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Database: PDB
Entry: 3RFE
LinkDB: 3RFE
Original site: 3RFE 
HEADER    CELL ADHESION                           06-APR-11   3RFE              
TITLE     CRYSTAL STRUCTURE OF GLYCOPROTEIN GPIB ECTODOMAIN                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET GLYCOPROTEIN IB BETA CHAIN;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 26-146;                                       
COMPND   5 SYNONYM: GP-IB BETA, GPIB-BETA, GPIBB, ANTIGEN CD42B-BETA;           
COMPND   6 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: GP1BB;                                                         
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    GLYCOPROTEIN, PLATELET SURFACE RECEPTOR, GPIX, CELL ADHESION          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.MCEWAN,W.YANG,K.H.CARR,X.MO,X.ZHENG,R.LI,J.EMSLEY                 
REVDAT   2   29-JUL-20 3RFE    1       COMPND REMARK SEQADV HETNAM              
REVDAT   2 2                   1       LINK   SITE                              
REVDAT   1   21-DEC-11 3RFE    0                                                
JRNL        AUTH   P.A.MCEWAN,W.YANG,K.H.CARR,X.MO,X.ZHENG,R.LI,J.EMSLEY        
JRNL        TITL   QUATERNARY ORGANIZATION OF GPIB-IX COMPLEX AND INSIGHTS INTO 
JRNL        TITL 2 BERNARD-SOULIER SYNDROME REVEALED BY THE STRUCTURES OF       
JRNL        TITL 3 GPIBBETA AND A GPIBBETA/GPIX CHIMER                          
JRNL        REF    BLOOD                         V. 118  5292 2011              
JRNL        REFN                   ISSN 0006-4971                               
JRNL        PMID   21908432                                                     
JRNL        DOI    10.1182/BLOOD-2011-05-356253                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 75004                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3906                            
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) : 1.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5039                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 250                          
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1782                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 448                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31000                                              
REMARK   3    B22 (A**2) : 0.08000                                              
REMARK   3    B33 (A**2) : -0.39000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.09000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.051         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.032         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.694         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1902 ; 0.030 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2626 ; 2.489 ; 2.044       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   236 ; 6.449 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    66 ;33.146 ;20.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   256 ;12.838 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ; 8.749 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   298 ; 0.163 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1436 ; 0.004 ; 0.023       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1204 ; 1.505 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1934 ; 2.415 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   698 ; 2.761 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   692 ; 3.912 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3RFE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064862.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 193                                
REMARK 200  PH                             : 6.5                                
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) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78352                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.245                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MRBUMP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M(NH4)2SO4, 0.4M LICL, 0.1M MES, PH   
REMARK 280  6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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       17.38200            
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                                                    
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 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   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     LEU A   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     SER A   123                                                      
REMARK 465     HIS A   124                                                      
REMARK 465     HIS A   125                                                      
REMARK 465     HIS A   126                                                      
REMARK 465     HIS A   127                                                      
REMARK 465     HIS A   128                                                      
REMARK 465     HIS A   129                                                      
REMARK 465     GLY B   119                                                      
REMARK 465     PRO B   120                                                      
REMARK 465     LEU B   121                                                      
REMARK 465     SER B   122                                                      
REMARK 465     SER B   123                                                      
REMARK 465     HIS B   124                                                      
REMARK 465     HIS B   125                                                      
REMARK 465     HIS B   126                                                      
REMARK 465     HIS B   127                                                      
REMARK 465     HIS B   128                                                      
REMARK 465     HIS B   129                                                      
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   O4   NAG B   130     O    HOH B   435              1.70            
REMARK 500   O    HOH A   183     O    HOH A   272              1.75            
REMARK 500   O    HOH A   268     O    HOH A   373              1.82            
REMARK 500   O    HOH B   300     O    HOH B   443              2.02            
REMARK 500   O    HOH B   198     O    HOH B   370              2.02            
REMARK 500   O    HOH B   195     O    HOH B   408              2.02            
REMARK 500   O    HOH B   290     O    HOH B   410              2.08            
REMARK 500   O    HOH A   251     O    HOH A   411              2.09            
REMARK 500   O    HOH B   314     O    HOH B   336              2.09            
REMARK 500   O    HOH B   217     O    HOH B   239              2.10            
REMARK 500   O    HOH A   340     O    HOH A   395              2.11            
REMARK 500   O    HOH A   225     O    HOH A   359              2.14            
REMARK 500   O    HOH A   202     O    HOH A   438              2.15            
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   206     O    HOH B   152     2656     2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  84   CG    GLU A  84   CD      0.098                       
REMARK 500    TYR A 106   CD1   TYR A 106   CE1     0.160                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  16   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A  16   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A  71   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  82   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP A 110   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    LEU B  11   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ASP B  13   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    CYS B  14   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG B  16   NE  -  CZ  -  NH1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG B  16   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG B  67   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG B  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP B  69   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG B 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  40     -157.13    -89.71                                   
REMARK 500    LEU A  53       79.27   -118.14                                   
REMARK 500    ASN B  40     -158.57    -93.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3REZ   RELATED DB: PDB                                   
DBREF  3RFE A    1   121  UNP    P13224   GP1BB_HUMAN     26    146             
DBREF  3RFE B    1   121  UNP    P13224   GP1BB_HUMAN     26    146             
SEQADV 3RFE PRO A    0  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE SER A  122  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE SER A  123  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS A  124  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS A  125  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS A  126  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS A  127  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS A  128  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS A  129  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE PRO B    0  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE SER B  122  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE SER B  123  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS B  124  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS B  125  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS B  126  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS B  127  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS B  128  UNP  P13224              EXPRESSION TAG                 
SEQADV 3RFE HIS B  129  UNP  P13224              EXPRESSION TAG                 
SEQRES   1 A  130  PRO CYS PRO ALA PRO CYS SER CYS ALA GLY THR LEU VAL          
SEQRES   2 A  130  ASP CYS GLY ARG ARG GLY LEU THR TRP ALA SER LEU PRO          
SEQRES   3 A  130  THR ALA PHE PRO VAL ASP THR THR GLU LEU VAL LEU THR          
SEQRES   4 A  130  GLY ASN ASN LEU THR ALA LEU PRO PRO GLY LEU LEU ASP          
SEQRES   5 A  130  ALA LEU PRO ALA LEU ARG THR ALA HIS LEU GLY ALA ASN          
SEQRES   6 A  130  PRO TRP ARG CYS ASP CYS ARG LEU VAL PRO LEU ARG ALA          
SEQRES   7 A  130  TRP LEU ALA GLY ARG PRO GLU ARG ALA PRO TYR ARG ASP          
SEQRES   8 A  130  LEU ARG CYS VAL ALA PRO PRO ALA LEU ARG GLY ARG LEU          
SEQRES   9 A  130  LEU PRO TYR LEU ALA GLU ASP GLU LEU ARG ALA ALA CYS          
SEQRES  10 A  130  ALA PRO GLY PRO LEU SER SER HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  130  PRO CYS PRO ALA PRO CYS SER CYS ALA GLY THR LEU VAL          
SEQRES   2 B  130  ASP CYS GLY ARG ARG GLY LEU THR TRP ALA SER LEU PRO          
SEQRES   3 B  130  THR ALA PHE PRO VAL ASP THR THR GLU LEU VAL LEU THR          
SEQRES   4 B  130  GLY ASN ASN LEU THR ALA LEU PRO PRO GLY LEU LEU ASP          
SEQRES   5 B  130  ALA LEU PRO ALA LEU ARG THR ALA HIS LEU GLY ALA ASN          
SEQRES   6 B  130  PRO TRP ARG CYS ASP CYS ARG LEU VAL PRO LEU ARG ALA          
SEQRES   7 B  130  TRP LEU ALA GLY ARG PRO GLU ARG ALA PRO TYR ARG ASP          
SEQRES   8 B  130  LEU ARG CYS VAL ALA PRO PRO ALA LEU ARG GLY ARG LEU          
SEQRES   9 B  130  LEU PRO TYR LEU ALA GLU ASP GLU LEU ARG ALA ALA CYS          
SEQRES  10 B  130  ALA PRO GLY PRO LEU SER SER HIS HIS HIS HIS HIS HIS          
MODRES 3RFE ASN A   41  ASN  GLYCOSYLATION SITE                                 
MODRES 3RFE ASN B   41  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 130      14                                                       
HET     MG  A 131       1                                                       
HET    SO4  A 132       5                                                       
HET    SO4  A 133       5                                                       
HET    SO4  A 134       5                                                       
HET    NAG  B 130      14                                                       
HET     MG  B 131       1                                                       
HET    SO4  B 132       5                                                       
HET    SO4  B 133       5                                                       
HET    SO4  B 134       5                                                       
HET    SO4  B 135       5                                                       
HET    SO4  B 136       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  SO4    8(O4 S 2-)                                                   
FORMUL  15  HOH   *448(H2 O)                                                    
HELIX    1   1 LEU A   49  LEU A   53  5                                   5    
HELIX    2   2 ASP A   69  ARG A   71  5                                   3    
HELIX    3   3 LEU A   72  GLY A   81  1                                  10    
HELIX    4   4 ARG A   85  ARG A   89  5                                   5    
HELIX    5   5 LEU A  103  LEU A  107  5                                   5    
HELIX    6   6 ALA A  108  ALA A  115  1                                   8    
HELIX    7   7 ASP B   69  ARG B   71  5                                   3    
HELIX    8   8 LEU B   72  GLY B   81  1                                  10    
HELIX    9   9 ARG B   85  ARG B   89  5                                   5    
HELIX   10  10 LEU B  103  LEU B  107  5                                   5    
HELIX   11  11 ALA B  108  ALA B  115  1                                   8    
SHEET    1   A 4 SER A   6  ALA A   8  0                                        
SHEET    2   A 4 LEU A  11  ASP A  13 -1  O  ASP A  13   N  SER A   6           
SHEET    3   A 4 GLU A  34  VAL A  36  1  O  VAL A  36   N  VAL A  12           
SHEET    4   A 4 THR A  58  HIS A  60  1  O  HIS A  60   N  LEU A  35           
SHEET    1   B 4 SER B   6  ALA B   8  0                                        
SHEET    2   B 4 LEU B  11  ASP B  13 -1  O  ASP B  13   N  SER B   6           
SHEET    3   B 4 GLU B  34  VAL B  36  1  O  GLU B  34   N  VAL B  12           
SHEET    4   B 4 THR B  58  HIS B  60  1  O  HIS B  60   N  LEU B  35           
SSBOND   1 CYS A    1    CYS A    7                          1555   1555  2.03  
SSBOND   2 CYS A    5    CYS A   14                          1555   1555  2.02  
SSBOND   3 CYS A   68    CYS A   93                          1555   1555  2.02  
SSBOND   4 CYS A   70    CYS A  116                          1555   1555  2.23  
SSBOND   5 CYS B    1    CYS B    7                          1555   1555  2.02  
SSBOND   6 CYS B    5    CYS B   14                          1555   1555  2.00  
SSBOND   7 CYS B   68    CYS B   93                          1555   1555  1.99  
SSBOND   8 CYS B   70    CYS B  116                          1555   1555  2.21  
LINK         ND2 ASN A  41                 C1  NAG A 130     1555   1555  1.40  
LINK         ND2 ASN B  41                 C1  NAG B 130     1555   1555  1.43  
CISPEP   1 ALA A   95    PRO A   96          0       -10.51                     
CISPEP   2 ALA B   95    PRO B   96          0        -9.10                     
CRYST1   61.506   34.764   71.532  90.00  92.15  90.00 P 1 21 1      4          
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      0.016259  0.000000  0.000610        0.00000                         
SCALE2      0.000000  0.028765  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013990        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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