GenomeNet

Database: PDB
Entry: 2GI7
LinkDB: 2GI7
Original site: 2GI7 
HEADER    BLOOD CLOTTING, CELL ADHESION           28-MAR-06   2GI7              
TITLE     CRYSTAL STRUCTURE OF HUMAN PLATELET GLYCOPROTEIN VI (GPVI)            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GPVI PROTEIN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: COLLAGEN BINDING DOMAIN, RESIDUES 21-203;                  
COMPND   5 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: HUMAN;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TUNER(DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST17                                   
KEYWDS    IG-LIKE DOMAINS, BLOOD CLOTTING, CELL ADHESION                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.HORII,M.L.KAHN,A.B.HERR                                             
REVDAT   3   13-JUL-11 2GI7    1       VERSN                                    
REVDAT   2   24-FEB-09 2GI7    1       VERSN                                    
REVDAT   1   03-APR-07 2GI7    0                                                
JRNL        AUTH   K.HORII,M.L.KAHN,A.B.HERR                                    
JRNL        TITL   STRUCTURAL BASIS FOR PLATELET COLLAGEN RESPONSES BY THE      
JRNL        TITL 2 IMMUNE-TYPE RECEPTOR GLYCOPROTEIN VI.                        
JRNL        REF    BLOOD                         V. 108   936 2006              
JRNL        REFN                   ISSN 0006-4971                               
JRNL        PMID   16861347                                                     
JRNL        DOI    10.1182/BLOOD-2006-01-010215                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1902639.420                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 15500                          
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) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 799                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2349                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3120                       
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 123                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.032                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2719                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 177                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.01000                                             
REMARK   3    B22 (A**2) : 10.30000                                             
REMARK   3    B33 (A**2) : -21.31000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.37                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.44                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92                            
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) : 1.540 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.630 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.050 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.090 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 65.02                                                
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.PARAM                                  
REMARK   3  PARAMETER FILE  2  : HETERO.PARAM                                   
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : HETERO.TOP                                     
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 0-1 IN MOLECULE A AND RESIDUES   
REMARK   3  99-107 AND 130-137 IN MOLECLUE B WERE DELETED DUE TO LOW ELECTRON   
REMARK   3  DENSITY                                                             
REMARK   4                                                                      
REMARK   4 2GI7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037149.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 7.40                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC CONFOCAL                     
REMARK 200  OPTICS                         : OSMIC CONFOCAL MIRRORS             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15739                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER V. 1.3.1                                       
REMARK 200 STARTING MODEL: PDB ENTRY 1G0X                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9M AMMONIUM SULFATE, 8% MPD, 20%       
REMARK 280  GLYCEROL, PH 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE        
REMARK 280  293K, PH 7.40                                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       57.02850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.64300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.02850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       22.64300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). AT 2MG/ML CONCENTRATION, THE           
REMARK 300 PROTEIN IS MONOMERIC IN SOLUTION. HOWEVER, THE BIOLOGICAL            
REMARK 300 UNIT IS LIKELY A DIMER ON THE SURFACE OF PLATELETS. SEE              
REMARK 300 REMARK 350 FOR INFORMATION ON GENERATING THE DIMER.                  
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 282  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 283  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 303  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 281  LIES ON A SPECIAL POSITION.                          
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     0                                                      
REMARK 465     GLN A     1                                                      
REMARK 465     GLN B    99                                                      
REMARK 465     PRO B   100                                                      
REMARK 465     GLY B   101                                                      
REMARK 465     PRO B   102                                                      
REMARK 465     ALA B   103                                                      
REMARK 465     VAL B   104                                                      
REMARK 465     SER B   105                                                      
REMARK 465     SER B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     ASP B   130                                                      
REMARK 465     PRO B   131                                                      
REMARK 465     ALA B   132                                                      
REMARK 465     PRO B   133                                                      
REMARK 465     TYR B   134                                                      
REMARK 465     LYS B   135                                                      
REMARK 465     ASN B   136                                                      
REMARK 465     PRO B   137                                                      
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 A  21      -16.87     80.26                                   
REMARK 500    ASP A  49       50.50    -90.42                                   
REMARK 500    SER A 105      152.51    -45.51                                   
REMARK 500    PRO A 133       27.69    -63.75                                   
REMARK 500    LYS A 135       86.09     34.19                                   
REMARK 500    SER B   2       88.24    -69.39                                   
REMARK 500    ASP B 109      116.56    174.36                                   
REMARK 500    TYR B 118       -3.24    -59.43                                   
REMARK 500    ARG B 139      122.43    178.07                                   
REMARK 500    SER B 144       32.74    -93.10                                   
REMARK 500    PRO B 146        2.05    -57.61                                   
REMARK 500    THR B 151      -73.11    -63.34                                   
REMARK 500    ALA B 153       80.47    -62.56                                   
REMARK 500    PRO B 168       -0.63    -58.15                                   
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 237        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A 253        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH A 269        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH A 278        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH A 292        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A 296        DISTANCE =  7.75 ANGSTROMS                       
REMARK 525    HOH B 223        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH B 225        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH B 245        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH B 249        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH B 251        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH B 266        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH B 274        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH B 281        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH B 282        DISTANCE =  5.75 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 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 202                 
DBREF  2GI7 A    1   183  GB     70673338 AAH69485        21    203             
DBREF  2GI7 B    1   183  GB     70673338 AAH69485        21    203             
SEQADV 2GI7 GLY A    0  GB   70673338            CLONING ARTIFACT               
SEQADV 2GI7 GLY B    0  GB   70673338            CLONING ARTIFACT               
SEQRES   1 A  184  GLY GLN SER GLY PRO LEU PRO LYS PRO SER LEU GLN ALA          
SEQRES   2 A  184  LEU PRO SER SER LEU VAL PRO LEU GLU LYS PRO VAL THR          
SEQRES   3 A  184  LEU ARG CYS GLN GLY PRO PRO GLY VAL ASP LEU TYR ARG          
SEQRES   4 A  184  LEU GLU LYS LEU SER SER SER ARG TYR GLN ASP GLN ALA          
SEQRES   5 A  184  VAL LEU PHE ILE PRO ALA MET LYS ARG SER LEU ALA GLY          
SEQRES   6 A  184  ARG TYR ARG CYS SER TYR GLN ASN GLY SER LEU TRP SER          
SEQRES   7 A  184  LEU PRO SER ASP GLN LEU GLU LEU VAL ALA THR GLY VAL          
SEQRES   8 A  184  PHE ALA LYS PRO SER LEU SER ALA GLN PRO GLY PRO ALA          
SEQRES   9 A  184  VAL SER SER GLY GLY ASP VAL THR LEU GLN CYS GLN THR          
SEQRES  10 A  184  ARG TYR GLY PHE ASP GLN PHE ALA LEU TYR LYS GLU GLY          
SEQRES  11 A  184  ASP PRO ALA PRO TYR LYS ASN PRO GLU ARG TRP TYR ARG          
SEQRES  12 A  184  ALA SER PHE PRO ILE ILE THR VAL THR ALA ALA HIS SER          
SEQRES  13 A  184  GLY THR TYR ARG CYS TYR SER PHE SER SER ARG ASP PRO          
SEQRES  14 A  184  TYR LEU TRP SER ALA PRO SER ASP PRO LEU GLU LEU VAL          
SEQRES  15 A  184  VAL THR                                                      
SEQRES   1 B  184  GLY GLN SER GLY PRO LEU PRO LYS PRO SER LEU GLN ALA          
SEQRES   2 B  184  LEU PRO SER SER LEU VAL PRO LEU GLU LYS PRO VAL THR          
SEQRES   3 B  184  LEU ARG CYS GLN GLY PRO PRO GLY VAL ASP LEU TYR ARG          
SEQRES   4 B  184  LEU GLU LYS LEU SER SER SER ARG TYR GLN ASP GLN ALA          
SEQRES   5 B  184  VAL LEU PHE ILE PRO ALA MET LYS ARG SER LEU ALA GLY          
SEQRES   6 B  184  ARG TYR ARG CYS SER TYR GLN ASN GLY SER LEU TRP SER          
SEQRES   7 B  184  LEU PRO SER ASP GLN LEU GLU LEU VAL ALA THR GLY VAL          
SEQRES   8 B  184  PHE ALA LYS PRO SER LEU SER ALA GLN PRO GLY PRO ALA          
SEQRES   9 B  184  VAL SER SER GLY GLY ASP VAL THR LEU GLN CYS GLN THR          
SEQRES  10 B  184  ARG TYR GLY PHE ASP GLN PHE ALA LEU TYR LYS GLU GLY          
SEQRES  11 B  184  ASP PRO ALA PRO TYR LYS ASN PRO GLU ARG TRP TYR ARG          
SEQRES  12 B  184  ALA SER PHE PRO ILE ILE THR VAL THR ALA ALA HIS SER          
SEQRES  13 B  184  GLY THR TYR ARG CYS TYR SER PHE SER SER ARG ASP PRO          
SEQRES  14 B  184  TYR LEU TRP SER ALA PRO SER ASP PRO LEU GLU LEU VAL          
SEQRES  15 B  184  VAL THR                                                      
HET    SO4  A 203       5                                                       
HET    SO4  A 204       5                                                       
HET     CL  B 205       1                                                       
HET    GOL  B 201       6                                                       
HET    GOL  A 202       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   8  HOH   *177(H2 O)                                                    
HELIX    1   1 LYS A   59  ALA A   63  5                                   5    
HELIX    2   2 LYS B   59  ALA B   63  5                                   5    
SHEET    1   A 3 SER A   9  LEU A  13  0                                        
SHEET    2   A 3 VAL A  24  GLN A  29 -1  O  GLN A  29   N  SER A   9           
SHEET    3   A 3 VAL A  52  ILE A  55 -1  O  LEU A  53   N  LEU A  26           
SHEET    1   B 5 LEU A  17  PRO A  19  0                                        
SHEET    2   B 5 LEU A  83  THR A  88  1  O  VAL A  86   N  VAL A  18           
SHEET    3   B 5 GLY A  64  ASN A  72 -1  N  TYR A  66   O  LEU A  83           
SHEET    4   B 5 LEU A  36  LYS A  41 -1  N  GLU A  40   O  ARG A  67           
SHEET    5   B 5 TYR A  47  GLN A  48 -1  O  GLN A  48   N  LEU A  39           
SHEET    1   C 4 LEU A  17  PRO A  19  0                                        
SHEET    2   C 4 LEU A  83  THR A  88  1  O  VAL A  86   N  VAL A  18           
SHEET    3   C 4 GLY A  64  ASN A  72 -1  N  TYR A  66   O  LEU A  83           
SHEET    4   C 4 LEU A  75  TRP A  76 -1  O  LEU A  75   N  ASN A  72           
SHEET    1   D 3 SER A  95  GLN A  99  0                                        
SHEET    2   D 3 VAL A 110  GLN A 115 -1  O  GLN A 113   N  SER A  97           
SHEET    3   D 3 ILE A 147  VAL A 150 -1  O  VAL A 150   N  VAL A 110           
SHEET    1   E 8 ARG A 139  ALA A 143  0                                        
SHEET    2   E 8 GLN A 122  LYS A 127 -1  N  LEU A 125   O  TYR A 141           
SHEET    3   E 8 GLY A 156  PHE A 163 -1  O  ARG A 159   N  TYR A 126           
SHEET    4   E 8 LEU A 178  VAL A 182 -1  O  LEU A 178   N  TYR A 158           
SHEET    5   E 8 LEU B 178  THR B 183  1  O  VAL B 181   N  GLU A 179           
SHEET    6   E 8 GLY B 156  PHE B 163 -1  N  GLY B 156   O  LEU B 180           
SHEET    7   E 8 GLN B 122  LYS B 127 -1  N  ALA B 124   O  TYR B 161           
SHEET    8   E 8 TRP B 140  ALA B 143 -1  O  TYR B 141   N  LEU B 125           
SHEET    1   F 3 SER B   9  LEU B  13  0                                        
SHEET    2   F 3 VAL B  24  GLN B  29 -1  O  GLN B  29   N  SER B   9           
SHEET    3   F 3 VAL B  52  ILE B  55 -1  O  ILE B  55   N  VAL B  24           
SHEET    1   G 5 LEU B  17  PRO B  19  0                                        
SHEET    2   G 5 LEU B  83  THR B  88  1  O  VAL B  86   N  VAL B  18           
SHEET    3   G 5 GLY B  64  ASN B  72 -1  N  TYR B  66   O  LEU B  83           
SHEET    4   G 5 LEU B  36  LYS B  41 -1  N  GLU B  40   O  ARG B  67           
SHEET    5   G 5 TYR B  47  GLN B  48 -1  O  GLN B  48   N  LEU B  39           
SHEET    1   H 4 LEU B  17  PRO B  19  0                                        
SHEET    2   H 4 LEU B  83  THR B  88  1  O  VAL B  86   N  VAL B  18           
SHEET    3   H 4 GLY B  64  ASN B  72 -1  N  TYR B  66   O  LEU B  83           
SHEET    4   H 4 LEU B  75  TRP B  76 -1  O  LEU B  75   N  ASN B  72           
SHEET    1   I 3 SER B  95  SER B  97  0                                        
SHEET    2   I 3 VAL B 110  GLN B 115 -1  O  GLN B 115   N  SER B  95           
SHEET    3   I 3 ILE B 147  VAL B 150 -1  O  ILE B 148   N  LEU B 112           
SSBOND   1 CYS A   28    CYS A   68                          1555   1555  2.04  
SSBOND   2 CYS A  114    CYS A  160                          1555   1555  2.05  
SSBOND   3 CYS B   28    CYS B   68                          1555   1555  2.03  
SSBOND   4 CYS B  114    CYS B  160                          1555   1555  2.04  
CISPEP   1 LEU A   13    PRO A   14          0         0.22                     
CISPEP   2 ALA A  132    PRO A  133          0         0.30                     
CISPEP   3 LEU B   13    PRO B   14          0        -0.16                     
SITE     1 AC1  4 GLY A  64  ARG A  65  TYR A 169  HOH A 206                    
SITE     1 AC2  4 LEU A  39  ARG A  46  GLN A  48  LEU A  53                    
SITE     1 AC3  1 ARG B  65                                                     
SITE     1 AC4  2 ARG B  60  SER B  61                                          
SITE     1 AC5  1 TRP A 171                                                     
CRYST1  114.057   45.286   75.131  90.00  90.00  90.00 P 21 21 2     8          
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      0.008768  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.022082  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013310        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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