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Database: PDB
Entry: 5VWK
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Original site: 5VWK 
HEADER    STRUCTURAL PROTEIN                      22-MAY-17   5VWK              
TITLE     CRYSTAL STRUCTURE OF HUMAN SCRIBBLE PDZ1:BETA-PIX COMPLEX             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN SCRIBBLE HOMOLOG;                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 700-816;                                          
COMPND   5 SYNONYM: HSCRIB,PROTEIN LAP4;                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-PIX;                                                  
COMPND   9 CHAIN: E, F, G, H;                                                   
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SCRIB, CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 83333                                       
KEYWDS    POLARITY, STRUCTURAL PROTEIN                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.Y.B.LIM,M.KVANSAKUL                                                 
REVDAT   4   04-OCT-23 5VWK    1       REMARK                                   
REVDAT   3   01-JAN-20 5VWK    1       REMARK                                   
REVDAT   2   27-DEC-17 5VWK    1       JRNL                                     
REVDAT   1   08-NOV-17 5VWK    0                                                
JRNL        AUTH   K.Y.B.LIM,N.J.GODDE,P.O.HUMBERT,M.KVANSAKUL                  
JRNL        TITL   STRUCTURAL BASIS FOR THE DIFFERENTIAL INTERACTION OF         
JRNL        TITL 2 SCRIBBLE PDZ DOMAINS WITH THE GUANINE NUCLEOTIDE EXCHANGE    
JRNL        TITL 3 FACTOR BETA-PIX.                                             
JRNL        REF    J. BIOL. CHEM.                V. 292 20425 2017              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   29061852                                                     
JRNL        DOI    10.1074/JBC.M117.799452                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155)                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.36                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26411                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1294                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.3620 -  4.8852    0.91     2833   160  0.2177 0.2835        
REMARK   3     2  4.8852 -  3.8787    0.95     2797   138  0.1753 0.1955        
REMARK   3     3  3.8787 -  3.3888    0.97     2799   144  0.2002 0.2209        
REMARK   3     4  3.3888 -  3.0791    0.97     2799   123  0.2186 0.2533        
REMARK   3     5  3.0791 -  2.8585    0.98     2791   127  0.2389 0.2619        
REMARK   3     6  2.8585 -  2.6900    0.98     2770   164  0.2502 0.2828        
REMARK   3     7  2.6900 -  2.5553    0.98     2775   147  0.2661 0.3003        
REMARK   3     8  2.5553 -  2.4441    0.99     2766   150  0.2794 0.3108        
REMARK   3     9  2.4441 -  2.3500    0.99     2787   141  0.2984 0.3395        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.940           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           3379                                  
REMARK   3   ANGLE     :  0.656           4566                                  
REMARK   3   CHIRALITY :  0.048            504                                  
REMARK   3   PLANARITY :  0.004            600                                  
REMARK   3   DIHEDRAL  : 19.482           1996                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VWK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228080.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.09                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26459                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.770                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2W4F                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.09M LITHIUM SULFATE AND 0.1M           
REMARK 280  TRISODIUM CITRATE-CITRIC ACID PH5.09, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      111.48150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       37.38000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       37.38000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      167.22225            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       37.38000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       37.38000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       55.74075            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       37.38000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.38000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      167.22225            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       37.38000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.38000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       55.74075            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      111.48150            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6900 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6830 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6930 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6860 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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     GLY A   695                                                      
REMARK 465     PRO A   696                                                      
REMARK 465     LEU A   697                                                      
REMARK 465     GLY A   698                                                      
REMARK 465     SER A   699                                                      
REMARK 465     SER A   700                                                      
REMARK 465     ALA A   701                                                      
REMARK 465     PRO A   702                                                      
REMARK 465     SER A   703                                                      
REMARK 465     VAL A   704                                                      
REMARK 465     LYS A   705                                                      
REMARK 465     GLY A   706                                                      
REMARK 465     VAL A   707                                                      
REMARK 465     SER A   708                                                      
REMARK 465     PHE A   709                                                      
REMARK 465     ASP A   710                                                      
REMARK 465     GLN A   711                                                      
REMARK 465     ALA A   712                                                      
REMARK 465     ASN A   713                                                      
REMARK 465     MET A   816                                                      
REMARK 465     GLY B   695                                                      
REMARK 465     PRO B   696                                                      
REMARK 465     LEU B   697                                                      
REMARK 465     GLY B   698                                                      
REMARK 465     SER B   699                                                      
REMARK 465     SER B   700                                                      
REMARK 465     ALA B   701                                                      
REMARK 465     PRO B   702                                                      
REMARK 465     SER B   703                                                      
REMARK 465     VAL B   704                                                      
REMARK 465     LYS B   705                                                      
REMARK 465     GLY B   706                                                      
REMARK 465     VAL B   707                                                      
REMARK 465     SER B   708                                                      
REMARK 465     PHE B   709                                                      
REMARK 465     ASP B   710                                                      
REMARK 465     GLN B   711                                                      
REMARK 465     ALA B   712                                                      
REMARK 465     ASN B   713                                                      
REMARK 465     MET B   816                                                      
REMARK 465     GLY C   695                                                      
REMARK 465     PRO C   696                                                      
REMARK 465     LEU C   697                                                      
REMARK 465     GLY C   698                                                      
REMARK 465     SER C   699                                                      
REMARK 465     SER C   700                                                      
REMARK 465     ALA C   701                                                      
REMARK 465     PRO C   702                                                      
REMARK 465     SER C   703                                                      
REMARK 465     VAL C   704                                                      
REMARK 465     LYS C   705                                                      
REMARK 465     GLY C   706                                                      
REMARK 465     VAL C   707                                                      
REMARK 465     SER C   708                                                      
REMARK 465     PHE C   709                                                      
REMARK 465     ASP C   710                                                      
REMARK 465     GLN C   711                                                      
REMARK 465     ALA C   712                                                      
REMARK 465     ASN C   713                                                      
REMARK 465     ASN C   714                                                      
REMARK 465     MET C   816                                                      
REMARK 465     GLY D   695                                                      
REMARK 465     PRO D   696                                                      
REMARK 465     LEU D   697                                                      
REMARK 465     GLY D   698                                                      
REMARK 465     SER D   699                                                      
REMARK 465     SER D   700                                                      
REMARK 465     ALA D   701                                                      
REMARK 465     PRO D   702                                                      
REMARK 465     SER D   703                                                      
REMARK 465     VAL D   704                                                      
REMARK 465     LYS D   705                                                      
REMARK 465     GLY D   706                                                      
REMARK 465     VAL D   707                                                      
REMARK 465     SER D   708                                                      
REMARK 465     PHE D   709                                                      
REMARK 465     ASP D   710                                                      
REMARK 465     GLN D   711                                                      
REMARK 465     ALA D   712                                                      
REMARK 465     ASN D   713                                                      
REMARK 465     ASN D   714                                                      
REMARK 465     MET D   816                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A 714    CG   OD1  ND2                                       
REMARK 470     LEU A 716    CG   CD1  CD2                                       
REMARK 470     ASN B 714    CG   OD1  ND2                                       
REMARK 470     LEU B 716    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU C   726     HE   ARG C   810              1.51            
REMARK 500   H    GLU D   766     O    HOH D  1002              1.51            
REMARK 500  HH22  ARG A   801     OD2  ASP E   159              1.59            
REMARK 500   O    GLU B   766     O    HOH B  1001              1.99            
REMARK 500   O    ALA C   720     O    HOH C  1001              2.16            
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   H    GLY B   785     O1   SO4 C   904     5444     1.57            
REMARK 500   O    HOH A  1032     O    HOH A  1034     8554     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU B 766       49.17   -143.80                                   
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 A1057        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1058        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH B1054        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B1055        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH B1056        DISTANCE =  6.74 ANGSTROMS                       
REMARK 525    HOH B1057        DISTANCE =  8.24 ANGSTROMS                       
REMARK 525    HOH C1047        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH C1048        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH D1053        DISTANCE =  7.38 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VWI   RELATED DB: PDB                                   
DBREF  5VWK A  700   816  UNP    Q14160   SCRIB_HUMAN    700    816             
DBREF  5VWK B  700   816  UNP    Q14160   SCRIB_HUMAN    700    816             
DBREF  5VWK C  700   816  UNP    Q14160   SCRIB_HUMAN    700    816             
DBREF  5VWK D  700   816  UNP    Q14160   SCRIB_HUMAN    700    816             
DBREF  5VWK E  156   163  PDB    5VWK     5VWK           156    163             
DBREF  5VWK F  156   163  PDB    5VWK     5VWK           156    163             
DBREF  5VWK G  156   163  PDB    5VWK     5VWK           156    163             
DBREF  5VWK H  156   163  PDB    5VWK     5VWK           156    163             
SEQADV 5VWK GLY A  695  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK PRO A  696  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK LEU A  697  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK GLY A  698  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK SER A  699  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK GLY B  695  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK PRO B  696  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK LEU B  697  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK GLY B  698  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK SER B  699  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK GLY C  695  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK PRO C  696  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK LEU C  697  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK GLY C  698  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK SER C  699  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK GLY D  695  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK PRO D  696  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK LEU D  697  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK GLY D  698  UNP  Q14160              EXPRESSION TAG                 
SEQADV 5VWK SER D  699  UNP  Q14160              EXPRESSION TAG                 
SEQRES   1 A  122  GLY PRO LEU GLY SER SER ALA PRO SER VAL LYS GLY VAL          
SEQRES   2 A  122  SER PHE ASP GLN ALA ASN ASN LEU LEU ILE GLU PRO ALA          
SEQRES   3 A  122  ARG ILE GLU GLU GLU GLU LEU THR LEU THR ILE LEU ARG          
SEQRES   4 A  122  GLN THR GLY GLY LEU GLY ILE SER ILE ALA GLY GLY LYS          
SEQRES   5 A  122  GLY SER THR PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE          
SEQRES   6 A  122  ILE SER ARG VAL SER GLU GLU GLY PRO ALA ALA ARG ALA          
SEQRES   7 A  122  GLY VAL ARG VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY          
SEQRES   8 A  122  VAL ALA LEU GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU          
SEQRES   9 A  122  ALA LEU ARG GLY ALA GLY THR ALA VAL GLN MET ARG VAL          
SEQRES  10 A  122  TRP ARG GLU ARG MET                                          
SEQRES   1 B  122  GLY PRO LEU GLY SER SER ALA PRO SER VAL LYS GLY VAL          
SEQRES   2 B  122  SER PHE ASP GLN ALA ASN ASN LEU LEU ILE GLU PRO ALA          
SEQRES   3 B  122  ARG ILE GLU GLU GLU GLU LEU THR LEU THR ILE LEU ARG          
SEQRES   4 B  122  GLN THR GLY GLY LEU GLY ILE SER ILE ALA GLY GLY LYS          
SEQRES   5 B  122  GLY SER THR PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE          
SEQRES   6 B  122  ILE SER ARG VAL SER GLU GLU GLY PRO ALA ALA ARG ALA          
SEQRES   7 B  122  GLY VAL ARG VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY          
SEQRES   8 B  122  VAL ALA LEU GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU          
SEQRES   9 B  122  ALA LEU ARG GLY ALA GLY THR ALA VAL GLN MET ARG VAL          
SEQRES  10 B  122  TRP ARG GLU ARG MET                                          
SEQRES   1 C  122  GLY PRO LEU GLY SER SER ALA PRO SER VAL LYS GLY VAL          
SEQRES   2 C  122  SER PHE ASP GLN ALA ASN ASN LEU LEU ILE GLU PRO ALA          
SEQRES   3 C  122  ARG ILE GLU GLU GLU GLU LEU THR LEU THR ILE LEU ARG          
SEQRES   4 C  122  GLN THR GLY GLY LEU GLY ILE SER ILE ALA GLY GLY LYS          
SEQRES   5 C  122  GLY SER THR PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE          
SEQRES   6 C  122  ILE SER ARG VAL SER GLU GLU GLY PRO ALA ALA ARG ALA          
SEQRES   7 C  122  GLY VAL ARG VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY          
SEQRES   8 C  122  VAL ALA LEU GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU          
SEQRES   9 C  122  ALA LEU ARG GLY ALA GLY THR ALA VAL GLN MET ARG VAL          
SEQRES  10 C  122  TRP ARG GLU ARG MET                                          
SEQRES   1 D  122  GLY PRO LEU GLY SER SER ALA PRO SER VAL LYS GLY VAL          
SEQRES   2 D  122  SER PHE ASP GLN ALA ASN ASN LEU LEU ILE GLU PRO ALA          
SEQRES   3 D  122  ARG ILE GLU GLU GLU GLU LEU THR LEU THR ILE LEU ARG          
SEQRES   4 D  122  GLN THR GLY GLY LEU GLY ILE SER ILE ALA GLY GLY LYS          
SEQRES   5 D  122  GLY SER THR PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE          
SEQRES   6 D  122  ILE SER ARG VAL SER GLU GLU GLY PRO ALA ALA ARG ALA          
SEQRES   7 D  122  GLY VAL ARG VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY          
SEQRES   8 D  122  VAL ALA LEU GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU          
SEQRES   9 D  122  ALA LEU ARG GLY ALA GLY THR ALA VAL GLN MET ARG VAL          
SEQRES  10 D  122  TRP ARG GLU ARG MET                                          
SEQRES   1 E    8  PRO ALA TRP ASP GLU THR ASN LEU                              
SEQRES   1 F    8  PRO ALA TRP ASP GLU THR ASN LEU                              
SEQRES   1 G    8  PRO ALA TRP ASP GLU THR ASN LEU                              
SEQRES   1 H    8  PRO ALA TRP ASP GLU THR ASN LEU                              
HET    SO4  A 901       5                                                       
HET    SO4  A 902       5                                                       
HET    SO4  B 901       5                                                       
HET    SO4  C 901       5                                                       
HET    SO4  C 902       5                                                       
HET    SO4  C 903       5                                                       
HET    SO4  C 904       5                                                       
HET    SO4  D 901       5                                                       
HET    SO4  D 902       5                                                       
HET    SO4  D 903       5                                                       
HET    SO4  G 201       5                                                       
HET    SO4  H 201       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  SO4    12(O4 S 2-)                                                  
FORMUL  21  HOH   *246(H2 O)                                                    
HELIX    1 AA1 GLY A  767  ALA A  772  1                                   6    
HELIX    2 AA2 GLU A  792  GLY A  802  1                                  11    
HELIX    3 AA3 GLY B  767  GLY B  773  1                                   7    
HELIX    4 AA4 GLU B  792  GLY B  802  1                                  11    
HELIX    5 AA5 GLY C  767  ALA C  772  1                                   6    
HELIX    6 AA6 GLU C  792  GLY C  802  1                                  11    
HELIX    7 AA7 GLY D  767  ALA D  772  1                                   6    
HELIX    8 AA8 GLU D  792  GLY D  802  1                                  11    
SHEET    1 AA1 4 GLU A 724  LEU A 732  0                                        
SHEET    2 AA1 4 ALA A 806  GLU A 814 -1  O  VAL A 807   N  ILE A 731           
SHEET    3 AA1 4 LYS A 779  VAL A 783 -1  N  LEU A 781   O  ARG A 810           
SHEET    4 AA1 4 VAL A 786  ALA A 787 -1  O  VAL A 786   N  VAL A 783           
SHEET    1 AA2 6 GLU A 724  LEU A 732  0                                        
SHEET    2 AA2 6 ALA A 806  GLU A 814 -1  O  VAL A 807   N  ILE A 731           
SHEET    3 AA2 6 LYS A 779  VAL A 783 -1  N  LEU A 781   O  ARG A 810           
SHEET    4 AA2 6 ILE A 758  VAL A 763 -1  N  ILE A 758   O  LEU A 780           
SHEET    5 AA2 6 ILE A 740  GLY A 744 -1  N  ALA A 743   O  PHE A 759           
SHEET    6 AA2 6 GLU H 160  ASN H 162 -1  O  THR H 161   N  ILE A 742           
SHEET    1 AA3 4 GLU B 725  LEU B 732  0                                        
SHEET    2 AA3 4 ALA B 806  ARG B 813 -1  O  VAL B 807   N  ILE B 731           
SHEET    3 AA3 4 LYS B 779  VAL B 783 -1  N  LYS B 779   O  TRP B 812           
SHEET    4 AA3 4 VAL B 786  ALA B 787 -1  O  VAL B 786   N  VAL B 783           
SHEET    1 AA4 6 GLU B 725  LEU B 732  0                                        
SHEET    2 AA4 6 ALA B 806  ARG B 813 -1  O  VAL B 807   N  ILE B 731           
SHEET    3 AA4 6 LYS B 779  VAL B 783 -1  N  LYS B 779   O  TRP B 812           
SHEET    4 AA4 6 ILE B 758  VAL B 763 -1  N  ILE B 758   O  LEU B 780           
SHEET    5 AA4 6 ILE B 740  GLY B 744 -1  N  SER B 741   O  SER B 761           
SHEET    6 AA4 6 GLU G 160  LEU G 163 -1  O  LEU G 163   N  ILE B 740           
SHEET    1 AA5 4 GLU C 724  LEU C 732  0                                        
SHEET    2 AA5 4 ALA C 806  GLU C 814 -1  O  MET C 809   N  LEU C 729           
SHEET    3 AA5 4 LYS C 779  VAL C 783 -1  N  LEU C 781   O  ARG C 810           
SHEET    4 AA5 4 VAL C 786  ALA C 787 -1  O  VAL C 786   N  VAL C 783           
SHEET    1 AA6 6 GLU C 724  LEU C 732  0                                        
SHEET    2 AA6 6 ALA C 806  GLU C 814 -1  O  MET C 809   N  LEU C 729           
SHEET    3 AA6 6 LYS C 779  VAL C 783 -1  N  LEU C 781   O  ARG C 810           
SHEET    4 AA6 6 ILE C 758  VAL C 763 -1  N  ILE C 758   O  LEU C 780           
SHEET    5 AA6 6 ILE C 740  GLY C 744 -1  N  ALA C 743   O  PHE C 759           
SHEET    6 AA6 6 GLU F 160  ASN F 162 -1  O  THR F 161   N  ILE C 742           
SHEET    1 AA7 4 GLU D 724  LEU D 732  0                                        
SHEET    2 AA7 4 ALA D 806  GLU D 814 -1  O  ARG D 813   N  GLU D 725           
SHEET    3 AA7 4 LYS D 779  VAL D 783 -1  N  LYS D 779   O  TRP D 812           
SHEET    4 AA7 4 VAL D 786  ALA D 787 -1  O  VAL D 786   N  VAL D 783           
SHEET    1 AA8 6 GLU D 724  LEU D 732  0                                        
SHEET    2 AA8 6 ALA D 806  GLU D 814 -1  O  ARG D 813   N  GLU D 725           
SHEET    3 AA8 6 LYS D 779  VAL D 783 -1  N  LYS D 779   O  TRP D 812           
SHEET    4 AA8 6 ILE D 758  VAL D 763 -1  N  ILE D 758   O  LEU D 780           
SHEET    5 AA8 6 ILE D 740  GLY D 744 -1  N  ALA D 743   O  PHE D 759           
SHEET    6 AA8 6 GLU E 160  ASN E 162 -1  O  THR E 161   N  ILE D 742           
LINK         NH2 ARG B 762                 O4  SO4 B 901     1555   1555  1.30  
SITE     1 AC1  6 ARG A 762  VAL A 763  SER A 764  GLU A 765                    
SITE     2 AC1  6 GLY C 736  PRO G 156                                          
SITE     1 AC2  7 GLU A 782  ASN A 784  GLY A 785  GLN A 808                    
SITE     2 AC2  7 MET A 809  ARG A 810  GLN D 808                               
SITE     1 AC3  5 ARG B 762  VAL B 763  SER B 764  GLY D 736                    
SITE     2 AC3  5 PRO H 156                                                     
SITE     1 AC4  9 GLU B 792  HIS B 793  HIS B 794  HOH B1010                    
SITE     2 AC4  9 HIS C 794  VAL C 797  ARG C 801  HOH F 202                    
SITE     3 AC4  9 ASP G 159                                                     
SITE     1 AC5  5 ARG A 762  ARG C 762  SER C 764  ASN H 162                    
SITE     2 AC5  5 HOH H 305                                                     
SITE     1 AC6  3 LYS C 779  LEU C 781  TRP C 812                               
SITE     1 AC7  9 GLU B 782  VAL B 783  ASN B 784  GLY B 785                    
SITE     2 AC7  9 GLN B 808  MET B 809  ARG B 810  GLN C 808                    
SITE     3 AC7  9 HOH C1003                                                     
SITE     1 AC8  8 GLU A 792  HIS A 793  HIS A 794  HIS D 794                    
SITE     2 AC8  8 ARG D 801  HOH D1004  HOH D1017  HOH H 303                    
SITE     1 AC9  8 ARG B 762  ARG D 762  SER D 764  HOH D1008                    
SITE     2 AC9  8 HOH D1021  HOH D1034  HOH D1037  ASN G 162                    
SITE     1 AD1  2 LYS D 779  TRP D 812                                          
SITE     1 AD2  6 TRP G 158  GLU G 160  HOH G 306  ALA H 157                    
SITE     2 AD2  6 TRP H 158  SO4 H 201                                          
SITE     1 AD3  5 ALA G 157  TRP G 158  SO4 G 201  TRP H 158                    
SITE     2 AD3  5 GLU H 160                                                     
CRYST1   74.760   74.760  222.963  90.00  90.00  90.00 P 43 21 2    32          
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      0.013376  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013376  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004485        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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