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Database: PDB
Entry: 4CAK
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Original site: 4CAK 
HEADER    CELL ADHESION                           08-OCT-13   4CAK              
TITLE     THREE-DIMENSIONAL RECONSTRUCTION OF INTACT HUMAN INTEGRIN             
TITLE    2 ALPHAIIBBETA3 IN A PHOSPHOLIPID BILAYER NANODISC                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ECTODOMAIN, UNP RESIDUES 32-990;                           
COMPND   5 SYNONYM: GPALPHA IIB, GPIIB, PLATELET MEMBRANE GLYCOPROTEIN IIB,     
COMPND   6 CD41, INTEGRIN ALPHA-IIB HEAVY CHAIN, INTEGRIN ALPHA-IIB LIGHT CHAIN,
COMPND   7 FORM 1, INTEGRIN ALPHA-IIB LIGHT CHAIN, FORM 2;                      
COMPND   8 OTHER_DETAILS: FITTED FROM PDB ID 3FCS;                              
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: RESIDUES 27-716;                                           
COMPND  13 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61;          
COMPND  14 OTHER_DETAILS: FITTED FROM PDB ID 3FCS                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 CELL_LINE: PLATELET;                                                 
SOURCE  11 TISSUE: BLOOD                                                        
KEYWDS    CELL ADHESION, INTEGRIN, SINGLE PARTICLE RECONSTRUCTION               
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    W.S.CHOI,W.J.RICE,D.L.STOKES,B.S.COLLER                               
REVDAT   4   23-AUG-17 4CAK    1       REMARK ATOM                              
REVDAT   3   08-JAN-14 4CAK    1       JRNL                                     
REVDAT   2   06-NOV-13 4CAK    1       ATOM                                     
REVDAT   1   30-OCT-13 4CAK    0                                                
JRNL        AUTH   W.S.CHOI,W.J.RICE,D.L.STOKES,B.S.COLLER                      
JRNL        TITL   THREE-DIMENSIONAL RECONSTRUCTION OF INTACT HUMAN INTEGRIN    
JRNL        TITL 2 ALPHAIIBBETA3; NEW IMPLICATIONS FOR ACTIVATION-DEPENDENT     
JRNL        TITL 3 LIGAND BINDING.                                              
JRNL        REF    BLOOD                         V. 122  4165 2013              
JRNL        REFN                   ISSN 0006-4971                               
JRNL        PMID   24136164                                                     
JRNL        DOI    10.1182/BLOOD-2013-04-499194                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.   20.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : UCSF CHIMERA, SPIDER                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 3FCS                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION COEFFICIENT       
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--RIGID BODY REFINEMENT PROTOCOL--X-RAY    
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 2.960                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 20.50                          
REMARK   3   NUMBER OF PARTICLES               : 25008                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: 23A LAYERLINE OF TMV    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: INITIAL MODEL FROM RANDOM CONICAL TILT FOLLOWED BY    
REMARK   3  REFERENCE BASED REFINEMENT PDB FILE 3FCS WAS SPLIT INTO 20          
REMARK   3  SUBDOMAINS. THESE SUBDOMAINS WERE MANUALLY FITTED INTO THE EM       
REMARK   3  VOLUME SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2281.    
REMARK   3  (DEPOSITION ID: 11378).                                             
REMARK   4                                                                      
REMARK   4 4CAK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290058667.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NEGATIVE STAIN                    
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : INTEGRIN ALPHAIIBBETA3 IN LIPID   
REMARK 245                                    BILAYER NANODISC                  
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.02                              
REMARK 245   SAMPLE SUPPORT DETAILS         : CARBON                            
REMARK 245   SAMPLE VITRIFICATION DETAILS   : VITRIFICATION 1 -- CRYOGEN-       
REMARK 245                                    NONE, INSTRUMENT- NONE,           
REMARK 245   SAMPLE BUFFER                  : 150 MM NACL, 10 MM HEPES, PH      
REMARK 245                                    7.4, 1 MM CACL2 AND 1 MM MGCL2    
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : MICROGRAPHS TAKEN ON CCD          
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 01-FEB-10                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI F20                 
REMARK 245   DETECTOR TYPE                     : GENERIC TVIPS (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : 1200.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : 50.00                          
REMARK 245   NOMINAL CS                        : 2.00                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 13.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 29000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 50592                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 120                            
REMARK 245   IMAGING DETAILS                   : LOW DOSE PACKAGE USED. CCD     
REMARK 245  MAGNIFICATION IS 1.76 TIMES FILM MAGNIFICATION                      
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LEU A     1                                                      
REMARK 465     GLU A   764                                                      
REMARK 465     GLU A   765                                                      
REMARK 465     GLY A   766                                                      
REMARK 465     GLU A   767                                                      
REMARK 465     ARG A   768                                                      
REMARK 465     GLU A   769                                                      
REMARK 465     GLN A   770                                                      
REMARK 465     ASN A   771                                                      
REMARK 465     SER A   772                                                      
REMARK 465     LEU A   773                                                      
REMARK 465     ASP A   774                                                      
REMARK 465     GLY A   840                                                      
REMARK 465     LEU A   841                                                      
REMARK 465     PRO A   842                                                      
REMARK 465     ILE A   843                                                      
REMARK 465     PRO A   844                                                      
REMARK 465     SER A   845                                                      
REMARK 465     PRO A   846                                                      
REMARK 465     SER A   847                                                      
REMARK 465     PRO A   848                                                      
REMARK 465     ILE A   849                                                      
REMARK 465     HIS A   850                                                      
REMARK 465     PRO A   851                                                      
REMARK 465     ALA A   852                                                      
REMARK 465     HIS A   853                                                      
REMARK 465     HIS A   854                                                      
REMARK 465     LYS A   855                                                      
REMARK 465     ARG A   856                                                      
REMARK 465     ASP A   857                                                      
REMARK 465     ARG A   858                                                      
REMARK 465     ARG A   859                                                      
REMARK 465     GLN A   860                                                      
REMARK 465     ILE A   861                                                      
REMARK 465     PHE A   862                                                      
REMARK 465     LEU A   863                                                      
REMARK 465     PRO A   864                                                      
REMARK 465     GLU A   865                                                      
REMARK 465     PRO A   866                                                      
REMARK 465     GLU A   867                                                      
REMARK 465     GLN A   868                                                      
REMARK 465     PRO A   869                                                      
REMARK 465     SER A   870                                                      
REMARK 465     ARG A   871                                                      
REMARK 465     LEU A   872                                                      
REMARK 465     GLN A   873                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     ASP B   477                                                      
REMARK 465     TYR B   478                                                      
REMARK 465     ARG B   479                                                      
REMARK 465     PRO B   480                                                      
REMARK 465     SER B   481                                                      
REMARK 465     GLN B   482                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 667    C    O    CB   CG   CD   OE1  OE2                   
REMARK 470     GLY A 668    N    CA                                             
REMARK 470     TRP A 839    C    O    CB   CG   CD1  CD2  NE1                   
REMARK 470     TRP A 839    CE2  CE3  CZ2  CZ3  CH2                             
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   N    VAL A   566     N    CYS A   602              0.13            
REMARK 500   O    VAL A   325     N    LEU B   292              0.15            
REMARK 500   CB   LEU A   312     CG   TYR B   164              0.17            
REMARK 500   C    SER A   384     O    ASP B   270              0.18            
REMARK 500   CD2  TYR B   190     CD1  TYR B   281              0.20            
REMARK 500   HD1  TYR A   155     O    GLY A   188              0.21            
REMARK 500   N    LEU A   346     O    ARG A   671              0.22            
REMARK 500   HD3  ARG A   327     O    GLU B   323              0.23            
REMARK 500   CA   PRO B   363     CG   GLN B   440              0.23            
REMARK 500   N    LYS B   350     CA   GLY B   504              0.23            
REMARK 500   C    VAL B   310     CB   THR B   517              0.23            
REMARK 500   O    GLN A   333     CG2  VAL A   685              0.24            
REMARK 500   CE1  TYR A   234     OG   SER B   168              0.24            
REMARK 500   HG   LEU A   346     CA   ARG A   671              0.24            
REMARK 500   OD2  ASP A   159     OD1  ASP A   232              0.24            
REMARK 500   HG   LEU A   346     CA   ARG A   671              0.24            
REMARK 500   CD1  LEU B    33     N    LEU B    92              0.26            
REMARK 500   HA   GLU A   315     C    SER B   322              0.27            
REMARK 500   CB   ARG A   327     C    LEU B   324              0.27            
REMARK 500   HA   ARG A   317     CD   GLN B   505              0.29            
REMARK 500   CA   CYS B   588     NE   ARG B   636              0.29            
REMARK 500   CD1  TYR A   432     CD1  LEU A   573              0.30            
REMARK 500   OD2  ASP A   365     N    GLY A   588              0.30            
REMARK 500   HZ3  LYS A   321     C    VAL B   332              0.31            
REMARK 500   C    MET A   314     N    SER B   322              0.31            
REMARK 500   HB   THR A   350     C    THR B   296              0.31            
REMARK 500   CA   THR B   254     CE1  TYR B   318              0.32            
REMARK 500   CB   ALA A   310     CD1  LEU B   324              0.33            
REMARK 500   CG   TYR A   155     N    TYR A   189              0.33            
REMARK 500   CA   GLN A    85     C    TRP A   214              0.33            
REMARK 500   HA   GLU A   397     N    LEU A   649              0.33            
REMARK 500   HB3  LYS A   321     CA   ALA B   309              0.33            
REMARK 500   C    HIS B   192     CG1  VAL B   275              0.34            
REMARK 500   CG   TYR B   190     CG   TYR B   281              0.35            
REMARK 500   N    SER B   300     O    ASN B   303              0.36            
REMARK 500   C    ASN A   639     C2   NAG B  3453              0.36            
REMARK 500   CB   VAL B   161     C    LEU B   258              0.36            
REMARK 500   CE2  PHE B   223     CA   ILE B   256              0.36            
REMARK 500  HD12  LEU A   312     OD1  ASP B   259              0.36            
REMARK 500   HG2  PRO A   337     N    GLY A   656              0.37            
REMARK 500   CE1  PHE B   223     O    HIS B   255              0.37            
REMARK 500   N    LYS B   253     CD   LYS B   515              0.37            
REMARK 500   C    SER B    35     N    CYS B   406              0.37            
REMARK 500   CB   SER A   316     N    VAL B   330              0.37            
REMARK 500   C    LEU A    84     CA   HIS A   215              0.37            
REMARK 500   CA   THR B   254     CD1  TYR B   318              0.37            
REMARK 500   CE2  TYR B   556     C5   NAG B  3559              0.38            
REMARK 500   NZ   LYS B   191     CD2  HIS B   280              0.38            
REMARK 500   C    ARG A   165     H    GLU A   168              0.38            
REMARK 500   C    ASP A   429     CA   ALA A   583              0.38            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    5809 CLOSE CONTACTS                                
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    THR B 562   C     ARG B 563   N      -0.463                       
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  32   CD  -  NE  -  CZ  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ARG A  77   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 276   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP A 305   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 317   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP A 373   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 434   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    THR B 562   CA  -  C   -  N   ANGL. DEV. = -24.7 DEGREES          
REMARK 500    THR B 562   O   -  C   -  N   ANGL. DEV. = -38.9 DEGREES          
REMARK 500    ARG B 563   C   -  N   -  CA  ANGL. DEV. = -28.4 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    PRO A   5       24.41    -70.02                                   
REMARK 500    GLN A  18       36.82     82.46                                   
REMARK 500    GLN A  47       11.73     81.00                                   
REMARK 500    ARG A  90        7.74     87.91                                   
REMARK 500    LEU A  93      108.60    -59.36                                   
REMARK 500    SER A 101     -125.00     62.54                                   
REMARK 500    LYS A 118     -119.95     75.26                                   
REMARK 500    GLU A 123      135.72     89.30                                   
REMARK 500    LYS A 124       95.94    -64.14                                   
REMARK 500    ASN A 158      -71.77    -96.88                                   
REMARK 500    CYS A 167      -70.59   -145.99                                   
REMARK 500    GLU A 168       31.15     85.30                                   
REMARK 500    TYR A 190       45.02     90.57                                   
REMARK 500    PHE A 191       14.26     80.71                                   
REMARK 500    ASP A 232       35.11     77.54                                   
REMARK 500    TRP A 235       97.89    -64.06                                   
REMARK 500    ASP A 245      -41.58   -132.95                                   
REMARK 500    SER A 261       53.80     70.61                                   
REMARK 500    THR A 263        6.22     99.99                                   
REMARK 500    TYR A 274       28.39     81.34                                   
REMARK 500    TYR A 288       36.65     77.51                                   
REMARK 500    PHE A 289       97.62    -53.11                                   
REMARK 500    THR A 296     -159.69   -151.81                                   
REMARK 500    VAL A 325      -49.39   -132.79                                   
REMARK 500    ARG A 355       43.64     72.82                                   
REMARK 500    ARG A 368       78.26     79.50                                   
REMARK 500    SER A 396       10.38    -66.92                                   
REMARK 500    GLU A 397       11.82   -141.32                                   
REMARK 500    ALA A 416       63.86     67.58                                   
REMARK 500    ALA A 424      -14.42     87.93                                   
REMARK 500    ASP A 429       88.02     63.62                                   
REMARK 500    ASN A 430       -8.86   -141.13                                   
REMARK 500    ASN A 443       34.20     70.88                                   
REMARK 500    GLN A 477      -52.81     72.06                                   
REMARK 500    MET A 580     -164.81     65.31                                   
REMARK 500    ALA A 581       80.86     99.71                                   
REMARK 500    ASP A 628       58.54   -108.01                                   
REMARK 500    MET A 660      -62.50   -106.82                                   
REMARK 500    ASN A 665       57.99   -105.45                                   
REMARK 500    PHE A 669       85.86   -175.59                                   
REMARK 500    ASN A 833       72.41     49.78                                   
REMARK 500    LYS A 836     -107.35    -74.83                                   
REMARK 500    VAL A 837      151.71     70.14                                   
REMARK 500    ARG A 917       67.48     72.07                                   
REMARK 500    ALA A 938      -71.34    -66.28                                   
REMARK 500    PRO A 940       70.11   -114.41                                   
REMARK 500    LEU A 942      -90.76   -130.40                                   
REMARK 500    THR B   7       49.24    -93.05                                   
REMARK 500    ARG B   8      -95.76   -152.82                                   
REMARK 500    VAL B 157      -78.32   -128.21                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR B 562        -47.86                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3570                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG A3015 bound   
REMARK 800  to ASN A 15                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B3099 through NAG B3100 bound to ASN B 99                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B3371 through BMA B3373 bound to ASN B 371                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B3452 through NAG B3453 bound to ASN B 452                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B3559 through MAN B3563 bound to ASN B 559                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B3321 through MAN B3323                                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-2281   RELATED DB: EMDB                              
REMARK 900 THREE-DIMENSIONAL RECONSTRUCTION OF INTACT HUMAN INTEGRIN            
REMARK 900 ALPHAIIBBETA3 IN A PHOSPHOLIPID BILAYER NANODISC                     
DBREF  4CAK A    1   959  UNP    P08514   ITA2B_HUMAN     32    990             
DBREF  4CAK B    1   690  UNP    P05106   ITB3_HUMAN      27    716             
SEQADV 4CAK CYS A  959  UNP  P08514    LEU   990 CONFLICT                       
SEQADV 4CAK CYS B  688  UNP  P05106    PRO   714 CONFLICT                       
SEQRES   1 A  959  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  959  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  959  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  959  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  959  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  959  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  959  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  959  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  959  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  959  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  959  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  959  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  959  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  959  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  959  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  959  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  959  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  959  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  959  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  959  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  959  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  959  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  959  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  959  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  959  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  959  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  959  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  959  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  959  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  959  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  959  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  959  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  959  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  959  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  959  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 A  959  ALA SER VAL GLN LEU LEU VAL GLN ASP SER LEU ASN PRO          
SEQRES  37 A  959  ALA VAL LYS SER CYS VAL LEU PRO GLN THR LYS THR PRO          
SEQRES  38 A  959  VAL SER CYS PHE ASN ILE GLN MET CYS VAL GLY ALA THR          
SEQRES  39 A  959  GLY HIS ASN ILE PRO GLN LYS LEU SER LEU ASN ALA GLU          
SEQRES  40 A  959  LEU GLN LEU ASP ARG GLN LYS PRO ARG GLN GLY ARG ARG          
SEQRES  41 A  959  VAL LEU LEU LEU GLY SER GLN GLN ALA GLY THR THR LEU          
SEQRES  42 A  959  ASN LEU ASP LEU GLY GLY LYS HIS SER PRO ILE CYS HIS          
SEQRES  43 A  959  THR THR MET ALA PHE LEU ARG ASP GLU ALA ASP PHE ARG          
SEQRES  44 A  959  ASP LYS LEU SER PRO ILE VAL LEU SER LEU ASN VAL SER          
SEQRES  45 A  959  LEU PRO PRO THR GLU ALA GLY MET ALA PRO ALA VAL VAL          
SEQRES  46 A  959  LEU HIS GLY ASP THR HIS VAL GLN GLU GLN THR ARG ILE          
SEQRES  47 A  959  VAL LEU ASP CYS GLY GLU ASP ASP VAL CYS VAL PRO GLN          
SEQRES  48 A  959  LEU GLN LEU THR ALA SER VAL THR GLY SER PRO LEU LEU          
SEQRES  49 A  959  VAL GLY ALA ASP ASN VAL LEU GLU LEU GLN MET ASP ALA          
SEQRES  50 A  959  ALA ASN GLU GLY GLU GLY ALA TYR GLU ALA GLU LEU ALA          
SEQRES  51 A  959  VAL HIS LEU PRO GLN GLY ALA HIS TYR MET ARG ALA LEU          
SEQRES  52 A  959  SER ASN VAL GLU GLY PHE GLU ARG LEU ILE CYS ASN GLN          
SEQRES  53 A  959  LYS LYS GLU ASN GLU THR ARG VAL VAL LEU CYS GLU LEU          
SEQRES  54 A  959  GLY ASN PRO MET LYS LYS ASN ALA GLN ILE GLY ILE ALA          
SEQRES  55 A  959  MET LEU VAL SER VAL GLY ASN LEU GLU GLU ALA GLY GLU          
SEQRES  56 A  959  SER VAL SER PHE GLN LEU GLN ILE ARG SER LYS ASN SER          
SEQRES  57 A  959  GLN ASN PRO ASN SER LYS ILE VAL LEU LEU ASP VAL PRO          
SEQRES  58 A  959  VAL ARG ALA GLU ALA GLN VAL GLU LEU ARG GLY ASN SER          
SEQRES  59 A  959  PHE PRO ALA SER LEU VAL VAL ALA ALA GLU GLU GLY GLU          
SEQRES  60 A  959  ARG GLU GLN ASN SER LEU ASP SER TRP GLY PRO LYS VAL          
SEQRES  61 A  959  GLU HIS THR TYR GLU LEU HIS ASN ASN GLY PRO GLY THR          
SEQRES  62 A  959  VAL ASN GLY LEU HIS LEU SER ILE HIS LEU PRO GLY GLN          
SEQRES  63 A  959  SER GLN PRO SER ASP LEU LEU TYR ILE LEU ASP ILE GLN          
SEQRES  64 A  959  PRO GLN GLY GLY LEU GLN CYS PHE PRO GLN PRO PRO VAL          
SEQRES  65 A  959  ASN PRO LEU LYS VAL ASP TRP GLY LEU PRO ILE PRO SER          
SEQRES  66 A  959  PRO SER PRO ILE HIS PRO ALA HIS HIS LYS ARG ASP ARG          
SEQRES  67 A  959  ARG GLN ILE PHE LEU PRO GLU PRO GLU GLN PRO SER ARG          
SEQRES  68 A  959  LEU GLN ASP PRO VAL LEU VAL SER CYS ASP SER ALA PRO          
SEQRES  69 A  959  CYS THR VAL VAL GLN CYS ASP LEU GLN GLU MET ALA ARG          
SEQRES  70 A  959  GLY GLN ARG ALA MET VAL THR VAL LEU ALA PHE LEU TRP          
SEQRES  71 A  959  LEU PRO SER LEU TYR GLN ARG PRO LEU ASP GLN PHE VAL          
SEQRES  72 A  959  LEU GLN SER HIS ALA TRP PHE ASN VAL SER SER LEU PRO          
SEQRES  73 A  959  TYR ALA VAL PRO PRO LEU SER LEU PRO ARG GLY GLU ALA          
SEQRES  74 A  959  GLN VAL TRP THR GLN LEU LEU ARG ALA CYS                      
SEQRES   1 B  690  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  690  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  690  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  690  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  690  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  690  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  690  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  690  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  690  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  690  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  690  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  690  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  690  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  690  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  690  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  690  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  690  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  690  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  690  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  690  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  690  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  690  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  690  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  690  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  690  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  690  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  690  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  690  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  690  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  690  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  690  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  690  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  690  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  690  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  690  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  690  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  690  SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER          
SEQRES  38 B  690  GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL          
SEQRES  39 B  690  CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL          
SEQRES  40 B  690  CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR          
SEQRES  41 B  690  CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY          
SEQRES  42 B  690  GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP          
SEQRES  43 B  690  CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN          
SEQRES  44 B  690  CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY          
SEQRES  45 B  690  LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER          
SEQRES  46 B  690  CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS          
SEQRES  47 B  690  GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS          
SEQRES  48 B  690  LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA          
SEQRES  49 B  690  LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP          
SEQRES  50 B  690  GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS          
SEQRES  51 B  690  ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS          
SEQRES  52 B  690  VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS          
SEQRES  53 B  690  SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS CYS LYS          
SEQRES  54 B  690  GLY                                                          
MODRES 4CAK ASN A   15  ASN  GLYCOSYLATION SITE                                 
MODRES 4CAK ASN A  570  ASN  GLYCOSYLATION SITE                                 
MODRES 4CAK ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 4CAK ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 4CAK ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 4CAK ASN B  452  ASN  GLYCOSYLATION SITE                                 
MODRES 4CAK ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 4CAK SER A  572  SER  GLYCOSYLATION SITE                                 
HET    NAG  A3015      14                                                       
HET    NAG  A3570      14                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3100      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    BMA  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    BMA  B3373      11                                                       
HET    NAG  B3452      14                                                       
HET    NAG  B3453      14                                                       
HET    NAG  B3559      14                                                       
HET    NAG  B3560      14                                                       
HET    BMA  B3561      11                                                       
HET    MAN  B3562      11                                                       
HET    MAN  B3563      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   3  NAG    12(C8 H15 N O6)                                              
FORMUL   6  BMA    3(C6 H12 O6)                                                 
FORMUL   6  MAN    3(C6 H12 O6)                                                 
HELIX    1   1 ASP A    4  VAL A    6  5                                   3    
HELIX    2   2 SER A  152  GLU A  157  1                                   6    
HELIX    3   3 GLY A  187  LEU A  192  1                                   6    
HELIX    4   4 VAL A  200  TYR A  207  1                                   8    
HELIX    5   5 ASN A  227  PHE A  231  5                                   5    
HELIX    6   6 PRO A  515  ARG A  519  5                                   5    
HELIX    7   7 TRP A  910  TYR A  915  1                                   6    
HELIX    8   8 SER B   12  SER B   20  1                                   9    
HELIX    9   9 LEU B   40  ASP B   47  1                                   8    
HELIX   10  10 ALA B   50  GLU B   52  5                                   3    
HELIX   11  11 SER B  121  SER B  123  5                                   3    
HELIX   12  12 MET B  124  ILE B  131  1                                   8    
HELIX   13  13 GLY B  135  THR B  146  1                                  12    
HELIX   14  14 GLN B  199  LYS B  208  1                                  10    
HELIX   15  15 GLY B  221  CYS B  232  1                                  12    
HELIX   16  16 CYS B  232  GLY B  237  1                                   6    
HELIX   17  17 GLY B  260  GLY B  264  5                                   5    
HELIX   18  18 SER B  282  THR B  286  5                                   5    
HELIX   19  19 SER B  291  LYS B  302  1                                  12    
HELIX   20  20 VAL B  314  ILE B  325  1                                  12    
HELIX   21  21 ASN B  339  ARG B  352  1                                  14    
HELIX   22  22 CYS B  435  ALA B  439  5                                   5    
HELIX   23  23 PRO B  493  GLN B  497  5                                   5    
HELIX   24  24 CYS B  536  GLY B  538  5                                   3    
HELIX   25  25 LYS B  612  GLU B  616  5                                   5    
SHEET    1  AA 5 GLY A  63  GLN A  64  0                                        
SHEET    2  AA 5 LEU A   8  ALA A  12  1  O  PHE A  10   N  GLY A  63           
SHEET    3  AA 5 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    4  AA 5 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    5  AA 5 LEU A 421  VAL A 425 -1  O  ARG A 422   N  ILE A 436           
SHEET    1  AB 3 LEU A  23  ASP A  28  0                                        
SHEET    2  AB 3 ARG A  32  ALA A  39 -1  O  ARG A  32   N  ASP A  28           
SHEET    3  AB 3 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    1  AC 4 GLU A  75  ASN A  78  0                                        
SHEET    2  AC 4 GLN A  82  THR A  86 -1  N  LEU A  84   O  ARG A  77           
SHEET    3  AC 4 HIS A 112  GLU A 117 -1  O  ASN A 114   N  GLN A  85           
SHEET    4  AC 4 GLU A 120  GLU A 121  1  O  GLU A 120   N  GLU A 117           
SHEET    1  AD 4 GLU A  75  ASN A  78  0                                        
SHEET    2  AD 4 GLN A  82  THR A  86 -1  N  LEU A  84   O  ARG A  77           
SHEET    3  AD 4 HIS A 112  GLU A 117 -1  O  ASN A 114   N  GLN A  85           
SHEET    4  AD 4 THR A 125  PRO A 126 -1  O  THR A 125   N  TRP A 113           
SHEET    1  AE 2 GLU A 120  GLU A 121  0                                        
SHEET    2  AE 2 HIS A 112  GLU A 117  1  O  GLU A 117   N  GLU A 120           
SHEET    1  AF 4 VAL A  97  TRP A 100  0                                        
SHEET    2  AF 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3  AF 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AF 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1  AG 4 SER A 173  VAL A 175  0                                        
SHEET    2  AG 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3  AG 4 LEU A 194  PRO A 199 -1  O  LEU A 194   N  ALA A 185           
SHEET    4  AG 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1  AH 4 VAL A 239  GLY A 242  0                                        
SHEET    2  AH 4 GLU A 252  ALA A 257 -1  O  GLU A 252   N  GLY A 242           
SHEET    3  AH 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4  AH 4 ARG A 276  ARG A 281 -1  N  LEU A 277   O  ILE A 269           
SHEET    1  AI 4 VAL A 293  THR A 296  0                                        
SHEET    2  AI 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3  AI 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4  AI 4 LEU A 345  THR A 348 -1  O  LEU A 347   N  VAL A 328           
SHEET    1  AJ 2 MET A 314  GLU A 315  0                                        
SHEET    2  AJ 2 ALA A 323  GLU A 324 -1  O  ALA A 323   N  GLU A 315           
SHEET    1  AK 2 ALA A 339  LEU A 340  0                                        
SHEET    2  AK 2 ALA A 697  SER A 706 -1  O  SER A 706   N  ALA A 339           
SHEET    1  AL 4 LEU A 612  THR A 619  0                                        
SHEET    2  AL 4 LEU A 631  ASN A 639 -1  O  GLU A 632   N  THR A 619           
SHEET    3  AL 4 ALA A 697  SER A 706 -1  O  ALA A 697   N  ASN A 639           
SHEET    4  AL 4 TYR A 659  SER A 664  1  N  MET A 660   O  LEU A 704           
SHEET    1  AM 4 LEU A 612  THR A 619  0                                        
SHEET    2  AM 4 LEU A 631  ASN A 639 -1  O  GLU A 632   N  THR A 619           
SHEET    3  AM 4 ALA A 697  SER A 706 -1  O  ALA A 697   N  ASN A 639           
SHEET    4  AM 4 ALA A 339  LEU A 340 -1  O  ALA A 339   N  SER A 706           
SHEET    1  AN 2 TYR A 659  SER A 664  0                                        
SHEET    2  AN 2 ALA A 697  SER A 706  1  O  ALA A 702   N  LEU A 663           
SHEET    1  AO 4 ILE A 360  GLY A 364  0                                        
SHEET    2  AO 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3  AO 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4  AO 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1  AP 2 GLY A 394  GLN A 395  0                                        
SHEET    2  AP 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1  AQ 5 VAL A 521  LEU A 523  0                                        
SHEET    2  AQ 5 ILE A 544  LEU A 552 -1  O  PHE A 551   N  LEU A 522           
SHEET    3  AQ 5 CYS A 484  THR A 494 -1  O  PHE A 485   N  ALA A 550           
SHEET    4  AQ 5 VAL A 454  VAL A 462 -1  O  LYS A 455   N  THR A 494           
SHEET    5  AQ 5 LEU A 586  GLY A 588  1  O  HIS A 587   N  ALA A 456           
SHEET    1  AR 2 CYS A 473  VAL A 474  0                                        
SHEET    2  AR 2 PRO A 481  VAL A 482 -1  O  VAL A 482   N  CYS A 473           
SHEET    1  AS 4 GLY A 530  ASP A 536  0                                        
SHEET    2  AS 4 SER A 503  LEU A 510 -1  O  LEU A 504   N  LEU A 535           
SHEET    3  AS 4 ILE A 565  SER A 572 -1  O  SER A 568   N  GLN A 509           
SHEET    4  AS 4 HIS A 591  THR A 596 -1  O  VAL A 592   N  LEU A 569           
SHEET    1  AT 2 PHE A 558  ARG A 559  0                                        
SHEET    2  AT 2 LEU B 366  THR B 373  1  O  LEU B 366   N  ARG A 559           
SHEET    1  BA 5 VAL B  83  SER B  84  0                                        
SHEET    2  BA 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BA 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BA 5 LEU B 366  THR B 373 -1  O  SER B 369   N  GLU B 400           
SHEET    5  BA 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BB 5 VAL B  83  SER B  84  0                                        
SHEET    2  BB 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BB 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BB 5 LEU B 366  THR B 373 -1  O  SER B 369   N  GLU B 400           
SHEET    5  BB 5 PHE A 558  ARG A 559  1  O  PHE A 558   N  SER B 367           
SHEET    1  BC 2 VAL B 379  PRO B 381  0                                        
SHEET    2  BC 2 LEU B 366  THR B 373 -1  O  ALA B 372   N  ILE B 380           
SHEET    1  AU 6 LEU A 623  LEU A 624  0                                        
SHEET    2  AU 6 VAL A 736  ARG A 743  1  O  PRO A 741   N  LEU A 623           
SHEET    3  AU 6 SER A 716  ARG A 724 -1  O  VAL A 717   N  VAL A 740           
SHEET    4  AU 6 ALA A 647  HIS A 652 -1  N  GLU A 648   O  ARG A 724           
SHEET    5  AU 6 VAL A 684  GLY A 690 -1  O  VAL A 685   N  VAL A 651           
SHEET    6  AU 6 CYS A 674  LYS A 677 -1  O  ASN A 675   N  LEU A 686           
SHEET    1  AV 2 VAL A 666  PHE A 669  0                                        
SHEET    2  AV 2 GLU B 475  GLU B 476 -1  N  GLU B 475   O  VAL A 666           
SHEET    1  AW 4 VAL A 748  PHE A 755  0                                        
SHEET    2  AW 4 LYS A 779  ASN A 788 -1  O  GLU A 781   N  PHE A 755           
SHEET    3  AW 4 ARG A 900  LEU A 909 -1  O  ALA A 901   N  LEU A 786           
SHEET    4  AW 4 LEU A 813  GLN A 821 -1  O  TYR A 814   N  PHE A 908           
SHEET    1  AX 4 SER A 758  VAL A 761  0                                        
SHEET    2  AX 4 ARG A 946  ARG A 957  1  O  GLN A 954   N  LEU A 759           
SHEET    3  AX 4 GLN A 921  SER A 934 -1  O  PHE A 922   N  LEU A 955           
SHEET    4  AX 4 PRO A 875  VAL A 878  1  O  VAL A 876   N  VAL A 923           
SHEET    1  AY 6 SER A 758  VAL A 761  0                                        
SHEET    2  AY 6 ARG A 946  ARG A 957  1  O  GLN A 954   N  LEU A 759           
SHEET    3  AY 6 GLN A 921  SER A 934 -1  O  PHE A 922   N  LEU A 955           
SHEET    4  AY 6 VAL A 794  PRO A 804 -1  O  ASN A 795   N  SER A 934           
SHEET    5  AY 6 CYS A 885  MET A 895 -1  O  THR A 886   N  LEU A 803           
SHEET    6  AY 6 GLN A 825  GLN A 829 -1  O  GLN A 825   N  ASP A 891           
SHEET    1  AZ 2 PRO A 875  VAL A 878  0                                        
SHEET    2  AZ 2 GLN A 921  SER A 934  1  O  GLN A 921   N  VAL A 876           
SHEET    1  BD 3 CYS B  38  ASP B  39  0                                        
SHEET    2  BD 3 ALA B  24  CYS B  26 -1  O  ALA B  24   N  ASP B  39           
SHEET    3  BD 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1  BE 6 GLU B  60  GLU B  65  0                                        
SHEET    2  BE 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3  BE 6 LEU B 425  PHE B 431  1  O  ILE B 426   N  ILE B  88           
SHEET    4  BE 6 GLU B 411  PRO B 418 -1  O  LYS B 412   N  VAL B 429           
SHEET    5  BE 6 VAL B 355  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BE 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1  BF 7 HIS B 280  TYR B 281  0                                        
SHEET    2  BF 7 TYR B 190  THR B 197 -1  O  LYS B 191   N  TYR B 281           
SHEET    3  BF 7 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    4  BF 7 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    5  BF 7 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    6  BF 7 ASN B 305  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    7  BF 7 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  BG 2 GLY B 453  GLU B 456  0                                        
SHEET    2  BG 2 VAL B 459  CYS B 462 -1  O  VAL B 459   N  GLU B 456           
SHEET    1  BH 2 GLY B 499  CYS B 501  0                                        
SHEET    2  BH 2 CYS B 506  CYS B 508 -1  O  VAL B 507   N  GLU B 500           
SHEET    1  BI 2 GLY B 540  SER B 543  0                                        
SHEET    2  BI 2 ASP B 546  CYS B 549 -1  O  ASP B 546   N  SER B 543           
SHEET    1  BJ 2 LYS B 580  GLU B 582  0                                        
SHEET    2  BJ 2 SER B 585  VAL B 587 -1  O  SER B 585   N  GLU B 582           
SHEET    1  BK 2 GLU B 638  GLU B 640  0                                        
SHEET    2  BK 2 ILE B 678  TYR B 680  1  O  LEU B 679   N  GLU B 640           
SHEET    1  BL 2 ASN B 654  LYS B 658  0                                        
SHEET    2  BL 2 VAL B 664  GLN B 668 -1  O  VAL B 665   N  TYR B 657           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.05  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.03  
SSBOND   4 CYS A  473    CYS A  484                          1555   1555  2.03  
SSBOND   5 CYS A  490    CYS A  545                          1555   1555  2.04  
SSBOND   6 CYS A  602    CYS A  608                          1555   1555  2.04  
SSBOND   7 CYS A  674    CYS A  687                          1555   1555  2.04  
SSBOND   8 CYS A  826    CYS A  890                          1555   1555  2.04  
SSBOND   9 CYS A  880    CYS A  885                          1555   1555  2.02  
SSBOND  10 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND  11 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  12 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND  13 CYS B  177    CYS B  184                          1555   1555  2.03  
SSBOND  14 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  15 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  16 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  17 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  18 CYS B  462    CYS B  471                          1555   1555  2.03  
SSBOND  19 CYS B  473    CYS B  503                          1555   1555  2.04  
SSBOND  20 CYS B  486    CYS B  501                          1555   1555  2.03  
SSBOND  21 CYS B  495    CYS B  506                          1555   1555  2.03  
SSBOND  22 CYS B  508    CYS B  521                          1555   1555  2.04  
SSBOND  23 CYS B  523    CYS B  544                          1555   1555  2.04  
SSBOND  24 CYS B  528    CYS B  542                          1555   1555  2.03  
SSBOND  25 CYS B  536    CYS B  547                          1555   1555  2.03  
SSBOND  26 CYS B  560    CYS B  583                          1555   1555  2.03  
SSBOND  27 CYS B  567    CYS B  581                          1555   1555  2.03  
SSBOND  28 CYS B  575    CYS B  586                          1555   1555  2.03  
SSBOND  29 CYS B  588    CYS B  598                          1555   1555  2.04  
SSBOND  30 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  31 CYS B  608    CYS B  655                          1555   1555  2.03  
SSBOND  32 CYS B  614    CYS B  635                          1555   1555  2.03  
SSBOND  33 CYS B  617    CYS B  631                          1555   1555  2.03  
SSBOND  34 CYS B  663    CYS B  687                          1555   1555  2.03  
LINK         O4  NAG B3321                 C1  BMA B3322     1555   1555  1.44  
LINK         O3  BMA B3322                 C1  MAN B3323     1555   1555  1.45  
LINK         O4  NAG B3372                 C1  BMA B3373     1555   1555  1.44  
LINK         O4  NAG B3560                 C1  BMA B3561     1555   1555  1.45  
LINK         O3  BMA B3561                 C1  MAN B3562     1555   1555  1.44  
LINK         O2  MAN B3562                 C1  MAN B3563     1555   1555  1.44  
LINK         ND2BASN A  15                 C1  NAG A3015     1555   1555  1.49  
LINK         ND2AASN A  15                 C1  NAG A3015     1555   1555  1.45  
LINK         ND2BASN A 570                 C1  NAG A3570     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         ND2BASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         ND2BASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK         ND2AASN B 371                 C1  NAG B3371     1555   1555  1.45  
LINK         ND2BASN B 452                 C1  NAG B3452     1555   1555  1.44  
LINK         ND2AASN B 452                 C1  NAG B3452     1555   1555  1.44  
LINK         ND2AASN B 559                 C1  NAG B3559     1555   1555  1.44  
LINK         O4  NAG B3099                 C1  NAG B3100     1555   1555  1.45  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3452                 C1  NAG B3453     1555   1555  1.44  
LINK         O4  NAG B3559                 C1  NAG B3560     1555   1555  1.45  
LINK         OG ASER A 572                 C8  NAG A3570     1555   1555  1.29  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
CISPEP   1 ASN A  691    PRO A  692          0         0.59                     
CISPEP   2 PHE A  755    PRO A  756          0         2.10                     
CISPEP   3 GLN A  829    PRO A  830          0         0.85                     
CISPEP   4 SER B   84    PRO B   85          0         3.28                     
CISPEP   5 SER B  162    PRO B  163          0         3.05                     
CISPEP   6 SER B  168    PRO B  169          0        -2.14                     
SITE     1 AC1  8 ASN A   2  LEU A   3  ASP A   4  SER A 404                    
SITE     2 AC1  8 PRO A 452  ASN A 570  VAL A 571  SER A 572                    
SITE     1 AC2 13 LEU A 264  GLY A 282  GLU A 283  GLN A 284                    
SITE     2 AC2 13 MET A 285  ALA A 286  LYS B 253  ASN B 316                    
SITE     3 AC2 13 LEU B 317  GLN B 319  ASN B 320  SER B 510                    
SITE     4 AC2 13 NAG B3321                                                     
SITE     1 AC3  1 ASN A  15                                                     
SITE     1 AC4  2 ASN B  99  NAG B3371                                          
SITE     1 AC5  7 LEU A 600  ASP A 601  SER B 369  ASN B 371                    
SITE     2 AC5  7 SER B 398  GLU B 400  NAG B3099                               
SITE     1 AC6 24 PRO A 564  VAL A 566  GLN A 595  CYS A 608                    
SITE     2 AC6 24 VAL A 609  PRO A 610  GLN A 611  GLN A 613                    
SITE     3 AC6 24 ALA A 638  ASN A 639  GLU A 640  GLY A 641                    
SITE     4 AC6 24 GLU A 642  GLY A 643  LYS A 694  LYS A 695                    
SITE     5 AC6 24 ASN A 696  ALA A 697  GLN A 698  MET B 387                    
SITE     6 AC6 24 ASN B 449  ASN B 450  GLY B 451  ASN B 452                    
SITE     1 AC7 10 VAL B 529  THR B 554  TYR B 556  TYR B 557                    
SITE     2 AC7 10 ASN B 559  ASP B 627  GLU B 628  ASN B 629                    
SITE     3 AC7 10 THR B 630  ARG B 633                                          
SITE     1 AC8  5 GLU A 229  SER A 261  LEU A 264  ARG A 281                    
SITE     2 AC8  5 NAG B3320                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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