    120  NH1 ARG A  14      11.502  32.554  25.379  1.00 30.72           N  
ATOM    121  NH2 ARG A  14       9.917  31.125  26.252  1.00 23.35           N  
ATOM    122  N   LEU A  15      14.558  28.765  30.467  1.00  2.14           N  
ATOM    123  CA  LEU A  15      14.281  28.037  31.691  1.00  4.68           C  
ATOM    124  C   LEU A  15      15.558  27.597  32.412  1.00  5.52           C  
ATOM    125  O   LEU A  15      15.501  26.774  33.326  1.00  5.42           O  
ATOM    126  CB  LEU A  15      13.370  26.836  31.414  1.00  4.66           C  
ATOM    127  CG  LEU A  15      11.971  27.118  30.854  1.00  6.89           C  
ATOM    128  CD1 LEU A  15      11.305  25.809  30.473  1.00  6.64           C  
ATOM    129  CD2 LEU A  15      11.124  27.844  31.873  1.00  7.64           C  
ATOM    130  N   GLY A  16      16.704  28.121  31.976  1.00  3.57           N  
ATOM    131  CA  GLY A  16      17.965  27.801  32.627  1.00  4.76           C  
ATOM    132  C   GLY A  16      18.518  26.405  32.396  1.00  4.91           C  
ATOM    133  O   GLY A  16      19.251  25.869  33.241  1.00  5.88           O  
ATOM    134  N   MET A  17      18.211  25.822  31.244  1.00  2.52           N  
ATOM    135  CA  MET A  17      18.708  24.478  30.939  1.00  4.23           C  
ATOM    136  C   MET A  17      20.098  24.421  30.295  1.00  2.00           C  
ATOM    137  O   MET A  17      20.759  23.384  30.333  1.00  4.28           O  
ATOM    138  CB  MET A  17      17.710  23.762  30.032  1.00  4.45           C  
ATOM    139  CG  MET A  17      16.421  23.456  30.712  1.00  7.87           C  
ATOM    140  SD  MET A  17      16.704  22.108  31.788  1.00 13.67           S  
ATOM    141  CE  MET A  17      15.992  20.752  30.841  1.00 13.01           C  
ATOM    142  N   ASP A  18      20.537  25.514  29.683  1.00  2.05           N  
ATOM    143  CA  ASP A  18      21.838  25.525  29.015  1.00  5.72           C  
ATOM    144  C   ASP A  18      23.010  25.408  30.014  1.00  6.82           C  
ATOM    145  O   ASP A  18      23.234  26.314  30.825  1.00  8.19           O  
ATOM    146  CB  ASP A  18      21.981  26.773  28.125  1.00  7.45           C  
ATOM    147  CG  ASP A  18      23.169  26.674  27.146  1.00 16.01           C  
ATOM    148  OD1 ASP A  18      23.617  25.544  26.843  1.00 13.22           O  
ATOM    149  OD2 ASP A  18      23.659  27.721  26.674  1.00 20.46           O  
ATOM    150  N   GLY A  19      23.683  24.254  29.992  1.00  2.00           N  
ATOM    151  CA  GLY A  19      24.812  24.014  30.871  1.00  2.00           C  
ATOM    152  C   GLY A  19      24.417  23.525  32.251  1.00  8.73           C  
ATOM    153  O   GLY A  19      25.279  23.426  33.136  1.00 13.36           O  
ATOM    154  N   TYR A  20      23.132  23.209  32.446  1.00  5.56           N  
ATOM    155  CA  TYR A  20      22.651  22.731  33.746  1.00  3.99           C  
ATOM    156  C   TYR A  20      23.348  21.431  34.104  1.00  3.22           C  
ATOM    157  O   TYR A  20      23.245  20.438  33.381  1.00  2.00           O  
ATOM    158  CB  TYR A  20      21.135  22.538  33.765  1.00  2.01           C  
ATOM    159  CG  TYR A  20      20.605  22.276  35.153  1.00  2.00           C  
ATOM    160  CD1 TYR A  20      20.400  23.322  36.044  1.00  2.00           C  
ATOM    161  CD2 TYR A  20      20.349  20.980  35.588  1.00  2.61           C  
ATOM    162  CE1 TYR A  20      19.960  23.085  37.337  1.00  6.26           C  
ATOM    163  CE2 TYR A  20      19.902  20.721  36.889  1.00  4.49           C  
ATOM    164  CZ  TYR A  20      19.716  21.777  37.752  1.00  8.71           C  
ATOM    165  OH  TYR A  20      19.313  21.541  39.037  1.00  8.72           O  
ATOM    166  N   ARG A  21      24.073  21.462  35.223  1.00  8.32           N  
ATOM    167  CA  ARG A  21      24.854  20.321  35.711  1.00  2.00           C  
ATOM    168  C   ARG A  21      25.801  19.849  34.621  1.00  4.02           C  
ATOM    169  O   ARG A  21      25.981  18.652  34.412  1.00  6.53           O  
ATOM    170  CB  ARG A  21      23.961  19.175  36.192  1.00  3.89           C  
ATOM    171  CG  ARG A  21      23.091  19.529  37.401  1.00 17.16           C  
ATOM    172  CD  ARG A  21      23.863  19.574  38.713  1.00 18.77           C  
ATOM    173  NE  ARG A  21      24.296  18.232  39.109  1.00 33.01           N  
ATOM    174  CZ  ARG A  21      25.293  17.973  39.954  1.00 24.73           C  
ATOM    175  NH1 ARG A  21      25.966  18.961  40.544  1.00 18.41           N  
ATOM    176  NH2 ARG A  21      25.593  16.714  40.231  1.00 25.89           N  
ATOM    177  N   GLY A  22      26.361  20.810  33.889  1.00  4.33           N  
ATOM    178  CA  GLY A  22      27.296  20.494  32.826  1.00  5.36           C  
ATOM    179  C   GLY A  22      26.693  19.973  31.545  1.00  4.54           C  
ATOM    180  O   GLY A  22      27.433  19.531  30.670  1.00 12.08           O  
ATOM    181  N   ILE A  23      25.368  20.010  31.418  1.00  5.11           N  
ATOM    182  CA  ILE A  23      24.712  19.518  30.207  1.00  2.45           C  
ATOM    183  C   ILE A  23      24.338  20.632  29.241  1.00  2.82           C  
ATOM    184  O   ILE A  23      23.529  21.496  29.569  1.00  5.03           O  
ATOM    185  CB  ILE A  23      23.454  18.756  30.549  1.00  2.00           C  
ATOM    186  CG1 ILE A  23      23.770  17.635  31.530  1.00  2.00           C  
ATOM    187  CG2 ILE A  23      22.833  18.185  29.283  1.00  4.59           C  
ATOM    188  CD1 ILE A  23      22.523  17.068  32.188  1.00  2.00           C  
ATOM    189  N   SER A  24      24.872  20.587  28.028  1.00  2.08           N  
ATOM    190  CA  SER A  24      24.592  21.625  27.034  1.00  2.00           C  
ATOM    191  C   SER A  24      23.161  21.594  26.499  1.00  2.18           C  
ATOM    192  O   SER A  24      22.547  20.530  26.391  1.00  2.00           O  
ATOM    193  CB  SER A  24      25.556  21.509  25.851  1.00  7.90           C  
ATOM    194  OG  SER A  24      25.291  20.330  25.088  1.00  9.37           O  
ATOM    195  N   LEU A  25      22.696  22.754  26.051  1.00  2.00           N  
ATOM    196  CA  LEU A  25      21.347  22.888  25.509  1.00  4.00           C  
ATOM    197  C   LEU A  25      21.090  21.869  24.368  1.00  3.28           C  
ATOM    198  O   LEU A  25      20.062  21.184  24.342  1.00  4.06           O  
ATOM    199  CB  LEU A  25      21.149  24.327  25.018  1.00  3.34           C  
ATOM    200  CG  LEU A  25      19.818  24.777  24.431  1.00  8.07           C  
ATOM    201  CD1 LEU A  25      18.710  24.594  25.466  1.00  5.99           C  
ATOM    202  CD2 LEU A  25      19.947  26.245  24.037  1.00 10.02           C  
ATOM    203  N   ALA A  26      22.044  21.744  23.451  1.00  2.00           N  
ATOM    204  CA  ALA A  26      21.909  20.824  22.335  1.00  2.00           C  
ATOM    205  C   ALA A  26      21.689  19.376  22.767  1.00  4.11           C  
ATOM    206  O   ALA A  26      21.073  18.598  22.030  1.00  3.28           O  
ATOM    207  CB  ALA A  26      23.111  20.928  21.425  1.00  2.32           C  
ATOM    208  N   ASN A  27      22.210  19.002  23.938  1.00  6.04           N  
ATOM    209  CA  ASN A  27      22.023  17.636  24.443  1.00  2.42           C  
ATOM    210  C   ASN A  27      20.593  17.448  24.910  1.00  5.64           C  
ATOM    211  O   ASN A  27      19.990  16.369  24.711  1.00  2.36           O  
ATOM    212  CB  ASN A  27      22.995  17.313  25.574  1.00  2.00           C  
ATOM    213  CG  ASN A  27      24.332  16.831  25.056  1.00 15.57           C  
ATOM    214  OD1 ASN A  27      24.457  15.717  24.512  1.00  4.56           O  
ATOM    215  ND2 ASN A  27      25.344  17.669  25.197  1.00  6.88           N  
ATOM    216  N   TRP A  28      20.036  18.511  25.493  1.00  2.00           N  
ATOM    217  CA  TRP A  28      18.656  18.460  25.952  1.00  3.18           C  
ATOM    218  C   TRP A  28      17.745  18.414  24.720  1.00  6.05           C  
ATOM    219  O   TRP A  28      16.713  17.755  24.749  1.00  6.60           O  
ATOM    220  CB  TRP A  28      18.308  19.674  26.815  1.00  2.00           C  
ATOM    221  CG  TRP A  28      18.938  19.719  28.208  1.00  2.81           C  
ATOM    222  CD1 TRP A  28      19.841  20.632  28.667  1.00  2.00           C  
ATOM    223  CD2 TRP A  28      18.616  18.886  29.332  1.00  2.78           C  
ATOM    224  NE1 TRP A  28      20.086  20.437  29.997  1.00  3.52           N  
ATOM    225  CE2 TRP A  28      19.352  19.368  30.436  1.00  2.18           C  
ATOM    226  CE3 TRP A  28      17.770  17.780  29.517  1.00  2.00           C  
ATOM    227  CZ2 TRP A  28      19.274  18.793  31.706  1.00  4.04           C  
ATOM    228  CZ3 TRP A  28      17.691  17.201  30.793  1.00  2.00           C  
ATOM    229  CH2 TRP A  28      18.439  17.712  31.864  1.00  2.33           C  
ATOM    230  N   MET A  29      18.145  19.080  23.632  1.00  4.52           N  
ATOM    231  CA  MET A  29      17.340  19.078  22.404  1.00  5.54           C  
ATOM    232  C   MET A  29      17.370  17.693  21.760  1.00  6.62           C  
ATOM    233  O   MET A  29      16.351  17.197  21.272  1.00  4.72           O  
ATOM    234  CB  MET A  29      17.846  20.115  21.400  1.00  5.00           C  
ATOM    235  CG  MET A  29      17.514  21.574  21.744  1.00  6.13           C  
ATOM    236  SD  MET A  29      15.754  21.944  21.823  1.00  8.05           S  
ATOM    237  CE  MET A  29      15.251  21.838  20.113  1.00  7.58           C  
ATOM    238  N   CYS A  30      18.546  17.080  21.751  1.00  4.36           N  
ATOM    239  CA  CYS A  30      18.707  15.748  21.191  1.00  4.18           C  
ATOM    240  C   CYS A  30      17.838  14.788  21.987  1.00  6.78           C  
ATOM    241  O   CYS A  30      17.200  13.917  21.408  1.00  5.66           O  
ATOM    242  CB  CYS A  30      20.169  15.316  21.242  1.00  4.69           C  
ATOM    243  SG  CYS A  30      20.488  13.726  20.429  1.00  7.76           S  
ATOM    244  N   LEU A  31      17.825  14.949  23.313  1.00  6.79           N  
ATOM    245  CA  LEU A  31      17.014  14.106  24.179  1.00  6.58           C  
ATOM    246  C   LEU A  31      15.505  14.227  23.885  1.00  6.67           C  
ATOM    247  O   LEU A  31      14.843  13.216  23.656  1.00  4.73           O  
ATOM    248  CB  LEU A  31      17.273  14.429  25.654  1.00  7.16           C  
ATOM    249  CG  LEU A  31      16.515  13.532  26.648  1.00  5.62           C  
ATOM    250  CD1 LEU A  31      17.054  12.086  26.604  1.00  2.00           C  
ATOM    251  CD2 LEU A  31      16.667  14.112  28.038  1.00  8.25           C  
ATOM    252  N   ALA A  32      14.958  15.447  23.941  1.00  2.00           N  
ATOM    253  CA  ALA A  32      13.538  15.688  23.662  1.00  2.00           C  
ATOM    254  C   ALA A  32      13.114  15.149  22.284  1.00  4.12           C  
ATOM    255  O   ALA A  32      12.001  14.631  22.113  1.00  4.56           O  
ATOM    256  CB  ALA A  32      13.242  17.169  23.735  1.00  2.00           C  
ATOM    257  N   LYS A  33      13.999  15.315  21.305  1.00  2.00           N  
ATOM    258  CA  LYS A  33      13.781  14.860  19.932  1.00  5.36           C  
ATOM    259  C   LYS A  33      13.552  13.342  19.813  1.00 11.18           C  
ATOM    260  O   LYS A  33      12.603  12.908  19.145  1.00 10.78           O  
ATOM    261  CB  LYS A  33      14.978  15.268  19.064  1.00 13.89           C  
ATOM    262  CG  LYS A  33      15.202  14.427  17.808  1.00 25.49           C  
ATOM    263  CD  LYS A  33      14.163  14.657  16.725  1.00 30.91           C  
ATOM    264  CE  LYS A  33      14.516  13.875  15.450  1.00 20.05           C  
ATOM    265  NZ  LYS A  33      14.416  12.397  15.610  1.00 27.09           N  
ATOM    266  N   TRP A  34      14.436  12.544  20.415  1.00  6.89           N  
ATOM    267  CA  TRP A  34      14.329  11.081  20.363  1.00  6.02           C  
ATOM    268  C   TRP A  34      13.407  10.495  21.426  1.00  6.61           C  
ATOM    269  O   TRP A  34      12.956   9.366  21.295  1.00  8.49           O  
ATOM    270  CB  TRP A  34      15.722  10.435  20.442  1.00  7.22           C  
ATOM    271  CG  TRP A  34      16.535  10.725  19.230  1.00  6.88           C  
ATOM    272  CD1 TRP A  34      17.528  11.652  19.109  1.00  8.29           C  
ATOM    273  CD2 TRP A  34      16.331  10.184  17.925  1.00  8.53           C  
ATOM    274  NE1 TRP A  34      17.940  11.738  17.807  1.00  6.80           N  
ATOM    275  CE2 TRP A  34      17.224  10.844  17.054  1.00  9.55           C  
ATOM    276  CE3 TRP A  34      15.476   9.196  17.401  1.00 11.50           C  
ATOM    277  CZ2 TRP A  34      17.287  10.560  15.684  1.00 10.78           C  
ATOM    278  CZ3 TRP A  34      15.537   8.913  16.029  1.00 13.12           C  
ATOM    279  CH2 TRP A  34      16.440   9.595  15.192  1.00 12.06           C  
ATOM    280  N   GLU A  35      13.137  11.241  22.488  1.00  2.43           N  
ATOM    281  CA  GLU A  35      12.244  10.711  23.505  1.00  4.45           C  
ATOM    282  C   GLU A  35      10.786  10.809  23.066  1.00  7.09           C  
ATOM    283  O   GLU A  35      10.071   9.815  23.074  1.00  9.44           O  
ATOM    284  CB  GLU A  35      12.432  11.405  24.866  1.00  9.51           C  
ATOM    285  CG  GLU A  35      13.708  11.021  25.642  1.00  2.00           C  
ATOM    286  CD  GLU A  35      13.809   9.542  26.014  1.00  6.92           C  
ATOM    287  OE1 GLU A  35      12.797   8.809  25.957  1.00 10.44           O  
ATOM    288  OE2 GLU A  35      14.918   9.105  26.392  1.00 13.03           O  
ATOM    289  N   ALA A  36      10.367  11.985  22.609  1.00 12.12           N  
ATOM    290  CA  ALA A  36       8.976  12.150  22.221  1.00 11.01           C  
ATOM    291  C   ALA A  36       8.702  12.929  20.943  1.00  7.96           C  
ATOM    292  O   ALA A  36       7.554  13.088  20.547  1.00 12.25           O  
ATOM    293  CB  ALA A  36       8.206  12.781  23.378  1.00 10.94           C  
ATOM    294  N   GLY A  37       9.742  13.404  20.286  1.00  6.41           N  
ATOM    295  CA  GLY A  37       9.538  14.164  19.072  1.00  2.56           C  
ATOM    296  C   GLY A  37       8.999  15.555  19.348  1.00  4.19           C  
ATOM    297  O   GLY A  37       8.202  16.084  18.580  1.00 12.17           O  
ATOM    298  N   TYR A  38       9.428  16.156  20.447  1.00  2.00           N  
ATOM    299  CA  TYR A  38       8.993  17.516  20.801  1.00  2.96           C  
ATOM    300  C   TYR A  38       7.486  17.587  21.102  1.00  3.67           C  
ATOM    301  O   TYR A  38       6.880  18.658  21.074  1.00  2.04           O  
ATOM    302  CB  TYR A  38       9.338  18.507  19.687  1.00  4.32           C  
ATOM    303  CG  TYR A  38      10.769  18.488  19.161  1.00  6.75           C  
ATOM    304  CD1 TYR A  38      11.864  18.289  20.007  1.00  9.33           C  
ATOM    305  CD2 TYR A  38      11.026  18.703  17.809  1.00  7.77           C  
ATOM    306  CE1 TYR A  38      13.167  18.307  19.512  1.00  2.96           C  
ATOM    307  CE2 TYR A  38      12.319  18.720  17.305  1.00 11.18           C  
ATOM    308  CZ  TYR A  38      13.378  18.521  18.164  1.00  4.06           C  
ATOM    309  OH  TYR A  38      14.645  18.526  17.652  1.00  2.00           O  
ATOM    310  N   ASN A  39       6.917  16.449  21.477  1.00  5.18           N  
ATOM    311  CA  ASN A  39       5.504  16.335  21.801  1.00  9.01           C  
ATOM    312  C   ASN A  39       5.300  16.223  23.318  1.00  5.24           C  
ATOM    313  O   ASN A  39       5.738  15.253  23.932  1.00  6.55           O  
ATOM    314  CB  ASN A  39       4.953  15.088  21.109  1.00 14.36           C  
ATOM    315  CG  ASN A  39       3.467  14.910  21.311  1.00 11.82           C  
ATOM    316  OD1 ASN A  39       2.801  15.746  21.933  1.00  9.02           O  
ATOM    317  ND2 ASN A  39       2.939  13.817  20.806  1.00  9.97           N  
ATOM    318  N   THR A  40       4.608  17.194  23.912  1.00  4.22           N  
ATOM    319  CA  THR A  40       4.369  17.207  25.354  1.00  3.82           C  
ATOM    320  C   THR A  40       3.344  16.184  25.865  1.00  6.69           C  
ATOM    321  O   THR A  40       3.344  15.860  27.044  1.00  6.02           O  
ATOM    322  CB  THR A  40       3.913  18.622  25.852  1.00  2.00           C  
ATOM    323  OG1 THR A  40       2.624  18.941  25.309  1.00  5.14           O  
ATOM    324  CG2 THR A  40       4.907  19.707  25.421  1.00  2.06           C  
ATOM    325  N   ARG A  41       2.451  15.695  25.007  1.00  6.56           N  
ATOM    326  CA  ARG A  41       1.435  14.746  25.480  1.00 12.97           C  
ATOM    327  C   ARG A  41       1.768  13.267  25.307  1.00 12.08           C  
ATOM    328  O   ARG A  41       0.950  12.404  25.618  1.00 13.31           O  
ATOM    329  CB  ARG A  41       0.068  15.042  24.849  1.00 17.86           C  
ATOM    330  CG  ARG A  41      -0.015  14.782  23.360  1.00 29.22           C  
ATOM    331  CD  ARG A  41      -1.132  13.798  23.003  1.00 42.24           C  
ATOM    332  NE  ARG A  41      -2.453  14.231  23.463  1.00 46.44           N  
ATOM    333  CZ  ARG A  41      -3.526  13.439  23.521  1.00 41.25           C  
ATOM    334  NH1 ARG A  41      -3.455  12.166  23.140  1.00 39.03           N  
ATOM    335  NH2 ARG A  41      -4.663  13.908  24.024  1.00 50.28           N  
ATOM    336  N   ALA A  42       2.980  12.976  24.851  1.00  9.27           N  
ATOM    337  CA  ALA A  42       3.388  11.607  24.623  1.00  9.13           C  
ATOM    338  C   ALA A  42       3.521  10.807  25.908  1.00  9.14           C  
ATOM    339  O   ALA A  42       4.096  11.268  26.895  1.00  2.00           O  
ATOM    340  CB  ALA A  42       4.688  11.578  23.851  1.00  7.49           C  
ATOM    341  N   THR A  43       2.947   9.613  25.902  1.00 11.54           N  
ATOM    342  CA  THR A  43       3.035   8.720  27.045  1.00 14.79           C  
ATOM    343  C   THR A  43       3.403   7.363  26.486  1.00 12.51           C  
ATOM    344  O   THR A  43       3.101   7.047  25.335  1.00 15.31           O  
ATOM    345  CB  THR A  43       1.714   8.613  27.841  1.00  7.39           C  
ATOM    346  OG1 THR A  43       0.646   8.211  26.977  1.00 17.83           O  
ATOM    347  CG2 THR A  43       1.380   9.927  28.485  1.00  3.67           C  
ATOM    348  N   ASN A  44       4.089   6.567  27.283  1.00 11.06           N  
ATOM    349  CA  ASN A  44       4.469   5.258  26.805  1.00 11.62           C  
ATOM    350  C   ASN A  44       4.456   4.272  27.937  1.00  6.45           C  
ATOM    351  O   ASN A  44       5.238   4.393  28.882  1.00  7.67           O  
ATOM    352  CB  ASN A  44       5.846   5.315  26.172  1.00 11.00           C  
ATOM    353  CG  ASN A  44       6.162   4.073  25.406  1.00 39.38           C  
ATOM    354  OD1 ASN A  44       5.783   3.939  24.240  1.00 57.33           O  
ATOM    355  ND2 ASN A  44       6.847   3.136  26.048  1.00 29.45           N  
ATOM    356  N   TYR A  45       3.551   3.307  27.846  1.00  9.08           N  
ATOM    357  CA  TYR A  45       3.404   2.285  28.868  1.00  6.85           C  
ATOM    358  C   TYR A  45       4.388   1.143  28.661  1.00  8.50           C  
ATOM    359  O   TYR A  45       4.495   0.600  27.573  1.00 12.74           O  
ATOM    360  CB  TYR A  45       1.980   1.748  28.860  1.00  7.50           C  
ATOM    361  CG  TYR A  45       1.751   0.642  29.859  1.00 10.94           C  
ATOM    362  CD1 TYR A  45       1.776   0.908  31.230  1.00  9.68           C  
ATOM    363  CD2 TYR A  45       1.512  -0.668  29.435  1.00 11.87           C  
ATOM    364  CE1 TYR A  45       1.567  -0.097  32.159  1.00 14.60           C  
ATOM    365  CE2 TYR A  45       1.298  -1.690  30.359  1.00 12.33           C  
ATOM    366  CZ  TYR A  45       1.328  -1.393  31.717  1.00 17.07           C  
ATOM    367  OH  TYR A  45       1.123  -2.376  32.644  1.00 20.23           O  
ATOM    368  N   ASN A  46       5.072   0.756  29.729  1.00 11.60           N  
ATOM    369  CA  ASN A  46       6.058  -0.325  29.689  1.00 11.58           C  
ATOM    370  C   ASN A  46       5.421  -1.525  30.372  1.00 12.71           C  
ATOM    371  O   ASN A  46       5.512  -1.678  31.596  1.00 15.34           O  
ATOM    372  CB  ASN A  46       7.318   0.087  30.448  1.00  8.37           C  
ATOM    373  CG  ASN A  46       7.846   1.446  30.008  1.00 38.75           C  
ATOM    374  OD1 ASN A  46       8.542   1.554  28.993  1.00 42.02           O  
ATOM    375  ND2 ASN A  46       7.497   2.496  30.757  1.00 24.29           N  
ATOM    376  N   ALA A  47       4.757  -2.357  29.577  1.00 15.99           N  
ATOM    377  CA  ALA A  47       4.050  -3.541  30.081  1.00 18.32           C  
ATOM    378  C   ALA A  47       4.917  -4.485  30.911  1.00 16.62           C  
ATOM    379  O   ALA A  47       4.407  -5.193  31.781  1.00 10.36           O  
ATOM    380  CB  ALA A  47       3.389  -4.298  28.934  1.00 18.96           C  
ATOM    381  N   GLY A  48       6.223  -4.445  30.662  1.00 18.91           N  
ATOM    382  CA  GLY A  48       7.159  -5.278  31.389  1.00 19.15           C  
ATOM    383  C   GLY A  48       7.299  -4.997  32.878  1.00 17.52           C  
ATOM    384  O   GLY A  48       7.496  -5.937  33.636  1.00 15.46           O  
ATOM    385  N   ASP A  49       7.265  -3.731  33.302  1.00 18.19           N  
ATOM    386  CA  ASP A  49       7.391  -3.411  34.733  1.00 14.74           C  
ATOM    387  C   ASP A  49       6.256  -2.556  35.295  1.00 14.54           C  
ATOM    388  O   ASP A  49       6.338  -2.091  36.426  1.00 16.20           O  
ATOM    389  CB  ASP A  49       8.747  -2.776  35.060  1.00 10.90           C  
ATOM    390  CG  ASP A  49       8.845  -1.313  34.638  1.00 17.90           C  
ATOM    391  OD1 ASP A  49       8.202  -0.918  33.650  1.00 22.77           O  
ATOM    392  OD2 ASP A  49       9.576  -0.552  35.304  1.00 25.09           O  
ATOM    393  N   ARG A  50       5.224  -2.335  34.477  1.00 14.92           N  
ATOM    394  CA  ARG A  50       4.014  -1.582  34.843  1.00 11.52           C  
ATOM    395  C   ARG A  50       4.145  -0.094  35.131  1.00  9.83           C  
ATOM    396  O   ARG A  50       3.318   0.490  35.845  1.00 11.44           O  
ATOM    397  CB  ARG A  50       3.277  -2.303  35.967  1.00 14.21           C  
ATOM    398  CG  ARG A  50       2.964  -3.743  35.566  1.00 15.45           C  
ATOM    399  CD  ARG A  50       2.101  -4.475  36.553  1.00 23.48           C  
ATOM    400  NE  ARG A  50       1.302  -5.483  35.849  1.00 45.48           N  
ATOM    401  CZ  ARG A  50       0.744  -6.541  36.431  1.00 44.99           C  
ATOM    402  NH1 ARG A  50       0.918  -6.756  37.732  1.00 57.52           N  
ATOM    403  NH2 ARG A  50       0.036  -7.402  35.712  1.00 30.12           N  
ATOM    404  N   SER A  51       5.156   0.523  34.533  1.00  6.52           N  
ATOM    405  CA  SER A  51       5.384   1.946  34.699  1.00  9.98           C  
ATOM    406  C   SER A  51       5.096   2.639  33.370  1.00  9.14           C  
ATOM    407  O   SER A  51       4.982   1.984  32.335  1.00  6.14           O  
ATOM    408  CB  SER A  51       6.821   2.223  35.169  1.00 14.31           C  
ATOM    409  OG  SER A  51       7.780   1.796  34.208  1.00 13.24           O  
ATOM    410  N   THR A  52       4.974   3.962  33.406  1.00 12.43           N  
ATOM    411  CA  THR A  52       4.677   4.742  32.212  1.00  7.07           C  
ATOM    412  C   THR A  52       5.596   5.960  32.178  1.00  4.37           C  
ATOM    413  O   THR A  52       5.954   6.503  33.224  1.00  6.80           O  
ATOM    414  CB  THR A  52       3.164   5.177  32.207  1.00  5.37           C  
ATOM    415  OG1 THR A  52       2.334   4.008  32.246  1.00  9.70           O  
ATOM    416  CG2 THR A  52       2.798   5.969  30.963  1.00  2.00           C  
ATOM    417  N   ASP A  53       6.087   6.276  30.983  1.00  4.53           N  
ATOM    418  CA  ASP A  53       6.964   7.419  30.741  1.00  4.07           C  
ATOM    419  C   ASP A  53       6.046   8.539  30.297  1.00  2.00           C  
ATOM    420  O   ASP A  53       5.259   8.356  29.369  1.00  3.93           O  
ATOM    421  CB  ASP A  53       7.929   7.084  29.610  1.00  6.67           C  
ATOM    422  CG  ASP A  53       8.816   5.915  29.939  1.00  6.29           C  
ATOM    423  OD1 ASP A  53       9.358   5.912  31.056  1.00 15.57           O  
ATOM    424  OD2 ASP A  53       8.959   4.992  29.102  1.00 14.91           O  
ATOM    425  N   TYR A  54       6.192   9.712  30.889  1.00  2.00           N  
ATOM    426  CA  TYR A  54       5.317  10.834  30.581  1.00  2.00           C  
ATOM    427  C   TYR A  54       5.952  12.099  30.046  1.00  3.13           C  
ATOM    428  O   TYR A  54       6.939  12.590  30.592  1.00  2.00           O  
ATOM    429  CB  TYR A  54       4.530  11.249  31.831  1.00  5.34           C  
ATOM    430  CG  TYR A  54       3.573  10.207  32.392  1.00  7.45           C  
ATOM    431  CD1 TYR A  54       4.012   9.237  33.308  1.00  7.64           C  
ATOM    432  CD2 TYR A  54       2.215  10.237  32.065  1.00  5.94           C  
ATOM    433  CE1 TYR A  54       3.115   8.336  33.892  1.00  7.32           C  
ATOM    434  CE2 TYR A  54       1.313   9.342  32.637  1.00  5.56           C  
ATOM    435  CZ  TYR A  54       1.767   8.395  33.550  1.00  5.29           C  
ATOM    436  OH  TYR A  54       0.873   7.509  34.117  1.00  8.80           O  
ATOM    437  N   GLY A  55       5.357  12.632  28.982  1.00  2.00           N  
ATOM    438  CA  GLY A  55       5.800  13.899  28.425  1.00  2.00           C  
ATOM    439  C   GLY A  55       6.962  14.023  27.463  1.00  6.34           C  
ATOM    440  O   GLY A  55       7.505  13.040  26.924  1.00  4.48           O  
ATOM    441  N   ILE A  56       7.383  15.272  27.314  1.00  2.00           N  
ATOM    442  CA  ILE A  56       8.456  15.628  26.411  1.00  3.16           C  
ATOM    443  C   ILE A  56       9.821  14.979  26.736  1.00  4.40           C  
ATOM    444  O   ILE A  56      10.580  14.639  25.816  1.00  8.21           O  
ATOM    445  CB  ILE A  56       8.497  17.192  26.210  1.00  2.98           C  
ATOM    446  CG1 ILE A  56       9.313  17.546  24.964  1.00 16.75           C  
ATOM    447  CG2 ILE A  56       9.037  17.915  27.450  1.00  2.00           C  
ATOM    448  CD1 ILE A  56       9.215  19.001  24.565  1.00 17.69           C  
ATOM    449  N   PHE A  57      10.109  14.743  28.019  1.00  3.18           N  
ATOM    450  CA  PHE A  57      11.382  14.109  28.404  1.00  2.00           C  
ATOM    451  C   PHE A  57      11.150  12.652  28.752  1.00  2.00           C  
ATOM    452  O   PHE A  57      12.063  11.970  29.192  1.00  2.24           O  
ATOM    453  CB  PHE A  57      12.047  14.832  29.590  1.00  2.00           C  
ATOM    454  CG  PHE A  57      12.496  16.230  29.268  1.00  4.46           C  
ATOM    455  CD1 PHE A  57      13.355  16.467  28.197  1.00  4.64           C  
ATOM    456  CD2 PHE A  57      11.998  17.320  29.982  1.00  4.87           C  
ATOM    457  CE1 PHE A  57      13.698  17.768  27.836  1.00  7.28           C  
ATOM    458  CE2 PHE A  57      12.335  18.621  29.636  1.00  2.72           C  
ATOM    459  CZ  PHE A  57      13.192  18.846  28.555  1.00  5.75           C  
ATOM    460  N   GLN A  58       9.916  12.190  28.543  1.00  2.00           N  
ATOM    461  CA  GLN A  58       9.515  10.812  28.833  1.00  2.38           C  
ATOM    462  C   GLN A  58      10.031  10.337  30.183  1.00  5.52           C  
ATOM    463  O   GLN A  58      10.780   9.351  30.276  1.00  6.97           O  
ATOM    464  CB  GLN A  58       9.975   9.874  27.722  1.00  5.14           C  
ATOM    465  CG  GLN A  58       9.158  10.011  26.443  1.00  7.68           C  
ATOM    466  CD  GLN A  58       7.775   9.420  26.580  1.00  2.00           C  
ATOM    467  OE1 GLN A  58       7.572   8.236  26.352  1.00  2.00           O  
ATOM    468  NE2 GLN A  58       6.819  10.243  26.946  1.00  4.01           N  
ATOM    469  N   ILE A  59       9.597  11.045  31.223  1.00  4.90           N  
ATOM    470  CA  ILE A  59       9.991  10.768  32.597  1.00  7.68           C  
ATOM    471  C   ILE A  59       9.191   9.598  33.180  1.00  6.17           C  
ATOM    472  O   ILE A  59       7.986   9.507  32.971  1.00  2.15           O  
ATOM    473  CB  ILE A  59       9.900  12.070  33.421  1.00  7.09           C  
ATOM    474  CG1 ILE A  59      11.054  12.991  33.000  1.00  4.07           C  
ATOM    475  CG2 ILE A  59       9.929  11.788  34.888  1.00  7.10           C  
ATOM    476  CD1 ILE A  59      10.900  14.405  33.442  1.00  3.57           C  
ATOM    477  N   ASN A  60       9.878   8.716  33.908  1.00  4.83           N  
ATOM    478  CA  ASN A  60       9.279   7.499  34.473  1.00  6.48           C  
ATOM    479  C   ASN A  60       8.545   7.608  35.826  1.00  4.37           C  
ATOM    480  O   ASN A  60       9.065   8.156  36.803  1.00  2.12           O  
ATOM    481  CB  ASN A  60      10.355   6.403  34.522  1.00  4.40           C  
ATOM    482  CG  ASN A  60       9.776   5.007  34.653  1.00  4.59           C  
ATOM    483  OD1 ASN A  60       9.673   4.473  35.750  1.00  9.97           O  
ATOM    484  ND2 ASN A  60       9.469   4.381  33.525  1.00 11.43           N  
ATOM    485  N   SER A  61       7.351   7.020  35.881  1.00  7.45           N  
ATOM    486  CA  SER A  61       6.502   7.045  37.069  1.00  8.16           C  
ATOM    487  C   SER A  61       7.003   6.236  38.258  1.00 14.34           C  
ATOM    488  O   SER A  61       6.465   6.364  39.359  1.00 12.24           O  
ATOM    489  CB  SER A  61       5.096   6.580  36.708  1.00  2.00           C  
ATOM    490  OG  SER A  61       5.115   5.229  36.291  1.00  2.00           O  
ATOM    491  N   ARG A  62       8.013   5.394  38.045  1.00 19.23           N  
ATOM    492  CA  ARG A  62       8.544   4.574  39.130  1.00 14.55           C  
ATOM    493  C   ARG A  62       9.383   5.353  40.124  1.00  8.06           C  
ATOM    494  O   ARG A  62       9.377   5.041  41.312  1.00  8.54           O  
ATOM    495  CB  ARG A  62       9.369   3.394  38.595  1.00 14.16           C  
ATOM    496  CG  ARG A  62       9.950   2.516  39.706  1.00 12.72           C  
ATOM    497  CD  ARG A  62      10.327   1.140  39.192  1.00 32.44           C  
ATOM    498  NE  ARG A  62       9.166   0.497  38.595  1.00 42.03           N  
ATOM    499  CZ  ARG A  62       8.246  -0.170  39.284  1.00 30.03           C  
ATOM    500  NH1 ARG A  62       8.395  -0.345  40.589  1.00 27.17           N  
ATOM    501  NH2 ARG A  62       7.203  -0.705  38.655  1.00 16.70           N  
ATOM    502  N   TYR A  63      10.070   6.389  39.653  1.00  7.84           N  
ATOM    503  CA  TYR A  63      10.943   7.168  40.522  1.00  9.93           C  
ATOM    504  C   TYR A  63      10.628   8.640  40.631  1.00 10.90           C  
ATOM    505  O   TYR A  63      10.790   9.223  41.697  1.00 14.46           O  
ATOM    506  CB  TYR A  63      12.407   7.077  40.045  1.00 14.75           C  
ATOM    507  CG  TYR A  63      12.846   5.695  39.607  1.00 24.60           C  
ATOM    508  CD1 TYR A  63      13.318   4.757  40.540  1.00 28.15           C  
ATOM    509  CD2 TYR A  63      12.710   5.284  38.268  1.00 27.05           C  
ATOM    510  CE1 TYR A  63      13.630   3.440  40.154  1.00 23.87           C  
ATOM    511  CE2 TYR A  63      13.023   3.967  37.874  1.00 22.35           C  
ATOM    512  CZ  TYR A  63      13.475   3.059  38.825  1.00 27.86           C  
ATOM    513  OH  TYR A  63      13.746   1.761  38.457  1.00 58.18           O  
ATOM    514  N   TRP A  64      10.165   9.243  39.539  1.00  6.79           N  
ATOM    515  CA  TRP A  64       9.970  10.688  39.504  1.00  3.92           C  
ATOM    516  C   TRP A  64       8.617  11.314  39.700  1.00  3.40           C  
ATOM    517  O   TRP A  64       8.530  12.400  40.241  1.00  3.88           O  
ATOM    518  CB  TRP A  64      10.600  11.218  38.225  1.00  5.59           C  
ATOM    519  CG  TRP A  64      11.910  10.557  37.986  1.00  6.72           C  
ATOM    520  CD1 TRP A  64      12.164   9.517  37.130  1.00  9.31           C  
ATOM    521  CD2 TRP A  64      13.129  10.801  38.692  1.00  6.70           C  
ATOM    522  NE1 TRP A  64      13.458   9.094  37.265  1.00  9.94           N  
ATOM    523  CE2 TRP A  64      14.084   9.871  38.220  1.00  9.83           C  
ATOM    524  CE3 TRP A  64      13.516  11.725  39.675  1.00  7.79           C  
ATOM    525  CZ2 TRP A  64      15.403   9.824  38.698  1.00  8.28           C  
ATOM    526  CZ3 TRP A  64      14.824  11.683  40.153  1.00  9.83           C  
ATOM    527  CH2 TRP A  64      15.753  10.735  39.659  1.00  9.18           C  
ATOM    528  N   CYS A  65       7.569  10.694  39.188  1.00  3.89           N  
ATOM    529  CA  CYS A  65       6.262  11.280  39.373  1.00  6.45           C  
ATOM    530  C   CYS A  65       5.295  10.204  39.817  1.00  8.05           C  
ATOM    531  O   CYS A  65       5.568   9.003  39.665  1.00  6.43           O  
ATOM    532  CB  CYS A  65       5.769  11.974  38.092  1.00  3.84           C  
ATOM    533  SG  CYS A  65       5.446  10.871  36.692  1.00  5.89           S  
ATOM    534  N   ASN A  66       4.184  10.644  40.398  1.00  7.24           N  
ATOM    535  CA  ASN A  66       3.148   9.743  40.893  1.00 10.00           C  
ATOM    536  C   ASN A  66       1.887   9.626  40.020  1.00 10.10           C  
ATOM    537  O   ASN A  66       1.240  10.632  39.713  1.00  6.59           O  
ATOM    538  CB  ASN A  66       2.734  10.181  42.307  1.00 14.67           C  
ATOM    539  CG  ASN A  66       1.669   9.288  42.899  1.00  7.97           C  
ATOM    540  OD1 ASN A  66       1.797   8.064  42.869  1.00 11.66           O  
ATOM    541  ND2 ASN A  66       0.609   9.885  43.424  1.00  9.37           N  
ATOM    542  N   ASP A  67       1.550   8.404  39.610  1.00  6.24           N  
ATOM    543  CA  ASP A  67       0.325   8.178  38.847  1.00  6.65           C  
ATOM    544  C   ASP A  67      -0.566   7.178  39.586  1.00  2.04           C  
ATOM    545  O   ASP A  67      -1.570   6.725  39.068  1.00  3.51           O  
ATOM    546  CB  ASP A  67       0.583   7.767  37.378  1.00  8.94           C  
ATOM    547  CG  ASP A  67       1.365   6.468  37.231  1.00 10.67           C  
ATOM    548  OD1 ASP A  67       1.644   5.783  38.236  1.00 11.11           O  
ATOM    549  OD2 ASP A  67       1.698   6.125  36.076  1.00  5.48           O  
ATOM    550  N   GLY A  68      -0.175   6.834  40.808  1.00  4.55           N  
ATOM    551  CA  GLY A  68      -0.963   5.915  41.627  1.00  7.39           C  
ATOM    552  C   GLY A  68      -1.123   4.443  41.241  1.00 14.54           C  
ATOM    553  O   GLY A  68      -1.644   3.664  42.038  1.00 18.16           O  
ATOM    554  N   LYS A  69      -0.719   4.039  40.041  1.00 17.08           N  
ATOM    555  CA  LYS A  69      -0.859   2.636  39.656  1.00 13.59           C  
ATOM    556  C   LYS A  69       0.457   1.902  39.414  1.00 11.83           C  
ATOM    557  O   LYS A  69       0.441   0.767  38.958  1.00 15.02           O  
ATOM    558  CB  LYS A  69      -1.765   2.495  38.426  1.00  8.16           C  
ATOM    559  CG  LYS A  69      -1.405   3.375  37.241  1.00  8.51           C  
ATOM    560  CD  LYS A  69      -2.126   2.905  35.983  1.00 10.18           C  
ATOM    561  CE  LYS A  69      -1.960   3.864  34.802  1.00 16.97           C  
ATOM    562  NZ  LYS A  69      -0.538   4.034  34.398  1.00 42.45           N  
ATOM    563  N   THR A  70       1.592   2.541  39.685  1.00 10.17           N  
ATOM    564  CA  THR A  70       2.888   1.888  39.486  1.00 10.44           C  
ATOM    565  C   THR A  70       3.368   1.343  40.825  1.00 12.34           C  
ATOM    566  O   THR A  70       3.523   2.087  41.794  1.00 11.80           O  
ATOM    567  CB  THR A  70       3.967   2.850  38.924  1.00 15.01           C  
ATOM    568  OG1 THR A  70       3.500   3.454  37.707  1.00 10.68           O  
ATOM    569  CG2 THR A  70       5.271   2.096  38.645  1.00  6.83           C  
ATOM    570  N   PRO A  71       3.605   0.028  40.895  1.00 13.47           N  
ATOM    571  CA  PRO A  71       4.062  -0.672  42.096  1.00 13.61           C  
ATOM    572  C   PRO A  71       5.345  -0.126  42.702  1.00 13.98           C  
ATOM    573  O   PRO A  71       6.300   0.154  41.986  1.00 14.14           O  
ATOM    574  CB  PRO A  71       4.279  -2.103  41.593  1.00 13.67           C  
ATOM    575  CG  PRO A  71       3.298  -2.241  40.489  1.00 14.53           C  
ATOM    576  CD  PRO A  71       3.441  -0.909  39.773  1.00 15.83           C  
ATOM    577  N   GLY A  72       5.349   0.011  44.025  1.00 19.28           N  
ATOM    578  CA  GLY A  72       6.521   0.476  44.755  1.00 19.82           C  
ATOM    579  C   GLY A  72       7.235   1.671  44.154  1.00 23.90           C  
ATOM    580  O   GLY A  72       8.465   1.758  44.164  1.00 24.81           O  
ATOM    581  N   ALA A  73       6.454   2.603  43.634  1.00 22.91           N  
ATOM    582  CA  ALA A  73       7.014   3.782  43.021  1.00 20.21           C  
ATOM    583  C   ALA A  73       7.229   4.868  44.052  1.00 19.30           C  
ATOM    584  O   ALA A  73       6.626   4.852  45.132  1.00 18.01           O  
ATOM    585  CB  ALA A  73       6.088   4.286  41.935  1.00 19.47           C  
ATOM    586  N   VAL A  74       8.150   5.768  43.732  1.00 16.75           N  
ATOM    587  CA  VAL A  74       8.420   6.929  44.561  1.00 18.91           C  
ATOM    588  C   VAL A  74       8.103   8.145  43.687  1.00 15.91           C  
ATOM    589  O   VAL A  74       7.875   8.027  42.468  1.00 16.72           O  
ATOM    590  CB  VAL A  74       9.865   6.973  45.158  1.00 20.93           C  
ATOM    591  CG1 VAL A  74      10.050   5.826  46.141  1.00 23.08           C  
ATOM    592  CG2 VAL A  74      10.923   6.917  44.078  1.00 21.77           C  
ATOM    593  N   ASN A  75       8.088   9.307  44.310  1.00 11.23           N  
ATOM    594  CA  ASN A  75       7.743  10.529  43.627  1.00 13.35           C  
ATOM    595  C   ASN A  75       8.790  11.596  43.990  1.00 11.35           C  
ATOM    596  O   ASN A  75       8.482  12.575  44.669  1.00  8.30           O  
ATOM    597  CB  ASN A  75       6.326  10.887  44.109  1.00 15.50           C  
ATOM    598  CG  ASN A  75       5.804  12.171  43.535  1.00  5.51           C  
ATOM    599  OD1 ASN A  75       6.315  12.689  42.538  1.00  5.22           O  
ATOM    600  ND2 ASN A  75       4.764  12.706  44.170  1.00  7.65           N  
ATOM    601  N   ALA A  76      10.018  11.411  43.504  1.00 10.21           N  
ATOM    602  CA  ALA A  76      11.116  12.338  43.799  1.00 13.24           C  
ATOM    603  C   ALA A  76      10.871  13.763  43.343  1.00 12.01           C  
ATOM    604  O   ALA A  76      11.306  14.706  44.002  1.00 11.74           O  
ATOM    605  CB  ALA A  76      12.455  11.822  43.228  1.00 14.98           C  
ATOM    606  N   CYS A  77      10.178  13.940  42.226  1.00 10.42           N  
ATOM    607  CA  CYS A  77       9.901  15.292  41.757  1.00  8.76           C  
ATOM    608  C   CYS A  77       8.741  15.935  42.513  1.00 12.39           C  
ATOM    609  O   CYS A  77       8.461  17.121  42.330  1.00 13.01           O  
ATOM    610  CB  CYS A  77       9.618  15.299  40.262  1.00  7.76           C  
ATOM    611  SG  CYS A  77      11.087  15.002  39.249  1.00  6.23           S  
ATOM    612  N   HIS A  78       8.089  15.149  43.372  1.00 15.66           N  
ATOM    613  CA  HIS A  78       6.939  15.595  44.159  1.00 19.25           C  
ATOM    614  C   HIS A  78       5.872  16.192  43.260  1.00 14.04           C  
ATOM    615  O   HIS A  78       5.387  17.300  43.493  1.00 13.92           O  
ATOM    616  CB  HIS A  78       7.371  16.579  45.244  1.00 25.93           C  
ATOM    617  CG  HIS A  78       8.411  16.017  46.163  1.00 37.40           C  
ATOM    618  ND1 HIS A  78       9.581  16.678  46.471  1.00 43.60           N  
ATOM    619  CD2 HIS A  78       8.497  14.803  46.765  1.00 42.46           C  
ATOM    620  CE1 HIS A  78      10.348  15.902  47.210  1.00 45.17           C  
ATOM    621  NE2 HIS A  78       9.711  14.752  47.406  1.00 44.63           N  
ATOM    622  N   LEU A  79       5.499  15.426  42.240  1.00  8.07           N  
ATOM    623  CA  LEU A  79       4.492  15.855  41.266  1.00 12.70           C  
ATOM    624  C   LEU A  79       3.613  14.696  40.846  1.00  9.18           C  
ATOM    625  O   LEU A  79       3.957  13.522  41.025  1.00  7.56           O  
ATOM    626  CB  LEU A  79       5.148  16.374  39.962  1.00 13.09           C  
ATOM    627  CG  LEU A  79       5.965  17.660  39.818  1.00 15.71           C  
ATOM    628  CD1 LEU A  79       6.637  17.655  38.460  1.00 12.14           C  
ATOM    629  CD2 LEU A  79       5.082  18.893  39.963  1.00  6.27           C  
ATOM    630  N   SER A  80       2.456  15.059  40.311  1.00  9.91           N  
ATOM    631  CA  SER A  80       1.515  14.102  39.735  1.00  6.87           C  
ATOM    632  C   SER A  80       2.078  13.982  38.317  1.00  7.24           C  
ATOM    633  O   SER A  80       2.579  14.979  37.761  1.00  8.97           O  
ATOM    634  CB  SER A  80       0.122  14.726  39.641  1.00  5.61           C  
ATOM    635  OG  SER A  80      -0.749  13.964  38.822  1.00  7.80           O  
ATOM    636  N   CYS A  81       2.043  12.784  37.744  1.00  7.47           N  
ATOM    637  CA  CYS A  81       2.532  12.598  36.384  1.00  4.09           C  
ATOM    638  C   CYS A  81       1.716  13.450  35.408  1.00  3.28           C  
ATOM    639  O   CYS A  81       2.208  13.825  34.338  1.00  2.79           O  
ATOM    640  CB  CYS A  81       2.472  11.131  36.001  1.00  5.04           C  
ATOM    641  SG  CYS A  81       3.576  10.119  37.028  1.00  5.83           S  
ATOM    642  N   SER A  82       0.483  13.787  35.789  1.00  2.00           N  
ATOM    643  CA  SER A  82      -0.364  14.631  34.938  1.00  5.74           C  
ATOM    644  C   SER A  82       0.302  15.967  34.602  1.00  5.04           C  
ATOM    645  O   SER A  82       0.105  16.499  33.513  1.00  5.12           O  
ATOM    646  CB  SER A  82      -1.717  14.927  35.604  1.00  8.64           C  
ATOM    647  OG  SER A  82      -2.548  15.719  34.753  1.00 12.86           O  
ATOM    648  N   ALA A  83       1.080  16.506  35.535  1.00  2.00           N  
ATOM    649  CA  ALA A  83       1.745  17.788  35.352  1.00  2.00           C  
ATOM    650  C   ALA A  83       2.726  17.772  34.208  1.00  3.06           C  
ATOM    651  O   ALA A  83       3.033  18.825  33.632  1.00  5.55           O  
ATOM    652  CB  ALA A  83       2.459  18.209  36.647  1.00  2.00           C  
ATOM    653  N   LEU A  84       3.208  16.579  33.870  1.00  2.00           N  
ATOM    654  CA  LEU A  84       4.180  16.425  32.804  1.00  3.30           C  
ATOM    655  C   LEU A  84       3.531  16.238  31.448  1.00  6.49           C  
ATOM    656  O   LEU A  84       4.202  15.849  30.488  1.00  8.68           O  
ATOM    657  CB  LEU A  84       5.107  15.246  33.108  1.00  5.36           C  
ATOM    658  CG  LEU A  84       5.830  15.256  34.454  1.00  5.61           C  
ATOM    659  CD1 LEU A  84       6.651  13.997  34.576  1.00  6.01           C  
ATOM    660  CD2 LEU A  84       6.689  16.486  34.620  1.00  7.49           C  
ATOM    661  N   LEU A  85       2.229  16.501  31.361  1.00  6.43           N  
ATOM    662  CA  LEU A  85       1.506  16.377  30.098  1.00  3.57           C  
ATOM    663  C   LEU A  85       0.900  17.716  29.670  1.00  2.94           C  
ATOM    664  O   LEU A  85       0.133  17.768  28.712  1.00  5.61           O  
ATOM    665  CB  LEU A  85       0.414  15.308  30.213  1.00  2.70           C  
ATOM    666  CG  LEU A  85       0.916  13.871  30.462  1.00  3.93           C  
ATOM    667  CD1 LEU A  85      -0.247  12.950  30.701  1.00  2.00           C  
ATOM    668  CD2 LEU A  85       1.744  13.404  29.280  1.00  2.00           C  
ATOM    669  N   GLN A  86       1.237  18.791  30.382  1.00  2.00           N  
ATOM    670  CA  GLN A  86       0.713  20.127  30.047  1.00  4.60           C  
ATOM    671  C   GLN A  86       1.462  20.705  28.851  1.00  7.68           C  
ATOM    672  O   GLN A  86       2.537  20.215  28.492  1.00  9.01           O  
ATOM    673  CB  GLN A  86       0.904  21.092  31.216  1.00  6.90           C  
ATOM    674  CG  GLN A  86       0.367  20.628  32.573  1.00 10.24           C  
ATOM    675  CD  GLN A  86       0.761  21.605  33.686  1.00 12.50           C  
ATOM    676  OE1 GLN A  86       0.215  22.703  33.781  1.00 12.72           O  
ATOM    677  NE2 GLN A  86       1.752  21.231  34.487  1.00 11.94           N  
ATOM    678  N   ASP A  87       0.918  21.763  28.254  1.00  6.23           N  
ATOM    679  CA  ASP A  87       1.569  22.410  27.115  1.00  3.13           C  
ATOM    680  C   ASP A  87       2.733  23.249  27.643  1.00  6.18           C  
ATOM    681  O   ASP A  87       3.726  23.483  26.926  1.00  8.63           O  
ATOM    682  CB  ASP A  87       0.595  23.324  26.372  1.00  6.07           C  
ATOM    683  CG  ASP A  87      -0.337  22.571  25.443  1.00  9.36           C  
ATOM    684  OD1 ASP A  87      -0.198  21.338  25.274  1.00 12.33           O  
ATOM    685  OD2 ASP A  87      -1.215  23.233  24.856  1.00 20.08           O  
ATOM    686  N   ASN A  88       2.561  23.772  28.857  1.00  2.00           N  
ATOM    687  CA  ASN A  88       3.587  24.574  29.517  1.00  3.77           C  
ATOM    688  C   ASN A  88       4.582  23.596  30.129  1.00  7.24           C  
ATOM    689  O   ASN A  88       4.242  22.877  31.070  1.00  7.62           O  
ATOM    690  CB  ASN A  88       2.987  25.457  30.623  1.00 10.43           C  
ATOM    691  CG  ASN A  88       4.032  26.378  31.275  1.00 22.95           C  
ATOM    692  OD1 ASN A  88       4.978  25.916  31.906  1.00 18.09           O  
ATOM    693  ND2 ASN A  88       3.869  27.681  31.101  1.00 27.82           N  
ATOM    694  N   ILE A  89       5.813  23.591  29.625  1.00  6.36           N  
ATOM    695  CA  ILE A  89       6.831  22.653  30.107  1.00  8.86           C  
ATOM    696  C   ILE A  89       7.634  22.998  31.382  1.00  7.64           C  
ATOM    697  O   ILE A  89       8.544  22.255  31.756  1.00  9.47           O  
ATOM    698  CB  ILE A  89       7.786  22.237  28.950  1.00  7.55           C  
ATOM    699  CG1 ILE A  89       8.612  23.433  28.451  1.00  7.08           C  
ATOM    700  CG2 ILE A  89       6.964  21.665  27.800  1.00  7.58           C  
ATOM    701  CD1 ILE A  89       9.649  23.055  27.369  1.00 10.18           C  
ATOM    702  N   ALA A  90       7.234  24.040  32.103  1.00  7.01           N  
ATOM    703  CA  ALA A  90       7.925  24.446  33.337  1.00  4.61           C  
ATOM    704  C   ALA A  90       8.136  23.343  34.381  1.00  5.73           C  
ATOM    705  O   ALA A  90       9.247  23.184  34.902  1.00  6.67           O  
ATOM    706  CB  ALA A  90       7.224  25.611  33.965  1.00  3.12           C  
ATOM    707  N   ASP A  91       7.091  22.580  34.701  1.00  8.62           N  
ATOM    708  CA  ASP A  91       7.239  21.515  35.694  1.00  8.65           C  
ATOM    709  C   ASP A  91       8.091  20.367  35.169  1.00 11.31           C  
ATOM    710  O   ASP A  91       8.887  19.807  35.916  1.00 17.35           O  
ATOM    711  CB  ASP A  91       5.888  20.976  36.163  1.00  2.42           C  
ATOM    712  CG  ASP A  91       5.072  22.008  36.916  1.00  9.89           C  
ATOM    713  OD1 ASP A  91       5.637  22.714  37.769  1.00 21.57           O  
ATOM    714  OD2 ASP A  91       3.851  22.094  36.668  1.00 13.90           O  
ATOM    715  N   ALA A  92       7.907  20.007  33.898  1.00  7.94           N  
ATOM    716  CA  ALA A  92       8.677  18.924  33.277  1.00  8.66           C  
ATOM    717  C   ALA A  92      10.176  19.249  33.322  1.00 12.64           C  
ATOM    718  O   ALA A  92      11.012  18.361  33.543  1.00 12.64           O  
ATOM    719  CB  ALA A  92       8.228  18.714  31.833  1.00  6.35           C  
ATOM    720  N   VAL A  93      10.508  20.520  33.095  1.00  9.62           N  
ATOM    721  CA  VAL A  93      11.891  20.969  33.127  1.00  5.30           C  
ATOM    722  C   VAL A  93      12.420  20.927  34.562  1.00  5.82           C  
ATOM    723  O   VAL A  93      13.554  20.516  34.785  1.00  6.76           O  
ATOM    724  CB  VAL A  93      12.051  22.393  32.547  1.00  4.41           C  
ATOM    725  CG1 VAL A  93      13.394  22.975  32.967  1.00  5.27           C  
ATOM    726  CG2 VAL A  93      11.953  22.353  31.036  1.00  2.00           C  
ATOM    727  N   ALA A  94      11.611  21.372  35.523  1.00  5.59           N  
ATOM    728  CA  ALA A  94      12.005  21.341  36.927  1.00  5.03           C  
ATOM    729  C   ALA A  94      12.256  19.880  37.320  1.00  3.23           C  
ATOM    730  O   ALA A  94      13.198  19.571  38.042  1.00  4.46           O  
ATOM    731  CB  ALA A  94      10.906  21.922  37.790  1.00  5.46           C  
ATOM    732  N   CYS A  95      11.430  18.968  36.823  1.00  2.00           N  
ATOM    733  CA  CYS A  95      11.613  17.557  37.148  1.00  2.00           C  
ATOM    734  C   CYS A  95      12.839  16.977  36.414  1.00  4.45           C  
ATOM    735  O   CYS A  95      13.599  16.202  37.000  1.00  9.19           O  
ATOM    736  CB  CYS A  95      10.329  16.762  36.885  1.00  2.00           C  
ATOM    737  SG  CYS A  95      10.391  14.989  37.343  1.00  5.14           S  
ATOM    738  N   ALA A  96      13.073  17.390  35.170  1.00  2.00           N  
ATOM    739  CA  ALA A  96      14.245  16.916  34.438  1.00  2.00           C  
ATOM    740  C   ALA A  96      15.527  17.359  35.170  1.00  3.77           C  
ATOM    741  O   ALA A  96      16.487  16.593  35.246  1.00  6.55           O  
ATOM    742  CB  ALA A  96      14.235  17.458  33.040  1.00  2.96           C  
ATOM    743  N   LYS A  97      15.546  18.586  35.702  1.00  2.00           N  
ATOM    744  CA  LYS A  97      16.706  19.092  36.451  1.00  2.00           C  
ATOM    745  C   LYS A  97      17.015  18.187  37.658  1.00  8.11           C  
ATOM    746  O   LYS A  97      18.179  17.914  37.973  1.00  7.36           O  
ATOM    747  CB  LYS A  97      16.465  20.526  36.937  1.00  2.00           C  
ATOM    748  CG  LYS A  97      16.450  21.588  35.824  1.00  5.53           C  
ATOM    749  CD  LYS A  97      16.198  22.977  36.366  1.00  2.00           C  
ATOM    750  CE  LYS A  97      16.292  23.983  35.273  1.00  2.00           C  
ATOM    751  NZ  LYS A  97      16.061  25.362  35.754  1.00  2.00           N  
ATOM    752  N   ARG A  98      15.955  17.704  38.306  1.00 10.43           N  
ATOM    753  CA  ARG A  98      16.063  16.803  39.459  1.00  4.44           C  
ATOM    754  C   ARG A  98      16.712  15.485  39.052  1.00  4.50           C  
ATOM    755  O   ARG A  98      17.647  15.031  39.694  1.00  9.66           O  
ATOM    756  CB  ARG A  98      14.663  16.544  40.035  1.00  9.64           C  
ATOM    757  CG  ARG A  98      14.569  15.462  41.094  1.00 12.93           C  
ATOM    758  CD  ARG A  98      15.254  15.849  42.387  1.00 27.96           C  
ATOM    759  NE  ARG A  98      15.289  14.721  43.309  1.00 33.89           N  
ATOM    760  CZ  ARG A  98      16.183  13.735  43.258  1.00 33.38           C  
ATOM    761  NH1 ARG A  98      17.158  13.731  42.342  1.00 24.31           N  
ATOM    762  NH2 ARG A  98      16.115  12.753  44.141  1.00 20.91           N  
ATOM    763  N   VAL A  99      16.205  14.872  37.994  1.00  2.25           N  
ATOM    764  CA  VAL A  99      16.751  13.616  37.497  1.00  5.31           C  
ATOM    765  C   VAL A  99      18.270  13.653  37.301  1.00  8.92           C  
ATOM    766  O   VAL A  99      18.950  12.711  37.693  1.00  9.47           O  
ATOM    767  CB  VAL A  99      16.138  13.224  36.144  1.00  3.67           C  
ATOM    768  CG1 VAL A  99      16.762  11.884  35.628  1.00  3.59           C  
ATOM    769  CG2 VAL A  99      14.625  13.116  36.289  1.00  2.15           C  
ATOM    770  N   VAL A 100      18.793  14.714  36.681  1.00  3.49           N  
ATOM    771  CA  VAL A 100      20.232  14.827  36.445  1.00  2.00           C  
ATOM    772  C   VAL A 100      21.067  15.236  37.667  1.00  9.83           C  
ATOM    773  O   VAL A 100      22.293  15.327  37.586  1.00  6.87           O  
ATOM    774  CB  VAL A 100      20.568  15.740  35.251  1.00  2.00           C  
ATOM    775  CG1 VAL A 100      19.937  15.192  33.971  1.00  2.00           C  
ATOM    776  CG2 VAL A 100      20.169  17.190  35.542  1.00  2.38           C  
ATOM    777  N   ARG A 101      20.405  15.501  38.788  1.00 10.53           N  
ATOM    778  CA  ARG A 101      21.119  15.842  40.008  1.00 12.11           C  
ATOM    779  C   ARG A 101      21.642  14.530  40.643  1.00 21.92           C  
ATOM    780  O   ARG A 101      22.429  14.554  41.605  1.00 29.39           O  
ATOM    781  CB  ARG A 101      20.217  16.611  40.963  1.00 14.31           C  
ATOM    782  CG  ARG A 101      20.600  18.062  41.129  1.00 14.89           C  
ATOM    783  CD  ARG A 101      19.641  18.771  42.080  1.00  9.13           C  
ATOM    784  NE  ARG A 101      18.753  19.638  41.331  1.00 36.70           N  
ATOM    785  CZ  ARG A 101      17.439  19.731  41.510  1.00 22.02           C  
ATOM    786  NH1 ARG A 101      16.819  19.022  42.437  1.00 13.06           N  
ATOM    787  NH2 ARG A 101      16.738  20.556  40.748  1.00 30.53           N  
ATOM    788  N   ASP A 102      21.194  13.395  40.105  1.00 15.16           N  
ATOM    789  CA  ASP A 102      21.642  12.070  40.542  1.00 12.55           C  
ATOM    790  C   ASP A 102      22.964  11.804  39.815  1.00 13.85           C  
ATOM    791  O   ASP A 102      23.214  12.386  38.768  1.00 11.58           O  
ATOM    792  CB  ASP A 102      20.640  10.996  40.127  1.00 14.82           C  
ATOM    793  CG  ASP A 102      19.603  10.706  41.188  1.00 25.83           C  
ATOM    794  OD1 ASP A 102      19.236  11.628  41.957  1.00 30.33           O  
ATOM    795  OD2 ASP A 102      19.134   9.546  41.234  1.00 32.84           O  
ATOM    796  N   PRO A 103      23.792  10.881  40.334  1.00 18.58           N  
ATOM    797  CA  PRO A 103      25.092  10.506  39.758  1.00 19.82           C  
ATOM    798  C   PRO A 103      25.185  10.243  38.264  1.00 18.17           C  
ATOM    799  O   PRO A 103      26.132  10.674  37.618  1.00 20.51           O  
ATOM    800  CB  PRO A 103      25.505   9.278  40.586  1.00 22.72           C  
ATOM    801  CG  PRO A 103      24.235   8.818  41.255  1.00 23.69           C  
ATOM    802  CD  PRO A 103      23.575  10.134  41.581  1.00 21.43           C  
ATOM    803  N   GLN A 104      24.229   9.501  37.715  1.00 17.08           N  
ATOM    804  CA  GLN A 104      24.232   9.188  36.286  1.00 15.62           C  
ATOM    805  C   GLN A 104      24.105  10.410  35.387  1.00 13.41           C  
ATOM    806  O   GLN A 104      24.496  10.367  34.210  1.00 14.47           O  
ATOM    807  CB  GLN A 104      23.076   8.259  35.936  1.00 20.06           C  
ATOM    808  CG  GLN A 104      23.208   6.848  36.393  1.00 22.84           C  
ATOM    809  CD  GLN A 104      22.134   6.016  35.771  1.00 35.87           C  
ATOM    810  OE1 GLN A 104      21.024   5.935  36.294  1.00 43.05           O  
ATOM    811  NE2 GLN A 104      22.419   5.462  34.599  1.00 25.58           N  
ATOM    812  N   GLY A 105      23.442  11.441  35.904  1.00 10.28           N  
ATOM    813  CA  GLY A 105      23.244  12.652  35.134  1.00  5.32           C  
ATOM    814  C   GLY A 105      22.351  12.394  33.936  1.00  5.01           C  
ATOM    815  O   GLY A 105      21.318  11.722  34.037  1.00  3.43           O  
ATOM    816  N   ILE A 106      22.779  12.900  32.787  1.00 14.89           N  
ATOM    817  CA  ILE A 106      22.042  12.758  31.535  1.00 14.57           C  
ATOM    818  C   ILE A 106      21.928  11.295  31.066  1.00 14.48           C  
ATOM    819  O   ILE A 106      20.998  10.942  30.343  1.00 12.72           O  
ATOM    820  CB  ILE A 106      22.709  13.636  30.444  1.00 16.48           C  
ATOM    821  CG1 ILE A 106      21.918  13.584  29.135  1.00 20.90           C  
ATOM    822  CG2 ILE A 106      24.188  13.272  30.284  1.00 13.39           C  
ATOM    823  CD1 ILE A 106      20.673  14.471  29.119  1.00 10.50           C  
ATOM    824  N   ARG A 107      22.853  10.440  31.501  1.00 14.12           N  
ATOM    825  CA  ARG A 107      22.845   9.023  31.121  1.00  8.13           C  
ATOM    826  C   ARG A 107      21.662   8.227  31.657  1.00 10.75           C  
ATOM    827  O   ARG A 107      21.488   7.067  31.300  1.00  9.58           O  
ATOM    828  CB  ARG A 107      24.152   8.349  31.544  1.00  8.38           C  
ATOM    829  CG  ARG A 107      25.354   8.813  30.723  1.00  7.42           C  
ATOM    830  CD  ARG A 107      26.681   8.478  31.405  1.00 25.48           C  
ATOM    831  NE  ARG A 107      27.810   8.564  30.478  1.00 17.40           N  
ATOM    832  CZ  ARG A 107      28.282   9.695  29.956  1.00 20.36           C  
ATOM    833  NH1 ARG A 107      27.774  10.874  30.305  1.00 13.46           N  
ATOM    834  NH2 ARG A 107      29.301   9.643  29.104  1.00 10.63           N  
ATOM    835  N   ALA A 108      20.858   8.841  32.525  1.00 13.97           N  
ATOM    836  CA  ALA A 108      19.676   8.168  33.087  1.00 12.56           C  
ATOM    837  C   ALA A 108      18.695   7.730  31.980  1.00 15.84           C  
ATOM    838  O   ALA A 108      17.875   6.826  32.178  1.00 18.10           O  
ATOM    839  CB  ALA A 108      18.979   9.078  34.081  1.00 10.70           C  
ATOM    840  N   TRP A 109      18.766   8.398  30.829  1.00 15.53           N  
ATOM    841  CA  TRP A 109      17.923   8.079  29.677  1.00 11.99           C  
ATOM    842  C   TRP A 109      18.751   7.265  28.695  1.00 10.20           C  
ATOM    843  O   TRP A 109      19.755   7.752  28.165  1.00  8.64           O  
ATOM    844  CB  TRP A 109      17.449   9.358  28.988  1.00 10.54           C  
ATOM    845  CG  TRP A 109      16.384  10.122  29.734  1.00 11.20           C  
ATOM    846  CD1 TRP A 109      15.036   9.876  29.714  1.00 11.62           C  
ATOM    847  CD2 TRP A 109      16.563  11.315  30.513  1.00  8.22           C  
ATOM    848  NE1 TRP A 109      14.365  10.851  30.411  1.00 11.23           N  
ATOM    849  CE2 TRP A 109      15.269  11.748  30.913  1.00  8.69           C  
ATOM    850  CE3 TRP A 109      17.678  12.068  30.902  1.00  5.60           C  
ATOM    851  CZ2 TRP A 109      15.068  12.905  31.679  1.00  3.83           C  
ATOM    852  CZ3 TRP A 109      17.482  13.214  31.663  1.00  5.68           C  
ATOM    853  CH2 TRP A 109      16.179  13.623  32.042  1.00  6.52           C  
ATOM    854  N   VAL A 110      18.324   6.037  28.426  1.00 11.87           N  
ATOM    855  CA  VAL A 110      19.069   5.191  27.505  1.00 13.43           C  
ATOM    856  C   VAL A 110      19.097   5.738  26.081  1.00 13.59           C  
ATOM    857  O   VAL A 110      20.134   5.673  25.413  1.00 18.69           O  
ATOM    858  CB  VAL A 110      18.582   3.710  27.517  1.00 12.76           C  
ATOM    859  CG1 VAL A 110      19.423   2.876  26.552  1.00  9.62           C  
ATOM    860  CG2 VAL A 110      18.737   3.127  28.916  1.00 13.40           C  
ATOM    861  N   ALA A 111      18.002   6.335  25.626  1.00  9.86           N  
ATOM    862  CA  ALA A 111      17.987   6.875  24.266  1.00  8.37           C  
ATOM    863  C   ALA A 111      19.086   7.927  24.055  1.00  9.72           C  
ATOM    864  O   ALA A 111      19.596   8.064  22.940  1.00  8.82           O  
ATOM    865  CB  ALA A 111      16.609   7.450  23.916  1.00  6.71           C  
ATOM    866  N   TRP A 112      19.466   8.648  25.117  1.00  9.93           N  
ATOM    867  CA  TRP A 112      20.525   9.662  25.008  1.00  8.77           C  
ATOM    868  C   TRP A 112      21.838   8.980  24.636  1.00  8.99           C  
ATOM    869  O   TRP A 112      22.577   9.455  23.773  1.00 12.46           O  
ATOM    870  CB  TRP A 112      20.697  10.470  26.301  1.00  6.85           C  
ATOM    871  CG  TRP A 112      21.794  11.498  26.199  1.00  6.43           C  
ATOM    872  CD1 TRP A 112      21.705  12.731  25.620  1.00  5.21           C  
ATOM    873  CD2 TRP A 112      23.167  11.344  26.610  1.00  6.81           C  
ATOM    874  NE1 TRP A 112      22.940  13.345  25.623  1.00  4.97           N  
ATOM    875  CE2 TRP A 112      23.851  12.521  26.221  1.00  7.62           C  
ATOM    876  CE3 TRP A 112      23.883  10.323  27.259  1.00  3.75           C  
ATOM    877  CZ2 TRP A 112      25.228  12.707  26.456  1.00  5.28           C  
ATOM    878  CZ3 TRP A 112      25.251  10.504  27.494  1.00  3.77           C  
ATOM    879  CH2 TRP A 112      25.906  11.690  27.091  1.00  3.44           C  
ATOM    880  N   ARG A 113      22.112   7.858  25.289  1.00  9.46           N  
ATOM    881  CA  ARG A 113      23.307   7.083  25.015  1.00  3.94           C  
ATOM    882  C   ARG A 113      23.306   6.552  23.590  1.00  4.80           C  
ATOM    883  O   ARG A 113      24.321   6.604  22.927  1.00  5.30           O  
ATOM    884  CB  ARG A 113      23.412   5.909  25.983  1.00  3.55           C  
ATOM    885  CG  ARG A 113      23.930   6.318  27.345  1.00  7.72           C  
ATOM    886  CD  ARG A 113      23.041   5.835  28.446  1.00 26.00           C  
ATOM    887  NE  ARG A 113      23.207   4.415  28.702  1.00 30.38           N  
ATOM    888  CZ  ARG A 113      22.807   3.815  29.824  1.00 46.75           C  
ATOM    889  NH1 ARG A 113      22.254   4.525  30.802  1.00 35.83           N  
ATOM    890  NH2 ARG A 113      22.987   2.508  29.987  1.00 24.88           N  
ATOM    891  N   ASN A 114      22.159   6.068  23.122  1.00  8.15           N  
ATOM    892  CA  ASN A 114      22.052   5.495  21.775  1.00  4.72           C  
ATOM    893  C   ASN A 114      22.123   6.481  20.632  1.00  8.73           C  
ATOM    894  O   ASN A 114      22.764   6.198  19.620  1.00  7.95           O  
ATOM    895  CB  ASN A 114      20.743   4.705  21.609  1.00 12.60           C  
ATOM    896  CG  ASN A 114      20.624   3.557  22.577  1.00 14.48           C  
ATOM    897  OD1 ASN A 114      21.622   3.010  23.016  1.00 19.90           O  
ATOM    898  ND2 ASN A 114      19.399   3.206  22.944  1.00 19.41           N  
ATOM    899  N   ARG A 115      21.436   7.617  20.772  1.00 10.68           N  
ATOM    900  CA  ARG A 115      21.367   8.613  19.692  1.00  9.40           C  
ATOM    901  C   ARG A 115      22.029   9.957  19.859  1.00  2.96           C  
ATOM    902  O   ARG A 115      22.025  10.730  18.912  1.00  8.18           O  
ATOM    903  CB  ARG A 115      19.914   8.876  19.277  1.00 12.29           C  
ATOM    904  CG  ARG A 115      18.849   8.118  20.046  1.00 11.92           C  
ATOM    905  CD  ARG A 115      18.585   6.745  19.450  1.00 26.97           C  
ATOM    906  NE  ARG A 115      18.357   6.804  18.008  1.00 27.26           N  
ATOM    907  CZ  ARG A 115      17.644   5.918  17.315  1.00 19.18           C  
ATOM    908  NH1 ARG A 115      17.034   4.914  17.923  1.00 26.74           N  
ATOM    909  NH2 ARG A 115      17.515   6.056  16.008  1.00 11.00           N  
ATOM    910  N   CYS A 116      22.550  10.269  21.045  1.00  4.52           N  
ATOM    911  CA  CYS A 116      23.197  11.580  21.275  1.00  7.77           C  
ATOM    912  C   CYS A 116      24.659  11.544  21.744  1.00  9.78           C  
ATOM    913  O   CYS A 116      25.455  12.376  21.327  1.00  9.39           O  
ATOM    914  CB  CYS A 116      22.425  12.391  22.313  1.00  7.61           C  
ATOM    915  SG  CYS A 116      20.639  12.475  22.023  1.00  7.62           S  
ATOM    916  N   GLN A 117      24.991  10.622  22.646  1.00  7.37           N  
ATOM    917  CA  GLN A 117      26.353  10.531  23.186  1.00  7.64           C  
ATOM    918  C   GLN A 117      27.434  10.367  22.101  1.00  7.52           C  
ATOM    919  O   GLN A 117      27.291   9.558  21.185  1.00  2.00           O  
ATOM    920  CB  GLN A 117      26.421   9.400  24.208  1.00 10.53           C  
ATOM    921  CG  GLN A 117      27.755   9.280  24.927  1.00  6.82           C  
ATOM    922  CD  GLN A 117      27.840   8.093  25.875  1.00 14.77           C  
ATOM    923  OE1 GLN A 117      28.916   7.776  26.362  1.00 25.98           O  
ATOM    924  NE2 GLN A 117      26.712   7.456  26.166  1.00 18.23           N  
ATOM    925  N   ASN A 118      28.490  11.175  22.183  1.00 13.10           N  
ATOM    926  CA  ASN A 118      29.595  11.125  21.212  1.00 16.77           C  
ATOM    927  C   ASN A 118      29.168  11.478  19.784  1.00 13.13           C  
ATOM    928  O   ASN A 118      29.851  11.138  18.819  1.00 13.90           O  
ATOM    929  CB  ASN A 118      30.286   9.740  21.196  1.00 19.24           C  
ATOM    930  CG  ASN A 118      30.901   9.368  22.533  1.00 28.89           C  
ATOM    931  OD1 ASN A 118      31.006   8.179  22.871  1.00 29.87           O  
ATOM    932  ND2 ASN A 118      31.347  10.371  23.286  1.00 34.74           N  
ATOM    933  N   ARG A 119      28.028  12.131  19.630  1.00 13.18           N  
ATOM    934  CA  ARG A 119      27.613  12.511  18.293  1.00  9.35           C  
ATOM    935  C   ARG A 119      27.664  14.008  18.114  1.00 11.67           C  
ATOM    936  O   ARG A 119      27.918  14.758  19.057  1.00 15.09           O  
ATOM    937  CB  ARG A 119      26.230  11.970  17.958  1.00  2.00           C  
ATOM    938  CG  ARG A 119      26.189  10.471  17.935  1.00 12.00           C  
ATOM    939  CD  ARG A 119      24.849  10.028  17.464  1.00 10.46           C  
ATOM    940  NE  ARG A 119      24.604   8.629  17.781  1.00 11.06           N  
ATOM    941  CZ  ARG A 119      24.386   7.691  16.869  1.00 27.78           C  
ATOM    942  NH1 ARG A 119      24.419   7.994  15.577  1.00 13.75           N  
ATOM    943  NH2 ARG A 119      24.149   6.443  17.248  1.00 42.15           N  
ATOM    944  N   ASP A 120      27.542  14.431  16.867  1.00 13.58           N  
ATOM    945  CA  ASP A 120      27.553  15.846  16.542  1.00 14.64           C  
ATOM    946  C   ASP A 120      26.128  16.321  16.775  1.00 12.17           C  
ATOM    947  O   ASP A 120      25.283  16.185  15.898  1.00 14.71           O  
ATOM    948  CB  ASP A 120      27.947  16.047  15.072  1.00 20.03           C  
ATOM    949  CG  ASP A 120      28.152  17.508  14.710  1.00 22.05           C  
ATOM    950  OD1 ASP A 120      27.859  18.407  15.533  1.00 18.61           O  
ATOM    951  OD2 ASP A 120      28.615  17.748  13.574  1.00 20.39           O  
ATOM    952  N   VAL A 121      25.869  16.883  17.949  1.00 10.91           N  
ATOM    953  CA  VAL A 121      24.528  17.359  18.265  1.00  9.74           C  
ATOM    954  C   VAL A 121      24.289  18.843  17.939  1.00 11.17           C  
ATOM    955  O   VAL A 121      23.251  19.406  18.318  1.00  5.47           O  
ATOM    956  CB  VAL A 121      24.150  17.069  19.744  1.00  6.79           C  
ATOM    957  CG1 VAL A 121      24.182  15.540  20.013  1.00  9.15           C  
ATOM    958  CG2 VAL A 121      25.093  17.807  20.690  1.00  4.60           C  
ATOM    959  N   ARG A 122      25.251  19.471  17.256  1.00  9.53           N  
ATOM    960  CA  ARG A 122      25.125  20.892  16.897  1.00 15.68           C  
ATOM    961  C   ARG A 122      23.890  21.177  16.050  1.00 12.44           C  
ATOM    962  O   ARG A 122      23.234  22.208  16.181  1.00 10.59           O  
ATOM    963  CB  ARG A 122      26.368  21.373  16.141  1.00 23.58           C  
ATOM    964  CG  ARG A 122      27.547  21.704  17.046  1.00 28.75           C  
ATOM    965  CD  ARG A 122      28.816  21.832  16.194  1.00 43.56           C  
ATOM    966  NE  ARG A 122      29.948  22.423  16.913  1.00 65.13           N  
ATOM    967  CZ  ARG A 122      30.949  21.737  17.472  1.00 63.30           C  
ATOM    968  NH1 ARG A 122      30.955  20.411  17.451  1.00 62.64           N  
ATOM    969  NH2 ARG A 122      31.934  22.382  18.094  1.00 46.47           N  
ATOM    970  N   GLN A 123      23.563  20.225  15.197  1.00 10.54           N  
ATOM    971  CA  GLN A 123      22.416  20.357  14.298  1.00 12.13           C  
ATOM    972  C   GLN A 123      21.063  20.637  14.989  1.00 12.39           C  
ATOM    973  O   GLN A 123      20.161  21.221  14.384  1.00 16.37           O  
ATOM    974  CB  GLN A 123      22.312  19.094  13.460  1.00 19.95           C  
ATOM    975  CG  GLN A 123      22.428  17.832  14.260  1.00 24.10           C  
ATOM    976  CD  GLN A 123      21.712  16.685  13.628  1.00 40.62           C  
ATOM    977  OE1 GLN A 123      20.572  16.824  13.197  1.00 47.78           O  
ATOM    978  NE2 GLN A 123      22.371  15.531  13.567  1.00 40.06           N  
ATOM    979  N   TYR A 124      20.934  20.285  16.254  1.00 10.11           N  
ATOM    980  CA  TYR A 124      19.703  20.525  16.999  1.00  9.27           C  
ATOM    981  C   TYR A 124      19.425  21.979  17.361  1.00 10.03           C  
ATOM    982  O   TYR A 124      18.268  22.345  17.525  1.00 13.52           O  
ATOM    983  CB  TYR A 124      19.666  19.646  18.253  1.00  7.22           C  
ATOM    984  CG  TYR A 124      19.634  18.198  17.893  1.00  9.45           C  
ATOM    985  CD1 TYR A 124      18.474  17.629  17.386  1.00  9.96           C  
ATOM    986  CD2 TYR A 124      20.755  17.404  18.034  1.00 11.77           C  
ATOM    987  CE1 TYR A 124      18.419  16.300  17.021  1.00 13.10           C  
ATOM    988  CE2 TYR A 124      20.722  16.055  17.672  1.00 17.77           C  
ATOM    989  CZ  TYR A 124      19.537  15.513  17.160  1.00 13.25           C  
ATOM    990  OH  TYR A 124      19.471  14.197  16.761  1.00 12.87           O  
ATOM    991  N   VAL A 125      20.468  22.793  17.512  1.00  8.81           N  
ATOM    992  CA  VAL A 125      20.253  24.200  17.856  1.00  5.48           C  
ATOM    993  C   VAL A 125      20.737  25.178  16.777  1.00  8.96           C  
ATOM    994  O   VAL A 125      20.774  26.386  17.010  1.00 12.13           O  
ATOM    995  CB  VAL A 125      20.942  24.549  19.178  1.00  6.59           C  
ATOM    996  CG1 VAL A 125      20.289  23.806  20.337  1.00  4.15           C  
ATOM    997  CG2 VAL A 125      22.432  24.223  19.101  1.00  8.38           C  
ATOM    998  N   GLN A 126      21.080  24.669  15.599  1.00  9.14           N  
ATOM    999  CA  GLN A 126      21.574  25.560  14.548  1.00 12.02           C  
ATOM   1000  C   GLN A 126      20.517  26.473  13.970  1.00 11.61           C  
ATOM   1001  O   GLN A 126      19.421  26.029  13.642  1.00 14.48           O  
ATOM   1002  CB  GLN A 126      22.254  24.784  13.420  1.00 19.39           C  
ATOM   1003  CG  GLN A 126      23.564  24.100  13.811  1.00 49.95           C  
ATOM   1004  CD  GLN A 126      24.572  25.030  14.496  1.00 56.40           C  
ATOM   1005  OE1 GLN A 126      25.368  25.710  13.834  1.00 56.12           O  
ATOM   1006  NE2 GLN A 126      24.559  25.036  15.829  1.00 38.46           N  
ATOM   1007  N   GLY A 127      20.852  27.756  13.900  1.00 11.96           N  
ATOM   1008  CA  GLY A 127      19.950  28.749  13.361  1.00 11.55           C  
ATOM   1009  C   GLY A 127      18.845  29.248  14.277  1.00 11.73           C  
ATOM   1010  O   GLY A 127      18.116  30.177  13.914  1.00 11.72           O  
ATOM   1011  N   CYS A 128      18.748  28.692  15.482  1.00 10.76           N  
ATOM   1012  CA  CYS A 128      17.695  29.092  16.423  1.00  7.88           C  
ATOM   1013  C   CYS A 128      18.010  30.351  17.207  1.00  7.16           C  
ATOM   1014  O   CYS A 128      17.161  30.842  17.945  1.00  9.38           O  
ATOM   1015  CB  CYS A 128      17.373  27.955  17.396  1.00  6.26           C  
ATOM   1016  SG  CYS A 128      16.974  26.377  16.586  1.00 11.36           S  
ATOM   1017  N   GLY A 129      19.238  30.846  17.076  1.00 11.76           N  
ATOM   1018  CA  GLY A 129      19.645  32.058  17.774  1.00 18.88           C  
ATOM   1019  C   GLY A 129      19.738  31.960  19.286  1.00 22.36           C  
ATOM   1020  O   GLY A 129      19.406  32.924  19.988  1.00 23.66           O  
ATOM   1021  N   VAL A 130      20.218  30.817  19.780  1.00 20.07           N  
ATOM   1022  CA  VAL A 130      20.378  30.576  21.213  1.00 20.40           C  
ATOM   1023  C   VAL A 130      21.849  30.457  21.579  1.00 25.29           C  
ATOM   1024  O   VAL A 130      22.642  29.960  20.767  1.00 26.35           O  
ATOM   1025  CB  VAL A 130      19.666  29.289  21.677  1.00 16.91           C  
ATOM   1026  CG1 VAL A 130      18.160  29.502  21.701  1.00 14.05           C  
ATOM   1027  CG2 VAL A 130      20.051  28.110  20.770  1.00 16.77           C  
ATOM   1028  OXT VAL A 130      22.190  30.837  22.702  1.00 28.59           O  
TER    1029      VAL A 130                                                      
HETATM 1030 NA    NA A 272       6.297   7.449   7.129  1.00 28.98          NA  
HETATM 1031  O   HOH A 131       0.107  12.949  43.004  1.00  2.00           O  
HETATM 1032  O   HOH A 132       1.210  18.252  40.694  1.00  2.00           O  
HETATM 1033  O   HOH A 133      12.094  25.508  14.009  1.00  3.97           O  
HETATM 1034  O   HOH A 134       5.223  20.517  32.671  1.00  5.02           O  
HETATM 1035  O   HOH A 135       8.481  14.907  30.535  1.00  8.69           O  
HETATM 1036  O   HOH A 136      24.865  15.169  38.134  1.00 15.67           O  
HETATM 1037  O   HOH A 137       3.838   6.357   6.391  1.00  7.56           O  
HETATM 1038  O   HOH A 138      -1.252  11.799  40.348  1.00  6.22           O  
HETATM 1039  O   HOH A 139       4.807  19.512  30.117  1.00 13.46           O  
HETATM 1040  O   HOH A 140       0.361  17.600  43.394  1.00 24.72           O  
HETATM 1041  O   HOH A 141      27.692   6.845  38.011  1.00  9.12           O  
HETATM 1042  O   HOH A 142      -0.220   4.042  31.089  1.00 15.77           O  
HETATM 1043  O   HOH A 143       4.463  23.218  33.763  1.00 18.32           O  
HETATM 1044  O   HOH A 144       8.370  19.812  15.142  1.00 26.65           O  
HETATM 1045  O   HOH A 145       2.164   3.462  35.014  1.00 19.34           O  
HETATM 1046  O   HOH A 146       2.452   4.572   7.940  1.00 17.04           O  
HETATM 1047  O   HOH A 147      12.606   8.612  33.055  1.00 20.20           O  
HETATM 1048  O   HOH A 148      11.204  29.766  15.308  1.00 17.66           O  
HETATM 1049  O   HOH A 149      29.175   9.410  15.302  1.00 19.14           O  
HETATM 1050  O   HOH A 150      10.643  21.281  14.160  1.00 21.47           O  
HETATM 1051  O   HOH A 151      15.096  18.327  14.936  1.00 15.19           O  
HETATM 1052  O   HOH A 152       6.057  17.357  29.060  1.00 10.00           O  
HETATM 1053  O   HOH A 153      23.462  29.214  14.713  1.00 24.81           O  
HETATM 1054  O   HOH A 154       4.358  21.931  15.440  1.00 14.21           O  
HETATM 1055  O   HOH A 155      10.518  25.685  35.660  1.00 23.43           O  
HETATM 1056  O   HOH A 156      26.931   4.931  15.008  1.00 36.55           O  
HETATM 1057  O   HOH A 157       1.325  -5.589  40.204  1.00 23.02           O  
HETATM 1058  O   HOH A 158      15.885   5.331  30.358  1.00 29.79           O  
HETATM 1059  O   HOH A 159       4.869   7.395   8.741  1.00 30.85           O  
HETATM 1060  O   HOH A 160       4.173  26.094  25.854  1.00 23.99           O  
HETATM 1061  O   HOH A 161      26.783  14.601  23.350  1.00 18.78           O  
HETATM 1062  O   HOH A 162      15.389   6.479  27.245  1.00 21.01           O  
HETATM 1063  O   HOH A 163      24.839  16.059  35.023  1.00 14.13           O  
HETATM 1064  O   HOH A 164       8.075   9.604  47.192  1.00 34.12           O  
HETATM 1065  O   HOH A 165      33.330  18.661  13.989  1.00 20.86           O  
HETATM 1066  O   HOH A 166      14.211  11.430  12.239  1.00 32.39           O  
HETATM 1067  O   HOH A 167      12.642   7.374  30.713  1.00 33.11           O  
HETATM 1068  O   HOH A 168      15.582  32.254  24.879  1.00 33.55           O  
HETATM 1069  O   HOH A 169      13.575  25.358  37.026  1.00 22.88           O  
HETATM 1070  O   HOH A 170      28.395  18.265  18.924  1.00 36.93           O  
HETATM 1071  O   HOH A 171      21.697  28.801  17.759  1.00 25.80           O  
HETATM 1072  O   HOH A 172      23.875  26.725  21.090  1.00 48.58           O  
HETATM 1073  O   HOH A 173       0.466   0.317  35.713  1.00 27.58           O  
HETATM 1074  O   HOH A 174      27.106  23.689  35.556  1.00 27.96           O  
HETATM 1075  O   HOH A 175      24.255  23.777  37.284  1.00 22.64           O  
HETATM 1076  O   HOH A 176      -1.404   8.856  45.481  1.00 29.00           O  
HETATM 1077  O   HOH A 177      11.011   1.837  35.343  1.00 22.53           O  
HETATM 1078  O   HOH A 178       1.486  26.494  26.092  1.00 38.70           O  
HETATM 1079  O   HOH A 179      18.571  25.839   9.663  1.00 39.86           O  
HETATM 1080  O   HOH A 180       7.478   8.579  21.934  1.00 45.06           O  
HETATM 1081  O   HOH A 181       7.572  24.772  38.294  1.00 40.72           O  
HETATM 1082  O   HOH A 182      14.089  20.376  40.419  1.00 33.00           O  
HETATM 1083  O   HOH A 183      26.554  12.866  35.801  1.00 33.74           O  
HETATM 1084  O   HOH A 184      20.406  10.519  36.855  1.00 21.28           O  
HETATM 1085  O   HOH A 185      15.509   8.671  33.034  1.00 26.14           O  
HETATM 1086  O   HOH A 186      -0.879   5.051  28.320  1.00 35.85           O  
HETATM 1087  O   HOH A 187      14.060   8.574  11.989  1.00 42.95           O  
HETATM 1088  O   HOH A 188      26.453   6.679  34.781  1.00 39.08           O  
HETATM 1089  O   HOH A 189      -4.050   0.293  39.422  1.00 37.66           O  
HETATM 1090  O   HOH A 190       9.456   6.167  25.701  1.00 30.65           O  
HETATM 1091  O   HOH A 191       1.299  14.704  46.563  1.00 33.38           O  
HETATM 1092  O   HOH A 192      17.542  18.480  13.503  1.00 36.68           O  
HETATM 1093  O   HOH A 193      13.398  14.125  12.197  1.00 36.05           O  
HETATM 1094  O   HOH A 194       4.453   7.446  45.875  1.00 39.33           O  
HETATM 1095  O   HOH A 195      25.246   5.062  31.612  1.00 41.32           O  
HETATM 1096  O   HOH A 196      26.449  21.834  41.085  1.00 41.35           O  
HETATM 1097  O   HOH A 197      -4.130   6.935  44.972  1.00  5.00           O  
HETATM 1098  O   HOH A 198      -1.961  18.931  35.233  1.00 13.88           O  
HETATM 1099  O   HOH A 199       6.322  26.266  27.919  1.00 14.11           O  
HETATM 1100  O   HOH A 200      28.539  11.718  41.517  1.00 13.24           O  
HETATM 1101  O   HOH A 201      27.433   5.501  29.753  1.00 32.42           O  
HETATM 1102  O   HOH A 202      18.910   8.365  37.709  1.00 25.99           O  
HETATM 1103  O   HOH A 203      25.321  21.334  11.893  1.00 35.86           O  
HETATM 1104  O   HOH A 204       2.861  16.622  44.924  1.00 28.48           O  
HETATM 1105  O   HOH A 205       1.567   8.393  46.974  1.00 34.61           O  
HETATM 1106  O   HOH A 206      -1.339  -1.307  37.866  1.00 37.37           O  
HETATM 1107  O   HOH A 207       1.458  24.774  35.175  1.00 36.55           O  
HETATM 1108  O   HOH A 208       7.747  -0.837  48.243  1.00 43.79           O  
HETATM 1109  O   HOH A 209      26.354  13.972  40.300  1.00 43.50           O  
HETATM 1110  O   HOH A 210       1.610   5.286  44.563  1.00 37.23           O  
HETATM 1111  O   HOH A 211      21.959   1.145  33.713  1.00 38.23           O  
HETATM 1112  O   HOH A 212      17.915   4.269  33.066  1.00 48.52           O  
HETATM 1113  O   HOH A 213      -5.584   1.202  37.192  1.00 31.10           O  
HETATM 1114  O   HOH A 214      20.858  27.153  35.012  1.00 27.29           O  
HETATM 1115  O   HOH A 215       2.021   5.596  23.130  1.00 49.45           O  
HETATM 1116  O   HOH A 216      14.012   5.811  44.607  1.00 26.16           O  
HETATM 1117  O   HOH A 217       0.217  -4.883  27.153  1.00 26.37           O  
HETATM 1118  O   HOH A 218      24.051  25.825  35.640  1.00 48.70           O  
HETATM 1119  O   HOH A 219      10.984  12.954  15.304  1.00 35.04           O  
HETATM 1120  O   HOH A 220      11.410  27.845  12.743  1.00 31.38           O  
HETATM 1121  O   HOH A 221      10.535  27.201  15.528  1.00 33.53           O  
HETATM 1122  O   HOH A 222      19.836  30.094  36.011  1.00 36.52           O  
HETATM 1123  O   HOH A 223       2.690  24.645  12.520  1.00 35.19           O  
HETATM 1124  O   HOH A 224       4.186  17.728  13.243  1.00 33.68           O  
HETATM 1125  O   HOH A 225      17.725  26.266  37.955  1.00 43.29           O  
HETATM 1126  O   HOH A 226      19.311  23.502  41.319  1.00 30.03           O  
HETATM 1127  O   HOH A 227      18.052  29.403  37.879  1.00 39.49           O  
HETATM 1128  O   HOH A 228      26.441   7.789  12.143  1.00 32.93           O  
HETATM 1129  O   HOH A 229      12.423  19.291  13.558  1.00 28.23           O  
HETATM 1130  O   HOH A 230      22.306  21.408  10.599  1.00 43.67           O  
HETATM 1131  O   HOH A 231      13.714  24.316  39.705  1.00 42.05           O  
HETATM 1132  O   HOH A 232       2.654  -1.978  45.428  1.00 31.55           O  
HETATM 1133  O   HOH A 233      11.061   2.900  44.629  1.00 44.61           O  
HETATM 1134  O   HOH A 234      17.524   6.670  36.079  1.00 39.77           O  
HETATM 1135  O   HOH A 235      27.873  20.351  43.256  1.00 40.33           O  
HETATM 1136  O   HOH A 236      -5.524   3.689  34.541  1.00 36.20           O  
HETATM 1137  O   HOH A 237       6.191  27.278  38.061  1.00 40.37           O  
HETATM 1138  O   HOH A 238       2.300  10.074  20.229  1.00 46.88           O  
HETATM 1139  O   HOH A 239      -1.604   0.643  33.195  1.00 36.24           O  
HETATM 1140  O   HOH A 240       1.893   3.431  24.736  1.00 35.14           O  
HETATM 1141  O   HOH A 241      26.705  11.060  44.417  1.00 38.35           O  
HETATM 1142  O   HOH A 242       1.655  12.476  17.169  1.00 37.60           O  
HETATM 1143  O   HOH A 243      22.004   8.174  38.864  1.00 38.32           O  
HETATM 1144  O   HOH A 244      14.751   7.036  35.523  1.00 36.33           O  
HETATM 1145  O   HOH A 245       5.899  14.843  17.106  1.00 33.39           O  
HETATM 1146  O   HOH A 246       3.539  10.855  45.925  1.00 39.52           O  
HETATM 1147  O   HOH A 247       2.824  14.843  15.695  1.00 40.63           O  
HETATM 1148  O   HOH A 248       1.022  27.855  28.403  1.00 45.75           O  
HETATM 1149  O   HOH A 249      -0.148  -1.336  40.548  1.00 41.70           O  
HETATM 1150  O   HOH A 250       4.860   9.183  21.570  1.00 39.28           O  
HETATM 1151  O   HOH A 251       7.733  28.519  16.261  1.00 42.65           O  
HETATM 1152  O   HOH A 252      -1.398   4.532  45.386  1.00 42.37           O  
HETATM 1153  O   HOH A 253       1.274  23.827  37.916  1.00 45.18           O  
HETATM 1154  O   HOH A 254      25.285  13.397  43.044  1.00 37.47           O  
HETATM 1155  O   HOH A 255      24.041  28.409  19.140  1.00 38.11           O  
HETATM 1156  O   HOH A 256      24.175   9.944  45.416  1.00 47.65           O  
HETATM 1157  O   HOH A 257      13.900   5.382  33.706  1.00 31.27           O  
HETATM 1158  O   HOH A 258      -1.376  -3.159  28.829  1.00 39.68           O  
HETATM 1159  O   HOH A 259      11.742  10.993  17.596  1.00 40.47           O  
HETATM 1160  O   HOH A 261      11.811   4.544  31.142  1.00 41.64           O  
HETATM 1161  O   HOH A 262       1.453  -4.674  44.154  1.00 40.15           O  
HETATM 1162  O   HOH A 263      10.737  23.455  12.636  1.00 40.98           O  
HETATM 1163  O   HOH A 264       9.595  18.703  40.055  1.00 36.79           O  
HETATM 1164  O   HOH A 265      16.865   4.675  37.960  1.00 46.51           O  
HETATM 1165  O   HOH A 266      -0.020  -3.649  38.931  1.00 35.52           O  
HETATM 1166  O   HOH A 267       5.424  -2.152  26.543  1.00 39.53           O  
HETATM 1167  O   HOH A 268      -4.293   0.057  35.024  1.00 41.70           O  
HETATM 1168  O   HOH A 269       8.273  16.777  15.554  1.00 40.79           O  
HETATM 1169  O   HOH A 270      29.213  13.169  12.288  1.00 15.12           O  
HETATM 1170  O   HOH A 271      21.799  31.385  15.552  1.00 17.86           O  
HETATM 1171  O   HOH A 273      11.472  -4.812  38.225  1.00 22.51           O  
HETATM 1172  O   HOH A 274      19.827  28.276  30.061  1.00 18.04           O  
HETATM 1173  O   HOH A 275      12.740  17.138  43.648  1.00 36.62           O  
HETATM 1174  O   HOH A 276      27.450  12.414  14.656  1.00 15.47           O  
HETATM 1175  O   HOH A 277       3.423  -7.904  37.460  1.00 23.64           O  
HETATM 1176  O   HOH A 278      21.141  32.651  12.872  1.00 41.86           O  
HETATM 1177  O   HOH A 279       4.219  25.103  18.265  1.00 38.20           O  
HETATM 1178  O   HOH A 280      14.764  17.479  45.202  1.00 40.93           O  
HETATM 1179  O   HOH A 281      11.615  -1.485  37.574  1.00 41.53           O  
HETATM 1180  O   HOH A 282      23.311  32.732  17.822  1.00 46.01           O  
HETATM 1181  O   HOH A 283      12.512   6.095  26.648  1.00 48.09           O  
HETATM 1182  O   HOH A 284      11.542  18.628  41.795  1.00 42.23           O  
HETATM 1183  O   HOH A 285      -0.702  -2.249  35.369  1.00 48.99           O  
HETATM 1184  O   HOH A 286       1.483   8.315  22.963  1.00 41.58           O  
HETATM 1185  O   HOH A 288      18.516  20.938  12.315  1.00 41.79           O  
HETATM 1186  O   HOH A 289       5.572  20.064  13.698  1.00 44.20           O  
HETATM 1187  O   HOH A 290       2.764  20.490  41.785  1.00 41.46           O  
HETATM 1188  O   HOH A 292       9.305  19.267  44.892  1.00 47.41           O  
HETATM 1189  O   HOH A 293      12.311  -3.368  40.456  1.00 46.05           O  
HETATM 1190  O   HOH A 294      26.441  22.847  38.311  1.00 48.21           O  
HETATM 1191  O   HOH A 295       9.230  29.914  13.658  1.00 48.53           O  
HETATM 1192  O   HOH A 296      11.592   1.585  32.764  1.00 49.73           O  
HETATM 1193  O   HOH A 298      16.304   0.774  28.325  1.00 43.03           O  
HETATM 1194  O   HOH A 299      17.237  32.675  27.259  1.00 47.36           O  
HETATM 1195  O   HOH A 301      22.133  23.994  40.229  1.00 46.03           O  
HETATM 1196  O   HOH A 302       6.685  27.873  25.479  1.00 48.24           O  
HETATM 1197  O   HOH A 303      24.402   2.050  33.693  1.00 48.55           O  
HETATM 1198  O   HOH A 305       6.088  13.331  47.671  1.00 48.63           O  
CONECT   53 1016                                                                
CONECT  243  915                                                                
CONECT  533  641                                                                
CONECT  611  737                                                                
CONECT  641  533                                                                
CONECT  737  611                                                                
CONECT  915  243                                                                
CONECT 1016   53                                                                
CONECT 1030 1037 1059                                                           
CONECT 1037 1030                                                                
CONECT 1059 1030                                                                
MASTER      262    0    1    8    2    0    2    6 1197    1   11   10          
END                                                                             
