HEADER    HYDROLASE                               24-JAN-99   1B7M              
TITLE     VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (LYSOZYME);                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.17;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    MUTANT STABILITY, HUMAN LYSOZYME, HYDROLASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAKANO,M.OTA,K.OGASAHARA,Y.YAMAGATA,K.NISHIKAWA,K.YUTANI            
REVDAT   6   03-APR-24 1B7M    1       REMARK                                   
REVDAT   5   27-DEC-23 1B7M    1       REMARK                                   
REVDAT   4   03-NOV-21 1B7M    1       REMARK SEQADV LINK                       
REVDAT   3   24-FEB-09 1B7M    1       VERSN                                    
REVDAT   2   29-DEC-99 1B7M    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   27-JAN-99 1B7M    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.OGASAWAHA,H.KANEDA,Y.YAMAGATA,S.FUJII,E.KANAYA,   
REMARK   1  AUTH 2 M.KIKUCHI,M.OOBATAKE,K.YUTANI                                
REMARK   1  TITL   CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF     
REMARK   1  TITL 2 HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL    
REMARK   1  TITL 3 ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS            
REMARK   1  REF    J.MOL.BIOL.                   V. 254    62 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 5410                           
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) : 0.170                           
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 590                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1930                       
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            : 1032                                    
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) : 1.700                           
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 1B7M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000000353.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29060                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.03500                            
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: WILD-TYPE HUMAN LYSOZYME                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
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       28.43000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       16.24500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.38500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       16.24500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.43000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.38500            
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   CD2  TRP A    34     O    HOH A   239              0.55            
REMARK 500   O    VAL A   130     O    HOH A   216              0.55            
REMARK 500   C    ASN A    88     O    HOH A   136              0.58            
REMARK 500   ND2  ASN A    66     O    HOH A   131              0.61            
REMARK 500   OG   SER A    82     O    HOH A   211              0.66            
REMARK 500   O    GLU A    35     O    HOH A   200              0.78            
REMARK 500   CZ   ARG A    50     O    HOH A   288              0.82            
REMARK 500   N    ILE A    89     O    HOH A   136              0.88            
REMARK 500   C    ALA A   108     O    HOH A   199              0.91            
REMARK 500   CB   SER A    82     O    HOH A   211              0.99            
REMARK 500   CZ2  TRP A   109     O    HOH A   230              1.04            
REMARK 500   CG2  ILE A    56     O    HOH A   133              1.05            
REMARK 500   OD2  ASP A    91     O    HOH A   173              1.07            
REMARK 500   CE3  TRP A    34     O    HOH A   239              1.08            
REMARK 500   N    TRP A   109     O    HOH A   199              1.09            
REMARK 500   NH2  ARG A    50     O    HOH A   288              1.13            
REMARK 500   CG   ARG A   115     O    HOH A   135              1.17            
REMARK 500   NE1  TRP A   109     O    HOH A   217              1.21            
REMARK 500   CB   CYS A    77     O    HOH A   190              1.25            
REMARK 500   CE2  TRP A   109     O    HOH A   230              1.25            
REMARK 500   OE1  GLN A   117     O    HOH A   254              1.26            
REMARK 500   O    ARG A    50     O    HOH A   300              1.26            
REMARK 500   C    ASP A    67     O    HOH A   145              1.28            
REMARK 500   O    THR A    70     O    HOH A   140              1.29            
REMARK 500   N    SER A    80     O    HOH A   132              1.33            
REMARK 500   CA   ALA A    94     O    HOH A   219              1.39            
REMARK 500   CD   ARG A   115     O    HOH A   135              1.41            
REMARK 500   CA   TYR A    20     O    HOH A   197              1.43            
REMARK 500   CG   ARG A    21     O    HOH A   163              1.44            
REMARK 500   CH2  TRP A   109     O    HOH A   230              1.44            
REMARK 500   O    ASN A    88     O    HOH A   136              1.46            
REMARK 500   CB   ARG A    98     O    HOH A   137              1.47            
REMARK 500   NH2  ARG A    21     O    HOH A   262              1.48            
REMARK 500   CA   CYS A    77     O    HOH A   190              1.49            
REMARK 500   OD2  ASP A    49     O    HOH A   208              1.53            
REMARK 500   CB   THR A    70     O    HOH A   194              1.54            
REMARK 500   NE   ARG A   101     O    HOH A   232              1.56            
REMARK 500   OE1  GLU A    35     O    HOH A   161              1.61            
REMARK 500   CG1  VAL A    74     O    HOH A   146              1.62            
REMARK 500   CD   GLU A    35     O    HOH A   161              1.65            
REMARK 500   O    ALA A   108     O    HOH A   199              1.66            
REMARK 500   N    GLY A    68     O    HOH A   145              1.67            
REMARK 500   CG2  ILE A    89     O    HOH A   297              1.67            
REMARK 500   NH1  ARG A    50     O    HOH A   288              1.68            
REMARK 500   CG   ASN A    66     O    HOH A   131              1.68            
REMARK 500   C    ARG A    21     O    HOH A   228              1.70            
REMARK 500   CE2  TRP A    34     O    HOH A   239              1.71            
REMARK 500   N    GLY A    22     O    HOH A   228              1.72            
REMARK 500   O    TRP A    34     O    HOH A   182              1.73            
REMARK 500   C    THR A    70     O    HOH A   140              1.74            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     100 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CG   ARG A   107     O    HOH A   196     4557     0.50            
REMARK 500   O    GLN A   117     O    HOH A   249     2554     0.75            
REMARK 500   CB   ALA A    73    NA     NA A   601     1556     0.80            
REMARK 500   CB   ALA A    47     O    HOH A   221     2555     0.91            
REMARK 500   NH1  ARG A    41     O    HOH A   264     4456     0.99            
REMARK 500   CD   ARG A   107     O    HOH A   196     4557     1.06            
REMARK 500   CA   ALA A    47     O    HOH A   221     2555     1.10            
REMARK 500   CD   ARG A    41     O    HOH A   262     4457     1.12            
REMARK 500   O    HOH A   191     O    HOH A   244     3556     1.15            
REMARK 500   NE   ARG A    41     O    HOH A   262     4457     1.30            
REMARK 500   O    GLY A    48     O    ASN A   114     2555     1.34            
REMARK 500   NH2  ARG A    21     NE   ARG A    41     4557     1.36            
REMARK 500   CE1  TYR A    45     O    HOH A   202     2555     1.41            
REMARK 500   O    ALA A    47     NH1  ARG A   119     2555     1.47            
REMARK 500   CZ   ARG A    14     O    HOH A   156     2565     1.48            
REMARK 500   OE1  GLN A    86     NE   ARG A   107     4457     1.54            
REMARK 500   CG   GLN A   117     O    HOH A   212     2554     1.54            
REMARK 500   C    GLN A   117     O    HOH A   249     2554     1.60            
REMARK 500   NH1  ARG A   122     O    HOH A   143     4557     1.62            
REMARK 500   CG   ARG A    41     O    HOH A   262     4457     1.62            
REMARK 500   C    ALA A    47     O    HOH A   221     2555     1.63            
REMARK 500   NE   ARG A    14     O    HOH A   156     2565     1.67            
REMARK 500   NH2  ARG A    21     CZ   ARG A    41     4557     1.72            
REMARK 500   OD1  ASN A   118     O    HOH A   290     4557     1.76            
REMARK 500   ND2  ASN A    39     O    HOH A   292     4456     1.78            
REMARK 500   CB   ARG A    41     O    HOH A   262     4457     1.80            
REMARK 500   CB   GLN A   117     O    HOH A   212     2554     1.82            
REMARK 500   CB   ARG A   107     O    HOH A   196     4557     1.85            
REMARK 500   O    ARG A    21     CD1  LEU A    85     4557     1.85            
REMARK 500   CZ   ARG A    21     NH2  ARG A    41     4557     1.86            
REMARK 500   NH2  ARG A   101     O    HOH A   286     1556     1.90            
REMARK 500   NE   ARG A    21     NH2  ARG A    41     4557     1.93            
REMARK 500   NE2  GLN A    86     NH1  ARG A   107     4457     1.94            
REMARK 500   OG1  THR A    43     O    HOH A   158     4457     1.95            
REMARK 500   O    GLY A    48     C    ASN A   114     2555     2.01            
REMARK 500   NE   ARG A   107     O    HOH A   196     4557     2.01            
REMARK 500   CZ   ARG A    21     NE   ARG A    41     4557     2.06            
REMARK 500   CD   GLN A    86     CZ   ARG A   107     4457     2.06            
REMARK 500   CZ   ARG A    21     CZ   ARG A    41     4557     2.07            
REMARK 500   CD   GLN A   117     O    HOH A   212     2554     2.11            
REMARK 500   NH1  ARG A    14     O    HOH A   156     2565     2.12            
REMARK 500   CD   ARG A    41     O    HOH A   251     4456     2.14            
REMARK 500   NH2  ARG A    41     O    HOH A   229     4457     2.14            
REMARK 500   NH2  ARG A    14     O    HOH A   156     2565     2.15            
REMARK 500   CB   SER A    24     O    HOH A   145     4557     2.16            
REMARK 500   OE1  GLN A    86     CZ   ARG A   107     4457     2.17            
REMARK 500   CG2  VAL A   121     O    HOH A   151     4557     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  1B7M A    1   130  UNP    P61626   LYSC_HUMAN      19    148             
SEQADV 1B7M MET A   96  UNP  P61626    ALA   114 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 VAL ASN ALA CYS HIS          
SEQRES   7 A  130  LEU SER CYS SER ALA LEU LEU GLN ASP ASN ILE ALA ASP          
SEQRES   8 A  130  ALA VAL ALA CYS MET 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 CYS A   81  LEU A   85  5                                   5    
HELIX    5   5 ALA A   90  ARG A  101  1                                  12    
HELIX    6   6 GLY A  105  ALA A  108  5                                   4    
HELIX    7   7 VAL A  110  ARG A  115  1                                   6    
HELIX    8   8 ARG A  122  TYR A  124  5                                   3    
SHEET    1   A 2 THR A  43  ASN A  46  0                                        
SHEET    2   A 2 SER A  51  TYR A  54 -1  N  ASP A  53   O  ASN A  44           
SSBOND   1 CYS A    6    CYS A  128                          1555   1555  2.03  
SSBOND   2 CYS A   30    CYS A  116                          1555   1555  2.03  
SSBOND   3 CYS A   65    CYS A   81                          1555   1555  2.04  
SSBOND   4 CYS A   77    CYS A   95                          1555   1555  2.03  
LINK         O   HOH A 194                NA    NA A 601     1554   1555  2.42  
SITE     1 AC1  5 SER A  61  ARG A  62  THR A  70  ALA A  73                    
SITE     2 AC1  5 HOH A 194                                                     
CRYST1   56.860   62.770   32.490  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      0.017587  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015931  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.030779        0.00000                         
ATOM      1  N   LYS A   1       1.058  19.256  22.931  1.00  6.07           N  
ATOM      2  CA  LYS A   1       1.661  20.269  22.025  1.00  6.66           C  
ATOM      3  C   LYS A   1       2.896  19.669  21.373  1.00  5.66           C  
ATOM      4  O   LYS A   1       3.629  18.929  22.020  1.00  6.56           O  
ATOM      5  CB  LYS A   1       2.054  21.527  22.818  1.00  7.25           C  
ATOM      6  CG  LYS A   1       3.035  22.449  22.092  1.00  9.19           C  
ATOM      7  CD  LYS A   1       3.229  23.782  22.797  1.00  5.08           C  
ATOM      8  CE  LYS A   1       4.171  24.640  21.995  1.00  7.13           C  
ATOM      9  NZ  LYS A   1       4.589  25.834  22.774  1.00 14.18           N  
ATOM     10  N   VAL A   2       3.081  19.913  20.081  1.00  4.46           N  
ATOM     11  CA  VAL A   2       4.273  19.421  19.409  1.00  7.81           C  
ATOM     12  C   VAL A   2       5.076  20.667  19.065  1.00  7.46           C  
ATOM     13  O   VAL A   2       4.604  21.519  18.308  1.00  9.66           O  
ATOM     14  CB  VAL A   2       3.967  18.608  18.132  1.00  6.78           C  
ATOM     15  CG1 VAL A   2       5.274  18.199  17.457  1.00  7.88           C  
ATOM     16  CG2 VAL A   2       3.151  17.361  18.479  1.00 10.01           C  
ATOM     17  N   PHE A   3       6.243  20.811  19.691  1.00  5.02           N  
ATOM     18  CA  PHE A   3       7.110  21.970  19.473  1.00  6.98           C  
ATOM     19  C   PHE A   3       7.868  21.971  18.156  1.00  8.79           C  
ATOM     20  O   PHE A   3       8.257  20.928  17.640  1.00 10.14           O  
ATOM     21  CB  PHE A   3       8.179  22.063  20.568  1.00  4.70           C  
ATOM     22  CG  PHE A   3       7.707  22.673  21.845  1.00  3.48           C  
ATOM     23  CD1 PHE A   3       8.084  23.966  22.185  1.00  2.00           C  
ATOM     24  CD2 PHE A   3       6.919  21.947  22.730  1.00  4.41           C  
ATOM     25  CE1 PHE A   3       7.685  24.532  23.396  1.00  4.05           C  
ATOM     26  CE2 PHE A   3       6.517  22.506  23.939  1.00  6.74           C  
ATOM     27  CZ  PHE A   3       6.900  23.798  24.270  1.00  4.03           C  
ATOM     28  N   GLU A   4       8.104  23.164  17.636  1.00 10.57           N  
ATOM     29  CA  GLU A   4       8.910  23.307  16.445  1.00  9.65           C  
ATOM     30  C   GLU A   4      10.286  23.284  17.101  1.00  9.86           C  
ATOM     31  O   GLU A   4      10.415  23.694  18.256  1.00 10.12           O  
ATOM     32  CB  GLU A   4       8.661  24.667  15.803  1.00 12.18           C  
ATOM     33  CG  GLU A   4       7.270  24.834  15.226  1.00 21.87           C  
ATOM     34  CD  GLU A   4       7.276  24.931  13.712  1.00 28.59           C  
ATOM     35  OE1 GLU A   4       7.231  23.869  13.043  1.00 29.33           O  
ATOM     36  OE2 GLU A   4       7.335  26.075  13.196  1.00 32.72           O  
ATOM     37  N   ARG A   5      11.293  22.803  16.387  1.00  7.91           N  
ATOM     38  CA  ARG A   5      12.657  22.709  16.895  1.00  7.60           C  
ATOM     39  C   ARG A   5      13.195  23.973  17.581  1.00 10.99           C  
ATOM     40  O   ARG A   5      13.587  23.939  18.747  1.00 11.22           O  
ATOM     41  CB  ARG A   5      13.596  22.306  15.759  1.00  6.23           C  
ATOM     42  CG  ARG A   5      15.068  22.211  16.171  1.00  7.78           C  
ATOM     43  CD  ARG A   5      15.945  21.736  15.010  1.00  8.53           C  
ATOM     44  NE  ARG A   5      16.072  22.708  13.920  1.00  7.69           N  
ATOM     45  CZ  ARG A   5      17.024  23.639  13.852  1.00  7.39           C  
ATOM     46  NH1 ARG A   5      17.072  24.462  12.823  1.00 11.46           N  
ATOM     47  NH2 ARG A   5      17.907  23.783  14.826  1.00  7.21           N  
ATOM     48  N   CYS A   6      13.221  25.094  16.867  1.00 10.38           N  
ATOM     49  CA  CYS A   6      13.734  26.311  17.467  1.00  9.23           C  
ATOM     50  C   CYS A   6      12.850  26.902  18.551  1.00  8.40           C  
ATOM     51  O   CYS A   6      13.345  27.606  19.438  1.00  8.81           O  
ATOM     52  CB  CYS A   6      14.076  27.339  16.397  1.00  8.07           C  
ATOM     53  SG  CYS A   6      15.535  26.841  15.427  1.00 10.00           S  
ATOM     54  N   GLU A   7      11.551  26.618  18.489  1.00  9.07           N  
ATOM     55  CA  GLU A   7      10.611  27.104  19.501  1.00  7.89           C  
ATOM     56  C   GLU A   7      11.021  26.450  20.817  1.00  6.40           C  
ATOM     57  O   GLU A   7      11.127  27.110  21.853  1.00  5.62           O  
ATOM     58  CB  GLU A   7       9.177  26.702  19.160  1.00  7.53           C  
ATOM     59  CG  GLU A   7       8.147  27.240  20.150  1.00 13.75           C  
ATOM     60  CD  GLU A   7       6.764  26.623  19.991  1.00 18.24           C  
ATOM     61  OE1 GLU A   7       6.576  25.724  19.136  1.00 17.27           O  
ATOM     62  OE2 GLU A   7       5.858  27.045  20.743  1.00 19.47           O  
ATOM     63  N   LEU A   8      11.309  25.154  20.737  1.00  4.60           N  
ATOM     64  CA  LEU A   8      11.732  24.377  21.885  1.00  3.35           C  
ATOM     65  C   LEU A   8      13.094  24.833  22.406  1.00  3.66           C  
ATOM     66  O   LEU A   8      13.296  24.924  23.621  1.00  2.33           O  
ATOM     67  CB  LEU A   8      11.784  22.886  21.524  1.00  2.18           C  
ATOM     68  CG  LEU A   8      12.097  21.991  22.723  1.00  2.00           C  
ATOM     69  CD1 LEU A   8      11.092  22.263  23.842  1.00  4.69           C  
ATOM     70  CD2 LEU A   8      12.062  20.543  22.333  1.00  2.00           C  
ATOM     71  N   ALA A   9      14.018  25.121  21.495  1.00  2.00           N  
ATOM     72  CA  ALA A   9      15.352  25.551  21.878  1.00  2.69           C  
ATOM     73  C   ALA A   9      15.329  26.810  22.700  1.00  4.85           C  
ATOM     74  O   ALA A   9      16.084  26.922  23.670  1.00 10.04           O  
ATOM     75  CB  ALA A   9      16.233  25.756  20.649  1.00  5.46           C  
ATOM     76  N   ARG A  10      14.517  27.785  22.301  1.00  3.20           N  
ATOM     77  CA  ARG A  10      14.427  29.046  23.047  1.00  2.49           C  
ATOM     78  C   ARG A  10      13.688  28.860  24.377  1.00  2.88           C  
ATOM     79  O   ARG A  10      14.064  29.445  25.397  1.00  2.44           O  
ATOM     80  CB  ARG A  10      13.766  30.131  22.197  1.00  2.00           C  
ATOM     81  CG  ARG A  10      14.677  30.672  21.099  1.00  2.00           C  
ATOM     82  CD  ARG A  10      14.043  31.830  20.375  1.00  3.54           C  
ATOM     83  NE  ARG A  10      12.895  31.419  19.571  1.00  3.10           N  
ATOM     84  CZ  ARG A  10      12.994  30.892  18.357  1.00  2.00           C  
ATOM     85  NH1 ARG A  10      11.903  30.557  17.702  1.00  2.25           N  
ATOM     86  NH2 ARG A  10      14.186  30.692  17.806  1.00  2.00           N  
ATOM     87  N   THR A  11      12.665  28.009  24.353  1.00  3.94           N  
ATOM     88  CA  THR A  11      11.867  27.672  25.530  1.00  5.13           C  
ATOM     89  C   THR A  11      12.769  27.043  26.594  1.00  4.09           C  
ATOM     90  O   THR A  11      12.726  27.450  27.743  1.00  7.76           O  
ATOM     91  CB  THR A  11      10.740  26.673  25.160  1.00  4.73           C  
ATOM     92  OG1 THR A  11       9.828  27.297  24.251  1.00  5.16           O  
ATOM     93  CG2 THR A  11       9.984  26.229  26.374  1.00  4.87           C  
ATOM     94  N   LEU A  12      13.612  26.090  26.201  1.00  2.00           N  
ATOM     95  CA  LEU A  12      14.507  25.418  27.138  1.00  2.41           C  
ATOM     96  C   LEU A  12      15.591  26.337  27.679  1.00  5.22           C  
ATOM     97  O   LEU A  12      15.980  26.234  28.844  1.00  5.37           O  
ATOM     98  CB  LEU A  12      15.163  24.195  26.490  1.00  2.04           C  
ATOM     99  CG  LEU A  12      14.303  22.950  26.277  1.00  2.29           C  
ATOM    100  CD1 LEU A  12      15.121  21.931  25.526  1.00  2.00           C  
ATOM    101  CD2 LEU A  12      13.812  22.385  27.607  1.00  2.00           C  
ATOM    102  N   LYS A  13      16.080  27.242  26.837  1.00  5.55           N  
ATOM    103  CA  LYS A  13      17.110  28.163  27.264  1.00  4.76           C  
ATOM    104  C   LYS A  13      16.554  29.145  28.289  1.00  5.81           C  
ATOM    105  O   LYS A  13      17.218  29.457  29.289  1.00  6.80           O  
ATOM    106  CB  LYS A  13      17.686  28.915  26.078  1.00  5.22           C  
ATOM    107  CG  LYS A  13      18.901  29.720  26.441  1.00 10.73           C  
ATOM    108  CD  LYS A  13      19.478  30.417  25.236  1.00 16.79           C  
ATOM    109  CE  LYS A  13      20.699  31.213  25.622  1.00 21.72           C  
ATOM    110  NZ  LYS A  13      20.354  32.270  26.616  1.00 27.50           N  
ATOM    111  N   ARG A  14      15.334  29.622  28.045  1.00  6.92           N  
ATOM    112  CA  ARG A  14      14.678  30.552  28.956  1.00  6.11           C  
ATOM    113  C   ARG A  14      14.417  29.921  30.318  1.00  6.87           C  
ATOM    114  O   ARG A  14      14.258  30.621  31.321  1.00  5.85           O  
ATOM    115  CB  ARG A  14      13.369  31.041  28.366  1.00  4.55           C  
ATOM    116  CG  ARG A  14      13.532  32.104  27.328  1.00  7.51           C  
ATOM    117  CD  ARG A  14      12.193  32.697  26.967  1.00 12.43           C  
ATOM    118  NE  ARG A  14      11.228  31.652  26.655  1.00 19.67           N  
ATOM    119  CZ  ARG A  14      10.733  31.415  25.444  1.00 24.93           C  
ATOM    120  NH1 ARG A  14       9.859  30.424  25.278  1.00 23.03           N  
ATOM    121  NH2 ARG A  14      11.094  32.170  24.401  1.00 26.95           N  
ATOM    122  N   LEU A  15      14.382  28.593  30.349  1.00  6.37           N  
ATOM    123  CA  LEU A  15      14.150  27.862  31.581  1.00  4.93           C  
ATOM    124  C   LEU A  15      15.447  27.501  32.296  1.00  3.60           C  
ATOM    125  O   LEU A  15      15.417  26.801  33.308  1.00  5.35           O  
ATOM    126  CB  LEU A  15      13.288  26.618  31.308  1.00  3.29           C  
ATOM    127  CG  LEU A  15      11.819  26.967  30.979  1.00  5.12           C  
ATOM    128  CD1 LEU A  15      11.016  25.734  30.693  1.00  2.00           C  
ATOM    129  CD2 LEU A  15      11.169  27.724  32.135  1.00  3.17           C  
ATOM    130  N   GLY A  16      16.574  27.989  31.779  1.00  2.00           N  
ATOM    131  CA  GLY A  16      17.883  27.713  32.369  1.00  4.61           C  
ATOM    132  C   GLY A  16      18.515  26.327  32.142  1.00  3.47           C  
ATOM    133  O   GLY A  16      19.312  25.858  32.959  1.00  5.61           O  
ATOM    134  N   MET A  17      18.190  25.686  31.026  1.00  2.68           N  
ATOM    135  CA  MET A  17      18.727  24.363  30.701  1.00  2.00           C  
ATOM    136  C   MET A  17      20.066  24.389  29.965  1.00  3.30           C  
ATOM    137  O   MET A  17      20.759  23.361  29.890  1.00  2.34           O  
ATOM    138  CB  MET A  17      17.722  23.593  29.853  1.00  2.00           C  
ATOM    139  CG  MET A  17      16.481  23.207  30.602  1.00  5.49           C  
ATOM    140  SD  MET A  17      16.875  21.992  31.846  1.00  8.75           S  
ATOM    141  CE  MET A  17      16.332  20.536  31.020  1.00  4.78           C  
ATOM    142  N   ASP A  18      20.412  25.544  29.393  1.00  4.25           N  
ATOM    143  CA  ASP A  18      21.661  25.669  28.654  1.00  5.58           C  
ATOM    144  C   ASP A  18      22.874  25.547  29.576  1.00  5.15           C  
ATOM    145  O   ASP A  18      23.242  26.501  30.261  1.00  2.88           O  
ATOM    146  CB  ASP A  18      21.705  27.002  27.886  1.00  8.71           C  
ATOM    147  CG  ASP A  18      22.938  27.125  26.995  1.00 12.21           C  
ATOM    148  OD1 ASP A  18      23.579  26.093  26.666  1.00 12.80           O  
ATOM    149  OD2 ASP A  18      23.273  28.264  26.623  1.00 17.93           O  
ATOM    150  N   GLY A  19      23.485  24.361  29.591  1.00  7.50           N  
ATOM    151  CA  GLY A  19      24.652  24.138  30.426  1.00  4.41           C  
ATOM    152  C   GLY A  19      24.322  23.639  31.820  1.00  6.03           C  
ATOM    153  O   GLY A  19      25.221  23.521  32.664  1.00  2.00           O  
ATOM    154  N   TYR A  20      23.058  23.269  32.044  1.00  4.35           N  
ATOM    155  CA  TYR A  20      22.635  22.793  33.350  1.00  4.76           C  
ATOM    156  C   TYR A  20      23.375  21.501  33.733  1.00  6.11           C  
ATOM    157  O   TYR A  20      23.165  20.451  33.130  1.00  2.86           O  
ATOM    158  CB  TYR A  20      21.129  22.585  33.375  1.00  4.30           C  
ATOM    159  CG  TYR A  20      20.639  22.291  34.759  1.00  7.13           C  
ATOM    160  CD1 TYR A  20      20.351  23.330  35.644  1.00  8.24           C  
ATOM    161  CD2 TYR A  20      20.540  20.976  35.221  1.00  5.36           C  
ATOM    162  CE1 TYR A  20      19.987  23.069  36.960  1.00  9.66           C  
ATOM    163  CE2 TYR A  20      20.176  20.702  36.543  1.00  9.78           C  
ATOM    164  CZ  TYR A  20      19.902  21.757  37.405  1.00  8.40           C  
ATOM    165  OH  TYR A  20      19.545  21.508  38.703  1.00 12.86           O  
ATOM    166  N   ARG A  21      24.227  21.596  34.756  1.00  7.00           N  
ATOM    167  CA  ARG A  21      25.044  20.472  35.235  1.00  9.38           C  
ATOM    168  C   ARG A  21      25.965  19.940  34.117  1.00  9.02           C  
ATOM    169  O   ARG A  21      26.284  18.742  34.042  1.00  5.54           O  
ATOM    170  CB  ARG A  21      24.173  19.376  35.850  1.00 10.74           C  
ATOM    171  CG  ARG A  21      23.393  19.841  37.075  1.00 15.84           C  
ATOM    172  CD  ARG A  21      24.115  19.562  38.377  1.00 20.55           C  
ATOM    173  NE  ARG A  21      24.207  18.118  38.625  1.00 28.86           N  
ATOM    174  CZ  ARG A  21      25.152  17.539  39.365  1.00 29.16           C  
ATOM    175  NH1 ARG A  21      25.160  16.222  39.525  1.00 28.50           N  
ATOM    176  NH2 ARG A  21      26.091  18.277  39.947  1.00 31.94           N  
ATOM    177  N   GLY A  22      26.431  20.880  33.292  1.00  9.94           N  
ATOM    178  CA  GLY A  22      27.321  20.582  32.181  1.00  9.42           C  
ATOM    179  C   GLY A  22      26.653  20.107  30.899  1.00  8.61           C  
ATOM    180  O   GLY A  22      27.351  19.748  29.944  1.00 11.12           O  
ATOM    181  N   ILE A  23      25.321  20.091  30.866  1.00  6.47           N  
ATOM    182  CA  ILE A  23      24.588  19.633  29.691  1.00  4.04           C  
ATOM    183  C   ILE A  23      24.140  20.784  28.784  1.00  4.96           C  
ATOM    184  O   ILE A  23      23.259  21.595  29.132  1.00  4.05           O  
ATOM    185  CB  ILE A  23      23.373  18.748  30.084  1.00  4.18           C  
ATOM    186  CG1 ILE A  23      23.840  17.566  30.928  1.00  3.98           C  
ATOM    187  CG2 ILE A  23      22.712  18.140  28.840  1.00  2.00           C  
ATOM    188  CD1 ILE A  23      22.734  16.946  31.769  1.00  3.93           C  
ATOM    189  N   SER A  24      24.774  20.861  27.620  1.00  4.53           N  
ATOM    190  CA  SER A  24      24.453  21.898  26.649  1.00  6.20           C  
ATOM    191  C   SER A  24      22.990  21.792  26.239  1.00  6.87           C  
ATOM    192  O   SER A  24      22.377  20.716  26.331  1.00  8.14           O  
ATOM    193  CB  SER A  24      25.325  21.747  25.406  1.00  3.32           C  
ATOM    194  OG  SER A  24      25.023  20.520  24.773  1.00  4.04           O  
ATOM    195  N   LEU A  25      22.468  22.895  25.714  1.00  5.94           N  
ATOM    196  CA  LEU A  25      21.084  22.981  25.261  1.00  4.81           C  
ATOM    197  C   LEU A  25      20.855  21.944  24.160  1.00  5.95           C  
ATOM    198  O   LEU A  25      19.814  21.280  24.127  1.00 10.62           O  
ATOM    199  CB  LEU A  25      20.812  24.388  24.721  1.00  4.64           C  
ATOM    200  CG  LEU A  25      19.365  24.851  24.603  1.00  6.83           C  
ATOM    201  CD1 LEU A  25      18.764  24.909  25.986  1.00  5.98           C  
ATOM    202  CD2 LEU A  25      19.323  26.234  23.940  1.00  5.71           C  
ATOM    203  N   ALA A  26      21.855  21.793  23.289  1.00  6.17           N  
ATOM    204  CA  ALA A  26      21.833  20.851  22.172  1.00  2.80           C  
ATOM    205  C   ALA A  26      21.594  19.403  22.612  1.00  4.11           C  
ATOM    206  O   ALA A  26      20.883  18.657  21.933  1.00  6.76           O  
ATOM    207  CB  ALA A  26      23.122  20.965  21.391  1.00  4.66           C  
ATOM    208  N   ASN A  27      22.176  18.997  23.739  1.00  3.17           N  
ATOM    209  CA  ASN A  27      21.969  17.632  24.253  1.00  3.09           C  
ATOM    210  C   ASN A  27      20.525  17.418  24.697  1.00  2.00           C  
ATOM    211  O   ASN A  27      19.956  16.357  24.475  1.00  2.00           O  
ATOM    212  CB  ASN A  27      22.904  17.334  25.423  1.00  2.00           C  
ATOM    213  CG  ASN A  27      24.256  16.850  24.973  1.00  4.94           C  
ATOM    214  OD1 ASN A  27      24.384  15.758  24.422  1.00  9.53           O  
ATOM    215  ND2 ASN A  27      25.281  17.656  25.201  1.00  6.65           N  
ATOM    216  N   TRP A  28      19.946  18.428  25.336  1.00  2.00           N  
ATOM    217  CA  TRP A  28      18.556  18.367  25.793  1.00  3.55           C  
ATOM    218  C   TRP A  28      17.622  18.283  24.578  1.00  3.46           C  
ATOM    219  O   TRP A  28      16.641  17.537  24.606  1.00  2.00           O  
ATOM    220  CB  TRP A  28      18.183  19.609  26.627  1.00  2.68           C  
ATOM    221  CG  TRP A  28      18.930  19.802  27.921  1.00  2.00           C  
ATOM    222  CD1 TRP A  28      19.744  20.842  28.231  1.00  4.28           C  
ATOM    223  CD2 TRP A  28      18.831  19.002  29.110  1.00  3.32           C  
ATOM    224  NE1 TRP A  28      20.149  20.762  29.543  1.00  5.94           N  
ATOM    225  CE2 TRP A  28      19.601  19.641  30.108  1.00  3.69           C  
ATOM    226  CE3 TRP A  28      18.150  17.814  29.437  1.00  4.86           C  
ATOM    227  CZ2 TRP A  28      19.712  19.140  31.413  1.00  2.00           C  
ATOM    228  CZ3 TRP A  28      18.257  17.315  30.731  1.00  2.00           C  
ATOM    229  CH2 TRP A  28      19.033  17.983  31.704  1.00  6.32           C  
ATOM    230  N   MET A  29      17.912  19.069  23.535  1.00  2.00           N  
ATOM    231  CA  MET A  29      17.103  19.055  22.302  1.00  5.23           C  
ATOM    232  C   MET A  29      17.115  17.650  21.671  1.00  5.50           C  
ATOM    233  O   MET A  29      16.072  17.122  21.255  1.00  4.21           O  
ATOM    234  CB  MET A  29      17.645  20.060  21.259  1.00  3.18           C  
ATOM    235  CG  MET A  29      17.411  21.531  21.552  1.00  2.00           C  
ATOM    236  SD  MET A  29      15.671  21.888  21.685  1.00  3.01           S  
ATOM    237  CE  MET A  29      15.149  21.647  20.051  1.00  4.30           C  
ATOM    238  N   CYS A  30      18.310  17.071  21.595  1.00  4.71           N  
ATOM    239  CA  CYS A  30      18.516  15.749  21.020  1.00  7.18           C  
ATOM    240  C   CYS A  30      17.763  14.711  21.826  1.00  5.69           C  
ATOM    241  O   CYS A  30      17.172  13.788  21.258  1.00  7.89           O  
ATOM    242  CB  CYS A  30      20.019  15.410  20.970  1.00  7.80           C  
ATOM    243  SG  CYS A  30      20.455  13.848  20.121  1.00 10.96           S  
ATOM    244  N   LEU A  31      17.779  14.852  23.146  1.00  3.31           N  
ATOM    245  CA  LEU A  31      17.061  13.905  24.000  1.00  4.33           C  
ATOM    246  C   LEU A  31      15.541  14.000  23.784  1.00  5.49           C  
ATOM    247  O   LEU A  31      14.884  12.979  23.615  1.00  4.78           O  
ATOM    248  CB  LEU A  31      17.387  14.140  25.479  1.00  4.48           C  
ATOM    249  CG  LEU A  31      16.737  13.187  26.480  1.00  3.34           C  
ATOM    250  CD1 LEU A  31      17.380  11.808  26.343  1.00  7.16           C  
ATOM    251  CD2 LEU A  31      16.945  13.711  27.880  1.00  7.40           C  
ATOM    252  N   ALA A  32      14.990  15.220  23.770  1.00  5.91           N  
ATOM    253  CA  ALA A  32      13.547  15.415  23.578  1.00  6.48           C  
ATOM    254  C   ALA A  32      13.094  14.920  22.210  1.00  5.28           C  
ATOM    255  O   ALA A  32      12.022  14.325  22.064  1.00  8.42           O  
ATOM    256  CB  ALA A  32      13.155  16.887  23.775  1.00  4.00           C  
ATOM    257  N   LYS A  33      13.922  15.153  21.207  1.00  6.66           N  
ATOM    258  CA  LYS A  33      13.623  14.718  19.856  1.00  7.56           C  
ATOM    259  C   LYS A  33      13.533  13.184  19.815  1.00  4.68           C  
ATOM    260  O   LYS A  33      12.545  12.625  19.332  1.00  2.00           O  
ATOM    261  CB  LYS A  33      14.700  15.256  18.897  1.00 10.26           C  
ATOM    262  CG  LYS A  33      14.890  14.487  17.597  1.00 17.83           C  
ATOM    263  CD  LYS A  33      13.717  14.612  16.641  1.00 21.27           C  
ATOM    264  CE  LYS A  33      13.848  13.561  15.546  1.00 24.61           C  
ATOM    265  NZ  LYS A  33      13.950  12.166  16.106  1.00 27.58           N  
ATOM    266  N   TRP A  34      14.520  12.501  20.375  1.00  3.47           N  
ATOM    267  CA  TRP A  34      14.473  11.055  20.334  1.00  4.74           C  
ATOM    268  C   TRP A  34      13.508  10.459  21.303  1.00  4.87           C  
ATOM    269  O   TRP A  34      12.935   9.404  21.041  1.00  8.06           O  
ATOM    270  CB  TRP A  34      15.866  10.461  20.456  1.00  6.08           C  
ATOM    271  CG  TRP A  34      16.588  10.722  19.197  1.00 11.54           C  
ATOM    272  CD1 TRP A  34      17.511  11.702  18.963  1.00 10.08           C  
ATOM    273  CD2 TRP A  34      16.357  10.076  17.938  1.00 11.77           C  
ATOM    274  NE1 TRP A  34      17.856  11.714  17.635  1.00 12.01           N  
ATOM    275  CE2 TRP A  34      17.167  10.721  16.984  1.00 11.24           C  
ATOM    276  CE3 TRP A  34      15.539   9.014  17.526  1.00  8.99           C  
ATOM    277  CZ2 TRP A  34      17.190  10.341  15.641  1.00 11.22           C  
ATOM    278  CZ3 TRP A  34      15.558   8.639  16.197  1.00 11.38           C  
ATOM    279  CH2 TRP A  34      16.382   9.301  15.269  1.00 12.47           C  
ATOM    280  N   GLU A  35      13.267  11.159  22.402  1.00  6.96           N  
ATOM    281  CA  GLU A  35      12.312  10.665  23.388  1.00  8.34           C  
ATOM    282  C   GLU A  35      10.856  10.759  22.932  1.00  7.06           C  
ATOM    283  O   GLU A  35      10.136   9.767  22.951  1.00  7.68           O  
ATOM    284  CB  GLU A  35      12.477  11.392  24.740  1.00  7.83           C  
ATOM    285  CG  GLU A  35      13.692  10.946  25.566  1.00  6.05           C  
ATOM    286  CD  GLU A  35      13.781   9.418  25.786  1.00  9.78           C  
ATOM    287  OE1 GLU A  35      12.739   8.733  25.820  1.00  6.48           O  
ATOM    288  OE2 GLU A  35      14.908   8.895  25.929  1.00 12.40           O  
ATOM    289  N   SER A  36      10.444  11.935  22.460  1.00  8.57           N  
ATOM    290  CA  SER A  36       9.044  12.158  22.082  1.00  7.37           C  
ATOM    291  C   SER A  36       8.786  12.792  20.710  1.00  7.17           C  
ATOM    292  O   SER A  36       7.661  12.794  20.223  1.00  4.65           O  
ATOM    293  CB  SER A  36       8.425  13.075  23.129  1.00  4.82           C  
ATOM    294  OG  SER A  36       9.065  14.341  23.063  1.00  2.00           O  
ATOM    295  N   GLY A  37       9.818  13.389  20.130  1.00  9.81           N  
ATOM    296  CA  GLY A  37       9.671  14.046  18.848  1.00  9.63           C  
ATOM    297  C   GLY A  37       9.121  15.430  19.103  1.00  9.13           C  
ATOM    298  O   GLY A  37       8.470  16.009  18.239  1.00 11.68           O  
ATOM    299  N   TYR A  38       9.380  15.952  20.302  1.00  7.09           N  
ATOM    300  CA  TYR A  38       8.918  17.285  20.717  1.00  6.57           C  
ATOM    301  C   TYR A  38       7.423  17.336  21.053  1.00  4.14           C  
ATOM    302  O   TYR A  38       6.827  18.414  21.070  1.00  5.03           O  
ATOM    303  CB  TYR A  38       9.227  18.334  19.645  1.00  5.84           C  
ATOM    304  CG  TYR A  38      10.670  18.384  19.219  1.00  3.91           C  
ATOM    305  CD1 TYR A  38      11.019  18.833  17.948  1.00  2.35           C  
ATOM    306  CD2 TYR A  38      11.691  18.021  20.100  1.00  2.00           C  
ATOM    307  CE1 TYR A  38      12.341  18.926  17.567  1.00  2.00           C  
ATOM    308  CE2 TYR A  38      13.008  18.111  19.735  1.00  2.00           C  
ATOM    309  CZ  TYR A  38      13.333  18.566  18.465  1.00  4.12           C  
ATOM    310  OH  TYR A  38      14.660  18.669  18.104  1.00  7.14           O  
ATOM    311  N   ASN A  39       6.835  16.177  21.352  1.00  5.25           N  
ATOM    312  CA  ASN A  39       5.416  16.077  21.678  1.00  2.18           C  
ATOM    313  C   ASN A  39       5.244  15.925  23.181  1.00  3.96           C  
ATOM    314  O   ASN A  39       5.726  14.955  23.762  1.00  6.47           O  
ATOM    315  CB  ASN A  39       4.808  14.864  20.975  1.00  2.93           C  
ATOM    316  CG  ASN A  39       3.303  14.764  21.163  1.00  3.75           C  
ATOM    317  OD1 ASN A  39       2.688  15.550  21.892  1.00  3.66           O  
ATOM    318  ND2 ASN A  39       2.701  13.809  20.491  1.00  4.04           N  
ATOM    319  N   THR A  40       4.570  16.893  23.798  1.00  4.76           N  
ATOM    320  CA  THR A  40       4.302  16.914  25.237  1.00  5.59           C  
ATOM    321  C   THR A  40       3.260  15.905  25.746  1.00  5.56           C  
ATOM    322  O   THR A  40       3.235  15.595  26.934  1.00  7.11           O  
ATOM    323  CB  THR A  40       3.826  18.307  25.698  1.00  4.79           C  
ATOM    324  OG1 THR A  40       2.625  18.665  24.998  1.00  3.96           O  
ATOM    325  CG2 THR A  40       4.891  19.357  25.443  1.00  6.78           C  
ATOM    326  N   ARG A  41       2.395  15.409  24.869  1.00  8.44           N  
ATOM    327  CA  ARG A  41       1.357  14.473  25.298  1.00 10.09           C  
ATOM    328  C   ARG A  41       1.743  13.018  25.091  1.00  9.04           C  
ATOM    329  O   ARG A  41       0.929  12.106  25.292  1.00  9.80           O  
ATOM    330  CB  ARG A  41       0.035  14.789  24.588  1.00 16.02           C  
ATOM    331  CG  ARG A  41      -0.108  14.206  23.194  1.00 24.87           C  
ATOM    332  CD  ARG A  41      -1.183  13.108  23.158  1.00 33.65           C  
ATOM    333  NE  ARG A  41      -2.450  13.552  23.757  1.00 35.81           N  
ATOM    334  CZ  ARG A  41      -3.544  12.799  23.852  1.00 37.09           C  
ATOM    335  NH1 ARG A  41      -3.540  11.559  23.375  1.00 40.96           N  
ATOM    336  NH2 ARG A  41      -4.624  13.259  24.471  1.00 32.69           N  
ATOM    337  N   ALA A  42       2.996  12.814  24.705  1.00  7.75           N  
ATOM    338  CA  ALA A  42       3.546  11.496  24.452  1.00  7.30           C  
ATOM    339  C   ALA A  42       3.653  10.667  25.739  1.00  8.78           C  
ATOM    340  O   ALA A  42       4.147  11.147  26.760  1.00  9.59           O  
ATOM    341  CB  ALA A  42       4.911  11.636  23.794  1.00  2.00           C  
ATOM    342  N   THR A  43       3.212   9.413  25.683  1.00  8.89           N  
ATOM    343  CA  THR A  43       3.270   8.538  26.847  1.00 10.42           C  
ATOM    344  C   THR A  43       3.630   7.136  26.380  1.00 10.82           C  
ATOM    345  O   THR A  43       3.334   6.772  25.242  1.00 11.75           O  
ATOM    346  CB  THR A  43       1.910   8.474  27.569  1.00  9.56           C  
ATOM    347  OG1 THR A  43       0.952   7.861  26.704  1.00  9.40           O  
ATOM    348  CG2 THR A  43       1.414   9.870  27.933  1.00  8.14           C  
ATOM    349  N   ASN A  44       4.283   6.359  27.242  1.00 13.92           N  
ATOM    350  CA  ASN A  44       4.660   4.995  26.895  1.00 15.75           C  
ATOM    351  C   ASN A  44       4.536   4.022  28.039  1.00 13.15           C  
ATOM    352  O   ASN A  44       5.314   4.062  28.975  1.00 12.22           O  
ATOM    353  CB  ASN A  44       6.075   4.928  26.329  1.00 22.62           C  
ATOM    354  CG  ASN A  44       6.092   4.922  24.809  1.00 33.05           C  
ATOM    355  OD1 ASN A  44       6.827   5.698  24.182  1.00 36.70           O  
ATOM    356  ND2 ASN A  44       5.288   4.041  24.201  1.00 34.74           N  
ATOM    357  N   TYR A  45       3.587   3.105  27.921  1.00 13.06           N  
ATOM    358  CA  TYR A  45       3.353   2.101  28.948  1.00 12.41           C  
ATOM    359  C   TYR A  45       4.365   0.969  28.851  1.00 13.42           C  
ATOM    360  O   TYR A  45       4.610   0.432  27.769  1.00 15.11           O  
ATOM    361  CB  TYR A  45       1.925   1.559  28.829  1.00 10.32           C  
ATOM    362  CG  TYR A  45       1.555   0.549  29.874  1.00  9.54           C  
ATOM    363  CD1 TYR A  45       1.307  -0.772  29.523  1.00 14.76           C  
ATOM    364  CD2 TYR A  45       1.490   0.896  31.217  1.00 10.23           C  
ATOM    365  CE1 TYR A  45       1.011  -1.736  30.493  1.00 12.90           C  
ATOM    366  CE2 TYR A  45       1.192  -0.048  32.188  1.00  7.37           C  
ATOM    367  CZ  TYR A  45       0.960  -1.368  31.823  1.00 12.39           C  
ATOM    368  OH  TYR A  45       0.735  -2.345  32.783  1.00 16.26           O  
ATOM    369  N   ASN A  46       5.007   0.669  29.974  1.00 13.24           N  
ATOM    370  CA  ASN A  46       5.984  -0.413  30.053  1.00 14.22           C  
ATOM    371  C   ASN A  46       5.258  -1.515  30.823  1.00 12.61           C  
ATOM    372  O   ASN A  46       5.012  -1.388  32.016  1.00 11.09           O  
ATOM    373  CB  ASN A  46       7.242   0.040  30.804  1.00 12.24           C  
ATOM    374  CG  ASN A  46       7.845   1.327  30.226  1.00 13.03           C  
ATOM    375  OD1 ASN A  46       8.656   1.290  29.296  1.00 12.56           O  
ATOM    376  ND2 ASN A  46       7.446   2.467  30.775  1.00  9.72           N  
ATOM    377  N   ALA A  47       4.843  -2.552  30.108  1.00 12.49           N  
ATOM    378  CA  ALA A  47       4.107  -3.672  30.686  1.00 13.49           C  
ATOM    379  C   ALA A  47       4.879  -4.476  31.727  1.00 15.56           C  
ATOM    380  O   ALA A  47       4.276  -5.065  32.627  1.00 18.46           O  
ATOM    381  CB  ALA A  47       3.602  -4.597  29.579  1.00 13.57           C  
ATOM    382  N   GLY A  48       6.201  -4.519  31.592  1.00 15.66           N  
ATOM    383  CA  GLY A  48       7.023  -5.249  32.535  1.00 15.75           C  
ATOM    384  C   GLY A  48       6.835  -4.774  33.966  1.00 18.22           C  
ATOM    385  O   GLY A  48       6.261  -5.494  34.786  1.00 16.58           O  
ATOM    386  N   ASP A  49       7.321  -3.566  34.265  1.00 18.04           N  
ATOM    387  CA  ASP A  49       7.199  -2.998  35.607  1.00 16.43           C  
ATOM    388  C   ASP A  49       5.975  -2.105  35.790  1.00 16.11           C  
ATOM    389  O   ASP A  49       5.919  -1.307  36.723  1.00 16.66           O  
ATOM    390  CB  ASP A  49       8.470  -2.240  36.002  1.00 17.29           C  
ATOM    391  CG  ASP A  49       8.581  -0.880  35.337  1.00 15.40           C  
ATOM    392  OD1 ASP A  49       8.008  -0.689  34.253  1.00 17.33           O  
ATOM    393  OD2 ASP A  49       9.255  -0.002  35.906  1.00 13.69           O  
ATOM    394  N   ARG A  50       5.044  -2.193  34.846  1.00 14.50           N  
ATOM    395  CA  ARG A  50       3.804  -1.433  34.886  1.00 16.08           C  
ATOM    396  C   ARG A  50       3.936   0.065  35.130  1.00 14.63           C  
ATOM    397  O   ARG A  50       3.096   0.678  35.799  1.00 13.91           O  
ATOM    398  CB  ARG A  50       2.844  -2.079  35.882  1.00 19.67           C  
ATOM    399  CG  ARG A  50       2.350  -3.417  35.394  1.00 25.37           C  
ATOM    400  CD  ARG A  50       2.021  -4.361  36.526  1.00 33.13           C  
ATOM    401  NE  ARG A  50       1.441  -5.599  36.008  1.00 39.76           N  
ATOM    402  CZ  ARG A  50       1.167  -6.669  36.748  1.00 42.80           C  
ATOM    403  NH1 ARG A  50       0.638  -7.747  36.187  1.00 46.93           N  
ATOM    404  NH2 ARG A  50       1.425  -6.667  38.048  1.00 47.71           N  
ATOM    405  N   SER A  51       4.982   0.653  34.557  1.00 14.65           N  
ATOM    406  CA  SER A  51       5.221   2.085  34.671  1.00 11.81           C  
ATOM    407  C   SER A  51       4.934   2.725  33.308  1.00 11.84           C  
ATOM    408  O   SER A  51       4.767   2.034  32.309  1.00 10.31           O  
ATOM    409  CB  SER A  51       6.660   2.361  35.110  1.00 10.59           C  
ATOM    410  OG  SER A  51       7.584   1.956  34.124  1.00  9.96           O  
ATOM    411  N   THR A  52       4.849   4.043  33.284  1.00 10.77           N  
ATOM    412  CA  THR A  52       4.577   4.774  32.064  1.00 10.81           C  
ATOM    413  C   THR A  52       5.567   5.945  31.963  1.00  9.95           C  
ATOM    414  O   THR A  52       6.001   6.490  32.982  1.00  6.32           O  
ATOM    415  CB  THR A  52       3.116   5.306  32.063  1.00 12.62           C  
ATOM    416  OG1 THR A  52       2.201   4.217  32.258  1.00 14.12           O  
ATOM    417  CG2 THR A  52       2.785   5.996  30.753  1.00 13.66           C  
ATOM    418  N   ASP A  53       6.014   6.236  30.744  1.00  9.11           N  
ATOM    419  CA  ASP A  53       6.926   7.349  30.500  1.00  7.62           C  
ATOM    420  C   ASP A  53       6.018   8.457  29.989  1.00  4.91           C  
ATOM    421  O   ASP A  53       5.208   8.227  29.084  1.00  2.00           O  
ATOM    422  CB  ASP A  53       7.964   6.969  29.446  1.00  7.38           C  
ATOM    423  CG  ASP A  53       8.707   5.700  29.792  1.00 10.38           C  
ATOM    424  OD1 ASP A  53       9.335   5.635  30.869  1.00  6.25           O  
ATOM    425  OD2 ASP A  53       8.645   4.754  28.982  1.00 14.89           O  
ATOM    426  N   TYR A  54       6.154   9.645  30.583  1.00  7.36           N  
ATOM    427  CA  TYR A  54       5.319  10.812  30.261  1.00  2.85           C  
ATOM    428  C   TYR A  54       6.003  12.032  29.661  1.00  3.21           C  
ATOM    429  O   TYR A  54       7.136  12.378  30.027  1.00  2.34           O  
ATOM    430  CB  TYR A  54       4.597  11.292  31.525  1.00  2.97           C  
ATOM    431  CG  TYR A  54       3.597  10.324  32.121  1.00  2.02           C  
ATOM    432  CD1 TYR A  54       2.244  10.436  31.822  1.00  4.45           C  
ATOM    433  CD2 TYR A  54       4.003   9.307  32.999  1.00  3.95           C  
ATOM    434  CE1 TYR A  54       1.312   9.566  32.373  1.00  3.20           C  
ATOM    435  CE2 TYR A  54       3.076   8.431  33.565  1.00  3.15           C  
ATOM    436  CZ  TYR A  54       1.726   8.572  33.240  1.00  3.34           C  
ATOM    437  OH  TYR A  54       0.774   7.740  33.781  1.00  2.83           O  
ATOM    438  N   GLY A  55       5.314  12.657  28.713  1.00  2.00           N  
ATOM    439  CA  GLY A  55       5.793  13.883  28.111  1.00  3.93           C  
ATOM    440  C   GLY A  55       6.953  13.943  27.143  1.00  3.84           C  
ATOM    441  O   GLY A  55       7.510  12.930  26.719  1.00  3.35           O  
ATOM    442  N   ILE A  56       7.338  15.186  26.850  1.00  3.39           N  
ATOM    443  CA  ILE A  56       8.412  15.524  25.913  1.00  4.38           C  
ATOM    444  C   ILE A  56       9.772  14.880  26.210  1.00  2.63           C  
ATOM    445  O   ILE A  56      10.568  14.675  25.298  1.00  2.00           O  
ATOM    446  CB  ILE A  56       8.515  17.095  25.734  1.00  6.67           C  
ATOM    447  CG1 ILE A  56       9.436  17.464  24.569  1.00  4.00           C  
ATOM    448  CG2 ILE A  56       8.963  17.773  27.019  1.00  4.22           C  
ATOM    449  CD1 ILE A  56       9.373  18.933  24.199  1.00  6.14           C  
ATOM    450  N   PHE A  57      10.022  14.546  27.475  1.00  4.57           N  
ATOM    451  CA  PHE A  57      11.276  13.903  27.870  1.00  3.28           C  
ATOM    452  C   PHE A  57      11.078  12.450  28.297  1.00  5.01           C  
ATOM    453  O   PHE A  57      12.040  11.778  28.672  1.00  9.00           O  
ATOM    454  CB  PHE A  57      11.934  14.663  29.021  1.00  3.12           C  
ATOM    455  CG  PHE A  57      12.475  16.018  28.635  1.00  5.27           C  
ATOM    456  CD1 PHE A  57      11.968  17.177  29.225  1.00  3.10           C  
ATOM    457  CD2 PHE A  57      13.497  16.131  27.688  1.00  5.92           C  
ATOM    458  CE1 PHE A  57      12.462  18.427  28.879  1.00  4.94           C  
ATOM    459  CE2 PHE A  57      14.004  17.366  27.331  1.00  8.05           C  
ATOM    460  CZ  PHE A  57      13.486  18.524  27.927  1.00  5.77           C  
ATOM    461  N   GLN A  58       9.830  11.975  28.248  1.00  4.97           N  
ATOM    462  CA  GLN A  58       9.469  10.611  28.641  1.00  4.04           C  
ATOM    463  C   GLN A  58       9.970  10.253  30.043  1.00  3.93           C  
ATOM    464  O   GLN A  58      10.733   9.319  30.231  1.00  2.00           O  
ATOM    465  CB  GLN A  58       9.940   9.596  27.591  1.00  2.00           C  
ATOM    466  CG  GLN A  58       9.205   9.704  26.263  1.00  2.00           C  
ATOM    467  CD  GLN A  58       7.770   9.275  26.368  1.00  2.00           C  
ATOM    468  OE1 GLN A  58       7.466   8.101  26.265  1.00  5.01           O  
ATOM    469  NE2 GLN A  58       6.879  10.214  26.587  1.00  2.00           N  
ATOM    470  N   ILE A  59       9.539  11.025  31.031  1.00  6.73           N  
ATOM    471  CA  ILE A  59       9.938  10.782  32.413  1.00  7.28           C  
ATOM    472  C   ILE A  59       9.098   9.618  32.971  1.00  5.14           C  
ATOM    473  O   ILE A  59       7.864   9.634  32.912  1.00  6.69           O  
ATOM    474  CB  ILE A  59       9.787  12.066  33.273  1.00  5.90           C  
ATOM    475  CG1 ILE A  59      10.732  13.154  32.766  1.00  2.00           C  
ATOM    476  CG2 ILE A  59      10.125  11.772  34.708  1.00  4.42           C  
ATOM    477  CD1 ILE A  59      10.387  14.523  33.272  1.00  4.59           C  
ATOM    478  N   ASN A  60       9.789   8.621  33.510  1.00  3.91           N  
ATOM    479  CA  ASN A  60       9.170   7.409  34.040  1.00  6.34           C  
ATOM    480  C   ASN A  60       8.515   7.527  35.412  1.00  7.27           C  
ATOM    481  O   ASN A  60       9.151   7.933  36.395  1.00  7.98           O  
ATOM    482  CB  ASN A  60      10.202   6.283  34.055  1.00  7.98           C  
ATOM    483  CG  ASN A  60       9.605   4.951  34.464  1.00 11.21           C  
ATOM    484  OD1 ASN A  60       9.634   4.573  35.644  1.00 11.21           O  
ATOM    485  ND2 ASN A  60       9.037   4.240  33.495  1.00  3.76           N  
ATOM    486  N   SER A  61       7.274   7.065  35.497  1.00  7.49           N  
ATOM    487  CA  SER A  61       6.504   7.120  36.738  1.00  7.13           C  
ATOM    488  C   SER A  61       6.958   6.234  37.905  1.00  8.63           C  
ATOM    489  O   SER A  61       6.392   6.328  39.003  1.00  6.14           O  
ATOM    490  CB  SER A  61       5.021   6.881  36.451  1.00  8.14           C  
ATOM    491  OG  SER A  61       4.819   5.618  35.835  1.00 11.17           O  
ATOM    492  N   ARG A  62       7.946   5.360  37.701  1.00  9.02           N  
ATOM    493  CA  ARG A  62       8.395   4.529  38.817  1.00  9.11           C  
ATOM    494  C   ARG A  62       9.202   5.325  39.832  1.00  8.93           C  
ATOM    495  O   ARG A  62       9.178   5.017  41.029  1.00  8.81           O  
ATOM    496  CB  ARG A  62       9.221   3.317  38.366  1.00  9.46           C  
ATOM    497  CG  ARG A  62       9.784   2.522  39.552  1.00 13.05           C  
ATOM    498  CD  ARG A  62      10.093   1.052  39.227  1.00 15.31           C  
ATOM    499  NE  ARG A  62       8.877   0.328  38.864  1.00 18.98           N  
ATOM    500  CZ  ARG A  62       7.935  -0.065  39.718  1.00 12.19           C  
ATOM    501  NH1 ARG A  62       6.860  -0.695  39.270  1.00  3.29           N  
ATOM    502  NH2 ARG A  62       8.091   0.134  41.017  1.00 15.82           N  
ATOM    503  N   TYR A  63       9.855   6.388  39.374  1.00  7.19           N  
ATOM    504  CA  TYR A  63      10.700   7.164  40.264  1.00  7.01           C  
ATOM    505  C   TYR A  63      10.489   8.672  40.290  1.00  7.69           C  
ATOM    506  O   TYR A  63      10.837   9.322  41.268  1.00  8.72           O  
ATOM    507  CB  TYR A  63      12.165   6.938  39.894  1.00  7.48           C  
ATOM    508  CG  TYR A  63      12.539   5.514  39.536  1.00 10.89           C  
ATOM    509  CD1 TYR A  63      12.573   5.094  38.207  1.00  9.82           C  
ATOM    510  CD2 TYR A  63      12.927   4.612  40.520  1.00 11.00           C  
ATOM    511  CE1 TYR A  63      12.989   3.819  37.870  1.00 12.30           C  
ATOM    512  CE2 TYR A  63      13.342   3.328  40.193  1.00 16.89           C  
ATOM    513  CZ  TYR A  63      13.371   2.936  38.867  1.00 16.95           C  
ATOM    514  OH  TYR A  63      13.750   1.643  38.552  1.00 22.25           O  
ATOM    515  N   TRP A  64       9.905   9.237  39.247  1.00  5.03           N  
ATOM    516  CA  TRP A  64       9.797  10.678  39.195  1.00  3.83           C  
ATOM    517  C   TRP A  64       8.466  11.342  39.413  1.00  6.23           C  
ATOM    518  O   TRP A  64       8.412  12.492  39.861  1.00  7.97           O  
ATOM    519  CB  TRP A  64      10.424  11.149  37.893  1.00  2.48           C  
ATOM    520  CG  TRP A  64      11.792  10.555  37.726  1.00  4.81           C  
ATOM    521  CD1 TRP A  64      12.136   9.498  36.933  1.00  4.98           C  
ATOM    522  CD2 TRP A  64      12.971  10.903  38.468  1.00  4.54           C  
ATOM    523  NE1 TRP A  64      13.449   9.151  37.150  1.00 10.20           N  
ATOM    524  CE2 TRP A  64      13.986  10.000  38.087  1.00  9.17           C  
ATOM    525  CE3 TRP A  64      13.264  11.884  39.428  1.00  7.68           C  
ATOM    526  CZ2 TRP A  64      15.278  10.046  38.633  1.00  8.49           C  
ATOM    527  CZ3 TRP A  64      14.544  11.928  39.975  1.00  5.29           C  
ATOM    528  CH2 TRP A  64      15.535  11.012  39.574  1.00  7.13           C  
ATOM    529  N   CYS A  65       7.389  10.643  39.094  1.00  5.67           N  
ATOM    530  CA  CYS A  65       6.087  11.235  39.272  1.00  5.17           C  
ATOM    531  C   CYS A  65       5.091  10.210  39.750  1.00  3.49           C  
ATOM    532  O   CYS A  65       5.323   8.996  39.665  1.00  2.80           O  
ATOM    533  CB  CYS A  65       5.611  11.903  37.968  1.00  5.92           C  
ATOM    534  SG  CYS A  65       5.378  10.801  36.529  1.00  5.97           S  
ATOM    535  N   ASN A  66       4.000  10.698  40.311  1.00  2.00           N  
ATOM    536  CA  ASN A  66       2.973   9.817  40.781  1.00  2.00           C  
ATOM    537  C   ASN A  66       1.808   9.807  39.822  1.00  2.00           C  
ATOM    538  O   ASN A  66       1.320  10.859  39.418  1.00  3.06           O  
ATOM    539  CB  ASN A  66       2.481  10.249  42.161  1.00  2.90           C  
ATOM    540  CG  ASN A  66       1.279   9.440  42.626  1.00  6.09           C  
ATOM    541  OD1 ASN A  66       1.253   8.217  42.479  1.00  4.09           O  
ATOM    542  ND2 ASN A  66       0.255  10.122  43.142  1.00  4.81           N  
ATOM    543  N   ASP A  67       1.394   8.615  39.414  1.00  5.90           N  
ATOM    544  CA  ASP A  67       0.228   8.480  38.559  1.00  5.90           C  
ATOM    545  C   ASP A  67      -0.753   7.550  39.249  1.00  6.81           C  
ATOM    546  O   ASP A  67      -1.805   7.224  38.710  1.00  7.12           O  
ATOM    547  CB  ASP A  67       0.584   8.018  37.136  1.00  7.75           C  
ATOM    548  CG  ASP A  67       1.250   6.657  37.078  1.00  8.40           C  
ATOM    549  OD1 ASP A  67       1.492   6.012  38.115  1.00 11.20           O  
ATOM    550  OD2 ASP A  67       1.545   6.225  35.951  1.00  7.46           O  
ATOM    551  N   GLY A  68      -0.403   7.150  40.468  1.00  6.60           N  
ATOM    552  CA  GLY A  68      -1.247   6.270  41.257  1.00  8.34           C  
ATOM    553  C   GLY A  68      -1.393   4.816  40.822  1.00  8.23           C  
ATOM    554  O   GLY A  68      -1.882   3.989  41.599  1.00  7.65           O  
ATOM    555  N   LYS A  69      -0.956   4.469  39.617  1.00  8.01           N  
ATOM    556  CA  LYS A  69      -1.106   3.083  39.168  1.00  8.24           C  
ATOM    557  C   LYS A  69       0.162   2.261  38.931  1.00  7.88           C  
ATOM    558  O   LYS A  69       0.095   1.189  38.331  1.00  9.38           O  
ATOM    559  CB  LYS A  69      -1.994   3.031  37.920  1.00  8.19           C  
ATOM    560  CG  LYS A  69      -1.558   3.957  36.797  1.00  8.53           C  
ATOM    561  CD  LYS A  69      -2.196   3.529  35.485  1.00 10.69           C  
ATOM    562  CE  LYS A  69      -1.929   4.530  34.387  1.00  7.64           C  
ATOM    563  NZ  LYS A  69      -0.495   4.832  34.313  1.00 16.26           N  
ATOM    564  N   THR A  70       1.314   2.767  39.363  1.00  9.27           N  
ATOM    565  CA  THR A  70       2.584   2.058  39.181  1.00  8.61           C  
ATOM    566  C   THR A  70       2.969   1.467  40.525  1.00  9.09           C  
ATOM    567  O   THR A  70       3.239   2.220  41.471  1.00  7.43           O  
ATOM    568  CB  THR A  70       3.717   3.012  38.759  1.00  5.88           C  
ATOM    569  OG1 THR A  70       3.266   3.871  37.706  1.00  6.18           O  
ATOM    570  CG2 THR A  70       4.929   2.214  38.308  1.00  4.84           C  
ATOM    571  N   PRO A  71       3.026   0.121  40.620  1.00  9.88           N  
ATOM    572  CA  PRO A  71       3.366  -0.655  41.821  1.00  8.95           C  
ATOM    573  C   PRO A  71       4.691  -0.311  42.484  1.00  8.66           C  
ATOM    574  O   PRO A  71       5.762  -0.471  41.888  1.00  5.01           O  
ATOM    575  CB  PRO A  71       3.364  -2.103  41.307  1.00  9.45           C  
ATOM    576  CG  PRO A  71       2.380  -2.078  40.219  1.00  8.96           C  
ATOM    577  CD  PRO A  71       2.735  -0.792  39.500  1.00  9.53           C  
ATOM    578  N   GLY A  72       4.606   0.139  43.735  1.00  9.30           N  
ATOM    579  CA  GLY A  72       5.792   0.483  44.507  1.00  9.01           C  
ATOM    580  C   GLY A  72       6.666   1.625  44.012  1.00  7.01           C  
ATOM    581  O   GLY A  72       7.846   1.708  44.360  1.00  6.75           O  
ATOM    582  N   ALA A  73       6.083   2.526  43.234  1.00  6.97           N  
ATOM    583  CA  ALA A  73       6.802   3.676  42.689  1.00  4.54           C  
ATOM    584  C   ALA A  73       7.003   4.787  43.717  1.00  5.79           C  
ATOM    585  O   ALA A  73       6.397   4.764  44.791  1.00  6.74           O  
ATOM    586  CB  ALA A  73       6.007   4.224  41.533  1.00  3.14           C  
ATOM    587  N   VAL A  74       7.895   5.726  43.402  1.00  7.34           N  
ATOM    588  CA  VAL A  74       8.119   6.913  44.232  1.00  7.81           C  
ATOM    589  C   VAL A  74       7.796   8.136  43.357  1.00  8.71           C  
ATOM    590  O   VAL A  74       7.378   7.983  42.198  1.00  8.59           O  
ATOM    591  CB  VAL A  74       9.536   7.005  44.866  1.00 10.58           C  
ATOM    592  CG1 VAL A  74       9.614   6.060  46.064  1.00 11.03           C  
ATOM    593  CG2 VAL A  74      10.643   6.693  43.845  1.00  7.86           C  
ATOM    594  N   ASN A  75       7.965   9.338  43.894  1.00  8.34           N  
ATOM    595  CA  ASN A  75       7.624  10.572  43.168  1.00  7.66           C  
ATOM    596  C   ASN A  75       8.670  11.623  43.510  1.00  4.72           C  
ATOM    597  O   ASN A  75       8.386  12.619  44.168  1.00  6.71           O  
ATOM    598  CB  ASN A  75       6.212  11.015  43.608  1.00  6.48           C  
ATOM    599  CG  ASN A  75       5.788  12.363  43.035  1.00  5.24           C  
ATOM    600  OD1 ASN A  75       6.518  13.019  42.290  1.00  5.53           O  
ATOM    601  ND2 ASN A  75       4.596  12.786  43.403  1.00  4.23           N  
ATOM    602  N   ALA A  76       9.890  11.384  43.046  1.00  5.80           N  
ATOM    603  CA  ALA A  76      11.012  12.250  43.333  1.00  3.45           C  
ATOM    604  C   ALA A  76      10.902  13.685  42.833  1.00  4.84           C  
ATOM    605  O   ALA A  76      11.536  14.564  43.398  1.00  3.57           O  
ATOM    606  CB  ALA A  76      12.301  11.609  42.874  1.00  5.49           C  
ATOM    607  N   CYS A  77      10.086  13.944  41.812  1.00  6.60           N  
ATOM    608  CA  CYS A  77       9.917  15.325  41.333  1.00  6.36           C  
ATOM    609  C   CYS A  77       8.732  15.984  42.022  1.00  7.06           C  
ATOM    610  O   CYS A  77       8.440  17.158  41.791  1.00  4.85           O  
ATOM    611  CB  CYS A  77       9.706  15.368  39.828  1.00  5.97           C  
ATOM    612  SG  CYS A  77      11.221  15.056  38.884  1.00  4.55           S  
ATOM    613  N   HIS A  78       8.038  15.200  42.846  1.00  9.89           N  
ATOM    614  CA  HIS A  78       6.873  15.656  43.600  1.00 10.30           C  
ATOM    615  C   HIS A  78       5.862  16.330  42.695  1.00 10.45           C  
ATOM    616  O   HIS A  78       5.443  17.471  42.917  1.00 10.82           O  
ATOM    617  CB  HIS A  78       7.314  16.544  44.759  1.00  9.23           C  
ATOM    618  CG  HIS A  78       8.179  15.819  45.738  1.00 12.40           C  
ATOM    619  ND1 HIS A  78       9.555  15.803  45.643  1.00 12.87           N  
ATOM    620  CD2 HIS A  78       7.862  14.998  46.764  1.00 13.99           C  
ATOM    621  CE1 HIS A  78      10.045  14.997  46.565  1.00 17.69           C  
ATOM    622  NE2 HIS A  78       9.039  14.493  47.258  1.00 15.74           N  
ATOM    623  N   LEU A  79       5.442  15.564  41.694  1.00 11.07           N  
ATOM    624  CA  LEU A  79       4.492  16.020  40.698  1.00  9.68           C  
ATOM    625  C   LEU A  79       3.582  14.893  40.309  1.00  8.29           C  
ATOM    626  O   LEU A  79       3.935  13.718  40.421  1.00  3.89           O  
ATOM    627  CB  LEU A  79       5.216  16.427  39.406  1.00 10.42           C  
ATOM    628  CG  LEU A  79       6.125  17.649  39.353  1.00  9.47           C  
ATOM    629  CD1 LEU A  79       6.937  17.594  38.077  1.00  3.91           C  
ATOM    630  CD2 LEU A  79       5.307  18.925  39.447  1.00  2.98           C  
ATOM    631  N   SER A  80       2.386  15.264  39.883  1.00  8.14           N  
ATOM    632  CA  SER A  80       1.449  14.283  39.381  1.00  8.37           C  
ATOM    633  C   SER A  80       2.025  14.103  37.966  1.00  9.01           C  
ATOM    634  O   SER A  80       2.521  15.074  37.373  1.00  7.20           O  
ATOM    635  CB  SER A  80       0.042  14.885  39.308  1.00  5.60           C  
ATOM    636  OG  SER A  80      -0.776  14.191  38.382  1.00  4.08           O  
ATOM    637  N   CYS A  81       1.997  12.881  37.444  1.00  8.12           N  
ATOM    638  CA  CYS A  81       2.506  12.628  36.097  1.00  7.20           C  
ATOM    639  C   CYS A  81       1.717  13.470  35.110  1.00  8.22           C  
ATOM    640  O   CYS A  81       2.177  13.753  34.010  1.00  9.70           O  
ATOM    641  CB  CYS A  81       2.409  11.151  35.750  1.00  4.70           C  
ATOM    642  SG  CYS A  81       3.482  10.084  36.765  1.00  2.45           S  
ATOM    643  N   SER A  82       0.542  13.910  35.541  1.00  4.78           N  
ATOM    644  CA  SER A  82      -0.300  14.762  34.734  1.00  6.51           C  
ATOM    645  C   SER A  82       0.468  16.034  34.373  1.00  6.43           C  
ATOM    646  O   SER A  82       0.385  16.514  33.249  1.00  8.10           O  
ATOM    647  CB  SER A  82      -1.546  15.133  35.536  1.00  6.42           C  
ATOM    648  OG  SER A  82      -2.341  16.070  34.850  1.00 15.99           O  
ATOM    649  N   ALA A  83       1.257  16.556  35.310  1.00  5.54           N  
ATOM    650  CA  ALA A  83       1.998  17.788  35.073  1.00  3.38           C  
ATOM    651  C   ALA A  83       2.960  17.633  33.913  1.00  6.19           C  
ATOM    652  O   ALA A  83       3.369  18.618  33.293  1.00  6.99           O  
ATOM    653  CB  ALA A  83       2.741  18.196  36.309  1.00  2.00           C  
ATOM    654  N   LEU A  84       3.257  16.383  33.575  1.00  6.83           N  
ATOM    655  CA  LEU A  84       4.191  16.077  32.506  1.00  7.21           C  
ATOM    656  C   LEU A  84       3.562  15.945  31.121  1.00  9.04           C  
ATOM    657  O   LEU A  84       4.247  15.567  30.165  1.00  5.67           O  
ATOM    658  CB  LEU A  84       4.994  14.824  32.864  1.00  7.34           C  
ATOM    659  CG  LEU A  84       5.775  14.956  34.175  1.00  6.71           C  
ATOM    660  CD1 LEU A  84       6.555  13.683  34.422  1.00  4.94           C  
ATOM    661  CD2 LEU A  84       6.706  16.170  34.160  1.00  2.00           C  
ATOM    662  N   LEU A  85       2.273  16.278  31.007  1.00  9.51           N  
ATOM    663  CA  LEU A  85       1.563  16.217  29.726  1.00 10.14           C  
ATOM    664  C   LEU A  85       0.990  17.603  29.364  1.00 12.55           C  
ATOM    665  O   LEU A  85       0.134  17.734  28.476  1.00 13.09           O  
ATOM    666  CB  LEU A  85       0.436  15.169  29.789  1.00  8.43           C  
ATOM    667  CG  LEU A  85       0.825  13.771  30.297  1.00  7.02           C  
ATOM    668  CD1 LEU A  85      -0.396  12.878  30.371  1.00  2.11           C  
ATOM    669  CD2 LEU A  85       1.878  13.157  29.386  1.00  8.14           C  
ATOM    670  N   GLN A  86       1.466  18.634  30.057  1.00  9.86           N  
ATOM    671  CA  GLN A  86       1.010  20.007  29.828  1.00 10.69           C  
ATOM    672  C   GLN A  86       1.719  20.609  28.619  1.00  8.68           C  
ATOM    673  O   GLN A  86       2.839  20.203  28.291  1.00  9.00           O  
ATOM    674  CB  GLN A  86       1.344  20.885  31.037  1.00 14.29           C  
ATOM    675  CG  GLN A  86       0.694  20.523  32.365  1.00 17.20           C  
ATOM    676  CD  GLN A  86       1.139  21.485  33.462  1.00 21.78           C  
ATOM    677  OE1 GLN A  86       0.628  22.604  33.570  1.00 25.93           O  
ATOM    678  NE2 GLN A  86       2.146  21.089  34.224  1.00 21.14           N  
ATOM    679  N   ASP A  87       1.090  21.592  27.978  1.00  7.46           N  
ATOM    680  CA  ASP A  87       1.717  22.248  26.838  1.00  7.22           C  
ATOM    681  C   ASP A  87       2.865  23.072  27.394  1.00  5.92           C  
ATOM    682  O   ASP A  87       3.882  23.259  26.730  1.00  6.96           O  
ATOM    683  CB  ASP A  87       0.746  23.174  26.093  1.00 11.81           C  
ATOM    684  CG  ASP A  87      -0.276  22.421  25.218  1.00 12.47           C  
ATOM    685  OD1 ASP A  87      -0.463  21.194  25.373  1.00 11.22           O  
ATOM    686  OD2 ASP A  87      -0.915  23.098  24.377  1.00 13.90           O  
ATOM    687  N   ASN A  88       2.677  23.620  28.595  1.00  5.32           N  
ATOM    688  CA  ASN A  88       3.737  24.399  29.232  1.00  4.16           C  
ATOM    689  C   ASN A  88       4.668  23.411  29.908  1.00  3.10           C  
ATOM    690  O   ASN A  88       4.255  22.681  30.806  1.00  2.00           O  
ATOM    691  CB  ASN A  88       3.204  25.362  30.269  1.00  3.64           C  
ATOM    692  CG  ASN A  88       4.300  26.199  30.853  1.00  5.05           C  
ATOM    693  OD1 ASN A  88       5.097  25.720  31.646  1.00  6.06           O  
ATOM    694  ND2 ASN A  88       4.402  27.431  30.407  1.00  7.72           N  
ATOM    695  N   ILE A  89       5.940  23.470  29.548  1.00  2.65           N  
ATOM    696  CA  ILE A  89       6.917  22.517  30.057  1.00  4.39           C  
ATOM    697  C   ILE A  89       7.811  22.904  31.241  1.00  2.91           C  
ATOM    698  O   ILE A  89       8.765  22.193  31.537  1.00  2.00           O  
ATOM    699  CB  ILE A  89       7.800  21.972  28.881  1.00  4.15           C  
ATOM    700  CG1 ILE A  89       8.689  23.086  28.319  1.00  5.17           C  
ATOM    701  CG2 ILE A  89       6.903  21.393  27.767  1.00  2.00           C  
ATOM    702  CD1 ILE A  89       9.918  22.579  27.580  1.00  4.20           C  
ATOM    703  N   ALA A  90       7.482  23.975  31.956  1.00  3.00           N  
ATOM    704  CA  ALA A  90       8.292  24.385  33.103  1.00  2.00           C  
ATOM    705  C   ALA A  90       8.401  23.266  34.143  1.00  2.69           C  
ATOM    706  O   ALA A  90       9.495  22.980  34.637  1.00  5.52           O  
ATOM    707  CB  ALA A  90       7.728  25.661  33.736  1.00  2.00           C  
ATOM    708  N   ASP A  91       7.290  22.604  34.450  1.00  3.10           N  
ATOM    709  CA  ASP A  91       7.313  21.511  35.419  1.00  4.36           C  
ATOM    710  C   ASP A  91       8.203  20.373  34.930  1.00  3.31           C  
ATOM    711  O   ASP A  91       9.078  19.909  35.668  1.00  3.13           O  
ATOM    712  CB  ASP A  91       5.903  20.994  35.706  1.00  5.14           C  
ATOM    713  CG  ASP A  91       5.063  21.998  36.469  1.00 10.59           C  
ATOM    714  OD1 ASP A  91       3.816  21.916  36.372  1.00 15.66           O  
ATOM    715  OD2 ASP A  91       5.644  22.867  37.167  1.00  9.48           O  
ATOM    716  N   ALA A  92       8.002  19.961  33.678  1.00  2.00           N  
ATOM    717  CA  ALA A  92       8.803  18.899  33.072  1.00  3.98           C  
ATOM    718  C   ALA A  92      10.293  19.244  33.148  1.00  3.90           C  
ATOM    719  O   ALA A  92      11.127  18.394  33.480  1.00  3.41           O  
ATOM    720  CB  ALA A  92       8.378  18.665  31.618  1.00  2.00           C  
ATOM    721  N   VAL A  93      10.622  20.502  32.872  1.00  4.29           N  
ATOM    722  CA  VAL A  93      12.010  20.968  32.928  1.00  3.66           C  
ATOM    723  C   VAL A  93      12.538  20.971  34.371  1.00  3.48           C  
ATOM    724  O   VAL A  93      13.661  20.541  34.618  1.00  2.00           O  
ATOM    725  CB  VAL A  93      12.166  22.372  32.268  1.00  5.13           C  
ATOM    726  CG1 VAL A  93      13.505  22.994  32.618  1.00  2.00           C  
ATOM    727  CG2 VAL A  93      12.034  22.243  30.753  1.00  2.00           C  
ATOM    728  N   ALA A  94      11.717  21.412  35.324  1.00  4.75           N  
ATOM    729  CA  ALA A  94      12.125  21.409  36.730  1.00  3.71           C  
ATOM    730  C   ALA A  94      12.382  19.960  37.138  1.00  2.73           C  
ATOM    731  O   ALA A  94      13.293  19.673  37.899  1.00  3.65           O  
ATOM    732  CB  ALA A  94      11.044  22.028  37.607  1.00  2.00           C  
ATOM    733  N   CYS A  95      11.579  19.038  36.618  1.00  5.34           N  
ATOM    734  CA  CYS A  95      11.763  17.624  36.931  1.00  5.56           C  
ATOM    735  C   CYS A  95      13.064  17.100  36.307  1.00  5.67           C  
ATOM    736  O   CYS A  95      13.871  16.457  36.978  1.00  7.97           O  
ATOM    737  CB  CYS A  95      10.559  16.801  36.464  1.00  2.01           C  
ATOM    738  SG  CYS A  95      10.556  15.039  36.971  1.00  9.63           S  
ATOM    739  N   MET A  96      13.300  17.428  35.043  1.00  4.61           N  
ATOM    740  CA  MET A  96      14.507  16.988  34.352  1.00  4.27           C  
ATOM    741  C   MET A  96      15.791  17.430  35.034  1.00  2.42           C  
ATOM    742  O   MET A  96      16.821  16.767  34.928  1.00  2.00           O  
ATOM    743  CB  MET A  96      14.483  17.464  32.911  1.00  5.67           C  
ATOM    744  CG  MET A  96      13.479  16.695  32.097  1.00  9.24           C  
ATOM    745  SD  MET A  96      13.983  14.999  31.971  1.00 11.34           S  
ATOM    746  CE  MET A  96      15.316  15.247  30.823  1.00 17.20           C  
ATOM    747  N   LYS A  97      15.724  18.558  35.728  1.00  3.93           N  
ATOM    748  CA  LYS A  97      16.876  19.090  36.459  1.00  3.46           C  
ATOM    749  C   LYS A  97      17.120  18.246  37.727  1.00  2.06           C  
ATOM    750  O   LYS A  97      18.255  17.958  38.085  1.00  2.00           O  
ATOM    751  CB  LYS A  97      16.638  20.566  36.792  1.00  2.35           C  
ATOM    752  CG  LYS A  97      16.536  21.475  35.579  1.00  2.00           C  
ATOM    753  CD  LYS A  97      16.193  22.879  36.028  1.00  3.33           C  
ATOM    754  CE  LYS A  97      16.318  23.877  34.928  1.00  4.08           C  
ATOM    755  NZ  LYS A  97      15.874  25.188  35.427  1.00  2.00           N  
ATOM    756  N   ARG A  98      16.039  17.813  38.371  1.00  2.42           N  
ATOM    757  CA  ARG A  98      16.119  16.966  39.555  1.00  3.82           C  
ATOM    758  C   ARG A  98      16.728  15.623  39.123  1.00  6.24           C  
ATOM    759  O   ARG A  98      17.635  15.101  39.774  1.00  7.32           O  
ATOM    760  CB  ARG A  98      14.711  16.762  40.124  1.00  7.41           C  
ATOM    761  CG  ARG A  98      14.578  15.662  41.157  1.00  8.44           C  
ATOM    762  CD  ARG A  98      15.445  15.924  42.373  1.00 12.11           C  
ATOM    763  NE  ARG A  98      15.439  14.766  43.254  1.00 10.46           N  
ATOM    764  CZ  ARG A  98      16.247  13.725  43.115  1.00 11.25           C  
ATOM    765  NH1 ARG A  98      16.154  12.706  43.961  1.00 14.81           N  
ATOM    766  NH2 ARG A  98      17.165  13.712  42.152  1.00  7.43           N  
ATOM    767  N   VAL A  99      16.234  15.084  38.009  1.00  5.31           N  
ATOM    768  CA  VAL A  99      16.724  13.827  37.439  1.00  3.81           C  
ATOM    769  C   VAL A  99      18.248  13.842  37.218  1.00  6.32           C  
ATOM    770  O   VAL A  99      18.946  12.909  37.635  1.00  9.02           O  
ATOM    771  CB  VAL A  99      16.009  13.493  36.098  1.00  2.77           C  
ATOM    772  CG1 VAL A  99      16.608  12.240  35.469  1.00  2.35           C  
ATOM    773  CG2 VAL A  99      14.516  13.300  36.326  1.00  2.00           C  
ATOM    774  N   VAL A 100      18.777  14.882  36.576  1.00  6.49           N  
ATOM    775  CA  VAL A 100      20.223  14.944  36.360  1.00  9.84           C  
ATOM    776  C   VAL A 100      21.060  15.429  37.570  1.00 13.24           C  
ATOM    777  O   VAL A 100      22.263  15.654  37.458  1.00 16.84           O  
ATOM    778  CB  VAL A 100      20.602  15.701  35.070  1.00  5.61           C  
ATOM    779  CG1 VAL A 100      19.812  15.141  33.903  1.00  4.78           C  
ATOM    780  CG2 VAL A 100      20.394  17.194  35.231  1.00  3.06           C  
ATOM    781  N   ARG A 101      20.422  15.615  38.719  1.00 15.62           N  
ATOM    782  CA  ARG A 101      21.158  15.972  39.920  1.00 17.73           C  
ATOM    783  C   ARG A 101      21.634  14.650  40.529  1.00 21.51           C  
ATOM    784  O   ARG A 101      22.316  14.629  41.555  1.00 26.31           O  
ATOM    785  CB  ARG A 101      20.282  16.709  40.910  1.00 13.98           C  
ATOM    786  CG  ARG A 101      20.372  18.200  40.796  1.00 13.97           C  
ATOM    787  CD  ARG A 101      19.435  18.829  41.804  1.00 16.10           C  
ATOM    788  NE  ARG A 101      18.622  19.866  41.187  1.00 18.20           N  
ATOM    789  CZ  ARG A 101      17.351  20.095  41.476  1.00 16.92           C  
ATOM    790  NH1 ARG A 101      16.705  21.072  40.854  1.00 15.33           N  
ATOM    791  NH2 ARG A 101      16.726  19.350  42.375  1.00 14.92           N  
ATOM    792  N   ASP A 102      21.231  13.547  39.906  1.00 23.03           N  
ATOM    793  CA  ASP A 102      21.625  12.202  40.313  1.00 24.48           C  
ATOM    794  C   ASP A 102      22.903  11.802  39.559  1.00 26.23           C  
ATOM    795  O   ASP A 102      23.243  12.405  38.537  1.00 25.87           O  
ATOM    796  CB  ASP A 102      20.486  11.218  40.034  1.00 23.26           C  
ATOM    797  CG  ASP A 102      19.510  11.112  41.194  1.00 24.97           C  
ATOM    798  OD1 ASP A 102      18.613  10.245  41.140  1.00 23.08           O  
ATOM    799  OD2 ASP A 102      19.647  11.878  42.172  1.00 27.30           O  
ATOM    800  N   PRO A 103      23.576  10.728  40.001  1.00 27.53           N  
ATOM    801  CA  PRO A 103      24.817  10.227  39.401  1.00 28.98           C  
ATOM    802  C   PRO A 103      24.849  10.007  37.891  1.00 28.71           C  
ATOM    803  O   PRO A 103      25.750  10.499  37.213  1.00 28.73           O  
ATOM    804  CB  PRO A 103      25.050   8.919  40.154  1.00 29.27           C  
ATOM    805  CG  PRO A 103      23.652   8.454  40.447  1.00 30.92           C  
ATOM    806  CD  PRO A 103      23.049   9.736  40.957  1.00 30.48           C  
ATOM    807  N   GLN A 104      23.898   9.237  37.372  1.00 29.91           N  
ATOM    808  CA  GLN A 104      23.860   8.935  35.939  1.00 31.01           C  
ATOM    809  C   GLN A 104      23.915  10.158  35.037  1.00 30.49           C  
ATOM    810  O   GLN A 104      24.632  10.168  34.017  1.00 27.94           O  
ATOM    811  CB  GLN A 104      22.622   8.112  35.597  1.00 30.27           C  
ATOM    812  CG  GLN A 104      22.721   6.684  36.059  1.00 36.42           C  
ATOM    813  CD  GLN A 104      22.307   5.700  34.984  1.00 39.17           C  
ATOM    814  OE1 GLN A 104      21.178   5.205  34.989  1.00 41.33           O  
ATOM    815  NE2 GLN A 104      23.216   5.413  34.051  1.00 38.57           N  
ATOM    816  N   GLY A 105      23.176  11.192  35.425  1.00 28.64           N  
ATOM    817  CA  GLY A 105      23.126  12.392  34.624  1.00 26.70           C  
ATOM    818  C   GLY A 105      22.123  12.125  33.515  1.00 26.51           C  
ATOM    819  O   GLY A 105      21.095  11.460  33.731  1.00 21.86           O  
ATOM    820  N   ILE A 106      22.454  12.573  32.308  1.00 24.81           N  
ATOM    821  CA  ILE A 106      21.576  12.399  31.155  1.00 22.79           C  
ATOM    822  C   ILE A 106      21.654  10.963  30.621  1.00 21.16           C  
ATOM    823  O   ILE A 106      20.731  10.485  29.957  1.00 20.26           O  
ATOM    824  CB  ILE A 106      21.917  13.447  30.062  1.00 21.74           C  
ATOM    825  CG1 ILE A 106      20.864  13.451  28.960  1.00 20.21           C  
ATOM    826  CG2 ILE A 106      23.320  13.219  29.521  1.00 23.46           C  
ATOM    827  CD1 ILE A 106      20.915  14.679  28.106  1.00 15.09           C  
ATOM    828  N   ARG A 107      22.721  10.263  30.998  1.00 19.79           N  
ATOM    829  CA  ARG A 107      22.951   8.881  30.599  1.00 20.43           C  
ATOM    830  C   ARG A 107      21.852   7.924  31.059  1.00 22.54           C  
ATOM    831  O   ARG A 107      21.807   6.769  30.639  1.00 24.16           O  
ATOM    832  CB  ARG A 107      24.295   8.415  31.131  1.00 17.87           C  
ATOM    833  CG  ARG A 107      25.462   8.902  30.325  1.00 20.06           C  
ATOM    834  CD  ARG A 107      26.728   8.839  31.148  1.00 22.16           C  
ATOM    835  NE  ARG A 107      27.952   8.976  30.353  1.00 23.71           N  
ATOM    836  CZ  ARG A 107      28.408  10.112  29.829  1.00 23.99           C  
ATOM    837  NH1 ARG A 107      29.540  10.092  29.134  1.00 27.78           N  
ATOM    838  NH2 ARG A 107      27.750  11.260  29.984  1.00 16.62           N  
ATOM    839  N   ALA A 108      20.961   8.414  31.913  1.00 24.58           N  
ATOM    840  CA  ALA A 108      19.853   7.612  32.426  1.00 26.02           C  
ATOM    841  C   ALA A 108      18.912   7.190  31.286  1.00 24.57           C  
ATOM    842  O   ALA A 108      18.147   6.217  31.402  1.00 24.78           O  
ATOM    843  CB  ALA A 108      19.087   8.413  33.493  1.00 27.10           C  
ATOM    844  N   TRP A 109      18.971   7.947  30.194  1.00 20.87           N  
ATOM    845  CA  TRP A 109      18.163   7.699  29.014  1.00 17.62           C  
ATOM    846  C   TRP A 109      19.034   6.980  27.977  1.00 15.76           C  
ATOM    847  O   TRP A 109      20.026   7.549  27.513  1.00 16.00           O  
ATOM    848  CB  TRP A 109      17.674   9.040  28.427  1.00 14.86           C  
ATOM    849  CG  TRP A 109      16.528   9.703  29.159  1.00 12.04           C  
ATOM    850  CD1 TRP A 109      15.188   9.513  28.937  1.00 10.24           C  
ATOM    851  CD2 TRP A 109      16.622  10.684  30.205  1.00 14.26           C  
ATOM    852  NE1 TRP A 109      14.444  10.313  29.775  1.00 11.00           N  
ATOM    853  CE2 TRP A 109      15.293  11.037  30.568  1.00 13.90           C  
ATOM    854  CE3 TRP A 109      17.696  11.306  30.866  1.00 13.45           C  
ATOM    855  CZ2 TRP A 109      15.012  11.986  31.565  1.00 19.53           C  
ATOM    856  CZ3 TRP A 109      17.421  12.254  31.856  1.00 17.40           C  
ATOM    857  CH2 TRP A 109      16.085  12.584  32.196  1.00 20.13           C  
ATOM    858  N   VAL A 110      18.671   5.747  27.610  1.00 13.40           N  
ATOM    859  CA  VAL A 110      19.423   4.985  26.603  1.00 11.83           C  
ATOM    860  C   VAL A 110      19.365   5.655  25.218  1.00  9.95           C  
ATOM    861  O   VAL A 110      20.290   5.529  24.409  1.00 10.88           O  
ATOM    862  CB  VAL A 110      18.897   3.535  26.472  1.00 15.27           C  
ATOM    863  CG1 VAL A 110      19.796   2.734  25.544  1.00 13.77           C  
ATOM    864  CG2 VAL A 110      18.812   2.879  27.841  1.00 14.12           C  
ATOM    865  N   ALA A 111      18.278   6.379  24.960  1.00  8.71           N  
ATOM    866  CA  ALA A 111      18.075   7.106  23.708  1.00  7.69           C  
ATOM    867  C   ALA A 111      19.167   8.162  23.536  1.00  8.33           C  
ATOM    868  O   ALA A 111      19.729   8.314  22.449  1.00  6.92           O  
ATOM    869  CB  ALA A 111      16.704   7.778  23.710  1.00  9.53           C  
ATOM    870  N   TRP A 112      19.454   8.908  24.603  1.00  8.44           N  
ATOM    871  CA  TRP A 112      20.504   9.915  24.550  1.00  6.75           C  
ATOM    872  C   TRP A 112      21.805   9.222  24.181  1.00  9.41           C  
ATOM    873  O   TRP A 112      22.578   9.718  23.367  1.00 12.05           O  
ATOM    874  CB  TRP A 112      20.693  10.587  25.911  1.00  7.15           C  
ATOM    875  CG  TRP A 112      21.817  11.590  25.877  1.00  9.07           C  
ATOM    876  CD1 TRP A 112      21.791  12.840  25.309  1.00  9.05           C  
ATOM    877  CD2 TRP A 112      23.160  11.399  26.362  1.00  7.36           C  
ATOM    878  NE1 TRP A 112      23.041  13.430  25.403  1.00 10.46           N  
ATOM    879  CE2 TRP A 112      23.892  12.568  26.048  1.00  8.22           C  
ATOM    880  CE3 TRP A 112      23.809  10.355  27.034  1.00  7.02           C  
ATOM    881  CZ2 TRP A 112      25.233  12.718  26.384  1.00  9.11           C  
ATOM    882  CZ3 TRP A 112      25.136  10.504  27.366  1.00  6.83           C  
ATOM    883  CH2 TRP A 112      25.838  11.679  27.043  1.00 11.09           C  
ATOM    884  N   ARG A 113      22.059   8.083  24.813  1.00 10.88           N  
ATOM    885  CA  ARG A 113      23.270   7.324  24.559  1.00 11.77           C  
ATOM    886  C   ARG A 113      23.374   6.816  23.127  1.00 11.89           C  
ATOM    887  O   ARG A 113      24.398   7.009  22.479  1.00 15.17           O  
ATOM    888  CB  ARG A 113      23.388   6.183  25.566  1.00 12.17           C  
ATOM    889  CG  ARG A 113      23.847   6.669  26.918  1.00 14.76           C  
ATOM    890  CD  ARG A 113      23.229   5.897  28.053  1.00 21.89           C  
ATOM    891  NE  ARG A 113      23.580   4.482  28.042  1.00 27.97           N  
ATOM    892  CZ  ARG A 113      23.033   3.578  28.854  1.00 32.71           C  
ATOM    893  NH1 ARG A 113      23.405   2.309  28.777  1.00 35.38           N  
ATOM    894  NH2 ARG A 113      22.118   3.942  29.752  1.00 34.13           N  
ATOM    895  N   ASN A 114      22.275   6.304  22.591  1.00 13.34           N  
ATOM    896  CA  ASN A 114      22.273   5.763  21.232  1.00 12.72           C  
ATOM    897  C   ASN A 114      22.245   6.757  20.097  1.00 11.65           C  
ATOM    898  O   ASN A 114      22.855   6.520  19.067  1.00 10.21           O  
ATOM    899  CB  ASN A 114      21.146   4.748  21.057  1.00 11.95           C  
ATOM    900  CG  ASN A 114      21.348   3.514  21.907  1.00 12.28           C  
ATOM    901  OD1 ASN A 114      22.482   3.132  22.200  1.00 12.82           O  
ATOM    902  ND2 ASN A 114      20.255   2.899  22.331  1.00 12.70           N  
ATOM    903  N   ARG A 115      21.525   7.859  20.263  1.00 13.97           N  
ATOM    904  CA  ARG A 115      21.450   8.855  19.198  1.00 13.64           C  
ATOM    905  C   ARG A 115      22.018  10.235  19.492  1.00 14.92           C  
ATOM    906  O   ARG A 115      21.980  11.098  18.613  1.00 17.47           O  
ATOM    907  CB  ARG A 115      20.026   9.006  18.644  1.00 13.70           C  
ATOM    908  CG  ARG A 115      18.887   8.408  19.461  1.00 17.70           C  
ATOM    909  CD  ARG A 115      18.725   6.903  19.255  1.00 20.97           C  
ATOM    910  NE  ARG A 115      18.506   6.532  17.861  1.00 24.49           N  
ATOM    911  CZ  ARG A 115      17.675   5.575  17.457  1.00 27.51           C  
ATOM    912  NH1 ARG A 115      17.549   5.309  16.164  1.00 29.23           N  
ATOM    913  NH2 ARG A 115      16.953   4.896  18.335  1.00 29.17           N  
ATOM    914  N   CYS A 116      22.618  10.433  20.665  1.00 11.49           N  
ATOM    915  CA  CYS A 116      23.160  11.742  21.004  1.00  9.89           C  
ATOM    916  C   CYS A 116      24.577  11.766  21.485  1.00 10.35           C  
ATOM    917  O   CYS A 116      25.345  12.641  21.083  1.00 10.00           O  
ATOM    918  CB  CYS A 116      22.299  12.416  22.057  1.00 11.49           C  
ATOM    919  SG  CYS A 116      20.535  12.504  21.638  1.00  9.80           S  
ATOM    920  N   GLN A 117      24.908  10.872  22.407  1.00 14.12           N  
ATOM    921  CA  GLN A 117      26.261  10.812  22.948  1.00 20.77           C  
ATOM    922  C   GLN A 117      27.294  10.525  21.855  1.00 23.78           C  
ATOM    923  O   GLN A 117      27.030   9.766  20.918  1.00 27.45           O  
ATOM    924  CB  GLN A 117      26.349   9.761  24.054  1.00 19.89           C  
ATOM    925  CG  GLN A 117      27.758   9.587  24.633  1.00 20.87           C  
ATOM    926  CD  GLN A 117      27.783   8.690  25.854  1.00 23.07           C  
ATOM    927  OE1 GLN A 117      28.553   8.919  26.789  1.00 25.83           O  
ATOM    928  NE2 GLN A 117      26.941   7.666  25.858  1.00 20.51           N  
ATOM    929  N   ASN A 118      28.457  11.160  21.963  1.00 27.05           N  
ATOM    930  CA  ASN A 118      29.539  10.979  20.989  1.00 32.12           C  
ATOM    931  C   ASN A 118      29.076  11.229  19.561  1.00 33.66           C  
ATOM    932  O   ASN A 118      29.505  10.554  18.625  1.00 36.51           O  
ATOM    933  CB  ASN A 118      30.144   9.571  21.085  1.00 32.91           C  
ATOM    934  CG  ASN A 118      30.770   9.287  22.436  1.00 34.44           C  
ATOM    935  OD1 ASN A 118      30.895   8.125  22.832  1.00 36.38           O  
ATOM    936  ND2 ASN A 118      31.167  10.339  23.156  1.00 35.33           N  
ATOM    937  N   ARG A 119      28.183  12.194  19.406  1.00 35.16           N  
ATOM    938  CA  ARG A 119      27.648  12.568  18.107  1.00 35.55           C  
ATOM    939  C   ARG A 119      27.528  14.091  18.096  1.00 36.38           C  
ATOM    940  O   ARG A 119      27.596  14.731  19.151  1.00 36.50           O  
ATOM    941  CB  ARG A 119      26.272  11.946  17.913  1.00 34.37           C  
ATOM    942  CG  ARG A 119      26.261  10.438  17.925  1.00 36.10           C  
ATOM    943  CD  ARG A 119      24.851   9.966  17.747  1.00 36.63           C  
ATOM    944  NE  ARG A 119      24.721   8.516  17.731  1.00 37.15           N  
ATOM    945  CZ  ARG A 119      24.382   7.814  16.653  1.00 37.81           C  
ATOM    946  NH1 ARG A 119      24.264   6.494  16.724  1.00 40.54           N  
ATOM    947  NH2 ARG A 119      24.186   8.429  15.494  1.00 39.84           N  
ATOM    948  N   ASP A 120      27.416  14.690  16.917  1.00 37.24           N  
ATOM    949  CA  ASP A 120      27.280  16.138  16.890  1.00 37.58           C  
ATOM    950  C   ASP A 120      25.798  16.504  16.978  1.00 34.95           C  
ATOM    951  O   ASP A 120      24.971  16.040  16.174  1.00 34.78           O  
ATOM    952  CB  ASP A 120      27.951  16.761  15.665  1.00 40.22           C  
ATOM    953  CG  ASP A 120      28.461  18.167  15.947  1.00 43.33           C  
ATOM    954  OD1 ASP A 120      28.741  18.462  17.134  1.00 39.40           O  
ATOM    955  OD2 ASP A 120      28.566  18.975  14.995  1.00 46.14           O  
ATOM    956  N   VAL A 121      25.466  17.247  18.034  1.00 30.59           N  
ATOM    957  CA  VAL A 121      24.096  17.674  18.299  1.00 25.77           C  
ATOM    958  C   VAL A 121      23.864  19.165  18.067  1.00 23.86           C  
ATOM    959  O   VAL A 121      22.736  19.639  18.231  1.00 22.62           O  
ATOM    960  CB  VAL A 121      23.656  17.300  19.734  1.00 24.25           C  
ATOM    961  CG1 VAL A 121      23.616  15.788  19.896  1.00 22.22           C  
ATOM    962  CG2 VAL A 121      24.610  17.917  20.749  1.00 23.81           C  
ATOM    963  N   ARG A 122      24.919  19.894  17.685  1.00 21.98           N  
ATOM    964  CA  ARG A 122      24.824  21.334  17.400  1.00 21.44           C  
ATOM    965  C   ARG A 122      23.694  21.572  16.410  1.00 19.43           C  
ATOM    966  O   ARG A 122      22.978  22.552  16.498  1.00 19.60           O  
ATOM    967  CB  ARG A 122      26.102  21.848  16.752  1.00 23.59           C  
ATOM    968  CG  ARG A 122      27.264  22.087  17.661  1.00 28.16           C  
ATOM    969  CD  ARG A 122      28.305  22.795  16.828  1.00 33.74           C  
ATOM    970  NE  ARG A 122      29.590  22.964  17.494  1.00 40.81           N  
ATOM    971  CZ  ARG A 122      30.428  21.972  17.773  1.00 43.42           C  
ATOM    972  NH1 ARG A 122      31.584  22.233  18.362  1.00 46.02           N  
ATOM    973  NH2 ARG A 122      30.100  20.719  17.490  1.00 46.14           N  
ATOM    974  N   GLN A 123      23.585  20.675  15.438  1.00 20.28           N  
ATOM    975  CA  GLN A 123      22.553  20.710  14.416  1.00 18.27           C  
ATOM    976  C   GLN A 123      21.151  20.924  15.013  1.00 18.24           C  
ATOM    977  O   GLN A 123      20.232  21.353  14.307  1.00 17.91           O  
ATOM    978  CB  GLN A 123      22.575  19.396  13.635  1.00 20.11           C  
ATOM    979  CG  GLN A 123      22.595  18.174  14.548  1.00 24.60           C  
ATOM    980  CD  GLN A 123      22.036  16.922  13.900  1.00 30.96           C  
ATOM    981  OE1 GLN A 123      20.994  16.962  13.234  1.00 33.92           O  
ATOM    982  NE2 GLN A 123      22.697  15.790  14.131  1.00 32.49           N  
ATOM    983  N   TYR A 124      20.968  20.585  16.289  1.00 14.07           N  
ATOM    984  CA  TYR A 124      19.669  20.767  16.925  1.00 12.73           C  
ATOM    985  C   TYR A 124      19.396  22.231  17.320  1.00 12.31           C  
ATOM    986  O   TYR A 124      18.248  22.661  17.348  1.00 13.35           O  
ATOM    987  CB  TYR A 124      19.513  19.824  18.131  1.00 13.00           C  
ATOM    988  CG  TYR A 124      19.447  18.344  17.768  1.00 12.20           C  
ATOM    989  CD1 TYR A 124      18.245  17.740  17.413  1.00 13.06           C  
ATOM    990  CD2 TYR A 124      20.593  17.555  17.769  1.00 14.73           C  
ATOM    991  CE1 TYR A 124      18.193  16.386  17.066  1.00 12.67           C  
ATOM    992  CE2 TYR A 124      20.551  16.209  17.429  1.00 12.80           C  
ATOM    993  CZ  TYR A 124      19.351  15.632  17.079  1.00 14.87           C  
ATOM    994  OH  TYR A 124      19.324  14.294  16.741  1.00 18.37           O  
ATOM    995  N   VAL A 125      20.445  23.006  17.591  1.00 11.16           N  
ATOM    996  CA  VAL A 125      20.270  24.401  17.981  1.00  7.14           C  
ATOM    997  C   VAL A 125      20.694  25.431  16.927  1.00  8.46           C  
ATOM    998  O   VAL A 125      20.624  26.643  17.177  1.00  6.13           O  
ATOM    999  CB  VAL A 125      20.971  24.703  19.330  1.00  7.24           C  
ATOM   1000  CG1 VAL A 125      20.459  23.750  20.408  1.00  4.61           C  
ATOM   1001  CG2 VAL A 125      22.469  24.575  19.207  1.00  3.43           C  
ATOM   1002  N   GLN A 126      21.084  24.966  15.742  1.00  7.27           N  
ATOM   1003  CA  GLN A 126      21.502  25.875  14.666  1.00  9.33           C  
ATOM   1004  C   GLN A 126      20.351  26.737  14.139  1.00  7.02           C  
ATOM   1005  O   GLN A 126      19.264  26.236  13.821  1.00  6.48           O  
ATOM   1006  CB  GLN A 126      22.129  25.089  13.504  1.00 13.76           C  
ATOM   1007  CG  GLN A 126      23.333  24.205  13.886  1.00 24.41           C  
ATOM   1008  CD  GLN A 126      24.504  24.968  14.520  1.00 30.50           C  
ATOM   1009  OE1 GLN A 126      25.498  25.282  13.846  1.00 33.40           O  
ATOM   1010  NE2 GLN A 126      24.408  25.232  15.828  1.00 27.75           N  
ATOM   1011  N   GLY A 127      20.597  28.034  14.036  1.00  5.74           N  
ATOM   1012  CA  GLY A 127      19.574  28.946  13.549  1.00  5.39           C  
ATOM   1013  C   GLY A 127      18.437  29.288  14.511  1.00  4.63           C  
ATOM   1014  O   GLY A 127      17.497  29.967  14.129  1.00  2.00           O  
ATOM   1015  N   CYS A 128      18.526  28.837  15.759  1.00  6.93           N  
ATOM   1016  CA  CYS A 128      17.484  29.112  16.741  1.00  9.12           C  
ATOM   1017  C   CYS A 128      17.716  30.354  17.585  1.00  8.96           C  
ATOM   1018  O   CYS A 128      16.844  30.716  18.378  1.00  7.22           O  
ATOM   1019  CB  CYS A 128      17.296  27.925  17.678  1.00  5.96           C  
ATOM   1020  SG  CYS A 128      16.925  26.372  16.834  1.00  5.93           S  
ATOM   1021  N   GLY A 129      18.909  30.942  17.471  1.00  8.96           N  
ATOM   1022  CA  GLY A 129      19.250  32.141  18.226  1.00 13.09           C  
ATOM   1023  C   GLY A 129      19.374  31.922  19.721  1.00 14.31           C  
ATOM   1024  O   GLY A 129      18.897  32.738  20.525  1.00 18.35           O  
ATOM   1025  N   VAL A 130      20.024  30.821  20.083  1.00 12.67           N  
ATOM   1026  CA  VAL A 130      20.237  30.426  21.480  1.00 13.16           C  
ATOM   1027  C   VAL A 130      21.742  30.318  21.759  1.00 14.76           C  
ATOM   1028  O   VAL A 130      22.525  30.775  20.891  1.00 15.47           O  
ATOM   1029  CB  VAL A 130      19.568  29.035  21.793  1.00 13.45           C  
ATOM   1030  CG1 VAL A 130      18.054  29.127  21.724  1.00  8.58           C  
ATOM   1031  CG2 VAL A 130      20.080  27.966  20.834  1.00 10.65           C  
ATOM   1032  OXT VAL A 130      22.131  29.751  22.810  1.00 14.67           O  
TER    1033      VAL A 130                                                      
HETATM 1034 NA    NA A 601       5.483   4.368   8.453  1.00 15.28          NA  
HETATM 1035  O   HOH A 131      -0.044  10.473  42.739  1.00  2.00           O  
HETATM 1036  O   HOH A 132       1.229  15.809  40.231  1.00  2.00           O  
HETATM 1037  O   HOH A 133       8.513  18.498  27.639  1.00  2.72           O  
HETATM 1038  O   HOH A 134      12.184  25.478  13.910  1.00  2.00           O  
HETATM 1039  O   HOH A 135      17.880   8.007  19.014  1.00  4.55           O  
HETATM 1040  O   HOH A 136       5.225  23.481  30.069  1.00  4.85           O  
HETATM 1041  O   HOH A 137      14.512  18.187  39.839  1.00  7.79           O  
HETATM 1042  O   HOH A 138      21.946  30.205  13.207  1.00  2.00           O  
HETATM 1043  O   HOH A 139       2.574   6.094  22.613  1.00 26.69           O  
HETATM 1044  O   HOH A 140       2.158   1.807  42.030  1.00  7.69           O  
HETATM 1045  O   HOH A 141      18.322  19.065  13.742  1.00 30.52           O  
HETATM 1046  O   HOH A 142      23.900  27.912  20.977  1.00  9.37           O  
HETATM 1047  O   HOH A 143       2.589   8.124  45.504  1.00 15.17           O  
HETATM 1048  O   HOH A 144      -0.616  26.825  27.398  1.00  5.96           O  
HETATM 1049  O   HOH A 145      -1.365   8.414  39.965  1.00 10.34           O  
HETATM 1050  O   HOH A 146       8.526   7.058  46.741  1.00 20.27           O  
HETATM 1051  O   HOH A 147       8.331  19.038  15.486  1.00 27.05           O  
HETATM 1052  O   HOH A 148       7.328  21.109  12.867  1.00 30.54           O  
HETATM 1053  O   HOH A 149      11.486  26.781   8.386  1.00 18.79           O  
HETATM 1054  O   HOH A 150      11.080  28.720  15.408  1.00 26.37           O  
HETATM 1055  O   HOH A 151      -1.886  12.486  44.367  1.00  9.76           O  
HETATM 1056  O   HOH A 152      23.158  29.650  14.899  1.00 25.40           O  
HETATM 1057  O   HOH A 153       6.184  29.248  25.519  1.00 17.31           O  
HETATM 1058  O   HOH A 154      15.581   9.739  23.961  1.00  8.65           O  
HETATM 1059  O   HOH A 155      -0.046  -3.219  39.292  1.00 27.92           O  
HETATM 1060  O   HOH A 156      18.613  30.407   9.880  1.00  3.23           O  
HETATM 1061  O   HOH A 157      -2.380   5.697  45.430  1.00 18.17           O  
HETATM 1062  O   HOH A 158      28.624  24.127  36.580  1.00 17.60           O  
HETATM 1063  O   HOH A 159      14.992  18.119  14.894  1.00 11.55           O  
HETATM 1064  O   HOH A 160      31.088  20.311  12.459  1.00 44.16           O  
HETATM 1065  O   HOH A 161      12.569  10.077  26.691  1.00 34.47           O  
HETATM 1066  O   HOH A 162      20.978  31.650  10.734  1.00  8.74           O  
HETATM 1067  O   HOH A 163      23.972  21.151  36.961  1.00 10.51           O  
HETATM 1068  O   HOH A 164       9.686  -0.192  46.616  1.00 26.16           O  
HETATM 1069  O   HOH A 165       4.427   5.360  45.467  1.00 21.49           O  
HETATM 1070  O   HOH A 166      -1.310  -3.332  35.464  1.00 26.30           O  
HETATM 1071  O   HOH A 167      26.831  20.415  37.679  1.00 16.94           O  
HETATM 1072  O   HOH A 168       4.256   2.947  22.861  1.00 42.00           O  
HETATM 1073  O   HOH A 169      20.983  32.771  15.690  1.00 14.87           O  
HETATM 1074  O   HOH A 170       2.175  12.224  43.931  1.00 20.62           O  
HETATM 1075  O   HOH A 171      25.134  31.322  14.917  1.00 39.02           O  
HETATM 1076  O   HOH A 172      17.046  16.792  13.204  1.00 26.77           O  
HETATM 1077  O   HOH A 173       5.819  23.784  36.650  1.00 35.58           O  
HETATM 1078  O   HOH A 174      16.761   0.822  27.312  1.00 44.70           O  
HETATM 1079  O   HOH A 175      -2.143  19.399  18.505  1.00 22.02           O  
HETATM 1080  O   HOH A 176       4.343  20.932  33.503  1.00  7.70           O  
HETATM 1081  O   HOH A 177      11.533  10.702  16.537  1.00 22.71           O  
HETATM 1082  O   HOH A 178      14.974   2.394  19.232  1.00 22.98           O  
HETATM 1083  O   HOH A 179      19.356   6.348  37.818  1.00 26.99           O  
HETATM 1084  O   HOH A 180      13.431  10.981  13.459  1.00 20.96           O  
HETATM 1085  O   HOH A 181      14.674  25.675   8.265  1.00 22.72           O  
HETATM 1086  O   HOH A 182      11.399  10.209  21.013  1.00 25.17           O  
HETATM 1087  O   HOH A 183      22.065  13.507  17.103  1.00 42.14           O  
HETATM 1088  O   HOH A 184      33.983  17.188  15.334  1.00 43.23           O  
HETATM 1089  O   HOH A 185      18.115  28.300  37.680  1.00 35.86           O  
HETATM 1090  O   HOH A 187      16.494   1.424  37.349  1.00 30.92           O  
HETATM 1091  O   HOH A 188      12.099   7.234  15.424  1.00 41.55           O  
HETATM 1092  O   HOH A 189      -1.489   1.103  22.092  1.00 30.56           O  
HETATM 1093  O   HOH A 190       9.625  16.465  40.419  1.00 24.90           O  
HETATM 1094  O   HOH A 191       4.007  26.342  16.190  1.00 42.15           O  
HETATM 1095  O   HOH A 192       7.501  -4.663  27.774  1.00 32.93           O  
HETATM 1096  O   HOH A 193      22.006  30.371  36.825  1.00 37.00           O  
HETATM 1097  O   HOH A 194       3.324   3.834  39.998  1.00 14.15           O  
HETATM 1098  O   HOH A 195       1.933   2.841  44.973  1.00 23.54           O  
HETATM 1099  O   HOH A 196      -2.485  22.510  34.544  1.00 34.69           O  
HETATM 1100  O   HOH A 197      23.201  24.036  33.778  1.00 34.29           O  
HETATM 1101  O   HOH A 198      29.149   6.996  16.629  1.00 13.67           O  
HETATM 1102  O   HOH A 199      18.312   7.829  31.049  1.00 39.22           O  
HETATM 1103  O   HOH A 200       9.612   9.605  23.502  1.00 18.45           O  
HETATM 1104  O   HOH A 201      17.808  20.847  11.828  1.00 36.96           O  
HETATM 1105  O   HOH A 202      27.501   3.145  14.249  1.00 31.24           O  
HETATM 1106  O   HOH A 203      11.840  24.287  36.174  1.00 37.89           O  
HETATM 1107  O   HOH A 204      20.802  27.168  34.964  1.00 36.73           O  
HETATM 1108  O   HOH A 205       4.028  29.205  23.254  1.00 17.43           O  
HETATM 1109  O   HOH A 206      13.318   0.462  13.122  1.00 30.81           O  
HETATM 1110  O   HOH A 207      16.504   3.531  39.587  1.00 20.87           O  
HETATM 1111  O   HOH A 208      10.349  -0.644  35.044  1.00 16.85           O  
HETATM 1112  O   HOH A 209       3.765  21.400  15.745  1.00 30.56           O  
HETATM 1113  O   HOH A 210      10.891  21.238  13.988  1.00 13.38           O  
HETATM 1114  O   HOH A 211      -2.378  15.470  35.130  1.00 34.79           O  
HETATM 1115  O   HOH A 212       0.985  -8.327  40.045  1.00 26.20           O  
HETATM 1116  O   HOH A 213      25.691  11.148  42.614  1.00 39.33           O  
HETATM 1117  O   HOH A 214       3.181  -2.862  43.279  1.00 42.91           O  
HETATM 1118  O   HOH A 215      27.246  26.219  35.270  1.00 24.69           O  
HETATM 1119  O   HOH A 216      22.900  30.850  20.493  1.00 30.80           O  
HETATM 1120  O   HOH A 217      13.539  11.066  29.488  1.00 39.90           O  
HETATM 1121  O   HOH A 218       6.479   5.369  47.341  1.00 45.47           O  
HETATM 1122  O   HOH A 219      13.314  22.121  36.764  1.00 17.63           O  
HETATM 1123  O   HOH A 220      -0.805   3.597  45.711  1.00 35.02           O  
HETATM 1124  O   HOH A 221      24.468   4.726  14.161  1.00 34.63           O  
HETATM 1125  O   HOH A 222      16.665   8.532  26.858  1.00 17.62           O  
HETATM 1126  O   HOH A 223      15.905   6.010  11.747  1.00 30.80           O  
HETATM 1127  O   HOH A 224       0.593  15.061  43.524  1.00 29.06           O  
HETATM 1128  O   HOH A 225      26.297   4.600  34.392  1.00 34.72           O  
HETATM 1129  O   HOH A 226      19.638  22.652  11.524  1.00 24.88           O  
HETATM 1130  O   HOH A 227       8.272  -7.158  30.555  1.00 40.76           O  
HETATM 1131  O   HOH A 228      27.075  20.969  34.885  1.00 15.95           O  
HETATM 1132  O   HOH A 229      22.875  19.822  39.587  1.00 26.07           O  
HETATM 1133  O   HOH A 230      15.743  12.171  30.855  1.00 37.98           O  
HETATM 1134  O   HOH A 231      18.009  14.249  12.513  1.00 35.95           O  
HETATM 1135  O   HOH A 232      20.010  20.501  41.501  1.00 24.12           O  
HETATM 1136  O   HOH A 233      13.852   3.556  35.854  1.00 24.47           O  
HETATM 1137  O   HOH A 234      17.066   4.260  28.148  1.00 38.89           O  
HETATM 1138  O   HOH A 235      12.573  18.996  13.592  1.00 22.70           O  
HETATM 1139  O   HOH A 236      24.786  33.324  22.982  1.00 44.45           O  
HETATM 1140  O   HOH A 237      21.126  23.880  39.074  1.00 35.19           O  
HETATM 1141  O   HOH A 238      32.548  16.695  18.245  1.00 35.55           O  
HETATM 1142  O   HOH A 239      15.832  10.013  17.795  1.00 35.11           O  
HETATM 1143  O   HOH A 240       9.310  22.913  38.785  1.00 29.41           O  
HETATM 1144  O   HOH A 241      10.381  16.500  44.026  1.00 31.57           O  
HETATM 1145  O   HOH A 242      17.891  23.518  37.481  1.00 15.24           O  
HETATM 1146  O   HOH A 243       9.635  23.504  12.107  1.00 36.33           O  
HETATM 1147  O   HOH A 244      -3.650  -3.969  32.371  1.00 18.64           O  
HETATM 1148  O   HOH A 245       6.933  11.944  16.964  1.00 40.92           O  
HETATM 1149  O   HOH A 246       6.185  32.545  24.945  1.00 42.24           O  
HETATM 1150  O   HOH A 247      23.794  22.000  11.571  1.00 22.88           O  
HETATM 1151  O   HOH A 248      22.052   7.591  12.175  1.00 42.45           O  
HETATM 1152  O   HOH A 249       1.440  -9.083  37.473  1.00 41.05           O  
HETATM 1153  O   HOH A 250      13.971   6.625  13.406  1.00 25.62           O  
HETATM 1154  O   HOH A 251      26.372  18.866  11.190  1.00 35.38           O  
HETATM 1155  O   HOH A 252      13.426  14.415  45.009  1.00 25.22           O  
HETATM 1156  O   HOH A 253       6.274  23.692  39.746  1.00 47.23           O  
HETATM 1157  O   HOH A 254      27.867   9.751  27.448  1.00 28.31           O  
HETATM 1158  O   HOH A 255      24.798  28.394  12.933  1.00 38.89           O  
HETATM 1159  O   HOH A 256      55.687  -0.475  13.383  1.00 47.27           O  
HETATM 1160  O   HOH A 258      13.118  -0.499  34.127  1.00 31.67           O  
HETATM 1161  O   HOH A 259      14.075  20.965  39.295  1.00 21.21           O  
HETATM 1162  O   HOH A 260       6.808   0.652  26.720  1.00 34.76           O  
HETATM 1163  O   HOH A 261      -1.147   3.768  25.653  1.00 33.06           O  
HETATM 1164  O   HOH A 262      27.207  17.823  40.798  1.00 35.20           O  
HETATM 1165  O   HOH A 263      -1.295  -1.551  30.554  1.00 35.38           O  
HETATM 1166  O   HOH A 264      25.018  20.723   9.521  1.00 32.91           O  
HETATM 1167  O   HOH A 265      26.066  19.784  13.997  1.00 33.25           O  
HETATM 1168  O   HOH A 266       8.560  25.809  41.087  1.00 32.97           O  
HETATM 1169  O   HOH A 267      25.836   8.592  12.903  1.00 36.26           O  
HETATM 1170  O   HOH A 268       5.313  25.673  10.808  1.00 31.49           O  
HETATM 1171  O   HOH A 269      25.912  28.471  35.817  1.00 36.32           O  
HETATM 1172  O   HOH A 270      25.207   2.668   7.522  1.00 40.81           O  
HETATM 1173  O   HOH A 271      19.321  25.996  10.574  1.00 23.85           O  
HETATM 1174  O   HOH A 272       1.242   3.001  22.513  1.00 26.64           O  
HETATM 1175  O   HOH A 273      14.126   4.461  10.519  1.00 39.55           O  
HETATM 1176  O   HOH A 274      15.670   2.125  11.098  1.00 30.64           O  
HETATM 1177  O   HOH A 275      12.312  16.571  41.782  1.00 33.74           O  
HETATM 1178  O   HOH A 276      10.564   5.733  22.286  1.00 31.24           O  
HETATM 1179  O   HOH A 277      10.831  26.865  11.746  1.00 36.70           O  
HETATM 1180  O   HOH A 278      12.948   6.450  31.000  1.00 40.50           O  
HETATM 1181  O   HOH A 279       7.733   1.573  23.808  1.00 35.63           O  
HETATM 1182  O   HOH A 280      12.037   5.041  28.763  1.00 38.71           O  
HETATM 1183  O   HOH A 281      23.237  27.898  36.325  1.00 37.14           O  
HETATM 1184  O   HOH A 282      28.569  21.085  11.347  1.00 41.83           O  
HETATM 1185  O   HOH A 284      15.617   2.813  15.263  1.00 42.55           O  
HETATM 1186  O   HOH A 285      11.818  23.823   9.418  1.00 30.91           O  
HETATM 1187  O   HOH A 286      15.425  19.455  11.265  1.00 42.45           O  
HETATM 1188  O   HOH A 287      13.877   6.024  17.162  1.00 45.04           O  
HETATM 1189  O   HOH A 288       0.595  -6.493  37.305  1.00 33.02           O  
HETATM 1190  O   HOH A 289       0.041   3.354  19.844  1.00 38.55           O  
HETATM 1191  O   HOH A 290       3.165  23.343  40.539  1.00 37.14           O  
HETATM 1192  O   HOH A 291       1.878  28.283   5.451  1.00 43.19           O  
HETATM 1193  O   HOH A 292      31.272  17.957  13.733  1.00 44.88           O  
HETATM 1194  O   HOH A 293       0.960  25.163  33.160  1.00 35.35           O  
HETATM 1195  O   HOH A 294       5.337   3.905  20.529  1.00 35.51           O  
HETATM 1196  O   HOH A 295       7.372   0.781  47.713  1.00 43.32           O  
HETATM 1197  O   HOH A 296      12.543   8.483  18.969  1.00 39.47           O  
HETATM 1198  O   HOH A 297       6.240  20.109  26.931  1.00  9.32           O  
HETATM 1199  O   HOH A 298      20.424   8.250  36.309  1.00 13.52           O  
HETATM 1200  O   HOH A 299       0.238  20.688  18.765  1.00 14.60           O  
HETATM 1201  O   HOH A 300       2.064   0.775  35.074  1.00 21.47           O  
CONECT   53 1020                                                                
CONECT  243  919                                                                
CONECT  534  642                                                                
CONECT  612  738                                                                
CONECT  642  534                                                                
CONECT  738  612                                                                
CONECT  919  243                                                                
CONECT 1020   53                                                                
MASTER      367    0    1    8    2    0    2    6 1200    1    8   10          
END                                                                             
