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Database: PDB
Entry: 5OU8
LinkDB: 5OU8
Original site: 5OU8 
HEADER    BLOOD CLOTTING                          23-AUG-17   5OU8              
TITLE     CRYSTAL STRUCTURE OF GLYCOPROTEIN VI IN COMPLEX WITH COLLAGEN-PEPTIDE 
TITLE    2 (GPO)5                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET GLYCOPROTEIN VI;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GPVI,GLYCOPROTEIN 6;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: (GPO)5;                                                    
COMPND   9 CHAIN: C, D, E;                                                      
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: GP6;                                                           
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293-EBNA1-S;                         
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    PLATELET, GLYCOPROTEIN, GPVI, COLLAGEN-BINDING, PLATELET ACTIVATION,  
KEYWDS   2 GPO5, CRP, BLOOD CLOTTING                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.FEITSMA,E.G.HUIZINGA                                              
REVDAT   2   29-JUL-20 5OU8    1       COMPND REMARK HETNAM LINK                
REVDAT   2 2                   1       SITE                                     
REVDAT   1   05-SEP-18 5OU8    0                                                
JRNL        AUTH   L.J.FEITSMA,T.H.C.BRONDIJK,G.JARVIS,D.HAGEMANS,D.BIHAN,      
JRNL        AUTH 2 N.JERAH,M.VERSTEEG,R.W.FARNDALE,E.G.HUIZINGA                 
JRNL        TITL   STRUCTURAL INSIGHTS INTO COLLAGEN-BINDING BY PLATELET        
JRNL        TITL 2 RECEPTOR GLYCOPROTEIN VI                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 78.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19700                          
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 + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
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      : 1022                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1399                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 65                           
REMARK   3   BIN FREE R VALUE                    : 0.4580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2959                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.28000                                             
REMARK   3    B22 (A**2) : -0.28000                                             
REMARK   3    B33 (A**2) : 0.56000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.348         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.261         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.193         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.995        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3134 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2870 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4296 ; 1.635 ; 2.055       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6693 ; 1.093 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   388 ; 6.894 ; 5.026       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   115 ;34.965 ;22.522       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   432 ;15.304 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;22.325 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   459 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3445 ; 0.007 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):   646 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1551 ; 2.009 ; 3.701       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1551 ; 2.008 ; 3.701       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1931 ; 3.399 ; 5.538       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1932 ; 3.399 ; 5.542       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1583 ; 2.026 ; 3.953       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1583 ; 2.025 ; 3.953       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2364 ; 3.310 ; 5.830       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3215 ; 5.668 ;29.805       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3199 ; 5.636 ;29.726       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   173                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.4880  13.2450 -23.3750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0751 T22:   0.2019                                     
REMARK   3      T33:   0.0821 T12:  -0.0685                                     
REMARK   3      T13:  -0.0350 T23:   0.0403                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2007 L22:   3.3948                                     
REMARK   3      L33:   1.4746 L12:   0.1842                                     
REMARK   3      L13:   0.1170 L23:  -1.5996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0260 S12:   0.0339 S13:   0.2463                       
REMARK   3      S21:   0.2431 S22:  -0.0241 S23:   0.0029                       
REMARK   3      S31:  -0.2611 S32:   0.0374 S33:   0.0501                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     5        B   173                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9670   6.1460  19.8840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2440 T22:   0.0655                                     
REMARK   3      T33:   0.0856 T12:   0.0040                                     
REMARK   3      T13:   0.0250 T23:   0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5737 L22:   2.1821                                     
REMARK   3      L33:   5.2260 L12:   0.9819                                     
REMARK   3      L13:   2.1626 L23:   2.3553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0082 S12:  -0.1554 S13:   0.0697                       
REMARK   3      S21:  -0.3536 S22:  -0.0227 S23:  -0.1877                       
REMARK   3      S31:  -0.3757 S32:  -0.2114 S33:   0.0145                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    15                          
REMARK   3    RESIDUE RANGE :   D     1        D    15                          
REMARK   3    RESIDUE RANGE :   E     1        E    15                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.8350  -1.5740  -6.3410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0839 T22:   0.1668                                     
REMARK   3      T33:   0.0639 T12:   0.0930                                     
REMARK   3      T13:   0.0092 T23:   0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4778 L22:  15.0488                                     
REMARK   3      L33:   7.3022 L12:   5.6800                                     
REMARK   3      L13:   3.2155 L23:   8.1082                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2721 S12:  -0.2283 S13:  -0.2100                       
REMARK   3      S21:  -0.1256 S22:   0.0782 S23:   0.0537                       
REMARK   3      S31:  -0.4419 S32:  -0.4708 S33:   0.1940                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5OU8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006353.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97242                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 1.0.7                      
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.1.30                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20736                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : 0.12100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.03000                            
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 2.7.0                                          
REMARK 200 STARTING MODEL: 5OU7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0 0.2 M MGCL2 20% (W/V)   
REMARK 280  PEG-6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
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      156.60600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       29.98500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       29.98500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       78.30300            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       29.98500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       29.98500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      234.90900            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       29.98500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       29.98500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       78.30300            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       29.98500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       29.98500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      234.90900            
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      156.60600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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    -1                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     ALA A   177                                                      
REMARK 465     ALA A   178                                                      
REMARK 465     ALA A   179                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     THR B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     ALA B   177                                                      
REMARK 465     ALA B   178                                                      
REMARK 465     ALA B   179                                                      
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    ASP A  49       50.36    -94.82                                   
REMARK 500    GLU B  21       -0.81     76.55                                   
REMARK 500    ASP B  49       44.48    -90.00                                   
REMARK 500    TYR B 114      153.02    -45.48                                   
REMARK 500    PRO B 136       40.25    -75.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG4 B  203                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5OU7   RELATED DB: PDB                                   
REMARK 900 UNCOMPLEXED FORM OF GPVI                                             
DBREF  5OU8 A    1   176  UNP    Q9HCN6   GPVI_HUMAN      21    206             
DBREF  5OU8 B    1   176  UNP    Q9HCN6   GPVI_HUMAN      21    206             
DBREF  5OU8 C    1    15  PDB    5OU8     5OU8             1     15             
DBREF  5OU8 D    1    15  PDB    5OU8     5OU8             1     15             
DBREF  5OU8 E    1    15  PDB    5OU8     5OU8             1     15             
SEQADV 5OU8 GLY A   -1  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8 SER A    0  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8     A       UNP  Q9HCN6    PRO   122 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    ALA   123 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    VAL   124 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    SER   125 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    PRO   151 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    ALA   152 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    PRO   153 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    TYR   154 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    LYS   155 DELETION                       
SEQADV 5OU8     A       UNP  Q9HCN6    ASN   156 DELETION                       
SEQADV 5OU8 ALA A  177  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8 ALA A  178  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8 ALA A  179  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8 GLY B   -1  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8 SER B    0  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8     B       UNP  Q9HCN6    PRO   122 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    ALA   123 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    VAL   124 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    SER   125 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    PRO   151 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    ALA   152 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    PRO   153 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    TYR   154 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    LYS   155 DELETION                       
SEQADV 5OU8     B       UNP  Q9HCN6    ASN   156 DELETION                       
SEQADV 5OU8 ALA B  177  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8 ALA B  178  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU8 ALA B  179  UNP  Q9HCN6              EXPRESSION TAG                 
SEQRES   1 A  181  GLY SER GLN SER GLY PRO LEU PRO LYS PRO SER LEU GLN          
SEQRES   2 A  181  ALA LEU PRO SER SER LEU VAL PRO LEU GLU LYS PRO VAL          
SEQRES   3 A  181  THR LEU ARG CYS GLN GLY PRO PRO GLY VAL ASP LEU TYR          
SEQRES   4 A  181  ARG LEU GLU LYS LEU SER SER SER ARG TYR GLN ASP GLN          
SEQRES   5 A  181  ALA VAL LEU PHE ILE PRO ALA MET LYS ARG SER LEU ALA          
SEQRES   6 A  181  GLY ARG TYR ARG CYS SER TYR GLN ASN GLY SER LEU TRP          
SEQRES   7 A  181  SER LEU PRO SER ASP GLN LEU GLU LEU VAL ALA THR GLY          
SEQRES   8 A  181  VAL PHE ALA LYS PRO SER LEU SER ALA GLN PRO GLY SER          
SEQRES   9 A  181  GLY GLY ASP VAL THR LEU GLN CYS GLN THR ARG TYR GLY          
SEQRES  10 A  181  PHE ASP GLN PHE ALA LEU TYR LYS GLU GLY ASP PRO GLU          
SEQRES  11 A  181  ARG TRP TYR ARG ALA SER PHE PRO ILE ILE THR VAL THR          
SEQRES  12 A  181  ALA ALA HIS SER GLY THR TYR ARG CYS TYR SER PHE SER          
SEQRES  13 A  181  SER ARG ASP PRO TYR LEU TRP SER ALA PRO SER ASP PRO          
SEQRES  14 A  181  LEU GLU LEU VAL VAL THR GLY THR SER ALA ALA ALA              
SEQRES   1 B  181  GLY SER GLN SER GLY PRO LEU PRO LYS PRO SER LEU GLN          
SEQRES   2 B  181  ALA LEU PRO SER SER LEU VAL PRO LEU GLU LYS PRO VAL          
SEQRES   3 B  181  THR LEU ARG CYS GLN GLY PRO PRO GLY VAL ASP LEU TYR          
SEQRES   4 B  181  ARG LEU GLU LYS LEU SER SER SER ARG TYR GLN ASP GLN          
SEQRES   5 B  181  ALA VAL LEU PHE ILE PRO ALA MET LYS ARG SER LEU ALA          
SEQRES   6 B  181  GLY ARG TYR ARG CYS SER TYR GLN ASN GLY SER LEU TRP          
SEQRES   7 B  181  SER LEU PRO SER ASP GLN LEU GLU LEU VAL ALA THR GLY          
SEQRES   8 B  181  VAL PHE ALA LYS PRO SER LEU SER ALA GLN PRO GLY SER          
SEQRES   9 B  181  GLY GLY ASP VAL THR LEU GLN CYS GLN THR ARG TYR GLY          
SEQRES  10 B  181  PHE ASP GLN PHE ALA LEU TYR LYS GLU GLY ASP PRO GLU          
SEQRES  11 B  181  ARG TRP TYR ARG ALA SER PHE PRO ILE ILE THR VAL THR          
SEQRES  12 B  181  ALA ALA HIS SER GLY THR TYR ARG CYS TYR SER PHE SER          
SEQRES  13 B  181  SER ARG ASP PRO TYR LEU TRP SER ALA PRO SER ASP PRO          
SEQRES  14 B  181  LEU GLU LEU VAL VAL THR GLY THR SER ALA ALA ALA              
SEQRES   1 C   15  GLY PRO HYP GLY PRO HYP GLY PRO HYP GLY PRO HYP GLY          
SEQRES   2 C   15  PRO HYP                                                      
SEQRES   1 D   15  GLY PRO HYP GLY PRO HYP GLY PRO HYP GLY PRO HYP GLY          
SEQRES   2 D   15  PRO HYP                                                      
SEQRES   1 E   15  GLY PRO HYP GLY PRO HYP GLY PRO HYP GLY PRO HYP GLY          
SEQRES   2 E   15  PRO HYP                                                      
HET    HYP  C   3       8                                                       
HET    HYP  C   6       8                                                       
HET    HYP  C   9       8                                                       
HET    HYP  C  12       8                                                       
HET    HYP  C  15       8                                                       
HET    HYP  D   3       8                                                       
HET    HYP  D   6       8                                                       
HET    HYP  D   9       8                                                       
HET    HYP  D  12       8                                                       
HET    HYP  D  15       8                                                       
HET    HYP  E   3       8                                                       
HET    HYP  E   6       8                                                       
HET    HYP  E   9       8                                                       
HET    HYP  E  12       8                                                       
HET    HYP  E  15       8                                                       
HET     CL  A 201       1                                                       
HET    NAG  A 202      14                                                       
HET    PG4  A 203      13                                                       
HET     CL  B 201       1                                                       
HET    NAG  B 202      14                                                       
HET    PG4  B 203      10                                                       
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     HYP HYDROXYPROLINE                                                   
FORMUL   3  HYP    15(C5 H9 N O3)                                               
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   7  NAG    2(C8 H15 N O6)                                               
FORMUL   8  PG4    2(C8 H18 O5)                                                 
FORMUL  12  HOH   *88(H2 O)                                                     
HELIX    1 AA1 LYS A   59  ALA A   63  5                                   5    
HELIX    2 AA2 LYS B   59  ALA B   63  5                                   5    
SHEET    1 AA1 3 SER A   9  LEU A  13  0                                        
SHEET    2 AA1 3 VAL A  24  GLN A  29 -1  O  GLN A  29   N  SER A   9           
SHEET    3 AA1 3 VAL A  52  ILE A  55 -1  O  ILE A  55   N  VAL A  24           
SHEET    1 AA2 5 LEU A  17  PRO A  19  0                                        
SHEET    2 AA2 5 LEU A  83  THR A  88  1  O  THR A  88   N  VAL A  18           
SHEET    3 AA2 5 GLY A  64  ASN A  72 -1  N  GLY A  64   O  LEU A  85           
SHEET    4 AA2 5 LEU A  36  LYS A  41 -1  N  ARG A  38   O  SER A  69           
SHEET    5 AA2 5 TYR A  47  GLN A  48 -1  O  GLN A  48   N  LEU A  39           
SHEET    1 AA3 4 LEU A  17  PRO A  19  0                                        
SHEET    2 AA3 4 LEU A  83  THR A  88  1  O  THR A  88   N  VAL A  18           
SHEET    3 AA3 4 GLY A  64  ASN A  72 -1  N  GLY A  64   O  LEU A  85           
SHEET    4 AA3 4 LEU A  75  TRP A  76 -1  O  LEU A  75   N  ASN A  72           
SHEET    1 AA4 3 SER A  95  PRO A 100  0                                        
SHEET    2 AA4 3 ASP A 105  GLN A 111 -1  O  THR A 107   N  GLN A  99           
SHEET    3 AA4 3 ILE A 137  THR A 141 -1  O  ILE A 138   N  LEU A 108           
SHEET    1 AA5 4 ARG A 129  ALA A 133  0                                        
SHEET    2 AA5 4 GLN A 118  LYS A 123 -1  N  LEU A 121   O  TYR A 131           
SHEET    3 AA5 4 GLY A 146  PHE A 153 -1  O  ARG A 149   N  TYR A 122           
SHEET    4 AA5 4 LEU A 168  LEU A 170 -1  O  LEU A 168   N  TYR A 148           
SHEET    1 AA6 3 SER B   9  LEU B  13  0                                        
SHEET    2 AA6 3 VAL B  24  GLN B  29 -1  O  GLN B  29   N  SER B   9           
SHEET    3 AA6 3 VAL B  52  ILE B  55 -1  O  ILE B  55   N  VAL B  24           
SHEET    1 AA7 5 LEU B  17  PRO B  19  0                                        
SHEET    2 AA7 5 LEU B  83  THR B  88  1  O  VAL B  86   N  VAL B  18           
SHEET    3 AA7 5 GLY B  64  ASN B  72 -1  N  TYR B  66   O  LEU B  83           
SHEET    4 AA7 5 LEU B  36  LYS B  41 -1  N  ARG B  38   O  SER B  69           
SHEET    5 AA7 5 ARG B  46  GLN B  48 -1  O  ARG B  46   N  LYS B  41           
SHEET    1 AA8 4 LEU B  17  PRO B  19  0                                        
SHEET    2 AA8 4 LEU B  83  THR B  88  1  O  VAL B  86   N  VAL B  18           
SHEET    3 AA8 4 GLY B  64  ASN B  72 -1  N  TYR B  66   O  LEU B  83           
SHEET    4 AA8 4 LEU B  75  TRP B  76 -1  O  LEU B  75   N  ASN B  72           
SHEET    1 AA9 3 SER B  95  PRO B 100  0                                        
SHEET    2 AA9 3 VAL B 106  GLN B 111 -1  O  GLN B 111   N  SER B  95           
SHEET    3 AA9 3 ILE B 137  VAL B 140 -1  O  ILE B 138   N  LEU B 108           
SHEET    1 AB1 4 ARG B 129  ALA B 133  0                                        
SHEET    2 AB1 4 GLN B 118  LYS B 123 -1  N  LEU B 121   O  TYR B 131           
SHEET    3 AB1 4 GLY B 146  SER B 154 -1  O  TYR B 151   N  ALA B 120           
SHEET    4 AB1 4 ASP B 157  TRP B 161 -1  O  ASP B 157   N  SER B 154           
SHEET    1 AB2 4 ARG B 129  ALA B 133  0                                        
SHEET    2 AB2 4 GLN B 118  LYS B 123 -1  N  LEU B 121   O  TYR B 131           
SHEET    3 AB2 4 GLY B 146  SER B 154 -1  O  TYR B 151   N  ALA B 120           
SHEET    4 AB2 4 LEU B 168  LEU B 170 -1  O  LEU B 168   N  TYR B 148           
SSBOND   1 CYS A   28    CYS A   68                          1555   1555  2.07  
SSBOND   2 CYS A  110    CYS A  150                          1555   1555  2.07  
SSBOND   3 CYS B   28    CYS B   68                          1555   1555  2.05  
SSBOND   4 CYS B  110    CYS B  150                          1555   1555  2.10  
LINK         ND2 ASN A  72                 C1  NAG A 202     1555   1555  1.44  
LINK         ND2 ASN B  72                 C1  NAG B 202     1555   1555  1.46  
LINK         C   PRO C   2                 N   HYP C   3     1555   1555  1.36  
LINK         C   HYP C   3                 N   GLY C   4     1555   1555  1.34  
LINK         C   PRO C   5                 N   HYP C   6     1555   1555  1.34  
LINK         C   HYP C   6                 N   GLY C   7     1555   1555  1.33  
LINK         C   PRO C   8                 N   HYP C   9     1555   1555  1.33  
LINK         C   HYP C   9                 N   GLY C  10     1555   1555  1.33  
LINK         C   PRO C  11                 N   HYP C  12     1555   1555  1.34  
LINK         C   HYP C  12                 N   GLY C  13     1555   1555  1.32  
LINK         C   PRO C  14                 N   HYP C  15     1555   1555  1.33  
LINK         C   PRO D   2                 N   HYP D   3     1555   1555  1.34  
LINK         C   HYP D   3                 N   GLY D   4     1555   1555  1.33  
LINK         C   PRO D   5                 N   HYP D   6     1555   1555  1.32  
LINK         C   HYP D   6                 N   GLY D   7     1555   1555  1.33  
LINK         C   PRO D   8                 N   HYP D   9     1555   1555  1.32  
LINK         C   HYP D   9                 N   GLY D  10     1555   1555  1.33  
LINK         C   PRO D  11                 N   HYP D  12     1555   1555  1.34  
LINK         C   HYP D  12                 N   GLY D  13     1555   1555  1.33  
LINK         C   PRO D  14                 N   HYP D  15     1555   1555  1.35  
LINK         C   PRO E   2                 N   HYP E   3     1555   1555  1.35  
LINK         C   HYP E   3                 N   GLY E   4     1555   1555  1.31  
LINK         C   PRO E   5                 N   HYP E   6     1555   1555  1.32  
LINK         C   HYP E   6                 N   GLY E   7     1555   1555  1.33  
LINK         C   PRO E   8                 N   HYP E   9     1555   1555  1.34  
LINK         C   HYP E   9                 N   GLY E  10     1555   1555  1.32  
LINK         C   PRO E  11                 N   HYP E  12     1555   1555  1.34  
LINK         C   HYP E  12                 N   GLY E  13     1555   1555  1.33  
LINK         C   PRO E  14                 N   HYP E  15     1555   1555  1.35  
CISPEP   1 LEU A   13    PRO A   14          0         5.19                     
CISPEP   2 ASP A  126    PRO A  127          0         2.18                     
CISPEP   3 LEU B   13    PRO B   14          0        13.25                     
CISPEP   4 ASP B  126    PRO B  127          0        -1.71                     
CRYST1   59.970   59.970  313.212  90.00  90.00  90.00 P 41 21 2    24          
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      0.016675  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016675  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003193        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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