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Database: PDB
Entry: 4WK4
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HEADER    CELL ADHESION/IMMUNE SYSTEM             01-OCT-14   4WK4              
TITLE     METAL ION AND LIGAND BINDING OF INTEGRIN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-5;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 42-491;                                       
COMPND   5 SYNONYM: CD49 ANTIGEN-LIKE FAMILY MEMBER E,FIBRONECTIN RECEPTOR      
COMPND   6 SUBUNIT ALPHA,INTEGRIN ALPHA-F,VLA-5;                                
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-1;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 21-465;                                       
COMPND  12 SYNONYM: FIBRONECTIN RECEPTOR SUBUNIT BETA,GLYCOPROTEIN IIA,GPIIA,   
COMPND  13 VLA-4 SUBUNIT BETA;                                                  
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: ALA-CYS-ARG-GLY-ASP-GLY-TRP-CYS;                           
COMPND  17 CHAIN: C;                                                            
COMPND  18 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: ITGA5, FNRA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: ITGB1, FNRB, MDF2, MSK12;                                      
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;                                
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION-FIBRONECTIN RECEPTOR, CELL ADHESION-IMMUNE SYSTEM       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.XIA,T.A.SPRINGER                                                    
REVDAT   4   22-NOV-17 4WK4    1       COMPND SOURCE KEYWDS JRNL                
REVDAT   4 2                   1       REMARK LINK   SITE   ATOM                
REVDAT   3   24-DEC-14 4WK4    1       JRNL                                     
REVDAT   2   17-DEC-14 4WK4    1       JRNL                                     
REVDAT   1   03-DEC-14 4WK4    0                                                
JRNL        AUTH   W.XIA,T.A.SPRINGER                                           
JRNL        TITL   METAL ION AND LIGAND BINDING OF INTEGRIN ALPHA 5 BETA 1.     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111 17863 2014              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   25475857                                                     
JRNL        DOI    10.1073/PNAS.1420645111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.60                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.430                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 38531                          
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) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.180                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1996                            
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 47.6057 -  6.0215    0.96     2712   149  0.1646 0.2092        
REMARK   3     2  6.0215 -  4.7809    0.98     2628   144  0.1466 0.1878        
REMARK   3     3  4.7809 -  4.1770    0.99     2632   143  0.1268 0.1616        
REMARK   3     4  4.1770 -  3.7952    0.99     2629   143  0.1589 0.2300        
REMARK   3     5  3.7952 -  3.5233    0.99     2609   143  0.1836 0.2748        
REMARK   3     6  3.5233 -  3.3156    1.00     2601   141  0.1980 0.2463        
REMARK   3     7  3.3156 -  3.1496    1.00     2596   143  0.2234 0.2824        
REMARK   3     8  3.1496 -  3.0125    1.00     2618   142  0.2486 0.3030        
REMARK   3     9  3.0125 -  2.8966    1.00     2585   141  0.2664 0.3036        
REMARK   3    10  2.8966 -  2.7966    1.00     2605   144  0.2824 0.3150        
REMARK   3    11  2.7966 -  2.7092    1.00     2591   140  0.3044 0.3735        
REMARK   3    12  2.7092 -  2.6318    1.00     2571   140  0.3313 0.3706        
REMARK   3    13  2.6318 -  2.5625    1.00     2601   143  0.3558 0.3947        
REMARK   3    14  2.5625 -  2.5000    1.00     2557   140  0.4015 0.4201        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.550           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 71.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 104.0                          
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      :  0.005           7468                                  
REMARK   3   ANGLE     :  0.985          10115                                  
REMARK   3   CHIRALITY :  0.033           1183                                  
REMARK   3   PLANARITY :  0.003           1284                                  
REMARK   3   DIHEDRAL  : 12.067           2764                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 39 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2417 -19.0280 -22.8646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4977 T22:   0.9545                                     
REMARK   3      T33:   1.1471 T12:  -0.2306                                     
REMARK   3      T13:   0.0080 T23:   0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6950 L22:   6.9552                                     
REMARK   3      L33:   6.8740 L12:  -1.1625                                     
REMARK   3      L13:   0.6071 L23:   2.9104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2119 S12:   0.1287 S13:  -0.9108                       
REMARK   3      S21:  -0.4238 S22:   0.1939 S23:   0.6034                       
REMARK   3      S31:   0.8970 S32:  -1.3099 S33:  -0.1084                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 203 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6510  -3.5789  -8.8146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5363 T22:   0.8388                                     
REMARK   3      T33:   0.6959 T12:   0.1177                                     
REMARK   3      T13:   0.1274 T23:   0.0817                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1899 L22:   2.9267                                     
REMARK   3      L33:   3.2357 L12:   0.7752                                     
REMARK   3      L13:  -0.4552 L23:  -0.2173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0216 S12:  -0.7439 S13:  -0.3389                       
REMARK   3      S21:   0.3425 S22:   0.0493 S23:   0.6762                       
REMARK   3      S31:  -0.2802 S32:  -0.4396 S33:   0.0156                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 387 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3597 -15.3899 -23.6607              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4654 T22:   0.5068                                     
REMARK   3      T33:   0.6194 T12:  -0.0277                                     
REMARK   3      T13:   0.0539 T23:  -0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9650 L22:   2.9166                                     
REMARK   3      L33:   2.4804 L12:   0.0956                                     
REMARK   3      L13:   0.1046 L23:   0.2537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1457 S12:  -0.0383 S13:  -0.5508                       
REMARK   3      S21:  -0.2523 S22:   0.1570 S23:   0.1166                       
REMARK   3      S31:   0.1856 S32:   0.0353 S33:  -0.0043                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 388 THROUGH 450 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8280 -21.3527 -30.7679              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6112 T22:   0.8130                                     
REMARK   3      T33:   0.9594 T12:  -0.2141                                     
REMARK   3      T13:  -0.1105 T23:  -0.0892                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3302 L22:   6.7404                                     
REMARK   3      L33:   3.1750 L12:  -1.0840                                     
REMARK   3      L13:  -0.2481 L23:   0.0692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0686 S12:   0.4049 S13:  -0.5772                       
REMARK   3      S21:  -0.3796 S22:   0.0134 S23:   1.1253                       
REMARK   3      S31:   0.2065 S32:  -0.6956 S33:  -0.0228                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 31 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9200 -32.8706 -75.0477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7107 T22:   1.2103                                     
REMARK   3      T33:   1.0098 T12:  -0.0298                                     
REMARK   3      T13:   0.0903 T23:  -0.2203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3474 L22:   8.4395                                     
REMARK   3      L33:   5.1208 L12:  -2.6719                                     
REMARK   3      L13:   4.4438 L23:  -5.9891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7516 S12:  -0.3049 S13:  -0.6099                       
REMARK   3      S21:   1.3600 S22:   0.2424 S23:   0.3962                       
REMARK   3      S31:  -0.5140 S32:  -0.1755 S33:   0.5833                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 59 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7781 -37.4844 -83.1147              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8022 T22:   1.3608                                     
REMARK   3      T33:   1.7515 T12:   0.1180                                     
REMARK   3      T13:   0.3392 T23:  -0.2224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2272 L22:   4.5975                                     
REMARK   3      L33:   4.6307 L12:   4.9371                                     
REMARK   3      L13:   0.3765 L23:  -2.1229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0197 S12:   1.0783 S13:  -1.1895                       
REMARK   3      S21:  -0.3179 S22:   0.7776 S23:  -1.2091                       
REMARK   3      S31:  -0.2294 S32:   0.3090 S33:  -0.6780                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 97 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9486   2.9629 -72.0278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1736 T22:   0.9900                                     
REMARK   3      T33:   0.5377 T12:  -0.1911                                     
REMARK   3      T13:  -0.1969 T23:   0.0691                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6368 L22:   6.7001                                     
REMARK   3      L33:   0.9104 L12:   1.5614                                     
REMARK   3      L13:  -0.0212 L23:   2.1720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4858 S12:   0.5727 S13:   0.0813                       
REMARK   3      S21:  -1.7110 S22:   0.7488 S23:   0.4400                       
REMARK   3      S31:  -0.6205 S32:   0.0073 S33:  -0.2386                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 98 THROUGH 144 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4677   8.7630 -51.0300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5724 T22:   0.5238                                     
REMARK   3      T33:   0.6123 T12:  -0.0275                                     
REMARK   3      T13:  -0.0732 T23:   0.0739                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3202 L22:   3.0419                                     
REMARK   3      L33:   6.6130 L12:   0.4336                                     
REMARK   3      L13:  -1.0984 L23:   1.1126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0521 S12:   0.1368 S13:   0.2604                       
REMARK   3      S21:  -0.6720 S22:   0.2601 S23:   0.1306                       
REMARK   3      S31:  -1.1332 S32:   0.4924 S33:  -0.3590                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 145 THROUGH 250 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2503  19.9999 -34.7216              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9659 T22:   0.5335                                     
REMARK   3      T33:   0.8118 T12:   0.0411                                     
REMARK   3      T13:   0.1188 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1497 L22:   1.7320                                     
REMARK   3      L33:   5.2705 L12:   1.3908                                     
REMARK   3      L13:  -2.8126 L23:  -2.3022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5691 S12:  -0.1871 S13:   0.9477                       
REMARK   3      S21:   0.3639 S22:   0.0781 S23:   0.4023                       
REMARK   3      S31:  -1.1438 S32:   0.2695 S33:  -0.6105                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 251 THROUGH 346 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6994   7.4322 -36.4283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6128 T22:   0.4756                                     
REMARK   3      T33:   0.5107 T12:  -0.0224                                     
REMARK   3      T13:  -0.0828 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9329 L22:   3.7484                                     
REMARK   3      L33:   6.5751 L12:   1.8301                                     
REMARK   3      L13:  -3.4607 L23:  -2.2088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0161 S12:   0.0077 S13:   0.3111                       
REMARK   3      S21:   0.0366 S22:   0.1666 S23:   0.1778                       
REMARK   3      S31:  -0.1912 S32:  -0.0788 S33:  -0.0936                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 347 THROUGH 380 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2693   1.3789 -53.3398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8647 T22:   0.7230                                     
REMARK   3      T33:   0.6343 T12:   0.0284                                     
REMARK   3      T13:  -0.0613 T23:   0.1343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5936 L22:   7.3958                                     
REMARK   3      L33:   8.8379 L12:   3.0167                                     
REMARK   3      L13:   2.8232 L23:   7.0206                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4765 S12:   0.1568 S13:  -0.0462                       
REMARK   3      S21:   0.7118 S22:   0.1322 S23:  -0.1458                       
REMARK   3      S31:   0.7858 S32:   0.0884 S33:  -0.6942                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 381 THROUGH 420 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4226  -4.8976 -61.1763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9231 T22:   0.8904                                     
REMARK   3      T33:   0.7009 T12:   0.0280                                     
REMARK   3      T13:  -0.0422 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8564 L22:   8.1459                                     
REMARK   3      L33:   5.4200 L12:   6.3201                                     
REMARK   3      L13:   3.1220 L23:   3.7956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1675 S12:  -0.1274 S13:  -0.8307                       
REMARK   3      S21:   0.2825 S22:  -0.0082 S23:  -0.9964                       
REMARK   3      S31:   0.4451 S32:  -0.0361 S33:  -0.1453                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 445 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5829  -6.1986 -65.7158              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9256 T22:   0.9002                                     
REMARK   3      T33:   0.5899 T12:  -0.1417                                     
REMARK   3      T13:  -0.1494 T23:   0.1453                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5045 L22:   9.7372                                     
REMARK   3      L33:   8.9067 L12:   1.6989                                     
REMARK   3      L13:   2.0452 L23:   7.0935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3629 S12:   0.4581 S13:  -0.2830                       
REMARK   3      S21:  -0.0177 S22:  -0.3480 S23:   1.4540                       
REMARK   3      S31:   0.4000 S32:  -0.5756 S33:   0.6416                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 8 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1514  12.7560 -15.2935              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1475 T22:   0.8688                                     
REMARK   3      T33:   0.9462 T12:  -0.2175                                     
REMARK   3      T13:  -0.1434 T23:  -0.2000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1040 L22:   5.2946                                     
REMARK   3      L33:   4.6773 L12:  -4.9392                                     
REMARK   3      L13:   5.1864 L23:  -4.9345                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.3369 S12:  -0.9770 S13:   2.1500                       
REMARK   3      S21:   1.6437 S22:   0.3281 S23:  -2.0364                       
REMARK   3      S31:  -2.1814 S32:   1.0920 S33:   1.0732                       
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 4WK4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203960.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38535                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES 7.2, 16% PEG 6000, PH 7.2,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       28.76000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       84.77000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.08000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       84.77000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.76000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.08000            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLN B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     LYS B    80                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     THR B    82                                                      
REMARK 465     ALA B    83                                                      
REMARK 465     GLU B    84                                                      
REMARK 465     LYS B   417                                                      
REMARK 465     LYS B   418                                                      
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  HD21  ASN B    30     C1   NAG B   511              0.85            
REMARK 500  HD21  ASN B   386     C1   NAG B   507              0.88            
REMARK 500  HD21  ASN B   386     O5   NAG B   507              1.15            
REMARK 500   ND2  ASN A    43     C1   NAG A   515              1.19            
REMARK 500  HD21  ASN B    30     C2   NAG B   511              1.28            
REMARK 500   C    SER A    87     H    GLU A    88              1.39            
REMARK 500  HD21  ASN B   249     C1   NAG B   504              1.51            
REMARK 500   O4   NAG A   520     H1   BMA A   521              1.54            
REMARK 500   ND2  ASN B    30     C1   NAG B   511              1.69            
REMARK 500   ND2  ASN B   386     C1   NAG B   507              1.73            
REMARK 500   ND2  ASN B   386     O5   NAG B   507              1.91            
REMARK 500   ND2  ASN A    43     O5   NAG A   515              1.96            
REMARK 500   ND2  ASN B    30     C2   NAG B   511              2.09            
REMARK 500   ND2  ASN A   266     O5   NAG A   519              2.09            
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    GLU A  88   C   -  N   -  CA  ANGL. DEV. =  18.2 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    ASP A   4       69.38    -69.34                                   
REMARK 500    PRO A  28       48.68    -81.44                                   
REMARK 500    SER A  82       43.91    -96.71                                   
REMARK 500    SER A  83       16.85   -163.25                                   
REMARK 500    SER A  85      -72.79    -83.44                                   
REMARK 500    SER A  86     -154.79     51.77                                   
REMARK 500    SER A  87      -61.94    -91.04                                   
REMARK 500    THR A 123      157.71     75.18                                   
REMARK 500    LYS A 125     -119.27   -126.07                                   
REMARK 500    ASN A 141       61.82     61.48                                   
REMARK 500    SER A 153     -169.40   -120.73                                   
REMARK 500    TRP A 157      177.23     65.48                                   
REMARK 500    TYR A 205       76.52   -162.91                                   
REMARK 500    ASP A 243     -154.32   -132.36                                   
REMARK 500    ASN A 256       73.01     47.91                                   
REMARK 500    ILE A 270       25.34     45.94                                   
REMARK 500    PHE A 285      108.35    -58.58                                   
REMARK 500    ASN A 295       24.98   -142.26                                   
REMARK 500    PRO A 374       -8.51    -57.20                                   
REMARK 500    SER A 409     -163.66    -79.12                                   
REMARK 500    SER A 437       69.98   -161.59                                   
REMARK 500    LYS B   9       47.09    -86.40                                   
REMARK 500    ASN B  11       67.43     35.53                                   
REMARK 500    THR B  32      -14.45     79.53                                   
REMARK 500    ALA B  42      -10.85   -150.19                                   
REMARK 500    ASN B  62       76.88   -154.64                                   
REMARK 500    SER B 105      108.25    -58.82                                   
REMARK 500    VAL B 168      -80.99   -139.58                                   
REMARK 500    THR B 171       44.90    -94.12                                   
REMARK 500    LYS B 208       90.99    -69.83                                   
REMARK 500    SER B 222     -153.52   -116.36                                   
REMARK 500    ASN B 224     -164.84   -160.40                                   
REMARK 500    LEU B 225      -68.99    -97.45                                   
REMARK 500    CYS B 241       76.99    -69.72                                   
REMARK 500    VAL B 250     -157.11   -145.91                                   
REMARK 500    CYS C   2       89.43     55.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A  515                                                       
REMARK 610     NAG B  507                                                       
REMARK 610     NAG B  511                                                       
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                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 239   OE1                                                    
REMARK 620 2 GLU A 239   OE2  53.3                                              
REMARK 620 3 SER A 241   OG  129.7  77.7                                        
REMARK 620 4 ASP A 243   OD1  73.1  68.3  79.2                                  
REMARK 620 5 THR A 245   O    66.7 118.2 148.8  82.5                            
REMARK 620 6 ASP A 247   OD1 128.6 133.8  92.1 154.2  93.5                      
REMARK 620 7 ASP A 247   OD2  87.3  82.5  98.1 150.6 110.0  54.2                
REMARK 620 8 HOH A 606   O   134.2 141.3  77.0  78.4  74.7  76.0 129.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 293   OD1                                                    
REMARK 620 2 ASN A 295   OD1  69.6                                              
REMARK 620 3 ASP A 297   OD1  67.6  80.3                                        
REMARK 620 4 LEU A 299   O    86.8 156.2  93.1                                  
REMARK 620 5 ASP A 301   OD1 135.2 114.9 154.9  80.1                            
REMARK 620 6 ASP A 301   OD2  87.8  77.0 151.2 100.6  53.6                      
REMARK 620 7 HOH A 632   O   146.2  85.9  86.1 116.6  75.8 109.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 360   OD1                                                    
REMARK 620 2 ASP A 362   OD1  79.6                                              
REMARK 620 3 ASP A 364   OD1  63.6  60.2                                        
REMARK 620 4 TYR A 366   O    56.9 133.7  84.7                                  
REMARK 620 5 ASP A 368   OD1 133.6 141.3 144.4  84.8                            
REMARK 620 6 ASP A 368   OD2 112.3  99.3 159.3 110.5  54.1                      
REMARK 620 7 HOH A 618   O   135.7  95.5  75.8 104.7  74.2 111.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 424   OD1                                                    
REMARK 620 2 ASP A 426   OD1  58.8                                              
REMARK 620 3 ASN A 428   OD1  74.2  73.8                                        
REMARK 620 4 TYR A 430   O    72.3 129.2  80.9                                  
REMARK 620 5 ASP A 432   OD1 135.2 126.6 148.8  97.1                            
REMARK 620 6 ASP A 432   OD2  87.3  83.4 155.8 108.7  54.1                      
REMARK 620 7 HOH A 633   O   146.4 106.5  72.5 106.6  78.4 122.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 132   OG                                                     
REMARK 620 2 SER B 134   OG   92.6                                              
REMARK 620 3 GLU B 229   OE1 102.9 164.5                                        
REMARK 620 4 ASP C   5   OD1 106.8  88.6  87.5                                  
REMARK 620 5 HOH B 623   O    81.1  72.3 109.1 159.9                            
REMARK 620 6 HOH B 617   O   169.9  94.4  70.2  80.8  94.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 134   O                                                      
REMARK 620 2 ASP B 137   OD1 120.8                                              
REMARK 620 3 ASP B 138   OD1 124.4  78.5                                        
REMARK 620 4 HOH B 622   O    56.1 140.1 139.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 169   OE1                                                    
REMARK 620 2 ASN B 224   OD1  90.6                                              
REMARK 620 3 ASP B 226   O   158.4  93.1                                        
REMARK 620 4 ASP B 226   OD1  86.5  84.6  72.7                                  
REMARK 620 5 PRO B 228   O    88.8 177.6  88.2  97.7                            
REMARK 620 6 GLU B 229   OE2 102.7  82.3  98.8 164.0  95.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  522 through MAN A 528 bound to ASN A 141                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  511 through MAN A 514 bound to ASN A 256                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  519 through BMA A 521 bound to ASN A 266                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  505 through MAN A 510 bound to ASN A 275                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  504 through BMA B 506 bound to ASN B 249                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 510 bound   
REMARK 800  to ASN B 343                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 509 bound   
REMARK 800  to ASN B 397                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  515 through MAN A 518                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  507 through NAG B 508                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WJK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WK0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WK2   RELATED DB: PDB                                   
DBREF  4WK4 A    1   450  UNP    P08648   ITA5_HUMAN      42    491             
DBREF  4WK4 B    1   445  UNP    P05556   ITB1_HUMAN      21    465             
DBREF  4WK4 C    1     8  PDB    4WK4     4WK4             1      8             
SEQADV 4WK4 THR B  195  UNP  P05556    SER   215 CONFLICT                       
SEQRES   1 A  450  PHE ASN LEU ASP ALA GLU ALA PRO ALA VAL LEU SER GLY          
SEQRES   2 A  450  PRO PRO GLY SER PHE PHE GLY PHE SER VAL GLU PHE TYR          
SEQRES   3 A  450  ARG PRO GLY THR ASP GLY VAL SER VAL LEU VAL GLY ALA          
SEQRES   4 A  450  PRO LYS ALA ASN THR SER GLN PRO GLY VAL LEU GLN GLY          
SEQRES   5 A  450  GLY ALA VAL TYR LEU CYS PRO TRP GLY ALA SER PRO THR          
SEQRES   6 A  450  GLN CYS THR PRO ILE GLU PHE ASP SER LYS GLY SER ARG          
SEQRES   7 A  450  LEU LEU GLU SER SER LEU SER SER SER GLU GLY GLU GLU          
SEQRES   8 A  450  PRO VAL GLU TYR LYS SER LEU GLN TRP PHE GLY ALA THR          
SEQRES   9 A  450  VAL ARG ALA HIS GLY SER SER ILE LEU ALA CYS ALA PRO          
SEQRES  10 A  450  LEU TYR SER TRP ARG THR GLU LYS GLU PRO LEU SER ASP          
SEQRES  11 A  450  PRO VAL GLY THR CYS TYR LEU SER THR ASP ASN PHE THR          
SEQRES  12 A  450  ARG ILE LEU GLU TYR ALA PRO CYS ARG SER ASP PHE SER          
SEQRES  13 A  450  TRP ALA ALA GLY GLN GLY TYR CYS GLN GLY GLY PHE SER          
SEQRES  14 A  450  ALA GLU PHE THR LYS THR GLY ARG VAL VAL LEU GLY GLY          
SEQRES  15 A  450  PRO GLY SER TYR PHE TRP GLN GLY GLN ILE LEU SER ALA          
SEQRES  16 A  450  THR GLN GLU GLN ILE ALA GLU SER TYR TYR PRO GLU TYR          
SEQRES  17 A  450  LEU ILE ASN LEU VAL GLN GLY GLN LEU GLN THR ARG GLN          
SEQRES  18 A  450  ALA SER SER ILE TYR ASP ASP SER TYR LEU GLY TYR SER          
SEQRES  19 A  450  VAL ALA VAL GLY GLU PHE SER GLY ASP ASP THR GLU ASP          
SEQRES  20 A  450  PHE VAL ALA GLY VAL PRO LYS GLY ASN LEU THR TYR GLY          
SEQRES  21 A  450  TYR VAL THR ILE LEU ASN GLY SER ASP ILE ARG SER LEU          
SEQRES  22 A  450  TYR ASN PHE SER GLY GLU GLN MET ALA SER TYR PHE GLY          
SEQRES  23 A  450  TYR ALA VAL ALA ALA THR ASP VAL ASN GLY ASP GLY LEU          
SEQRES  24 A  450  ASP ASP LEU LEU VAL GLY ALA PRO LEU LEU MET ASP ARG          
SEQRES  25 A  450  THR PRO ASP GLY ARG PRO GLN GLU VAL GLY ARG VAL TYR          
SEQRES  26 A  450  VAL TYR LEU GLN HIS PRO ALA GLY ILE GLU PRO THR PRO          
SEQRES  27 A  450  THR LEU THR LEU THR GLY HIS ASP GLU PHE GLY ARG PHE          
SEQRES  28 A  450  GLY SER SER LEU THR PRO LEU GLY ASP LEU ASP GLN ASP          
SEQRES  29 A  450  GLY TYR ASN ASP VAL ALA ILE GLY ALA PRO PHE GLY GLY          
SEQRES  30 A  450  GLU THR GLN GLN GLY VAL VAL PHE VAL PHE PRO GLY GLY          
SEQRES  31 A  450  PRO GLY GLY LEU GLY SER LYS PRO SER GLN VAL LEU GLN          
SEQRES  32 A  450  PRO LEU TRP ALA ALA SER HIS THR PRO ASP PHE PHE GLY          
SEQRES  33 A  450  SER ALA LEU ARG GLY GLY ARG ASP LEU ASP GLY ASN GLY          
SEQRES  34 A  450  TYR PRO ASP LEU ILE VAL GLY SER PHE GLY VAL ASP LYS          
SEQRES  35 A  450  ALA VAL VAL TYR ARG GLY ARG PRO                              
SEQRES   1 B  445  GLN THR ASP GLU ASN ARG CYS LEU LYS ALA ASN ALA LYS          
SEQRES   2 B  445  SER CYS GLY GLU CYS ILE GLN ALA GLY PRO ASN CYS GLY          
SEQRES   3 B  445  TRP CYS THR ASN SER THR PHE LEU GLN GLU GLY MET PRO          
SEQRES   4 B  445  THR SER ALA ARG CYS ASP ASP LEU GLU ALA LEU LYS LYS          
SEQRES   5 B  445  LYS GLY CYS PRO PRO ASP ASP ILE GLU ASN PRO ARG GLY          
SEQRES   6 B  445  SER LYS ASP ILE LYS LYS ASN LYS ASN VAL THR ASN ARG          
SEQRES   7 B  445  SER LYS GLY THR ALA GLU LYS LEU LYS PRO GLU ASP ILE          
SEQRES   8 B  445  THR GLN ILE GLN PRO GLN GLN LEU VAL LEU ARG LEU ARG          
SEQRES   9 B  445  SER GLY GLU PRO GLN THR PHE THR LEU LYS PHE LYS ARG          
SEQRES  10 B  445  ALA GLU ASP TYR PRO ILE ASP LEU TYR TYR LEU MET ASP          
SEQRES  11 B  445  LEU SER TYR SER MET LYS ASP ASP LEU GLU ASN VAL LYS          
SEQRES  12 B  445  SER LEU GLY THR ASP LEU MET ASN GLU MET ARG ARG ILE          
SEQRES  13 B  445  THR SER ASP PHE ARG ILE GLY PHE GLY SER PHE VAL GLU          
SEQRES  14 B  445  LYS THR VAL MET PRO TYR ILE SER THR THR PRO ALA LYS          
SEQRES  15 B  445  LEU ARG ASN PRO CYS THR SER GLU GLN ASN CYS THR THR          
SEQRES  16 B  445  PRO PHE SER TYR LYS ASN VAL LEU SER LEU THR ASN LYS          
SEQRES  17 B  445  GLY GLU VAL PHE ASN GLU LEU VAL GLY LYS GLN ARG ILE          
SEQRES  18 B  445  SER GLY ASN LEU ASP SER PRO GLU GLY GLY PHE ASP ALA          
SEQRES  19 B  445  ILE MET GLN VAL ALA VAL CYS GLY SER LEU ILE GLY TRP          
SEQRES  20 B  445  ARG ASN VAL THR ARG LEU LEU VAL PHE SER THR ASP ALA          
SEQRES  21 B  445  GLY PHE HIS PHE ALA GLY ASP GLY LYS LEU GLY GLY ILE          
SEQRES  22 B  445  VAL LEU PRO ASN ASP GLY GLN CYS HIS LEU GLU ASN ASN          
SEQRES  23 B  445  MET TYR THR MET SER HIS TYR TYR ASP TYR PRO SER ILE          
SEQRES  24 B  445  ALA HIS LEU VAL GLN LYS LEU SER GLU ASN ASN ILE GLN          
SEQRES  25 B  445  THR ILE PHE ALA VAL THR GLU GLU PHE GLN PRO VAL TYR          
SEQRES  26 B  445  LYS GLU LEU LYS ASN LEU ILE PRO LYS SER ALA VAL GLY          
SEQRES  27 B  445  THR LEU SER ALA ASN SER SER ASN VAL ILE GLN LEU ILE          
SEQRES  28 B  445  ILE ASP ALA TYR ASN SER LEU SER SER GLU VAL ILE LEU          
SEQRES  29 B  445  GLU ASN GLY LYS LEU SER GLU GLY VAL THR ILE SER TYR          
SEQRES  30 B  445  LYS SER TYR CYS LYS ASN GLY VAL ASN GLY THR GLY GLU          
SEQRES  31 B  445  ASN GLY ARG LYS CYS SER ASN ILE SER ILE GLY ASP GLU          
SEQRES  32 B  445  VAL GLN PHE GLU ILE SER ILE THR SER ASN LYS CYS PRO          
SEQRES  33 B  445  LYS LYS ASP SER ASP SER PHE LYS ILE ARG PRO LEU GLY          
SEQRES  34 B  445  PHE THR GLU GLU VAL GLU VAL ILE LEU GLN TYR ILE CYS          
SEQRES  35 B  445  GLU CYS GLU                                                  
SEQRES   1 C    8  ALA CYS ARG GLY ASP GLY TRP CYS                              
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET    NAG  A 505      27                                                       
HET    NAG  A 506      27                                                       
HET    BMA  A 507      20                                                       
HET    MAN  A 508      21                                                       
HET    MAN  A 509      20                                                       
HET    MAN  A 510      21                                                       
HET    NAG  A 511      27                                                       
HET    NAG  A 512      27                                                       
HET    BMA  A 513      20                                                       
HET    MAN  A 514      21                                                       
HET    NAG  A 515      27                                                       
HET    NAG  A 516      27                                                       
HET    BMA  A 517      20                                                       
HET    MAN  A 518      21                                                       
HET    NAG  A 519      27                                                       
HET    NAG  A 520      27                                                       
HET    BMA  A 521      21                                                       
HET    NAG  A 522      27                                                       
HET    NAG  A 523      27                                                       
HET    BMA  A 524      20                                                       
HET    MAN  A 525      21                                                       
HET    MAN  A 526      20                                                       
HET    MAN  A 527      21                                                       
HET    MAN  A 528      21                                                       
HET     MG  B 501       1                                                       
HET     CA  B 502       1                                                       
HET     CA  B 503       1                                                       
HET    NAG  B 504      27                                                       
HET    NAG  B 505      27                                                       
HET    BMA  B 506      21                                                       
HET    NAG  B 507      27                                                       
HET    NAG  B 508      28                                                       
HET    NAG  B 509      28                                                       
HET    NAG  B 510      28                                                       
HET    NAG  B 511      28                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   4   CA    6(CA 2+)                                                     
FORMUL   8  NAG    17(C8 H15 N O6)                                              
FORMUL   8  BMA    6(C6 H12 O6)                                                 
FORMUL   8  MAN    9(C6 H12 O6)                                                 
FORMUL  13   MG    MG 2+                                                        
FORMUL  21  HOH   *188(H2 O)                                                    
HELIX    1 AA1 LEU A   80  LEU A   84  5                                   5    
HELIX    2 AA2 GLY A  184  GLN A  189  1                                   6    
HELIX    3 AA3 THR A  196  GLU A  202  1                                   7    
HELIX    4 AA4 SER A  223  ASP A  227  5                                   5    
HELIX    5 AA5 PHE A  438  VAL A  440  5                                   3    
HELIX    6 AA6 CYS B    7  ASN B   11  5                                   5    
HELIX    7 AA7 SER B   14  ALA B   21  1                                   8    
HELIX    8 AA8 LEU B   47  GLY B   54  1                                   8    
HELIX    9 AA9 PRO B   56  ASP B   58  5                                   3    
HELIX   10 AB1 SER B  132  SER B  134  5                                   3    
HELIX   11 AB2 MET B  135  GLU B  140  1                                   6    
HELIX   12 AB3 ASN B  141  LYS B  143  5                                   3    
HELIX   13 AB4 SER B  144  ARG B  154  1                                  11    
HELIX   14 AB5 THR B  179  ASN B  185  1                                   7    
HELIX   15 AB6 LYS B  208  GLY B  217  1                                  10    
HELIX   16 AB7 GLY B  230  CYS B  241  1                                  12    
HELIX   17 AB8 CYS B  241  GLY B  246  1                                   6    
HELIX   18 AB9 GLY B  266  GLY B  272  5                                   7    
HELIX   19 AC1 SER B  298  ASN B  309  1                                  12    
HELIX   20 AC2 PHE B  321  ILE B  332  1                                  12    
HELIX   21 AC3 ASN B  346  SER B  360  1                                  15    
HELIX   22 AC4 CYS B  381  VAL B  385  5                                   5    
HELIX   23 AC5 GLU B  390  GLY B  392  5                                   3    
SHEET    1 AA1 4 ALA A   9  SER A  12  0                                        
SHEET    2 AA1 4 LYS A 442  TYR A 446 -1  O  ALA A 443   N  LEU A  11           
SHEET    3 AA1 4 ASP A 432  SER A 437 -1  N  LEU A 433   O  TYR A 446           
SHEET    4 AA1 4 LEU A 419  ARG A 423 -1  N  ARG A 420   O  ILE A 434           
SHEET    1 AA2 4 VAL A  23  TYR A  26  0                                        
SHEET    2 AA2 4 SER A  34  ALA A  39 -1  O  LEU A  36   N  GLU A  24           
SHEET    3 AA2 4 ALA A  54  PRO A  59 -1  O  CYS A  58   N  VAL A  35           
SHEET    4 AA2 4 THR A  68  ILE A  70 -1  O  THR A  68   N  LEU A  57           
SHEET    1 AA3 2 GLU A  94  TYR A  95  0                                        
SHEET    2 AA3 2 SER A 120  TRP A 121 -1  O  SER A 120   N  TYR A  95           
SHEET    1 AA4 4 VAL A 105  HIS A 108  0                                        
SHEET    2 AA4 4 SER A 111  ALA A 116 -1  O  LEU A 113   N  ARG A 106           
SHEET    3 AA4 4 THR A 134  THR A 139 -1  O  THR A 134   N  ALA A 116           
SHEET    4 AA4 4 ARG A 144  TYR A 148 -1  O  LEU A 146   N  LEU A 137           
SHEET    1 AA5 4 SER A 169  PHE A 172  0                                        
SHEET    2 AA5 4 VAL A 178  GLY A 182 -1  O  GLY A 181   N  SER A 169           
SHEET    3 AA5 4 GLN A 191  ALA A 195 -1  O  LEU A 193   N  LEU A 180           
SHEET    4 AA5 4 LEU A 217  GLN A 218 -1  O  LEU A 217   N  SER A 194           
SHEET    1 AA6 4 VAL A 235  GLY A 238  0                                        
SHEET    2 AA6 4 ASP A 247  VAL A 252 -1  O  ASP A 247   N  GLY A 238           
SHEET    3 AA6 4 TYR A 261  LEU A 265 -1  O  THR A 263   N  ALA A 250           
SHEET    4 AA6 4 SER A 272  SER A 277 -1  O  LEU A 273   N  ILE A 264           
SHEET    1 AA7 4 VAL A 289  THR A 292  0                                        
SHEET    2 AA7 4 ASP A 301  ALA A 306 -1  O  LEU A 303   N  ALA A 290           
SHEET    3 AA7 4 ARG A 323  TYR A 327 -1  O  ARG A 323   N  ALA A 306           
SHEET    4 AA7 4 LEU A 340  THR A 343 -1  O  LEU A 342   N  VAL A 324           
SHEET    1 AA8 2 MET A 310  ARG A 312  0                                        
SHEET    2 AA8 2 PRO A 318  GLU A 320 -1  O  GLN A 319   N  ASP A 311           
SHEET    1 AA9 4 LEU A 355  GLY A 359  0                                        
SHEET    2 AA9 4 ASP A 368  ALA A 373 -1  O  ASP A 368   N  GLY A 359           
SHEET    3 AA9 4 VAL A 383  PHE A 387 -1  O  PHE A 387   N  VAL A 369           
SHEET    4 AA9 4 GLN A 400  LEU A 402 -1  O  GLN A 400   N  VAL A 386           
SHEET    1 AB1 3 CYS B  44  ASP B  46  0                                        
SHEET    2 AB1 3 CYS B  25  CYS B  28 -1  N  GLY B  26   O  ASP B  45           
SHEET    3 AB1 3 ILE B  60  GLU B  61 -1  O  GLU B  61   N  TRP B  27           
SHEET    1 AB2 6 LYS B  67  LYS B  71  0                                        
SHEET    2 AB2 6 GLN B  98  ARG B 104 -1  O  VAL B 100   N  ASP B  68           
SHEET    3 AB2 6 VAL B 434  ILE B 441  1  O  GLN B 439   N  LEU B 103           
SHEET    4 AB2 6 ASP B 421  PRO B 427 -1  N  ILE B 425   O  VAL B 434           
SHEET    5 AB2 6 VAL B 362  ASN B 366 -1  N  GLU B 365   O  ARG B 426           
SHEET    6 AB2 6 LYS B 394  CYS B 395 -1  O  CYS B 395   N  VAL B 362           
SHEET    1 AB3 4 ILE B  94  GLN B  95  0                                        
SHEET    2 AB3 4 PRO B 108  LYS B 116 -1  O  LYS B 114   N  GLN B  95           
SHEET    3 AB3 4 GLU B 403  THR B 411 -1  O  VAL B 404   N  PHE B 115           
SHEET    4 AB3 4 THR B 374  TYR B 380 -1  N  LYS B 378   O  GLU B 407           
SHEET    1 AB4 6 TYR B 199  THR B 206  0                                        
SHEET    2 AB4 6 PHE B 160  PHE B 167 -1  N  ILE B 162   O  THR B 206           
SHEET    3 AB4 6 ILE B 123  ASP B 130  1  N  TYR B 127   O  GLY B 165           
SHEET    4 AB4 6 THR B 251  THR B 258  1  O  LEU B 253   N  ASP B 124           
SHEET    5 AB4 6 GLN B 312  VAL B 317  1  O  ILE B 314   N  LEU B 254           
SHEET    6 AB4 6 SER B 335  THR B 339  1  O  ALA B 336   N  PHE B 315           
SHEET    1 AB5 2 LEU B 283  GLU B 284  0                                        
SHEET    2 AB5 2 MET B 287  TYR B 288 -1  O  MET B 287   N  GLU B 284           
SSBOND   1 CYS A   58    CYS A   67                          1555   1555  2.03  
SSBOND   2 CYS A  115    CYS A  135                          1555   1555  2.03  
SSBOND   3 CYS A  151    CYS A  164                          1555   1555  2.04  
SSBOND   4 CYS B    7    CYS B   25                          1555   1555  2.03  
SSBOND   5 CYS B   15    CYS B  444                          1555   1555  2.03  
SSBOND   6 CYS B   18    CYS B   44                          1555   1555  2.03  
SSBOND   7 CYS B   28    CYS B   55                          1555   1555  2.03  
SSBOND   8 CYS B  187    CYS B  193                          1555   1555  2.03  
SSBOND   9 CYS B  241    CYS B  281                          1555   1555  2.03  
SSBOND  10 CYS B  381    CYS B  395                          1555   1555  2.04  
SSBOND  11 CYS B  415    CYS B  442                          1555   1555  2.03  
SSBOND  12 CYS C    2    CYS C    8                          1555   1555  2.03  
LINK         ND2 ASN A 141                 C1  NAG A 522     1555   1555  1.44  
LINK         OE1 GLU A 239                CA    CA A 501     1555   1555  2.46  
LINK         OE2 GLU A 239                CA    CA A 501     1555   1555  2.43  
LINK         OG  SER A 241                CA    CA A 501     1555   1555  2.38  
LINK         OD1 ASP A 243                CA    CA A 501     1555   1555  2.35  
LINK         O   THR A 245                CA    CA A 501     1555   1555  2.31  
LINK         OD1 ASP A 247                CA    CA A 501     1555   1555  2.34  
LINK         OD2 ASP A 247                CA    CA A 501     1555   1555  2.47  
LINK         ND2 ASN A 256                 C1  NAG A 511     1555   1555  1.45  
LINK         ND2 ASN A 266                 C1  NAG A 519     1555   1555  1.29  
LINK         ND2 ASN A 275                 C1  NAG A 505     1555   1555  1.44  
LINK         OD1 ASP A 293                CA    CA A 502     1555   1555  2.40  
LINK         OD1 ASN A 295                CA    CA A 502     1555   1555  2.33  
LINK         OD1 ASP A 297                CA    CA A 502     1555   1555  2.39  
LINK         O   LEU A 299                CA    CA A 502     1555   1555  2.41  
LINK         OD1 ASP A 301                CA    CA A 502     1555   1555  2.44  
LINK         OD2 ASP A 301                CA    CA A 502     1555   1555  2.43  
LINK         OD1 ASP A 360                CA    CA A 503     1555   1555  2.38  
LINK         OD1 ASP A 362                CA    CA A 503     1555   1555  2.34  
LINK         OD1 ASP A 364                CA    CA A 503     1555   1555  2.38  
LINK         O   TYR A 366                CA    CA A 503     1555   1555  2.29  
LINK         OD1 ASP A 368                CA    CA A 503     1555   1555  2.43  
LINK         OD2 ASP A 368                CA    CA A 503     1555   1555  2.38  
LINK         OD1 ASP A 424                CA    CA A 504     1555   1555  2.33  
LINK         OD1 ASP A 426                CA    CA A 504     1555   1555  2.34  
LINK         OD1 ASN A 428                CA    CA A 504     1555   1555  2.40  
LINK         O   TYR A 430                CA    CA A 504     1555   1555  2.29  
LINK         OD1 ASP A 432                CA    CA A 504     1555   1555  2.37  
LINK         OD2 ASP A 432                CA    CA A 504     1555   1555  2.45  
LINK         OG  SER B 132                MG    MG B 501     1555   1555  2.07  
LINK         O   SER B 134                CA    CA B 502     1555   1555  2.41  
LINK         OG  SER B 134                MG    MG B 501     1555   1555  2.14  
LINK         OD1 ASP B 137                CA    CA B 502     1555   1555  2.40  
LINK         OD1 ASP B 138                CA    CA B 502     1555   1555  2.37  
LINK         OE1 GLU B 169                CA    CA B 503     1555   1555  2.38  
LINK         OD1 ASN B 224                CA    CA B 503     1555   1555  2.29  
LINK         O   ASP B 226                CA    CA B 503     1555   1555  2.45  
LINK         OD1 ASP B 226                CA    CA B 503     1555   1555  2.26  
LINK         O   PRO B 228                CA    CA B 503     1555   1555  2.36  
LINK         OE1 GLU B 229                MG    MG B 501     1555   1555  2.13  
LINK         OE2 GLU B 229                CA    CA B 503     1555   1555  2.37  
LINK         ND2 ASN B 249                 C1  NAG B 504     1555   1555  1.44  
LINK         ND2 ASN B 343                 C1  NAG B 510     1555   1555  1.44  
LINK         ND2 ASN B 397                 C1  NAG B 509     1555   1555  1.44  
LINK         OD1 ASP C   5                MG    MG B 501     1555   1555  2.04  
LINK        CA    CA A 501                 O   HOH A 606     1555   1555  2.30  
LINK        CA    CA A 502                 O   HOH A 632     1555   1555  2.41  
LINK        CA    CA A 503                 O   HOH A 618     1555   1555  2.46  
LINK        CA    CA A 504                 O   HOH A 633     1555   1555  2.41  
LINK         O4  NAG A 505                 C1  NAG A 506     1555   1555  1.44  
LINK         O4  NAG A 506                 C1  BMA A 507     1555   1555  1.44  
LINK         O3  BMA A 507                 C1  MAN A 508     1555   1555  1.44  
LINK         O6  BMA A 507                 C1  MAN A 509     1555   1555  1.44  
LINK         O3  MAN A 509                 C1  MAN A 510     1555   1555  1.44  
LINK         O4  NAG A 511                 C1  NAG A 512     1555   1555  1.44  
LINK         O4  NAG A 512                 C1  BMA A 513     1555   1555  1.45  
LINK         O3  BMA A 513                 C1  MAN A 514     1555   1555  1.45  
LINK         O4  NAG A 515                 C1  NAG A 516     1555   1555  1.44  
LINK         O4  NAG A 516                 C1  BMA A 517     1555   1555  1.44  
LINK         O3  BMA A 517                 C1  MAN A 518     1555   1555  1.44  
LINK         O4  NAG A 519                 C1  NAG A 520     1555   1555  1.44  
LINK         O4  NAG A 520                 C1  BMA A 521     1555   1555  1.44  
LINK         O4  NAG A 522                 C1  NAG A 523     1555   1555  1.44  
LINK         O4  NAG A 523                 C1  BMA A 524     1555   1555  1.44  
LINK         O3  BMA A 524                 C1  MAN A 525     1555   1555  1.44  
LINK         O6  BMA A 524                 C1  MAN A 526     1555   1555  1.44  
LINK         O3  MAN A 526                 C1  MAN A 527     1555   1555  1.44  
LINK         O6  MAN A 526                 C1  MAN A 528     1555   1555  1.44  
LINK        MG    MG B 501                 O   HOH B 623     1555   1555  2.07  
LINK        MG    MG B 501                 O   HOH B 617     1555   1555  2.08  
LINK        CA    CA B 502                 O   HOH B 622     1555   1555  2.88  
LINK         O4  NAG B 504                 C1  NAG B 505     1555   1555  1.44  
LINK         O4  NAG B 505                 C1  BMA B 506     1555   1555  1.45  
LINK         O4  NAG B 507                 C1  NAG B 508     1555   1555  1.44  
CISPEP   1 SER A   63    PRO A   64          0        -8.48                     
CISPEP   2 GLN B   95    PRO B   96          0        -0.59                     
CISPEP   3 MET B  173    PRO B  174          0         1.91                     
SITE     1 AC1  6 GLU A 239  SER A 241  ASP A 243  THR A 245                    
SITE     2 AC1  6 ASP A 247  HOH A 606                                          
SITE     1 AC2  6 ASP A 293  ASN A 295  ASP A 297  LEU A 299                    
SITE     2 AC2  6 ASP A 301  HOH A 632                                          
SITE     1 AC3  6 ASP A 360  ASP A 362  ASP A 364  TYR A 366                    
SITE     2 AC3  6 ASP A 368  HOH A 618                                          
SITE     1 AC4  6 ASP A 424  ASP A 426  ASN A 428  TYR A 430                    
SITE     2 AC4  6 ASP A 432  HOH A 633                                          
SITE     1 AC5  6 SER B 132  SER B 134  GLU B 229  HOH B 617                    
SITE     2 AC5  6 HOH B 623  ASP C   5                                          
SITE     1 AC6  5 SER B 134  MET B 135  ASP B 137  ASP B 138                    
SITE     2 AC6  5 HOH B 622                                                     
SITE     1 AC7  5 GLU B 169  ASN B 224  ASP B 226  PRO B 228                    
SITE     2 AC7  5 GLU B 229                                                     
SITE     1 AC8  3 ASN B  30  SER B  31  ASP B  59                               
SITE     1 AC9 13 ASN A 141  PHE A 142  SER A 272  LEU A 273                    
SITE     2 AC9 13 TYR A 274  ALA A 332  NAG A 505  NAG A 506                    
SITE     3 AC9 13 NAG A 519  NAG A 520  HOH A 601  HOH A 604                    
SITE     4 AC9 13 LYS B  85                                                     
SITE     1 AD1  5 ASN A 256  SER A 277  GLY A 278  HOH A 667                    
SITE     2 AD1  5 LYS B 208                                                     
SITE     1 AD2  7 ASN A 266  SER A 268  ASP A 269  LEU A 273                    
SITE     2 AD2  7 MAN A 525  HOH A 620  HOH A 631                               
SITE     1 AD3 13 ARG A 220  ALA A 222  SER A 223  TYR A 226                    
SITE     2 AD3 13 TYR A 261  SER A 272  LEU A 273  ASN A 275                    
SITE     3 AD3 13 MAN A 526  MAN A 527  HOH A 603  HOH A 614                    
SITE     4 AD3 13 HOH A 700                                                     
SITE     1 AD4  2 ASN B 249  THR B 431                                          
SITE     1 AD5  2 ASN B 141  ASN B 343                                          
SITE     1 AD6  3 LYS B 382  ASN B 383  ASN B 397                               
SITE     1 AD7  6 PRO A  15  GLY A  16  ASN A  43  LEU A  50                    
SITE     2 AD7  6 GLN A  51  THR B 339                                          
SITE     1 AD8  7 NAG A 506  MAN A 509  NAG A 515  HOH A 700                    
SITE     2 AD8  7 THR B 339  GLY B 384  ASN B 386                               
CRYST1   57.520  112.160  169.540  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017385  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008916  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005898        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system