HEADER    MUTANT STABILITY                        25-JAN-99   1B7S              
TITLE     VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSOZYME;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 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                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAKANO,M.OTA,K.OGASAHARA,Y.YAMAGATA,K.NISHIKAWA,K.YUTANI            
REVDAT   5   03-APR-24 1B7S    1       REMARK                                   
REVDAT   4   03-NOV-21 1B7S    1       REMARK SEQADV LINK                       
REVDAT   3   24-FEB-09 1B7S    1       VERSN                                    
REVDAT   2   27-APR-99 1B7S    3       ATOM   HET    SOURCE REMARK              
REVDAT   2 2                   3       HETATM SEQRES SEQADV FORMUL              
REVDAT   2 3                   3       SSBOND                                   
REVDAT   1   02-FEB-99 1B7S    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    BIOCHEMISTRY                  V.  37  9355 1998              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.TAKANO,Y.YAMAGATA,S.FUJII,K.YUTANI                         
REMARK   1  TITL   CONTRIBUTION OF 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.OGASAHARA,H.KANEDA,Y.YAMAGATA,S.FUJII,E.KANAYA,   
REMARK   1  AUTH 2 M.KIKUCHI,M.OOBATAKE,K.YUTANI                                
REMARK   1  TITL   CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF     
REMARK   1  TITL 2 HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL    
REMARK   1  TITL 3 ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS            
REMARK   1  REF    J.MOL.BIOL.                   V. 254    62 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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)   (%) : 78.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 6198                           
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) : 0.188                           
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) (%) : 61.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 583                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1028                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 167                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.640                           
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 1B7S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171508.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.708                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21097                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.05600                            
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) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS METHOD           
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
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   (%): 35.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91                     
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       28.24500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       16.00500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.00500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       16.00500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.24500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.00500            
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   OE1  GLU A    35     O    HOH A   184              0.40            
REMARK 500   CG   LYS A    13     O    HOH A   305              0.47            
REMARK 500   CB   ILE A    56     O    HOH A   134              1.09            
REMARK 500   CB   PRO A    71     O    HOH A   296              1.12            
REMARK 500   NH2  ARG A    50     O    HOH A   186              1.23            
REMARK 500   CD   LYS A    13     O    HOH A   305              1.28            
REMARK 500   OG   SER A    82     O    HOH A   146              1.28            
REMARK 500   CA   ILE A    56     O    HOH A   134              1.30            
REMARK 500   CG2  ILE A    56     O    HOH A   134              1.31            
REMARK 500   NE1  TRP A   109     O    HOH A   154              1.33            
REMARK 500   CG2  VAL A   110     O    HOH A   177              1.35            
REMARK 500   CB   VAL A   110     O    HOH A   177              1.36            
REMARK 500   CA   VAL A   110     O    HOH A   177              1.39            
REMARK 500   CG2  THR A    40     O    HOH A   161              1.46            
REMARK 500   CB   ALA A   111     O    HOH A   137              1.49            
REMARK 500   O    HOH A   216     O    HOH A   268              1.53            
REMARK 500   N    ILE A    89     O    HOH A   145              1.59            
REMARK 500   CD   GLU A    35     O    HOH A   184              1.59            
REMARK 500   N    VAL A   110     O    HOH A   177              1.68            
REMARK 500   O    HOH A   259     O    HOH A   311              1.71            
REMARK 500   CD1  TRP A   109     O    HOH A   154              1.72            
REMARK 500   NH1  ARG A    50     O    HOH A   265              1.73            
REMARK 500   C    ASN A    88     O    HOH A   145              1.77            
REMARK 500   OD2  ASP A    49     O    HOH A   261              1.82            
REMARK 500   ND2  ASN A    66     O    HOH A   131              1.82            
REMARK 500   CZ   ARG A    50     O    HOH A   186              1.83            
REMARK 500   NZ   LYS A     1     O    HOH A   285              1.86            
REMARK 500   CB   SER A    82     O    HOH A   146              1.92            
REMARK 500   O    ASN A    75     O    HOH A   196              1.93            
REMARK 500   O    HIS A    78     O    HOH A   281              1.94            
REMARK 500   N    ILE A    56     O    HOH A   134              1.98            
REMARK 500   CB   LYS A    13     O    HOH A   305              1.98            
REMARK 500   ND2  ASN A    44     O    HOH A   271              2.01            
REMARK 500   C    ILE A    56     O    HOH A   134              2.03            
REMARK 500   NE2  HIS A    78     O    HOH A   196              2.04            
REMARK 500   N    SER A    80     O    HOH A   132              2.07            
REMARK 500   CG   PRO A    71     O    HOH A   296              2.09            
REMARK 500   O    CYS A    77     O    HOH A   237              2.10            
REMARK 500   CA   ILE A    89     O    HOH A   145              2.11            
REMARK 500   CB   THR A    40     O    HOH A   161              2.11            
REMARK 500   CE   LYS A    13     O    HOH A   305              2.11            
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   CZ   ARG A    21     CZ   ARG A    41     4557     0.48            
REMARK 500   NH2  ARG A    21     NH1  ARG A    41     4557     0.51            
REMARK 500   NH2  ARG A   122     O    HOH A   287     4557     0.65            
REMARK 500   NE   ARG A    21     NH2  ARG A    41     4557     0.83            
REMARK 500   O    HOH A   166     O    HOH A   215     2564     0.92            
REMARK 500   CZ   ARG A    21     NH2  ARG A    41     4557     0.92            
REMARK 500   OD1  ASP A   120     O    HOH A   269     4557     0.99            
REMARK 500   NH1  ARG A    21     NE   ARG A    41     4557     0.99            
REMARK 500   NH1  ARG A   122     O    HOH A   202     4557     1.02            
REMARK 500   NH2  ARG A    21     CZ   ARG A    41     4557     1.03            
REMARK 500   NE2  GLN A    86     NH1  ARG A   107     4457     1.13            
REMARK 500   NE   ARG A   115     O    HOH A   135     2554     1.23            
REMARK 500   CZ   ARG A   115     O    HOH A   135     2554     1.27            
REMARK 500   OE1  GLN A    86     NE   ARG A   107     4457     1.31            
REMARK 500   NH1  ARG A    21     CZ   ARG A    41     4557     1.32            
REMARK 500   O    HOH A   199     O    HOH A   249     4456     1.32            
REMARK 500   O    THR A    70     O    HOH A   222     1556     1.38            
REMARK 500   CD   GLN A    86     CZ   ARG A   107     4457     1.38            
REMARK 500   N    LYS A     1     O    HOH A   156     4457     1.45            
REMARK 500   NH2  ARG A   115     O    HOH A   308     2554     1.46            
REMARK 500   O    ALA A    47     NH1  ARG A   119     2555     1.48            
REMARK 500   CZ   ARG A    21     NE   ARG A    41     4557     1.50            
REMARK 500   NH1  ARG A   113     O    HOH A   321     2554     1.55            
REMARK 500   CD   GLN A    86     NE   ARG A   107     4457     1.68            
REMARK 500   NZ   LYS A    13     O    HOH A   201     2565     1.69            
REMARK 500   CZ   ARG A    21     NH1  ARG A    41     4557     1.70            
REMARK 500   CD   GLN A    86     NH1  ARG A   107     4457     1.76            
REMARK 500   NE2  GLN A    86     CZ   ARG A   107     4457     1.76            
REMARK 500   NE   ARG A    21     CZ   ARG A    41     4557     1.79            
REMARK 500   NH1  ARG A    21     NH2  ARG A    41     4557     1.80            
REMARK 500   NH2  ARG A   113     O    HOH A   321     2554     1.83            
REMARK 500   CE   LYS A    13     O    HOH A   201     2565     1.84            
REMARK 500   CZ   ARG A   113     O    HOH A   321     2554     1.84            
REMARK 500   CZ   ARG A   122     O    HOH A   202     4557     1.90            
REMARK 500   CG   ASP A   120     O    HOH A   269     4557     1.91            
REMARK 500   ND1  HIS A    78     O    HOH A   193     1556     1.91            
REMARK 500   OE1  GLN A    86     CZ   ARG A   107     4457     1.93            
REMARK 500   NH1  ARG A   115     O    HOH A   135     2554     1.95            
REMARK 500   CZ   ARG A   122     O    HOH A   287     4557     1.96            
REMARK 500   NH2  ARG A    21     NH2  ARG A    41     4557     1.99            
REMARK 500   O    VAL A   130     O    HOH A   320     4557     2.01            
REMARK 500   CA   LYS A     1     O    HOH A   156     4457     2.02            
REMARK 500   O    HOH A   202     O    HOH A   274     4457     2.04            
REMARK 500   CD   ARG A    21     NH2  ARG A    41     4557     2.04            
REMARK 500   NH2  ARG A    21     NE   ARG A    41     4557     2.06            
REMARK 500   O    ARG A    21     CD1  LEU A    85     4557     2.06            
REMARK 500   O    ALA A    76     O    HOH A   157     1556     2.07            
REMARK 500   OG   SER A    24     O    HOH A   219     4557     2.07            
REMARK 500   CG   GLN A    86     NH2  ARG A   107     4457     2.09            
REMARK 500   O    HOH A   192     O    HOH A   320     4557     2.10            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 SYMMETRY CONTACTS                             
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 139   O   112.3                                              
REMARK 620 3 HOH A 264   O   147.9  85.3                                        
REMARK 620 N                    1     2                                         
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  1B7S A    1   130  UNP    P61626   LYSC_HUMAN       1    130             
SEQADV 1B7S SER A   74  UNP  P61626    VAL    74 ENGINEERED MUTATION            
SEQRES   1 A  130  LYS VAL PHE GLU ARG CYS GLU LEU ALA ARG THR LEU LYS          
SEQRES   2 A  130  ARG LEU GLY MET ASP GLY TYR ARG GLY ILE SER LEU ALA          
SEQRES   3 A  130  ASN TRP MET CYS LEU ALA LYS TRP GLU 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 SER 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   *167(H2 O)                                                    
HELIX    1   1 ARG A    5  ARG A   14  1                                  10    
HELIX    2   2 TYR A   20  GLY A   22  5                                   3    
HELIX    3   3 LEU A   25  GLU A   35  1                                  11    
HELIX    4   4 ALA A   83  LEU A   85  5                                   3    
HELIX    5   5 ALA A   90  VAL A  100  1                                  11    
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  2.05  
SSBOND   4 CYS A   77    CYS A   95                          1555   1555  2.02  
LINK         O   SER A  61                NA    NA A 601     1554   1555  2.30  
LINK         O   HOH A 139                NA    NA A 601     1555   1555  2.22  
LINK         O   HOH A 264                NA    NA A 601     1555   1555  2.45  
SITE     1 AC1  6 SER A  61  CYS A  65  ALA A  73  SER A  74                    
SITE     2 AC1  6 HOH A 139  HOH A 264                                          
CRYST1   56.490   62.010   32.010  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      0.017702  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016126  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.031240        0.00000                         
ATOM      1  N   LYS A   1       0.991  19.351  22.802  1.00 22.28           N  
ATOM      2  CA  LYS A   1       1.668  20.405  21.980  1.00 24.46           C  
ATOM      3  C   LYS A   1       2.884  19.819  21.282  1.00 23.61           C  
ATOM      4  O   LYS A   1       3.613  19.024  21.872  1.00 22.94           O  
ATOM      5  CB  LYS A   1       2.127  21.580  22.852  1.00 21.98           C  
ATOM      6  CG  LYS A   1       2.836  22.673  22.078  1.00 20.94           C  
ATOM      7  CD  LYS A   1       3.376  23.743  22.991  1.00 21.48           C  
ATOM      8  CE  LYS A   1       3.870  24.929  22.178  1.00 24.20           C  
ATOM      9  NZ  LYS A   1       4.351  26.065  23.017  1.00 22.16           N  
ATOM     10  N   VAL A   2       3.055  20.156  20.011  1.00 23.47           N  
ATOM     11  CA  VAL A   2       4.207  19.681  19.269  1.00 24.82           C  
ATOM     12  C   VAL A   2       5.034  20.912  18.889  1.00 24.93           C  
ATOM     13  O   VAL A   2       4.622  21.750  18.067  1.00 22.64           O  
ATOM     14  CB  VAL A   2       3.816  18.836  18.035  1.00 25.64           C  
ATOM     15  CG1 VAL A   2       5.063  18.341  17.320  1.00 25.91           C  
ATOM     16  CG2 VAL A   2       2.997  17.627  18.476  1.00 27.76           C  
ATOM     17  N   PHE A   3       6.148  21.058  19.603  1.00 22.76           N  
ATOM     18  CA  PHE A   3       7.071  22.159  19.404  1.00 19.65           C  
ATOM     19  C   PHE A   3       7.814  22.048  18.085  1.00 19.67           C  
ATOM     20  O   PHE A   3       8.011  20.960  17.523  1.00 19.42           O  
ATOM     21  CB  PHE A   3       8.123  22.189  20.506  1.00 12.86           C  
ATOM     22  CG  PHE A   3       7.682  22.850  21.778  1.00 13.37           C  
ATOM     23  CD1 PHE A   3       7.899  24.204  21.981  1.00 11.48           C  
ATOM     24  CD2 PHE A   3       7.188  22.097  22.831  1.00 12.18           C  
ATOM     25  CE1 PHE A   3       7.646  24.794  23.205  1.00 10.64           C  
ATOM     26  CE2 PHE A   3       6.934  22.685  24.058  1.00 14.60           C  
ATOM     27  CZ  PHE A   3       7.168  24.035  24.244  1.00 10.83           C  
ATOM     28  N   GLU A   4       8.172  23.209  17.574  1.00 20.29           N  
ATOM     29  CA  GLU A   4       8.961  23.307  16.375  1.00 20.40           C  
ATOM     30  C   GLU A   4      10.347  23.259  16.996  1.00 17.50           C  
ATOM     31  O   GLU A   4      10.494  23.577  18.183  1.00 16.08           O  
ATOM     32  CB  GLU A   4       8.731  24.665  15.743  1.00 24.35           C  
ATOM     33  CG  GLU A   4       7.261  24.969  15.535  1.00 35.49           C  
ATOM     34  CD  GLU A   4       6.892  25.094  14.074  1.00 39.86           C  
ATOM     35  OE1 GLU A   4       7.213  24.173  13.285  1.00 43.00           O  
ATOM     36  OE2 GLU A   4       6.274  26.121  13.719  1.00 46.49           O  
ATOM     37  N   ARG A   5      11.348  22.848  16.225  1.00 17.01           N  
ATOM     38  CA  ARG A   5      12.726  22.767  16.709  1.00 13.39           C  
ATOM     39  C   ARG A   5      13.196  24.049  17.411  1.00 15.56           C  
ATOM     40  O   ARG A   5      13.342  24.089  18.644  1.00 13.89           O  
ATOM     41  CB  ARG A   5      13.653  22.441  15.534  1.00 15.58           C  
ATOM     42  CG  ARG A   5      15.150  22.406  15.858  1.00 14.89           C  
ATOM     43  CD  ARG A   5      15.970  21.899  14.665  1.00 15.11           C  
ATOM     44  NE  ARG A   5      16.075  22.880  13.583  1.00 16.42           N  
ATOM     45  CZ  ARG A   5      17.038  23.801  13.493  1.00 20.25           C  
ATOM     46  NH1 ARG A   5      17.061  24.657  12.469  1.00 14.34           N  
ATOM     47  NH2 ARG A   5      17.985  23.870  14.428  1.00 16.69           N  
ATOM     48  N   CYS A   6      13.345  25.126  16.651  1.00 13.96           N  
ATOM     49  CA  CYS A   6      13.824  26.360  17.245  1.00 16.80           C  
ATOM     50  C   CYS A   6      12.950  26.939  18.332  1.00 18.31           C  
ATOM     51  O   CYS A   6      13.456  27.627  19.217  1.00 21.00           O  
ATOM     52  CB  CYS A   6      14.169  27.389  16.169  1.00 19.45           C  
ATOM     53  SG  CYS A   6      15.677  26.918  15.254  1.00 19.56           S  
ATOM     54  N   GLU A   7      11.646  26.644  18.273  1.00 18.62           N  
ATOM     55  CA  GLU A   7      10.671  27.089  19.278  1.00 18.45           C  
ATOM     56  C   GLU A   7      11.040  26.432  20.618  1.00 16.14           C  
ATOM     57  O   GLU A   7      11.106  27.079  21.673  1.00 15.45           O  
ATOM     58  CB  GLU A   7       9.250  26.659  18.852  1.00 22.32           C  
ATOM     59  CG  GLU A   7       8.117  27.058  19.819  1.00 26.81           C  
ATOM     60  CD  GLU A   7       6.742  26.413  19.499  1.00 25.22           C  
ATOM     61  OE1 GLU A   7       6.641  25.537  18.607  1.00 24.72           O  
ATOM     62  OE2 GLU A   7       5.757  26.786  20.167  1.00 24.15           O  
ATOM     63  N   LEU A   8      11.300  25.135  20.566  1.00 14.03           N  
ATOM     64  CA  LEU A   8      11.682  24.417  21.766  1.00 11.68           C  
ATOM     65  C   LEU A   8      13.005  24.950  22.329  1.00 10.99           C  
ATOM     66  O   LEU A   8      13.099  25.251  23.527  1.00 11.03           O  
ATOM     67  CB  LEU A   8      11.787  22.911  21.481  1.00  8.41           C  
ATOM     68  CG  LEU A   8      12.152  22.056  22.689  1.00  2.00           C  
ATOM     69  CD1 LEU A   8      11.148  22.281  23.807  1.00  6.79           C  
ATOM     70  CD2 LEU A   8      12.195  20.594  22.305  1.00  8.50           C  
ATOM     71  N   ALA A   9      14.012  25.098  21.467  1.00 10.16           N  
ATOM     72  CA  ALA A   9      15.330  25.581  21.903  1.00 13.09           C  
ATOM     73  C   ALA A   9      15.246  26.893  22.697  1.00 11.79           C  
ATOM     74  O   ALA A   9      15.787  26.973  23.797  1.00 16.47           O  
ATOM     75  CB  ALA A   9      16.301  25.689  20.713  1.00 10.34           C  
ATOM     76  N   ARG A  10      14.512  27.888  22.195  1.00 14.02           N  
ATOM     77  CA  ARG A  10      14.359  29.160  22.929  1.00 14.35           C  
ATOM     78  C   ARG A  10      13.668  28.978  24.282  1.00 15.25           C  
ATOM     79  O   ARG A  10      14.058  29.599  25.279  1.00 16.03           O  
ATOM     80  CB  ARG A  10      13.570  30.180  22.115  1.00 15.75           C  
ATOM     81  CG  ARG A  10      14.360  30.840  20.993  1.00 21.09           C  
ATOM     82  CD  ARG A  10      13.492  31.867  20.259  1.00 21.95           C  
ATOM     83  NE  ARG A  10      12.595  31.268  19.266  1.00 24.04           N  
ATOM     84  CZ  ARG A  10      12.967  30.901  18.040  1.00 23.63           C  
ATOM     85  NH1 ARG A  10      12.080  30.374  17.208  1.00 22.26           N  
ATOM     86  NH2 ARG A  10      14.223  31.060  17.645  1.00 25.74           N  
ATOM     87  N   THR A  11      12.647  28.122  24.313  1.00 15.45           N  
ATOM     88  CA  THR A  11      11.914  27.857  25.538  1.00 15.49           C  
ATOM     89  C   THR A  11      12.798  27.152  26.555  1.00 14.54           C  
ATOM     90  O   THR A  11      12.772  27.497  27.738  1.00 15.37           O  
ATOM     91  CB  THR A  11      10.684  26.996  25.276  1.00 17.84           C  
ATOM     92  OG1 THR A  11       9.955  27.534  24.165  1.00 20.07           O  
ATOM     93  CG2 THR A  11       9.795  26.980  26.509  1.00 20.46           C  
ATOM     94  N   LEU A  12      13.568  26.152  26.114  1.00 15.06           N  
ATOM     95  CA  LEU A  12      14.460  25.455  27.050  1.00 14.54           C  
ATOM     96  C   LEU A  12      15.510  26.432  27.587  1.00 12.14           C  
ATOM     97  O   LEU A  12      15.777  26.473  28.809  1.00  8.10           O  
ATOM     98  CB  LEU A  12      15.134  24.230  26.411  1.00 13.69           C  
ATOM     99  CG  LEU A  12      14.320  22.943  26.226  1.00 15.02           C  
ATOM    100  CD1 LEU A  12      15.163  21.891  25.539  1.00 13.99           C  
ATOM    101  CD2 LEU A  12      13.830  22.426  27.555  1.00 16.41           C  
ATOM    102  N   LYS A  13      16.057  27.252  26.690  1.00 12.49           N  
ATOM    103  CA  LYS A  13      17.064  28.221  27.098  1.00 16.78           C  
ATOM    104  C   LYS A  13      16.474  29.176  28.110  1.00 19.04           C  
ATOM    105  O   LYS A  13      17.057  29.396  29.182  1.00 17.23           O  
ATOM    106  CB  LYS A  13      17.635  28.999  25.919  1.00 18.34           C  
ATOM    107  CG  LYS A  13      18.775  29.944  26.342  1.00 20.39           C  
ATOM    108  CD  LYS A  13      19.578  30.445  25.144  1.00 25.48           C  
ATOM    109  CE  LYS A  13      20.822  31.233  25.561  1.00 24.75           C  
ATOM    110  NZ  LYS A  13      20.481  32.540  26.176  1.00 29.36           N  
ATOM    111  N   ARG A  14      15.288  29.693  27.799  1.00 18.52           N  
ATOM    112  CA  ARG A  14      14.601  30.620  28.687  1.00 20.09           C  
ATOM    113  C   ARG A  14      14.363  30.020  30.078  1.00 17.77           C  
ATOM    114  O   ARG A  14      14.391  30.720  31.093  1.00 15.47           O  
ATOM    115  CB  ARG A  14      13.284  31.064  28.046  1.00 20.91           C  
ATOM    116  CG  ARG A  14      13.234  32.544  27.700  1.00 24.31           C  
ATOM    117  CD  ARG A  14      12.107  32.877  26.733  1.00 28.94           C  
ATOM    118  NE  ARG A  14      10.978  31.965  26.870  1.00 31.57           N  
ATOM    119  CZ  ARG A  14      10.398  31.349  25.845  1.00 34.33           C  
ATOM    120  NH1 ARG A  14       9.385  30.519  26.054  1.00 32.63           N  
ATOM    121  NH2 ARG A  14      10.810  31.588  24.601  1.00 36.81           N  
ATOM    122  N   LEU A  15      14.224  28.700  30.120  1.00 20.09           N  
ATOM    123  CA  LEU A  15      13.988  27.980  31.367  1.00 19.51           C  
ATOM    124  C   LEU A  15      15.247  27.568  32.132  1.00 18.78           C  
ATOM    125  O   LEU A  15      15.168  26.813  33.108  1.00 17.17           O  
ATOM    126  CB  LEU A  15      13.096  26.766  31.107  1.00 18.74           C  
ATOM    127  CG  LEU A  15      11.646  27.178  30.805  1.00 19.07           C  
ATOM    128  CD1 LEU A  15      10.772  25.971  30.453  1.00 16.83           C  
ATOM    129  CD2 LEU A  15      11.097  27.892  32.022  1.00 18.45           C  
ATOM    130  N   GLY A  16      16.397  28.072  31.691  1.00 16.97           N  
ATOM    131  CA  GLY A  16      17.657  27.777  32.361  1.00 16.89           C  
ATOM    132  C   GLY A  16      18.281  26.407  32.141  1.00 14.40           C  
ATOM    133  O   GLY A  16      18.984  25.897  33.013  1.00 10.14           O  
ATOM    134  N   MET A  17      18.067  25.841  30.959  1.00 13.90           N  
ATOM    135  CA  MET A  17      18.605  24.529  30.610  1.00 15.47           C  
ATOM    136  C   MET A  17      19.983  24.548  29.939  1.00 14.37           C  
ATOM    137  O   MET A  17      20.624  23.511  29.853  1.00 12.91           O  
ATOM    138  CB  MET A  17      17.628  23.768  29.710  1.00 13.13           C  
ATOM    139  CG  MET A  17      16.338  23.361  30.399  1.00 14.30           C  
ATOM    140  SD  MET A  17      16.561  22.092  31.660  1.00 21.92           S  
ATOM    141  CE  MET A  17      16.087  20.699  30.701  1.00  8.10           C  
ATOM    142  N   ASP A  18      20.430  25.706  29.462  1.00 16.02           N  
ATOM    143  CA  ASP A  18      21.730  25.793  28.789  1.00 20.13           C  
ATOM    144  C   ASP A  18      22.851  25.585  29.794  1.00 15.69           C  
ATOM    145  O   ASP A  18      23.109  26.457  30.637  1.00 15.03           O  
ATOM    146  CB  ASP A  18      21.906  27.144  28.057  1.00 19.69           C  
ATOM    147  CG  ASP A  18      22.958  27.088  26.929  1.00 20.53           C  
ATOM    148  OD1 ASP A  18      23.498  25.996  26.616  1.00 19.08           O  
ATOM    149  OD2 ASP A  18      23.227  28.152  26.334  1.00 18.85           O  
ATOM    150  N   GLY A  19      23.397  24.369  29.778  1.00 14.91           N  
ATOM    151  CA  GLY A  19      24.500  24.021  30.654  1.00 13.74           C  
ATOM    152  C   GLY A  19      24.122  23.609  32.057  1.00 14.65           C  
ATOM    153  O   GLY A  19      24.992  23.524  32.944  1.00 13.83           O  
ATOM    154  N   TYR A  20      22.844  23.324  32.286  1.00 14.66           N  
ATOM    155  CA  TYR A  20      22.423  22.933  33.622  1.00 11.16           C  
ATOM    156  C   TYR A  20      23.210  21.664  33.946  1.00 13.88           C  
ATOM    157  O   TYR A  20      23.151  20.682  33.193  1.00 16.87           O  
ATOM    158  CB  TYR A  20      20.898  22.693  33.676  1.00 11.07           C  
ATOM    159  CG  TYR A  20      20.393  22.386  35.068  1.00  6.94           C  
ATOM    160  CD1 TYR A  20      20.223  23.391  36.016  1.00 11.21           C  
ATOM    161  CD2 TYR A  20      20.187  21.069  35.472  1.00 13.48           C  
ATOM    162  CE1 TYR A  20      19.868  23.079  37.347  1.00  8.83           C  
ATOM    163  CE2 TYR A  20      19.841  20.751  36.785  1.00  8.53           C  
ATOM    164  CZ  TYR A  20      19.691  21.748  37.709  1.00 11.00           C  
ATOM    165  OH  TYR A  20      19.423  21.380  39.003  1.00 13.05           O  
ATOM    166  N   ARG A  21      24.009  21.715  35.015  1.00 13.70           N  
ATOM    167  CA  ARG A  21      24.832  20.568  35.427  1.00 14.34           C  
ATOM    168  C   ARG A  21      25.791  20.053  34.331  1.00 11.24           C  
ATOM    169  O   ARG A  21      26.020  18.852  34.215  1.00 10.19           O  
ATOM    170  CB  ARG A  21      23.923  19.431  35.909  1.00 17.35           C  
ATOM    171  CG  ARG A  21      23.113  19.830  37.101  1.00 21.06           C  
ATOM    172  CD  ARG A  21      23.936  19.739  38.344  1.00 27.11           C  
ATOM    173  NE  ARG A  21      24.115  18.341  38.717  1.00 36.31           N  
ATOM    174  CZ  ARG A  21      24.785  17.936  39.789  1.00 42.16           C  
ATOM    175  NH1 ARG A  21      24.890  16.638  40.058  1.00 40.51           N  
ATOM    176  NH2 ARG A  21      25.373  18.829  40.581  1.00 47.16           N  
ATOM    177  N   GLY A  22      26.259  20.950  33.470  1.00  9.93           N  
ATOM    178  CA  GLY A  22      27.178  20.565  32.421  1.00  9.72           C  
ATOM    179  C   GLY A  22      26.549  20.136  31.125  1.00 11.43           C  
ATOM    180  O   GLY A  22      27.267  19.870  30.156  1.00 11.10           O  
ATOM    181  N   ILE A  23      25.219  20.119  31.068  1.00 11.91           N  
ATOM    182  CA  ILE A  23      24.520  19.679  29.858  1.00 11.81           C  
ATOM    183  C   ILE A  23      24.152  20.832  28.912  1.00 13.04           C  
ATOM    184  O   ILE A  23      23.420  21.752  29.295  1.00 15.85           O  
ATOM    185  CB  ILE A  23      23.238  18.872  30.232  1.00 10.52           C  
ATOM    186  CG1 ILE A  23      23.577  17.785  31.250  1.00  6.91           C  
ATOM    187  CG2 ILE A  23      22.632  18.233  28.985  1.00  8.68           C  
ATOM    188  CD1 ILE A  23      22.376  17.161  31.981  1.00  4.35           C  
ATOM    189  N   SER A  24      24.632  20.772  27.671  1.00  9.36           N  
ATOM    190  CA  SER A  24      24.328  21.817  26.710  1.00  8.46           C  
ATOM    191  C   SER A  24      22.910  21.731  26.169  1.00 13.00           C  
ATOM    192  O   SER A  24      22.322  20.647  26.065  1.00 13.08           O  
ATOM    193  CB  SER A  24      25.278  21.769  25.536  1.00  8.46           C  
ATOM    194  OG  SER A  24      25.119  20.569  24.831  1.00 11.99           O  
ATOM    195  N   LEU A  25      22.413  22.871  25.712  1.00 12.97           N  
ATOM    196  CA  LEU A  25      21.074  22.972  25.166  1.00 17.90           C  
ATOM    197  C   LEU A  25      20.871  21.953  24.039  1.00 18.35           C  
ATOM    198  O   LEU A  25      19.820  21.303  23.954  1.00 18.82           O  
ATOM    199  CB  LEU A  25      20.849  24.393  24.648  1.00 19.42           C  
ATOM    200  CG  LEU A  25      19.423  24.915  24.622  1.00 21.37           C  
ATOM    201  CD1 LEU A  25      18.955  25.183  26.046  1.00 19.77           C  
ATOM    202  CD2 LEU A  25      19.409  26.195  23.802  1.00 22.79           C  
ATOM    203  N   ALA A  26      21.894  21.781  23.206  1.00 17.36           N  
ATOM    204  CA  ALA A  26      21.834  20.835  22.089  1.00 12.66           C  
ATOM    205  C   ALA A  26      21.697  19.381  22.567  1.00 11.46           C  
ATOM    206  O   ALA A  26      21.190  18.527  21.836  1.00 11.77           O  
ATOM    207  CB  ALA A  26      23.039  20.999  21.204  1.00 12.55           C  
ATOM    208  N   ASN A  27      22.133  19.094  23.789  1.00  8.53           N  
ATOM    209  CA  ASN A  27      21.985  17.733  24.310  1.00 12.03           C  
ATOM    210  C   ASN A  27      20.530  17.486  24.711  1.00 14.07           C  
ATOM    211  O   ASN A  27      19.959  16.448  24.376  1.00 14.39           O  
ATOM    212  CB  ASN A  27      22.936  17.477  25.467  1.00  7.34           C  
ATOM    213  CG  ASN A  27      24.320  17.066  24.983  1.00 11.10           C  
ATOM    214  OD1 ASN A  27      24.492  15.987  24.424  1.00  7.16           O  
ATOM    215  ND2 ASN A  27      25.291  17.942  25.142  1.00 11.21           N  
ATOM    216  N   TRP A  28      19.930  18.475  25.377  1.00 15.43           N  
ATOM    217  CA  TRP A  28      18.529  18.432  25.800  1.00 14.59           C  
ATOM    218  C   TRP A  28      17.619  18.365  24.547  1.00 15.81           C  
ATOM    219  O   TRP A  28      16.628  17.622  24.528  1.00 17.55           O  
ATOM    220  CB  TRP A  28      18.179  19.677  26.639  1.00 12.30           C  
ATOM    221  CG  TRP A  28      18.787  19.758  28.026  1.00  4.33           C  
ATOM    222  CD1 TRP A  28      19.606  20.734  28.490  1.00  6.21           C  
ATOM    223  CD2 TRP A  28      18.514  18.898  29.156  1.00  6.26           C  
ATOM    224  NE1 TRP A  28      19.849  20.560  29.840  1.00  4.43           N  
ATOM    225  CE2 TRP A  28      19.195  19.440  30.270  1.00  2.79           C  
ATOM    226  CE3 TRP A  28      17.742  17.737  29.335  1.00  5.28           C  
ATOM    227  CZ2 TRP A  28      19.127  18.866  31.546  1.00  2.72           C  
ATOM    228  CZ3 TRP A  28      17.669  17.165  30.606  1.00  3.05           C  
ATOM    229  CH2 TRP A  28      18.355  17.730  31.690  1.00  3.80           C  
ATOM    230  N   MET A  29      17.943  19.142  23.514  1.00 13.21           N  
ATOM    231  CA  MET A  29      17.164  19.141  22.266  1.00 13.81           C  
ATOM    232  C   MET A  29      17.219  17.772  21.632  1.00 16.04           C  
ATOM    233  O   MET A  29      16.239  17.305  21.053  1.00 18.86           O  
ATOM    234  CB  MET A  29      17.710  20.154  21.251  1.00  9.56           C  
ATOM    235  CG  MET A  29      17.400  21.599  21.558  1.00  7.88           C  
ATOM    236  SD  MET A  29      15.629  21.872  21.460  1.00 14.99           S  
ATOM    237  CE  MET A  29      15.409  21.741  19.675  1.00  6.11           C  
ATOM    238  N   CYS A  30      18.393  17.148  21.690  1.00 16.43           N  
ATOM    239  CA  CYS A  30      18.592  15.819  21.118  1.00 13.06           C  
ATOM    240  C   CYS A  30      17.791  14.771  21.894  1.00 11.62           C  
ATOM    241  O   CYS A  30      17.213  13.862  21.301  1.00 10.64           O  
ATOM    242  CB  CYS A  30      20.081  15.477  21.105  1.00 12.49           C  
ATOM    243  SG  CYS A  30      20.522  13.927  20.262  1.00 12.58           S  
ATOM    244  N   LEU A  31      17.745  14.912  23.217  1.00  9.67           N  
ATOM    245  CA  LEU A  31      16.974  13.991  24.057  1.00 11.30           C  
ATOM    246  C   LEU A  31      15.478  14.087  23.668  1.00 12.70           C  
ATOM    247  O   LEU A  31      14.886  13.107  23.191  1.00 16.02           O  
ATOM    248  CB  LEU A  31      17.151  14.356  25.546  1.00 10.50           C  
ATOM    249  CG  LEU A  31      16.271  13.590  26.542  1.00  3.44           C  
ATOM    250  CD1 LEU A  31      16.591  12.116  26.449  1.00  6.93           C  
ATOM    251  CD2 LEU A  31      16.516  14.061  27.953  1.00  6.94           C  
ATOM    252  N   ALA A  32      14.905  15.290  23.800  1.00 13.28           N  
ATOM    253  CA  ALA A  32      13.489  15.543  23.482  1.00 14.44           C  
ATOM    254  C   ALA A  32      13.114  14.973  22.106  1.00 18.73           C  
ATOM    255  O   ALA A  32      12.139  14.199  21.975  1.00 19.28           O  
ATOM    256  CB  ALA A  32      13.192  17.030  23.542  1.00 11.77           C  
ATOM    257  N   LYS A  33      13.918  15.309  21.097  1.00 18.55           N  
ATOM    258  CA  LYS A  33      13.723  14.829  19.724  1.00 19.47           C  
ATOM    259  C   LYS A  33      13.590  13.309  19.668  1.00 19.77           C  
ATOM    260  O   LYS A  33      12.681  12.777  19.028  1.00 19.60           O  
ATOM    261  CB  LYS A  33      14.903  15.266  18.852  1.00 20.41           C  
ATOM    262  CG  LYS A  33      15.108  14.454  17.589  1.00 24.87           C  
ATOM    263  CD  LYS A  33      14.119  14.815  16.504  1.00 29.75           C  
ATOM    264  CE  LYS A  33      14.511  14.139  15.181  1.00 34.88           C  
ATOM    265  NZ  LYS A  33      14.413  12.629  15.160  1.00 29.01           N  
ATOM    266  N   TRP A  34      14.480  12.611  20.360  1.00 16.30           N  
ATOM    267  CA  TRP A  34      14.427  11.175  20.331  1.00 15.88           C  
ATOM    268  C   TRP A  34      13.459  10.562  21.327  1.00 17.92           C  
ATOM    269  O   TRP A  34      12.990   9.437  21.125  1.00 16.57           O  
ATOM    270  CB  TRP A  34      15.844  10.581  20.432  1.00 15.60           C  
ATOM    271  CG  TRP A  34      16.601  10.820  19.158  1.00 14.84           C  
ATOM    272  CD1 TRP A  34      17.556  11.775  18.934  1.00 14.96           C  
ATOM    273  CD2 TRP A  34      16.375  10.183  17.893  1.00 14.09           C  
ATOM    274  NE1 TRP A  34      17.921  11.784  17.613  1.00 13.37           N  
ATOM    275  CE2 TRP A  34      17.216  10.817  16.949  1.00 14.76           C  
ATOM    276  CE3 TRP A  34      15.530   9.149  17.461  1.00 14.49           C  
ATOM    277  CZ2 TRP A  34      17.241  10.451  15.595  1.00 16.53           C  
ATOM    278  CZ3 TRP A  34      15.548   8.785  16.115  1.00 15.96           C  
ATOM    279  CH2 TRP A  34      16.401   9.440  15.198  1.00 20.72           C  
ATOM    280  N   GLU A  35      13.097  11.312  22.364  1.00 17.70           N  
ATOM    281  CA  GLU A  35      12.172  10.787  23.363  1.00 16.96           C  
ATOM    282  C   GLU A  35      10.708  10.855  22.940  1.00 18.07           C  
ATOM    283  O   GLU A  35      10.002   9.868  23.018  1.00 16.22           O  
ATOM    284  CB  GLU A  35      12.312  11.510  24.714  1.00 17.38           C  
ATOM    285  CG  GLU A  35      13.506  11.104  25.562  1.00 20.68           C  
ATOM    286  CD  GLU A  35      13.653   9.595  25.724  1.00 24.50           C  
ATOM    287  OE1 GLU A  35      12.629   8.893  25.863  1.00 26.16           O  
ATOM    288  OE2 GLU A  35      14.804   9.105  25.721  1.00 21.89           O  
ATOM    289  N   SER A  36      10.270  12.026  22.494  1.00 20.20           N  
ATOM    290  CA  SER A  36       8.870  12.253  22.129  1.00 19.15           C  
ATOM    291  C   SER A  36       8.670  12.952  20.784  1.00 19.35           C  
ATOM    292  O   SER A  36       7.541  13.149  20.345  1.00 19.79           O  
ATOM    293  CB  SER A  36       8.256  13.144  23.198  1.00 17.65           C  
ATOM    294  OG  SER A  36       8.911  14.409  23.198  1.00 18.92           O  
ATOM    295  N   GLY A  37       9.763  13.383  20.164  1.00 20.94           N  
ATOM    296  CA  GLY A  37       9.669  14.086  18.896  1.00 16.02           C  
ATOM    297  C   GLY A  37       9.067  15.453  19.108  1.00 14.78           C  
ATOM    298  O   GLY A  37       8.257  15.895  18.292  1.00  9.39           O  
ATOM    299  N   TYR A  38       9.416  16.070  20.244  1.00 12.88           N  
ATOM    300  CA  TYR A  38       8.971  17.414  20.654  1.00 14.33           C  
ATOM    301  C   TYR A  38       7.491  17.503  21.040  1.00 14.98           C  
ATOM    302  O   TYR A  38       6.941  18.605  21.162  1.00 10.44           O  
ATOM    303  CB  TYR A  38       9.266  18.471  19.575  1.00 16.30           C  
ATOM    304  CG  TYR A  38      10.703  18.517  19.080  1.00 18.07           C  
ATOM    305  CD1 TYR A  38      10.981  18.828  17.752  1.00 15.15           C  
ATOM    306  CD2 TYR A  38      11.778  18.247  19.931  1.00 18.85           C  
ATOM    307  CE1 TYR A  38      12.279  18.868  17.277  1.00 15.21           C  
ATOM    308  CE2 TYR A  38      13.092  18.285  19.455  1.00 19.52           C  
ATOM    309  CZ  TYR A  38      13.321  18.599  18.125  1.00 16.89           C  
ATOM    310  OH  TYR A  38      14.594  18.647  17.628  1.00 23.00           O  
ATOM    311  N   ASN A  39       6.892  16.344  21.308  1.00 16.09           N  
ATOM    312  CA  ASN A  39       5.482  16.214  21.668  1.00 16.00           C  
ATOM    313  C   ASN A  39       5.292  16.104  23.185  1.00 15.93           C  
ATOM    314  O   ASN A  39       5.688  15.099  23.809  1.00 13.73           O  
ATOM    315  CB  ASN A  39       4.922  14.969  20.973  1.00 18.21           C  
ATOM    316  CG  ASN A  39       3.471  14.674  21.342  1.00 20.92           C  
ATOM    317  OD1 ASN A  39       2.738  15.528  21.851  1.00 18.35           O  
ATOM    318  ND2 ASN A  39       3.059  13.445  21.090  1.00 23.37           N  
ATOM    319  N   THR A  40       4.640  17.123  23.748  1.00 15.53           N  
ATOM    320  CA  THR A  40       4.347  17.233  25.179  1.00 16.22           C  
ATOM    321  C   THR A  40       3.321  16.235  25.732  1.00 15.98           C  
ATOM    322  O   THR A  40       3.194  16.071  26.952  1.00 14.84           O  
ATOM    323  CB  THR A  40       3.843  18.644  25.519  1.00 16.85           C  
ATOM    324  OG1 THR A  40       2.558  18.841  24.916  1.00 19.95           O  
ATOM    325  CG2 THR A  40       4.786  19.700  24.981  1.00 17.25           C  
ATOM    326  N   ARG A  41       2.517  15.621  24.877  1.00 19.16           N  
ATOM    327  CA  ARG A  41       1.572  14.663  25.436  1.00 24.66           C  
ATOM    328  C   ARG A  41       1.841  13.211  25.046  1.00 23.60           C  
ATOM    329  O   ARG A  41       0.942  12.372  25.051  1.00 27.37           O  
ATOM    330  CB  ARG A  41       0.113  15.097  25.225  1.00 28.76           C  
ATOM    331  CG  ARG A  41      -0.284  15.393  23.797  1.00 35.90           C  
ATOM    332  CD  ARG A  41      -1.157  14.294  23.238  1.00 42.78           C  
ATOM    333  NE  ARG A  41      -2.401  14.107  23.982  1.00 43.86           N  
ATOM    334  CZ  ARG A  41      -3.212  13.067  23.821  1.00 45.30           C  
ATOM    335  NH1 ARG A  41      -2.909  12.118  22.937  1.00 43.87           N  
ATOM    336  NH2 ARG A  41      -4.321  12.969  24.551  1.00 44.80           N  
ATOM    337  N   ALA A  42       3.110  12.918  24.754  1.00 26.29           N  
ATOM    338  CA  ALA A  42       3.549  11.566  24.407  1.00 24.28           C  
ATOM    339  C   ALA A  42       3.616  10.727  25.681  1.00 22.38           C  
ATOM    340  O   ALA A  42       4.058  11.205  26.735  1.00 21.03           O  
ATOM    341  CB  ALA A  42       4.908  11.619  23.765  1.00 25.90           C  
ATOM    342  N   THR A  43       3.141   9.492  25.606  1.00 23.51           N  
ATOM    343  CA  THR A  43       3.181   8.591  26.762  1.00 23.02           C  
ATOM    344  C   THR A  43       3.537   7.208  26.267  1.00 23.14           C  
ATOM    345  O   THR A  43       3.294   6.869  25.094  1.00 24.45           O  
ATOM    346  CB  THR A  43       1.844   8.488  27.499  1.00 21.93           C  
ATOM    347  OG1 THR A  43       0.827   8.115  26.568  1.00 24.03           O  
ATOM    348  CG2 THR A  43       1.476   9.805  28.168  1.00 22.16           C  
ATOM    349  N   ASN A  44       4.143   6.419  27.146  1.00 22.66           N  
ATOM    350  CA  ASN A  44       4.550   5.071  26.784  1.00 21.22           C  
ATOM    351  C   ASN A  44       4.416   4.158  27.962  1.00 20.05           C  
ATOM    352  O   ASN A  44       5.083   4.334  28.983  1.00 15.16           O  
ATOM    353  CB  ASN A  44       5.996   5.048  26.293  1.00 24.56           C  
ATOM    354  CG  ASN A  44       6.102   4.769  24.806  1.00 31.97           C  
ATOM    355  OD1 ASN A  44       6.100   5.695  23.987  1.00 38.82           O  
ATOM    356  ND2 ASN A  44       6.198   3.492  24.442  1.00 28.30           N  
ATOM    357  N   TYR A  45       3.493   3.216  27.834  1.00 20.84           N  
ATOM    358  CA  TYR A  45       3.247   2.239  28.870  1.00 17.38           C  
ATOM    359  C   TYR A  45       4.238   1.103  28.652  1.00 16.42           C  
ATOM    360  O   TYR A  45       4.396   0.601  27.539  1.00 17.89           O  
ATOM    361  CB  TYR A  45       1.805   1.724  28.799  1.00 12.54           C  
ATOM    362  CG  TYR A  45       1.510   0.703  29.852  1.00  9.14           C  
ATOM    363  CD1 TYR A  45       1.200  -0.612  29.516  1.00 12.02           C  
ATOM    364  CD2 TYR A  45       1.614   1.030  31.198  1.00 15.67           C  
ATOM    365  CE1 TYR A  45       1.012  -1.586  30.507  1.00 12.71           C  
ATOM    366  CE2 TYR A  45       1.422   0.072  32.195  1.00 14.19           C  
ATOM    367  CZ  TYR A  45       1.128  -1.228  31.846  1.00 12.79           C  
ATOM    368  OH  TYR A  45       0.989  -2.161  32.848  1.00 17.31           O  
ATOM    369  N   ASN A  46       4.966   0.765  29.703  1.00 15.60           N  
ATOM    370  CA  ASN A  46       5.944  -0.305  29.654  1.00 17.84           C  
ATOM    371  C   ASN A  46       5.261  -1.408  30.436  1.00 18.01           C  
ATOM    372  O   ASN A  46       5.178  -1.348  31.672  1.00 18.30           O  
ATOM    373  CB  ASN A  46       7.237   0.127  30.349  1.00 18.67           C  
ATOM    374  CG  ASN A  46       7.865   1.368  29.710  1.00 19.33           C  
ATOM    375  OD1 ASN A  46       8.438   1.308  28.620  1.00 21.25           O  
ATOM    376  ND2 ASN A  46       7.757   2.499  30.393  1.00 23.28           N  
ATOM    377  N   ALA A  47       4.704  -2.371  29.705  1.00 18.43           N  
ATOM    378  CA  ALA A  47       3.973  -3.483  30.314  1.00 22.41           C  
ATOM    379  C   ALA A  47       4.828  -4.358  31.240  1.00 24.05           C  
ATOM    380  O   ALA A  47       4.304  -5.026  32.133  1.00 21.73           O  
ATOM    381  CB  ALA A  47       3.297  -4.328  29.239  1.00 19.93           C  
ATOM    382  N   GLY A  48       6.141  -4.326  31.036  1.00 23.02           N  
ATOM    383  CA  GLY A  48       7.037  -5.107  31.861  1.00 21.80           C  
ATOM    384  C   GLY A  48       6.979  -4.741  33.331  1.00 20.12           C  
ATOM    385  O   GLY A  48       6.604  -5.567  34.152  1.00 20.68           O  
ATOM    386  N   ASP A  49       7.361  -3.518  33.683  1.00 18.59           N  
ATOM    387  CA  ASP A  49       7.336  -3.134  35.089  1.00 19.26           C  
ATOM    388  C   ASP A  49       6.155  -2.235  35.425  1.00 20.90           C  
ATOM    389  O   ASP A  49       6.193  -1.495  36.417  1.00 20.43           O  
ATOM    390  CB  ASP A  49       8.658  -2.482  35.505  1.00 20.96           C  
ATOM    391  CG  ASP A  49       8.853  -1.114  34.897  1.00 22.53           C  
ATOM    392  OD1 ASP A  49       8.789  -0.996  33.653  1.00 25.79           O  
ATOM    393  OD2 ASP A  49       9.079  -0.160  35.668  1.00 23.60           O  
ATOM    394  N   ARG A  50       5.141  -2.265  34.558  1.00 22.14           N  
ATOM    395  CA  ARG A  50       3.908  -1.493  34.748  1.00 23.45           C  
ATOM    396  C   ARG A  50       4.104  -0.004  35.045  1.00 23.39           C  
ATOM    397  O   ARG A  50       3.456   0.550  35.940  1.00 20.52           O  
ATOM    398  CB  ARG A  50       3.088  -2.126  35.864  1.00 23.37           C  
ATOM    399  CG  ARG A  50       2.604  -3.504  35.532  1.00 30.01           C  
ATOM    400  CD  ARG A  50       2.108  -4.202  36.772  1.00 34.58           C  
ATOM    401  NE  ARG A  50       1.333  -5.379  36.409  1.00 44.01           N  
ATOM    402  CZ  ARG A  50       0.354  -5.885  37.153  1.00 47.32           C  
ATOM    403  NH1 ARG A  50      -0.304  -6.960  36.728  1.00 48.23           N  
ATOM    404  NH2 ARG A  50       0.042  -5.324  38.320  1.00 48.03           N  
ATOM    405  N   SER A  51       5.014   0.629  34.307  1.00 23.28           N  
ATOM    406  CA  SER A  51       5.312   2.045  34.469  1.00 20.87           C  
ATOM    407  C   SER A  51       4.959   2.745  33.161  1.00 19.32           C  
ATOM    408  O   SER A  51       4.725   2.077  32.150  1.00 18.63           O  
ATOM    409  CB  SER A  51       6.803   2.230  34.773  1.00 25.80           C  
ATOM    410  OG  SER A  51       7.609   1.747  33.702  1.00 28.18           O  
ATOM    411  N   THR A  52       4.917   4.073  33.171  1.00 13.46           N  
ATOM    412  CA  THR A  52       4.601   4.831  31.961  1.00 14.10           C  
ATOM    413  C   THR A  52       5.629   5.957  31.856  1.00 13.30           C  
ATOM    414  O   THR A  52       6.116   6.438  32.877  1.00  8.58           O  
ATOM    415  CB  THR A  52       3.144   5.455  32.031  1.00 14.30           C  
ATOM    416  OG1 THR A  52       2.187   4.415  32.245  1.00 12.04           O  
ATOM    417  CG2 THR A  52       2.772   6.188  30.741  1.00 10.42           C  
ATOM    418  N   ASP A  53       6.033   6.284  30.629  1.00 13.92           N  
ATOM    419  CA  ASP A  53       6.960   7.380  30.370  1.00 15.51           C  
ATOM    420  C   ASP A  53       6.032   8.505  29.892  1.00 16.96           C  
ATOM    421  O   ASP A  53       5.227   8.285  28.980  1.00 17.07           O  
ATOM    422  CB  ASP A  53       7.948   7.016  29.262  1.00 16.13           C  
ATOM    423  CG  ASP A  53       8.711   5.735  29.552  1.00 18.45           C  
ATOM    424  OD1 ASP A  53       9.224   5.581  30.684  1.00 16.60           O  
ATOM    425  OD2 ASP A  53       8.773   4.868  28.648  1.00 17.86           O  
ATOM    426  N   TYR A  54       6.155   9.688  30.508  1.00 17.53           N  
ATOM    427  CA  TYR A  54       5.307  10.853  30.222  1.00 17.18           C  
ATOM    428  C   TYR A  54       5.979  12.099  29.643  1.00 17.42           C  
ATOM    429  O   TYR A  54       7.101  12.463  30.027  1.00 19.54           O  
ATOM    430  CB  TYR A  54       4.619  11.318  31.519  1.00 15.90           C  
ATOM    431  CG  TYR A  54       3.674  10.315  32.158  1.00 18.98           C  
ATOM    432  CD1 TYR A  54       2.296  10.437  31.991  1.00 16.64           C  
ATOM    433  CD2 TYR A  54       4.153   9.280  32.981  1.00 13.89           C  
ATOM    434  CE1 TYR A  54       1.414   9.573  32.627  1.00 14.71           C  
ATOM    435  CE2 TYR A  54       3.276   8.400  33.626  1.00 11.13           C  
ATOM    436  CZ  TYR A  54       1.899   8.565  33.442  1.00 11.37           C  
ATOM    437  OH  TYR A  54       1.002   7.760  34.105  1.00  7.07           O  
ATOM    438  N   GLY A  55       5.256  12.779  28.763  1.00 14.94           N  
ATOM    439  CA  GLY A  55       5.729  14.031  28.206  1.00 14.03           C  
ATOM    440  C   GLY A  55       6.889  14.113  27.234  1.00 12.55           C  
ATOM    441  O   GLY A  55       7.445  13.107  26.754  1.00 13.12           O  
ATOM    442  N   ILE A  56       7.280  15.358  27.013  1.00 10.42           N  
ATOM    443  CA  ILE A  56       8.349  15.727  26.094  1.00 13.13           C  
ATOM    444  C   ILE A  56       9.709  15.062  26.383  1.00 11.07           C  
ATOM    445  O   ILE A  56      10.441  14.760  25.451  1.00  8.02           O  
ATOM    446  CB  ILE A  56       8.436  17.304  25.933  1.00 10.22           C  
ATOM    447  CG1 ILE A  56       9.166  17.679  24.643  1.00 11.75           C  
ATOM    448  CG2 ILE A  56       9.034  17.968  27.162  1.00  4.42           C  
ATOM    449  CD1 ILE A  56       9.113  19.168  24.299  1.00  8.77           C  
ATOM    450  N   PHE A  57      10.016  14.779  27.649  1.00  9.16           N  
ATOM    451  CA  PHE A  57      11.290  14.117  27.969  1.00 10.79           C  
ATOM    452  C   PHE A  57      11.125  12.645  28.285  1.00 14.80           C  
ATOM    453  O   PHE A  57      12.104  11.951  28.481  1.00 15.71           O  
ATOM    454  CB  PHE A  57      12.021  14.810  29.120  1.00  9.20           C  
ATOM    455  CG  PHE A  57      12.521  16.183  28.770  1.00 10.08           C  
ATOM    456  CD1 PHE A  57      12.287  17.261  29.624  1.00 10.08           C  
ATOM    457  CD2 PHE A  57      13.169  16.411  27.549  1.00 12.31           C  
ATOM    458  CE1 PHE A  57      12.686  18.555  29.266  1.00 11.93           C  
ATOM    459  CE2 PHE A  57      13.572  17.696  27.176  1.00 10.49           C  
ATOM    460  CZ  PHE A  57      13.328  18.770  28.036  1.00 12.77           C  
ATOM    461  N   GLN A  58       9.880  12.173  28.321  1.00 15.18           N  
ATOM    462  CA  GLN A  58       9.569  10.786  28.613  1.00 11.09           C  
ATOM    463  C   GLN A  58      10.072  10.299  29.962  1.00 11.01           C  
ATOM    464  O   GLN A  58      10.749   9.281  30.063  1.00 13.96           O  
ATOM    465  CB  GLN A  58      10.032   9.873  27.487  1.00 14.79           C  
ATOM    466  CG  GLN A  58       9.173   9.972  26.229  1.00 17.15           C  
ATOM    467  CD  GLN A  58       7.788   9.339  26.409  1.00 19.33           C  
ATOM    468  OE1 GLN A  58       7.663   8.115  26.510  1.00 18.52           O  
ATOM    469  NE2 GLN A  58       6.754  10.168  26.455  1.00 14.98           N  
ATOM    470  N   ILE A  59       9.665  11.017  30.998  1.00 10.70           N  
ATOM    471  CA  ILE A  59       9.997  10.719  32.380  1.00  8.85           C  
ATOM    472  C   ILE A  59       9.119   9.572  32.880  1.00 15.87           C  
ATOM    473  O   ILE A  59       7.900   9.567  32.667  1.00 18.47           O  
ATOM    474  CB  ILE A  59       9.858  11.981  33.219  1.00  4.49           C  
ATOM    475  CG1 ILE A  59      10.937  12.990  32.761  1.00  7.38           C  
ATOM    476  CG2 ILE A  59       9.934  11.662  34.684  1.00  6.54           C  
ATOM    477  CD1 ILE A  59      10.996  14.295  33.540  1.00  4.81           C  
ATOM    478  N   ASN A  60       9.772   8.578  33.487  1.00 14.72           N  
ATOM    479  CA  ASN A  60       9.156   7.360  33.996  1.00 12.33           C  
ATOM    480  C   ASN A  60       8.498   7.444  35.391  1.00 15.52           C  
ATOM    481  O   ASN A  60       9.111   7.896  36.365  1.00 13.89           O  
ATOM    482  CB  ASN A  60      10.215   6.244  33.970  1.00 12.67           C  
ATOM    483  CG  ASN A  60       9.663   4.890  34.335  1.00  9.92           C  
ATOM    484  OD1 ASN A  60       9.671   4.482  35.505  1.00 13.27           O  
ATOM    485  ND2 ASN A  60       9.222   4.164  33.338  1.00  6.77           N  
ATOM    486  N   SER A  61       7.282   6.894  35.481  1.00 16.72           N  
ATOM    487  CA  SER A  61       6.469   6.864  36.694  1.00 14.24           C  
ATOM    488  C   SER A  61       7.031   6.150  37.905  1.00 14.57           C  
ATOM    489  O   SER A  61       6.707   6.527  39.040  1.00 13.51           O  
ATOM    490  CB  SER A  61       5.087   6.279  36.386  1.00 14.24           C  
ATOM    491  OG  SER A  61       5.174   5.006  35.755  1.00 15.60           O  
ATOM    492  N   ARG A  62       7.831   5.103  37.690  1.00 17.32           N  
ATOM    493  CA  ARG A  62       8.409   4.356  38.815  1.00 15.09           C  
ATOM    494  C   ARG A  62       9.297   5.169  39.753  1.00 16.15           C  
ATOM    495  O   ARG A  62       9.323   4.927  40.967  1.00 14.37           O  
ATOM    496  CB  ARG A  62       9.200   3.147  38.327  1.00 20.11           C  
ATOM    497  CG  ARG A  62       9.998   2.443  39.447  1.00 16.23           C  
ATOM    498  CD  ARG A  62      10.287   1.013  39.093  1.00 22.86           C  
ATOM    499  NE  ARG A  62       9.073   0.280  38.723  1.00 24.22           N  
ATOM    500  CZ  ARG A  62       8.024   0.093  39.525  1.00 23.06           C  
ATOM    501  NH1 ARG A  62       6.973  -0.595  39.082  1.00 20.23           N  
ATOM    502  NH2 ARG A  62       8.032   0.592  40.764  1.00 22.97           N  
ATOM    503  N   TYR A  63       9.961   6.181  39.212  1.00 15.33           N  
ATOM    504  CA  TYR A  63      10.878   6.934  40.022  1.00 16.17           C  
ATOM    505  C   TYR A  63      10.608   8.416  40.217  1.00 15.27           C  
ATOM    506  O   TYR A  63      10.711   8.937  41.334  1.00 13.73           O  
ATOM    507  CB  TYR A  63      12.282   6.764  39.427  1.00 18.85           C  
ATOM    508  CG  TYR A  63      12.678   5.330  39.087  1.00 19.24           C  
ATOM    509  CD1 TYR A  63      12.688   4.878  37.762  1.00 16.42           C  
ATOM    510  CD2 TYR A  63      13.075   4.436  40.088  1.00 20.65           C  
ATOM    511  CE1 TYR A  63      13.079   3.577  37.440  1.00 12.92           C  
ATOM    512  CE2 TYR A  63      13.468   3.126  39.778  1.00 20.03           C  
ATOM    513  CZ  TYR A  63      13.466   2.704  38.450  1.00 20.79           C  
ATOM    514  OH  TYR A  63      13.836   1.402  38.148  1.00 21.03           O  
ATOM    515  N   TRP A  64      10.182   9.076  39.154  1.00 15.55           N  
ATOM    516  CA  TRP A  64      10.024  10.522  39.167  1.00 12.12           C  
ATOM    517  C   TRP A  64       8.695  11.200  39.506  1.00 16.07           C  
ATOM    518  O   TRP A  64       8.695  12.261  40.142  1.00 13.77           O  
ATOM    519  CB  TRP A  64      10.592  11.020  37.851  1.00 11.04           C  
ATOM    520  CG  TRP A  64      11.934  10.365  37.610  1.00 15.78           C  
ATOM    521  CD1 TRP A  64      12.201   9.314  36.769  1.00 14.54           C  
ATOM    522  CD2 TRP A  64      13.154  10.630  38.322  1.00 16.09           C  
ATOM    523  NE1 TRP A  64      13.511   8.901  36.933  1.00 16.60           N  
ATOM    524  CE2 TRP A  64      14.118   9.688  37.875  1.00 17.27           C  
ATOM    525  CE3 TRP A  64      13.531  11.570  39.299  1.00 19.02           C  
ATOM    526  CZ2 TRP A  64      15.434   9.661  38.374  1.00 11.92           C  
ATOM    527  CZ3 TRP A  64      14.855  11.538  39.797  1.00 14.92           C  
ATOM    528  CH2 TRP A  64      15.779  10.586  39.327  1.00  8.63           C  
ATOM    529  N   CYS A  65       7.576  10.597  39.112  1.00 14.06           N  
ATOM    530  CA  CYS A  65       6.249  11.177  39.394  1.00 16.59           C  
ATOM    531  C   CYS A  65       5.229  10.142  39.870  1.00 13.79           C  
ATOM    532  O   CYS A  65       5.454   8.928  39.786  1.00 13.02           O  
ATOM    533  CB  CYS A  65       5.696  11.939  38.180  1.00 12.90           C  
ATOM    534  SG  CYS A  65       5.417  10.938  36.687  1.00 16.08           S  
ATOM    535  N   ASN A  66       4.111  10.617  40.405  1.00 13.63           N  
ATOM    536  CA  ASN A  66       3.095   9.704  40.908  1.00 11.41           C  
ATOM    537  C   ASN A  66       1.865   9.653  40.035  1.00 10.73           C  
ATOM    538  O   ASN A  66       1.255  10.697  39.783  1.00 11.10           O  
ATOM    539  CB  ASN A  66       2.708  10.111  42.318  1.00 11.04           C  
ATOM    540  CG  ASN A  66       1.565   9.286  42.864  1.00 16.13           C  
ATOM    541  OD1 ASN A  66       1.489   8.079  42.622  1.00 10.73           O  
ATOM    542  ND2 ASN A  66       0.665   9.929  43.608  1.00 12.99           N  
ATOM    543  N   ASP A  67       1.531   8.458  39.542  1.00 11.67           N  
ATOM    544  CA  ASP A  67       0.341   8.244  38.714  1.00 12.09           C  
ATOM    545  C   ASP A  67      -0.610   7.257  39.396  1.00 12.88           C  
ATOM    546  O   ASP A  67      -1.610   6.817  38.828  1.00 13.57           O  
ATOM    547  CB  ASP A  67       0.686   7.799  37.275  1.00 13.11           C  
ATOM    548  CG  ASP A  67       1.353   6.429  37.193  1.00 14.59           C  
ATOM    549  OD1 ASP A  67       1.701   5.825  38.222  1.00 19.00           O  
ATOM    550  OD2 ASP A  67       1.551   5.951  36.062  1.00 16.56           O  
ATOM    551  N   GLY A  68      -0.268   6.892  40.623  1.00 11.59           N  
ATOM    552  CA  GLY A  68      -1.083   5.984  41.393  1.00  7.89           C  
ATOM    553  C   GLY A  68      -1.200   4.543  40.939  1.00 12.23           C  
ATOM    554  O   GLY A  68      -1.590   3.698  41.742  1.00 12.65           O  
ATOM    555  N   LYS A  69      -0.849   4.230  39.692  1.00 13.88           N  
ATOM    556  CA  LYS A  69      -0.980   2.852  39.210  1.00 16.04           C  
ATOM    557  C   LYS A  69       0.297   2.021  39.035  1.00 16.92           C  
ATOM    558  O   LYS A  69       0.222   0.842  38.702  1.00 17.61           O  
ATOM    559  CB  LYS A  69      -1.797   2.822  37.920  1.00 12.89           C  
ATOM    560  CG  LYS A  69      -1.365   3.811  36.867  1.00 12.71           C  
ATOM    561  CD  LYS A  69      -1.300   3.123  35.532  1.00 19.16           C  
ATOM    562  CE  LYS A  69      -1.969   3.939  34.457  1.00 22.59           C  
ATOM    563  NZ  LYS A  69      -1.269   5.213  34.211  1.00 29.73           N  
ATOM    564  N   THR A  70       1.457   2.640  39.233  1.00 18.47           N  
ATOM    565  CA  THR A  70       2.744   1.951  39.109  1.00 19.98           C  
ATOM    566  C   THR A  70       3.071   1.315  40.452  1.00 19.41           C  
ATOM    567  O   THR A  70       3.190   2.026  41.451  1.00 17.80           O  
ATOM    568  CB  THR A  70       3.859   2.937  38.768  1.00 21.62           C  
ATOM    569  OG1 THR A  70       3.513   3.670  37.581  1.00 23.33           O  
ATOM    570  CG2 THR A  70       5.182   2.191  38.566  1.00 24.39           C  
ATOM    571  N   PRO A  71       3.210  -0.027  40.499  1.00 23.63           N  
ATOM    572  CA  PRO A  71       3.516  -0.780  41.727  1.00 23.44           C  
ATOM    573  C   PRO A  71       4.830  -0.414  42.385  1.00 24.61           C  
ATOM    574  O   PRO A  71       5.861  -0.400  41.729  1.00 24.91           O  
ATOM    575  CB  PRO A  71       3.542  -2.227  41.243  1.00 22.26           C  
ATOM    576  CG  PRO A  71       2.634  -2.216  40.053  1.00 24.30           C  
ATOM    577  CD  PRO A  71       3.062  -0.952  39.363  1.00 21.44           C  
ATOM    578  N   GLY A  72       4.778  -0.127  43.686  1.00 24.65           N  
ATOM    579  CA  GLY A  72       5.969   0.233  44.446  1.00 24.28           C  
ATOM    580  C   GLY A  72       6.836   1.352  43.875  1.00 22.47           C  
ATOM    581  O   GLY A  72       8.060   1.317  44.008  1.00 23.77           O  
ATOM    582  N   ALA A  73       6.204   2.326  43.229  1.00 20.19           N  
ATOM    583  CA  ALA A  73       6.879   3.461  42.613  1.00 16.84           C  
ATOM    584  C   ALA A  73       7.292   4.501  43.633  1.00 14.92           C  
ATOM    585  O   ALA A  73       6.950   4.401  44.812  1.00 15.28           O  
ATOM    586  CB  ALA A  73       5.963   4.108  41.581  1.00 17.89           C  
ATOM    587  N   SER A  74       7.984   5.525  43.147  1.00 16.24           N  
ATOM    588  CA  SER A  74       8.441   6.652  43.966  1.00 17.44           C  
ATOM    589  C   SER A  74       8.113   7.965  43.248  1.00 12.39           C  
ATOM    590  O   SER A  74       7.862   7.960  42.041  1.00 14.94           O  
ATOM    591  CB  SER A  74       9.944   6.554  44.250  1.00 17.58           C  
ATOM    592  OG  SER A  74      10.179   6.258  45.621  1.00 23.84           O  
ATOM    593  N   ASN A  75       8.158   9.078  43.975  1.00 11.41           N  
ATOM    594  CA  ASN A  75       7.829  10.395  43.419  1.00 13.75           C  
ATOM    595  C   ASN A  75       8.879  11.454  43.773  1.00 14.17           C  
ATOM    596  O   ASN A  75       8.612  12.389  44.543  1.00 14.19           O  
ATOM    597  CB  ASN A  75       6.453  10.821  43.945  1.00 12.96           C  
ATOM    598  CG  ASN A  75       5.896  12.042  43.240  1.00 11.72           C  
ATOM    599  OD1 ASN A  75       6.316  12.391  42.139  1.00 13.02           O  
ATOM    600  ND2 ASN A  75       4.909  12.677  43.862  1.00 10.22           N  
ATOM    601  N   ALA A  76      10.060  11.320  43.167  1.00 15.78           N  
ATOM    602  CA  ALA A  76      11.198  12.223  43.401  1.00 15.84           C  
ATOM    603  C   ALA A  76      10.989  13.679  43.005  1.00 12.57           C  
ATOM    604  O   ALA A  76      11.448  14.560  43.713  1.00 14.24           O  
ATOM    605  CB  ALA A  76      12.447  11.669  42.745  1.00 11.13           C  
ATOM    606  N   CYS A  77      10.331  13.933  41.873  1.00 13.78           N  
ATOM    607  CA  CYS A  77      10.035  15.300  41.432  1.00 12.77           C  
ATOM    608  C   CYS A  77       8.853  15.880  42.180  1.00 14.60           C  
ATOM    609  O   CYS A  77       8.543  17.066  42.032  1.00 16.45           O  
ATOM    610  CB  CYS A  77       9.695  15.337  39.941  1.00 11.93           C  
ATOM    611  SG  CYS A  77      11.111  14.829  38.945  1.00 10.64           S  
ATOM    612  N   HIS A  78       8.182  15.032  42.955  1.00 16.27           N  
ATOM    613  CA  HIS A  78       6.990  15.396  43.714  1.00 16.32           C  
ATOM    614  C   HIS A  78       5.940  16.050  42.865  1.00 16.21           C  
ATOM    615  O   HIS A  78       5.402  17.098  43.199  1.00 17.78           O  
ATOM    616  CB  HIS A  78       7.335  16.196  44.954  1.00 17.83           C  
ATOM    617  CG  HIS A  78       7.998  15.359  45.989  1.00 24.46           C  
ATOM    618  ND1 HIS A  78       9.341  15.047  45.931  1.00 27.92           N  
ATOM    619  CD2 HIS A  78       7.483  14.618  46.998  1.00 27.00           C  
ATOM    620  CE1 HIS A  78       9.620  14.139  46.848  1.00 28.62           C  
ATOM    621  NE2 HIS A  78       8.510  13.860  47.508  1.00 27.43           N  
ATOM    622  N   LEU A  79       5.619  15.368  41.776  1.00 17.15           N  
ATOM    623  CA  LEU A  79       4.637  15.851  40.832  1.00 16.46           C  
ATOM    624  C   LEU A  79       3.688  14.731  40.506  1.00 17.28           C  
ATOM    625  O   LEU A  79       3.991  13.560  40.775  1.00 10.26           O  
ATOM    626  CB  LEU A  79       5.312  16.250  39.520  1.00 19.45           C  
ATOM    627  CG  LEU A  79       6.274  17.423  39.555  1.00 22.33           C  
ATOM    628  CD1 LEU A  79       6.858  17.614  38.171  1.00 21.91           C  
ATOM    629  CD2 LEU A  79       5.528  18.668  40.028  1.00 22.40           C  
ATOM    630  N   SER A  80       2.508  15.112  40.007  1.00 11.98           N  
ATOM    631  CA  SER A  80       1.525  14.158  39.545  1.00  7.56           C  
ATOM    632  C   SER A  80       2.015  14.030  38.105  1.00  6.28           C  
ATOM    633  O   SER A  80       2.362  15.045  37.484  1.00  7.12           O  
ATOM    634  CB  SER A  80       0.109  14.778  39.524  1.00  9.23           C  
ATOM    635  OG  SER A  80      -0.711  14.138  38.539  1.00  7.12           O  
ATOM    636  N   CYS A  81       1.982  12.823  37.555  1.00  7.53           N  
ATOM    637  CA  CYS A  81       2.431  12.624  36.188  1.00 12.38           C  
ATOM    638  C   CYS A  81       1.611  13.417  35.168  1.00 13.85           C  
ATOM    639  O   CYS A  81       1.955  13.465  33.985  1.00 16.03           O  
ATOM    640  CB  CYS A  81       2.470  11.138  35.842  1.00 11.81           C  
ATOM    641  SG  CYS A  81       3.546  10.136  36.922  1.00 17.88           S  
ATOM    642  N   SER A  82       0.493  13.995  35.606  1.00 16.34           N  
ATOM    643  CA  SER A  82      -0.295  14.831  34.716  1.00 13.69           C  
ATOM    644  C   SER A  82       0.499  16.125  34.518  1.00  8.46           C  
ATOM    645  O   SER A  82       0.500  16.700  33.444  1.00  8.28           O  
ATOM    646  CB  SER A  82      -1.650  15.160  35.340  1.00 17.29           C  
ATOM    647  OG  SER A  82      -2.359  16.099  34.543  1.00 19.22           O  
ATOM    648  N   ALA A  83       1.203  16.572  35.551  1.00 10.97           N  
ATOM    649  CA  ALA A  83       2.002  17.798  35.434  1.00 13.09           C  
ATOM    650  C   ALA A  83       3.003  17.717  34.271  1.00  9.61           C  
ATOM    651  O   ALA A  83       3.424  18.739  33.737  1.00 12.10           O  
ATOM    652  CB  ALA A  83       2.732  18.085  36.747  1.00  7.21           C  
ATOM    653  N   LEU A  84       3.342  16.496  33.863  1.00 11.57           N  
ATOM    654  CA  LEU A  84       4.285  16.244  32.777  1.00 13.56           C  
ATOM    655  C   LEU A  84       3.662  16.119  31.395  1.00 15.38           C  
ATOM    656  O   LEU A  84       4.372  15.821  30.438  1.00 11.66           O  
ATOM    657  CB  LEU A  84       5.093  14.975  33.065  1.00 14.67           C  
ATOM    658  CG  LEU A  84       5.874  14.961  34.376  1.00 15.41           C  
ATOM    659  CD1 LEU A  84       6.445  13.594  34.581  1.00 20.86           C  
ATOM    660  CD2 LEU A  84       6.955  16.026  34.382  1.00 10.07           C  
ATOM    661  N   LEU A  85       2.342  16.307  31.293  1.00 17.98           N  
ATOM    662  CA  LEU A  85       1.625  16.232  30.018  1.00 18.22           C  
ATOM    663  C   LEU A  85       1.027  17.590  29.578  1.00 23.13           C  
ATOM    664  O   LEU A  85       0.197  17.653  28.659  1.00 20.84           O  
ATOM    665  CB  LEU A  85       0.503  15.196  30.122  1.00 19.17           C  
ATOM    666  CG  LEU A  85       0.910  13.721  30.101  1.00 19.45           C  
ATOM    667  CD1 LEU A  85      -0.334  12.851  30.249  1.00 13.94           C  
ATOM    668  CD2 LEU A  85       1.609  13.413  28.785  1.00 15.26           C  
ATOM    669  N   GLN A  86       1.452  18.665  30.242  1.00 22.72           N  
ATOM    670  CA  GLN A  86       0.982  20.023  29.967  1.00 23.05           C  
ATOM    671  C   GLN A  86       1.599  20.642  28.721  1.00 22.42           C  
ATOM    672  O   GLN A  86       2.651  20.212  28.274  1.00 24.32           O  
ATOM    673  CB  GLN A  86       1.340  20.938  31.139  1.00 21.18           C  
ATOM    674  CG  GLN A  86       0.752  20.551  32.480  1.00 21.04           C  
ATOM    675  CD  GLN A  86       1.115  21.557  33.557  1.00 21.64           C  
ATOM    676  OE1 GLN A  86       0.752  22.732  33.471  1.00 22.40           O  
ATOM    677  NE2 GLN A  86       1.852  21.113  34.559  1.00 23.26           N  
ATOM    678  N   ASP A  87       0.946  21.654  28.163  1.00 20.66           N  
ATOM    679  CA  ASP A  87       1.516  22.356  27.015  1.00 22.59           C  
ATOM    680  C   ASP A  87       2.639  23.242  27.575  1.00 19.30           C  
ATOM    681  O   ASP A  87       3.572  23.571  26.860  1.00 16.52           O  
ATOM    682  CB  ASP A  87       0.472  23.221  26.284  1.00 27.65           C  
ATOM    683  CG  ASP A  87      -0.305  22.448  25.191  1.00 31.61           C  
ATOM    684  OD1 ASP A  87      -0.372  21.193  25.270  1.00 33.69           O  
ATOM    685  OD2 ASP A  87      -0.863  23.099  24.259  1.00 28.69           O  
ATOM    686  N   ASN A  88       2.528  23.639  28.846  1.00 15.87           N  
ATOM    687  CA  ASN A  88       3.554  24.448  29.493  1.00 18.68           C  
ATOM    688  C   ASN A  88       4.584  23.508  30.129  1.00 21.38           C  
ATOM    689  O   ASN A  88       4.343  22.923  31.197  1.00 19.11           O  
ATOM    690  CB  ASN A  88       2.975  25.385  30.571  1.00 18.97           C  
ATOM    691  CG  ASN A  88       4.050  26.309  31.185  1.00 21.05           C  
ATOM    692  OD1 ASN A  88       4.610  26.026  32.239  1.00 23.21           O  
ATOM    693  ND2 ASN A  88       4.350  27.394  30.506  1.00 26.42           N  
ATOM    694  N   ILE A  89       5.749  23.411  29.502  1.00 18.72           N  
ATOM    695  CA  ILE A  89       6.798  22.514  29.991  1.00 16.97           C  
ATOM    696  C   ILE A  89       7.586  22.885  31.268  1.00 15.09           C  
ATOM    697  O   ILE A  89       8.424  22.107  31.705  1.00  9.89           O  
ATOM    698  CB  ILE A  89       7.787  22.142  28.851  1.00 14.32           C  
ATOM    699  CG1 ILE A  89       8.537  23.382  28.352  1.00 12.86           C  
ATOM    700  CG2 ILE A  89       7.032  21.481  27.698  1.00 14.66           C  
ATOM    701  CD1 ILE A  89       9.899  23.057  27.706  1.00 12.49           C  
ATOM    702  N   ALA A  90       7.279  24.012  31.908  1.00 15.29           N  
ATOM    703  CA  ALA A  90       8.006  24.417  33.120  1.00 16.14           C  
ATOM    704  C   ALA A  90       8.173  23.340  34.192  1.00 16.84           C  
ATOM    705  O   ALA A  90       9.229  23.251  34.813  1.00 16.60           O  
ATOM    706  CB  ALA A  90       7.396  25.660  33.728  1.00 15.67           C  
ATOM    707  N   ASP A  91       7.144  22.534  34.434  1.00 18.94           N  
ATOM    708  CA  ASP A  91       7.268  21.477  35.435  1.00 15.84           C  
ATOM    709  C   ASP A  91       8.092  20.302  34.891  1.00 13.54           C  
ATOM    710  O   ASP A  91       8.870  19.708  35.636  1.00 11.77           O  
ATOM    711  CB  ASP A  91       5.899  20.981  35.913  1.00 21.22           C  
ATOM    712  CG  ASP A  91       5.147  22.011  36.741  1.00 24.06           C  
ATOM    713  OD1 ASP A  91       4.025  22.392  36.333  1.00 31.07           O  
ATOM    714  OD2 ASP A  91       5.651  22.417  37.807  1.00 23.48           O  
ATOM    715  N   ALA A  92       7.909  19.960  33.612  1.00  8.60           N  
ATOM    716  CA  ALA A  92       8.660  18.873  32.981  1.00  8.96           C  
ATOM    717  C   ALA A  92      10.174  19.203  32.980  1.00 10.45           C  
ATOM    718  O   ALA A  92      11.013  18.326  33.159  1.00 12.22           O  
ATOM    719  CB  ALA A  92       8.171  18.639  31.557  1.00  2.00           C  
ATOM    720  N   VAL A  93      10.504  20.465  32.753  1.00 10.14           N  
ATOM    721  CA  VAL A  93      11.889  20.923  32.753  1.00  9.95           C  
ATOM    722  C   VAL A  93      12.425  20.892  34.187  1.00 13.22           C  
ATOM    723  O   VAL A  93      13.591  20.569  34.401  1.00 17.15           O  
ATOM    724  CB  VAL A  93      12.000  22.358  32.191  1.00  5.89           C  
ATOM    725  CG1 VAL A  93      13.330  23.009  32.610  1.00 11.50           C  
ATOM    726  CG2 VAL A  93      11.878  22.326  30.686  1.00  5.61           C  
ATOM    727  N   ALA A  94      11.584  21.222  35.166  1.00 12.29           N  
ATOM    728  CA  ALA A  94      12.010  21.201  36.557  1.00  9.93           C  
ATOM    729  C   ALA A  94      12.272  19.759  37.011  1.00 13.63           C  
ATOM    730  O   ALA A  94      13.161  19.503  37.835  1.00 16.50           O  
ATOM    731  CB  ALA A  94      10.970  21.855  37.437  1.00 14.88           C  
ATOM    732  N   CYS A  95      11.509  18.810  36.474  1.00 11.78           N  
ATOM    733  CA  CYS A  95      11.697  17.409  36.827  1.00 12.73           C  
ATOM    734  C   CYS A  95      12.907  16.789  36.103  1.00 11.28           C  
ATOM    735  O   CYS A  95      13.596  15.956  36.677  1.00 12.92           O  
ATOM    736  CB  CYS A  95      10.426  16.598  36.554  1.00  8.40           C  
ATOM    737  SG  CYS A  95      10.514  14.845  37.014  1.00 13.67           S  
ATOM    738  N   ALA A  96      13.149  17.191  34.855  1.00 12.42           N  
ATOM    739  CA  ALA A  96      14.269  16.699  34.089  1.00 10.22           C  
ATOM    740  C   ALA A  96      15.557  17.164  34.776  1.00 16.33           C  
ATOM    741  O   ALA A  96      16.581  16.498  34.683  1.00 19.53           O  
ATOM    742  CB  ALA A  96      14.199  17.220  32.695  1.00 11.64           C  
ATOM    743  N   LYS A  97      15.504  18.299  35.474  1.00 16.18           N  
ATOM    744  CA  LYS A  97      16.671  18.811  36.194  1.00 13.64           C  
ATOM    745  C   LYS A  97      16.931  17.915  37.407  1.00 17.46           C  
ATOM    746  O   LYS A  97      18.087  17.552  37.677  1.00 15.08           O  
ATOM    747  CB  LYS A  97      16.471  20.268  36.649  1.00  6.81           C  
ATOM    748  CG  LYS A  97      16.538  21.290  35.517  1.00  4.82           C  
ATOM    749  CD  LYS A  97      16.368  22.738  36.023  1.00  3.26           C  
ATOM    750  CE  LYS A  97      16.319  23.701  34.839  1.00  5.60           C  
ATOM    751  NZ  LYS A  97      16.232  25.129  35.246  1.00  5.34           N  
ATOM    752  N   ARG A  98      15.856  17.531  38.104  1.00 12.81           N  
ATOM    753  CA  ARG A  98      15.953  16.668  39.280  1.00 13.14           C  
ATOM    754  C   ARG A  98      16.550  15.318  38.895  1.00 15.48           C  
ATOM    755  O   ARG A  98      17.291  14.698  39.670  1.00 18.61           O  
ATOM    756  CB  ARG A  98      14.564  16.465  39.901  1.00 16.23           C  
ATOM    757  CG  ARG A  98      14.480  15.336  40.939  1.00 17.35           C  
ATOM    758  CD  ARG A  98      15.457  15.572  42.065  1.00 14.90           C  
ATOM    759  NE  ARG A  98      15.417  14.554  43.105  1.00 12.48           N  
ATOM    760  CZ  ARG A  98      16.172  13.466  43.118  1.00 15.31           C  
ATOM    761  NH1 ARG A  98      16.079  12.608  44.127  1.00 17.25           N  
ATOM    762  NH2 ARG A  98      17.004  13.218  42.115  1.00 18.58           N  
ATOM    763  N   VAL A  99      16.199  14.852  37.703  1.00 12.49           N  
ATOM    764  CA  VAL A  99      16.705  13.593  37.200  1.00 10.00           C  
ATOM    765  C   VAL A  99      18.215  13.700  37.013  1.00 12.54           C  
ATOM    766  O   VAL A  99      18.944  12.791  37.417  1.00 15.91           O  
ATOM    767  CB  VAL A  99      16.063  13.220  35.838  1.00  9.96           C  
ATOM    768  CG1 VAL A  99      16.660  11.899  35.307  1.00  5.23           C  
ATOM    769  CG2 VAL A  99      14.537  13.106  35.993  1.00  8.36           C  
ATOM    770  N   VAL A 100      18.690  14.786  36.394  1.00 13.47           N  
ATOM    771  CA  VAL A 100      20.138  14.949  36.162  1.00 13.92           C  
ATOM    772  C   VAL A 100      20.969  15.366  37.386  1.00 18.74           C  
ATOM    773  O   VAL A 100      22.188  15.492  37.297  1.00 22.15           O  
ATOM    774  CB  VAL A 100      20.475  15.809  34.918  1.00 12.33           C  
ATOM    775  CG1 VAL A 100      19.704  15.309  33.712  1.00 10.78           C  
ATOM    776  CG2 VAL A 100      20.237  17.303  35.182  1.00 10.88           C  
ATOM    777  N   ARG A 101      20.314  15.571  38.527  1.00 17.99           N  
ATOM    778  CA  ARG A 101      21.008  15.862  39.772  1.00 17.76           C  
ATOM    779  C   ARG A 101      21.311  14.505  40.418  1.00 22.04           C  
ATOM    780  O   ARG A 101      21.571  14.405  41.620  1.00 24.40           O  
ATOM    781  CB  ARG A 101      20.147  16.698  40.708  1.00 17.26           C  
ATOM    782  CG  ARG A 101      20.253  18.191  40.465  1.00 18.44           C  
ATOM    783  CD  ARG A 101      19.543  18.959  41.563  1.00 24.50           C  
ATOM    784  NE  ARG A 101      18.113  19.125  41.294  1.00 32.99           N  
ATOM    785  CZ  ARG A 101      17.149  19.047  42.211  1.00 36.10           C  
ATOM    786  NH1 ARG A 101      15.894  19.222  41.842  1.00 39.26           N  
ATOM    787  NH2 ARG A 101      17.422  18.776  43.485  1.00 39.86           N  
ATOM    788  N   ASP A 102      21.229  13.458  39.602  1.00 22.79           N  
ATOM    789  CA  ASP A 102      21.497  12.087  40.004  1.00 24.87           C  
ATOM    790  C   ASP A 102      22.854  11.719  39.375  1.00 27.96           C  
ATOM    791  O   ASP A 102      23.201  12.236  38.300  1.00 28.49           O  
ATOM    792  CB  ASP A 102      20.405  11.187  39.431  1.00 25.30           C  
ATOM    793  CG  ASP A 102      19.689  10.410  40.481  1.00 24.48           C  
ATOM    794  OD1 ASP A 102      19.440   9.221  40.226  1.00 34.31           O  
ATOM    795  OD2 ASP A 102      19.371  10.961  41.560  1.00 29.37           O  
ATOM    796  N   PRO A 103      23.582  10.746  39.973  1.00 28.97           N  
ATOM    797  CA  PRO A 103      24.900  10.255  39.540  1.00 26.12           C  
ATOM    798  C   PRO A 103      25.137  10.087  38.042  1.00 23.85           C  
ATOM    799  O   PRO A 103      26.193  10.479  37.538  1.00 24.15           O  
ATOM    800  CB  PRO A 103      25.028   8.924  40.282  1.00 28.10           C  
ATOM    801  CG  PRO A 103      23.606   8.522  40.569  1.00 29.98           C  
ATOM    802  CD  PRO A 103      23.029   9.839  40.994  1.00 31.98           C  
ATOM    803  N   GLN A 104      24.190   9.474  37.334  1.00 19.92           N  
ATOM    804  CA  GLN A 104      24.347   9.279  35.894  1.00 17.91           C  
ATOM    805  C   GLN A 104      24.201  10.560  35.064  1.00 15.60           C  
ATOM    806  O   GLN A 104      24.694  10.632  33.934  1.00 18.05           O  
ATOM    807  CB  GLN A 104      23.356   8.233  35.367  1.00 19.23           C  
ATOM    808  CG  GLN A 104      23.786   6.780  35.527  1.00 29.65           C  
ATOM    809  CD  GLN A 104      23.038   5.810  34.589  1.00 30.60           C  
ATOM    810  OE1 GLN A 104      21.882   5.458  34.832  1.00 31.19           O  
ATOM    811  NE2 GLN A 104      23.715   5.357  33.536  1.00 31.79           N  
ATOM    812  N   GLY A 105      23.512  11.561  35.600  1.00 15.01           N  
ATOM    813  CA  GLY A 105      23.298  12.781  34.833  1.00 13.48           C  
ATOM    814  C   GLY A 105      22.388  12.515  33.627  1.00 14.57           C  
ATOM    815  O   GLY A 105      21.462  11.701  33.700  1.00  9.04           O  
ATOM    816  N   ILE A 106      22.695  13.140  32.494  1.00 14.44           N  
ATOM    817  CA  ILE A 106      21.906  12.987  31.279  1.00 16.74           C  
ATOM    818  C   ILE A 106      21.892  11.531  30.807  1.00 20.52           C  
ATOM    819  O   ILE A 106      21.029  11.111  30.021  1.00 20.58           O  
ATOM    820  CB  ILE A 106      22.424  13.950  30.154  1.00 16.20           C  
ATOM    821  CG1 ILE A 106      21.531  13.877  28.901  1.00 17.03           C  
ATOM    822  CG2 ILE A 106      23.889  13.685  29.844  1.00 13.84           C  
ATOM    823  CD1 ILE A 106      20.500  15.018  28.751  1.00 18.08           C  
ATOM    824  N   ARG A 107      22.828  10.747  31.333  1.00 22.03           N  
ATOM    825  CA  ARG A 107      22.939   9.334  30.981  1.00 19.07           C  
ATOM    826  C   ARG A 107      21.789   8.524  31.525  1.00 17.55           C  
ATOM    827  O   ARG A 107      21.665   7.355  31.210  1.00 19.11           O  
ATOM    828  CB  ARG A 107      24.266   8.755  31.487  1.00 16.61           C  
ATOM    829  CG  ARG A 107      25.416   9.062  30.565  1.00 16.56           C  
ATOM    830  CD  ARG A 107      26.753   8.876  31.250  1.00 16.54           C  
ATOM    831  NE  ARG A 107      27.828   8.792  30.263  1.00 21.49           N  
ATOM    832  CZ  ARG A 107      28.344   9.826  29.605  1.00 21.02           C  
ATOM    833  NH1 ARG A 107      29.305   9.611  28.712  1.00 17.86           N  
ATOM    834  NH2 ARG A 107      27.927  11.069  29.859  1.00 15.92           N  
ATOM    835  N   ALA A 108      20.950   9.133  32.351  1.00 20.47           N  
ATOM    836  CA  ALA A 108      19.806   8.422  32.908  1.00 18.81           C  
ATOM    837  C   ALA A 108      18.924   7.845  31.795  1.00 17.26           C  
ATOM    838  O   ALA A 108      18.444   6.712  31.884  1.00 20.46           O  
ATOM    839  CB  ALA A 108      19.013   9.352  33.789  1.00 22.25           C  
ATOM    840  N   TRP A 109      18.791   8.604  30.714  1.00 16.10           N  
ATOM    841  CA  TRP A 109      17.986   8.219  29.552  1.00 14.45           C  
ATOM    842  C   TRP A 109      18.775   7.422  28.513  1.00 14.34           C  
ATOM    843  O   TRP A 109      19.608   7.996  27.799  1.00 14.39           O  
ATOM    844  CB  TRP A 109      17.464   9.485  28.858  1.00 12.38           C  
ATOM    845  CG  TRP A 109      16.401  10.236  29.590  1.00 15.62           C  
ATOM    846  CD1 TRP A 109      15.065  10.039  29.476  1.00 16.18           C  
ATOM    847  CD2 TRP A 109      16.570  11.368  30.470  1.00 15.14           C  
ATOM    848  NE1 TRP A 109      14.382  10.983  30.206  1.00 18.32           N  
ATOM    849  CE2 TRP A 109      15.276  11.810  30.830  1.00 15.45           C  
ATOM    850  CE3 TRP A 109      17.683  12.053  30.981  1.00 12.85           C  
ATOM    851  CZ2 TRP A 109      15.054  12.906  31.677  1.00 12.28           C  
ATOM    852  CZ3 TRP A 109      17.468  13.146  31.823  1.00  7.39           C  
ATOM    853  CH2 TRP A 109      16.158  13.560  32.162  1.00 17.28           C  
ATOM    854  N   VAL A 110      18.446   6.148  28.339  1.00 12.45           N  
ATOM    855  CA  VAL A 110      19.136   5.308  27.354  1.00 15.87           C  
ATOM    856  C   VAL A 110      19.104   5.813  25.898  1.00 14.66           C  
ATOM    857  O   VAL A 110      20.014   5.519  25.127  1.00 18.08           O  
ATOM    858  CB  VAL A 110      18.645   3.829  27.406  1.00 14.89           C  
ATOM    859  CG1 VAL A 110      19.274   3.004  26.301  1.00 17.22           C  
ATOM    860  CG2 VAL A 110      19.021   3.219  28.718  1.00 16.83           C  
ATOM    861  N   ALA A 111      18.075   6.552  25.499  1.00 16.05           N  
ATOM    862  CA  ALA A 111      18.020   7.063  24.117  1.00 15.33           C  
ATOM    863  C   ALA A 111      19.060   8.161  23.914  1.00 16.66           C  
ATOM    864  O   ALA A 111      19.476   8.419  22.775  1.00 15.09           O  
ATOM    865  CB  ALA A 111      16.636   7.591  23.771  1.00 15.39           C  
ATOM    866  N   TRP A 112      19.405   8.870  25.000  1.00 15.32           N  
ATOM    867  CA  TRP A 112      20.436   9.902  24.933  1.00 14.66           C  
ATOM    868  C   TRP A 112      21.720   9.145  24.589  1.00 14.30           C  
ATOM    869  O   TRP A 112      22.418   9.481  23.632  1.00 16.46           O  
ATOM    870  CB  TRP A 112      20.617  10.618  26.271  1.00 15.98           C  
ATOM    871  CG  TRP A 112      21.686  11.646  26.165  1.00 18.69           C  
ATOM    872  CD1 TRP A 112      21.570  12.877  25.602  1.00 22.70           C  
ATOM    873  CD2 TRP A 112      23.078  11.487  26.497  1.00 21.83           C  
ATOM    874  NE1 TRP A 112      22.803  13.491  25.543  1.00 24.50           N  
ATOM    875  CE2 TRP A 112      23.742  12.661  26.090  1.00 26.43           C  
ATOM    876  CE3 TRP A 112      23.824  10.464  27.093  1.00 23.05           C  
ATOM    877  CZ2 TRP A 112      25.121  12.841  26.261  1.00 25.69           C  
ATOM    878  CZ3 TRP A 112      25.191  10.643  27.261  1.00 24.52           C  
ATOM    879  CH2 TRP A 112      25.823  11.822  26.846  1.00 25.83           C  
ATOM    880  N   ARG A 113      21.980   8.091  25.355  1.00 13.57           N  
ATOM    881  CA  ARG A 113      23.136   7.235  25.138  1.00 16.82           C  
ATOM    882  C   ARG A 113      23.191   6.752  23.686  1.00 17.28           C  
ATOM    883  O   ARG A 113      24.188   6.982  23.011  1.00 22.14           O  
ATOM    884  CB  ARG A 113      23.117   6.049  26.103  1.00 12.73           C  
ATOM    885  CG  ARG A 113      23.817   6.344  27.420  1.00 20.70           C  
ATOM    886  CD  ARG A 113      23.032   5.928  28.652  1.00 20.21           C  
ATOM    887  NE  ARG A 113      23.112   4.502  28.954  1.00 30.39           N  
ATOM    888  CZ  ARG A 113      22.733   3.969  30.119  1.00 34.44           C  
ATOM    889  NH1 ARG A 113      22.833   2.657  30.325  1.00 37.41           N  
ATOM    890  NH2 ARG A 113      22.265   4.744  31.090  1.00 31.55           N  
ATOM    891  N   ASN A 114      22.099   6.175  23.188  1.00 16.50           N  
ATOM    892  CA  ASN A 114      22.033   5.665  21.817  1.00 16.40           C  
ATOM    893  C   ASN A 114      22.128   6.719  20.702  1.00 16.34           C  
ATOM    894  O   ASN A 114      22.808   6.506  19.706  1.00 16.82           O  
ATOM    895  CB  ASN A 114      20.739   4.868  21.574  1.00 17.44           C  
ATOM    896  CG  ASN A 114      20.553   3.692  22.517  1.00 17.39           C  
ATOM    897  OD1 ASN A 114      21.493   3.143  23.070  1.00 20.72           O  
ATOM    898  ND2 ASN A 114      19.307   3.270  22.660  1.00 20.12           N  
ATOM    899  N   ARG A 115      21.439   7.846  20.825  1.00 18.97           N  
ATOM    900  CA  ARG A 115      21.493   8.800  19.719  1.00 20.06           C  
ATOM    901  C   ARG A 115      22.107  10.167  19.896  1.00 20.30           C  
ATOM    902  O   ARG A 115      22.156  10.929  18.919  1.00 20.27           O  
ATOM    903  CB  ARG A 115      20.131   8.949  19.016  1.00 25.96           C  
ATOM    904  CG  ARG A 115      18.923   8.523  19.821  1.00 24.31           C  
ATOM    905  CD  ARG A 115      18.535   7.079  19.526  1.00 26.56           C  
ATOM    906  NE  ARG A 115      18.232   6.859  18.114  1.00 24.90           N  
ATOM    907  CZ  ARG A 115      17.578   5.801  17.649  1.00 27.64           C  
ATOM    908  NH1 ARG A 115      17.346   5.676  16.352  1.00 28.66           N  
ATOM    909  NH2 ARG A 115      17.165   4.855  18.478  1.00 29.14           N  
ATOM    910  N   CYS A 116      22.612  10.477  21.090  1.00 18.44           N  
ATOM    911  CA  CYS A 116      23.231  11.788  21.303  1.00 21.60           C  
ATOM    912  C   CYS A 116      24.669  11.740  21.788  1.00 22.55           C  
ATOM    913  O   CYS A 116      25.441  12.659  21.504  1.00 21.00           O  
ATOM    914  CB  CYS A 116      22.416  12.632  22.277  1.00 18.70           C  
ATOM    915  SG  CYS A 116      20.657  12.670  21.845  1.00 13.21           S  
ATOM    916  N   GLN A 117      25.000  10.721  22.577  1.00 24.43           N  
ATOM    917  CA  GLN A 117      26.346  10.589  23.108  1.00 30.20           C  
ATOM    918  C   GLN A 117      27.270  10.256  21.952  1.00 31.95           C  
ATOM    919  O   GLN A 117      27.009   9.312  21.221  1.00 36.55           O  
ATOM    920  CB  GLN A 117      26.395   9.495  24.164  1.00 29.17           C  
ATOM    921  CG  GLN A 117      27.772   9.294  24.759  1.00 31.15           C  
ATOM    922  CD  GLN A 117      27.860   8.071  25.666  1.00 36.97           C  
ATOM    923  OE1 GLN A 117      28.674   8.034  26.595  1.00 38.52           O  
ATOM    924  NE2 GLN A 117      27.042   7.056  25.390  1.00 38.37           N  
ATOM    925  N   ASN A 118      28.318  11.056  21.762  1.00 34.71           N  
ATOM    926  CA  ASN A 118      29.263  10.844  20.662  1.00 36.60           C  
ATOM    927  C   ASN A 118      28.566  10.899  19.312  1.00 36.47           C  
ATOM    928  O   ASN A 118      28.755  10.049  18.437  1.00 35.88           O  
ATOM    929  CB  ASN A 118      30.022   9.524  20.810  1.00 41.28           C  
ATOM    930  CG  ASN A 118      31.184   9.633  21.766  1.00 45.73           C  
ATOM    931  OD1 ASN A 118      31.028   9.450  22.978  1.00 48.16           O  
ATOM    932  ND2 ASN A 118      32.356   9.955  21.234  1.00 46.60           N  
ATOM    933  N   ARG A 119      27.720  11.901  19.176  1.00 36.09           N  
ATOM    934  CA  ARG A 119      26.992  12.147  17.951  1.00 35.07           C  
ATOM    935  C   ARG A 119      27.018  13.664  17.870  1.00 32.03           C  
ATOM    936  O   ARG A 119      27.166  14.339  18.891  1.00 27.76           O  
ATOM    937  CB  ARG A 119      25.554  11.665  18.082  1.00 36.75           C  
ATOM    938  CG  ARG A 119      25.419  10.216  18.456  1.00 38.78           C  
ATOM    939  CD  ARG A 119      25.089   9.356  17.261  1.00 43.18           C  
ATOM    940  NE  ARG A 119      24.685   8.019  17.695  1.00 49.87           N  
ATOM    941  CZ  ARG A 119      24.517   6.981  16.880  1.00 52.77           C  
ATOM    942  NH1 ARG A 119      24.150   5.806  17.374  1.00 53.13           N  
ATOM    943  NH2 ARG A 119      24.736   7.113  15.574  1.00 56.31           N  
ATOM    944  N   ASP A 120      26.938  14.212  16.667  1.00 31.45           N  
ATOM    945  CA  ASP A 120      26.945  15.650  16.564  1.00 32.10           C  
ATOM    946  C   ASP A 120      25.531  16.140  16.850  1.00 32.44           C  
ATOM    947  O   ASP A 120      24.600  15.873  16.090  1.00 31.10           O  
ATOM    948  CB  ASP A 120      27.435  16.111  15.190  1.00 33.20           C  
ATOM    949  CG  ASP A 120      28.037  17.523  15.211  1.00 31.57           C  
ATOM    950  OD1 ASP A 120      28.118  18.156  16.301  1.00 28.74           O  
ATOM    951  OD2 ASP A 120      28.435  17.994  14.122  1.00 28.38           O  
ATOM    952  N   VAL A 121      25.381  16.768  18.014  1.00 34.24           N  
ATOM    953  CA  VAL A 121      24.109  17.322  18.473  1.00 31.31           C  
ATOM    954  C   VAL A 121      23.948  18.794  18.099  1.00 31.28           C  
ATOM    955  O   VAL A 121      22.869  19.347  18.217  1.00 30.15           O  
ATOM    956  CB  VAL A 121      23.945  17.180  20.015  1.00 28.34           C  
ATOM    957  CG1 VAL A 121      23.753  15.731  20.392  1.00 23.58           C  
ATOM    958  CG2 VAL A 121      25.146  17.749  20.738  1.00 24.80           C  
ATOM    959  N   ARG A 122      25.018  19.421  17.619  1.00 34.75           N  
ATOM    960  CA  ARG A 122      24.984  20.839  17.249  1.00 35.38           C  
ATOM    961  C   ARG A 122      23.876  21.168  16.230  1.00 32.38           C  
ATOM    962  O   ARG A 122      23.287  22.252  16.248  1.00 28.04           O  
ATOM    963  CB  ARG A 122      26.345  21.226  16.678  1.00 41.25           C  
ATOM    964  CG  ARG A 122      26.715  22.688  16.754  1.00 45.17           C  
ATOM    965  CD  ARG A 122      27.966  22.914  15.904  1.00 53.32           C  
ATOM    966  NE  ARG A 122      29.213  23.139  16.650  1.00 60.41           N  
ATOM    967  CZ  ARG A 122      29.770  22.304  17.533  1.00 62.82           C  
ATOM    968  NH1 ARG A 122      30.914  22.641  18.117  1.00 63.58           N  
ATOM    969  NH2 ARG A 122      29.199  21.148  17.855  1.00 62.79           N  
ATOM    970  N   GLN A 123      23.572  20.200  15.373  1.00 30.95           N  
ATOM    971  CA  GLN A 123      22.556  20.359  14.342  1.00 31.41           C  
ATOM    972  C   GLN A 123      21.153  20.661  14.886  1.00 33.45           C  
ATOM    973  O   GLN A 123      20.286  21.161  14.155  1.00 34.50           O  
ATOM    974  CB  GLN A 123      22.496  19.097  13.480  1.00 30.65           C  
ATOM    975  CG  GLN A 123      22.194  17.827  14.273  1.00 31.87           C  
ATOM    976  CD  GLN A 123      21.782  16.659  13.398  1.00 33.29           C  
ATOM    977  OE1 GLN A 123      21.536  16.814  12.199  1.00 35.31           O  
ATOM    978  NE2 GLN A 123      21.700  15.481  13.995  1.00 34.98           N  
ATOM    979  N   TYR A 124      20.925  20.358  16.162  1.00 32.23           N  
ATOM    980  CA  TYR A 124      19.614  20.569  16.766  1.00 28.47           C  
ATOM    981  C   TYR A 124      19.339  22.004  17.177  1.00 28.14           C  
ATOM    982  O   TYR A 124      18.188  22.360  17.388  1.00 29.84           O  
ATOM    983  CB  TYR A 124      19.404  19.618  17.945  1.00 24.46           C  
ATOM    984  CG  TYR A 124      19.449  18.146  17.570  1.00 21.76           C  
ATOM    985  CD1 TYR A 124      18.456  17.582  16.774  1.00 24.39           C  
ATOM    986  CD2 TYR A 124      20.463  17.310  18.042  1.00 19.70           C  
ATOM    987  CE1 TYR A 124      18.470  16.212  16.462  1.00 24.43           C  
ATOM    988  CE2 TYR A 124      20.486  15.940  17.733  1.00 19.88           C  
ATOM    989  CZ  TYR A 124      19.491  15.407  16.949  1.00 22.57           C  
ATOM    990  OH  TYR A 124      19.499  14.079  16.630  1.00 24.93           O  
ATOM    991  N   VAL A 125      20.383  22.826  17.289  1.00 27.36           N  
ATOM    992  CA  VAL A 125      20.209  24.229  17.669  1.00 25.09           C  
ATOM    993  C   VAL A 125      20.768  25.210  16.650  1.00 26.19           C  
ATOM    994  O   VAL A 125      20.962  26.388  16.956  1.00 28.08           O  
ATOM    995  CB  VAL A 125      20.842  24.546  19.033  1.00 23.49           C  
ATOM    996  CG1 VAL A 125      20.161  23.757  20.120  1.00 20.52           C  
ATOM    997  CG2 VAL A 125      22.334  24.245  19.009  1.00 25.61           C  
ATOM    998  N   GLN A 126      21.013  24.742  15.434  1.00 29.29           N  
ATOM    999  CA  GLN A 126      21.562  25.614  14.411  1.00 33.61           C  
ATOM   1000  C   GLN A 126      20.517  26.540  13.825  1.00 33.99           C  
ATOM   1001  O   GLN A 126      19.487  26.107  13.308  1.00 34.30           O  
ATOM   1002  CB  GLN A 126      22.263  24.813  13.312  1.00 39.32           C  
ATOM   1003  CG  GLN A 126      23.535  24.079  13.787  1.00 48.93           C  
ATOM   1004  CD  GLN A 126      24.499  24.975  14.598  1.00 53.50           C  
ATOM   1005  OE1 GLN A 126      25.451  25.559  14.055  1.00 53.60           O  
ATOM   1006  NE2 GLN A 126      24.258  25.065  15.904  1.00 54.61           N  
ATOM   1007  N   GLY A 127      20.795  27.832  13.930  1.00 33.82           N  
ATOM   1008  CA  GLY A 127      19.883  28.836  13.422  1.00 32.88           C  
ATOM   1009  C   GLY A 127      18.844  29.295  14.424  1.00 31.22           C  
ATOM   1010  O   GLY A 127      18.071  30.206  14.127  1.00 34.35           O  
ATOM   1011  N   CYS A 128      18.848  28.716  15.621  1.00 27.66           N  
ATOM   1012  CA  CYS A 128      17.859  29.069  16.626  1.00 23.23           C  
ATOM   1013  C   CYS A 128      18.219  30.284  17.475  1.00 22.46           C  
ATOM   1014  O   CYS A 128      17.464  30.647  18.378  1.00 23.72           O  
ATOM   1015  CB  CYS A 128      17.543  27.866  17.532  1.00 23.73           C  
ATOM   1016  SG  CYS A 128      16.927  26.326  16.742  1.00 24.22           S  
ATOM   1017  N   GLY A 129      19.370  30.897  17.208  1.00 22.21           N  
ATOM   1018  CA  GLY A 129      19.793  32.067  17.968  1.00 23.12           C  
ATOM   1019  C   GLY A 129      19.949  31.862  19.469  1.00 24.14           C  
ATOM   1020  O   GLY A 129      19.750  32.786  20.270  1.00 23.60           O  
ATOM   1021  N   VAL A 130      20.352  30.656  19.845  1.00 26.66           N  
ATOM   1022  CA  VAL A 130      20.520  30.303  21.252  1.00 31.79           C  
ATOM   1023  C   VAL A 130      21.985  30.209  21.678  1.00 30.85           C  
ATOM   1024  O   VAL A 130      22.864  30.344  20.801  1.00 29.90           O  
ATOM   1025  CB  VAL A 130      19.799  28.956  21.585  1.00 33.34           C  
ATOM   1026  CG1 VAL A 130      18.282  29.150  21.579  1.00 32.40           C  
ATOM   1027  CG2 VAL A 130      20.193  27.876  20.578  1.00 35.36           C  
ATOM   1028  OXT VAL A 130      22.232  29.986  22.885  1.00 29.95           O  
TER    1029      VAL A 130                                                      
HETATM 1030 NA    NA A 601       5.526   5.644   8.798  1.00 28.79          NA  
HETATM 1031  O   HOH A 131       0.097  11.541  42.976  1.00  2.00           O  
HETATM 1032  O   HOH A 132       1.343  16.766  40.440  1.00  4.97           O  
HETATM 1033  O   HOH A 133      12.093  25.821  13.467  1.00  5.72           O  
HETATM 1034  O   HOH A 134       8.673  16.747  26.835  1.00 12.90           O  
HETATM 1035  O   HOH A 135      11.195  -6.942  33.805  1.00 12.00           O  
HETATM 1036  O   HOH A 136      -4.439   4.630  44.269  1.00 11.42           O  
HETATM 1037  O   HOH A 137      15.280   8.191  23.620  1.00 10.01           O  
HETATM 1038  O   HOH A 138      24.775  14.826  35.087  1.00 18.05           O  
HETATM 1039  O   HOH A 139       3.585   4.765   8.162  1.00 14.96           O  
HETATM 1040  O   HOH A 140       8.233  19.428  14.960  1.00 29.57           O  
HETATM 1041  O   HOH A 141      19.877  29.307  31.910  1.00 48.89           O  
HETATM 1042  O   HOH A 142      10.925   0.273  43.007  1.00 30.26           O  
HETATM 1043  O   HOH A 143      23.885  23.309  37.143  1.00 29.07           O  
HETATM 1044  O   HOH A 144      14.462  19.610  39.897  1.00 11.66           O  
HETATM 1045  O   HOH A 145       4.929  22.105  29.100  1.00 20.04           O  
HETATM 1046  O   HOH A 146      -1.729  17.067  35.104  1.00 20.62           O  
HETATM 1047  O   HOH A 148      25.493  20.539  11.766  1.00 30.62           O  
HETATM 1048  O   HOH A 149      17.838  18.776  13.804  1.00 23.60           O  
HETATM 1049  O   HOH A 150      -1.958  24.103  34.796  1.00 42.79           O  
HETATM 1050  O   HOH A 151      16.603   3.426  36.607  1.00 26.72           O  
HETATM 1051  O   HOH A 152      18.602  15.160  12.480  1.00 34.15           O  
HETATM 1052  O   HOH A 153      14.795  18.169  14.689  1.00 21.04           O  
HETATM 1053  O   HOH A 154      13.403  10.477  29.463  1.00 21.14           O  
HETATM 1054  O   HOH A 155       6.919  29.447  25.799  1.00 25.64           O  
HETATM 1055  O   HOH A 156      28.038  10.849  41.324  1.00 14.55           O  
HETATM 1056  O   HOH A 157      12.776  16.080  12.154  1.00 28.14           O  
HETATM 1057  O   HOH A 158       9.483   8.022  21.833  1.00 23.43           O  
HETATM 1058  O   HOH A 159      17.515  24.832  37.681  1.00 11.43           O  
HETATM 1059  O   HOH A 160      26.353  11.362  13.271  1.00 26.25           O  
HETATM 1060  O   HOH A 161       5.934  18.925  25.443  1.00 30.40           O  
HETATM 1061  O   HOH A 162       2.215   4.735  21.312  1.00 20.70           O  
HETATM 1062  O   HOH A 163       5.947  21.815  14.165  1.00 42.47           O  
HETATM 1063  O   HOH A 164      -1.665   0.918  44.242  1.00 19.74           O  
HETATM 1064  O   HOH A 165      25.953   3.991  16.173  1.00 40.86           O  
HETATM 1065  O   HOH A 166      23.676  28.793  14.641  1.00 28.13           O  
HETATM 1066  O   HOH A 167       0.630  15.914  43.522  1.00 25.42           O  
HETATM 1067  O   HOH A 168      27.149   5.797  37.776  1.00 18.75           O  
HETATM 1068  O   HOH A 169      10.462  27.971  15.541  1.00 32.25           O  
HETATM 1069  O   HOH A 170      -1.448  -1.998  29.573  1.00 39.72           O  
HETATM 1070  O   HOH A 171      22.057   8.980  12.148  1.00 42.95           O  
HETATM 1071  O   HOH A 172      13.461   8.380  17.833  1.00 36.67           O  
HETATM 1072  O   HOH A 174      -1.479   5.371  44.811  1.00 23.01           O  
HETATM 1073  O   HOH A 175      22.367  13.264  16.107  1.00 38.17           O  
HETATM 1074  O   HOH A 176      15.946   7.228  26.268  1.00 30.16           O  
HETATM 1075  O   HOH A 177      18.968   4.555  28.505  1.00 43.91           O  
HETATM 1076  O   HOH A 178      13.284  -2.037  32.678  1.00 26.43           O  
HETATM 1077  O   HOH A 179       2.041  28.563  13.649  1.00 40.30           O  
HETATM 1078  O   HOH A 180      11.108  24.314  35.808  1.00 38.70           O  
HETATM 1079  O   HOH A 181      11.947   5.544  27.475  1.00 36.25           O  
HETATM 1080  O   HOH A 182       4.482  24.967  36.361  1.00 43.11           O  
HETATM 1081  O   HOH A 183      14.087  24.443  11.196  1.00 34.13           O  
HETATM 1082  O   HOH A 184      12.244   8.851  25.769  1.00 31.14           O  
HETATM 1083  O   HOH A 185      22.964  19.225   8.948  1.00 31.96           O  
HETATM 1084  O   HOH A 186       0.758  -6.117  38.922  1.00 33.75           O  
HETATM 1085  O   HOH A 188      16.690  34.551  24.110  1.00 21.81           O  
HETATM 1086  O   HOH A 190      22.855  25.173  34.023  1.00 26.16           O  
HETATM 1087  O   HOH A 191       1.565  24.739  34.892  1.00 32.88           O  
HETATM 1088  O   HOH A 192      26.297  32.418  21.335  1.00 38.92           O  
HETATM 1089  O   HOH A 193       9.876  16.828  14.373  1.00 36.90           O  
HETATM 1090  O   HOH A 194       2.549   3.224  44.568  1.00 31.06           O  
HETATM 1091  O   HOH A 195      18.919  24.709   9.444  1.00 41.49           O  
HETATM 1092  O   HOH A 196       7.761  12.427  46.270  1.00 30.06           O  
HETATM 1093  O   HOH A 197      18.041  29.370  37.752  1.00 37.34           O  
HETATM 1094  O   HOH A 198      15.923   3.325  14.673  1.00 45.25           O  
HETATM 1095  O   HOH A 199       4.709  12.567  18.058  1.00 45.53           O  
HETATM 1096  O   HOH A 200      17.738  22.164   9.312  1.00 43.27           O  
HETATM 1097  O   HOH A 201       6.135  29.816  10.447  1.00 38.73           O  
HETATM 1098  O   HOH A 202       3.379   9.022  46.237  1.00 18.77           O  
HETATM 1099  O   HOH A 203      -0.035   5.863  26.576  1.00 29.55           O  
HETATM 1100  O   HOH A 204      22.035  30.590  11.890  1.00 28.39           O  
HETATM 1101  O   HOH A 205      20.498  12.943  12.383  1.00 38.29           O  
HETATM 1102  O   HOH A 207       2.065  29.006  24.598  1.00 37.72           O  
HETATM 1103  O   HOH A 209      27.518  28.608  13.775  1.00 45.69           O  
HETATM 1104  O   HOH A 210      16.401   3.456  27.958  1.00 29.88           O  
HETATM 1105  O   HOH A 211      14.622   6.214  34.954  1.00 40.78           O  
HETATM 1106  O   HOH A 212       8.256   8.120  46.720  1.00 19.91           O  
HETATM 1107  O   HOH A 213      27.606   4.232  14.061  1.00 41.20           O  
HETATM 1108  O   HOH A 215       4.080  32.492  30.365  1.00 32.53           O  
HETATM 1109  O   HOH A 216       5.783   1.080  21.972  1.00 41.29           O  
HETATM 1110  O   HOH A 217       4.732   6.288  45.953  1.00 17.37           O  
HETATM 1111  O   HOH A 218       6.631  31.002  23.750  1.00 34.41           O  
HETATM 1112  O   HOH A 219      -1.354   9.903  40.121  1.00 13.32           O  
HETATM 1113  O   HOH A 220      10.632  21.145  13.697  1.00 30.17           O  
HETATM 1114  O   HOH A 221      24.863  14.016  37.757  1.00 12.44           O  
HETATM 1115  O   HOH A 222       2.448   3.125   9.812  1.00 27.92           O  
HETATM 1116  O   HOH A 223      11.536  10.724  16.028  1.00 30.92           O  
HETATM 1117  O   HOH A 224       2.722  12.858  43.325  1.00 36.39           O  
HETATM 1118  O   HOH A 225       3.389   2.358  47.772  1.00 41.37           O  
HETATM 1119  O   HOH A 227      21.853  28.949  17.121  1.00 18.71           O  
HETATM 1120  O   HOH A 228      16.523   7.270  11.369  1.00 37.35           O  
HETATM 1121  O   HOH A 229       4.164  14.817  15.106  1.00 34.72           O  
HETATM 1122  O   HOH A 230      25.969  21.410  38.749  1.00 39.58           O  
HETATM 1123  O   HOH A 231       8.217  20.025  39.491  1.00 47.37           O  
HETATM 1124  O   HOH A 232      19.173  21.741  11.555  1.00 36.75           O  
HETATM 1125  O   HOH A 233      12.567  17.696  42.067  1.00 19.58           O  
HETATM 1126  O   HOH A 235      19.364   7.591  13.521  1.00 40.00           O  
HETATM 1127  O   HOH A 236      13.155  23.170  37.391  1.00 38.92           O  
HETATM 1128  O   HOH A 237       9.929  18.219  40.962  1.00 27.96           O  
HETATM 1129  O   HOH A 238      -2.006   5.755  24.139  1.00 29.01           O  
HETATM 1130  O   HOH A 239      28.487   1.329   5.396  1.00 43.84           O  
HETATM 1131  O   HOH A 242      16.930   3.708  41.341  1.00 33.70           O  
HETATM 1132  O   HOH A 243       8.200   0.458  24.883  1.00 30.81           O  
HETATM 1133  O   HOH A 245      20.109  35.526  23.629  1.00 33.35           O  
HETATM 1134  O   HOH A 246       5.046  25.072  38.986  1.00 40.26           O  
HETATM 1135  O   HOH A 249      32.417  19.609  13.645  1.00 45.34           O  
HETATM 1136  O   HOH A 250       2.418  22.440  37.943  1.00 36.61           O  
HETATM 1137  O   HOH A 251      27.611  18.991  11.845  1.00 42.28           O  
HETATM 1138  O   HOH A 253      21.525  27.314   9.234  1.00 42.90           O  
HETATM 1139  O   HOH A 254      22.062  21.615  10.262  1.00 44.21           O  
HETATM 1140  O   HOH A 255      24.711  29.093  17.039  1.00 35.71           O  
HETATM 1141  O   HOH A 257       0.134  -3.021  27.612  1.00 27.65           O  
HETATM 1142  O   HOH A 259      33.791  23.498  14.791  1.00 40.79           O  
HETATM 1143  O   HOH A 260      18.939   2.027  13.279  1.00 37.43           O  
HETATM 1144  O   HOH A 261      10.497   0.600  34.813  1.00 33.31           O  
HETATM 1145  O   HOH A 262      18.727   7.099  37.747  1.00 43.07           O  
HETATM 1146  O   HOH A 263      14.313  21.620  11.874  1.00 30.03           O  
HETATM 1147  O   HOH A 264       4.418   6.023  10.955  1.00 18.47           O  
HETATM 1148  O   HOH A 265      -1.629  -7.264  35.661  1.00 26.64           O  
HETATM 1149  O   HOH A 266      25.626  22.301  41.599  1.00 31.49           O  
HETATM 1150  O   HOH A 267      17.275   4.810  38.773  1.00 28.33           O  
HETATM 1151  O   HOH A 268       5.504   2.341  21.151  1.00 39.86           O  
HETATM 1152  O   HOH A 269       0.114  13.393  46.929  1.00 45.48           O  
HETATM 1153  O   HOH A 270       2.186   0.934  22.888  1.00 43.92           O  
HETATM 1154  O   HOH A 271       7.309   3.370  22.766  1.00 40.91           O  
HETATM 1155  O   HOH A 272      26.423  28.158   7.552  1.00 35.21           O  
HETATM 1156  O   HOH A 273      18.774   3.289  33.908  1.00 34.11           O  
HETATM 1157  O   HOH A 274      31.755  20.820  16.116  1.00 40.90           O  
HETATM 1158  O   HOH A 276      27.057  22.442  35.710  1.00 29.31           O  
HETATM 1159  O   HOH A 277       7.744  22.673  39.189  1.00 44.96           O  
HETATM 1160  O   HOH A 280      20.235  25.971  34.944  1.00 49.45           O  
HETATM 1161  O   HOH A 281       6.629  18.525  42.710  1.00 36.96           O  
HETATM 1162  O   HOH A 283      25.618  12.050  41.730  1.00 38.53           O  
HETATM 1163  O   HOH A 284       4.431  22.048  33.766  1.00 18.88           O  
HETATM 1164  O   HOH A 285       4.100  27.729  22.236  1.00 24.65           O  
HETATM 1165  O   HOH A 286      13.627   3.276  34.606  1.00 26.75           O  
HETATM 1166  O   HOH A 287       0.798  10.395  45.830  1.00 38.01           O  
HETATM 1167  O   HOH A 288      27.947  29.172   9.893  1.00 46.94           O  
HETATM 1168  O   HOH A 289      -0.403  -2.272  38.420  1.00 38.75           O  
HETATM 1169  O   HOH A 290      12.614   7.181  20.984  1.00 37.23           O  
HETATM 1170  O   HOH A 291      19.951  26.400  37.729  1.00 49.33           O  
HETATM 1171  O   HOH A 292      -1.238  13.981  44.482  1.00 36.99           O  
HETATM 1172  O   HOH A 293       6.164   9.846  18.992  1.00 45.26           O  
HETATM 1173  O   HOH A 294      11.932  21.904  10.749  1.00 30.50           O  
HETATM 1174  O   HOH A 295       9.112   9.039  49.004  1.00 40.39           O  
HETATM 1175  O   HOH A 296       3.137  -3.043  41.901  1.00 38.24           O  
HETATM 1176  O   HOH A 298       2.359   0.394  44.801  1.00 45.22           O  
HETATM 1177  O   HOH A 300       4.591  26.981  34.697  1.00 38.57           O  
HETATM 1178  O   HOH A 301      15.120  26.346   8.040  1.00 40.78           O  
HETATM 1179  O   HOH A 302      27.121   4.944  35.050  1.00 38.22           O  
HETATM 1180  O   HOH A 303      -0.528  -1.411  25.577  1.00 47.16           O  
HETATM 1181  O   HOH A 304       1.895   2.183  34.682  1.00 25.82           O  
HETATM 1182  O   HOH A 305      19.082  30.300  26.311  1.00 34.42           O  
HETATM 1183  O   HOH A 306      14.481   5.173  20.707  1.00 48.95           O  
HETATM 1184  O   HOH A 307      -2.250   8.087  44.993  1.00 38.97           O  
HETATM 1185  O   HOH A 308      12.370  -4.246  34.189  1.00 40.11           O  
HETATM 1186  O   HOH A 309      11.060  24.050  40.619  1.00 45.23           O  
HETATM 1187  O   HOH A 310       0.330   6.550  23.082  1.00 42.84           O  
HETATM 1188  O   HOH A 311      34.027  25.042  14.105  1.00 37.34           O  
HETATM 1189  O   HOH A 312      11.034  -4.275  36.812  1.00 38.42           O  
HETATM 1190  O   HOH A 315      26.283   1.516   3.839  1.00 46.10           O  
HETATM 1191  O   HOH A 316       7.444  11.138  16.656  1.00 46.01           O  
HETATM 1192  O   HOH A 317      29.655  20.845  13.428  1.00 41.10           O  
HETATM 1193  O   HOH A 318       9.757   2.486  22.129  1.00 42.55           O  
HETATM 1194  O   HOH A 320      -3.724  -0.481  43.301  1.00 45.52           O  
HETATM 1195  O   HOH A 321       6.564  -3.023  47.306  1.00 40.75           O  
HETATM 1196  O   HOH A 322      11.610   3.301  28.799  1.00 43.58           O  
HETATM 1197  O   HOH A 323      19.218   5.267  35.849  1.00 41.10           O  
CONECT   53 1016                                                                
CONECT  243  915                                                                
CONECT  534  641                                                                
CONECT  611  737                                                                
CONECT  641  534                                                                
CONECT  737  611                                                                
CONECT  915  243                                                                
CONECT 1016   53                                                                
CONECT 1030 1039 1147                                                           
CONECT 1039 1030                                                                
CONECT 1147 1030                                                                
MASTER      373    0    1    8    2    0    2    6 1196    1   11   10          
END                                                                             
