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Database: PDB
Entry: 5OU7
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Original site: 5OU7 
HEADER    BLOOD CLOTTING                          23-AUG-17   5OU7              
TITLE     CRYSTAL STRUCTURE OF THE GLYCOPROTEIN VI LOOP TRUNCATION MUTANT PAVS- 
TITLE    2 PAPYKN                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET GLYCOPROTEIN VI;                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: GPVI,GLYCOPROTEIN 6;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 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                          
KEYWDS    PLATELET, GLYCOPROTEIN, GPVI, COLLAGEN-BINDING, PLATELET ACTIVATION,  
KEYWDS   2 BLOOD CLOTTING                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.FEITSMA,E.G.HUIZINGA                                              
REVDAT   2   29-JUL-20 5OU7    1       COMPND REMARK HETNAM LINK                
REVDAT   2 2                   1       SITE                                     
REVDAT   1   05-SEP-18 5OU7    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 113.81                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 55826                          
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) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2967                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3987                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 190                          
REMARK   3   BIN FREE R VALUE                    : 0.4060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5426                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 112                                     
REMARK   3   SOLVENT ATOMS            : 344                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.61000                                             
REMARK   3    B22 (A**2) : -0.48000                                             
REMARK   3    B33 (A**2) : 0.93000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.192         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.169         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.313        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5945 ; 0.011 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  5615 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8148 ; 1.480 ; 2.004       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13009 ; 0.779 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   770 ; 7.032 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   239 ;30.025 ;22.259       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   943 ;14.435 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;16.737 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   888 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6648 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1348 ; 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):  2876 ; 1.984 ; 2.621       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2875 ; 1.982 ; 2.621       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3606 ; 3.314 ; 3.916       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3607 ; 3.314 ; 3.916       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3069 ; 2.201 ; 2.978       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3069 ; 2.201 ; 2.978       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4507 ; 3.605 ; 4.346       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6279 ; 6.225 ;21.793       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6182 ; 6.139 ;21.528       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      2       B     174      2                      
REMARK   3           1     A      2       A     174      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1838 ;  0.71 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1029 ;  0.57 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1838 ;  1.43 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : D C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D      2       D     179      2                      
REMARK   3           1     C      2       C     179      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    C    (A):   1678 ;  0.42 ;  0.50           
REMARK   3   TIGHT THERMAL      2    C (A**2):   1039 ;  1.37 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    C (A**2):   1678 ;  1.88 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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     2        A   174                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.3152  -4.2205  -8.0809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0065 T22:   0.0038                                     
REMARK   3      T33:   0.0883 T12:  -0.0023                                     
REMARK   3      T13:  -0.0064 T23:   0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3153 L22:   0.6745                                     
REMARK   3      L33:   0.0767 L12:  -0.2482                                     
REMARK   3      L13:   0.1494 L23:  -0.1064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0029 S12:   0.0255 S13:  -0.0074                       
REMARK   3      S21:  -0.0440 S22:  -0.0150 S23:  -0.0431                       
REMARK   3      S31:  -0.0060 S32:   0.0153 S33:   0.0179                       
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     2        B   174                          
REMARK   3    ORIGIN FOR THE GROUP (A): -69.7232  -8.1676 -48.8131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0071 T22:   0.0093                                     
REMARK   3      T33:   0.0912 T12:   0.0056                                     
REMARK   3      T13:  -0.0030 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3218 L22:   0.7931                                     
REMARK   3      L33:   0.0663 L12:   0.2744                                     
REMARK   3      L13:   0.1381 L23:   0.1640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0073 S12:  -0.0408 S13:  -0.0211                       
REMARK   3      S21:   0.0499 S22:  -0.0058 S23:   0.0404                       
REMARK   3      S31:  -0.0007 S32:  -0.0181 S33:   0.0132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4190 -16.5085 -17.6900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0289 T22:   0.0440                                     
REMARK   3      T33:   0.1059 T12:  -0.0213                                     
REMARK   3      T13:  -0.0036 T23:  -0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0753 L22:   0.2655                                     
REMARK   3      L33:   0.1677 L12:  -0.0940                                     
REMARK   3      L13:  -0.3140 L23:  -0.1110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0556 S12:   0.1545 S13:   0.0569                       
REMARK   3      S21:  -0.0746 S22:   0.0414 S23:  -0.0303                       
REMARK   3      S31:   0.0597 S32:  -0.0762 S33:   0.0142                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):-111.5443 -20.4611 -39.1851              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0232 T22:   0.0356                                     
REMARK   3      T33:   0.1098 T12:   0.0177                                     
REMARK   3      T13:  -0.0086 T23:   0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1681 L22:   0.1263                                     
REMARK   3      L33:   0.1376 L12:   0.0835                                     
REMARK   3      L13:  -0.2942 L23:   0.0661                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0561 S12:  -0.1399 S13:   0.0119                       
REMARK   3      S21:   0.0377 S22:   0.0236 S23:   0.0381                       
REMARK   3      S31:   0.0440 S32:   0.0574 S33:   0.0325                       
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 5OU7 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_1200006350.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99999                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
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   : 58873                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 113.810                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.08000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
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: 2GI7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PHOSPHATE-CITRATE BUFFER PH 4.0    
REMARK 280  40% (V/V) PEG-300, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       22.02500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     SER A     0                                                      
REMARK 465     GLN A     1                                                      
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     THR B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     ALA B   177                                                      
REMARK 465     ALA B   178                                                      
REMARK 465     ALA B   179                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     GLN C     1                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     GLN D     1                                                      
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   O    HOH C   340     O    HOH C   350              1.96            
REMARK 500   NE2  GLN A    11     O    HOH A   301              2.00            
REMARK 500   O    HOH C   355     O    HOH C   356              2.02            
REMARK 500   O    HOH A   377     O    HOH A   394              2.07            
REMARK 500   CZ3  TRP C    76     O    HOH C   342              2.13            
REMARK 500   O    HOH C   357     O    HOH C   359              2.13            
REMARK 500   NH2  ARG C    65     O    HOH C   301              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   395     O    HOH C   359     1455     2.03            
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    ASP A  49       49.46    -90.73                                   
REMARK 500    ASP B  49       52.35    -90.64                                   
REMARK 500    ASP C  49       40.08    -98.21                                   
REMARK 500    ASP D  49       44.40   -103.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER C   74     LEU C   75                 -149.47                    
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 B 408        DISTANCE =  6.65 ANGSTROMS                       
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     PG6 A  207                                                       
REMARK 610     PG6 B  207                                                       
DBREF  5OU7 A    1   176  UNP    Q9HCN6   GPVI_HUMAN      21    206             
DBREF  5OU7 B    1   176  UNP    Q9HCN6   GPVI_HUMAN      21    206             
DBREF  5OU7 C    1   176  UNP    Q9HCN6   GPVI_HUMAN      21    206             
DBREF  5OU7 D    1   176  UNP    Q9HCN6   GPVI_HUMAN      21    206             
SEQADV 5OU7 GLY A   -1  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 SER A    0  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7     A       UNP  Q9HCN6    PRO   122 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    ALA   123 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    VAL   124 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    SER   125 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    PRO   151 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    ALA   152 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    PRO   153 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    TYR   154 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    LYS   155 DELETION                       
SEQADV 5OU7     A       UNP  Q9HCN6    ASN   156 DELETION                       
SEQADV 5OU7 ALA A  177  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 ALA A  178  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 ALA A  179  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 GLY B   -1  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 SER B    0  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7     B       UNP  Q9HCN6    PRO   122 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    ALA   123 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    VAL   124 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    SER   125 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    PRO   151 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    ALA   152 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    PRO   153 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    TYR   154 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    LYS   155 DELETION                       
SEQADV 5OU7     B       UNP  Q9HCN6    ASN   156 DELETION                       
SEQADV 5OU7 ALA B  177  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 ALA B  178  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 ALA B  179  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 GLY C   -1  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 SER C    0  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7     C       UNP  Q9HCN6    PRO   122 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    ALA   123 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    VAL   124 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    SER   125 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    PRO   151 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    ALA   152 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    PRO   153 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    TYR   154 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    LYS   155 DELETION                       
SEQADV 5OU7     C       UNP  Q9HCN6    ASN   156 DELETION                       
SEQADV 5OU7 ALA C  177  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 ALA C  178  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 ALA C  179  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 GLY D   -1  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 SER D    0  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7     D       UNP  Q9HCN6    PRO   122 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    ALA   123 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    VAL   124 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    SER   125 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    PRO   151 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    ALA   152 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    PRO   153 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    TYR   154 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    LYS   155 DELETION                       
SEQADV 5OU7     D       UNP  Q9HCN6    ASN   156 DELETION                       
SEQADV 5OU7 ALA D  177  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 ALA D  178  UNP  Q9HCN6              EXPRESSION TAG                 
SEQADV 5OU7 ALA D  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  181  GLY SER GLN SER GLY PRO LEU PRO LYS PRO SER LEU GLN          
SEQRES   2 C  181  ALA LEU PRO SER SER LEU VAL PRO LEU GLU LYS PRO VAL          
SEQRES   3 C  181  THR LEU ARG CYS GLN GLY PRO PRO GLY VAL ASP LEU TYR          
SEQRES   4 C  181  ARG LEU GLU LYS LEU SER SER SER ARG TYR GLN ASP GLN          
SEQRES   5 C  181  ALA VAL LEU PHE ILE PRO ALA MET LYS ARG SER LEU ALA          
SEQRES   6 C  181  GLY ARG TYR ARG CYS SER TYR GLN ASN GLY SER LEU TRP          
SEQRES   7 C  181  SER LEU PRO SER ASP GLN LEU GLU LEU VAL ALA THR GLY          
SEQRES   8 C  181  VAL PHE ALA LYS PRO SER LEU SER ALA GLN PRO GLY SER          
SEQRES   9 C  181  GLY GLY ASP VAL THR LEU GLN CYS GLN THR ARG TYR GLY          
SEQRES  10 C  181  PHE ASP GLN PHE ALA LEU TYR LYS GLU GLY ASP PRO GLU          
SEQRES  11 C  181  ARG TRP TYR ARG ALA SER PHE PRO ILE ILE THR VAL THR          
SEQRES  12 C  181  ALA ALA HIS SER GLY THR TYR ARG CYS TYR SER PHE SER          
SEQRES  13 C  181  SER ARG ASP PRO TYR LEU TRP SER ALA PRO SER ASP PRO          
SEQRES  14 C  181  LEU GLU LEU VAL VAL THR GLY THR SER ALA ALA ALA              
SEQRES   1 D  181  GLY SER GLN SER GLY PRO LEU PRO LYS PRO SER LEU GLN          
SEQRES   2 D  181  ALA LEU PRO SER SER LEU VAL PRO LEU GLU LYS PRO VAL          
SEQRES   3 D  181  THR LEU ARG CYS GLN GLY PRO PRO GLY VAL ASP LEU TYR          
SEQRES   4 D  181  ARG LEU GLU LYS LEU SER SER SER ARG TYR GLN ASP GLN          
SEQRES   5 D  181  ALA VAL LEU PHE ILE PRO ALA MET LYS ARG SER LEU ALA          
SEQRES   6 D  181  GLY ARG TYR ARG CYS SER TYR GLN ASN GLY SER LEU TRP          
SEQRES   7 D  181  SER LEU PRO SER ASP GLN LEU GLU LEU VAL ALA THR GLY          
SEQRES   8 D  181  VAL PHE ALA LYS PRO SER LEU SER ALA GLN PRO GLY SER          
SEQRES   9 D  181  GLY GLY ASP VAL THR LEU GLN CYS GLN THR ARG TYR GLY          
SEQRES  10 D  181  PHE ASP GLN PHE ALA LEU TYR LYS GLU GLY ASP PRO GLU          
SEQRES  11 D  181  ARG TRP TYR ARG ALA SER PHE PRO ILE ILE THR VAL THR          
SEQRES  12 D  181  ALA ALA HIS SER GLY THR TYR ARG CYS TYR SER PHE SER          
SEQRES  13 D  181  SER ARG ASP PRO TYR LEU TRP SER ALA PRO SER ASP PRO          
SEQRES  14 D  181  LEU GLU LEU VAL VAL THR GLY THR SER ALA ALA ALA              
MODRES 5OU7 NAG A  208  NAG  -D                                                 
MODRES 5OU7 NAG B  208  NAG  -D                                                 
MODRES 5OU7 NAG C  203  NAG  -D                                                 
MODRES 5OU7 NAG D  203  NAG  -D                                                 
HET     CL  A 201       1                                                       
HET     CL  A 202       1                                                       
HET     CL  A 203       1                                                       
HET     CL  A 204       1                                                       
HET     CL  A 205       1                                                       
HET    PO4  A 206       5                                                       
HET    PG6  A 207      16                                                       
HET    NAG  A 208      14                                                       
HET     CL  B 201       1                                                       
HET     CL  B 202       1                                                       
HET     CL  B 203       1                                                       
HET     CL  B 204       1                                                       
HET     CL  B 205       1                                                       
HET    PO4  B 206       5                                                       
HET    PG6  B 207      16                                                       
HET    NAG  B 208      14                                                       
HET     CL  C 201       1                                                       
HET     CL  C 202       1                                                       
HET    NAG  C 203      14                                                       
HET     CL  D 201       1                                                       
HET     CL  D 202       1                                                       
HET    NAG  D 203      14                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-                 
HETNAM   2 PG6  ETHOXY}-ETHANE                                                  
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   5   CL    14(CL 1-)                                                    
FORMUL  10  PO4    2(O4 P 3-)                                                   
FORMUL  11  PG6    2(C12 H26 O6)                                                
FORMUL  12  NAG    4(C8 H15 N O6)                                               
FORMUL  27  HOH   *344(H2 O)                                                    
HELIX    1   1 ARG A   60  LEU A   62  5                                   3    
HELIX    2   2 SER A  155  ASP A  157  5                                   3    
HELIX    3   3 ARG B   60  LEU B   62  5                                   3    
HELIX    4   4 SER B  155  ASP B  157  5                                   3    
HELIX    5   5 ARG C   60  LEU C   62  5                                   3    
HELIX    6   6 SER C  155  ASP C  157  5                                   3    
HELIX    7   7 ARG D   60  LEU D   62  5                                   3    
HELIX    8   8 SER D  155  ASP D  157  5                                   3    
SHEET    1   A 3 SER A   9  LEU A  13  0                                        
SHEET    2   A 3 VAL A  24  GLN A  29 -1                                        
SHEET    3   A 3 VAL A  52  ILE A  55 -1                                        
SHEET    1   B 2 LEU A  17  PRO A  19  0                                        
SHEET    2   B 2 VAL A  86  THR A  88  1                                        
SHEET    1   C 4 ARG A  46  GLN A  48  0                                        
SHEET    2   C 4 LEU A  36  LYS A  41 -1                                        
SHEET    3   C 4 GLY A  64  GLN A  71 -1                                        
SHEET    4   C 4 LEU A  83  LEU A  85 -1                                        
SHEET    1   D 3 SER A  95  PRO A 100  0                                        
SHEET    2   D 3 VAL A 106  GLN A 111 -1                                        
SHEET    3   D 3 ILE A 137  VAL A 140 -1                                        
SHEET    1   E 4 ARG A 129  ALA A 133  0                                        
SHEET    2   E 4 GLN A 118  LYS A 123 -1                                        
SHEET    3   E 4 GLY A 146  PHE A 153 -1                                        
SHEET    4   E 4 LEU A 168  LEU A 170 -1                                        
SHEET    1   F 3 SER B   9  LEU B  13  0                                        
SHEET    2   F 3 VAL B  24  GLN B  29 -1                                        
SHEET    3   F 3 VAL B  52  ILE B  55 -1                                        
SHEET    1   G 2 LEU B  17  PRO B  19  0                                        
SHEET    2   G 2 VAL B  86  THR B  88  1                                        
SHEET    1   H 4 ARG B  46  GLN B  48  0                                        
SHEET    2   H 4 LEU B  36  LYS B  41 -1                                        
SHEET    3   H 4 GLY B  64  GLN B  71 -1                                        
SHEET    4   H 4 LEU B  83  LEU B  85 -1                                        
SHEET    1   I 3 SER B  95  PRO B 100  0                                        
SHEET    2   I 3 VAL B 106  GLN B 111 -1                                        
SHEET    3   I 3 ILE B 137  VAL B 140 -1                                        
SHEET    1   J 4 ARG B 129  ALA B 133  0                                        
SHEET    2   J 4 GLN B 118  LYS B 123 -1                                        
SHEET    3   J 4 GLY B 146  PHE B 153 -1                                        
SHEET    4   J 4 LEU B 168  LEU B 170 -1                                        
SHEET    1   K 3 SER C   9  LEU C  13  0                                        
SHEET    2   K 3 VAL C  24  GLN C  29 -1                                        
SHEET    3   K 3 VAL C  52  ILE C  55 -1                                        
SHEET    1   L 2 LEU C  17  PRO C  19  0                                        
SHEET    2   L 2 VAL C  86  THR C  88  1                                        
SHEET    1   M 3 LEU C  36  LYS C  41  0                                        
SHEET    2   M 3 GLY C  64  GLN C  71 -1                                        
SHEET    3   M 3 LEU C  83  LEU C  85 -1                                        
SHEET    1   N 3 SER C  95  PRO C 100  0                                        
SHEET    2   N 3 ASP C 105  GLN C 111 -1                                        
SHEET    3   N 3 ILE C 137  THR C 141 -1                                        
SHEET    1   O 4 ARG C 129  ALA C 133  0                                        
SHEET    2   O 4 GLN C 118  LYS C 123 -1                                        
SHEET    3   O 4 GLY C 146  PHE C 153 -1                                        
SHEET    4   O 4 LEU C 168  LEU C 170 -1                                        
SHEET    1   P 3 SER D   9  LEU D  13  0                                        
SHEET    2   P 3 VAL D  24  GLN D  29 -1                                        
SHEET    3   P 3 VAL D  52  ILE D  55 -1                                        
SHEET    1   Q 2 LEU D  17  PRO D  19  0                                        
SHEET    2   Q 2 VAL D  86  THR D  88  1                                        
SHEET    1   R 3 LEU D  36  LYS D  41  0                                        
SHEET    2   R 3 GLY D  64  GLN D  71 -1                                        
SHEET    3   R 3 LEU D  83  LEU D  85 -1                                        
SHEET    1   S 3 SER D  95  PRO D 100  0                                        
SHEET    2   S 3 ASP D 105  GLN D 111 -1                                        
SHEET    3   S 3 ILE D 137  THR D 141 -1                                        
SHEET    1   T 4 ARG D 129  ALA D 133  0                                        
SHEET    2   T 4 GLN D 118  LYS D 123 -1                                        
SHEET    3   T 4 GLY D 146  PHE D 153 -1                                        
SHEET    4   T 4 LEU D 168  LEU D 170 -1                                        
SSBOND   1 CYS A   28    CYS A   68                          1555   1555  2.05  
SSBOND   2 CYS A  110    CYS A  150                          1555   1555  2.13  
SSBOND   3 CYS B   28    CYS B   68                          1555   1555  2.05  
SSBOND   4 CYS B  110    CYS B  150                          1555   1555  2.13  
SSBOND   5 CYS C   28    CYS C   68                          1555   1555  2.11  
SSBOND   6 CYS C  110    CYS C  150                          1555   1555  2.09  
SSBOND   7 CYS D   28    CYS D   68                          1555   1555  2.07  
SSBOND   8 CYS D  110    CYS D  150                          1555   1555  2.12  
LINK         ND2 ASN A  72                 C1  NAG A 208     1555   1555  1.45  
LINK         ND2 ASN B  72                 C1  NAG B 208     1555   1555  1.45  
LINK         ND2 ASN C  72                 C1  NAG C 203     1555   1555  1.44  
LINK         ND2 ASN D  72                 C1  NAG D 203     1555   1555  1.45  
CISPEP   1 LEU A   13    PRO A   14          0         1.76                     
CISPEP   2 ASP A  126    PRO A  127          0        -0.40                     
CISPEP   3 LEU B   13    PRO B   14          0         7.89                     
CISPEP   4 ASP B  126    PRO B  127          0         3.79                     
CISPEP   5 LEU C   13    PRO C   14          0         3.49                     
CISPEP   6 LEU C   13    PRO C   14          0         3.97                     
CISPEP   7 LEU D   13    PRO D   14          0         2.22                     
CISPEP   8 LEU D   13    PRO D   14          0         2.36                     
CRYST1   78.650   44.050  117.660  90.00 104.69  90.00 P 1 21 1      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      0.012715  0.000000  0.003333        0.00000                         
SCALE2      0.000000  0.022701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008786        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.999998  0.000885 -0.001835     -103.05657    1                    
MTRIX2   2  0.000886  0.999999 -0.000759       -3.93706    1                    
MTRIX3   2  0.001835 -0.000761 -0.999998      -56.82741    1                    
MTRIX1   3  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   3  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   3  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   4 -0.999995 -0.001239  0.002865     -103.07332    1                    
MTRIX2   4 -0.001232  0.999996  0.002430       -3.91525    1                    
MTRIX3   4 -0.002868  0.002427 -0.999993      -56.82080    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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