HEADER    HYDROLASE                               25-JAN-99   1B7Q              
TITLE     VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES                     
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 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    MUTANT STABILITY, HUMAN LYSOZYME, HYDROLASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAKANO,M.OTA,K.OGASAHARA,Y.YAMAGATA,K.NISHIKAWA,K.YUTANI            
REVDAT   6   03-APR-24 1B7Q    1       REMARK                                   
REVDAT   5   27-DEC-23 1B7Q    1       REMARK                                   
REVDAT   4   03-NOV-21 1B7Q    1       REMARK SEQADV LINK                       
REVDAT   3   24-FEB-09 1B7Q    1       VERSN                                    
REVDAT   2   29-DEC-99 1B7Q    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   02-FEB-99 1B7Q    0                                                
JRNL        AUTH   K.TAKANO,M.OTA,K.OGASAHARA,Y.YAMAGATA,K.NISHIKAWA,K.YUTANI   
JRNL        TITL   EXPERIMENTAL VERIFICATION OF THE 'STABILITY PROFILE OF       
JRNL        TITL 2 MUTANT PROTEIN' (SPMP) DATA USING MUTANT HUMAN LYSOZYMES.    
JRNL        REF    PROTEIN ENG.                  V.  12   663 1999              
JRNL        REFN                   ISSN 0269-2139                               
JRNL        PMID   10469827                                                     
JRNL        DOI    10.1093/PROTEIN/12.8.663                                     
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 TYROSINE->PHENYLALANINE MUTANTS                       
REMARK   1  REF    J.MOL.BIOL.                   V.  37  9355 1998              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.TAKANO,Y.YAMAGATA,S.FUJII,K.YUTANI                         
REMARK   1  TITL   CONTRIBUTION OF THE HYDROPHOBIC EFFECT TO THE STABILITY OF   
REMARK   1  TITL 2 HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL    
REMARK   1  TITL 3 ANALYSES OF THE NINE VALINE TO ALANINE MUTANTS               
REMARK   1  REF    BIOCHEMISTRY                  V.  36   688 1997              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   K.TAKANO,J.FUNAHASHI,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   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.    2.00 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) : 2.00                           
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)   (%) : 76.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 6004                           
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) : 0.163                           
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.09                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 606                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1830                       
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            : 1029                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 245                                     
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.670                           
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 1B7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000000370.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS                            
REMARK 200  DATA SCALING SOFTWARE          : PROCESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17068                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 74.2                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 51.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
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   (%): 35.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 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       28.34000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       16.17500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.54500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       16.17500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.34000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.54500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG A    21     O    HOH A   268              1.18            
REMARK 500   OD2  ASP A    49     O    HOH A   178              1.27            
REMARK 500   NE   ARG A   119     O    HOH A   354              1.33            
REMARK 500   OD2  ASP A    91     O    HOH A   351              1.39            
REMARK 500   O    HOH A   245     O    HOH A   335              1.39            
REMARK 500   OG1  THR A    52     O    HOH A   174              1.40            
REMARK 500   OE1  GLU A    35     O    HOH A   293              1.42            
REMARK 500   O    THR A    70     O    HOH A   152              1.44            
REMARK 500   O    ALA A    90     O    HOH A   237              1.45            
REMARK 500   O    HOH A   203     O    HOH A   307              1.48            
REMARK 500   ND2  ASN A    66     O    HOH A   133              1.49            
REMARK 500   N    ILE A    56     O    HOH A   146              1.51            
REMARK 500   O    ASN A    88     O    HOH A   136              1.53            
REMARK 500   NE   ARG A    50     O    HOH A   264              1.56            
REMARK 500   O    HOH A   155     O    HOH A   160              1.57            
REMARK 500   NE2  GLN A   126     O    HOH A   306              1.57            
REMARK 500   CG2  VAL A   110     O    HOH A   183              1.57            
REMARK 500   OE2  GLU A    35     O    HOH A   181              1.58            
REMARK 500   O    PRO A   103     O    HOH A   355              1.63            
REMARK 500   CA   PRO A   103     O    HOH A   272              1.64            
REMARK 500   NH1  ARG A   113     O    HOH A   267              1.66            
REMARK 500   CG   ARG A   101     O    HOH A   193              1.67            
REMARK 500   NH1  ARG A    50     O    HOH A   212              1.70            
REMARK 500   CB   SER A    80     O    HOH A   140              1.71            
REMARK 500   NH1  ARG A   101     O    HOH A   290              1.77            
REMARK 500   CD   ARG A    50     O    HOH A   264              1.82            
REMARK 500   CA   TYR A    20     O    HOH A   244              1.83            
REMARK 500   CG   ARG A   119     O    HOH A   354              1.87            
REMARK 500   NE1  TRP A   109     O    HOH A   169              1.89            
REMARK 500   O    HIS A    78     O    HOH A   275              1.89            
REMARK 500   CD   ARG A   119     O    HOH A   354              1.89            
REMARK 500   O    ALA A    94     O    HOH A   156              1.89            
REMARK 500   O    GLN A    86     O    HOH A   153              1.92            
REMARK 500   OD2  ASP A    53     O    HOH A   292              1.92            
REMARK 500   CA   ILE A    56     O    HOH A   146              1.95            
REMARK 500   O    HOH A   140     O    HOH A   196              1.95            
REMARK 500   CA   ALA A    94     O    HOH A   167              1.97            
REMARK 500   N    PRO A   103     O    HOH A   272              1.97            
REMARK 500   CB   HIS A    78     O    HOH A   274              1.97            
REMARK 500   C    ASN A    88     O    HOH A   136              1.97            
REMARK 500   O    ASP A   102     O    HOH A   316              1.97            
REMARK 500   CD2  LEU A    79     O    HOH A   314              1.99            
REMARK 500   N    GLY A    72     O    HOH A   229              1.99            
REMARK 500   NZ   LYS A     1     O    HOH A   158              2.01            
REMARK 500   CB   THR A    40     O    HOH A   353              2.02            
REMARK 500   CG2  THR A    40     O    HOH A   153              2.02            
REMARK 500   NE2  GLN A    86     O    HOH A   206              2.03            
REMARK 500   ND2  ASN A    75     O    HOH A   226              2.03            
REMARK 500   CZ   ARG A    50     O    HOH A   264              2.04            
REMARK 500   N    ARG A    21     O    HOH A   195              2.04            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   261     O    HOH A   328     4457     0.83            
REMARK 500   NH1  ARG A    14     O    HOH A   149     2565     1.01            
REMARK 500   OD1  ASN A   118     O    HOH A   185     4557     1.21            
REMARK 500   CG   ASN A   118     O    HOH A   185     4557     1.46            
REMARK 500   NH2  ARG A   115     O    HOH A   170     2554     1.57            
REMARK 500   N    LYS A     1     O    HOH A   147     4457     1.59            
REMARK 500   ND2  ASN A   118     O    HOH A   185     4557     1.61            
REMARK 500   CB   ALA A    73    NA     NA A   601     1556     1.64            
REMARK 500   O    ALA A    76     O    HOH A   321     1556     1.67            
REMARK 500   NE   ARG A   101     O    HOH A   271     1556     1.74            
REMARK 500   CZ   ARG A    14     O    HOH A   149     2565     1.75            
REMARK 500   CD2  HIS A    78     O    HOH A   179     1556     1.78            
REMARK 500   NH2  ARG A    41     O    ARG A   101     4457     1.81            
REMARK 500   OD1  ASP A    87     O    HOH A   147     4457     1.86            
REMARK 500   NH1  ARG A    21     CZ   ARG A    41     4557     1.89            
REMARK 500   O    ARG A   119     O    HOH A   341     4557     1.89            
REMARK 500   CB   SER A    24     O    ASP A    67     4557     1.90            
REMARK 500   CB   SER A    24     O    HOH A   235     4557     1.99            
REMARK 500   CG   HIS A    78     O    HOH A   179     1556     2.04            
REMARK 500   ND2  ASN A   118     O    HOH A   314     4557     2.05            
REMARK 500   NH2  ARG A    98     O    HOH A   360     1556     2.11            
REMARK 500   OE1  GLN A    86     NE   ARG A   107     4457     2.11            
REMARK 500   O    ALA A    47     NH1  ARG A   119     2555     2.12            
REMARK 500   OG   SER A    24     O    HOH A   235     4557     2.12            
REMARK 500   NE   ARG A    14     O    HOH A   149     2565     2.13            
REMARK 500   O    HOH A   173     O    HOH A   209     2565     2.14            
REMARK 500   NH1  ARG A   122     O    HOH A   176     4557     2.15            
REMARK 500   CG   ARG A   122     O    HOH A   154     4557     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A   5      -78.72    -43.30                                   
REMARK 500    TYR A  63      -32.72   -130.97                                   
REMARK 500    CYS A 116      -33.28   -130.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  61   O                                                      
REMARK 620 2 HOH A 164   O   129.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 601                  
DBREF  1B7Q A    1   130  UNP    P61626   LYSC_HUMAN      19    148             
SEQADV 1B7Q LEU A   27  UNP  P61626    ASN    45 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  LEU TRP MET CYS LEU ALA LYS TRP GLU SER GLY TYR ASN          
SEQRES   4 A  130  THR ARG ALA THR ASN TYR ASN ALA GLY ASP ARG SER THR          
SEQRES   5 A  130  ASP TYR GLY ILE PHE GLN ILE ASN SER ARG TYR TRP CYS          
SEQRES   6 A  130  ASN ASP GLY LYS THR PRO GLY ALA VAL ASN ALA CYS HIS          
SEQRES   7 A  130  LEU SER CYS SER ALA LEU LEU GLN ASP ASN ILE ALA ASP          
SEQRES   8 A  130  ALA VAL ALA CYS ALA LYS ARG VAL VAL ARG ASP PRO GLN          
SEQRES   9 A  130  GLY ILE ARG ALA TRP VAL ALA TRP ARG ASN ARG CYS GLN          
SEQRES  10 A  130  ASN ARG ASP VAL ARG GLN TYR VAL GLN GLY CYS GLY VAL          
HET     NA  A 601       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   2   NA    NA 1+                                                        
FORMUL   3  HOH   *245(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  SER A   36  1                                  12    
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  2.03  
SSBOND   4 CYS A   77    CYS A   95                          1555   1555  2.03  
LINK         O   SER A  61                NA    NA A 601     1554   1555  2.13  
LINK         O   HOH A 164                NA    NA A 601     1554   1555  2.13  
SITE     1 AC1  5 SER A  61  ARG A  62  ALA A  73  VAL A  74                    
SITE     2 AC1  5 HOH A 164                                                     
CRYST1   56.680   61.090   32.350  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      0.017643  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016369  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.030912        0.00000                         
ATOM      1  N   LYS A   1       1.276  19.386  23.276  1.00  5.79           N  
ATOM      2  CA  LYS A   1       1.763  20.328  22.240  1.00  4.87           C  
ATOM      3  C   LYS A   1       2.950  19.680  21.570  1.00  3.22           C  
ATOM      4  O   LYS A   1       3.755  19.059  22.248  1.00  2.56           O  
ATOM      5  CB  LYS A   1       2.236  21.641  22.897  1.00  5.00           C  
ATOM      6  CG  LYS A   1       2.848  22.616  21.927  1.00  8.34           C  
ATOM      7  CD  LYS A   1       3.517  23.832  22.582  1.00  4.95           C  
ATOM      8  CE  LYS A   1       4.207  24.608  21.506  1.00  2.00           C  
ATOM      9  NZ  LYS A   1       4.513  25.982  21.911  1.00  8.33           N  
ATOM     10  N   VAL A   2       3.028  19.769  20.247  1.00  3.53           N  
ATOM     11  CA  VAL A   2       4.183  19.244  19.523  1.00  4.68           C  
ATOM     12  C   VAL A   2       4.974  20.500  19.110  1.00  3.65           C  
ATOM     13  O   VAL A   2       4.500  21.308  18.292  1.00  2.02           O  
ATOM     14  CB  VAL A   2       3.799  18.460  18.238  1.00  5.58           C  
ATOM     15  CG1 VAL A   2       5.055  17.863  17.594  1.00  6.82           C  
ATOM     16  CG2 VAL A   2       2.796  17.358  18.550  1.00  6.54           C  
ATOM     17  N   PHE A   3       6.139  20.689  19.721  1.00  2.00           N  
ATOM     18  CA  PHE A   3       7.003  21.840  19.444  1.00  2.00           C  
ATOM     19  C   PHE A   3       7.750  21.844  18.122  1.00  2.41           C  
ATOM     20  O   PHE A   3       8.039  20.800  17.546  1.00  2.00           O  
ATOM     21  CB  PHE A   3       8.075  21.947  20.523  1.00  2.00           C  
ATOM     22  CG  PHE A   3       7.622  22.604  21.782  1.00  2.60           C  
ATOM     23  CD1 PHE A   3       7.875  23.961  21.995  1.00  2.24           C  
ATOM     24  CD2 PHE A   3       7.053  21.858  22.805  1.00  3.23           C  
ATOM     25  CE1 PHE A   3       7.574  24.555  23.218  1.00  5.20           C  
ATOM     26  CE2 PHE A   3       6.746  22.445  24.030  1.00  5.64           C  
ATOM     27  CZ  PHE A   3       7.015  23.800  24.240  1.00  2.00           C  
ATOM     28  N   GLU A   4       8.057  23.043  17.640  1.00  5.06           N  
ATOM     29  CA  GLU A   4       8.865  23.186  16.449  1.00  6.83           C  
ATOM     30  C   GLU A   4      10.256  23.265  17.053  1.00  5.23           C  
ATOM     31  O   GLU A   4      10.389  23.680  18.202  1.00  2.62           O  
ATOM     32  CB  GLU A   4       8.516  24.456  15.664  1.00 13.51           C  
ATOM     33  CG  GLU A   4       7.213  24.348  14.858  1.00 20.09           C  
ATOM     34  CD  GLU A   4       6.965  25.568  13.980  1.00 27.31           C  
ATOM     35  OE1 GLU A   4       6.976  25.416  12.732  1.00 31.69           O  
ATOM     36  OE2 GLU A   4       6.760  26.676  14.535  1.00 27.97           O  
ATOM     37  N   ARG A   5      11.264  22.797  16.315  1.00  3.98           N  
ATOM     38  CA  ARG A   5      12.656  22.778  16.763  1.00  4.60           C  
ATOM     39  C   ARG A   5      13.121  24.055  17.467  1.00  5.97           C  
ATOM     40  O   ARG A   5      13.177  24.108  18.689  1.00  6.66           O  
ATOM     41  CB  ARG A   5      13.586  22.461  15.577  1.00  2.96           C  
ATOM     42  CG  ARG A   5      15.044  22.186  15.978  1.00  2.00           C  
ATOM     43  CD  ARG A   5      15.937  21.703  14.800  1.00  2.00           C  
ATOM     44  NE  ARG A   5      16.047  22.645  13.680  1.00  2.54           N  
ATOM     45  CZ  ARG A   5      16.957  23.619  13.582  1.00  6.96           C  
ATOM     46  NH1 ARG A   5      16.964  24.420  12.520  1.00  4.04           N  
ATOM     47  NH2 ARG A   5      17.849  23.815  14.550  1.00  2.00           N  
ATOM     48  N   CYS A   6      13.430  25.096  16.698  1.00  7.43           N  
ATOM     49  CA  CYS A   6      13.915  26.346  17.283  1.00  5.26           C  
ATOM     50  C   CYS A   6      13.026  26.944  18.359  1.00  6.57           C  
ATOM     51  O   CYS A   6      13.526  27.534  19.316  1.00  3.86           O  
ATOM     52  CB  CYS A   6      14.268  27.351  16.186  1.00  5.08           C  
ATOM     53  SG  CYS A   6      15.757  26.812  15.289  1.00  3.39           S  
ATOM     54  N   GLU A   7      11.717  26.724  18.243  1.00  7.10           N  
ATOM     55  CA  GLU A   7      10.745  27.199  19.232  1.00  8.21           C  
ATOM     56  C   GLU A   7      11.075  26.518  20.590  1.00  9.19           C  
ATOM     57  O   GLU A   7      11.170  27.197  21.634  1.00  5.81           O  
ATOM     58  CB  GLU A   7       9.332  26.828  18.762  1.00 12.83           C  
ATOM     59  CG  GLU A   7       8.195  27.290  19.660  1.00 17.03           C  
ATOM     60  CD  GLU A   7       6.831  26.647  19.305  1.00 16.14           C  
ATOM     61  OE1 GLU A   7       6.782  25.559  18.684  1.00  5.36           O  
ATOM     62  OE2 GLU A   7       5.797  27.251  19.677  1.00 20.73           O  
ATOM     63  N   LEU A   8      11.314  25.198  20.552  1.00  4.47           N  
ATOM     64  CA  LEU A   8      11.668  24.423  21.745  1.00  4.18           C  
ATOM     65  C   LEU A   8      13.026  24.867  22.316  1.00  3.13           C  
ATOM     66  O   LEU A   8      13.158  25.057  23.523  1.00  3.40           O  
ATOM     67  CB  LEU A   8      11.668  22.912  21.441  1.00  2.00           C  
ATOM     68  CG  LEU A   8      12.025  21.942  22.573  1.00  2.00           C  
ATOM     69  CD1 LEU A   8      11.242  22.233  23.818  1.00  2.00           C  
ATOM     70  CD2 LEU A   8      11.759  20.540  22.142  1.00  2.00           C  
ATOM     71  N   ALA A   9      14.005  25.097  21.444  1.00  3.01           N  
ATOM     72  CA  ALA A   9      15.342  25.545  21.863  1.00  2.00           C  
ATOM     73  C   ALA A   9      15.327  26.810  22.748  1.00  2.80           C  
ATOM     74  O   ALA A   9      15.882  26.827  23.847  1.00  2.00           O  
ATOM     75  CB  ALA A   9      16.218  25.757  20.644  1.00  2.00           C  
ATOM     76  N   ARG A  10      14.655  27.858  22.300  1.00  4.55           N  
ATOM     77  CA  ARG A  10      14.573  29.090  23.093  1.00  4.44           C  
ATOM     78  C   ARG A  10      13.746  28.882  24.359  1.00  4.47           C  
ATOM     79  O   ARG A  10      14.028  29.500  25.399  1.00  2.00           O  
ATOM     80  CB  ARG A  10      13.960  30.216  22.263  1.00  2.00           C  
ATOM     81  CG  ARG A  10      14.801  30.584  21.100  1.00  3.62           C  
ATOM     82  CD  ARG A  10      14.215  31.768  20.401  1.00  4.84           C  
ATOM     83  NE  ARG A  10      12.999  31.428  19.673  1.00  4.61           N  
ATOM     84  CZ  ARG A  10      12.971  30.884  18.464  1.00  5.19           C  
ATOM     85  NH1 ARG A  10      11.809  30.631  17.887  1.00  9.05           N  
ATOM     86  NH2 ARG A  10      14.096  30.584  17.832  1.00 10.43           N  
ATOM     87  N   THR A  11      12.709  28.039  24.259  1.00  3.90           N  
ATOM     88  CA  THR A  11      11.846  27.748  25.410  1.00  2.27           C  
ATOM     89  C   THR A  11      12.680  27.069  26.503  1.00  2.36           C  
ATOM     90  O   THR A  11      12.551  27.395  27.678  1.00  2.22           O  
ATOM     91  CB  THR A  11      10.625  26.838  25.042  1.00  2.00           C  
ATOM     92  OG1 THR A  11       9.812  27.464  24.035  1.00  2.94           O  
ATOM     93  CG2 THR A  11       9.773  26.600  26.259  1.00  2.00           C  
ATOM     94  N   LEU A  12      13.568  26.158  26.115  1.00  3.97           N  
ATOM     95  CA  LEU A  12      14.413  25.472  27.094  1.00  2.00           C  
ATOM     96  C   LEU A  12      15.467  26.409  27.656  1.00  2.27           C  
ATOM     97  O   LEU A  12      15.698  26.421  28.864  1.00  2.00           O  
ATOM     98  CB  LEU A  12      15.047  24.220  26.503  1.00  2.00           C  
ATOM     99  CG  LEU A  12      14.077  23.036  26.335  1.00  3.01           C  
ATOM    100  CD1 LEU A  12      14.693  21.955  25.445  1.00  3.61           C  
ATOM    101  CD2 LEU A  12      13.673  22.473  27.690  1.00  2.00           C  
ATOM    102  N   LYS A  13      16.061  27.234  26.795  1.00  2.00           N  
ATOM    103  CA  LYS A  13      17.067  28.193  27.232  1.00  2.55           C  
ATOM    104  C   LYS A  13      16.451  29.145  28.261  1.00  4.98           C  
ATOM    105  O   LYS A  13      17.036  29.380  29.315  1.00  6.17           O  
ATOM    106  CB  LYS A  13      17.600  28.994  26.044  1.00  4.05           C  
ATOM    107  CG  LYS A  13      18.841  29.821  26.354  1.00  4.70           C  
ATOM    108  CD  LYS A  13      19.353  30.484  25.091  1.00  9.28           C  
ATOM    109  CE  LYS A  13      20.803  30.964  25.219  1.00 11.29           C  
ATOM    110  NZ  LYS A  13      20.926  32.295  25.859  1.00  7.95           N  
ATOM    111  N   ARG A  14      15.244  29.642  27.987  1.00  4.60           N  
ATOM    112  CA  ARG A  14      14.577  30.552  28.919  1.00  4.41           C  
ATOM    113  C   ARG A  14      14.406  29.894  30.300  1.00  4.95           C  
ATOM    114  O   ARG A  14      14.618  30.516  31.343  1.00  2.00           O  
ATOM    115  CB  ARG A  14      13.219  30.963  28.342  1.00  4.40           C  
ATOM    116  CG  ARG A  14      12.977  32.464  28.317  1.00  7.53           C  
ATOM    117  CD  ARG A  14      12.242  32.899  27.077  1.00  4.74           C  
ATOM    118  NE  ARG A  14      11.232  31.917  26.702  1.00 10.75           N  
ATOM    119  CZ  ARG A  14      10.928  31.586  25.453  1.00  8.12           C  
ATOM    120  NH1 ARG A  14      10.001  30.654  25.237  1.00 14.60           N  
ATOM    121  NH2 ARG A  14      11.501  32.213  24.427  1.00 12.80           N  
ATOM    122  N   LEU A  15      14.081  28.607  30.298  1.00  4.94           N  
ATOM    123  CA  LEU A  15      13.902  27.875  31.546  1.00  5.86           C  
ATOM    124  C   LEU A  15      15.212  27.474  32.264  1.00  4.97           C  
ATOM    125  O   LEU A  15      15.184  26.777  33.276  1.00  5.25           O  
ATOM    126  CB  LEU A  15      12.990  26.674  31.305  1.00  7.21           C  
ATOM    127  CG  LEU A  15      11.601  27.137  30.871  1.00  6.63           C  
ATOM    128  CD1 LEU A  15      10.786  25.990  30.331  1.00  7.20           C  
ATOM    129  CD2 LEU A  15      10.914  27.789  32.052  1.00  9.80           C  
ATOM    130  N   GLY A  16      16.345  27.953  31.752  1.00  6.17           N  
ATOM    131  CA  GLY A  16      17.641  27.693  32.364  1.00  4.89           C  
ATOM    132  C   GLY A  16      18.321  26.359  32.110  1.00  4.92           C  
ATOM    133  O   GLY A  16      19.180  25.958  32.885  1.00  6.33           O  
ATOM    134  N   MET A  17      17.988  25.711  30.998  1.00  4.50           N  
ATOM    135  CA  MET A  17      18.542  24.404  30.633  1.00  3.98           C  
ATOM    136  C   MET A  17      19.909  24.415  29.969  1.00  4.40           C  
ATOM    137  O   MET A  17      20.642  23.412  30.001  1.00  2.91           O  
ATOM    138  CB  MET A  17      17.564  23.668  29.713  1.00  2.00           C  
ATOM    139  CG  MET A  17      16.282  23.334  30.409  1.00  2.21           C  
ATOM    140  SD  MET A  17      16.549  22.097  31.688  1.00  6.41           S  
ATOM    141  CE  MET A  17      15.892  20.638  30.726  1.00  2.00           C  
ATOM    142  N   ASP A  18      20.278  25.554  29.404  1.00  3.16           N  
ATOM    143  CA  ASP A  18      21.550  25.654  28.702  1.00  5.49           C  
ATOM    144  C   ASP A  18      22.739  25.561  29.669  1.00  6.28           C  
ATOM    145  O   ASP A  18      23.034  26.511  30.397  1.00  6.80           O  
ATOM    146  CB  ASP A  18      21.574  26.955  27.888  1.00  4.32           C  
ATOM    147  CG  ASP A  18      22.764  27.061  26.950  1.00  6.09           C  
ATOM    148  OD1 ASP A  18      23.560  26.110  26.781  1.00  3.36           O  
ATOM    149  OD2 ASP A  18      22.901  28.140  26.359  1.00 13.19           O  
ATOM    150  N   GLY A  19      23.405  24.403  29.666  1.00  6.58           N  
ATOM    151  CA  GLY A  19      24.561  24.172  30.516  1.00  2.64           C  
ATOM    152  C   GLY A  19      24.211  23.741  31.929  1.00  2.73           C  
ATOM    153  O   GLY A  19      25.084  23.719  32.804  1.00  2.00           O  
ATOM    154  N   TYR A  20      22.941  23.406  32.166  1.00  2.00           N  
ATOM    155  CA  TYR A  20      22.501  22.986  33.498  1.00  2.64           C  
ATOM    156  C   TYR A  20      23.317  21.759  33.833  1.00  2.53           C  
ATOM    157  O   TYR A  20      23.244  20.768  33.109  1.00  3.23           O  
ATOM    158  CB  TYR A  20      20.998  22.625  33.534  1.00  2.00           C  
ATOM    159  CG  TYR A  20      20.527  22.255  34.920  1.00  2.14           C  
ATOM    160  CD1 TYR A  20      20.304  23.244  35.880  1.00  2.23           C  
ATOM    161  CD2 TYR A  20      20.338  20.910  35.301  1.00  2.00           C  
ATOM    162  CE1 TYR A  20      19.910  22.927  37.189  1.00  3.75           C  
ATOM    163  CE2 TYR A  20      19.939  20.574  36.625  1.00  2.00           C  
ATOM    164  CZ  TYR A  20      19.724  21.600  37.561  1.00  2.00           C  
ATOM    165  OH  TYR A  20      19.301  21.344  38.851  1.00  2.00           O  
ATOM    166  N   ARG A  21      24.132  21.852  34.884  1.00  2.91           N  
ATOM    167  CA  ARG A  21      24.985  20.752  35.324  1.00  4.71           C  
ATOM    168  C   ARG A  21      25.872  20.215  34.188  1.00  6.74           C  
ATOM    169  O   ARG A  21      26.006  18.992  33.991  1.00  2.04           O  
ATOM    170  CB  ARG A  21      24.114  19.643  35.933  1.00  8.42           C  
ATOM    171  CG  ARG A  21      23.407  20.075  37.209  1.00  8.57           C  
ATOM    172  CD  ARG A  21      24.375  20.105  38.390  1.00 13.81           C  
ATOM    173  NE  ARG A  21      24.838  18.742  38.681  1.00 16.62           N  
ATOM    174  CZ  ARG A  21      25.692  18.394  39.643  1.00 12.39           C  
ATOM    175  NH1 ARG A  21      26.009  17.120  39.777  1.00  4.92           N  
ATOM    176  NH2 ARG A  21      26.246  19.303  40.450  1.00 14.79           N  
ATOM    177  N   GLY A  22      26.389  21.153  33.391  1.00  4.32           N  
ATOM    178  CA  GLY A  22      27.273  20.838  32.290  1.00  3.99           C  
ATOM    179  C   GLY A  22      26.595  20.339  31.038  1.00  2.67           C  
ATOM    180  O   GLY A  22      27.278  20.018  30.082  1.00  2.00           O  
ATOM    181  N   ILE A  23      25.268  20.259  31.043  1.00  2.93           N  
ATOM    182  CA  ILE A  23      24.538  19.780  29.871  1.00  3.61           C  
ATOM    183  C   ILE A  23      24.179  20.910  28.902  1.00  2.00           C  
ATOM    184  O   ILE A  23      23.448  21.819  29.254  1.00  3.36           O  
ATOM    185  CB  ILE A  23      23.242  18.971  30.253  1.00  2.00           C  
ATOM    186  CG1 ILE A  23      23.592  17.830  31.227  1.00  2.00           C  
ATOM    187  CG2 ILE A  23      22.613  18.363  28.991  1.00  2.13           C  
ATOM    188  CD1 ILE A  23      22.423  17.244  31.956  1.00  2.00           C  
ATOM    189  N   SER A  24      24.703  20.846  27.681  1.00  2.19           N  
ATOM    190  CA  SER A  24      24.391  21.858  26.687  1.00  2.71           C  
ATOM    191  C   SER A  24      22.946  21.734  26.168  1.00  3.92           C  
ATOM    192  O   SER A  24      22.284  20.690  26.293  1.00  2.00           O  
ATOM    193  CB  SER A  24      25.379  21.789  25.518  1.00  2.66           C  
ATOM    194  OG  SER A  24      25.021  20.778  24.617  1.00  3.20           O  
ATOM    195  N   LEU A  25      22.471  22.807  25.549  1.00  2.00           N  
ATOM    196  CA  LEU A  25      21.131  22.842  24.989  1.00  2.06           C  
ATOM    197  C   LEU A  25      20.920  21.799  23.895  1.00  2.00           C  
ATOM    198  O   LEU A  25      19.878  21.150  23.854  1.00  2.00           O  
ATOM    199  CB  LEU A  25      20.851  24.235  24.419  1.00  4.24           C  
ATOM    200  CG  LEU A  25      19.388  24.651  24.406  1.00  4.13           C  
ATOM    201  CD1 LEU A  25      18.848  24.629  25.855  1.00  6.99           C  
ATOM    202  CD2 LEU A  25      19.282  26.047  23.811  1.00  4.83           C  
ATOM    203  N   ALA A  26      21.903  21.666  23.000  1.00  3.98           N  
ATOM    204  CA  ALA A  26      21.843  20.708  21.892  1.00  2.67           C  
ATOM    205  C   ALA A  26      21.551  19.284  22.381  1.00  3.39           C  
ATOM    206  O   ALA A  26      20.758  18.562  21.777  1.00  2.96           O  
ATOM    207  CB  ALA A  26      23.144  20.748  21.090  1.00  2.00           C  
ATOM    208  N   LEU A  27      22.202  18.890  23.471  1.00  2.06           N  
ATOM    209  CA  LEU A  27      22.019  17.572  24.056  1.00  2.00           C  
ATOM    210  C   LEU A  27      20.599  17.412  24.594  1.00  4.04           C  
ATOM    211  O   LEU A  27      20.008  16.331  24.473  1.00  2.00           O  
ATOM    212  CB  LEU A  27      23.013  17.367  25.194  1.00  4.03           C  
ATOM    213  CG  LEU A  27      24.502  17.328  24.858  1.00  4.73           C  
ATOM    214  CD1 LEU A  27      25.275  17.309  26.157  1.00  7.79           C  
ATOM    215  CD2 LEU A  27      24.847  16.113  24.007  1.00  2.94           C  
ATOM    216  N   TRP A  28      20.087  18.458  25.255  1.00  2.96           N  
ATOM    217  CA  TRP A  28      18.720  18.432  25.780  1.00  5.74           C  
ATOM    218  C   TRP A  28      17.750  18.367  24.602  1.00  5.90           C  
ATOM    219  O   TRP A  28      16.704  17.718  24.683  1.00  5.74           O  
ATOM    220  CB  TRP A  28      18.394  19.679  26.600  1.00  4.19           C  
ATOM    221  CG  TRP A  28      18.955  19.731  27.964  1.00  2.00           C  
ATOM    222  CD1 TRP A  28      19.823  20.668  28.442  1.00  3.47           C  
ATOM    223  CD2 TRP A  28      18.603  18.904  29.088  1.00  2.99           C  
ATOM    224  NE1 TRP A  28      20.020  20.496  29.795  1.00  2.40           N  
ATOM    225  CE2 TRP A  28      19.287  19.418  30.218  1.00  2.00           C  
ATOM    226  CE3 TRP A  28      17.767  17.785  29.255  1.00  2.00           C  
ATOM    227  CZ2 TRP A  28      19.165  18.857  31.492  1.00  4.44           C  
ATOM    228  CZ3 TRP A  28      17.644  17.220  30.541  1.00  2.53           C  
ATOM    229  CH2 TRP A  28      18.337  17.758  31.633  1.00  2.00           C  
ATOM    230  N   MET A  29      18.062  19.106  23.540  1.00  5.66           N  
ATOM    231  CA  MET A  29      17.241  19.099  22.342  1.00  7.72           C  
ATOM    232  C   MET A  29      17.262  17.682  21.739  1.00  8.57           C  
ATOM    233  O   MET A  29      16.232  17.148  21.312  1.00  7.16           O  
ATOM    234  CB  MET A  29      17.778  20.103  21.309  1.00  7.14           C  
ATOM    235  CG  MET A  29      17.416  21.569  21.578  1.00  7.64           C  
ATOM    236  SD  MET A  29      15.622  21.862  21.500  1.00  6.61           S  
ATOM    237  CE  MET A  29      15.316  21.495  19.784  1.00  4.06           C  
ATOM    238  N   CYS A  30      18.435  17.060  21.739  1.00  6.42           N  
ATOM    239  CA  CYS A  30      18.559  15.727  21.188  1.00  5.68           C  
ATOM    240  C   CYS A  30      17.686  14.736  21.972  1.00  4.94           C  
ATOM    241  O   CYS A  30      16.940  13.953  21.374  1.00  2.00           O  
ATOM    242  CB  CYS A  30      20.019  15.307  21.202  1.00  5.86           C  
ATOM    243  SG  CYS A  30      20.317  13.718  20.379  1.00  4.07           S  
ATOM    244  N   LEU A  31      17.707  14.874  23.301  1.00  2.50           N  
ATOM    245  CA  LEU A  31      16.931  14.031  24.210  1.00  2.88           C  
ATOM    246  C   LEU A  31      15.443  14.099  23.893  1.00  3.49           C  
ATOM    247  O   LEU A  31      14.816  13.076  23.675  1.00  2.00           O  
ATOM    248  CB  LEU A  31      17.142  14.438  25.681  1.00  3.05           C  
ATOM    249  CG  LEU A  31      16.344  13.593  26.683  1.00  2.00           C  
ATOM    250  CD1 LEU A  31      16.849  12.131  26.628  1.00  2.00           C  
ATOM    251  CD2 LEU A  31      16.457  14.143  28.093  1.00  3.12           C  
ATOM    252  N   ALA A  32      14.881  15.304  23.894  1.00  3.68           N  
ATOM    253  CA  ALA A  32      13.450  15.519  23.599  1.00  2.97           C  
ATOM    254  C   ALA A  32      13.016  14.972  22.233  1.00  2.23           C  
ATOM    255  O   ALA A  32      11.968  14.339  22.114  1.00  3.29           O  
ATOM    256  CB  ALA A  32      13.101  17.042  23.714  1.00  2.00           C  
ATOM    257  N   LYS A  33      13.821  15.204  21.200  1.00  3.81           N  
ATOM    258  CA  LYS A  33      13.506  14.730  19.851  1.00  4.88           C  
ATOM    259  C   LYS A  33      13.341  13.224  19.853  1.00  6.26           C  
ATOM    260  O   LYS A  33      12.342  12.690  19.369  1.00  3.79           O  
ATOM    261  CB  LYS A  33      14.625  15.086  18.864  1.00  6.35           C  
ATOM    262  CG  LYS A  33      14.325  14.702  17.400  1.00  7.90           C  
ATOM    263  CD  LYS A  33      12.955  15.257  16.993  1.00 12.29           C  
ATOM    264  CE  LYS A  33      12.632  15.067  15.519  1.00 17.23           C  
ATOM    265  NZ  LYS A  33      12.628  13.640  15.099  1.00 22.48           N  
ATOM    266  N   TRP A  34      14.331  12.543  20.408  1.00  4.65           N  
ATOM    267  CA  TRP A  34      14.304  11.100  20.449  1.00  7.09           C  
ATOM    268  C   TRP A  34      13.370  10.526  21.491  1.00  6.38           C  
ATOM    269  O   TRP A  34      12.804   9.450  21.307  1.00  7.71           O  
ATOM    270  CB  TRP A  34      15.729  10.569  20.586  1.00  8.88           C  
ATOM    271  CG  TRP A  34      16.447  10.724  19.295  1.00  6.39           C  
ATOM    272  CD1 TRP A  34      17.496  11.549  19.027  1.00  5.86           C  
ATOM    273  CD2 TRP A  34      16.097  10.098  18.059  1.00  6.88           C  
ATOM    274  NE1 TRP A  34      17.810  11.491  17.694  1.00  8.11           N  
ATOM    275  CE2 TRP A  34      16.960  10.608  17.074  1.00  7.49           C  
ATOM    276  CE3 TRP A  34      15.120   9.159  17.686  1.00  6.58           C  
ATOM    277  CZ2 TRP A  34      16.877  10.218  15.734  1.00  9.60           C  
ATOM    278  CZ3 TRP A  34      15.036   8.772  16.357  1.00  6.91           C  
ATOM    279  CH2 TRP A  34      15.908   9.301  15.396  1.00  8.53           C  
ATOM    280  N   GLU A  35      13.155  11.257  22.570  1.00  6.53           N  
ATOM    281  CA  GLU A  35      12.267  10.755  23.602  1.00  5.40           C  
ATOM    282  C   GLU A  35      10.793  10.875  23.225  1.00  6.07           C  
ATOM    283  O   GLU A  35      10.009   9.949  23.483  1.00  4.02           O  
ATOM    284  CB  GLU A  35      12.526  11.443  24.950  1.00  4.80           C  
ATOM    285  CG  GLU A  35      13.764  10.960  25.706  1.00  4.78           C  
ATOM    286  CD  GLU A  35      13.786   9.449  25.952  1.00 11.62           C  
ATOM    287  OE1 GLU A  35      12.713   8.852  26.207  1.00  9.88           O  
ATOM    288  OE2 GLU A  35      14.887   8.851  25.886  1.00 12.14           O  
ATOM    289  N   SER A  36      10.427  11.957  22.542  1.00  3.31           N  
ATOM    290  CA  SER A  36       9.022  12.176  22.203  1.00  4.06           C  
ATOM    291  C   SER A  36       8.708  12.913  20.907  1.00  4.09           C  
ATOM    292  O   SER A  36       7.543  13.253  20.670  1.00  3.60           O  
ATOM    293  CB  SER A  36       8.388  12.997  23.330  1.00  6.51           C  
ATOM    294  OG  SER A  36       8.968  14.297  23.377  1.00  5.35           O  
ATOM    295  N   GLY A  37       9.717  13.189  20.084  1.00  3.77           N  
ATOM    296  CA  GLY A  37       9.489  13.938  18.860  1.00  2.96           C  
ATOM    297  C   GLY A  37       8.912  15.305  19.186  1.00  3.68           C  
ATOM    298  O   GLY A  37       8.001  15.770  18.499  1.00  2.34           O  
ATOM    299  N   TYR A  38       9.385  15.895  20.288  1.00  4.75           N  
ATOM    300  CA  TYR A  38       8.941  17.211  20.770  1.00  6.43           C  
ATOM    301  C   TYR A  38       7.457  17.319  21.144  1.00  8.22           C  
ATOM    302  O   TYR A  38       6.894  18.427  21.131  1.00  9.09           O  
ATOM    303  CB  TYR A  38       9.264  18.314  19.757  1.00  2.00           C  
ATOM    304  CG  TYR A  38      10.676  18.338  19.227  1.00  4.30           C  
ATOM    305  CD1 TYR A  38      10.919  18.675  17.897  1.00  2.00           C  
ATOM    306  CD2 TYR A  38      11.774  18.109  20.066  1.00  4.34           C  
ATOM    307  CE1 TYR A  38      12.208  18.793  17.418  1.00  3.61           C  
ATOM    308  CE2 TYR A  38      13.071  18.231  19.599  1.00  2.00           C  
ATOM    309  CZ  TYR A  38      13.277  18.573  18.271  1.00  4.44           C  
ATOM    310  OH  TYR A  38      14.554  18.689  17.767  1.00  3.97           O  
ATOM    311  N   ASN A  39       6.847  16.205  21.544  1.00  6.45           N  
ATOM    312  CA  ASN A  39       5.427  16.166  21.906  1.00  3.79           C  
ATOM    313  C   ASN A  39       5.287  16.075  23.433  1.00  5.25           C  
ATOM    314  O   ASN A  39       5.751  15.111  24.044  1.00  5.81           O  
ATOM    315  CB  ASN A  39       4.798  14.941  21.218  1.00  5.54           C  
ATOM    316  CG  ASN A  39       3.335  14.699  21.597  1.00  5.39           C  
ATOM    317  OD1 ASN A  39       2.612  15.599  22.035  1.00  3.16           O  
ATOM    318  ND2 ASN A  39       2.884  13.465  21.383  1.00  2.50           N  
ATOM    319  N   THR A  40       4.675  17.088  24.048  1.00  3.68           N  
ATOM    320  CA  THR A  40       4.468  17.120  25.489  1.00  5.97           C  
ATOM    321  C   THR A  40       3.397  16.115  25.963  1.00  5.78           C  
ATOM    322  O   THR A  40       3.295  15.822  27.164  1.00  6.11           O  
ATOM    323  CB  THR A  40       4.063  18.549  26.001  1.00  6.98           C  
ATOM    324  OG1 THR A  40       2.800  18.932  25.437  1.00  6.65           O  
ATOM    325  CG2 THR A  40       5.108  19.593  25.609  1.00  4.68           C  
ATOM    326  N   ARG A  41       2.546  15.639  25.060  1.00  8.04           N  
ATOM    327  CA  ARG A  41       1.551  14.664  25.503  1.00 10.71           C  
ATOM    328  C   ARG A  41       1.968  13.200  25.202  1.00  9.72           C  
ATOM    329  O   ARG A  41       1.195  12.245  25.426  1.00  7.28           O  
ATOM    330  CB  ARG A  41       0.139  15.003  24.998  1.00 11.87           C  
ATOM    331  CG  ARG A  41       0.043  15.738  23.679  1.00 17.59           C  
ATOM    332  CD  ARG A  41      -1.219  15.361  22.854  1.00 22.63           C  
ATOM    333  NE  ARG A  41      -2.464  15.299  23.628  1.00 25.57           N  
ATOM    334  CZ  ARG A  41      -3.325  14.283  23.568  1.00 28.78           C  
ATOM    335  NH1 ARG A  41      -3.074  13.243  22.777  1.00 27.05           N  
ATOM    336  NH2 ARG A  41      -4.442  14.303  24.291  1.00 26.77           N  
ATOM    337  N   ALA A  42       3.226  13.025  24.788  1.00  8.59           N  
ATOM    338  CA  ALA A  42       3.769  11.697  24.469  1.00  7.40           C  
ATOM    339  C   ALA A  42       3.678  10.754  25.662  1.00  6.63           C  
ATOM    340  O   ALA A  42       3.931  11.154  26.802  1.00  4.76           O  
ATOM    341  CB  ALA A  42       5.204  11.809  23.997  1.00  3.42           C  
ATOM    342  N   THR A  43       3.245   9.520  25.410  1.00  6.79           N  
ATOM    343  CA  THR A  43       3.133   8.545  26.484  1.00  7.85           C  
ATOM    344  C   THR A  43       3.592   7.191  26.043  1.00  9.20           C  
ATOM    345  O   THR A  43       3.412   6.801  24.881  1.00 10.03           O  
ATOM    346  CB  THR A  43       1.710   8.408  27.023  1.00  7.80           C  
ATOM    347  OG1 THR A  43       0.797   8.208  25.930  1.00  7.06           O  
ATOM    348  CG2 THR A  43       1.329   9.646  27.866  1.00  7.76           C  
ATOM    349  N   ASN A  44       4.175   6.473  26.999  1.00  9.99           N  
ATOM    350  CA  ASN A  44       4.671   5.139  26.757  1.00 10.55           C  
ATOM    351  C   ASN A  44       4.443   4.209  27.930  1.00  9.22           C  
ATOM    352  O   ASN A  44       5.012   4.404  29.004  1.00  7.64           O  
ATOM    353  CB  ASN A  44       6.156   5.190  26.473  1.00 17.03           C  
ATOM    354  CG  ASN A  44       6.491   4.634  25.127  1.00 20.71           C  
ATOM    355  OD1 ASN A  44       6.502   5.373  24.120  1.00 26.99           O  
ATOM    356  ND2 ASN A  44       6.748   3.326  25.074  1.00 21.10           N  
ATOM    357  N   TYR A  45       3.582   3.217  27.735  1.00  6.92           N  
ATOM    358  CA  TYR A  45       3.333   2.247  28.779  1.00  5.71           C  
ATOM    359  C   TYR A  45       4.342   1.121  28.630  1.00  5.59           C  
ATOM    360  O   TYR A  45       4.657   0.705  27.524  1.00  6.63           O  
ATOM    361  CB  TYR A  45       1.936   1.666  28.673  1.00  7.12           C  
ATOM    362  CG  TYR A  45       1.634   0.690  29.775  1.00  6.09           C  
ATOM    363  CD1 TYR A  45       1.133  -0.570  29.484  1.00  5.34           C  
ATOM    364  CD2 TYR A  45       1.851   1.024  31.117  1.00  8.91           C  
ATOM    365  CE1 TYR A  45       0.848  -1.480  30.493  1.00  5.65           C  
ATOM    366  CE2 TYR A  45       1.569   0.123  32.137  1.00  7.58           C  
ATOM    367  CZ  TYR A  45       1.063  -1.131  31.816  1.00  6.68           C  
ATOM    368  OH  TYR A  45       0.743  -2.040  32.800  1.00  2.54           O  
ATOM    369  N   ASN A  46       4.862   0.647  29.752  1.00  8.55           N  
ATOM    370  CA  ASN A  46       5.838  -0.428  29.744  1.00  8.56           C  
ATOM    371  C   ASN A  46       5.198  -1.600  30.493  1.00  8.62           C  
ATOM    372  O   ASN A  46       5.294  -1.691  31.722  1.00  8.20           O  
ATOM    373  CB  ASN A  46       7.118   0.036  30.445  1.00 12.76           C  
ATOM    374  CG  ASN A  46       7.666   1.344  29.872  1.00 15.23           C  
ATOM    375  OD1 ASN A  46       8.350   1.344  28.840  1.00 15.87           O  
ATOM    376  ND2 ASN A  46       7.363   2.466  30.533  1.00 11.95           N  
ATOM    377  N   ALA A  47       4.500  -2.464  29.760  1.00  7.09           N  
ATOM    378  CA  ALA A  47       3.825  -3.628  30.362  1.00  9.21           C  
ATOM    379  C   ALA A  47       4.758  -4.511  31.198  1.00  8.16           C  
ATOM    380  O   ALA A  47       4.348  -5.048  32.225  1.00  8.84           O  
ATOM    381  CB  ALA A  47       3.139  -4.458  29.286  1.00  7.88           C  
ATOM    382  N   GLY A  48       6.020  -4.614  30.790  1.00  7.49           N  
ATOM    383  CA  GLY A  48       6.969  -5.430  31.530  1.00  9.30           C  
ATOM    384  C   GLY A  48       7.097  -5.059  33.000  1.00 11.27           C  
ATOM    385  O   GLY A  48       7.196  -5.938  33.866  1.00 10.38           O  
ATOM    386  N   ASP A  49       7.119  -3.760  33.304  1.00 10.81           N  
ATOM    387  CA  ASP A  49       7.252  -3.357  34.691  1.00 10.10           C  
ATOM    388  C   ASP A  49       6.133  -2.460  35.164  1.00 12.83           C  
ATOM    389  O   ASP A  49       6.196  -1.900  36.254  1.00 14.47           O  
ATOM    390  CB  ASP A  49       8.625  -2.749  34.965  1.00  9.83           C  
ATOM    391  CG  ASP A  49       8.769  -1.331  34.455  1.00  8.82           C  
ATOM    392  OD1 ASP A  49       7.995  -0.892  33.574  1.00 11.88           O  
ATOM    393  OD2 ASP A  49       9.690  -0.652  34.944  1.00  9.81           O  
ATOM    394  N   ARG A  50       5.103  -2.347  34.329  1.00 13.04           N  
ATOM    395  CA  ARG A  50       3.909  -1.559  34.620  1.00 12.06           C  
ATOM    396  C   ARG A  50       4.092  -0.092  35.034  1.00 10.97           C  
ATOM    397  O   ARG A  50       3.456   0.388  35.970  1.00 13.12           O  
ATOM    398  CB  ARG A  50       3.036  -2.307  35.633  1.00 13.33           C  
ATOM    399  CG  ARG A  50       2.567  -3.666  35.162  1.00 13.67           C  
ATOM    400  CD  ARG A  50       1.215  -3.977  35.758  1.00 19.23           C  
ATOM    401  NE  ARG A  50       0.857  -5.390  35.634  1.00 21.41           N  
ATOM    402  CZ  ARG A  50       0.591  -6.173  36.673  1.00 20.63           C  
ATOM    403  NH1 ARG A  50       0.280  -7.445  36.486  1.00 21.08           N  
ATOM    404  NH2 ARG A  50       0.635  -5.677  37.904  1.00 22.09           N  
ATOM    405  N   SER A  51       4.984   0.609  34.353  1.00 10.54           N  
ATOM    406  CA  SER A  51       5.210   2.019  34.631  1.00  8.54           C  
ATOM    407  C   SER A  51       4.943   2.757  33.315  1.00  8.77           C  
ATOM    408  O   SER A  51       4.799   2.120  32.268  1.00  5.49           O  
ATOM    409  CB  SER A  51       6.647   2.251  35.066  1.00  6.52           C  
ATOM    410  OG  SER A  51       7.520   1.970  33.997  1.00  5.38           O  
ATOM    411  N   THR A  52       4.928   4.087  33.357  1.00  6.94           N  
ATOM    412  CA  THR A  52       4.681   4.893  32.163  1.00  5.71           C  
ATOM    413  C   THR A  52       5.660   6.077  32.023  1.00  4.92           C  
ATOM    414  O   THR A  52       6.051   6.697  33.011  1.00  4.30           O  
ATOM    415  CB  THR A  52       3.221   5.440  32.171  1.00  3.91           C  
ATOM    416  OG1 THR A  52       2.296   4.345  32.180  1.00  6.08           O  
ATOM    417  CG2 THR A  52       2.950   6.310  30.946  1.00  3.38           C  
ATOM    418  N   ASP A  53       6.060   6.366  30.782  1.00  6.13           N  
ATOM    419  CA  ASP A  53       6.946   7.488  30.477  1.00  3.00           C  
ATOM    420  C   ASP A  53       6.021   8.611  30.009  1.00  4.53           C  
ATOM    421  O   ASP A  53       5.213   8.424  29.104  1.00  2.00           O  
ATOM    422  CB  ASP A  53       7.929   7.126  29.374  1.00  2.89           C  
ATOM    423  CG  ASP A  53       8.842   5.987  29.762  1.00  6.01           C  
ATOM    424  OD1 ASP A  53       9.348   5.980  30.909  1.00  2.35           O  
ATOM    425  OD2 ASP A  53       9.038   5.085  28.918  1.00 11.19           O  
ATOM    426  N   TYR A  54       6.153   9.777  30.631  1.00  4.46           N  
ATOM    427  CA  TYR A  54       5.282  10.910  30.319  1.00  6.20           C  
ATOM    428  C   TYR A  54       5.936  12.157  29.759  1.00  4.49           C  
ATOM    429  O   TYR A  54       7.023  12.531  30.191  1.00  3.74           O  
ATOM    430  CB  TYR A  54       4.535  11.330  31.581  1.00  3.99           C  
ATOM    431  CG  TYR A  54       3.568  10.308  32.132  1.00  5.56           C  
ATOM    432  CD1 TYR A  54       2.225  10.373  31.800  1.00  2.00           C  
ATOM    433  CD2 TYR A  54       3.982   9.340  33.075  1.00  4.32           C  
ATOM    434  CE1 TYR A  54       1.301   9.528  32.392  1.00  4.68           C  
ATOM    435  CE2 TYR A  54       3.065   8.493  33.680  1.00  2.00           C  
ATOM    436  CZ  TYR A  54       1.718   8.599  33.332  1.00  4.44           C  
ATOM    437  OH  TYR A  54       0.768   7.816  33.940  1.00  3.79           O  
ATOM    438  N   GLY A  55       5.251  12.782  28.800  1.00  5.72           N  
ATOM    439  CA  GLY A  55       5.692  14.035  28.206  1.00  3.44           C  
ATOM    440  C   GLY A  55       6.843  14.140  27.231  1.00  3.06           C  
ATOM    441  O   GLY A  55       7.345  13.146  26.686  1.00  3.25           O  
ATOM    442  N   ILE A  56       7.286  15.381  27.053  1.00  4.02           N  
ATOM    443  CA  ILE A  56       8.376  15.722  26.141  1.00  2.44           C  
ATOM    444  C   ILE A  56       9.750  15.044  26.444  1.00  2.00           C  
ATOM    445  O   ILE A  56      10.512  14.753  25.523  1.00  2.26           O  
ATOM    446  CB  ILE A  56       8.473  17.285  25.977  1.00  3.03           C  
ATOM    447  CG1 ILE A  56       9.165  17.647  24.669  1.00  3.92           C  
ATOM    448  CG2 ILE A  56       9.221  17.954  27.155  1.00  2.00           C  
ATOM    449  CD1 ILE A  56       9.008  19.112  24.318  1.00  4.03           C  
ATOM    450  N   PHE A  57      10.042  14.755  27.718  1.00  3.64           N  
ATOM    451  CA  PHE A  57      11.299  14.101  28.092  1.00  2.58           C  
ATOM    452  C   PHE A  57      11.128  12.633  28.464  1.00  4.88           C  
ATOM    453  O   PHE A  57      12.104  11.955  28.817  1.00  2.65           O  
ATOM    454  CB  PHE A  57      11.958  14.833  29.261  1.00  3.20           C  
ATOM    455  CG  PHE A  57      12.425  16.229  28.923  1.00  5.54           C  
ATOM    456  CD1 PHE A  57      12.003  17.326  29.684  1.00  5.90           C  
ATOM    457  CD2 PHE A  57      13.280  16.456  27.842  1.00  3.49           C  
ATOM    458  CE1 PHE A  57      12.422  18.618  29.369  1.00  2.83           C  
ATOM    459  CE2 PHE A  57      13.703  17.760  27.523  1.00  2.00           C  
ATOM    460  CZ  PHE A  57      13.275  18.831  28.284  1.00  2.00           C  
ATOM    461  N   GLN A  58       9.881  12.153  28.382  1.00  2.88           N  
ATOM    462  CA  GLN A  58       9.512  10.774  28.703  1.00  3.20           C  
ATOM    463  C   GLN A  58      10.044  10.323  30.056  1.00  2.28           C  
ATOM    464  O   GLN A  58      10.882   9.430  30.175  1.00  2.27           O  
ATOM    465  CB  GLN A  58       9.922   9.837  27.570  1.00  5.52           C  
ATOM    466  CG  GLN A  58       9.095  10.062  26.299  1.00  5.08           C  
ATOM    467  CD  GLN A  58       7.691   9.477  26.439  1.00  8.43           C  
ATOM    468  OE1 GLN A  58       7.502   8.274  26.272  1.00  9.21           O  
ATOM    469  NE2 GLN A  58       6.712  10.319  26.771  1.00  2.00           N  
ATOM    470  N   ILE A  59       9.523  10.962  31.084  1.00  2.00           N  
ATOM    471  CA  ILE A  59       9.942  10.699  32.447  1.00  3.04           C  
ATOM    472  C   ILE A  59       9.103   9.577  33.052  1.00  3.93           C  
ATOM    473  O   ILE A  59       7.877   9.639  33.051  1.00  5.44           O  
ATOM    474  CB  ILE A  59       9.893  11.996  33.257  1.00  2.00           C  
ATOM    475  CG1 ILE A  59      10.909  12.979  32.656  1.00  2.00           C  
ATOM    476  CG2 ILE A  59      10.212  11.726  34.723  1.00  2.00           C  
ATOM    477  CD1 ILE A  59      10.761  14.409  33.105  1.00  2.00           C  
ATOM    478  N   ASN A  60       9.793   8.518  33.458  1.00  2.80           N  
ATOM    479  CA  ASN A  60       9.187   7.323  34.026  1.00  3.60           C  
ATOM    480  C   ASN A  60       8.497   7.495  35.393  1.00  6.62           C  
ATOM    481  O   ASN A  60       9.064   8.040  36.356  1.00  5.29           O  
ATOM    482  CB  ASN A  60      10.245   6.211  34.063  1.00  5.21           C  
ATOM    483  CG  ASN A  60       9.670   4.878  34.476  1.00  3.65           C  
ATOM    484  OD1 ASN A  60       9.610   4.568  35.647  1.00  4.69           O  
ATOM    485  ND2 ASN A  60       9.219   4.096  33.511  1.00  6.77           N  
ATOM    486  N   SER A  61       7.282   6.966  35.481  1.00  6.77           N  
ATOM    487  CA  SER A  61       6.452   7.043  36.679  1.00  7.18           C  
ATOM    488  C   SER A  61       6.895   6.215  37.884  1.00 11.32           C  
ATOM    489  O   SER A  61       6.471   6.463  39.026  1.00  8.00           O  
ATOM    490  CB  SER A  61       5.039   6.613  36.322  1.00 10.51           C  
ATOM    491  OG  SER A  61       5.036   5.280  35.834  1.00  9.93           O  
ATOM    492  N   ARG A  62       7.686   5.182  37.623  1.00 12.38           N  
ATOM    493  CA  ARG A  62       8.157   4.298  38.676  1.00 14.70           C  
ATOM    494  C   ARG A  62       9.149   4.976  39.615  1.00 14.22           C  
ATOM    495  O   ARG A  62       9.281   4.555  40.773  1.00 17.27           O  
ATOM    496  CB  ARG A  62       8.755   3.037  38.044  1.00 17.61           C  
ATOM    497  CG  ARG A  62       9.315   2.025  39.015  1.00 23.48           C  
ATOM    498  CD  ARG A  62       9.502   0.689  38.307  1.00 27.99           C  
ATOM    499  NE  ARG A  62       8.216   0.037  38.070  1.00 33.62           N  
ATOM    500  CZ  ARG A  62       7.394  -0.340  39.045  1.00 37.17           C  
ATOM    501  NH1 ARG A  62       6.236  -0.923  38.759  1.00 38.06           N  
ATOM    502  NH2 ARG A  62       7.740  -0.154  40.322  1.00 37.51           N  
ATOM    503  N   TYR A  63       9.757   6.081  39.170  1.00 12.25           N  
ATOM    504  CA  TYR A  63      10.751   6.769  39.991  1.00 10.78           C  
ATOM    505  C   TYR A  63      10.649   8.283  40.194  1.00 11.36           C  
ATOM    506  O   TYR A  63      10.991   8.783  41.268  1.00 14.57           O  
ATOM    507  CB  TYR A  63      12.155   6.481  39.446  1.00 11.43           C  
ATOM    508  CG  TYR A  63      12.410   5.049  38.989  1.00 13.49           C  
ATOM    509  CD1 TYR A  63      12.371   4.718  37.634  1.00 12.74           C  
ATOM    510  CD2 TYR A  63      12.702   4.030  39.911  1.00 10.10           C  
ATOM    511  CE1 TYR A  63      12.614   3.411  37.201  1.00 13.91           C  
ATOM    512  CE2 TYR A  63      12.941   2.732  39.495  1.00 10.28           C  
ATOM    513  CZ  TYR A  63      12.897   2.427  38.136  1.00 13.07           C  
ATOM    514  OH  TYR A  63      13.146   1.142  37.708  1.00 16.86           O  
ATOM    515  N   TRP A  64      10.153   8.998  39.184  1.00  9.61           N  
ATOM    516  CA  TRP A  64      10.095  10.466  39.174  1.00  4.77           C  
ATOM    517  C   TRP A  64       8.795  11.193  39.422  1.00  3.50           C  
ATOM    518  O   TRP A  64       8.798  12.287  39.991  1.00  5.07           O  
ATOM    519  CB  TRP A  64      10.654  10.938  37.840  1.00  2.00           C  
ATOM    520  CG  TRP A  64      11.971  10.342  37.619  1.00  2.32           C  
ATOM    521  CD1 TRP A  64      12.275   9.330  36.778  1.00  2.00           C  
ATOM    522  CD2 TRP A  64      13.176  10.676  38.313  1.00  3.18           C  
ATOM    523  NE1 TRP A  64      13.602   8.998  36.901  1.00  7.33           N  
ATOM    524  CE2 TRP A  64      14.179   9.815  37.839  1.00  2.76           C  
ATOM    525  CE3 TRP A  64      13.500  11.621  39.297  1.00  2.00           C  
ATOM    526  CZ2 TRP A  64      15.494   9.868  38.306  1.00  4.45           C  
ATOM    527  CZ3 TRP A  64      14.807  11.673  39.764  1.00  5.78           C  
ATOM    528  CH2 TRP A  64      15.788  10.800  39.269  1.00  3.92           C  
ATOM    529  N   CYS A  65       7.693  10.620  38.954  1.00  5.28           N  
ATOM    530  CA  CYS A  65       6.391  11.246  39.137  1.00  5.47           C  
ATOM    531  C   CYS A  65       5.349  10.208  39.504  1.00  4.06           C  
ATOM    532  O   CYS A  65       5.482   9.034  39.172  1.00  5.25           O  
ATOM    533  CB  CYS A  65       5.971  11.970  37.863  1.00  8.10           C  
ATOM    534  SG  CYS A  65       5.621  10.848  36.469  1.00  2.71           S  
ATOM    535  N   ASN A  66       4.312  10.648  40.191  1.00  3.83           N  
ATOM    536  CA  ASN A  66       3.237   9.771  40.629  1.00  3.12           C  
ATOM    537  C   ASN A  66       2.008   9.802  39.726  1.00  4.56           C  
ATOM    538  O   ASN A  66       1.503  10.883  39.392  1.00  2.37           O  
ATOM    539  CB  ASN A  66       2.819  10.163  42.056  1.00  3.53           C  
ATOM    540  CG  ASN A  66       1.648   9.343  42.585  1.00  2.00           C  
ATOM    541  OD1 ASN A  66       1.691   8.117  42.614  1.00  4.44           O  
ATOM    542  ND2 ASN A  66       0.609  10.022  43.027  1.00  7.96           N  
ATOM    543  N   ASP A  67       1.567   8.614  39.300  1.00  4.54           N  
ATOM    544  CA  ASP A  67       0.341   8.458  38.504  1.00  2.60           C  
ATOM    545  C   ASP A  67      -0.633   7.584  39.281  1.00  4.23           C  
ATOM    546  O   ASP A  67      -1.748   7.339  38.844  1.00  6.57           O  
ATOM    547  CB  ASP A  67       0.571   7.925  37.071  1.00  2.00           C  
ATOM    548  CG  ASP A  67       1.230   6.535  36.999  1.00  2.00           C  
ATOM    549  OD1 ASP A  67       1.463   5.856  38.021  1.00  2.00           O  
ATOM    550  OD2 ASP A  67       1.514   6.117  35.856  1.00  2.39           O  
ATOM    551  N   GLY A  68      -0.199   7.129  40.455  1.00  5.38           N  
ATOM    552  CA  GLY A  68      -1.048   6.310  41.302  1.00  6.38           C  
ATOM    553  C   GLY A  68      -1.304   4.874  40.880  1.00  7.58           C  
ATOM    554  O   GLY A  68      -1.700   4.070  41.720  1.00  8.52           O  
ATOM    555  N   LYS A  69      -1.141   4.550  39.599  1.00  9.15           N  
ATOM    556  CA  LYS A  69      -1.368   3.183  39.132  1.00  9.98           C  
ATOM    557  C   LYS A  69      -0.115   2.328  38.902  1.00 12.49           C  
ATOM    558  O   LYS A  69      -0.235   1.171  38.505  1.00 12.90           O  
ATOM    559  CB  LYS A  69      -2.260   3.161  37.879  1.00  8.34           C  
ATOM    560  CG  LYS A  69      -1.669   3.800  36.644  1.00 12.83           C  
ATOM    561  CD  LYS A  69      -2.691   3.837  35.520  1.00 12.25           C  
ATOM    562  CE  LYS A  69      -2.221   4.662  34.327  1.00 12.03           C  
ATOM    563  NZ  LYS A  69      -1.106   4.031  33.593  1.00 14.13           N  
ATOM    564  N   THR A  70       1.076   2.887  39.124  1.00 12.47           N  
ATOM    565  CA  THR A  70       2.334   2.140  38.950  1.00 10.79           C  
ATOM    566  C   THR A  70       2.670   1.398  40.239  1.00 14.23           C  
ATOM    567  O   THR A  70       2.737   2.012  41.310  1.00 11.02           O  
ATOM    568  CB  THR A  70       3.534   3.076  38.633  1.00 10.22           C  
ATOM    569  OG1 THR A  70       3.325   3.735  37.378  1.00  7.47           O  
ATOM    570  CG2 THR A  70       4.823   2.266  38.550  1.00  5.59           C  
ATOM    571  N   PRO A  71       2.891   0.071  40.161  1.00 16.79           N  
ATOM    572  CA  PRO A  71       3.219  -0.678  41.380  1.00 18.21           C  
ATOM    573  C   PRO A  71       4.584  -0.255  41.935  1.00 20.22           C  
ATOM    574  O   PRO A  71       5.465   0.145  41.170  1.00 21.23           O  
ATOM    575  CB  PRO A  71       3.241  -2.133  40.892  1.00 17.63           C  
ATOM    576  CG  PRO A  71       2.334  -2.124  39.675  1.00 17.12           C  
ATOM    577  CD  PRO A  71       2.742  -0.839  39.011  1.00 17.32           C  
ATOM    578  N   GLY A  72       4.695  -0.230  43.264  1.00 19.81           N  
ATOM    579  CA  GLY A  72       5.936   0.119  43.940  1.00 21.41           C  
ATOM    580  C   GLY A  72       6.739   1.252  43.344  1.00 21.47           C  
ATOM    581  O   GLY A  72       7.962   1.142  43.147  1.00 21.24           O  
ATOM    582  N   ALA A  73       6.045   2.344  43.048  1.00 20.10           N  
ATOM    583  CA  ALA A  73       6.680   3.517  42.478  1.00 19.49           C  
ATOM    584  C   ALA A  73       7.066   4.520  43.565  1.00 18.17           C  
ATOM    585  O   ALA A  73       6.635   4.405  44.719  1.00 18.85           O  
ATOM    586  CB  ALA A  73       5.737   4.169  41.474  1.00 18.37           C  
ATOM    587  N   VAL A  74       7.934   5.459  43.196  1.00 18.11           N  
ATOM    588  CA  VAL A  74       8.372   6.558  44.071  1.00 17.67           C  
ATOM    589  C   VAL A  74       8.068   7.859  43.278  1.00 16.13           C  
ATOM    590  O   VAL A  74       7.650   7.789  42.106  1.00 15.66           O  
ATOM    591  CB  VAL A  74       9.895   6.462  44.494  1.00 17.75           C  
ATOM    592  CG1 VAL A  74      10.139   5.249  45.405  1.00 17.40           C  
ATOM    593  CG2 VAL A  74      10.791   6.370  43.299  1.00 21.10           C  
ATOM    594  N   ASN A  75       8.220   9.020  43.910  1.00 13.30           N  
ATOM    595  CA  ASN A  75       7.929  10.309  43.262  1.00 11.92           C  
ATOM    596  C   ASN A  75       9.058  11.307  43.572  1.00  9.17           C  
ATOM    597  O   ASN A  75       8.886  12.235  44.348  1.00 10.20           O  
ATOM    598  CB  ASN A  75       6.568  10.822  43.767  1.00 10.01           C  
ATOM    599  CG  ASN A  75       6.103  12.094  43.074  1.00 11.80           C  
ATOM    600  OD1 ASN A  75       6.722  12.591  42.119  1.00  9.54           O  
ATOM    601  ND2 ASN A  75       4.988  12.625  43.548  1.00  5.60           N  
ATOM    602  N   ALA A  76      10.204  11.108  42.928  1.00  7.82           N  
ATOM    603  CA  ALA A  76      11.387  11.943  43.122  1.00  7.39           C  
ATOM    604  C   ALA A  76      11.308  13.427  42.725  1.00  7.63           C  
ATOM    605  O   ALA A  76      12.031  14.241  43.290  1.00  7.71           O  
ATOM    606  CB  ALA A  76      12.619  11.272  42.496  1.00  7.80           C  
ATOM    607  N   CYS A  77      10.492  13.787  41.738  1.00  7.84           N  
ATOM    608  CA  CYS A  77      10.361  15.210  41.378  1.00  7.26           C  
ATOM    609  C   CYS A  77       9.118  15.802  42.037  1.00  7.90           C  
ATOM    610  O   CYS A  77       8.672  16.896  41.663  1.00  8.20           O  
ATOM    611  CB  CYS A  77      10.220  15.413  39.873  1.00  7.10           C  
ATOM    612  SG  CYS A  77      11.538  14.776  38.799  1.00  7.88           S  
ATOM    613  N   HIS A  78       8.526  15.040  42.962  1.00  6.46           N  
ATOM    614  CA  HIS A  78       7.323  15.440  43.690  1.00  7.82           C  
ATOM    615  C   HIS A  78       6.294  16.126  42.801  1.00  4.82           C  
ATOM    616  O   HIS A  78       5.845  17.234  43.070  1.00  4.02           O  
ATOM    617  CB  HIS A  78       7.694  16.256  44.934  1.00  9.37           C  
ATOM    618  CG  HIS A  78       8.674  15.549  45.828  1.00 15.67           C  
ATOM    619  ND1 HIS A  78      10.021  15.465  45.539  1.00 18.63           N  
ATOM    620  CD2 HIS A  78       8.489  14.817  46.958  1.00 17.84           C  
ATOM    621  CE1 HIS A  78      10.618  14.704  46.442  1.00 20.01           C  
ATOM    622  NE2 HIS A  78       9.710  14.300  47.314  1.00 18.70           N  
ATOM    623  N   LEU A  79       5.904  15.418  41.746  1.00  4.63           N  
ATOM    624  CA  LEU A  79       4.940  15.923  40.784  1.00  7.68           C  
ATOM    625  C   LEU A  79       3.940  14.865  40.355  1.00  7.00           C  
ATOM    626  O   LEU A  79       4.249  13.664  40.344  1.00  7.64           O  
ATOM    627  CB  LEU A  79       5.656  16.386  39.503  1.00  7.96           C  
ATOM    628  CG  LEU A  79       6.536  17.619  39.509  1.00  9.41           C  
ATOM    629  CD1 LEU A  79       7.154  17.774  38.131  1.00  9.43           C  
ATOM    630  CD2 LEU A  79       5.701  18.829  39.891  1.00 10.44           C  
ATOM    631  N   SER A  80       2.731  15.312  40.015  1.00  7.16           N  
ATOM    632  CA  SER A  80       1.722  14.392  39.484  1.00  5.38           C  
ATOM    633  C   SER A  80       2.310  14.165  38.095  1.00  7.60           C  
ATOM    634  O   SER A  80       2.876  15.098  37.507  1.00  4.97           O  
ATOM    635  CB  SER A  80       0.353  15.075  39.332  1.00  4.59           C  
ATOM    636  OG  SER A  80      -0.551  14.298  38.533  1.00  2.00           O  
ATOM    637  N   CYS A  81       2.153  12.957  37.559  1.00  7.70           N  
ATOM    638  CA  CYS A  81       2.688  12.656  36.240  1.00  5.85           C  
ATOM    639  C   CYS A  81       1.928  13.483  35.224  1.00  4.80           C  
ATOM    640  O   CYS A  81       2.448  13.792  34.151  1.00  2.76           O  
ATOM    641  CB  CYS A  81       2.617  11.149  35.933  1.00  5.99           C  
ATOM    642  SG  CYS A  81       3.777  10.113  36.906  1.00  9.60           S  
ATOM    643  N   SER A  82       0.716  13.874  35.613  1.00  2.04           N  
ATOM    644  CA  SER A  82      -0.168  14.719  34.813  1.00  2.22           C  
ATOM    645  C   SER A  82       0.500  16.068  34.473  1.00  2.00           C  
ATOM    646  O   SER A  82       0.278  16.623  33.394  1.00  2.00           O  
ATOM    647  CB  SER A  82      -1.467  14.954  35.589  1.00  3.06           C  
ATOM    648  OG  SER A  82      -2.412  15.711  34.853  1.00 13.91           O  
ATOM    649  N   ALA A  83       1.377  16.549  35.347  1.00  2.91           N  
ATOM    650  CA  ALA A  83       2.070  17.826  35.115  1.00  3.81           C  
ATOM    651  C   ALA A  83       3.001  17.774  33.905  1.00  4.61           C  
ATOM    652  O   ALA A  83       3.349  18.811  33.337  1.00  2.00           O  
ATOM    653  CB  ALA A  83       2.854  18.245  36.354  1.00  2.50           C  
ATOM    654  N   LEU A  84       3.346  16.550  33.504  1.00  2.02           N  
ATOM    655  CA  LEU A  84       4.245  16.284  32.390  1.00  3.54           C  
ATOM    656  C   LEU A  84       3.529  16.142  31.046  1.00  2.55           C  
ATOM    657  O   LEU A  84       4.167  15.862  30.025  1.00  4.93           O  
ATOM    658  CB  LEU A  84       5.083  15.024  32.688  1.00  2.30           C  
ATOM    659  CG  LEU A  84       5.863  15.143  34.002  1.00  4.08           C  
ATOM    660  CD1 LEU A  84       6.622  13.884  34.314  1.00  2.00           C  
ATOM    661  CD2 LEU A  84       6.798  16.354  33.922  1.00  2.00           C  
ATOM    662  N   LEU A  85       2.220  16.365  31.042  1.00  2.00           N  
ATOM    663  CA  LEU A  85       1.416  16.298  29.824  1.00  3.65           C  
ATOM    664  C   LEU A  85       0.853  17.681  29.461  1.00  4.29           C  
ATOM    665  O   LEU A  85      -0.043  17.802  28.616  1.00  3.35           O  
ATOM    666  CB  LEU A  85       0.266  15.295  30.009  1.00  5.69           C  
ATOM    667  CG  LEU A  85       0.696  13.878  30.390  1.00  5.44           C  
ATOM    668  CD1 LEU A  85      -0.436  13.170  31.041  1.00  7.63           C  
ATOM    669  CD2 LEU A  85       1.213  13.120  29.182  1.00  8.94           C  
ATOM    670  N   GLN A  86       1.391  18.718  30.107  1.00  5.97           N  
ATOM    671  CA  GLN A  86       0.977  20.104  29.886  1.00  5.58           C  
ATOM    672  C   GLN A  86       1.674  20.687  28.666  1.00  5.04           C  
ATOM    673  O   GLN A  86       2.763  20.248  28.298  1.00  6.18           O  
ATOM    674  CB  GLN A  86       1.373  20.944  31.091  1.00  5.44           C  
ATOM    675  CG  GLN A  86       0.677  20.605  32.382  1.00  5.68           C  
ATOM    676  CD  GLN A  86       1.088  21.533  33.510  1.00 10.12           C  
ATOM    677  OE1 GLN A  86       0.460  22.578  33.743  1.00 11.94           O  
ATOM    678  NE2 GLN A  86       2.149  21.166  34.217  1.00 10.01           N  
ATOM    679  N   ASP A  87       1.049  21.661  28.019  1.00  3.62           N  
ATOM    680  CA  ASP A  87       1.681  22.309  26.868  1.00  4.59           C  
ATOM    681  C   ASP A  87       2.864  23.115  27.415  1.00  2.97           C  
ATOM    682  O   ASP A  87       3.880  23.262  26.747  1.00  2.95           O  
ATOM    683  CB  ASP A  87       0.717  23.269  26.140  1.00  2.70           C  
ATOM    684  CG  ASP A  87      -0.169  22.569  25.107  1.00  7.25           C  
ATOM    685  OD1 ASP A  87      -0.250  21.307  25.084  1.00  9.16           O  
ATOM    686  OD2 ASP A  87      -0.799  23.295  24.313  1.00  2.00           O  
ATOM    687  N   ASN A  88       2.698  23.680  28.608  1.00  2.94           N  
ATOM    688  CA  ASN A  88       3.759  24.456  29.238  1.00  3.35           C  
ATOM    689  C   ASN A  88       4.713  23.466  29.869  1.00  4.43           C  
ATOM    690  O   ASN A  88       4.314  22.673  30.709  1.00  5.73           O  
ATOM    691  CB  ASN A  88       3.202  25.377  30.310  1.00  2.02           C  
ATOM    692  CG  ASN A  88       4.301  26.168  31.021  1.00  2.00           C  
ATOM    693  OD1 ASN A  88       4.925  25.680  31.938  1.00  2.00           O  
ATOM    694  ND2 ASN A  88       4.520  27.392  30.597  1.00  3.24           N  
ATOM    695  N   ILE A  89       5.987  23.542  29.514  1.00  5.87           N  
ATOM    696  CA  ILE A  89       6.942  22.585  30.038  1.00  5.62           C  
ATOM    697  C   ILE A  89       7.780  22.973  31.265  1.00  4.35           C  
ATOM    698  O   ILE A  89       8.700  22.248  31.650  1.00  2.00           O  
ATOM    699  CB  ILE A  89       7.821  22.046  28.886  1.00  6.38           C  
ATOM    700  CG1 ILE A  89       8.799  23.112  28.360  1.00  4.23           C  
ATOM    701  CG2 ILE A  89       6.907  21.579  27.765  1.00  4.61           C  
ATOM    702  CD1 ILE A  89       9.748  22.584  27.266  1.00  2.00           C  
ATOM    703  N   ALA A  90       7.401  24.043  31.955  1.00  4.05           N  
ATOM    704  CA  ALA A  90       8.189  24.454  33.104  1.00  2.24           C  
ATOM    705  C   ALA A  90       8.307  23.337  34.139  1.00  4.94           C  
ATOM    706  O   ALA A  90       9.382  23.146  34.709  1.00  4.29           O  
ATOM    707  CB  ALA A  90       7.641  25.713  33.719  1.00  2.36           C  
ATOM    708  N   ASP A  91       7.230  22.578  34.363  1.00  4.36           N  
ATOM    709  CA  ASP A  91       7.286  21.494  35.343  1.00  3.94           C  
ATOM    710  C   ASP A  91       8.092  20.293  34.854  1.00  3.34           C  
ATOM    711  O   ASP A  91       8.825  19.674  35.632  1.00  5.24           O  
ATOM    712  CB  ASP A  91       5.892  21.079  35.803  1.00  7.93           C  
ATOM    713  CG  ASP A  91       5.231  22.130  36.679  1.00 10.03           C  
ATOM    714  OD1 ASP A  91       4.015  22.366  36.506  1.00 14.46           O  
ATOM    715  OD2 ASP A  91       5.924  22.718  37.540  1.00  8.74           O  
ATOM    716  N   ALA A  92       7.978  19.975  33.570  1.00  2.00           N  
ATOM    717  CA  ALA A  92       8.752  18.883  32.996  1.00  2.35           C  
ATOM    718  C   ALA A  92      10.221  19.222  33.237  1.00  4.20           C  
ATOM    719  O   ALA A  92      10.968  18.392  33.746  1.00  2.00           O  
ATOM    720  CB  ALA A  92       8.482  18.757  31.483  1.00  2.76           C  
ATOM    721  N   VAL A  93      10.598  20.460  32.881  1.00  3.87           N  
ATOM    722  CA  VAL A  93      11.953  20.996  33.030  1.00  2.04           C  
ATOM    723  C   VAL A  93      12.433  20.944  34.482  1.00  2.94           C  
ATOM    724  O   VAL A  93      13.567  20.540  34.730  1.00  7.94           O  
ATOM    725  CB  VAL A  93      12.050  22.448  32.468  1.00  3.57           C  
ATOM    726  CG1 VAL A  93      13.422  23.073  32.736  1.00  2.00           C  
ATOM    727  CG2 VAL A  93      11.798  22.426  30.979  1.00  3.47           C  
ATOM    728  N   ALA A  94      11.587  21.299  35.447  1.00  2.00           N  
ATOM    729  CA  ALA A  94      12.012  21.213  36.840  1.00  2.00           C  
ATOM    730  C   ALA A  94      12.353  19.739  37.169  1.00  2.00           C  
ATOM    731  O   ALA A  94      13.354  19.447  37.858  1.00  2.00           O  
ATOM    732  CB  ALA A  94      10.946  21.754  37.773  1.00  2.00           C  
ATOM    733  N   CYS A  95      11.575  18.808  36.613  1.00  2.07           N  
ATOM    734  CA  CYS A  95      11.813  17.379  36.835  1.00  2.33           C  
ATOM    735  C   CYS A  95      13.019  16.837  36.027  1.00  2.78           C  
ATOM    736  O   CYS A  95      13.791  16.029  36.526  1.00  2.00           O  
ATOM    737  CB  CYS A  95      10.558  16.563  36.507  1.00  5.29           C  
ATOM    738  SG  CYS A  95      10.642  14.794  36.980  1.00  6.88           S  
ATOM    739  N   ALA A  96      13.175  17.286  34.789  1.00  2.69           N  
ATOM    740  CA  ALA A  96      14.300  16.873  33.957  1.00  2.84           C  
ATOM    741  C   ALA A  96      15.598  17.296  34.666  1.00  2.06           C  
ATOM    742  O   ALA A  96      16.616  16.610  34.609  1.00  2.14           O  
ATOM    743  CB  ALA A  96      14.201  17.529  32.609  1.00  2.00           C  
ATOM    744  N   LYS A  97      15.549  18.420  35.370  1.00  4.34           N  
ATOM    745  CA  LYS A  97      16.730  18.896  36.093  1.00  3.87           C  
ATOM    746  C   LYS A  97      16.991  18.022  37.345  1.00  3.46           C  
ATOM    747  O   LYS A  97      18.141  17.670  37.653  1.00  2.00           O  
ATOM    748  CB  LYS A  97      16.565  20.373  36.463  1.00  4.36           C  
ATOM    749  CG  LYS A  97      16.847  21.320  35.314  1.00  3.41           C  
ATOM    750  CD  LYS A  97      16.457  22.736  35.699  1.00  4.17           C  
ATOM    751  CE  LYS A  97      16.684  23.717  34.564  1.00  2.00           C  
ATOM    752  NZ  LYS A  97      16.045  24.999  34.942  1.00  2.00           N  
ATOM    753  N   ARG A  98      15.918  17.650  38.036  1.00  2.00           N  
ATOM    754  CA  ARG A  98      16.040  16.815  39.221  1.00  3.49           C  
ATOM    755  C   ARG A  98      16.741  15.515  38.813  1.00  6.07           C  
ATOM    756  O   ARG A  98      17.694  15.080  39.456  1.00  4.57           O  
ATOM    757  CB  ARG A  98      14.648  16.526  39.791  1.00  5.96           C  
ATOM    758  CG  ARG A  98      14.590  15.410  40.848  1.00  4.10           C  
ATOM    759  CD  ARG A  98      15.492  15.699  42.053  1.00  4.05           C  
ATOM    760  NE  ARG A  98      15.561  14.569  42.985  1.00  3.77           N  
ATOM    761  CZ  ARG A  98      16.376  13.528  42.850  1.00  2.79           C  
ATOM    762  NH1 ARG A  98      16.363  12.570  43.757  1.00  5.89           N  
ATOM    763  NH2 ARG A  98      17.217  13.446  41.824  1.00  2.00           N  
ATOM    764  N   VAL A  99      16.294  14.935  37.703  1.00  4.58           N  
ATOM    765  CA  VAL A  99      16.873  13.696  37.214  1.00  4.71           C  
ATOM    766  C   VAL A  99      18.375  13.785  37.000  1.00  4.92           C  
ATOM    767  O   VAL A  99      19.115  12.910  37.434  1.00  5.48           O  
ATOM    768  CB  VAL A  99      16.244  13.246  35.878  1.00  6.18           C  
ATOM    769  CG1 VAL A  99      16.885  11.935  35.423  1.00  3.46           C  
ATOM    770  CG2 VAL A  99      14.725  13.105  36.011  1.00  2.00           C  
ATOM    771  N   VAL A 100      18.833  14.813  36.295  1.00  4.50           N  
ATOM    772  CA  VAL A 100      20.259  14.912  36.025  1.00  6.54           C  
ATOM    773  C   VAL A 100      21.112  15.337  37.212  1.00  8.45           C  
ATOM    774  O   VAL A 100      22.334  15.316  37.139  1.00 12.09           O  
ATOM    775  CB  VAL A 100      20.556  15.736  34.761  1.00  2.54           C  
ATOM    776  CG1 VAL A 100      19.608  15.294  33.652  1.00  5.54           C  
ATOM    777  CG2 VAL A 100      20.428  17.233  35.027  1.00  4.80           C  
ATOM    778  N   ARG A 101      20.477  15.704  38.315  1.00 10.16           N  
ATOM    779  CA  ARG A 101      21.223  16.078  39.511  1.00  9.47           C  
ATOM    780  C   ARG A 101      21.831  14.789  40.108  1.00  6.66           C  
ATOM    781  O   ARG A 101      22.826  14.843  40.841  1.00  5.71           O  
ATOM    782  CB  ARG A 101      20.291  16.751  40.512  1.00 10.27           C  
ATOM    783  CG  ARG A 101      20.830  18.017  41.120  1.00 13.27           C  
ATOM    784  CD  ARG A 101      19.746  18.703  41.908  1.00 14.17           C  
ATOM    785  NE  ARG A 101      18.904  19.533  41.058  1.00 17.03           N  
ATOM    786  CZ  ARG A 101      17.575  19.608  41.128  1.00 12.08           C  
ATOM    787  NH1 ARG A 101      16.933  20.418  40.305  1.00 13.95           N  
ATOM    788  NH2 ARG A 101      16.879  18.852  41.964  1.00  4.00           N  
ATOM    789  N   ASP A 102      21.218  13.639  39.819  1.00  5.03           N  
ATOM    790  CA  ASP A 102      21.724  12.338  40.280  1.00  6.93           C  
ATOM    791  C   ASP A 102      23.050  12.045  39.541  1.00  8.18           C  
ATOM    792  O   ASP A 102      23.298  12.610  38.479  1.00  7.49           O  
ATOM    793  CB  ASP A 102      20.705  11.235  39.979  1.00  8.53           C  
ATOM    794  CG  ASP A 102      19.529  11.228  40.949  1.00  9.99           C  
ATOM    795  OD1 ASP A 102      18.635  10.380  40.753  1.00 11.14           O  
ATOM    796  OD2 ASP A 102      19.494  12.039  41.906  1.00  8.12           O  
ATOM    797  N   PRO A 103      23.872  11.103  40.057  1.00  8.40           N  
ATOM    798  CA  PRO A 103      25.176  10.710  39.495  1.00  6.83           C  
ATOM    799  C   PRO A 103      25.306  10.431  38.003  1.00  7.56           C  
ATOM    800  O   PRO A 103      26.297  10.825  37.385  1.00  8.36           O  
ATOM    801  CB  PRO A 103      25.570   9.497  40.331  1.00  7.69           C  
ATOM    802  CG  PRO A 103      24.267   9.022  40.988  1.00  9.25           C  
ATOM    803  CD  PRO A 103      23.545  10.297  41.251  1.00  7.64           C  
ATOM    804  N   GLN A 104      24.356   9.693  37.441  1.00  8.53           N  
ATOM    805  CA  GLN A 104      24.355   9.359  36.018  1.00  9.98           C  
ATOM    806  C   GLN A 104      24.194  10.587  35.136  1.00  8.77           C  
ATOM    807  O   GLN A 104      24.617  10.577  33.981  1.00 10.36           O  
ATOM    808  CB  GLN A 104      23.162   8.460  35.684  1.00  8.55           C  
ATOM    809  CG  GLN A 104      23.416   6.986  35.665  1.00 13.29           C  
ATOM    810  CD  GLN A 104      22.198   6.233  35.174  1.00 12.57           C  
ATOM    811  OE1 GLN A 104      21.084   6.438  35.666  1.00 11.86           O  
ATOM    812  NE2 GLN A 104      22.394   5.390  34.179  1.00 15.84           N  
ATOM    813  N   GLY A 105      23.462  11.575  35.645  1.00  8.05           N  
ATOM    814  CA  GLY A 105      23.190  12.777  34.886  1.00  8.21           C  
ATOM    815  C   GLY A 105      22.247  12.449  33.741  1.00  5.70           C  
ATOM    816  O   GLY A 105      21.395  11.575  33.860  1.00  7.92           O  
ATOM    817  N   ILE A 106      22.425  13.134  32.622  1.00  7.49           N  
ATOM    818  CA  ILE A 106      21.610  12.949  31.427  1.00  7.81           C  
ATOM    819  C   ILE A 106      21.619  11.495  30.906  1.00  7.67           C  
ATOM    820  O   ILE A 106      20.738  11.084  30.161  1.00  7.89           O  
ATOM    821  CB  ILE A 106      22.065  13.945  30.314  1.00  7.80           C  
ATOM    822  CG1 ILE A 106      21.068  13.956  29.160  1.00  6.74           C  
ATOM    823  CG2 ILE A 106      23.478  13.613  29.832  1.00  8.01           C  
ATOM    824  CD1 ILE A 106      21.114  15.208  28.330  1.00  9.31           C  
ATOM    825  N   ARG A 107      22.589  10.702  31.348  1.00  9.96           N  
ATOM    826  CA  ARG A 107      22.669   9.322  30.912  1.00  9.80           C  
ATOM    827  C   ARG A 107      21.553   8.469  31.528  1.00  9.35           C  
ATOM    828  O   ARG A 107      21.350   7.325  31.144  1.00  9.96           O  
ATOM    829  CB  ARG A 107      24.066   8.776  31.192  1.00 12.24           C  
ATOM    830  CG  ARG A 107      25.141   9.431  30.321  1.00 13.39           C  
ATOM    831  CD  ARG A 107      26.555   9.196  30.880  1.00 19.07           C  
ATOM    832  NE  ARG A 107      27.624   9.350  29.878  1.00 22.72           N  
ATOM    833  CZ  ARG A 107      28.202  10.506  29.529  1.00 23.36           C  
ATOM    834  NH1 ARG A 107      29.162  10.512  28.607  1.00 22.38           N  
ATOM    835  NH2 ARG A 107      27.822  11.651  30.086  1.00 22.64           N  
ATOM    836  N   ALA A 108      20.804   9.037  32.467  1.00  8.95           N  
ATOM    837  CA  ALA A 108      19.683   8.324  33.066  1.00  8.32           C  
ATOM    838  C   ALA A 108      18.768   7.837  31.934  1.00  7.73           C  
ATOM    839  O   ALA A 108      18.076   6.832  32.076  1.00  9.57           O  
ATOM    840  CB  ALA A 108      18.914   9.236  34.010  1.00  9.04           C  
ATOM    841  N   TRP A 109      18.737   8.561  30.822  1.00  7.82           N  
ATOM    842  CA  TRP A 109      17.922   8.142  29.687  1.00  8.26           C  
ATOM    843  C   TRP A 109      18.826   7.298  28.780  1.00  7.25           C  
ATOM    844  O   TRP A 109      19.789   7.800  28.194  1.00 10.79           O  
ATOM    845  CB  TRP A 109      17.378   9.345  28.918  1.00  4.10           C  
ATOM    846  CG  TRP A 109      16.279  10.134  29.625  1.00  5.34           C  
ATOM    847  CD1 TRP A 109      14.941   9.883  29.577  1.00  3.67           C  
ATOM    848  CD2 TRP A 109      16.437  11.327  30.415  1.00  3.72           C  
ATOM    849  NE1 TRP A 109      14.247  10.847  30.273  1.00  6.51           N  
ATOM    850  CE2 TRP A 109      15.138  11.748  30.798  1.00  5.27           C  
ATOM    851  CE3 TRP A 109      17.550  12.077  30.836  1.00  3.30           C  
ATOM    852  CZ2 TRP A 109      14.916  12.893  31.583  1.00  6.17           C  
ATOM    853  CZ3 TRP A 109      17.337  13.216  31.620  1.00  2.00           C  
ATOM    854  CH2 TRP A 109      16.022  13.612  31.984  1.00  6.23           C  
ATOM    855  N   VAL A 110      18.503   6.020  28.651  1.00  9.29           N  
ATOM    856  CA  VAL A 110      19.294   5.107  27.834  1.00  8.41           C  
ATOM    857  C   VAL A 110      19.265   5.466  26.342  1.00  8.83           C  
ATOM    858  O   VAL A 110      20.269   5.344  25.633  1.00 10.38           O  
ATOM    859  CB  VAL A 110      18.833   3.672  28.065  1.00  8.44           C  
ATOM    860  CG1 VAL A 110      19.566   2.749  27.140  1.00 11.62           C  
ATOM    861  CG2 VAL A 110      19.090   3.285  29.511  1.00  9.96           C  
ATOM    862  N   ALA A 111      18.116   5.935  25.865  1.00 10.26           N  
ATOM    863  CA  ALA A 111      17.996   6.334  24.473  1.00  9.23           C  
ATOM    864  C   ALA A 111      18.979   7.484  24.184  1.00 10.79           C  
ATOM    865  O   ALA A 111      19.470   7.616  23.066  1.00  8.94           O  
ATOM    866  CB  ALA A 111      16.570   6.763  24.177  1.00 11.15           C  
ATOM    867  N   TRP A 112      19.275   8.299  25.200  1.00  9.26           N  
ATOM    868  CA  TRP A 112      20.210   9.416  25.062  1.00  8.39           C  
ATOM    869  C   TRP A 112      21.592   8.848  24.741  1.00  6.61           C  
ATOM    870  O   TRP A 112      22.355   9.390  23.937  1.00  5.08           O  
ATOM    871  CB  TRP A 112      20.284  10.241  26.365  1.00  9.72           C  
ATOM    872  CG  TRP A 112      21.124  11.465  26.197  1.00  9.31           C  
ATOM    873  CD1 TRP A 112      20.741  12.641  25.618  1.00  7.68           C  
ATOM    874  CD2 TRP A 112      22.528  11.594  26.477  1.00 10.44           C  
ATOM    875  NE1 TRP A 112      21.820  13.487  25.509  1.00  9.25           N  
ATOM    876  CE2 TRP A 112      22.930  12.871  26.025  1.00  9.32           C  
ATOM    877  CE3 TRP A 112      23.487  10.753  27.067  1.00 12.28           C  
ATOM    878  CZ2 TRP A 112      24.247  13.330  26.139  1.00 10.56           C  
ATOM    879  CZ3 TRP A 112      24.807  11.215  27.181  1.00 10.85           C  
ATOM    880  CH2 TRP A 112      25.170  12.491  26.718  1.00 10.62           C  
ATOM    881  N   ARG A 113      21.911   7.755  25.408  1.00  8.05           N  
ATOM    882  CA  ARG A 113      23.172   7.074  25.209  1.00  7.76           C  
ATOM    883  C   ARG A 113      23.206   6.560  23.770  1.00  8.60           C  
ATOM    884  O   ARG A 113      24.178   6.794  23.039  1.00 11.40           O  
ATOM    885  CB  ARG A 113      23.313   5.944  26.243  1.00  7.64           C  
ATOM    886  CG  ARG A 113      23.511   6.474  27.666  1.00  8.37           C  
ATOM    887  CD  ARG A 113      22.581   5.865  28.678  1.00 11.22           C  
ATOM    888  NE  ARG A 113      22.997   4.530  29.068  1.00 16.33           N  
ATOM    889  CZ  ARG A 113      22.934   4.054  30.313  1.00 19.22           C  
ATOM    890  NH1 ARG A 113      23.349   2.821  30.571  1.00 19.19           N  
ATOM    891  NH2 ARG A 113      22.459   4.800  31.299  1.00 18.92           N  
ATOM    892  N   ASN A 114      22.107   5.946  23.340  1.00  8.12           N  
ATOM    893  CA  ASN A 114      21.988   5.423  21.968  1.00  6.56           C  
ATOM    894  C   ASN A 114      22.067   6.509  20.865  1.00  8.34           C  
ATOM    895  O   ASN A 114      22.841   6.372  19.913  1.00  7.71           O  
ATOM    896  CB  ASN A 114      20.653   4.682  21.762  1.00  7.19           C  
ATOM    897  CG  ASN A 114      20.206   3.841  22.980  1.00 10.73           C  
ATOM    898  OD1 ASN A 114      20.998   3.474  23.851  1.00  9.67           O  
ATOM    899  ND2 ASN A 114      18.908   3.551  23.038  1.00 13.35           N  
ATOM    900  N   ARG A 115      21.288   7.592  20.985  1.00  5.40           N  
ATOM    901  CA  ARG A 115      21.284   8.597  19.928  1.00  6.54           C  
ATOM    902  C   ARG A 115      21.856   9.991  20.116  1.00  5.32           C  
ATOM    903  O   ARG A 115      21.805  10.793  19.170  1.00  4.66           O  
ATOM    904  CB  ARG A 115      19.901   8.718  19.259  1.00  6.82           C  
ATOM    905  CG  ARG A 115      18.681   8.196  20.035  1.00 10.13           C  
ATOM    906  CD  ARG A 115      18.206   6.827  19.521  1.00  8.81           C  
ATOM    907  NE  ARG A 115      18.145   6.758  18.061  1.00  7.05           N  
ATOM    908  CZ  ARG A 115      17.386   5.931  17.344  1.00  4.95           C  
ATOM    909  NH1 ARG A 115      17.455   5.986  16.032  1.00 13.16           N  
ATOM    910  NH2 ARG A 115      16.533   5.082  17.900  1.00 10.60           N  
ATOM    911  N   CYS A 116      22.458  10.281  21.262  1.00  3.23           N  
ATOM    912  CA  CYS A 116      22.988  11.637  21.474  1.00  5.44           C  
ATOM    913  C   CYS A 116      24.419  11.698  21.980  1.00  5.82           C  
ATOM    914  O   CYS A 116      25.171  12.616  21.637  1.00  3.35           O  
ATOM    915  CB  CYS A 116      22.080  12.412  22.434  1.00  4.97           C  
ATOM    916  SG  CYS A 116      20.312  12.442  21.952  1.00  8.86           S  
ATOM    917  N   GLN A 117      24.781  10.704  22.790  1.00  7.99           N  
ATOM    918  CA  GLN A 117      26.101  10.590  23.388  1.00  7.08           C  
ATOM    919  C   GLN A 117      27.164  10.458  22.320  1.00  7.31           C  
ATOM    920  O   GLN A 117      27.053   9.635  21.424  1.00  2.43           O  
ATOM    921  CB  GLN A 117      26.131   9.374  24.312  1.00 10.95           C  
ATOM    922  CG  GLN A 117      27.368   9.239  25.190  1.00 14.33           C  
ATOM    923  CD  GLN A 117      27.096   8.363  26.394  1.00 17.52           C  
ATOM    924  OE1 GLN A 117      27.952   7.607  26.846  1.00 22.19           O  
ATOM    925  NE2 GLN A 117      25.889   8.452  26.914  1.00 22.22           N  
ATOM    926  N   ASN A 118      28.162  11.330  22.382  1.00  8.82           N  
ATOM    927  CA  ASN A 118      29.269  11.322  21.421  1.00 11.47           C  
ATOM    928  C   ASN A 118      28.849  11.480  19.956  1.00 10.19           C  
ATOM    929  O   ASN A 118      29.502  10.971  19.026  1.00  7.89           O  
ATOM    930  CB  ASN A 118      30.127  10.080  21.644  1.00 15.63           C  
ATOM    931  CG  ASN A 118      30.770  10.070  23.019  1.00 21.34           C  
ATOM    932  OD1 ASN A 118      30.441   9.237  23.872  1.00 27.94           O  
ATOM    933  ND2 ASN A 118      31.669  11.023  23.262  1.00 25.72           N  
ATOM    934  N   ARG A 119      27.790  12.259  19.768  1.00  9.62           N  
ATOM    935  CA  ARG A 119      27.234  12.564  18.448  1.00 11.53           C  
ATOM    936  C   ARG A 119      27.368  14.056  18.090  1.00 10.53           C  
ATOM    937  O   ARG A 119      27.614  14.883  18.960  1.00 13.68           O  
ATOM    938  CB  ARG A 119      25.753  12.221  18.443  1.00 10.65           C  
ATOM    939  CG  ARG A 119      25.450  10.794  18.777  1.00  8.50           C  
ATOM    940  CD  ARG A 119      25.189  10.026  17.525  1.00  9.47           C  
ATOM    941  NE  ARG A 119      24.591   8.745  17.845  1.00  5.99           N  
ATOM    942  CZ  ARG A 119      24.225   7.848  16.941  1.00  3.76           C  
ATOM    943  NH1 ARG A 119      23.690   6.707  17.334  1.00  3.19           N  
ATOM    944  NH2 ARG A 119      24.385   8.098  15.647  1.00  7.93           N  
ATOM    945  N   ASP A 120      27.208  14.391  16.812  1.00 11.73           N  
ATOM    946  CA  ASP A 120      27.249  15.787  16.365  1.00 11.32           C  
ATOM    947  C   ASP A 120      25.806  16.255  16.538  1.00  9.96           C  
ATOM    948  O   ASP A 120      24.920  15.846  15.790  1.00 10.36           O  
ATOM    949  CB  ASP A 120      27.662  15.876  14.882  1.00 11.04           C  
ATOM    950  CG  ASP A 120      27.903  17.326  14.399  1.00 14.85           C  
ATOM    951  OD1 ASP A 120      27.350  18.302  14.974  1.00 15.51           O  
ATOM    952  OD2 ASP A 120      28.647  17.487  13.411  1.00 11.07           O  
ATOM    953  N   VAL A 121      25.553  17.065  17.557  1.00  9.62           N  
ATOM    954  CA  VAL A 121      24.205  17.537  17.808  1.00  8.18           C  
ATOM    955  C   VAL A 121      23.991  19.022  17.499  1.00  8.26           C  
ATOM    956  O   VAL A 121      22.915  19.543  17.762  1.00  7.68           O  
ATOM    957  CB  VAL A 121      23.756  17.193  19.262  1.00  5.57           C  
ATOM    958  CG1 VAL A 121      23.579  15.676  19.403  1.00 10.03           C  
ATOM    959  CG2 VAL A 121      24.797  17.659  20.279  1.00 10.59           C  
ATOM    960  N   ARG A 122      24.983  19.672  16.886  1.00  9.03           N  
ATOM    961  CA  ARG A 122      24.913  21.111  16.539  1.00 10.63           C  
ATOM    962  C   ARG A 122      23.640  21.424  15.783  1.00  8.61           C  
ATOM    963  O   ARG A 122      22.964  22.423  16.042  1.00  6.38           O  
ATOM    964  CB  ARG A 122      26.095  21.525  15.653  1.00 11.67           C  
ATOM    965  CG  ARG A 122      27.427  21.617  16.348  1.00 15.87           C  
ATOM    966  CD  ARG A 122      28.554  21.636  15.317  1.00 21.67           C  
ATOM    967  NE  ARG A 122      29.847  22.062  15.866  1.00 24.60           N  
ATOM    968  CZ  ARG A 122      30.765  21.248  16.383  1.00 27.08           C  
ATOM    969  NH1 ARG A 122      31.911  21.753  16.847  1.00 27.37           N  
ATOM    970  NH2 ARG A 122      30.530  19.937  16.471  1.00 27.80           N  
ATOM    971  N   GLN A 123      23.326  20.543  14.842  1.00  9.88           N  
ATOM    972  CA  GLN A 123      22.143  20.647  13.999  1.00 12.75           C  
ATOM    973  C   GLN A 123      20.863  20.995  14.751  1.00  8.25           C  
ATOM    974  O   GLN A 123      20.041  21.725  14.221  1.00  8.28           O  
ATOM    975  CB  GLN A 123      21.942  19.336  13.225  1.00 14.09           C  
ATOM    976  CG  GLN A 123      21.711  18.125  14.127  1.00 18.70           C  
ATOM    977  CD  GLN A 123      21.892  16.819  13.403  1.00 22.77           C  
ATOM    978  OE1 GLN A 123      21.005  16.361  12.674  1.00 24.69           O  
ATOM    979  NE2 GLN A 123      23.041  16.202  13.603  1.00 24.40           N  
ATOM    980  N   TYR A 124      20.720  20.511  15.982  1.00  6.47           N  
ATOM    981  CA  TYR A 124      19.519  20.762  16.793  1.00  7.48           C  
ATOM    982  C   TYR A 124      19.253  22.220  17.167  1.00  7.62           C  
ATOM    983  O   TYR A 124      18.106  22.638  17.293  1.00  7.84           O  
ATOM    984  CB  TYR A 124      19.532  19.892  18.063  1.00  4.83           C  
ATOM    985  CG  TYR A 124      19.325  18.430  17.764  1.00  5.31           C  
ATOM    986  CD1 TYR A 124      18.073  17.948  17.405  1.00  9.38           C  
ATOM    987  CD2 TYR A 124      20.382  17.524  17.808  1.00  8.22           C  
ATOM    988  CE1 TYR A 124      17.873  16.593  17.089  1.00  7.24           C  
ATOM    989  CE2 TYR A 124      20.193  16.155  17.504  1.00  6.65           C  
ATOM    990  CZ  TYR A 124      18.939  15.707  17.147  1.00  7.77           C  
ATOM    991  OH  TYR A 124      18.724  14.380  16.847  1.00  6.71           O  
ATOM    992  N   VAL A 125      20.308  23.005  17.333  1.00  8.10           N  
ATOM    993  CA  VAL A 125      20.115  24.392  17.726  1.00 10.66           C  
ATOM    994  C   VAL A 125      20.654  25.392  16.723  1.00  8.68           C  
ATOM    995  O   VAL A 125      20.688  26.591  17.002  1.00  7.70           O  
ATOM    996  CB  VAL A 125      20.736  24.667  19.119  1.00 11.03           C  
ATOM    997  CG1 VAL A 125      19.992  23.869  20.197  1.00 10.47           C  
ATOM    998  CG2 VAL A 125      22.208  24.296  19.115  1.00  8.74           C  
ATOM    999  N   GLN A 126      21.097  24.902  15.566  1.00  9.04           N  
ATOM   1000  CA  GLN A 126      21.635  25.788  14.534  1.00 10.85           C  
ATOM   1001  C   GLN A 126      20.484  26.606  13.960  1.00  8.79           C  
ATOM   1002  O   GLN A 126      19.434  26.070  13.590  1.00  6.91           O  
ATOM   1003  CB  GLN A 126      22.362  25.015  13.409  1.00 14.66           C  
ATOM   1004  CG  GLN A 126      23.634  24.200  13.812  1.00 19.57           C  
ATOM   1005  CD  GLN A 126      24.762  24.982  14.551  1.00 21.74           C  
ATOM   1006  OE1 GLN A 126      25.633  25.598  13.924  1.00 21.29           O  
ATOM   1007  NE2 GLN A 126      24.791  24.870  15.883  1.00 18.31           N  
ATOM   1008  N   GLY A 127      20.662  27.918  13.967  1.00  7.64           N  
ATOM   1009  CA  GLY A 127      19.643  28.806  13.456  1.00  6.23           C  
ATOM   1010  C   GLY A 127      18.591  29.211  14.478  1.00  6.28           C  
ATOM   1011  O   GLY A 127      17.717  29.999  14.154  1.00  3.73           O  
ATOM   1012  N   CYS A 128      18.705  28.746  15.723  1.00  6.02           N  
ATOM   1013  CA  CYS A 128      17.697  29.071  16.733  1.00  5.34           C  
ATOM   1014  C   CYS A 128      17.867  30.332  17.595  1.00  6.65           C  
ATOM   1015  O   CYS A 128      16.977  30.661  18.398  1.00  3.99           O  
ATOM   1016  CB  CYS A 128      17.480  27.870  17.645  1.00  3.57           C  
ATOM   1017  SG  CYS A 128      17.015  26.321  16.800  1.00  2.00           S  
ATOM   1018  N   GLY A 129      19.007  31.012  17.459  1.00  6.89           N  
ATOM   1019  CA  GLY A 129      19.268  32.215  18.238  1.00  8.89           C  
ATOM   1020  C   GLY A 129      19.608  31.945  19.694  1.00  9.52           C  
ATOM   1021  O   GLY A 129      19.319  32.765  20.576  1.00 11.38           O  
ATOM   1022  N   VAL A 130      20.225  30.795  19.948  1.00  8.67           N  
ATOM   1023  CA  VAL A 130      20.609  30.381  21.301  1.00  9.26           C  
ATOM   1024  C   VAL A 130      22.122  30.142  21.361  1.00 10.44           C  
ATOM   1025  O   VAL A 130      22.780  30.181  20.300  1.00 13.05           O  
ATOM   1026  CB  VAL A 130      19.881  29.064  21.738  1.00  9.87           C  
ATOM   1027  CG1 VAL A 130      18.377  29.263  21.766  1.00  6.03           C  
ATOM   1028  CG2 VAL A 130      20.246  27.914  20.811  1.00 11.30           C  
ATOM   1029  OXT VAL A 130      22.644  29.918  22.467  1.00 13.06           O  
TER    1030      VAL A 130                                                      
HETATM 1031 NA    NA A 601       5.516   5.606   8.376  1.00 19.06          NA  
HETATM 1032  O   HOH A 131      12.277  25.790  13.762  1.00  2.00           O  
HETATM 1033  O   HOH A 132      -0.905  24.865  26.953  1.00  2.00           O  
HETATM 1034  O   HOH A 133      -0.004  11.376  42.881  1.00  2.00           O  
HETATM 1035  O   HOH A 134      24.665  14.695  34.738  1.00  2.00           O  
HETATM 1036  O   HOH A 135      22.138  30.750  13.336  1.00  5.91           O  
HETATM 1037  O   HOH A 136       4.869  21.501  29.904  1.00  4.22           O  
HETATM 1038  O   HOH A 137      19.657   7.986  15.563  1.00  3.73           O  
HETATM 1039  O   HOH A 138       4.022  21.775  33.577  1.00  5.89           O  
HETATM 1040  O   HOH A 139      14.806  18.330  14.694  1.00  2.00           O  
HETATM 1041  O   HOH A 140       0.950  16.501  40.064  1.00  5.76           O  
HETATM 1042  O   HOH A 141      -4.409   5.266  43.815  1.00  2.00           O  
HETATM 1043  O   HOH A 142      26.335  12.268  14.849  1.00  2.00           O  
HETATM 1044  O   HOH A 143      10.927  29.951  15.594  1.00  2.00           O  
HETATM 1045  O   HOH A 144      13.804   7.779  20.016  1.00 10.49           O  
HETATM 1046  O   HOH A 145      20.184   9.126  36.323  1.00  6.95           O  
HETATM 1047  O   HOH A 146       8.244  15.943  28.075  1.00  2.00           O  
HETATM 1048  O   HOH A 147      28.227  10.621  40.859  1.00  2.86           O  
HETATM 1049  O   HOH A 148      -0.453  -1.179  38.946  1.00 23.77           O  
HETATM 1050  O   HOH A 149      18.244  30.882   9.958  1.00 10.16           O  
HETATM 1051  O   HOH A 150      22.603   7.842  12.607  1.00 10.47           O  
HETATM 1052  O   HOH A 151      -3.459  23.896  33.273  1.00 10.24           O  
HETATM 1053  O   HOH A 152       1.752   3.008  41.650  1.00  2.07           O  
HETATM 1054  O   HOH A 153       4.436  20.317  27.368  1.00  9.78           O  
HETATM 1055  O   HOH A 154      -1.595   8.122  46.465  1.00  2.69           O  
HETATM 1056  O   HOH A 155      24.585  28.819  15.214  1.00 26.00           O  
HETATM 1057  O   HOH A 156      13.922  19.232  39.653  1.00  2.93           O  
HETATM 1058  O   HOH A 157      25.203  18.763  13.642  1.00 19.14           O  
HETATM 1059  O   HOH A 158       4.230  26.905  23.677  1.00  5.41           O  
HETATM 1060  O   HOH A 159      19.346  34.432  24.043  1.00  9.87           O  
HETATM 1061  O   HOH A 160      23.134  29.240  14.798  1.00  8.03           O  
HETATM 1062  O   HOH A 161      33.700  16.172  16.186  1.00 15.94           O  
HETATM 1063  O   HOH A 162      21.657   6.479  38.840  1.00 33.07           O  
HETATM 1064  O   HOH A 163       6.805  29.078  21.568  1.00 29.04           O  
HETATM 1065  O   HOH A 164       3.496   5.001  40.991  1.00 27.58           O  
HETATM 1066  O   HOH A 165      25.843   9.888  14.001  1.00 35.20           O  
HETATM 1067  O   HOH A 166      20.962  32.017  10.530  1.00  5.10           O  
HETATM 1068  O   HOH A 167      13.143  22.783  36.493  1.00 16.19           O  
HETATM 1069  O   HOH A 168      28.708   9.146  16.285  1.00  9.56           O  
HETATM 1070  O   HOH A 169      13.459   9.254  30.913  1.00 14.87           O  
HETATM 1071  O   HOH A 170      12.355  -5.921  35.287  1.00  5.17           O  
HETATM 1072  O   HOH A 171      16.739  33.452  24.628  1.00  4.49           O  
HETATM 1073  O   HOH A 172       6.290  26.700  25.531  1.00  3.48           O  
HETATM 1074  O   HOH A 173      19.577  27.613  35.029  1.00 19.94           O  
HETATM 1075  O   HOH A 174       1.189   3.501  32.357  1.00 37.53           O  
HETATM 1076  O   HOH A 175      24.441  28.849  21.032  1.00 35.77           O  
HETATM 1077  O   HOH A 176       2.626   9.039  45.937  1.00 13.21           O  
HETATM 1078  O   HOH A 177       8.996  11.753  15.750  1.00 27.86           O  
HETATM 1079  O   HOH A 178      10.249   0.304  34.324  1.00 12.10           O  
HETATM 1080  O   HOH A 179       8.493  16.462  15.296  1.00 24.87           O  
HETATM 1081  O   HOH A 180      33.417  20.573  12.405  1.00  7.51           O  
HETATM 1082  O   HOH A 181      14.830   7.311  25.539  1.00  2.00           O  
HETATM 1083  O   HOH A 182      11.408  11.173  16.966  1.00 19.19           O  
HETATM 1084  O   HOH A 183      19.303   3.811  30.979  1.00 32.56           O  
HETATM 1085  O   HOH A 184       9.933   0.536  42.208  1.00 34.54           O  
HETATM 1086  O   HOH A 185       2.777  20.478  40.267  1.00 25.20           O  
HETATM 1087  O   HOH A 186      11.093  27.643  11.532  1.00 12.98           O  
HETATM 1088  O   HOH A 187      18.177  19.614  13.262  1.00 25.48           O  
HETATM 1089  O   HOH A 188      10.633   8.066  21.306  1.00 19.28           O  
HETATM 1090  O   HOH A 189      14.739  -0.427  41.678  1.00 14.19           O  
HETATM 1091  O   HOH A 190      16.829  27.190  37.701  1.00 10.89           O  
HETATM 1092  O   HOH A 191       0.926  -4.462  30.902  1.00 14.81           O  
HETATM 1093  O   HOH A 192      -1.601  23.243  35.940  1.00 17.33           O  
HETATM 1094  O   HOH A 193      21.971  19.075  40.525  1.00 20.82           O  
HETATM 1095  O   HOH A 194       8.834  10.228  18.092  1.00 22.71           O  
HETATM 1096  O   HOH A 195      23.512  22.154  36.806  1.00  2.05           O  
HETATM 1097  O   HOH A 196      -0.171  16.177  41.631  1.00 13.53           O  
HETATM 1098  O   HOH A 197      11.434  23.563  12.280  1.00 23.99           O  
HETATM 1099  O   HOH A 198      23.161   3.924  40.145  1.00 35.94           O  
HETATM 1100  O   HOH A 199       4.277  21.290  15.360  1.00 21.91           O  
HETATM 1101  O   HOH A 200      15.671   6.400  27.989  1.00 17.48           O  
HETATM 1102  O   HOH A 201       5.410  26.187  39.420  1.00 17.96           O  
HETATM 1103  O   HOH A 202      17.219  24.633  37.251  1.00 10.39           O  
HETATM 1104  O   HOH A 203       8.177   7.527  46.595  1.00 38.28           O  
HETATM 1105  O   HOH A 204      26.517   4.990  25.338  1.00  8.94           O  
HETATM 1106  O   HOH A 205      30.619  26.985   9.591  1.00 14.07           O  
HETATM 1107  O   HOH A 206       2.180  23.022  35.032  1.00 37.17           O  
HETATM 1108  O   HOH A 207       5.571  30.771  19.818  1.00 25.60           O  
HETATM 1109  O   HOH A 208      30.943  16.980  15.256  1.00 20.60           O  
HETATM 1110  O   HOH A 209       9.333  31.431  19.116  1.00 18.11           O  
HETATM 1111  O   HOH A 210       4.315  30.096  22.668  1.00 30.60           O  
HETATM 1112  O   HOH A 211      12.117  -2.730  39.291  1.00 16.01           O  
HETATM 1113  O   HOH A 212      -1.393  -7.387  36.761  1.00 14.66           O  
HETATM 1114  O   HOH A 213      11.521   8.253  15.069  1.00 24.15           O  
HETATM 1115  O   HOH A 214      19.171   6.539  37.940  1.00 14.82           O  
HETATM 1116  O   HOH A 215      14.515  21.256  11.588  1.00 13.00           O  
HETATM 1117  O   HOH A 216      19.219  10.818  12.415  1.00 26.27           O  
HETATM 1118  O   HOH A 217      10.852  21.014  14.200  1.00  9.08           O  
HETATM 1119  O   HOH A 218      22.777  22.141  10.623  1.00 26.02           O  
HETATM 1120  O   HOH A 219      30.254  24.371  13.107  1.00 17.96           O  
HETATM 1121  O   HOH A 220      10.781   5.647  15.668  1.00 20.63           O  
HETATM 1122  O   HOH A 221      23.684  10.136  12.174  1.00 35.09           O  
HETATM 1123  O   HOH A 222       8.502  19.328  14.974  1.00 27.81           O  
HETATM 1124  O   HOH A 223      -2.543  17.540  33.639  1.00 12.16           O  
HETATM 1125  O   HOH A 224      13.132   5.537  31.625  1.00 21.09           O  
HETATM 1126  O   HOH A 225       1.965  24.711  15.850  1.00 21.06           O  
HETATM 1127  O   HOH A 226       2.972  12.879  43.653  1.00 10.85           O  
HETATM 1128  O   HOH A 227      24.212  28.708  17.824  1.00 27.29           O  
HETATM 1129  O   HOH A 228      19.574  22.688  11.698  1.00 22.23           O  
HETATM 1130  O   HOH A 229       3.326  -1.676  43.380  1.00 35.40           O  
HETATM 1131  O   HOH A 230       0.733  27.753  21.303  1.00 16.92           O  
HETATM 1132  O   HOH A 231      11.493  -3.153  35.311  1.00 18.92           O  
HETATM 1133  O   HOH A 232      15.057   2.640  37.332  1.00 37.77           O  
HETATM 1134  O   HOH A 233      25.237   7.691  12.422  1.00 36.13           O  
HETATM 1135  O   HOH A 234      27.262  30.073  15.366  1.00 16.69           O  
HETATM 1136  O   HOH A 235      -1.500  10.098  39.039  1.00  3.68           O  
HETATM 1137  O   HOH A 236      22.599  14.521  15.926  1.00 16.59           O  
HETATM 1138  O   HOH A 237      10.693  23.457  35.254  1.00 16.66           O  
HETATM 1139  O   HOH A 238      -0.654  11.271  47.484  1.00 16.51           O  
HETATM 1140  O   HOH A 239      -1.424  24.906  29.546  1.00 21.27           O  
HETATM 1141  O   HOH A 240      29.193  12.181  13.607  1.00 13.86           O  
HETATM 1142  O   HOH A 241      23.803  27.920  35.010  1.00 23.34           O  
HETATM 1143  O   HOH A 242      31.584  15.123  18.099  1.00 27.05           O  
HETATM 1144  O   HOH A 243       4.045  26.924  15.560  1.00 26.18           O  
HETATM 1145  O   HOH A 244      22.676  24.690  34.154  1.00 16.23           O  
HETATM 1146  O   HOH A 245       6.893  31.219  13.331  1.00 14.12           O  
HETATM 1147  O   HOH A 246      18.215  16.111  13.259  1.00 16.89           O  
HETATM 1148  O   HOH A 247       1.303  33.122  24.476  1.00  6.52           O  
HETATM 1149  O   HOH A 248      13.281   5.183  10.131  1.00 10.72           O  
HETATM 1150  O   HOH A 249      18.015   3.752  34.468  1.00 21.25           O  
HETATM 1151  O   HOH A 250       9.148   7.161  23.232  1.00 16.14           O  
HETATM 1152  O   HOH A 251       1.378  28.052  24.554  1.00 24.95           O  
HETATM 1153  O   HOH A 252      20.468  24.782  38.137  1.00 15.43           O  
HETATM 1154  O   HOH A 253      12.253  17.665  41.678  1.00 17.15           O  
HETATM 1155  O   HOH A 254       1.626   0.921  22.111  1.00 19.35           O  
HETATM 1156  O   HOH A 255      19.220  26.778  10.334  1.00 37.44           O  
HETATM 1157  O   HOH A 256      19.922  36.711  25.542  1.00 32.29           O  
HETATM 1158  O   HOH A 257      19.827   2.412  38.743  1.00 18.81           O  
HETATM 1159  O   HOH A 258      32.655  18.757  14.161  1.00 17.17           O  
HETATM 1160  O   HOH A 259      19.407   5.722  11.129  1.00 29.63           O  
HETATM 1161  O   HOH A 260      21.244  22.674  39.785  1.00 20.31           O  
HETATM 1162  O   HOH A 261       1.877   2.350  48.324  1.00 24.13           O  
HETATM 1163  O   HOH A 262      27.722  25.149  36.330  1.00 32.18           O  
HETATM 1164  O   HOH A 263      26.876  22.632  35.239  1.00 13.26           O  
HETATM 1165  O   HOH A 264      -0.481  -4.625  35.888  1.00 29.62           O  
HETATM 1166  O   HOH A 265       8.619  28.869  14.229  1.00 18.45           O  
HETATM 1167  O   HOH A 266       4.420  27.165  34.654  1.00 20.41           O  
HETATM 1168  O   HOH A 267      22.800   2.363  32.065  1.00 29.41           O  
HETATM 1169  O   HOH A 268      26.550  20.439  40.332  1.00 21.27           O  
HETATM 1170  O   HOH A 269      19.132   2.303  14.021  1.00 31.88           O  
HETATM 1171  O   HOH A 270      13.832  17.432  11.558  1.00 34.79           O  
HETATM 1172  O   HOH A 271      19.676  20.947   9.358  1.00 33.49           O  
HETATM 1173  O   HOH A 272      25.563  12.077  40.321  1.00 34.61           O  
HETATM 1174  O   HOH A 273      11.307  22.293  40.606  1.00 11.53           O  
HETATM 1175  O   HOH A 274       7.962  17.587  43.507  1.00 20.77           O  
HETATM 1176  O   HOH A 275       5.466  17.861  44.813  1.00 35.80           O  
HETATM 1177  O   HOH A 276       3.516  31.741  21.300  1.00 24.61           O  
HETATM 1178  O   HOH A 277       3.203   3.543  45.399  1.00 23.82           O  
HETATM 1179  O   HOH A 278       1.525   1.149  45.165  1.00 34.41           O  
HETATM 1180  O   HOH A 279       3.922   6.757  45.397  1.00 16.85           O  
HETATM 1181  O   HOH A 280       8.638   0.906  25.912  1.00 37.53           O  
HETATM 1182  O   HOH A 281      14.667   3.094  14.857  1.00 33.82           O  
HETATM 1183  O   HOH A 282      25.938   2.099  30.693  1.00 31.14           O  
HETATM 1184  O   HOH A 283      -2.328  -0.854  31.413  1.00 34.66           O  
HETATM 1185  O   HOH A 284       5.141  11.184  48.232  1.00 37.16           O  
HETATM 1186  O   HOH A 285      25.104  22.318  41.457  1.00 28.54           O  
HETATM 1187  O   HOH A 286      27.786  19.305  11.192  1.00 30.25           O  
HETATM 1188  O   HOH A 287      29.512   3.215  26.920  1.00 20.94           O  
HETATM 1189  O   HOH A 288      27.620  24.730  39.152  1.00 28.03           O  
HETATM 1190  O   HOH A 289      12.677   5.525  28.800  1.00 36.68           O  
HETATM 1191  O   HOH A 290      16.518  21.970  39.567  1.00 21.66           O  
HETATM 1192  O   HOH A 291      25.912  10.650  43.099  1.00 25.38           O  
HETATM 1193  O   HOH A 292      10.541   4.117  29.611  1.00 34.07           O  
HETATM 1194  O   HOH A 293      11.567   8.159  26.670  1.00 24.39           O  
HETATM 1195  O   HOH A 294       2.533  15.896  43.723  1.00 18.05           O  
HETATM 1196  O   HOH A 295      13.514   6.131  23.442  1.00 20.24           O  
HETATM 1197  O   HOH A 296      10.308   0.750  46.329  1.00 37.35           O  
HETATM 1198  O   HOH A 297       4.342  24.566  36.114  1.00 21.11           O  
HETATM 1199  O   HOH A 298      -1.925  -2.577  34.475  1.00 35.99           O  
HETATM 1200  O   HOH A 299      15.097   7.224  10.647  1.00 25.43           O  
HETATM 1201  O   HOH A 300      13.762  21.730  38.758  1.00 25.48           O  
HETATM 1202  O   HOH A 301      -1.485   1.468  31.672  1.00  7.72           O  
HETATM 1203  O   HOH A 302       1.671  29.212  26.960  1.00 27.79           O  
HETATM 1204  O   HOH A 303      23.487  31.415  26.621  1.00 23.77           O  
HETATM 1205  O   HOH A 304      24.116   0.140  31.735  1.00 16.50           O  
HETATM 1206  O   HOH A 305      21.207  12.048  16.599  1.00 38.95           O  
HETATM 1207  O   HOH A 306      25.620  24.634  17.198  1.00 38.97           O  
HETATM 1208  O   HOH A 307       8.017   7.749  48.047  1.00 33.34           O  
HETATM 1209  O   HOH A 308      11.833  -2.240  42.264  1.00 20.90           O  
HETATM 1210  O   HOH A 309       7.369   4.021  48.627  1.00 26.03           O  
HETATM 1211  O   HOH A 310      11.762   7.200  17.361  1.00 37.40           O  
HETATM 1212  O   HOH A 311      15.099   1.617  17.451  1.00 34.17           O  
HETATM 1213  O   HOH A 312       2.973  23.410  38.224  1.00 36.34           O  
HETATM 1214  O   HOH A 313      11.087  20.527  42.652  1.00 34.94           O  
HETATM 1215  O   HOH A 314       5.350  19.448  41.750  1.00 27.72           O  
HETATM 1216  O   HOH A 315       6.826  30.623  24.341  1.00 30.44           O  
HETATM 1217  O   HOH A 316      24.394  13.826  37.376  1.00  6.43           O  
HETATM 1218  O   HOH A 317       5.528   1.776  22.547  1.00 35.08           O  
HETATM 1219  O   HOH A 318      -1.553   2.925  28.793  1.00 25.25           O  
HETATM 1220  O   HOH A 319      26.048  21.778  37.868  1.00 16.83           O  
HETATM 1221  O   HOH A 320      30.683  20.870  12.687  1.00 32.92           O  
HETATM 1222  O   HOH A 321      11.636  15.750  11.537  1.00 21.10           O  
HETATM 1223  O   HOH A 322      10.361  27.199  15.548  1.00 23.04           O  
HETATM 1224  O   HOH A 323      16.914   4.748  37.616  1.00 38.26           O  
HETATM 1225  O   HOH A 324      12.489  19.150  13.276  1.00 29.02           O  
HETATM 1226  O   HOH A 325       7.650   8.173  20.177  1.00 34.95           O  
HETATM 1227  O   HOH A 326      16.487   4.734  30.062  1.00 29.14           O  
HETATM 1228  O   HOH A 327      21.696  -0.381  30.367  1.00 35.60           O  
HETATM 1229  O   HOH A 328      30.850  27.673  16.254  1.00 35.49           O  
HETATM 1230  O   HOH A 329       0.650   6.953  46.996  1.00 26.29           O  
HETATM 1231  O   HOH A 330      -1.675   6.037  43.812  1.00 20.21           O  
HETATM 1232  O   HOH A 331      20.598  24.703   9.401  1.00 20.99           O  
HETATM 1233  O   HOH A 332       6.282  23.140  40.710  1.00 34.53           O  
HETATM 1234  O   HOH A 333       4.147  -1.134  26.309  1.00 32.63           O  
HETATM 1235  O   HOH A 334      14.398  -2.195  37.475  1.00 37.75           O  
HETATM 1236  O   HOH A 335       6.690  29.891  13.673  1.00 32.02           O  
HETATM 1237  O   HOH A 336      24.499   2.385  35.268  1.00 22.08           O  
HETATM 1238  O   HOH A 337      -0.049  25.508  32.912  1.00 26.86           O  
HETATM 1239  O   HOH A 338      31.736  27.010  12.308  1.00 26.82           O  
HETATM 1240  O   HOH A 339      13.845   4.184  26.815  1.00 37.54           O  
HETATM 1241  O   HOH A 340      16.797  24.847   9.407  1.00 37.26           O  
HETATM 1242  O   HOH A 341       0.446  14.595  44.705  1.00 32.32           O  
HETATM 1243  O   HOH A 342      14.696   3.536  11.959  1.00 35.08           O  
HETATM 1244  O   HOH A 343       9.076   2.879  50.519  1.00 22.59           O  
HETATM 1245  O   HOH A 344      10.867   4.072  22.275  1.00 31.66           O  
HETATM 1246  O   HOH A 345      11.863   4.993  25.374  1.00 32.30           O  
HETATM 1247  O   HOH A 346      12.321   3.798  18.107  1.00 35.32           O  
HETATM 1248  O   HOH A 347       2.126  -1.621  21.387  1.00 30.80           O  
HETATM 1249  O   HOH A 348      17.282   4.614  13.579  1.00 33.24           O  
HETATM 1250  O   HOH A 349      12.392  25.219  38.813  1.00 35.60           O  
HETATM 1251  O   HOH A 350       4.992   4.371  47.520  1.00 32.58           O  
HETATM 1252  O   HOH A 351       6.533  23.876  37.997  1.00 37.80           O  
HETATM 1253  O   HOH A 352      24.053  25.289  36.437  1.00 31.42           O  
HETATM 1254  O   HOH A 353       5.786  17.925  26.841  1.00  3.24           O  
HETATM 1255  O   HOH A 354      24.872   9.045  19.112  1.00 16.66           O  
HETATM 1256  O   HOH A 355      25.878  11.755  36.119  1.00 19.77           O  
HETATM 1257  O   HOH A 356      21.081  12.678  11.055  1.00 34.06           O  
HETATM 1258  O   HOH A 357      -2.057   9.691  43.712  1.00 17.00           O  
HETATM 1259  O   HOH A 358      24.633  20.482  11.751  1.00 31.96           O  
HETATM 1260  O   HOH A 359      17.410   8.578  11.232  1.00 33.79           O  
HETATM 1261  O   HOH A 360      18.625  13.986  10.949  1.00 36.42           O  
HETATM 1262  O   HOH A 361       2.522   0.420  24.605  1.00 38.33           O  
HETATM 1263  O   HOH A 362      11.909   5.999  20.200  1.00 33.20           O  
HETATM 1264  O   HOH A 363       7.376  20.202  39.577  1.00 33.49           O  
HETATM 1265  O   HOH A 364      19.558   8.057  12.887  1.00 36.89           O  
HETATM 1266  O   HOH A 365       0.189   4.424  44.239  1.00 38.10           O  
HETATM 1267  O   HOH A 366      11.714   1.440  44.227  1.00 33.14           O  
HETATM 1268  O   HOH A 367      31.609  24.525  16.053  1.00 39.87           O  
HETATM 1269  O   HOH A 368      22.868   2.141  37.585  1.00 35.59           O  
HETATM 1270  O   HOH A 369      28.284  25.235  15.609  1.00 34.12           O  
HETATM 1271  O   HOH A 370      18.900   0.786  35.769  1.00 39.27           O  
HETATM 1272  O   HOH A 371      27.426  21.783  12.535  1.00 38.83           O  
HETATM 1273  O   HOH A 372       8.373   6.543  50.453  1.00 38.54           O  
HETATM 1274  O   HOH A 373       3.870  12.834  46.525  1.00 33.23           O  
HETATM 1275  O   HOH A 374       2.943  31.798  26.733  1.00 35.68           O  
HETATM 1276  O   HOH A 375       7.201   9.970  47.274  1.00 36.93           O  
CONECT   53 1017                                                                
CONECT  243  916                                                                
CONECT  534  642                                                                
CONECT  612  738                                                                
CONECT  642  534                                                                
CONECT  738  612                                                                
CONECT  916  243                                                                
CONECT 1017   53                                                                
MASTER      379    0    1    8    2    0    2    6 1275    1    8   10          
END                                                                             
