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Database: PDB
Entry: 6BXJ
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HEADER    CELL ADHESION                           18-DEC-17   6BXJ              
TITLE     STRUCTURE OF A SINGLE-CHAIN BETA3 INTEGRIN                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHIMERA PROTEIN OF INTEGRIN BETA-3 AND INTEGRIN ALPHA-L;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA,GPIIIA,CD11 ANTIGEN-LIKE
COMPND   5 FAMILY MEMBER A,LEUKOCYTE ADHESION GLYCOPROTEIN LFA-1 ALPHA CHAIN,   
COMPND   6 LFA-1A,LEUKOCYTE FUNCTION-ASSOCIATED MOLECULE 1 ALPHA CHAIN;         
COMPND   7 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: ITGB3, GP3A, ITGAL, CD11A;                                     
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    INTEGRIN, CELL ADHESION                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.M.THINN,Z.WANG,D.ZHOU,Y.ZHAO,B.R.CURTIS,J.ZHU                     
REVDAT   3   20-FEB-19 6BXJ    1       COMPND                                   
REVDAT   2   10-OCT-18 6BXJ    1       COMPND JRNL                              
REVDAT   1   03-OCT-18 6BXJ    0                                                
JRNL        AUTH   A.M.M.THINN,Z.WANG,D.ZHOU,Y.ZHAO,B.R.CURTIS,J.ZHU            
JRNL        TITL   AUTONOMOUS CONFORMATIONAL REGULATION OF BETA3INTEGRIN AND    
JRNL        TITL 2 THE CONFORMATION-DEPENDENT PROPERTY OF HPA-1A                
JRNL        TITL 3 ALLOANTIBODIES.                                              
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 115 E9105 2018              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   30209215                                                     
JRNL        DOI    10.1073/PNAS.1806205115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.12_2829                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.29                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 50811                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2556                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.3042 -  5.4799    0.99     2748   163  0.1637 0.2072        
REMARK   3     2  5.4799 -  4.3505    0.99     2717   171  0.1349 0.1730        
REMARK   3     3  4.3505 -  3.8009    0.99     2715   164  0.1473 0.1748        
REMARK   3     4  3.8009 -  3.4535    0.99     2712   147  0.1589 0.2141        
REMARK   3     5  3.4535 -  3.2060    0.99     2707   131  0.1782 0.2557        
REMARK   3     6  3.2060 -  3.0170    0.99     2732   138  0.1861 0.2511        
REMARK   3     7  3.0170 -  2.8659    0.99     2699   134  0.1896 0.2649        
REMARK   3     8  2.8659 -  2.7412    0.98     2702   137  0.1893 0.2629        
REMARK   3     9  2.7412 -  2.6357    0.98     2646   152  0.2058 0.2408        
REMARK   3    10  2.6357 -  2.5447    0.98     2677   161  0.2097 0.2511        
REMARK   3    11  2.5447 -  2.4652    0.98     2716   132  0.2103 0.2657        
REMARK   3    12  2.4652 -  2.3947    0.98     2617   148  0.2237 0.2958        
REMARK   3    13  2.3947 -  2.3317    0.97     2668   136  0.2412 0.3151        
REMARK   3    14  2.3317 -  2.2748    0.98     2679   132  0.2657 0.3129        
REMARK   3    15  2.2748 -  2.2231    0.97     2684   122  0.2869 0.3550        
REMARK   3    16  2.2231 -  2.1758    0.96     2647   131  0.2939 0.3746        
REMARK   3    17  2.1758 -  2.1322    0.96     2613   130  0.3049 0.3698        
REMARK   3    18  2.1322 -  2.0920    0.93     2576   127  0.3230 0.3405        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.630           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           4958                                  
REMARK   3   ANGLE     :  0.551           6710                                  
REMARK   3   CHIRALITY :  0.044            738                                  
REMARK   3   PLANARITY :  0.003            880                                  
REMARK   3   DIHEDRAL  : 14.928           3098                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 59 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  50.5861  36.2360  85.6662              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7136 T22:   1.0146                                     
REMARK   3      T33:   1.6186 T12:  -0.1668                                     
REMARK   3      T13:  -0.2835 T23:  -0.4973                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2039 L22:   0.0069                                     
REMARK   3      L33:   0.9807 L12:  -0.0892                                     
REMARK   3      L13:   1.0872 L23:  -0.0818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0567 S12:   0.1039 S13:   0.4344                       
REMARK   3      S21:   0.0293 S22:   0.6473 S23:  -1.2693                       
REMARK   3      S31:  -0.4927 S32:   1.3832 S33:   0.3262                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 60 THROUGH 86 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  31.3679   3.3966  68.8311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2313 T22:   0.3308                                     
REMARK   3      T33:   0.6910 T12:   0.0156                                     
REMARK   3      T13:   0.0201 T23:  -0.0612                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5062 L22:   3.1301                                     
REMARK   3      L33:   9.3979 L12:  -2.6858                                     
REMARK   3      L13:  -0.4979 L23:  -3.4816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0472 S12:   0.3041 S13:  -1.1229                       
REMARK   3      S21:  -0.0294 S22:   0.0498 S23:  -0.2247                       
REMARK   3      S31:   0.7258 S32:  -0.3888 S33:  -0.2152                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 125 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8721   9.2389  71.5587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2344 T22:   0.2312                                     
REMARK   3      T33:   0.3858 T12:   0.0372                                     
REMARK   3      T13:  -0.0535 T23:   0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6400 L22:   2.8082                                     
REMARK   3      L33:   0.4459 L12:   2.8634                                     
REMARK   3      L13:   0.6700 L23:   0.3893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1742 S12:  -0.0131 S13:   0.0833                       
REMARK   3      S21:   0.0668 S22:   0.1120 S23:  -0.2652                       
REMARK   3      S31:  -0.0283 S32:   0.0599 S33:   0.0171                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 271 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1685   0.2449  69.6828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1707 T22:   0.1950                                     
REMARK   3      T33:   0.2813 T12:  -0.0157                                     
REMARK   3      T13:   0.0031 T23:   0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6062 L22:   3.4912                                     
REMARK   3      L33:   1.2792 L12:  -0.2278                                     
REMARK   3      L13:  -0.1747 L23:  -0.1120                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0429 S12:  -0.0451 S13:  -0.0559                       
REMARK   3      S21:  -0.0158 S22:   0.0781 S23:   0.0329                       
REMARK   3      S31:   0.0329 S32:   0.0046 S33:  -0.0330                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 272 THROUGH 348 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3176  15.0678  68.4262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2218 T22:   0.2280                                     
REMARK   3      T33:   0.3396 T12:   0.0650                                     
REMARK   3      T13:   0.0115 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6323 L22:   4.3667                                     
REMARK   3      L33:   2.5057 L12:   3.6174                                     
REMARK   3      L13:   2.9009 L23:   2.0597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0934 S12:  -0.0775 S13:   0.0123                       
REMARK   3      S21:   0.0187 S22:   0.0904 S23:  -0.1647                       
REMARK   3      S31:  -0.0334 S32:  -0.0314 S33:  -0.0601                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 349 THROUGH 377 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1602  15.5614  83.1232              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4563 T22:   0.3408                                     
REMARK   3      T33:   0.6892 T12:   0.1387                                     
REMARK   3      T13:  -0.1749 T23:  -0.0360                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5203 L22:   2.3548                                     
REMARK   3      L33:   5.2898 L12:   2.3035                                     
REMARK   3      L13:   2.2086 L23:   1.0715                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3990 S12:  -0.7626 S13:   0.3869                       
REMARK   3      S21:   0.4836 S22:  -0.0044 S23:  -0.4952                       
REMARK   3      S31:  -0.4835 S32:  -0.1113 S33:   0.3158                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 378 THROUGH 413 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  53.9673  36.5459 105.6550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2056 T22:   1.2392                                     
REMARK   3      T33:   1.6599 T12:   0.0142                                     
REMARK   3      T13:  -0.9432 T23:  -0.3299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6494 L22:   0.1155                                     
REMARK   3      L33:   1.6794 L12:   0.3574                                     
REMARK   3      L13:   1.0902 L23:   0.4286                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2493 S12:  -0.3737 S13:  -0.2916                       
REMARK   3      S21:   0.2166 S22:  -0.0236 S23:  -0.1771                       
REMARK   3      S31:   0.2400 S32:   0.0261 S33:   0.7382                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 420 THROUGH 430 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1597  57.8043  96.9907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3512 T22:   1.0335                                     
REMARK   3      T33:   1.4494 T12:  -0.3531                                     
REMARK   3      T13:  -0.1704 T23:   0.0655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6762 L22:   2.5735                                     
REMARK   3      L33:   5.3442 L12:   3.0388                                     
REMARK   3      L13:   4.2702 L23:   3.7073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4425 S12:   0.9109 S13:   3.1476                       
REMARK   3      S21:   0.4936 S22:  -0.0763 S23:  -1.5387                       
REMARK   3      S31:  -2.7723 S32:   1.9440 S33:   0.5256                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 431 THROUGH 465 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.5914  46.5485  99.1668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7874 T22:   0.5599                                     
REMARK   3      T33:   0.7353 T12:  -0.1061                                     
REMARK   3      T13:  -0.2209 T23:  -0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5373 L22:   6.5412                                     
REMARK   3      L33:   7.4727 L12:   3.8392                                     
REMARK   3      L13:   1.8811 L23:   1.1400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0505 S12:  -0.1099 S13:   0.1867                       
REMARK   3      S21:   0.6766 S22:   0.0906 S23:  -0.8281                       
REMARK   3      S31:  -0.5402 S32:   0.5265 S33:  -0.0153                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 466 THROUGH 501 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.1568  36.7792  82.0849              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5197 T22:   0.4752                                     
REMARK   3      T33:   0.4741 T12:   0.0170                                     
REMARK   3      T13:  -0.0641 T23:  -0.0805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0886 L22:   8.6495                                     
REMARK   3      L33:   2.8617 L12:   0.5520                                     
REMARK   3      L13:   1.1644 L23:   3.3489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1438 S12:  -0.4436 S13:   0.4110                       
REMARK   3      S21:   0.3670 S22:  -0.4133 S23:   0.2558                       
REMARK   3      S31:  -0.8029 S32:  -0.1484 S33:   0.5402                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 502 THROUGH 588 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6498  28.5848  53.5072              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2380 T22:   0.2863                                     
REMARK   3      T33:   0.3274 T12:  -0.0200                                     
REMARK   3      T13:   0.0590 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6960 L22:   4.9625                                     
REMARK   3      L33:   4.2347 L12:  -0.9113                                     
REMARK   3      L13:   2.9392 L23:   0.1457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0576 S12:   0.0757 S13:  -0.2204                       
REMARK   3      S21:  -0.0873 S22:   0.0868 S23:  -0.1099                       
REMARK   3      S31:   0.0800 S32:   0.0803 S33:  -0.0318                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 589 THROUGH 625 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3839  28.3121  44.0409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4021 T22:   0.2926                                     
REMARK   3      T33:   0.3587 T12:  -0.0524                                     
REMARK   3      T13:  -0.0578 T23:  -0.0445                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1618 L22:   6.8466                                     
REMARK   3      L33:   7.8335 L12:   1.1347                                     
REMARK   3      L13:   1.6744 L23:   3.3624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2136 S12:   0.6142 S13:  -0.5774                       
REMARK   3      S21:  -0.6494 S22:  -0.0576 S23:   0.3613                       
REMARK   3      S31:   0.5857 S32:  -0.1442 S33:   0.3501                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6BXJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231752.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : TRUNCATE                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50880                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 64.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 20% 1,5-PENTANEDIOL, 4     
REMARK 280  MM ALKALIS, 66 MM GLY-GLY, 33 MM AMPD, PH 8.5., VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
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       62.64500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     ASP A   414                                                      
REMARK 465     TYR A   415                                                      
REMARK 465     ARG A   416                                                      
REMARK 465     PRO A   417                                                      
REMARK 465     SER A   418                                                      
REMARK 465     GLN A   419                                                      
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   NZ   LYS A   245     O    HOH A   801              2.05            
REMARK 500   OD2  ASP A   609     OG   SER A   611              2.15            
REMARK 500   O    HOH A  1099     O    HOH A  1202              2.17            
REMARK 500   O    HOH A  1339     O    HOH A  1357              2.19            
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    THR A   7       31.80    -98.16                                   
REMARK 500    PHE A  56       88.66   -151.90                                   
REMARK 500    ASP A  71     -105.70    -82.66                                   
REMARK 500    GLN A  79      156.67     66.56                                   
REMARK 500    SER A 156      -99.74   -142.47                                   
REMARK 500    LYS A 172      -28.54     68.24                                   
REMARK 500    LEU A 186     -133.43   -131.80                                   
REMARK 500    LEU A 187     -159.15    -89.87                                   
REMARK 500    GLN A 377       48.65   -109.63                                   
REMARK 500    ASN A 386     -139.36     64.39                                   
REMARK 500    LEU A 404     -167.14   -128.68                                   
REMARK 500    SER A 411      -99.40   -115.79                                   
REMARK 500    SER A 474       15.77     57.97                                   
REMARK 500    CYS A 538       76.64   -159.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1394        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH A1395        DISTANCE =  7.26 ANGSTROMS                       
REMARK 525    HOH A1396        DISTANCE =  8.75 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 121   OG                                                     
REMARK 620 2 SER A 123   OG   95.0                                              
REMARK 620 3 ASP A 221   OD2  93.1  97.8                                        
REMARK 620 4 HOH A 897   O    84.9 179.8  82.4                                  
REMARK 620 5 HOH A 835   O   160.7  85.9 105.9  94.2                            
REMARK 620 6 HOH A 941   O    86.3  86.8 175.4  93.1  74.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 702  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1391   O                                                      
REMARK 620 2 HOH A1244   O   105.2                                              
REMARK 620 3 HOH A1362   O   161.4  89.6                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 706 bound   
REMARK 800  to ASN A 99                                                         
DBREF  6BXJ A    1   109  UNP    P05106   ITB3_HUMAN      27    135             
DBREF  6BXJ A  110   286  UNP    P20701   ITAL_HUMAN     153    329             
DBREF  6BXJ A  287   625  UNP    P05106   ITB3_HUMAN     376    714             
SEQADV 6BXJ TRP A  171  UNP  P20701    ARG   214 CONFLICT                       
SEQRES   1 A  625  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 A  625  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 A  625  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 A  625  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 A  625  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 A  625  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 A  625  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 A  625  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 A  625  ARG GLN VAL GLU ASP GLY ASN VAL ASP LEU VAL PHE LEU          
SEQRES  10 A  625  PHE ASP GLY SER MET SER LEU GLN PRO ASP GLU PHE GLN          
SEQRES  11 A  625  LYS ILE LEU ASP PHE MET LYS ASP VAL MET LYS LYS LEU          
SEQRES  12 A  625  SER ASN THR SER TYR GLN PHE ALA ALA VAL GLN PHE SER          
SEQRES  13 A  625  THR SER TYR LYS THR GLU PHE ASP PHE SER ASP TYR VAL          
SEQRES  14 A  625  LYS TRP LYS ASP PRO ASP ALA LEU LEU LYS HIS VAL LYS          
SEQRES  15 A  625  HIS MET LEU LEU LEU THR ASN THR PHE GLY ALA ILE ASN          
SEQRES  16 A  625  TYR VAL ALA THR GLU VAL PHE ARG GLU GLU LEU GLY ALA          
SEQRES  17 A  625  ARG PRO ASP ALA THR LYS VAL LEU ILE ILE ILE THR ASP          
SEQRES  18 A  625  GLY GLU ALA THR ASP SER GLY ASN ILE ASP ALA ALA LYS          
SEQRES  19 A  625  ASP ILE ILE ARG TYR ILE ILE GLY ILE GLY LYS HIS PHE          
SEQRES  20 A  625  GLN THR LYS GLU SER GLN GLU THR LEU HIS LYS PHE ALA          
SEQRES  21 A  625  SER LYS PRO ALA SER GLU PHE VAL LYS ILE LEU ASP THR          
SEQRES  22 A  625  PHE GLU LYS LEU LYS ASP LEU PHE THR GLU LEU GLN LYS          
SEQRES  23 A  625  LYS ILE ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU          
SEQRES  24 A  625  PRO GLU GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU          
SEQRES  25 A  625  ASN ASN GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY          
SEQRES  26 A  625  LEU LYS ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA          
SEQRES  27 A  625  LYS VAL ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE          
SEQRES  28 A  625  THR ILE LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL          
SEQRES  29 A  625  GLN VAL THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN          
SEQRES  30 A  625  ALA GLU PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY          
SEQRES  31 A  625  THR PHE GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP          
SEQRES  32 A  625  LEU GLY SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG          
SEQRES  33 A  625  PRO SER GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN          
SEQRES  34 A  625  PRO VAL CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN          
SEQRES  35 A  625  CYS VAL CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY          
SEQRES  36 A  625  LYS TYR CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR          
SEQRES  37 A  625  LYS GLY GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS          
SEQRES  38 A  625  GLY ASP CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR          
SEQRES  39 A  625  CYS ASN CYS THR THR ARG THR ASP THR CYS MET SER SER          
SEQRES  40 A  625  ASN GLY LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS          
SEQRES  41 A  625  GLY SER CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP          
SEQRES  42 A  625  THR CYS GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR          
SEQRES  43 A  625  PHE LYS LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG          
SEQRES  44 A  625  GLY ALA LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS          
SEQRES  45 A  625  ARG ASP GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR          
SEQRES  46 A  625  GLY LYS ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP          
SEQRES  47 A  625  ASP CYS VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER          
SEQRES  48 A  625  GLY LYS SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS          
SEQRES  49 A  625  PRO                                                          
HET     MG  A 701       1                                                       
HET     MG  A 702       1                                                       
HET    NAG  A 703      14                                                       
HET    NAG  A 704      14                                                       
HET    NAG  A 705      14                                                       
HET    NAG  A 706      14                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   2   MG    2(MG 2+)                                                     
FORMUL   4  NAG    4(C8 H15 N O6)                                               
FORMUL   8  HOH   *596(H2 O)                                                    
HELIX    1 AA1 SER A   12  SER A   20  1                                   9    
HELIX    2 AA2 LEU A   40  ASP A   47  1                                   8    
HELIX    3 AA3 GLN A  125  LEU A  143  1                                  19    
HELIX    4 AA4 ASP A  164  LYS A  172  1                                   9    
HELIX    5 AA5 ASP A  173  LEU A  178  1                                   6    
HELIX    6 AA6 ASN A  189  VAL A  201  1                                  13    
HELIX    7 AA7 ARG A  203  GLY A  207  5                                   5    
HELIX    8 AA8 ILE A  230  LYS A  234  5                                   5    
HELIX    9 AA9 LYS A  245  GLN A  248  5                                   4    
HELIX   10 AB1 THR A  249  THR A  255  1                                   7    
HELIX   11 AB2 LEU A  256  ALA A  260  5                                   5    
HELIX   12 AB3 PRO A  263  PHE A  267  1                                   5    
HELIX   13 AB4 THR A  273  ASP A  279  5                                   7    
HELIX   14 AB5 LEU A  280  ILE A  288  1                                   9    
HELIX   15 AB6 CYS A  372  ALA A  378  5                                   7    
HELIX   16 AB7 PRO A  430  GLN A  434  5                                   5    
HELIX   17 AB8 THR A  501  MET A  505  5                                   5    
HELIX   18 AB9 LEU A  510  GLY A  514  5                                   5    
HELIX   19 AC1 ASP A  543  PHE A  557  1                                  15    
HELIX   20 AC2 GLY A  560  GLU A  565  1                                   6    
HELIX   21 AC3 THR A  567  CYS A  572  1                                   6    
SHEET    1 AA1 2 ALA A  24  TRP A  25  0                                        
SHEET    2 AA1 2 CYS A  38  ASP A  39 -1  O  ASP A  39   N  ALA A  24           
SHEET    1 AA2 6 GLU A  60  GLU A  65  0                                        
SHEET    2 AA2 6 ARG A  87  LEU A  92 -1  O  ALA A  89   N  ARG A  62           
SHEET    3 AA2 6 LEU A 362  PHE A 368  1  O  GLN A 365   N  LEU A  90           
SHEET    4 AA2 6 LYS A 349  PRO A 355 -1  N  LYS A 349   O  VAL A 366           
SHEET    5 AA2 6 VAL A 292  ARG A 297 -1  N  ARG A 297   O  THR A 352           
SHEET    6 AA2 6 SER A 322  CYS A 323 -1  O  CYS A 323   N  VAL A 292           
SHEET    1 AA3 5 VAL A  83  SER A  84  0                                        
SHEET    2 AA3 5 SER A  97  ARG A 105 -1  O  GLN A 103   N  SER A  84           
SHEET    3 AA3 5 THR A 331  VAL A 340 -1  O  ILE A 336   N  PHE A 100           
SHEET    4 AA3 5 LEU A 303  THR A 310 -1  N  THR A 310   O  SER A 333           
SHEET    5 AA3 5 VAL A 316  PRO A 318 -1  O  ILE A 317   N  ALA A 309           
SHEET    1 AA4 6 TYR A 159  PHE A 163  0                                        
SHEET    2 AA4 6 TYR A 148  PHE A 155 -1  N  GLN A 154   O  LYS A 160           
SHEET    3 AA4 6 VAL A 112  ASP A 119  1  N  PHE A 116   O  VAL A 153           
SHEET    4 AA4 6 THR A 213  THR A 220  1  O  ILE A 217   N  LEU A 117           
SHEET    5 AA4 6 ILE A 237  ILE A 243  1  O  ILE A 241   N  ILE A 218           
SHEET    6 AA4 6 VAL A 268  LEU A 271  1  O  LEU A 271   N  GLY A 242           
SHEET    1 AA5 3 GLU A 379  PRO A 380  0                                        
SHEET    2 AA5 3 THR A 391  GLU A 393 -1  O  PHE A 392   N  GLU A 379           
SHEET    3 AA5 3 VAL A 396  ARG A 398 -1  O  ARG A 398   N  THR A 391           
SHEET    1 AA6 2 GLY A 436  LEU A 439  0                                        
SHEET    2 AA6 2 GLN A 442  CYS A 445 -1  O  GLN A 442   N  LEU A 439           
SHEET    1 AA7 2 ILE A 453  THR A 454  0                                        
SHEET    2 AA7 2 CYS A 460  ASP A 461 -1  O  CYS A 460   N  THR A 454           
SHEET    1 AA8 2 ARG A 467  TYR A 468  0                                        
SHEET    2 AA8 2 GLU A 471  MET A 472 -1  O  GLU A 471   N  TYR A 468           
SHEET    1 AA9 2 GLY A 477  SER A 480  0                                        
SHEET    2 AA9 2 ASP A 483  CYS A 486 -1  O  LEU A 485   N  GLN A 478           
SHEET    1 AB1 2 TRP A 490  THR A 491  0                                        
SHEET    2 AB1 2 CYS A 497  THR A 498 -1  O  CYS A 497   N  THR A 491           
SHEET    1 AB2 2 GLY A 516  GLU A 519  0                                        
SHEET    2 AB2 2 SER A 522  CYS A 525 -1  O  VAL A 524   N  LYS A 517           
SHEET    1 AB3 4 GLU A 575  VAL A 579  0                                        
SHEET    2 AB3 4 SER A 614  VAL A 619  1  O  LEU A 616   N  GLU A 577           
SHEET    3 AB3 4 VAL A 601  GLU A 608 -1  N  TYR A 607   O  ILE A 615           
SHEET    4 AB3 4 ALA A 589  LYS A 595 -1  N  TYR A 594   O  VAL A 602           
SSBOND   1 CYS A    5    CYS A   23                          1555   1555  2.03  
SSBOND   2 CYS A   13    CYS A  372                          1555   1555  2.03  
SSBOND   3 CYS A   16    CYS A   38                          1555   1555  2.03  
SSBOND   4 CYS A   26    CYS A   49                          1555   1555  2.03  
SSBOND   5 CYS A  311    CYS A  323                          1555   1555  2.04  
SSBOND   6 CYS A  343    CYS A  370                          1555   1555  2.03  
SSBOND   7 CYS A  374    CYS A  394                          1555   1555  2.03  
SSBOND   8 CYS A  385    CYS A  397                          1555   1555  2.03  
SSBOND   9 CYS A  399    CYS A  408                          1555   1555  2.03  
SSBOND  10 CYS A  410    CYS A  440                          1555   1555  2.03  
SSBOND  11 CYS A  423    CYS A  438                          1555   1555  2.03  
SSBOND  12 CYS A  432    CYS A  443                          1555   1555  2.03  
SSBOND  13 CYS A  445    CYS A  458                          1555   1555  2.04  
SSBOND  14 CYS A  460    CYS A  481                          1555   1555  2.04  
SSBOND  15 CYS A  465    CYS A  479                          1555   1555  2.03  
SSBOND  16 CYS A  473    CYS A  484                          1555   1555  2.04  
SSBOND  17 CYS A  486    CYS A  495                          1555   1555  2.04  
SSBOND  18 CYS A  497    CYS A  520                          1555   1555  2.05  
SSBOND  19 CYS A  504    CYS A  518                          1555   1555  2.04  
SSBOND  20 CYS A  512    CYS A  523                          1555   1555  2.05  
SSBOND  21 CYS A  525    CYS A  535                          1555   1555  2.05  
SSBOND  22 CYS A  538    CYS A  541                          1555   1555  2.03  
SSBOND  23 CYS A  545    CYS A  592                          1555   1555  2.03  
SSBOND  24 CYS A  551    CYS A  572                          1555   1555  2.04  
SSBOND  25 CYS A  554    CYS A  568                          1555   1555  2.03  
SSBOND  26 CYS A  600    CYS A  624                          1555   1555  2.03  
LINK         ND2 ASN A  99                 C1  NAG A 706     1555   1555  1.43  
LINK         OG  SER A 121                MG    MG A 701     1555   1555  2.16  
LINK         OG  SER A 123                MG    MG A 701     1555   1555  2.00  
LINK         OD2 ASP A 221                MG    MG A 701     1555   1555  1.97  
LINK         ND2 ASN A 308                 C1  NAG A 703     1555   1555  1.44  
LINK         ND2 ASN A 496                 C1  NAG A 704     1555   1555  1.44  
LINK         ND2 ASN A 591                 C1  NAG A 705     1555   1555  1.44  
LINK        MG    MG A 701                 O   HOH A 897     1555   1555  2.15  
LINK        MG    MG A 702                 O   HOH A1391     1555   1555  2.65  
LINK        MG    MG A 702                 O   HOH A1244     1555   1555  3.00  
LINK        MG    MG A 701                 O   HOH A 835     1555   1455  2.06  
LINK        MG    MG A 701                 O   HOH A 941     1555   1455  2.07  
LINK        MG    MG A 702                 O   HOH A1362     1555   2647  2.52  
CISPEP   1 SER A   84    PRO A   85          0        -2.44                     
CISPEP   2 LYS A  262    PRO A  263          0        -2.57                     
SITE     1 AC1  6 SER A 121  SER A 123  ASP A 221  HOH A 835                    
SITE     2 AC1  6 HOH A 897  HOH A 941                                          
SITE     1 AC2  3 HOH A1074  HOH A1244  HOH A1391                               
SITE     1 AC3  6 ASN A 308  SER A 335  GLU A 337  NAG A 706                    
SITE     2 AC3  6 HOH A 871  HOH A 999                                          
SITE     1 AC4  4 TYR A 468  ASN A 496  HOH A 846  HOH A 988                    
SITE     1 AC5 12 ASP A 449  LEU A 582  LYS A 583  ASP A 584                    
SITE     2 AC5 12 ALA A 589  ASN A 591  HOH A 821  HOH A 904                    
SITE     3 AC5 12 HOH A 920  HOH A1002  HOH A1091  HOH A1100                    
SITE     1 AC6  4 SER A  97  ASN A  99  GLU A 337  NAG A 703                    
CRYST1   55.460  125.290   70.020  90.00 112.95  90.00 P 1 21 1      2          
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      0.018031  0.000000  0.007635        0.00000                         
SCALE2      0.000000  0.007981  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015509        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system