path: root/plip/test/pdb/1vfy.pdb

HEADER    TRANSPORT PROTEIN                       26-APR-99   1VFY              
TITLE     PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE DOMAIN OF               
TITLE    2 VPS27P PROTEIN FROM SACCHAROMYCES CEREVISIAE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE              
COMPND   3 DOMAIN OF PROTEIN VPS27;                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: 163-229, FYVE DOMAIN;                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 CELLULAR_LOCATION: CYTOPLASM, ENDOSOMAL MEMBRANES;                   
SOURCE   6 GENE: VPS27;                                                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VARIANT: DE3;                                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    FYVE DOMAIN, ENDOSOME MATURATION, INTRACELLULAR TRAFFICKING,          
KEYWDS   2 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.HURLEY,S.MISRA                                                    
REVDAT   4   24-FEB-09 1VFY    1       VERSN                                    
REVDAT   3   25-NOV-03 1VFY    1       SOURCE JRNL   REMARK MASTER              
REVDAT   2   22-DEC-99 1VFY    1       JRNL   HEADER DBREF                      
REVDAT   1   06-MAY-99 1VFY    0                                                
JRNL        AUTH   S.MISRA,J.H.HURLEY                                           
JRNL        TITL   CRYSTAL STRUCTURE OF A PHOSPHATIDYLINOSITOL                  
JRNL        TITL 2 3-PHOSPHATE-SPECIFIC MEMBRANE-TARGETING MOTIF, THE           
JRNL        TITL 3 FYVE DOMAIN OF VPS27P.                                       
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  97   657 1999              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   10367894                                                     
JRNL        DOI    10.1016/S0092-8674(00)80776-X                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.5                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 20972                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 977                             
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1609                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE                    : 0.2480                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 67                           
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            : 532                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 109                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11900                                              
REMARK   3    B22 (A**2) : 0.78600                                              
REMARK   3    B33 (A**2) : -0.90000                                             
REMARK   3    B12 (A**2) : 0.17600                                              
REMARK   3    B13 (A**2) : 0.53700                                              
REMARK   3    B23 (A**2) : 1.79500                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.12                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.08                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.13                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.07                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.77                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.03                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.570 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.200 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.430 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.860 ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.41                                                 
REMARK   3   BSOL        : 46.40                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : PARAM19.ION                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : GENERATE_9.MTF                                 
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1VFY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000947.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2830,1.2822,1.2320               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20972                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.01100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M            
REMARK 280  SODIUM ACETATE PH 4.6, 15% PEG 4000, PH 5.6                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   163                                                      
REMARK 465     SER A   164                                                      
REMARK 465     LYS A   165                                                      
REMARK 465     THR A   166                                                      
REMARK 465     PRO A   167                                                      
REMARK 465     ALA A   168                                                      
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   OG   SER A   173     O    HOH A    10              1.91            
REMARK 500   O    HOH A    48     O    HOH A   103              1.94            
REMARK 500   O    HOH A    79     O    HOH A    94              2.08            
REMARK 500   O    HOH A     9     O    HOH A    42              2.08            
REMARK 500   OD1  ASP A   223     O    HOH A    31              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A    59     O    HOH A    60     1445     2.05            
REMARK 500   O    HOH A     1     O    HOH A     6     1455     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 187       83.91   -154.10                                   
REMARK 500    SER A 204       44.21   -152.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  48        DISTANCE =  5.05 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 176   SG                                                     
REMARK 620 2 CYS A 179   SG  108.2                                              
REMARK 620 3 CYS A 200   SG  113.2 115.8                                        
REMARK 620 4 HIS A 203   ND1 114.1 109.1  96.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 192   SG                                                     
REMARK 620 2 CYS A 195   SG  103.6                                              
REMARK 620 3 CYS A 222   SG  115.6 116.2                                        
REMARK 620 4 CYS A 225   SG  106.1 112.8 102.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ZNA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ZINC ION A LIGANDING RESIDUES                      
REMARK 800 SITE_IDENTIFIER: ZNB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ZINC ION B LIGANDING RESIDUES                      
REMARK 800 SITE_IDENTIFIER: POS                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RKHHCR MOTIF ; PUTATIVE PI3P BINDING SITE          
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301                  
DBREF  1VFY A  163   230  UNP    P40343   VPS27_YEAST    163    230             
SEQADV 1VFY GLU A  230  UNP  P40343    ASP   230 ENGINEERED                     
SEQRES   1 A   73  ASP SER LYS THR PRO ALA ASP TRP ILE ASP SER ASP ALA          
SEQRES   2 A   73  CYS MET ILE CYS SER LYS LYS PHE SER LEU LEU ASN ARG          
SEQRES   3 A   73  LYS HIS HIS CYS ARG SER CYS GLY GLY VAL PHE CYS GLN          
SEQRES   4 A   73  GLU HIS SER SER ASN SER ILE PRO LEU PRO ASP LEU GLY          
SEQRES   5 A   73  ILE TYR GLU PRO VAL ARG VAL CYS ASP SER CYS PHE GLU          
SEQRES   6 A   73  ASP TYR GLU PHE ILE VAL THR ASP                              
HET     ZN  A 300       1                                                       
HET     ZN  A 301       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    2(ZN 2+)                                                     
FORMUL   4  HOH   *109(H2 O)                                                    
HELIX    1   1 GLN A  201  HIS A  203  5                                   3    
HELIX    2   2 PRO A  211  LEU A  213  5                                   3    
HELIX    3   3 ASP A  223  VAL A  233  1                                  11    
SHEET    1   A 2 ASN A 206  ILE A 208  0                                        
SHEET    2   A 2 VAL A 219  VAL A 221 -1  N  VAL A 221   O  ASN A 206           
LINK         SG  CYS A 176                ZN    ZN A 301     1555   1555  2.34  
LINK         SG  CYS A 179                ZN    ZN A 301     1555   1555  2.31  
LINK         SG  CYS A 192                ZN    ZN A 300     1555   1555  2.37  
LINK         SG  CYS A 195                ZN    ZN A 300     1555   1555  2.37  
LINK         SG  CYS A 200                ZN    ZN A 301     1555   1555  2.33  
LINK         ND1 HIS A 203                ZN    ZN A 301     1555   1555  2.14  
LINK         SG  CYS A 222                ZN    ZN A 300     1555   1555  2.33  
LINK         SG  CYS A 225                ZN    ZN A 300     1555   1555  2.35  
SITE     1 ZNA  4 CYS A 176  CYS A 179  CYS A 200  HIS A 203                    
SITE     1 ZNB  4 CYS A 192  CYS A 195  CYS A 222  CYS A 225                    
SITE     1 POS  7 ARG A 188  LYS A 189  HIS A 190  HIS A 191                    
SITE     2 POS  7 CYS A 192  ARG A 193  ARG A 220                               
SITE     1 AC1  4 CYS A 192  CYS A 195  CYS A 222  CYS A 225                    
SITE     1 AC2  4 CYS A 176  CYS A 179  CYS A 200  HIS A 203                    
CRYST1   24.090   26.570   31.610 111.79  92.70 105.70 P 1           1          
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      0.041511  0.011668  0.007217        0.00000                         
SCALE2      0.000000  0.039095  0.017026        0.00000                         
SCALE3      0.000000  0.000000  0.034544        0.00000                         
ATOM      1  N   ASP A 169       7.887  17.852  47.781  1.00 18.09           N  
ATOM      2  CA  ASP A 169       9.275  17.917  47.212  1.00 16.84           C  
ATOM      3  C   ASP A 169       9.383  17.094  45.931  1.00  9.03           C  
ATOM      4  O   ASP A 169       9.425  17.684  44.892  1.00 12.14           O  
ATOM      5  CB  ASP A 169      10.316  17.476  48.223  1.00 27.95           C  
ATOM      6  CG  ASP A 169      11.709  17.957  47.846  1.00 25.30           C  
ATOM      7  OD1 ASP A 169      11.867  19.181  47.597  1.00 30.03           O  
ATOM      8  OD2 ASP A 169      12.634  17.118  47.800  1.00 37.73           O  
ATOM      9  N   TRP A 170       9.435  15.768  45.983  1.00  9.21           N  
ATOM     10  CA  TRP A 170       9.470  15.019  44.727  1.00  7.79           C  
ATOM     11  C   TRP A 170       8.087  14.982  44.070  1.00  8.32           C  
ATOM     12  O   TRP A 170       7.047  14.927  44.756  1.00  8.38           O  
ATOM     13  CB  TRP A 170       9.950  13.593  44.982  1.00  9.26           C  
ATOM     14  CG  TRP A 170      11.423  13.433  45.264  1.00  8.90           C  
ATOM     15  CD1 TRP A 170      12.286  14.383  45.694  1.00 11.52           C  
ATOM     16  CD2 TRP A 170      12.185  12.220  45.141  1.00  9.02           C  
ATOM     17  NE1 TRP A 170      13.556  13.840  45.853  1.00 11.26           N  
ATOM     18  CE2 TRP A 170      13.511  12.519  45.521  1.00 10.65           C  
ATOM     19  CE3 TRP A 170      11.867  10.920  44.748  1.00 13.23           C  
ATOM     20  CZ2 TRP A 170      14.521  11.557  45.523  1.00 11.59           C  
ATOM     21  CZ3 TRP A 170      12.866   9.967  44.750  1.00 14.05           C  
ATOM     22  CH2 TRP A 170      14.180  10.293  45.137  1.00 11.18           C  
ATOM     23  N   ILE A 171       8.064  15.036  42.737  1.00  6.81           N  
ATOM     24  CA  ILE A 171       6.823  14.892  41.990  1.00  6.58           C  
ATOM     25  C   ILE A 171       6.959  13.578  41.212  1.00  6.19           C  
ATOM     26  O   ILE A 171       7.948  12.869  41.370  1.00  7.51           O  
ATOM     27  CB  ILE A 171       6.571  16.073  41.029  1.00  6.25           C  
ATOM     28  CG1 ILE A 171       7.744  16.256  40.070  1.00  8.25           C  
ATOM     29  CG2 ILE A 171       6.370  17.358  41.848  1.00  8.23           C  
ATOM     30  CD1 ILE A 171       7.453  17.222  38.943  1.00 19.47           C  
ATOM     31  N   ASP A 172       5.959  13.227  40.420  1.00  6.16           N  
ATOM     32  CA  ASP A 172       6.070  12.058  39.570  1.00  6.80           C  
ATOM     33  C   ASP A 172       5.394  12.348  38.230  1.00  6.37           C  
ATOM     34  O   ASP A 172       4.529  13.235  38.082  1.00  6.23           O  
ATOM     35  CB  ASP A 172       5.421  10.837  40.227  1.00  7.86           C  
ATOM     36  CG  ASP A 172       6.051   9.523  39.789  1.00 14.11           C  
ATOM     37  OD1 ASP A 172       6.906   9.481  38.861  1.00  9.81           O  
ATOM     38  OD2 ASP A 172       5.674   8.503  40.397  1.00 17.66           O  
ATOM     39  N   SER A 173       5.862  11.615  37.217  1.00  6.83           N  
ATOM     40  CA  SER A 173       5.280  11.702  35.884  1.00  8.03           C  
ATOM     41  C   SER A 173       5.711  10.463  35.128  1.00  8.71           C  
ATOM     42  O   SER A 173       6.599   9.708  35.580  1.00  8.86           O  
ATOM     43  CB  SER A 173       5.771  12.935  35.149  1.00  7.20           C  
ATOM     44  OG  SER A 173       5.046  13.081  33.951  1.00 12.07           O  
ATOM     45  N   ASP A 174       5.049  10.238  33.998  1.00  8.89           N  
ATOM     46  CA  ASP A 174       5.382   9.096  33.161  1.00  9.00           C  
ATOM     47  C   ASP A 174       6.435   9.383  32.084  1.00  8.66           C  
ATOM     48  O   ASP A 174       6.805   8.462  31.332  1.00  8.74           O  
ATOM     49  CB  ASP A 174       4.104   8.504  32.542  1.00 12.61           C  
ATOM     50  CG  ASP A 174       3.421   9.435  31.592  1.00 12.82           C  
ATOM     51  OD1 ASP A 174       3.852  10.580  31.399  1.00 18.53           O  
ATOM     52  OD2 ASP A 174       2.401   8.986  31.015  1.00 21.51           O  
ATOM     53  N   ALA A 175       6.937  10.609  32.011  1.00  9.08           N  
ATOM     54  CA  ALA A 175       7.913  10.948  30.983  1.00  8.25           C  
ATOM     55  C   ALA A 175       8.933  11.944  31.505  1.00  8.05           C  
ATOM     56  O   ALA A 175       8.689  12.666  32.472  1.00  7.53           O  
ATOM     57  CB  ALA A 175       7.177  11.526  29.749  1.00 10.62           C  
ATOM     58  N   CYS A 176      10.092  11.966  30.872  1.00  7.64           N  
ATOM     59  CA  CYS A 176      11.168  12.872  31.233  1.00  7.20           C  
ATOM     60  C   CYS A 176      10.713  14.313  31.069  1.00  8.99           C  
ATOM     61  O   CYS A 176      10.135  14.684  30.029  1.00 10.70           O  
ATOM     62  CB  CYS A 176      12.381  12.628  30.348  1.00  7.60           C  
ATOM     63  SG  CYS A 176      13.775  13.781  30.615  1.00  8.16           S  
ATOM     64  N   MET A 177      10.985  15.140  32.068  1.00  9.14           N  
ATOM     65  CA  MET A 177      10.564  16.540  32.001  1.00  9.57           C  
ATOM     66  C   MET A 177      11.317  17.351  30.943  1.00 13.74           C  
ATOM     67  O   MET A 177      10.811  18.401  30.493  1.00 16.85           O  
ATOM     68  CB  MET A 177      10.722  17.186  33.370  1.00 11.73           C  
ATOM     69  CG  MET A 177       9.740  16.636  34.349  1.00 11.14           C  
ATOM     70  SD  MET A 177       9.932  17.448  35.905  1.00 13.67           S  
ATOM     71  CE  MET A 177       8.653  18.685  35.787  1.00 20.85           C  
ATOM     72  N   ILE A 178      12.476  16.871  30.510  1.00 12.91           N  
ATOM     73  CA  ILE A 178      13.226  17.597  29.501  1.00 12.63           C  
ATOM     74  C   ILE A 178      12.849  17.148  28.093  1.00 14.40           C  
ATOM     75  O   ILE A 178      12.416  17.967  27.262  1.00 17.65           O  
ATOM     76  CB  ILE A 178      14.747  17.406  29.697  1.00 14.99           C  
ATOM     77  CG1 ILE A 178      15.209  18.079  30.993  1.00 14.19           C  
ATOM     78  CG2 ILE A 178      15.515  17.961  28.499  1.00 17.45           C  
ATOM     79  CD1 ILE A 178      14.840  19.529  31.101  1.00 19.37           C  
ATOM     80  N   CYS A 179      12.942  15.853  27.825  1.00 11.66           N  
ATOM     81  CA  CYS A 179      12.671  15.379  26.478  1.00 11.05           C  
ATOM     82  C   CYS A 179      11.329  14.755  26.190  1.00 13.12           C  
ATOM     83  O   CYS A 179      11.034  14.414  25.035  1.00 15.44           O  
ATOM     84  CB  CYS A 179      13.773  14.423  26.033  1.00 12.68           C  
ATOM     85  SG  CYS A 179      13.873  12.870  26.965  1.00 10.34           S  
ATOM     86  N   SER A 180      10.526  14.573  27.235  1.00 11.13           N  
ATOM     87  CA  SER A 180       9.192  14.025  27.113  1.00 11.84           C  
ATOM     88  C   SER A 180       9.095  12.577  26.657  1.00 12.02           C  
ATOM     89  O   SER A 180       8.015  12.107  26.339  1.00 13.89           O  
ATOM     90  CB  SER A 180       8.345  14.922  26.202  1.00 16.99           C  
ATOM     91  OG  SER A 180       8.156  16.212  26.770  1.00 21.08           O  
ATOM     92  N   LYS A 181      10.210  11.858  26.652  1.00 10.20           N  
ATOM     93  CA  LYS A 181      10.192  10.450  26.293  1.00 11.65           C  
ATOM     94  C   LYS A 181       9.590   9.691  27.476  1.00  9.55           C  
ATOM     95  O   LYS A 181       9.858   9.985  28.659  1.00  9.53           O  
ATOM     96  CB  LYS A 181      11.604   9.965  25.955  1.00  9.48           C  
ATOM     97  CG  LYS A 181      12.081  10.520  24.621  1.00 12.97           C  
ATOM     98  CD  LYS A 181      13.459  10.040  24.235  1.00 12.13           C  
ATOM     99  CE  LYS A 181      13.906  10.713  22.946  1.00 16.33           C  
ATOM    100  NZ  LYS A 181      15.240  10.221  22.553  1.00 22.59           N  
ATOM    101  N   LYS A 182       8.725   8.730  27.176  1.00  9.30           N  
ATOM    102  CA  LYS A 182       8.048   7.972  28.215  1.00  8.67           C  
ATOM    103  C   LYS A 182       8.927   6.913  28.832  1.00  8.04           C  
ATOM    104  O   LYS A 182       9.632   6.185  28.127  1.00  8.12           O  
ATOM    105  CB  LYS A 182       6.799   7.328  27.627  1.00 10.54           C  
ATOM    106  CG  LYS A 182       5.923   6.600  28.633  1.00 17.74           C  
ATOM    107  CD  LYS A 182       4.713   5.968  27.956  1.00 19.68           C  
ATOM    108  CE  LYS A 182       3.414   6.352  28.633  1.00 30.63           C  
ATOM    109  NZ  LYS A 182       3.262   5.658  29.931  1.00 33.39           N  
ATOM    110  N   PHE A 183       8.892   6.813  30.148  1.00  8.01           N  
ATOM    111  CA  PHE A 183       9.743   5.843  30.810  1.00  6.91           C  
ATOM    112  C   PHE A 183       9.273   4.420  30.583  1.00  8.20           C  
ATOM    113  O   PHE A 183       8.076   4.180  30.483  1.00  9.02           O  
ATOM    114  CB  PHE A 183       9.791   6.106  32.322  1.00  7.34           C  
ATOM    115  CG  PHE A 183      10.256   7.487  32.681  1.00  7.05           C  
ATOM    116  CD1 PHE A 183      11.533   7.918  32.317  1.00  6.60           C  
ATOM    117  CD2 PHE A 183       9.440   8.347  33.409  1.00  8.01           C  
ATOM    118  CE1 PHE A 183      11.980   9.176  32.677  1.00  6.91           C  
ATOM    119  CE2 PHE A 183       9.885   9.609  33.779  1.00  8.15           C  
ATOM    120  CZ  PHE A 183      11.139  10.014  33.417  1.00  7.28           C  
ATOM    121  N   SER A 184      10.218   3.479  30.552  1.00  7.75           N  
ATOM    122  CA  SER A 184       9.883   2.061  30.422  1.00  6.79           C  
ATOM    123  C   SER A 184      11.102   1.326  30.968  1.00  7.40           C  
ATOM    124  O   SER A 184      12.081   1.951  31.390  1.00  8.09           O  
ATOM    125  CB  SER A 184       9.669   1.689  28.946  1.00 10.99           C  
ATOM    126  OG  SER A 184      10.916   1.500  28.305  1.00 13.91           O  
ATOM    127  N   LEU A 185      11.071  -0.004  30.973  1.00  8.27           N  
ATOM    128  CA  LEU A 185      12.231  -0.730  31.442  1.00  8.66           C  
ATOM    129  C   LEU A 185      13.480  -0.419  30.621  1.00  9.88           C  
ATOM    130  O   LEU A 185      14.588  -0.579  31.135  1.00 10.97           O  
ATOM    131  CB  LEU A 185      11.981  -2.241  31.434  1.00 11.19           C  
ATOM    132  CG  LEU A 185      10.889  -2.724  32.390  1.00 11.54           C  
ATOM    133  CD1 LEU A 185      10.739  -4.242  32.270  1.00 15.41           C  
ATOM    134  CD2 LEU A 185      11.252  -2.305  33.792  1.00 15.29           C  
ATOM    135  N   LEU A 186      13.304  -0.008  29.366  1.00  8.63           N  
ATOM    136  CA  LEU A 186      14.443   0.329  28.499  1.00  9.63           C  
ATOM    137  C   LEU A 186      14.871   1.809  28.587  1.00 10.10           C  
ATOM    138  O   LEU A 186      15.825   2.219  27.914  1.00 12.23           O  
ATOM    139  CB  LEU A 186      14.133  -0.022  27.037  1.00 10.62           C  
ATOM    140  CG  LEU A 186      13.939  -1.521  26.756  1.00 15.06           C  
ATOM    141  CD1 LEU A 186      13.636  -1.725  25.265  1.00 17.75           C  
ATOM    142  CD2 LEU A 186      15.184  -2.289  27.131  1.00 19.92           C  
ATOM    143  N   ASN A 187      14.141   2.622  29.358  1.00  8.14           N  
ATOM    144  CA  ASN A 187      14.519   4.031  29.571  1.00  8.00           C  
ATOM    145  C   ASN A 187      13.891   4.355  30.926  1.00  6.44           C  
ATOM    146  O   ASN A 187      12.786   4.892  31.037  1.00  7.18           O  
ATOM    147  CB  ASN A 187      13.974   4.923  28.470  1.00 10.02           C  
ATOM    148  CG  ASN A 187      14.668   6.263  28.418  1.00  9.47           C  
ATOM    149  OD1 ASN A 187      15.743   6.442  29.015  1.00  9.22           O  
ATOM    150  ND2 ASN A 187      14.075   7.210  27.708  1.00  9.23           N  
ATOM    151  N   ARG A 188      14.611   4.006  31.964  1.00  6.62           N  
ATOM    152  CA  ARG A 188      14.054   4.089  33.300  1.00  6.70           C  
ATOM    153  C   ARG A 188      13.879   5.474  33.875  1.00  6.00           C  
ATOM    154  O   ARG A 188      14.545   6.433  33.489  1.00  6.97           O  
ATOM    155  CB  ARG A 188      14.881   3.229  34.244  1.00  8.55           C  
ATOM    156  CG  ARG A 188      14.754   1.760  33.905  1.00 11.77           C  
ATOM    157  CD  ARG A 188      15.620   0.938  34.737  1.00 20.30           C  
ATOM    158  NE  ARG A 188      15.479  -0.474  34.392  1.00 20.56           N  
ATOM    159  CZ  ARG A 188      15.283  -1.412  35.300  1.00 11.56           C  
ATOM    160  NH1 ARG A 188      15.198  -1.069  36.574  1.00 11.90           N  
ATOM    161  NH2 ARG A 188      15.205  -2.687  34.933  1.00 12.54           N  
ATOM    162  N   LYS A 189      12.944   5.556  34.809  1.00  7.40           N  
ATOM    163  CA  LYS A 189      12.623   6.784  35.518  1.00  6.72           C  
ATOM    164  C   LYS A 189      13.672   7.112  36.589  1.00  6.05           C  
ATOM    165  O   LYS A 189      14.161   6.217  37.284  1.00  8.03           O  
ATOM    166  CB  LYS A 189      11.275   6.591  36.206  1.00  6.93           C  
ATOM    167  CG  LYS A 189      10.811   7.762  37.069  1.00  8.19           C  
ATOM    168  CD  LYS A 189       9.445   7.466  37.712  1.00 10.43           C  
ATOM    169  CE  LYS A 189       8.328   7.361  36.690  1.00  9.20           C  
ATOM    170  NZ  LYS A 189       7.009   7.114  37.366  1.00 10.16           N  
ATOM    171  N   HIS A 190      14.000   8.399  36.714  1.00  6.00           N  
ATOM    172  CA  HIS A 190      14.900   8.816  37.780  1.00  5.54           C  
ATOM    173  C   HIS A 190      14.474  10.173  38.308  1.00  5.57           C  
ATOM    174  O   HIS A 190      14.035  11.037  37.549  1.00  9.33           O  
ATOM    175  CB  HIS A 190      16.334   8.958  37.295  1.00  7.15           C  
ATOM    176  CG  HIS A 190      16.897   7.719  36.696  1.00  7.28           C  
ATOM    177  ND1 HIS A 190      17.297   6.648  37.460  1.00  9.42           N  
ATOM    178  CD2 HIS A 190      17.080   7.374  35.405  1.00  7.67           C  
ATOM    179  CE1 HIS A 190      17.704   5.683  36.652  1.00  7.62           C  
ATOM    180  NE2 HIS A 190      17.586   6.094  35.401  1.00  8.78           N  
ATOM    181  N   HIS A 191      14.614  10.377  39.601  1.00  4.89           N  
ATOM    182  CA  HIS A 191      14.353  11.682  40.178  1.00  6.19           C  
ATOM    183  C   HIS A 191      15.638  12.493  40.362  1.00  5.59           C  
ATOM    184  O   HIS A 191      16.706  11.944  40.690  1.00  5.56           O  
ATOM    185  CB  HIS A 191      13.717  11.523  41.574  1.00  5.97           C  
ATOM    186  CG  HIS A 191      12.261  11.206  41.540  1.00  5.68           C  
ATOM    187  ND1 HIS A 191      11.764   9.921  41.395  1.00  7.63           N  
ATOM    188  CD2 HIS A 191      11.184  12.028  41.592  1.00  7.42           C  
ATOM    189  CE1 HIS A 191      10.443   9.977  41.355  1.00  8.67           C  
ATOM    190  NE2 HIS A 191      10.068  11.239  41.470  1.00  7.81           N  
ATOM    191  N   CYS A 192      15.514  13.808  40.191  1.00  4.92           N  
ATOM    192  CA  CYS A 192      16.589  14.741  40.535  1.00  4.78           C  
ATOM    193  C   CYS A 192      16.465  14.967  42.058  1.00  4.40           C  
ATOM    194  O   CYS A 192      15.407  15.370  42.557  1.00  5.76           O  
ATOM    195  CB  CYS A 192      16.397  16.066  39.824  1.00  4.98           C  
ATOM    196  SG  CYS A 192      17.613  17.288  40.404  1.00  4.80           S  
ATOM    197  N   ARG A 193      17.526  14.697  42.797  1.00  4.69           N  
ATOM    198  CA  ARG A 193      17.500  14.873  44.255  1.00  5.24           C  
ATOM    199  C   ARG A 193      17.494  16.342  44.669  1.00  5.44           C  
ATOM    200  O   ARG A 193      17.176  16.659  45.828  1.00  6.02           O  
ATOM    201  CB  ARG A 193      18.682  14.161  44.895  1.00  5.16           C  
ATOM    202  CG  ARG A 193      18.431  12.666  45.167  1.00  7.17           C  
ATOM    203  CD  ARG A 193      18.151  11.832  43.909  1.00  6.74           C  
ATOM    204  NE  ARG A 193      18.053  10.430  44.323  1.00  7.72           N  
ATOM    205  CZ  ARG A 193      17.702   9.417  43.542  1.00  8.79           C  
ATOM    206  NH1 ARG A 193      17.399   9.625  42.278  1.00  7.49           N  
ATOM    207  NH2 ARG A 193      17.677   8.171  44.015  1.00  9.31           N  
ATOM    208  N   SER A 194      17.827  17.243  43.765  1.00  4.70           N  
ATOM    209  CA  SER A 194      17.793  18.669  44.065  1.00  6.19           C  
ATOM    210  C   SER A 194      16.403  19.299  43.831  1.00  6.12           C  
ATOM    211  O   SER A 194      15.860  19.927  44.758  1.00  9.35           O  
ATOM    212  CB  SER A 194      18.827  19.396  43.206  1.00  6.78           C  
ATOM    213  OG  SER A 194      18.754  20.809  43.306  1.00 10.28           O  
ATOM    214  N   CYS A 195      15.822  19.120  42.647  1.00  4.94           N  
ATOM    215  CA  CYS A 195      14.548  19.773  42.362  1.00  6.16           C  
ATOM    216  C   CYS A 195      13.337  18.859  42.468  1.00  5.23           C  
ATOM    217  O   CYS A 195      12.189  19.354  42.456  1.00  6.66           O  
ATOM    218  CB  CYS A 195      14.599  20.464  40.980  1.00  6.83           C  
ATOM    219  SG  CYS A 195      14.589  19.297  39.585  1.00  6.21           S  
ATOM    220  N   GLY A 196      13.529  17.551  42.571  1.00  5.90           N  
ATOM    221  CA  GLY A 196      12.401  16.631  42.723  1.00  5.92           C  
ATOM    222  C   GLY A 196      11.716  16.198  41.438  1.00  5.44           C  
ATOM    223  O   GLY A 196      10.791  15.389  41.515  1.00  5.76           O  
ATOM    224  N   GLY A 197      12.133  16.750  40.300  1.00  5.70           N  
ATOM    225  CA  GLY A 197      11.555  16.365  39.023  1.00  5.61           C  
ATOM    226  C   GLY A 197      11.966  14.961  38.589  1.00  4.52           C  
ATOM    227  O   GLY A 197      12.816  14.322  39.215  1.00  5.68           O  
ATOM    228  N   VAL A 198      11.352  14.481  37.510  1.00  5.96           N  
ATOM    229  CA  VAL A 198      11.698  13.163  36.929  1.00  6.50           C  
ATOM    230  C   VAL A 198      12.323  13.335  35.556  1.00  5.98           C  
ATOM    231  O   VAL A 198      11.875  14.164  34.752  1.00  5.85           O  
ATOM    232  CB  VAL A 198      10.505  12.178  36.828  1.00  7.47           C  
ATOM    233  CG1 VAL A 198      10.093  11.729  38.233  1.00  8.92           C  
ATOM    234  CG2 VAL A 198       9.344  12.805  36.069  1.00  9.54           C  
ATOM    235  N   PHE A 199      13.373  12.544  35.337  1.00  6.09           N  
ATOM    236  CA  PHE A 199      14.215  12.666  34.158  1.00  5.07           C  
ATOM    237  C   PHE A 199      14.705  11.311  33.702  1.00  6.37           C  
ATOM    238  O   PHE A 199      14.787  10.373  34.481  1.00  6.55           O  
ATOM    239  CB  PHE A 199      15.463  13.534  34.481  1.00  5.84           C  
ATOM    240  CG  PHE A 199      15.102  14.888  35.014  1.00  5.33           C  
ATOM    241  CD1 PHE A 199      14.893  15.091  36.361  1.00  6.65           C  
ATOM    242  CD2 PHE A 199      14.887  15.928  34.151  1.00  7.26           C  
ATOM    243  CE1 PHE A 199      14.468  16.337  36.834  1.00  5.10           C  
ATOM    244  CE2 PHE A 199      14.465  17.167  34.600  1.00  6.90           C  
ATOM    245  CZ  PHE A 199      14.257  17.382  35.928  1.00  5.44           C  
ATOM    246  N   CYS A 200      15.012  11.210  32.410  1.00  6.92           N  
ATOM    247  CA  CYS A 200      15.636   9.997  31.899  1.00  7.08           C  
ATOM    248  C   CYS A 200      17.154  10.081  32.252  1.00  5.98           C  
ATOM    249  O   CYS A 200      17.669  11.131  32.691  1.00  7.16           O  
ATOM    250  CB  CYS A 200      15.461   9.893  30.381  1.00  8.39           C  
ATOM    251  SG  CYS A 200      16.399  11.158  29.437  1.00  8.01           S  
ATOM    252  N   GLN A 201      17.878   8.990  32.048  1.00  6.29           N  
ATOM    253  CA  GLN A 201      19.307   8.936  32.312  1.00  6.48           C  
ATOM    254  C   GLN A 201      20.071   9.990  31.514  1.00  7.08           C  
ATOM    255  O   GLN A 201      20.979  10.643  32.033  1.00  7.26           O  
ATOM    256  CB  GLN A 201      19.836   7.546  31.945  1.00  7.79           C  
ATOM    257  CG  GLN A 201      21.333   7.442  31.839  1.00  9.51           C  
ATOM    258  CD  GLN A 201      22.009   7.655  33.164  1.00 15.44           C  
ATOM    259  OE1 GLN A 201      21.452   7.354  34.218  1.00 16.08           O  
ATOM    260  NE2 GLN A 201      23.245   8.162  33.115  1.00 20.70           N  
ATOM    261  N   GLU A 202      19.704  10.166  30.242  1.00  7.64           N  
ATOM    262  CA  GLU A 202      20.428  11.109  29.418  1.00  8.07           C  
ATOM    263  C   GLU A 202      20.371  12.524  29.992  1.00  9.70           C  
ATOM    264  O   GLU A 202      21.287  13.325  29.790  1.00  9.52           O  
ATOM    265  CB  GLU A 202      19.851  11.115  27.996  1.00 10.33           C  
ATOM    266  CG  GLU A 202      20.456  12.216  27.150  1.00 15.22           C  
ATOM    267  CD  GLU A 202      19.934  12.247  25.732  1.00 33.14           C  
ATOM    268  OE1 GLU A 202      18.876  11.636  25.453  1.00 31.48           O  
ATOM    269  OE2 GLU A 202      20.584  12.903  24.893  1.00 32.73           O  
ATOM    270  N   HIS A 203      19.292  12.833  30.689  1.00  7.27           N  
ATOM    271  CA  HIS A 203      19.122  14.162  31.255  1.00  8.16           C  
ATOM    272  C   HIS A 203      19.338  14.252  32.749  1.00  6.38           C  
ATOM    273  O   HIS A 203      18.951  15.245  33.372  1.00  9.47           O  
ATOM    274  CB  HIS A 203      17.759  14.696  30.817  1.00  8.73           C  
ATOM    275  CG  HIS A 203      17.713  14.942  29.344  1.00  9.72           C  
ATOM    276  ND1 HIS A 203      16.830  14.317  28.492  1.00  9.67           N  
ATOM    277  CD2 HIS A 203      18.555  15.650  28.557  1.00 11.61           C  
ATOM    278  CE1 HIS A 203      17.135  14.617  27.243  1.00 11.04           C  
ATOM    279  NE2 HIS A 203      18.179  15.424  27.253  1.00 12.67           N  
ATOM    280  N   SER A 204      19.963  13.230  33.321  1.00  6.12           N  
ATOM    281  CA  SER A 204      20.293  13.245  34.757  1.00  6.19           C  
ATOM    282  C   SER A 204      21.522  12.373  34.971  1.00  5.78           C  
ATOM    283  O   SER A 204      21.598  11.623  35.936  1.00  7.37           O  
ATOM    284  CB  SER A 204      19.103  12.762  35.607  1.00  7.84           C  
ATOM    285  OG  SER A 204      18.711  11.423  35.322  1.00  7.26           O  
ATOM    286  N   SER A 205      22.522  12.523  34.095  1.00  7.49           N  
ATOM    287  CA  SER A 205      23.716  11.677  34.166  1.00  7.15           C  
ATOM    288  C   SER A 205      24.779  12.097  35.162  1.00  7.74           C  
ATOM    289  O   SER A 205      25.709  11.333  35.427  1.00  8.58           O  
ATOM    290  CB  SER A 205      24.347  11.526  32.784  1.00 10.72           C  
ATOM    291  OG  SER A 205      24.971  12.726  32.397  1.00 11.89           O  
ATOM    292  N   ASN A 206      24.637  13.294  35.743  1.00  6.46           N  
ATOM    293  CA  ASN A 206      25.594  13.797  36.713  1.00  5.65           C  
ATOM    294  C   ASN A 206      25.043  13.648  38.132  1.00  6.69           C  
ATOM    295  O   ASN A 206      23.810  13.556  38.338  1.00  6.77           O  
ATOM    296  CB  ASN A 206      25.859  15.264  36.420  1.00  7.05           C  
ATOM    297  CG  ASN A 206      26.380  15.479  35.026  1.00  7.24           C  
ATOM    298  OD1 ASN A 206      27.521  15.119  34.732  1.00  9.78           O  
ATOM    299  ND2 ASN A 206      25.553  16.050  34.147  1.00 10.03           N  
ATOM    300  N   SER A 207      25.952  13.637  39.111  1.00  6.08           N  
ATOM    301  CA  SER A 207      25.583  13.544  40.516  1.00  4.83           C  
ATOM    302  C   SER A 207      26.427  14.511  41.300  1.00  5.78           C  
ATOM    303  O   SER A 207      27.626  14.673  41.006  1.00  7.25           O  
ATOM    304  CB  SER A 207      25.834  12.145  41.012  1.00  6.53           C  
ATOM    305  OG  SER A 207      25.074  11.210  40.255  1.00  8.56           O  
ATOM    306  N   ILE A 208      25.824  15.100  42.332  1.00  5.60           N  
ATOM    307  CA  ILE A 208      26.504  16.089  43.148  1.00  4.63           C  
ATOM    308  C   ILE A 208      26.089  15.936  44.583  1.00  5.01           C  
ATOM    309  O   ILE A 208      25.024  15.364  44.880  1.00  5.60           O  
ATOM    310  CB  ILE A 208      26.104  17.548  42.731  1.00  5.10           C  
ATOM    311  CG1 ILE A 208      24.594  17.781  42.945  1.00  6.03           C  
ATOM    312  CG2 ILE A 208      26.512  17.825  41.277  1.00  7.43           C  
ATOM    313  CD1 ILE A 208      24.116  19.228  42.571  1.00  6.71           C  
ATOM    314  N   PRO A 209      26.916  16.401  45.520  1.00  5.64           N  
ATOM    315  CA  PRO A 209      26.506  16.325  46.932  1.00  5.65           C  
ATOM    316  C   PRO A 209      25.472  17.445  47.082  1.00  5.32           C  
ATOM    317  O   PRO A 209      25.426  18.382  46.273  1.00  5.95           O  
ATOM    318  CB  PRO A 209      27.790  16.654  47.692  1.00  6.79           C  
ATOM    319  CG  PRO A 209      28.525  17.578  46.750  1.00  8.95           C  
ATOM    320  CD  PRO A 209      28.257  16.999  45.369  1.00  5.75           C  
ATOM    321  N   LEU A 210      24.637  17.372  48.118  1.00  5.58           N  
ATOM    322  CA  LEU A 210      23.647  18.418  48.413  1.00  6.47           C  
ATOM    323  C   LEU A 210      23.807  18.731  49.910  1.00  7.39           C  
ATOM    324  O   LEU A 210      23.000  18.314  50.736  1.00  6.81           O  
ATOM    325  CB  LEU A 210      22.223  17.946  48.090  1.00  6.55           C  
ATOM    326  CG  LEU A 210      21.997  17.622  46.608  1.00  6.51           C  
ATOM    327  CD1 LEU A 210      20.619  16.974  46.457  1.00  9.27           C  
ATOM    328  CD2 LEU A 210      22.111  18.873  45.778  1.00  9.96           C  
ATOM    329  N   PRO A 211      24.864  19.483  50.246  1.00  8.28           N  
ATOM    330  CA  PRO A 211      25.109  19.826  51.653  1.00 10.26           C  
ATOM    331  C   PRO A 211      23.955  20.471  52.386  1.00 12.37           C  
ATOM    332  O   PRO A 211      23.808  20.263  53.606  1.00 13.53           O  
ATOM    333  CB  PRO A 211      26.337  20.732  51.588  1.00 13.15           C  
ATOM    334  CG  PRO A 211      27.064  20.210  50.373  1.00 12.85           C  
ATOM    335  CD  PRO A 211      25.952  19.971  49.384  1.00  8.74           C  
ATOM    336  N   ASP A 212      23.129  21.240  51.677  1.00 12.83           N  
ATOM    337  CA  ASP A 212      22.001  21.910  52.322  1.00 14.71           C  
ATOM    338  C   ASP A 212      20.941  20.929  52.770  1.00 17.08           C  
ATOM    339  O   ASP A 212      20.055  21.296  53.539  1.00 21.09           O  
ATOM    340  CB  ASP A 212      21.378  22.972  51.407  1.00 22.01           C  
ATOM    341  CG  ASP A 212      22.356  24.068  51.050  1.00 35.74           C  
ATOM    342  OD1 ASP A 212      23.217  24.396  51.899  1.00 36.78           O  
ATOM    343  OD2 ASP A 212      22.260  24.607  49.923  1.00 39.62           O  
ATOM    344  N   LEU A 213      21.027  19.699  52.285  1.00 13.40           N  
ATOM    345  CA  LEU A 213      20.117  18.637  52.682  1.00 12.92           C  
ATOM    346  C   LEU A 213      20.872  17.630  53.569  1.00  8.87           C  
ATOM    347  O   LEU A 213      20.347  16.562  53.899  1.00 15.13           O  
ATOM    348  CB  LEU A 213      19.574  17.897  51.453  1.00 15.56           C  
ATOM    349  CG  LEU A 213      18.662  18.649  50.477  1.00 20.43           C  
ATOM    350  CD1 LEU A 213      18.244  17.720  49.331  1.00 18.11           C  
ATOM    351  CD2 LEU A 213      17.427  19.135  51.223  1.00 21.32           C  
ATOM    352  N   GLY A 214      22.117  17.955  53.917  1.00  9.80           N  
ATOM    353  CA  GLY A 214      22.920  17.063  54.738  1.00 10.63           C  
ATOM    354  C   GLY A 214      23.437  15.860  53.961  1.00  9.82           C  
ATOM    355  O   GLY A 214      23.757  14.850  54.565  1.00 11.16           O  
ATOM    356  N   ILE A 215      23.545  15.980  52.626  1.00  7.74           N  
ATOM    357  CA  ILE A 215      23.990  14.880  51.760  1.00  8.48           C  
ATOM    358  C   ILE A 215      25.388  15.212  51.242  1.00  7.71           C  
ATOM    359  O   ILE A 215      25.579  16.192  50.502  1.00  8.49           O  
ATOM    360  CB  ILE A 215      23.005  14.692  50.570  1.00  9.04           C  
ATOM    361  CG1 ILE A 215      21.643  14.219  51.107  1.00 11.28           C  
ATOM    362  CG2 ILE A 215      23.586  13.694  49.573  1.00 10.94           C  
ATOM    363  CD1 ILE A 215      20.528  14.198  50.052  1.00 13.32           C  
ATOM    364  N   TYR A 216      26.353  14.368  51.629  1.00  7.66           N  
ATOM    365  CA  TYR A 216      27.761  14.590  51.303  1.00  8.29           C  
ATOM    366  C   TYR A 216      28.419  13.552  50.400  1.00 11.13           C  
ATOM    367  O   TYR A 216      29.649  13.392  50.393  1.00 22.13           O  
ATOM    368  CB  TYR A 216      28.567  14.776  52.598  1.00 10.09           C  
ATOM    369  CG  TYR A 216      28.149  16.018  53.338  1.00  8.98           C  
ATOM    370  CD1 TYR A 216      28.676  17.267  52.980  1.00  8.70           C  
ATOM    371  CD2 TYR A 216      27.172  15.961  54.341  1.00  8.71           C  
ATOM    372  CE1 TYR A 216      28.245  18.421  53.601  1.00 10.18           C  
ATOM    373  CE2 TYR A 216      26.724  17.119  54.964  1.00  9.84           C  
ATOM    374  CZ  TYR A 216      27.270  18.339  54.592  1.00  9.08           C  
ATOM    375  OH  TYR A 216      26.923  19.516  55.219  1.00 10.69           O  
ATOM    376  N   GLU A 217      27.600  12.800  49.695  1.00  7.59           N  
ATOM    377  CA  GLU A 217      28.067  11.871  48.680  1.00  8.51           C  
ATOM    378  C   GLU A 217      27.295  12.326  47.431  1.00  8.64           C  
ATOM    379  O   GLU A 217      26.215  12.923  47.536  1.00  8.66           O  
ATOM    380  CB  GLU A 217      27.664  10.448  49.040  1.00 11.07           C  
ATOM    381  CG  GLU A 217      26.166  10.340  49.189  1.00 21.61           C  
ATOM    382  CD  GLU A 217      25.672   8.925  49.368  1.00 41.95           C  
ATOM    383  OE1 GLU A 217      26.520   8.010  49.475  1.00 49.12           O  
ATOM    384  OE2 GLU A 217      24.432   8.735  49.401  1.00 47.03           O  
ATOM    385  N   PRO A 218      27.811  12.025  46.244  1.00  7.31           N  
ATOM    386  CA  PRO A 218      27.096  12.454  45.036  1.00  7.64           C  
ATOM    387  C   PRO A 218      25.756  11.740  44.854  1.00  6.93           C  
ATOM    388  O   PRO A 218      25.680  10.506  44.963  1.00  9.23           O  
ATOM    389  CB  PRO A 218      28.065  12.102  43.890  1.00  8.76           C  
ATOM    390  CG  PRO A 218      29.415  12.001  44.588  1.00 10.57           C  
ATOM    391  CD  PRO A 218      29.062  11.343  45.901  1.00  8.48           C  
ATOM    392  N   VAL A 219      24.714  12.509  44.569  1.00  5.76           N  
ATOM    393  CA  VAL A 219      23.395  11.948  44.278  1.00  6.35           C  
ATOM    394  C   VAL A 219      22.926  12.560  42.952  1.00  5.08           C  
ATOM    395  O   VAL A 219      23.314  13.680  42.541  1.00  4.76           O  
ATOM    396  CB  VAL A 219      22.341  12.205  45.403  1.00  7.78           C  
ATOM    397  CG1 VAL A 219      22.773  11.475  46.663  1.00  9.22           C  
ATOM    398  CG2 VAL A 219      22.183  13.695  45.685  1.00  7.73           C  
ATOM    399  N   ARG A 220      22.087  11.810  42.258  1.00  5.66           N  
ATOM    400  CA  ARG A 220      21.637  12.196  40.950  1.00  5.89           C  
ATOM    401  C   ARG A 220      20.911  13.503  40.875  1.00  5.23           C  
ATOM    402  O   ARG A 220      20.022  13.760  41.672  1.00  5.90           O  
ATOM    403  CB  ARG A 220      20.740  11.096  40.413  1.00  6.40           C  
ATOM    404  CG  ARG A 220      20.124  11.402  39.063  1.00  7.27           C  
ATOM    405  CD  ARG A 220      19.169  10.308  38.630  1.00  9.10           C  
ATOM    406  NE  ARG A 220      19.762   8.975  38.599  1.00  9.44           N  
ATOM    407  CZ  ARG A 220      20.270   8.412  37.507  1.00  9.79           C  
ATOM    408  NH1 ARG A 220      20.269   9.037  36.340  1.00 11.94           N  
ATOM    409  NH2 ARG A 220      20.767   7.186  37.592  1.00 12.02           N  
ATOM    410  N   VAL A 221      21.279  14.314  39.886  1.00  4.83           N  
ATOM    411  CA  VAL A 221      20.583  15.563  39.609  1.00  6.67           C  
ATOM    412  C   VAL A 221      20.374  15.759  38.113  1.00  4.57           C  
ATOM    413  O   VAL A 221      21.095  15.182  37.281  1.00  6.33           O  
ATOM    414  CB  VAL A 221      21.333  16.815  40.185  1.00  3.98           C  
ATOM    415  CG1 VAL A 221      21.364  16.717  41.712  1.00  5.47           C  
ATOM    416  CG2 VAL A 221      22.713  16.946  39.607  1.00  6.44           C  
ATOM    417  N   CYS A 222      19.370  16.550  37.774  1.00  6.01           N  
ATOM    418  CA  CYS A 222      19.142  16.899  36.380  1.00  5.02           C  
ATOM    419  C   CYS A 222      20.209  17.899  35.909  1.00  6.50           C  
ATOM    420  O   CYS A 222      20.985  18.455  36.707  1.00  6.09           O  
ATOM    421  CB  CYS A 222      17.753  17.519  36.222  1.00  7.54           C  
ATOM    422  SG  CYS A 222      17.563  19.216  36.930  1.00  6.51           S  
ATOM    423  N   ASP A 223      20.270  18.091  34.593  1.00  6.81           N  
ATOM    424  CA  ASP A 223      21.264  18.982  34.021  1.00  7.76           C  
ATOM    425  C   ASP A 223      21.179  20.412  34.496  1.00  7.94           C  
ATOM    426  O   ASP A 223      22.198  21.088  34.650  1.00  8.74           O  
ATOM    427  CB  ASP A 223      21.220  18.952  32.501  1.00  9.40           C  
ATOM    428  CG  ASP A 223      21.560  17.587  31.942  1.00 10.75           C  
ATOM    429  OD1 ASP A 223      22.285  16.842  32.638  1.00 10.82           O  
ATOM    430  OD2 ASP A 223      21.128  17.263  30.793  1.00 14.30           O  
ATOM    431  N   SER A 224      19.964  20.904  34.718  1.00  8.22           N  
ATOM    432  CA  SER A 224      19.783  22.257  35.200  1.00  9.54           C  
ATOM    433  C   SER A 224      20.367  22.433  36.616  1.00  6.54           C  
ATOM    434  O   SER A 224      21.066  23.410  36.897  1.00  8.57           O  
ATOM    435  CB  SER A 224      18.299  22.618  35.204  1.00 10.39           C  
ATOM    436  OG  SER A 224      18.094  23.900  35.778  1.00 13.21           O  
ATOM    437  N   CYS A 225      20.048  21.498  37.517  1.00  6.61           N  
ATOM    438  CA  CYS A 225      20.552  21.566  38.878  1.00  4.38           C  
ATOM    439  C   CYS A 225      22.056  21.348  38.891  1.00  5.95           C  
ATOM    440  O   CYS A 225      22.753  21.950  39.695  1.00  5.93           O  
ATOM    441  CB  CYS A 225      19.841  20.541  39.772  1.00  5.09           C  
ATOM    442  SG  CYS A 225      18.088  21.009  40.057  1.00  6.45           S  
ATOM    443  N   PHE A 226      22.574  20.524  37.989  1.00  5.47           N  
ATOM    444  CA  PHE A 226      24.014  20.311  37.908  1.00  6.33           C  
ATOM    445  C   PHE A 226      24.709  21.620  37.507  1.00  6.50           C  
ATOM    446  O   PHE A 226      25.728  21.963  38.079  1.00  6.03           O  
ATOM    447  CB  PHE A 226      24.328  19.231  36.867  1.00  5.33           C  
ATOM    448  CG  PHE A 226      25.808  18.934  36.742  1.00  7.06           C  
ATOM    449  CD1 PHE A 226      26.535  18.391  37.815  1.00  6.13           C  
ATOM    450  CD2 PHE A 226      26.497  19.207  35.553  1.00  7.34           C  
ATOM    451  CE1 PHE A 226      27.905  18.143  37.676  1.00  7.06           C  
ATOM    452  CE2 PHE A 226      27.856  18.949  35.434  1.00  7.48           C  
ATOM    453  CZ  PHE A 226      28.551  18.429  36.480  1.00  7.07           C  
ATOM    454  N   GLU A 227      24.140  22.338  36.539  1.00  7.19           N  
ATOM    455  CA  GLU A 227      24.751  23.587  36.096  1.00  8.13           C  
ATOM    456  C   GLU A 227      24.752  24.582  37.238  1.00  7.53           C  
ATOM    457  O   GLU A 227      25.745  25.286  37.463  1.00  8.50           O  
ATOM    458  CB  GLU A 227      24.001  24.139  34.861  1.00  7.52           C  
ATOM    459  CG  GLU A 227      24.583  25.454  34.345  1.00 11.10           C  
ATOM    460  CD  GLU A 227      23.714  26.103  33.293  1.00 17.22           C  
ATOM    461  OE1 GLU A 227      22.663  26.652  33.668  1.00 21.59           O  
ATOM    462  OE2 GLU A 227      24.079  26.064  32.108  1.00 17.51           O  
ATOM    463  N   ASP A 228      23.651  24.654  37.976  1.00  7.62           N  
ATOM    464  CA  ASP A 228      23.554  25.588  39.097  1.00  8.33           C  
ATOM    465  C   ASP A 228      24.694  25.327  40.072  1.00  7.96           C  
ATOM    466  O   ASP A 228      25.333  26.256  40.571  1.00  8.98           O  
ATOM    467  CB  ASP A 228      22.245  25.394  39.887  1.00 10.56           C  
ATOM    468  CG  ASP A 228      21.010  25.835  39.134  1.00 13.53           C  
ATOM    469  OD1 ASP A 228      21.128  26.548  38.131  1.00 14.50           O  
ATOM    470  OD2 ASP A 228      19.897  25.462  39.581  1.00 16.52           O  
ATOM    471  N   TYR A 229      24.918  24.060  40.395  1.00  7.90           N  
ATOM    472  CA  TYR A 229      25.941  23.678  41.352  1.00  7.26           C  
ATOM    473  C   TYR A 229      27.324  23.975  40.820  1.00  7.34           C  
ATOM    474  O   TYR A 229      28.157  24.512  41.538  1.00  7.42           O  
ATOM    475  CB  TYR A 229      25.803  22.171  41.660  1.00  7.05           C  
ATOM    476  CG  TYR A 229      26.893  21.628  42.536  1.00  7.62           C  
ATOM    477  CD1 TYR A 229      26.795  21.717  43.910  1.00  9.18           C  
ATOM    478  CD2 TYR A 229      28.033  21.042  41.989  1.00  8.72           C  
ATOM    479  CE1 TYR A 229      27.792  21.247  44.730  1.00  7.68           C  
ATOM    480  CE2 TYR A 229      29.046  20.559  42.821  1.00  7.46           C  
ATOM    481  CZ  TYR A 229      28.916  20.666  44.179  1.00  7.01           C  
ATOM    482  OH  TYR A 229      29.905  20.137  44.994  1.00  9.73           O  
ATOM    483  N   GLU A 230      27.574  23.612  39.578  1.00  6.58           N  
ATOM    484  CA  GLU A 230      28.863  23.848  38.971  1.00  7.58           C  
ATOM    485  C   GLU A 230      29.173  25.334  38.932  1.00  6.58           C  
ATOM    486  O   GLU A 230      30.321  25.723  39.185  1.00  8.08           O  
ATOM    487  CB  GLU A 230      28.912  23.253  37.564  1.00  6.61           C  
ATOM    488  CG  GLU A 230      29.084  21.746  37.552  1.00  9.19           C  
ATOM    489  CD  GLU A 230      30.389  21.346  38.187  1.00  9.20           C  
ATOM    490  OE1 GLU A 230      31.443  21.748  37.651  1.00 12.50           O  
ATOM    491  OE2 GLU A 230      30.386  20.662  39.224  1.00 13.07           O  
ATOM    492  N   PHE A 231      28.182  26.165  38.626  1.00  6.84           N  
ATOM    493  CA  PHE A 231      28.439  27.605  38.616  1.00  6.60           C  
ATOM    494  C   PHE A 231      28.925  28.093  39.991  1.00  7.75           C  
ATOM    495  O   PHE A 231      29.840  28.942  40.082  1.00  8.63           O  
ATOM    496  CB  PHE A 231      27.181  28.378  38.237  1.00  8.00           C  
ATOM    497  CG  PHE A 231      26.907  28.424  36.754  1.00  7.20           C  
ATOM    498  CD1 PHE A 231      27.790  27.933  35.824  1.00  8.70           C  
ATOM    499  CD2 PHE A 231      25.725  28.973  36.311  1.00  8.56           C  
ATOM    500  CE1 PHE A 231      27.477  27.992  34.441  1.00 10.47           C  
ATOM    501  CE2 PHE A 231      25.424  29.029  34.956  1.00 11.13           C  
ATOM    502  CZ  PHE A 231      26.296  28.540  34.039  1.00 11.04           C  
ATOM    503  N   ILE A 232      28.319  27.594  41.069  1.00  7.13           N  
ATOM    504  CA  ILE A 232      28.712  27.998  42.413  1.00  8.33           C  
ATOM    505  C   ILE A 232      30.141  27.540  42.717  1.00  8.59           C  
ATOM    506  O   ILE A 232      30.953  28.313  43.262  1.00 11.63           O  
ATOM    507  CB  ILE A 232      27.716  27.430  43.459  1.00 11.09           C  
ATOM    508  CG1 ILE A 232      26.385  28.178  43.333  1.00 12.16           C  
ATOM    509  CG2 ILE A 232      28.309  27.516  44.871  1.00 14.04           C  
ATOM    510  CD1 ILE A 232      25.284  27.654  44.185  1.00 19.24           C  
ATOM    511  N   VAL A 233      30.474  26.299  42.368  1.00  8.88           N  
ATOM    512  CA  VAL A 233      31.799  25.758  42.623  1.00 11.18           C  
ATOM    513  C   VAL A 233      32.931  26.537  41.970  1.00 11.13           C  
ATOM    514  O   VAL A 233      33.965  26.767  42.612  1.00 13.66           O  
ATOM    515  CB  VAL A 233      31.893  24.276  42.163  1.00 15.95           C  
ATOM    516  CG1 VAL A 233      33.334  23.772  42.310  1.00 17.42           C  
ATOM    517  CG2 VAL A 233      30.908  23.425  42.968  1.00 20.30           C  
ATOM    518  N   THR A 234      32.765  26.925  40.714  1.00  8.89           N  
ATOM    519  CA  THR A 234      33.832  27.624  40.023  1.00  9.51           C  
ATOM    520  C   THR A 234      33.685  29.135  39.961  1.00  9.47           C  
ATOM    521  O   THR A 234      34.460  29.814  39.271  1.00 10.05           O  
ATOM    522  CB  THR A 234      34.041  27.081  38.561  1.00 11.03           C  
ATOM    523  OG1 THR A 234      32.800  27.064  37.832  1.00  9.76           O  
ATOM    524  CG2 THR A 234      34.607  25.671  38.600  1.00 15.73           C  
ATOM    525  N   ASP A 235      32.715  29.677  40.681  1.00  7.29           N  
ATOM    526  CA  ASP A 235      32.525  31.116  40.631  1.00  8.56           C  
ATOM    527  C   ASP A 235      33.810  31.901  40.950  1.00  9.13           C  
ATOM    528  O   ASP A 235      34.333  31.696  42.046  1.00 11.00           O  
ATOM    529  CB  ASP A 235      31.428  31.509  41.606  1.00  9.56           C  
ATOM    530  CG  ASP A 235      31.027  32.944  41.405  1.00 10.41           C  
ATOM    531  OD1 ASP A 235      31.922  33.815  41.296  1.00 10.71           O  
ATOM    532  OD2 ASP A 235      29.841  33.224  41.259  1.00 12.52           O  
TER     533      ASP A 235                                                      
HETATM  534 ZN    ZN A 300      16.916  19.183  39.167  1.00  5.81          ZN  
HETATM  535 ZN    ZN A 301      15.152  13.042  28.880  1.00  8.84          ZN  
HETATM  536  O   HOH A   1      11.899  19.763  37.981  1.00 21.60           O  
HETATM  537  O   HOH A   2      19.348  18.556  29.813  1.00 27.66           O  
HETATM  538  O   HOH A   3       5.931   5.876  34.633  1.00 25.69           O  
HETATM  539  O   HOH A   4      19.774  24.331  42.014  1.00 21.76           O  
HETATM  540  O   HOH A   5      26.272  15.632  31.331  1.00 26.51           O  
HETATM  541  O   HOH A   6      35.149  21.621  38.670  1.00 30.73           O  
HETATM  542  O   HOH A   7      22.298  29.064  42.643  1.00 26.72           O  
HETATM  543  O   HOH A   8      24.081  12.286  29.043  1.00 28.48           O  
HETATM  544  O   HOH A   9      11.802  14.592  49.668  1.00 28.54           O  
HETATM  545  O   HOH A  10       3.385  12.898  33.025  1.00 28.82           O  
HETATM  546  O   HOH A  11       4.770  13.825  31.068  1.00 28.91           O  
HETATM  547  O   HOH A  12      15.680  23.052  44.363  1.00 30.24           O  
HETATM  548  O   HOH A  13      30.511  29.949  45.416  1.00 31.53           O  
HETATM  549  O   HOH A  14      19.123   0.079  35.400  1.00 30.14           O  
HETATM  550  O   HOH A  15      16.975   5.812  24.617  1.00 29.13           O  
HETATM  551  O   HOH A  16      20.149   7.443  41.161  1.00 11.65           O  
HETATM  552  O   HOH A  17      22.886  15.344  35.262  1.00 12.14           O  
HETATM  553  O   HOH A  18      31.019  29.135  37.511  1.00 11.90           O  
HETATM  554  O   HOH A  19       5.983   5.893  31.219  1.00 26.60           O  
HETATM  555  O   HOH A  20      33.740  18.908  42.038  1.00 18.91           O  
HETATM  556  O   HOH A  21      26.707  10.348  38.097  1.00 16.63           O  
HETATM  557  O   HOH A  22      30.157  18.622  49.688  1.00 29.44           O  
HETATM  558  O   HOH A  23      15.040   7.642  22.575  1.00 19.19           O  
HETATM  559  O   HOH A  24      15.094  20.840  34.846  1.00 21.33           O  
HETATM  560  O   HOH A  25      24.527  20.821  33.059  1.00 18.51           O  
HETATM  561  O   HOH A  26      28.841  31.376  39.678  1.00 21.31           O  
HETATM  562  O   HOH A  27      25.198   8.435  34.854  1.00 25.25           O  
HETATM  563  O   HOH A  28      23.286  10.521  38.092  1.00 13.42           O  
HETATM  564  O   HOH A  29       6.381   2.321  29.587  1.00 28.47           O  
HETATM  565  O   HOH A  30      24.788   8.694  41.837  1.00 29.68           O  
HETATM  566  O   HOH A  31      22.792  14.928  31.820  1.00 16.03           O  
HETATM  567  O   HOH A  32      29.954  20.672  47.698  1.00 22.43           O  
HETATM  568  O   HOH A  33      10.621  -1.428  23.158  1.00 30.94           O  
HETATM  569  O   HOH A  34      30.815  18.904  33.146  1.00 22.22           O  
HETATM  570  O   HOH A  35       9.276  -1.533  28.905  1.00 29.51           O  
HETATM  571  O   HOH A  36      21.439   9.063  43.357  1.00 14.06           O  
HETATM  572  O   HOH A  37      30.302  16.490  33.795  1.00 21.52           O  
HETATM  573  O   HOH A  38      16.996  23.354  38.299  1.00 23.34           O  
HETATM  574  O   HOH A  39      28.652  23.042  48.080  1.00 24.43           O  
HETATM  575  O   HOH A  40       9.260   6.908  41.624  1.00 29.18           O  
HETATM  576  O   HOH A  41      16.578  11.983  24.938  1.00 22.99           O  
HETATM  577  O   HOH A  42       9.929  14.529  48.758  1.00 25.14           O  
HETATM  578  O   HOH A  43      15.622  15.141  47.327  1.00 19.64           O  
HETATM  579  O   HOH A  44      18.630   2.633  35.410  1.00 29.24           O  
HETATM  580  O   HOH A  45      10.305  -0.272  26.164  1.00 27.29           O  
HETATM  581  O   HOH A  46      16.694  14.574  23.381  1.00 29.19           O  
HETATM  582  O   HOH A  47       7.649  15.329  32.035  1.00 23.97           O  
HETATM  583  O   HOH A  48      14.609  19.832  51.784  1.00 28.56           O  
HETATM  584  O   HOH A  49      36.687  26.057  42.539  1.00 29.90           O  
HETATM  585  O   HOH A  50      23.657  22.254  48.834  1.00 23.46           O  
HETATM  586  O   HOH A  51       0.205   9.332  29.993  1.00 22.84           O  
HETATM  587  O   HOH A  52       6.945  15.954  29.716  1.00 24.51           O  
HETATM  588  O   HOH A  53       8.054  17.611  50.031  1.00 26.44           O  
HETATM  589  O   HOH A  54      16.416   8.776  27.095  1.00 26.83           O  
HETATM  590  O   HOH A  55      18.129   4.798  32.855  1.00 22.75           O  
HETATM  591  O   HOH A  56      37.314  23.672  41.298  1.00 26.82           O  
HETATM  592  O   HOH A  57       8.465  11.544  47.961  1.00 28.61           O  
HETATM  593  O   HOH A  58      18.463  17.575  32.813  1.00 19.88           O  
HETATM  594  O   HOH A  59       6.448   4.636  38.686  1.00 22.27           O  
HETATM  595  O   HOH A  60      24.147  29.347  40.366  1.00 27.72           O  
HETATM  596  O   HOH A  61      17.619   2.652  31.763  1.00 23.79           O  
HETATM  597  O   HOH A  62      19.549  22.101  45.247  1.00 29.75           O  
HETATM  598  O   HOH A  63      15.128  18.147  48.111  1.00 28.56           O  
HETATM  599  O   HOH A  64      17.842   7.861  28.702  1.00 14.01           O  
HETATM  600  O   HOH A  65      35.066  29.549  43.494  1.00 25.19           O  
HETATM  601  O   HOH A  66      22.197  13.014  56.800  1.00 28.80           O  
HETATM  602  O   HOH A  67      12.190  21.524  44.638  1.00 32.94           O  
HETATM  603  O   HOH A  68       6.738  13.600  47.248  1.00 20.57           O  
HETATM  604  O   HOH A  69      22.459  16.066  28.643  1.00 26.56           O  
HETATM  605  O   HOH A  70      24.719  21.390  46.489  1.00 11.46           O  
HETATM  606  O   HOH A  71       8.393   9.563  44.077  1.00 29.30           O  
HETATM  607  O   HOH A  72      17.084  12.680  49.038  1.00 29.51           O  
HETATM  608  O   HOH A  73      16.077  21.452  47.168  1.00 31.28           O  
HETATM  609  O   HOH A  74      20.501  15.992  25.832  1.00 32.99           O  
HETATM  610  O   HOH A  75       9.825  21.823  45.172  1.00 27.58           O  
HETATM  611  O   HOH A  76      32.167  13.224  52.477  1.00 27.31           O  
HETATM  612  O   HOH A  77      17.305   4.391  26.372  1.00 31.04           O  
HETATM  613  O   HOH A  78       8.492  20.052  44.443  1.00 20.94           O  
HETATM  614  O   HOH A  79      19.781   9.406  46.534  1.00 24.37           O  
HETATM  615  O   HOH A  80      29.124   7.435  47.465  1.00 31.18           O  
HETATM  616  O   HOH A  81       9.938  17.557  25.889  1.00 28.69           O  
HETATM  617  O   HOH A  82      33.010  20.011  39.767  1.00 21.08           O  
HETATM  618  O   HOH A  83      31.824  15.272  49.737  1.00 31.95           O  
HETATM  619  O   HOH A  84      21.896  21.899  42.528  1.00 19.07           O  
HETATM  620  O   HOH A  85       9.047  22.594  32.076  1.00 29.30           O  
HETATM  621  O   HOH A  86      28.235  31.995  42.972  1.00 28.33           O  
HETATM  622  O   HOH A  87      19.915   5.156  39.499  1.00 26.48           O  
HETATM  623  O   HOH A  88      27.747   7.842  41.700  1.00 29.87           O  
HETATM  624  O   HOH A  89      16.355   6.647  31.490  1.00 10.32           O  
HETATM  625  O   HOH A  90      17.507  -0.546  31.999  1.00 31.60           O  
HETATM  626  O   HOH A  91      23.026  22.402  44.778  1.00 18.18           O  
HETATM  627  O   HOH A  92      17.700  20.098  33.488  1.00 18.05           O  
HETATM  628  O   HOH A  94      21.244   8.162  45.727  1.00 25.90           O  
HETATM  629  O   HOH A  95      21.439   4.137  36.456  1.00 28.17           O  
HETATM  630  O   HOH A  96      18.446   4.892  29.550  1.00 26.81           O  
HETATM  631  O   HOH A  97       7.237   6.287  40.158  1.00 28.76           O  
HETATM  632  O   HOH A  99      12.359  20.092  34.968  1.00 27.84           O  
HETATM  633  O   HOH A 100      22.818  28.119  36.707  1.00 25.20           O  
HETATM  634  O   HOH A 101      27.726   8.403  45.107  1.00 29.61           O  
HETATM  635  O   HOH A 102      21.210  26.225  43.632  1.00 28.53           O  
HETATM  636  O   HOH A 103      14.624  21.221  53.143  1.00 29.14           O  
HETATM  637  O   HOH A 104       4.639   7.043  36.059  1.00 25.87           O  
HETATM  638  O   HOH A 105      18.253  14.537  53.565  1.00 29.76           O  
HETATM  639  O   HOH A 106      19.034  11.565  48.598  1.00 29.95           O  
HETATM  640  O   HOH A 107      17.013  23.394  53.956  1.00 31.67           O  
HETATM  641  O   HOH A 108      26.384  23.084  47.622  1.00 27.98           O  
HETATM  642  O   HOH A 109       8.361  19.373  31.600  1.00 28.40           O  
HETATM  643  O   HOH A 110       3.500  10.267  28.414  1.00 28.84           O  
HETATM  644  O   HOH A 111      11.093  21.358  41.673  1.00 27.54           O  
CONECT   63  535                                                                
CONECT   85  535                                                                
CONECT  196  534                                                                
CONECT  219  534                                                                
CONECT  251  535                                                                
CONECT  276  535                                                                
CONECT  422  534                                                                
CONECT  442  534                                                                
CONECT  534  196  219  422  442                                                 
CONECT  535   63   85  251  276                                                 
MASTER      321    0    2    3    2    0    6    6  643    1   10    6          
END