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Database: PDB
Entry: 4WK0
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Original site: 4WK0 
HEADER    CELL ADHESION/IMMUNE SYSTEM             01-OCT-14   4WK0              
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 42-493;                                       
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 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INTEGRIN BETA-1;                                           
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 21-465;                                       
COMPND  13 SYNONYM: FIBRONECTIN RECEPTOR SUBUNIT BETA,GLYCOPROTEIN IIA,GPIIA,   
COMPND  14 VLA-4 SUBUNIT BETA;                                                  
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: ARG-GLY-ASP;                                               
COMPND  18 CHAIN: C;                                                            
COMPND  19 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 4WK0    1       COMPND SOURCE JRNL   REMARK              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   24-DEC-14 4WK0    1       JRNL                                     
REVDAT   2   17-DEC-14 4WK0    1       JRNL                                     
REVDAT   1   03-DEC-14 4WK0    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.    1.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1760)                     
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) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 113319                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.760                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1997                            
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 47.9567 -  4.2892    0.94     7997   143  0.1343 0.1602        
REMARK   3     2  4.2892 -  3.4048    0.95     7796   139  0.1253 0.1721        
REMARK   3     3  3.4048 -  2.9745    0.96     7864   142  0.1560 0.2068        
REMARK   3     4  2.9745 -  2.7025    0.98     7932   141  0.1701 0.1768        
REMARK   3     5  2.7025 -  2.5088    0.98     7960   144  0.1831 0.2115        
REMARK   3     6  2.5088 -  2.3609    0.99     7953   142  0.1946 0.2459        
REMARK   3     7  2.3609 -  2.2427    0.99     7971   143  0.2114 0.2350        
REMARK   3     8  2.2427 -  2.1451    0.99     8009   144  0.2291 0.2408        
REMARK   3     9  2.1451 -  2.0625    1.00     7979   143  0.2569 0.2953        
REMARK   3    10  2.0625 -  1.9913    1.00     7976   144  0.2931 0.3409        
REMARK   3    11  1.9913 -  1.9290    1.00     8019   143  0.3185 0.3635        
REMARK   3    12  1.9290 -  1.8739    0.99     7947   143  0.3531 0.4075        
REMARK   3    13  1.8739 -  1.8246    1.00     7985   143  0.3863 0.4281        
REMARK   3    14  1.8246 -  1.7800    1.00     7934   143  0.4321 0.4821        
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)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.29                          
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      :  0.007           7156                                  
REMARK   3   ANGLE     :  1.086           9724                                  
REMARK   3   CHIRALITY :  0.042           1104                                  
REMARK   3   PLANARITY :  0.005           1260                                  
REMARK   3   DIHEDRAL  : 14.076           2608                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 39 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4467 -17.8950 -25.7064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2225 T22:   0.2824                                     
REMARK   3      T33:   0.2854 T12:  -0.0714                                     
REMARK   3      T13:   0.0562 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1684 L22:   4.3078                                     
REMARK   3      L33:   3.3718 L12:  -1.5715                                     
REMARK   3      L13:  -0.5962 L23:   1.4612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0195 S12:  -0.0658 S13:  -0.1738                       
REMARK   3      S21:   0.2885 S22:  -0.0987 S23:   0.5068                       
REMARK   3      S31:   0.3591 S32:  -0.5081 S33:   0.0211                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 116 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9882  -0.7445 -14.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3383 T22:   0.3544                                     
REMARK   3      T33:   0.3629 T12:   0.0502                                     
REMARK   3      T13:   0.1581 T23:  -0.0432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7511 L22:   2.6631                                     
REMARK   3      L33:   1.9090 L12:  -0.0221                                     
REMARK   3      L13:   0.3252 L23:   0.0915                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1351 S12:  -0.2066 S13:   0.2576                       
REMARK   3      S21:   0.4623 S22:  -0.1474 S23:   0.5933                       
REMARK   3      S31:  -0.3547 S32:  -0.3931 S33:   0.1606                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 177 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9067  -0.9661 -10.7288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4117 T22:   0.3047                                     
REMARK   3      T33:   0.2099 T12:  -0.0057                                     
REMARK   3      T13:   0.0630 T23:  -0.0433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2705 L22:   2.6098                                     
REMARK   3      L33:   1.6482 L12:   0.2510                                     
REMARK   3      L13:  -0.1997 L23:  -0.3296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0821 S12:  -0.2396 S13:   0.1542                       
REMARK   3      S21:   0.6567 S22:  -0.0830 S23:   0.2551                       
REMARK   3      S31:  -0.2420 S32:  -0.1038 S33:   0.0303                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 246 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0344  -6.1114 -11.0187              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2819 T22:   0.3059                                     
REMARK   3      T33:   0.1883 T12:  -0.0095                                     
REMARK   3      T13:  -0.0246 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1811 L22:   2.0957                                     
REMARK   3      L33:   2.9465 L12:   0.5072                                     
REMARK   3      L13:  -0.7813 L23:  -0.3212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0769 S12:  -0.3110 S13:   0.0465                       
REMARK   3      S21:   0.5330 S22:  -0.1006 S23:  -0.0153                       
REMARK   3      S31:  -0.1962 S32:   0.0645 S33:   0.0226                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 247 THROUGH 271 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7763 -10.2911 -20.4335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2863 T22:   0.2545                                     
REMARK   3      T33:   0.2561 T12:   0.0042                                     
REMARK   3      T13:  -0.0116 T23:  -0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4988 L22:   4.8130                                     
REMARK   3      L33:   4.6994 L12:   2.4313                                     
REMARK   3      L13:  -3.0904 L23:  -4.6625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1174 S12:  -0.1449 S13:   0.0830                       
REMARK   3      S21:   0.6279 S22:  -0.0355 S23:  -0.3170                       
REMARK   3      S31:  -0.3772 S32:   0.0835 S33:   0.4018                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 272 THROUGH 312 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0289 -15.4977 -29.8441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1556 T22:   0.2080                                     
REMARK   3      T33:   0.1861 T12:   0.0363                                     
REMARK   3      T13:   0.0442 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2442 L22:   4.4138                                     
REMARK   3      L33:   1.6249 L12:  -0.7837                                     
REMARK   3      L13:   0.7062 L23:  -1.1186                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0278 S12:   0.0380 S13:  -0.1305                       
REMARK   3      S21:  -0.1824 S22:  -0.0242 S23:  -0.0202                       
REMARK   3      S31:   0.1448 S32:   0.1007 S33:   0.0947                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 313 THROUGH 350 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0072 -16.5900 -37.7300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2177 T22:   0.2049                                     
REMARK   3      T33:   0.2091 T12:   0.0153                                     
REMARK   3      T13:   0.0313 T23:  -0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2629 L22:   3.7179                                     
REMARK   3      L33:   4.2929 L12:  -1.0755                                     
REMARK   3      L13:   0.8586 L23:  -2.7775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:   0.2056 S13:  -0.0511                       
REMARK   3      S21:  -0.2974 S22:  -0.1473 S23:  -0.1503                       
REMARK   3      S31:   0.2182 S32:   0.3396 S33:   0.1419                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 351 THROUGH 397 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5569 -22.8424 -35.0249              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2165 T22:   0.2273                                     
REMARK   3      T33:   0.2049 T12:  -0.0148                                     
REMARK   3      T13:   0.0483 T23:  -0.0354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3281 L22:   3.2763                                     
REMARK   3      L33:   4.2724 L12:  -1.1832                                     
REMARK   3      L13:   1.6807 L23:  -3.1093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0324 S12:   0.1471 S13:  -0.1327                       
REMARK   3      S21:  -0.1292 S22:  -0.0884 S23:  -0.0813                       
REMARK   3      S31:   0.2324 S32:  -0.0185 S33:   0.0143                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 398 THROUGH 431 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1637 -19.1375 -33.5862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2015 T22:   0.2506                                     
REMARK   3      T33:   0.2343 T12:  -0.0407                                     
REMARK   3      T13:  -0.0060 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3052 L22:   2.7283                                     
REMARK   3      L33:   5.0358 L12:   0.9550                                     
REMARK   3      L13:  -0.7477 L23:  -1.9135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0535 S12:   0.0722 S13:  -0.0410                       
REMARK   3      S21:  -0.0022 S22:   0.1209 S23:   0.3560                       
REMARK   3      S31:   0.1809 S32:  -0.2204 S33:  -0.2119                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 432 THROUGH 452 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7853 -21.1958 -31.7362              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1895 T22:   0.2545                                     
REMARK   3      T33:   0.2971 T12:  -0.0517                                     
REMARK   3      T13:   0.0015 T23:  -0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5032 L22:   2.2365                                     
REMARK   3      L33:   1.8830 L12:  -1.6906                                     
REMARK   3      L13:  -0.4839 L23:  -0.2230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0140 S12:   0.1089 S13:  -0.1696                       
REMARK   3      S21:  -0.0055 S22:  -0.0266 S23:   0.4925                       
REMARK   3      S31:   0.1862 S32:  -0.2442 S33:  -0.0081                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 53 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7038 -36.2657 -77.4267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3406 T22:   0.7271                                     
REMARK   3      T33:   1.4014 T12:  -0.1372                                     
REMARK   3      T13:  -0.0294 T23:  -0.3234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1494 L22:   9.4241                                     
REMARK   3      L33:   7.5986 L12:  -1.5342                                     
REMARK   3      L13:  -1.4303 L23:   3.7792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3905 S12:   0.8897 S13:  -1.8979                       
REMARK   3      S21:  -0.7063 S22:   0.2031 S23:  -1.0672                       
REMARK   3      S31:   1.1902 S32:   0.0921 S33:  -0.5141                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 54 THROUGH 132 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4576  -1.1176 -69.2728              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4138 T22:   0.3816                                     
REMARK   3      T33:   0.2664 T12:  -0.0618                                     
REMARK   3      T13:  -0.0255 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1209 L22:   4.0096                                     
REMARK   3      L33:   4.4800 L12:   0.1688                                     
REMARK   3      L13:  -0.6096 L23:   2.7157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1800 S12:   0.3715 S13:  -0.1828                       
REMARK   3      S21:  -0.6647 S22:   0.2224 S23:  -0.0773                       
REMARK   3      S31:   0.2497 S32:  -0.0206 S33:  -0.0887                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 133 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2272  22.0783 -35.5877              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3564 T22:   0.2172                                     
REMARK   3      T33:   0.3383 T12:  -0.0266                                     
REMARK   3      T13:   0.0310 T23:  -0.0480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9637 L22:   1.6956                                     
REMARK   3      L33:   3.9345 L12:   0.8175                                     
REMARK   3      L13:  -2.6238 L23:  -1.1363                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3630 S12:  -0.2881 S13:   0.5438                       
REMARK   3      S21:   0.4490 S22:  -0.0100 S23:   0.1136                       
REMARK   3      S31:  -0.6685 S32:   0.3051 S33:  -0.3729                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 200 THROUGH 346 OR RESID 449)     
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9172  12.1107 -41.2470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2631 T22:   0.2374                                     
REMARK   3      T33:   0.2586 T12:   0.0009                                     
REMARK   3      T13:   0.0026 T23:   0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9339 L22:   1.0072                                     
REMARK   3      L33:   1.4597 L12:   0.1116                                     
REMARK   3      L13:  -0.7137 L23:  -0.7784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0646 S12:   0.0281 S13:   0.1790                       
REMARK   3      S21:   0.1278 S22:   0.0187 S23:   0.0141                       
REMARK   3      S31:  -0.1884 S32:  -0.0035 S33:  -0.0832                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 347 THROUGH 380 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6984   1.4407 -56.1943              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2474 T22:   0.2422                                     
REMARK   3      T33:   0.2361 T12:   0.0071                                     
REMARK   3      T13:  -0.0087 T23:   0.0614                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3563 L22:   7.6272                                     
REMARK   3      L33:   6.2260 L12:   1.8563                                     
REMARK   3      L13:   1.2170 L23:   5.7258                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1389 S12:  -0.0073 S13:  -0.1967                       
REMARK   3      S21:   0.1799 S22:   0.0831 S23:  -0.5130                       
REMARK   3      S31:   0.4330 S32:   0.1062 S33:  -0.2532                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 381 THROUGH 420 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0761  -6.2061 -63.4755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3974 T22:   0.3194                                     
REMARK   3      T33:   0.3473 T12:   0.0692                                     
REMARK   3      T13:  -0.0219 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1451 L22:   3.8667                                     
REMARK   3      L33:   5.8437 L12:   4.3923                                     
REMARK   3      L13:   1.7181 L23:   2.1351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4022 S12:   0.0726 S13:  -0.5245                       
REMARK   3      S21:   0.3204 S22:  -0.0080 S23:  -0.5476                       
REMARK   3      S31:   0.8100 S32:   0.1783 S33:  -0.4055                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 444 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0624  -6.4100 -67.6637              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4981 T22:   0.3586                                     
REMARK   3      T33:   0.2760 T12:  -0.1235                                     
REMARK   3      T13:  -0.0303 T23:   0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4002 L22:   4.2935                                     
REMARK   3      L33:   8.7759 L12:   3.0346                                     
REMARK   3      L13:   3.4732 L23:   6.0382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1157 S12:   0.1310 S13:  -0.3410                       
REMARK   3      S21:   0.2840 S22:   0.0557 S23:   0.2190                       
REMARK   3      S31:   0.7214 S32:  -0.5000 S33:   0.0439                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1524 THROUGH 1526 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  21.8584  12.3444 -21.3407              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8163 T22:   0.6295                                     
REMARK   3      T33:   0.5055 T12:   0.1048                                     
REMARK   3      T13:  -0.0417 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3381 L22:   3.5638                                     
REMARK   3      L33:   2.0006 L12:  -3.4017                                     
REMARK   3      L13:   4.3575 L23:   0.4055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0011 S12:  -1.1906 S13:   0.7321                       
REMARK   3      S21:   4.4022 S22:   1.1614 S23:  -1.1156                       
REMARK   3      S31:  -2.5987 S32:  -0.5738 S33:  -0.0075                       
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 4WK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203934.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-13                          
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   : 113328                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
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   (%): 59.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
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       30.53000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       83.54500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.53500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       83.54500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.53000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.53500            
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: 8650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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     SER A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     THR A    65                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLN B    35                                                      
REMARK 465     GLU B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     MET B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     SER B    79                                                      
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    85                                                      
REMARK 465     GLU B   445                                                      
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   397     C1   NAG B   508              0.45            
REMARK 500  HD21  ASN B   397     H1   NAG B   508              1.03            
REMARK 500  HD22  ASN B    30     OG1  THR B    32              1.14            
REMARK 500  HD21  ASN A   256     O    HOH A   721              1.53            
REMARK 500   O    LEU A   257     HG1  THR A   258              1.58            
REMARK 500   ND2  ASN B    30     OG1  THR B    32              1.62            
REMARK 500   O    HOH A   733     O    HOH A   755              2.04            
REMARK 500   O    HOH B   712     O    HOH B   745              2.08            
REMARK 500   O    HOH A   827     O    HOH A   940              2.08            
REMARK 500   O    HOH B   786     O    HOH B   811              2.08            
REMARK 500   O    HOH A   659     O    HOH A   695              2.10            
REMARK 500   O    HOH A   770     O    HOH A   871              2.10            
REMARK 500   O    HOH A   688     O    HOH B   673              2.13            
REMARK 500   O    HOH B   789     O    HOH B   805              2.13            
REMARK 500   O    HOH A   800     O    HOH A   899              2.13            
REMARK 500   O    HOH B   658     O    HOH B   689              2.13            
REMARK 500   O    HOH B   712     O    HOH B   746              2.14            
REMARK 500   O    HOH A   718     O    HOH A   777              2.14            
REMARK 500   O    HOH A   733     O    HOH A   787              2.15            
REMARK 500   O    HOH A   778     O    HOH A   822              2.16            
REMARK 500   O    HOH A   800     O    HOH A   911              2.16            
REMARK 500   O    HOH A   777     O    HOH A   839              2.17            
REMARK 500   O    HOH B   617     O    HOH B   631              2.17            
REMARK 500   O    HOH B   603     O    HOH B   630              2.18            
REMARK 500   O    HOH A   909     O    HOH A   940              2.19            
REMARK 500   O    HOH A   761     O    HOH B   797              2.19            
REMARK 500   O    HOH A   821     O    HOH A   903              2.19            
REMARK 500   O    HOH A   659     O    HOH A   777              2.19            
REMARK 500   O    HOH B   729     O    HOH B   787              2.19            
REMARK 500   ND2  ASN B   343     O5   NAG B   509              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    ALA A   7       62.92   -153.79                                   
REMARK 500    THR A  30      -38.01   -145.66                                   
REMARK 500    SER A  85      -22.15   -161.28                                   
REMARK 500    THR A 123      165.35     64.48                                   
REMARK 500    LYS A 125     -117.44   -111.78                                   
REMARK 500    TRP A 157      175.83     69.14                                   
REMARK 500    ASP A 243     -157.09   -124.34                                   
REMARK 500    ILE A 270       16.81     57.99                                   
REMARK 500    PHE B  33       50.62    -98.31                                   
REMARK 500    ASN B  72       58.47   -154.67                                   
REMARK 500    VAL B 168      -78.15   -133.52                                   
REMARK 500    THR B 171       52.80    -91.16                                   
REMARK 500    CYS B 187     -165.07   -105.96                                   
REMARK 500    ASN B 192       49.51   -101.36                                   
REMARK 500    SER B 222     -154.49   -124.80                                   
REMARK 500    ASN B 224     -165.38   -163.21                                   
REMARK 500    CYS B 381     -169.26   -111.33                                   
REMARK 500    LYS B 414     -154.65   -135.29                                   
REMARK 500    LYS B 417      169.71     63.40                                   
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 A 842        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A 941        DISTANCE =  6.24 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                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 239   OE1                                                    
REMARK 620 2 GLU A 239   OE2  51.7                                              
REMARK 620 3 SER A 241   OG  126.9  75.2                                        
REMARK 620 4 ASP A 243   OD1  81.2  76.9  87.8                                  
REMARK 620 5 THR A 245   O    68.6 119.9 163.1  88.5                            
REMARK 620 6 ASP A 247   OD1 120.0 126.2  89.1 154.8  87.3                      
REMARK 620 7 ASP A 247   OD2  79.6  77.0  89.4 153.6 101.1  51.3                
REMARK 620 8 HOH A 636   O   144.1 148.7  82.7  80.3  80.4  74.4 125.3          
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  75.9                                              
REMARK 620 3 ASP A 297   OD1  78.0  84.2                                        
REMARK 620 4 LEU A 299   O    85.6 161.5  92.2                                  
REMARK 620 5 ASP A 301   OD1 133.2 114.6 145.2  78.0                            
REMARK 620 6 ASP A 301   OD2  86.5  86.6 163.5  92.2  51.3                      
REMARK 620 7 HOH A 604   O   152.6  83.8  81.9 113.8  72.1 110.6                
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  83.5                                              
REMARK 620 3 ASP A 364   OD1  78.3  95.3                                        
REMARK 620 4 TYR A 366   O    77.8 160.8  85.2                                  
REMARK 620 5 ASP A 368   OD1 133.4 110.1 139.9  80.4                            
REMARK 620 6 ASP A 368   OD2  90.4  84.6 168.6  91.2  49.3                      
REMARK 620 7 HOH A 634   O   150.6 101.9  72.4  96.5  72.3 118.8                
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  74.9                                              
REMARK 620 3 ASN A 428   OD1  86.6  85.6                                        
REMARK 620 4 TYR A 430   O    82.7 156.0  84.6                                  
REMARK 620 5 ASP A 432   OD1 129.1 118.1 139.7  82.8                            
REMARK 620 6 ASP A 432   OD2  84.7  87.6 170.1  98.9  50.2                      
REMARK 620 7 HOH A 635   O   154.5  81.4  82.2 118.7  70.9 103.9                
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 GLU B 229   OE1  92.1                                              
REMARK 620 3 ASP C1526   OD1  85.3  93.2                                        
REMARK 620 4 HOH B 634   O    83.3  98.9 163.7                                  
REMARK 620 5 HOH B 633   O   176.2  84.8  97.0  94.9                            
REMARK 620 6 HOH B 637   O    92.1 164.4  72.2  96.5  91.4                      
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  77.2                                              
REMARK 620 3 ASP B 137   OD2 121.2  48.7                                        
REMARK 620 4 ASP B 138   OD1  92.0  82.5 100.7                                  
REMARK 620 5 ALA B 342   O   171.0 111.6  67.6  87.7                            
REMARK 620 6 HOH B 632   O    84.2 158.4 152.6  87.3  86.8                      
REMARK 620 7 HOH B 638   O    83.0  97.2  82.7 175.0  97.1  91.4                
REMARK 620 N                    1     2     3     4     5     6                 
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  95.4                                              
REMARK 620 3 ASP B 226   O   160.5  91.8                                        
REMARK 620 4 ASP B 226   OD1  86.4  98.5  74.6                                  
REMARK 620 5 PRO B 228   O    84.0 171.1  91.7  90.3                            
REMARK 620 6 GLU B 229   OE2  97.7  83.6 101.1 175.2  87.7                      
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 Poly-Saccharide residues NAG A    
REMARK 800  512 through NAG A 513 bound to ASN A 43                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 516 bound   
REMARK 800  to ASN A 141                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 511 bound   
REMARK 800  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  514 through NAG A 515 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 NAG B 505 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 509 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 Poly-Saccharide residues NAG B    
REMARK 800  506 through NAG B 507 bound to ASN B 386                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 508 bound   
REMARK 800  to ASN B 397                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WJK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WK2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WK4   RELATED DB: PDB                                   
DBREF  4WK0 A    1   452  UNP    P08648   ITA5_HUMAN      42    493             
DBREF  4WK0 B    1   445  UNP    P05556   ITB1_HUMAN      21    465             
DBREF  4WK0 C 1524  1526  PDB    4WK0     4WK0          1524   1526             
SEQADV 4WK0 VAL A  451  UNP  P08648    ILE   492 ENGINEERED MUTATION            
SEQADV 4WK0 THR B  195  UNP  P05556    SER   215 CONFLICT                       
SEQRES   1 A  452  PHE ASN LEU ASP ALA GLU ALA PRO ALA VAL LEU SER GLY          
SEQRES   2 A  452  PRO PRO GLY SER PHE PHE GLY PHE SER VAL GLU PHE TYR          
SEQRES   3 A  452  ARG PRO GLY THR ASP GLY VAL SER VAL LEU VAL GLY ALA          
SEQRES   4 A  452  PRO LYS ALA ASN THR SER GLN PRO GLY VAL LEU GLN GLY          
SEQRES   5 A  452  GLY ALA VAL TYR LEU CYS PRO TRP GLY ALA SER PRO THR          
SEQRES   6 A  452  GLN CYS THR PRO ILE GLU PHE ASP SER LYS GLY SER ARG          
SEQRES   7 A  452  LEU LEU GLU SER SER LEU SER SER SER GLU GLY GLU GLU          
SEQRES   8 A  452  PRO VAL GLU TYR LYS SER LEU GLN TRP PHE GLY ALA THR          
SEQRES   9 A  452  VAL ARG ALA HIS GLY SER SER ILE LEU ALA CYS ALA PRO          
SEQRES  10 A  452  LEU TYR SER TRP ARG THR GLU LYS GLU PRO LEU SER ASP          
SEQRES  11 A  452  PRO VAL GLY THR CYS TYR LEU SER THR ASP ASN PHE THR          
SEQRES  12 A  452  ARG ILE LEU GLU TYR ALA PRO CYS ARG SER ASP PHE SER          
SEQRES  13 A  452  TRP ALA ALA GLY GLN GLY TYR CYS GLN GLY GLY PHE SER          
SEQRES  14 A  452  ALA GLU PHE THR LYS THR GLY ARG VAL VAL LEU GLY GLY          
SEQRES  15 A  452  PRO GLY SER TYR PHE TRP GLN GLY GLN ILE LEU SER ALA          
SEQRES  16 A  452  THR GLN GLU GLN ILE ALA GLU SER TYR TYR PRO GLU TYR          
SEQRES  17 A  452  LEU ILE ASN LEU VAL GLN GLY GLN LEU GLN THR ARG GLN          
SEQRES  18 A  452  ALA SER SER ILE TYR ASP ASP SER TYR LEU GLY TYR SER          
SEQRES  19 A  452  VAL ALA VAL GLY GLU PHE SER GLY ASP ASP THR GLU ASP          
SEQRES  20 A  452  PHE VAL ALA GLY VAL PRO LYS GLY ASN LEU THR TYR GLY          
SEQRES  21 A  452  TYR VAL THR ILE LEU ASN GLY SER ASP ILE ARG SER LEU          
SEQRES  22 A  452  TYR ASN PHE SER GLY GLU GLN MET ALA SER TYR PHE GLY          
SEQRES  23 A  452  TYR ALA VAL ALA ALA THR ASP VAL ASN GLY ASP GLY LEU          
SEQRES  24 A  452  ASP ASP LEU LEU VAL GLY ALA PRO LEU LEU MET ASP ARG          
SEQRES  25 A  452  THR PRO ASP GLY ARG PRO GLN GLU VAL GLY ARG VAL TYR          
SEQRES  26 A  452  VAL TYR LEU GLN HIS PRO ALA GLY ILE GLU PRO THR PRO          
SEQRES  27 A  452  THR LEU THR LEU THR GLY HIS ASP GLU PHE GLY ARG PHE          
SEQRES  28 A  452  GLY SER SER LEU THR PRO LEU GLY ASP LEU ASP GLN ASP          
SEQRES  29 A  452  GLY TYR ASN ASP VAL ALA ILE GLY ALA PRO PHE GLY GLY          
SEQRES  30 A  452  GLU THR GLN GLN GLY VAL VAL PHE VAL PHE PRO GLY GLY          
SEQRES  31 A  452  PRO GLY GLY LEU GLY SER LYS PRO SER GLN VAL LEU GLN          
SEQRES  32 A  452  PRO LEU TRP ALA ALA SER HIS THR PRO ASP PHE PHE GLY          
SEQRES  33 A  452  SER ALA LEU ARG GLY GLY ARG ASP LEU ASP GLY ASN GLY          
SEQRES  34 A  452  TYR PRO ASP LEU ILE VAL GLY SER PHE GLY VAL ASP LYS          
SEQRES  35 A  452  ALA VAL VAL TYR ARG GLY ARG PRO VAL VAL                      
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    3  ARG GLY ASP                                                  
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      28                                                       
HET    NAG  A 512      26                                                       
HET    NAG  A 513      28                                                       
HET    NAG  A 514      27                                                       
HET    NAG  A 515      28                                                       
HET    NAG  A 516      28                                                       
HET     MG  B 501       1                                                       
HET     CA  B 502       1                                                       
HET     CA  B 503       1                                                       
HET    NAG  B 504      27                                                       
HET    NAG  B 505      28                                                       
HET    NAG  B 506      27                                                       
HET    NAG  B 507      28                                                       
HET    NAG  B 508      28                                                       
HET    NAG  B 509      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    14(C8 H15 N O6)                                              
FORMUL   8  BMA    C6 H12 O6                                                    
FORMUL   8  MAN    3(C6 H12 O6)                                                 
FORMUL  13   MG    MG 2+                                                        
FORMUL  20  HOH   *629(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  SER A  203  1                                   8    
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 SER B   14  ALA B   21  1                                   8    
HELIX    7 AA7 THR B   40  ALA B   42  5                                   3    
HELIX    8 AA8 LEU B   47  LYS B   52  1                                   6    
HELIX    9 AA9 LYS B   87  ILE B   91  5                                   5    
HELIX   10 AB1 SER B  132  SER B  134  5                                   3    
HELIX   11 AB2 MET B  135  VAL B  142  1                                   8    
HELIX   12 AB3 SER B  144  ARG B  154  1                                  11    
HELIX   13 AB4 THR B  179  ASN B  185  1                                   7    
HELIX   14 AB5 LYS B  208  GLY B  217  1                                  10    
HELIX   15 AB6 GLY B  230  CYS B  241  1                                  12    
HELIX   16 AB7 GLY B  242  ILE B  245  5                                   4    
HELIX   17 AB8 GLY B  266  GLY B  272  5                                   7    
HELIX   18 AB9 SER B  298  ASN B  309  1                                  12    
HELIX   19 AC1 PHE B  321  ILE B  332  1                                  12    
HELIX   20 AC2 ASN B  346  SER B  360  1                                  15    
HELIX   21 AC3 LYS B  382  GLY B  384  5                                   3    
HELIX   22 AC4 THR B  388  GLY B  392  5                                   5    
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  VAL A 435   O  VAL A 444           
SHEET    4 AA1 4 ALA A 418  ARG A 423 -1  N  ARG A 423   O  ASP A 432           
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  ALA A  54   N  ALA A  39           
SHEET    4 AA2 4 THR A  68  PRO A  69 -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  VAL A 249   N  ALA A 236           
SHEET    3 AA6 4 TYR A 261  LEU A 265 -1  O  LEU A 265   N  PHE A 248           
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  TYR A 327   N  LEU A 302           
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 2 GLN A 329  HIS A 330  0                                        
SHEET    2 AA9 2 GLY A 333  ILE A 334 -1  O  GLY A 333   N  HIS A 330           
SHEET    1 AB1 4 LEU A 355  GLY A 359  0                                        
SHEET    2 AB1 4 ASP A 368  ALA A 373 -1  O  ASP A 368   N  GLY A 359           
SHEET    3 AB1 4 VAL A 383  PHE A 387 -1  O  PHE A 387   N  VAL A 369           
SHEET    4 AB1 4 GLN A 400  LEU A 402 -1  O  LEU A 402   N  VAL A 384           
SHEET    1 AB2 2 CYS B  25  TRP B  27  0                                        
SHEET    2 AB2 2 CYS B  44  ASP B  46 -1  O  ASP B  45   N  GLY B  26           
SHEET    1 AB3 6 SER B  66  LYS B  71  0                                        
SHEET    2 AB3 6 GLN B  98  ARG B 104 -1  O  GLN B  98   N  LYS B  70           
SHEET    3 AB3 6 VAL B 434  ILE B 441  1  O  GLN B 439   N  LEU B 103           
SHEET    4 AB3 6 ASP B 421  PRO B 427 -1  N  ILE B 425   O  VAL B 434           
SHEET    5 AB3 6 VAL B 362  ASN B 366 -1  N  GLU B 365   O  ARG B 426           
SHEET    6 AB3 6 LYS B 394  CYS B 395 -1  O  CYS B 395   N  VAL B 362           
SHEET    1 AB4 5 ILE B  94  GLN B  95  0                                        
SHEET    2 AB4 5 GLN B 109  LYS B 116 -1  O  LYS B 114   N  GLN B  95           
SHEET    3 AB4 5 GLU B 403  SER B 412 -1  O  VAL B 404   N  PHE B 115           
SHEET    4 AB4 5 VAL B 373  TYR B 380 -1  N  THR B 374   O  THR B 411           
SHEET    5 AB4 5 ASN B 386  GLY B 387 -1  O  GLY B 387   N  SER B 379           
SHEET    1 AB5 6 TYR B 199  THR B 206  0                                        
SHEET    2 AB5 6 PHE B 160  PHE B 167 -1  N  ILE B 162   O  THR B 206           
SHEET    3 AB5 6 ILE B 123  ASP B 130  1  N  MET B 129   O  GLY B 165           
SHEET    4 AB5 6 THR B 251  THR B 258  1  O  VAL B 255   N  LEU B 128           
SHEET    5 AB5 6 ILE B 311  VAL B 317  1  O  ILE B 314   N  PHE B 256           
SHEET    6 AB5 6 SER B 335  THR B 339  1  O  ALA B 336   N  PHE B 315           
SHEET    1 AB6 2 LEU B 283  GLU B 284  0                                        
SHEET    2 AB6 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  2.05  
SSBOND   2 CYS A  115    CYS A  135                          1555   1555  2.07  
SSBOND   3 CYS A  151    CYS A  164                          1555   1555  2.06  
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  2.04  
SSBOND   7 CYS B   28    CYS B   55                          1555   1555  2.03  
SSBOND   8 CYS B  187    CYS B  193                          1555   1555  2.04  
SSBOND   9 CYS B  241    CYS B  281                          1555   1555  2.06  
SSBOND  10 CYS B  381    CYS B  395                          1555   1555  2.00  
SSBOND  11 CYS B  415    CYS B  442                          1555   1555  2.03  
LINK         ND2 ASN A  43                 C1  NAG A 512     1555   1555  1.43  
LINK         ND2 ASN A 141                 C1  NAG A 516     1555   1555  1.45  
LINK         OE1 GLU A 239                CA    CA A 501     1555   1555  2.51  
LINK         OE2 GLU A 239                CA    CA A 501     1555   1555  2.50  
LINK         OG  SER A 241                CA    CA A 501     1555   1555  2.23  
LINK         OD1 ASP A 243                CA    CA A 501     1555   1555  2.40  
LINK         O   THR A 245                CA    CA A 501     1555   1555  2.27  
LINK         OD1 ASP A 247                CA    CA A 501     1555   1555  2.54  
LINK         OD2 ASP A 247                CA    CA A 501     1555   1555  2.57  
LINK         ND2 ASN A 256                 C1  NAG A 511     1555   1555  1.38  
LINK         ND2 ASN A 266                 C1  NAG A 514     1555   1555  1.43  
LINK         ND2 ASN A 275                 C1  NAG A 505     1555   1555  1.43  
LINK         OD1 ASP A 293                CA    CA A 502     1555   1555  2.40  
LINK         OD1 ASN A 295                CA    CA A 502     1555   1555  2.30  
LINK         OD1 ASP A 297                CA    CA A 502     1555   1555  2.52  
LINK         O   LEU A 299                CA    CA A 502     1555   1555  2.29  
LINK         OD1 ASP A 301                CA    CA A 502     1555   1555  2.60  
LINK         OD2 ASP A 301                CA    CA A 502     1555   1555  2.50  
LINK         OD1 ASP A 360                CA    CA A 503     1555   1555  2.56  
LINK         OD1 ASP A 362                CA    CA A 503     1555   1555  2.29  
LINK         OD1 ASP A 364                CA    CA A 503     1555   1555  2.57  
LINK         O   TYR A 366                CA    CA A 503     1555   1555  2.38  
LINK         OD1 ASP A 368                CA    CA A 503     1555   1555  2.64  
LINK         OD2 ASP A 368                CA    CA A 503     1555   1555  2.66  
LINK         OD1 ASP A 424                CA    CA A 504     1555   1555  2.36  
LINK         OD1 ASP A 426                CA    CA A 504     1555   1555  2.29  
LINK         OD1 ASN A 428                CA    CA A 504     1555   1555  2.52  
LINK         O   TYR A 430                CA    CA A 504     1555   1555  2.24  
LINK         OD1 ASP A 432                CA    CA A 504     1555   1555  2.62  
LINK         OD2 ASP A 432                CA    CA A 504     1555   1555  2.58  
LINK         OG  SER B 132                MG    MG B 501     1555   1555  2.16  
LINK         O   SER B 134                CA    CA B 502     1555   1555  2.53  
LINK         OD1 ASP B 137                CA    CA B 502     1555   1555  2.36  
LINK         OD2 ASP B 137                CA    CA B 502     1555   1555  2.87  
LINK         OD1 ASP B 138                CA    CA B 502     1555   1555  2.37  
LINK         OE1 GLU B 169                CA    CA B 503     1555   1555  2.40  
LINK         OD1 ASN B 224                CA    CA B 503     1555   1555  2.29  
LINK         O   ASP B 226                CA    CA B 503     1555   1555  2.34  
LINK         OD1 ASP B 226                CA    CA B 503     1555   1555  2.22  
LINK         O   PRO B 228                CA    CA B 503     1555   1555  2.26  
LINK         OE1 GLU B 229                MG    MG B 501     1555   1555  2.03  
LINK         OE2 GLU B 229                CA    CA B 503     1555   1555  2.34  
LINK         ND2 ASN B 249                 C1  NAG B 504     1555   1555  1.43  
LINK         O   ALA B 342                CA    CA B 502     1555   1555  2.47  
LINK         ND2 ASN B 343                 C1  NAG B 509     1555   1555  1.44  
LINK         ND2 ASN B 386                 C1  NAG B 506     1555   1555  1.45  
LINK         ND2 ASN B 397                 C1  NAG B 508     1555   1555  1.39  
LINK         OD1 ASP C1526                MG    MG B 501     1555   1555  2.04  
LINK        CA    CA A 501                 O   HOH A 636     1555   1555  2.43  
LINK        CA    CA A 502                 O   HOH A 604     1555   1555  2.41  
LINK        CA    CA A 503                 O   HOH A 634     1555   1555  2.61  
LINK        CA    CA A 504                 O   HOH A 635     1555   1555  2.49  
LINK         O4  NAG A 505                 C1  NAG A 506     1555   1555  1.42  
LINK         O4  NAG A 506                 C1  BMA A 507     1555   1555  1.43  
LINK         O3  BMA A 507                 C1  MAN A 508     1555   1555  1.45  
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 512                 C1  NAG A 513     1555   1555  1.44  
LINK         O4  NAG A 514                 C1  NAG A 515     1555   1555  1.44  
LINK        MG    MG B 501                 O   HOH B 634     1555   1555  2.08  
LINK        MG    MG B 501                 O   HOH B 633     1555   1555  2.11  
LINK        MG    MG B 501                 O   HOH B 637     1555   1555  2.03  
LINK        CA    CA B 502                 O   HOH B 632     1555   1555  2.46  
LINK        CA    CA B 502                 O   HOH B 638     1555   1555  2.32  
LINK         O4  NAG B 504                 C1  NAG B 505     1555   1555  1.44  
LINK         O4  NAG B 506                 C1  NAG B 507     1555   1555  1.45  
CISPEP   1 GLN B   95    PRO B   96          0        -1.00                     
CISPEP   2 MET B  173    PRO B  174          0         2.40                     
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 636                                          
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 604                                          
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 634                                          
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 635                                          
SITE     1 AC5  6 SER B 132  GLU B 229  HOH B 633  HOH B 634                    
SITE     2 AC5  6 HOH B 637  ASP C1526                                          
SITE     1 AC6  6 SER B 134  ASP B 137  ASP B 138  ALA B 342                    
SITE     2 AC6  6 HOH B 632  HOH B 638                                          
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  6 PRO A  15  GLY A  16  LYS A  41  ASN A  43                    
SITE     2 AC8  6 LEU A  50  GLN A  51                                          
SITE     1 AC9  1 ASN A 141                                                     
SITE     1 AD1  7 ASN A 256  SER A 277  HOH A 721  HOH A 812                    
SITE     2 AD1  7 HOH A 828  HOH A 850  HOH A 955                               
SITE     1 AD2  4 ASN A 266  SER A 268  ASP A 269  HOH A 708                    
SITE     1 AD3 16 ARG A 220  ALA A 222  SER A 223  TYR A 226                    
SITE     2 AD3 16 TYR A 261  SER A 272  LEU A 273  ASN A 275                    
SITE     3 AD3 16 HOH A 732  HOH A 743  HOH A 853  HOH A 861                    
SITE     4 AD3 16 HOH A 868  HOH A 869  HOH A 912  HOH A 930                    
SITE     1 AD4  3 TRP B 247  ASN B 249  THR B 431                               
SITE     1 AD5  3 ASN B 141  ASN B 343  SER B 345                               
SITE     1 AD6  2 GLY B 384  ASN B 386                                          
SITE     1 AD7  3 LYS B 382  ASN B 383  ASN B 397                               
CRYST1   61.060  117.070  167.090  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      0.016377  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008542  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005985        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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