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Database: PDB
Entry: 3F7Q
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Original site: 3F7Q 
HEADER    CELL ADHESION                           10-NOV-08   3F7Q              
TITLE     FIRST PAIR OF FIBRONECTIN TYPE III DOMAINS AND PART OF THE            
TITLE    2 CONNECTING SEGMENT OF THE INTEGRIN BETA4                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN BETA-4;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: FIBRONECTIN TYPE-III, RESIDUES 1126-1355;                  
COMPND   5 SYNONYM: GP150;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGB4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: DERIVATIVE OF PET15B                      
KEYWDS    INTEGRIN, HEMIDESMOSOME, CELL ADHESION, CARCINOMA,                    
KEYWDS   2 EPIDERMOLYSIS BULLOSA, ALTERNATIVE SPLICING, DISEASE                 
KEYWDS   3 MUTATION, GLYCOPROTEIN, MEMBRANE, PHOSPHOPROTEIN,                    
KEYWDS   4 POLYMORPHISM, RECEPTOR, TRANSMEMBRANE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.DE PEREDA                                                         
REVDAT   2   28-APR-09 3F7Q    1       JRNL                                     
REVDAT   1   10-MAR-09 3F7Q    0                                                
JRNL        AUTH   J.M.DE PEREDA,M.P.LILLO,A.SONNENBERG                         
JRNL        TITL   STRUCTURAL BASIS OF THE INTERACTION BETWEEN                  
JRNL        TITL 2 INTEGRIN ALPHA6BETA4 AND PLECTIN AT THE                      
JRNL        TITL 3 HEMIDESMOSOMES                                               
JRNL        REF    EMBO J.                       V.  28  1180 2009              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   19242489                                                     
JRNL        DOI    10.1038/EMBOJ.2009.48                                        
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.870                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 50835                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2589                            
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 22.2735 -  4.5738    0.95     2790   144  0.1547 0.1546        
REMARK   3     2  4.5738 -  3.6355    0.96     2799   154  0.1316 0.1317        
REMARK   3     3  3.6355 -  3.1774    0.95     2777   163  0.1395 0.1633        
REMARK   3     4  3.1774 -  2.8876    0.95     2783   139  0.1434 0.2092        
REMARK   3     5  2.8876 -  2.6810    0.94     2761   159  0.1433 0.1667        
REMARK   3     6  2.6810 -  2.5231    0.94     2713   160  0.1381 0.1502        
REMARK   3     7  2.5231 -  2.3969    0.94     2744   113  0.1327 0.1790        
REMARK   3     8  2.3969 -  2.2927    0.93     2757   150  0.1341 0.1860        
REMARK   3     9  2.2927 -  2.2045    0.90     2660   141  0.1379 0.1619        
REMARK   3    10  2.2045 -  2.1285    0.92     2660   140  0.1392 0.1857        
REMARK   3    11  2.1285 -  2.0620    0.90     2599   137  0.1499 0.1710        
REMARK   3    12  2.0620 -  2.0031    0.91     2711   129  0.1557 0.1856        
REMARK   3    13  2.0031 -  1.9504    0.90     2616   152  0.1643 0.2113        
REMARK   3    14  1.9504 -  1.9028    0.89     2598   139  0.1804 0.2404        
REMARK   3    15  1.9028 -  1.8596    0.90     2638   143  0.1991 0.2617        
REMARK   3    16  1.8596 -  1.8200    0.90     2644   159  0.2048 0.2332        
REMARK   3    17  1.8200 -  1.7836    0.89     2585   135  0.2231 0.2205        
REMARK   3    18  1.7836 -  1.7500    0.82     2411   132  0.2548 0.3079        
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              : 0.43                                          
REMARK   3   B_SOL              : 49.66                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.530           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.43820                                             
REMARK   3    B22 (A**2) : -5.44840                                             
REMARK   3    B33 (A**2) : -8.26380                                             
REMARK   3    B12 (A**2) : 3.80150                                              
REMARK   3    B13 (A**2) : -1.07710                                             
REMARK   3    B23 (A**2) : 1.32350                                              
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           6981                                  
REMARK   3   ANGLE     :  0.878          12628                                  
REMARK   3   CHIRALITY :  0.068            513                                  
REMARK   3   PLANARITY :  0.004           1111                                  
REMARK   3   DIHEDRAL  : 17.145           1804                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1126-1207                           
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2218  -3.8919  43.8523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1365 T22:   0.1649                                     
REMARK   3      T33:   0.1673 T12:  -0.0237                                     
REMARK   3      T13:  -0.0013 T23:  -0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2905 L22:   1.0082                                     
REMARK   3      L33:   1.0326 L12:   0.0068                                     
REMARK   3      L13:  -0.3696 L23:  -0.1755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0549 S12:  -0.0958 S13:  -0.0195                       
REMARK   3      S21:  -0.0137 S22:  -0.0454 S23:  -0.0801                       
REMARK   3      S31:  -0.1011 S32:   0.1149 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1208-1229                           
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0968 -16.4944  26.9127              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2281 T22:   0.2171                                     
REMARK   3      T33:   0.2233 T12:   0.0184                                     
REMARK   3      T13:  -0.0120 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1296 L22:   0.0795                                     
REMARK   3      L33:   0.0652 L12:   0.0354                                     
REMARK   3      L13:  -0.2652 L23:   0.1980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0276 S12:   0.1117 S13:   0.0791                       
REMARK   3      S21:  -0.0383 S22:   0.0436 S23:   0.0443                       
REMARK   3      S31:  -0.0610 S32:   0.0046 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1230-1254                           
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4776 -27.4318  14.2894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1960 T22:   0.2021                                     
REMARK   3      T33:   0.1753 T12:   0.0351                                     
REMARK   3      T13:  -0.0094 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4463 L22:   0.1274                                     
REMARK   3      L33:   0.5180 L12:  -0.2367                                     
REMARK   3      L13:  -0.2710 L23:  -0.2070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0660 S12:  -0.0465 S13:   0.0957                       
REMARK   3      S21:  -0.0802 S22:   0.0432 S23:   0.0558                       
REMARK   3      S31:  -0.2308 S32:  -0.1585 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1255-1282                           
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3804 -36.3143  11.5727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1877 T22:   0.1821                                     
REMARK   3      T33:   0.1794 T12:   0.0197                                     
REMARK   3      T13:  -0.0088 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4528 L22:   0.1905                                     
REMARK   3      L33:   0.4050 L12:  -0.4281                                     
REMARK   3      L13:  -0.2584 L23:   0.6791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0730 S12:   0.0210 S13:  -0.1065                       
REMARK   3      S21:   0.1622 S22:   0.0671 S23:  -0.1749                       
REMARK   3      S31:  -0.0564 S32:   0.0445 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1283-1317                           
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2901 -37.1152  12.6306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1603 T22:   0.2075                                     
REMARK   3      T33:   0.2109 T12:  -0.0039                                     
REMARK   3      T13:  -0.0151 T23:   0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6008 L22:   0.3258                                     
REMARK   3      L33:   0.1353 L12:  -0.0093                                     
REMARK   3      L13:  -0.0424 L23:  -0.3951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0651 S12:  -0.0016 S13:  -0.1195                       
REMARK   3      S21:   0.0397 S22:   0.0989 S23:  -0.0045                       
REMARK   3      S31:   0.0086 S32:  -0.0890 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1318-1339                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.2646 -32.6168   1.7199              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2470 T22:   0.2969                                     
REMARK   3      T33:   0.2578 T12:  -0.0250                                     
REMARK   3      T13:  -0.0207 T23:   0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2935 L22:   0.1402                                     
REMARK   3      L33:  -0.0825 L12:  -0.0704                                     
REMARK   3      L13:   0.3822 L23:   0.1168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3178 S12:  -0.0355 S13:   0.0698                       
REMARK   3      S21:   0.1187 S22:   0.2345 S23:  -0.1283                       
REMARK   3      S31:  -0.0919 S32:   0.0050 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND RESSEQ 1126-1163                           
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5622 -38.4006  28.4976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1810 T22:   0.1664                                     
REMARK   3      T33:   0.1773 T12:   0.0262                                     
REMARK   3      T13:   0.0061 T23:  -0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1664 L22:   0.3956                                     
REMARK   3      L33:   0.5210 L12:  -0.1687                                     
REMARK   3      L13:   0.2619 L23:  -0.5234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0431 S12:   0.0836 S13:   0.0342                       
REMARK   3      S21:   0.0245 S22:  -0.0298 S23:  -0.0894                       
REMARK   3      S31:   0.1120 S32:   0.0375 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND RESSEQ 1164-1215                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2193 -37.2544  30.9006              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1774 T22:   0.1600                                     
REMARK   3      T33:   0.1595 T12:   0.0032                                     
REMARK   3      T13:   0.0045 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0656 L22:   0.7308                                     
REMARK   3      L33:   0.5114 L12:  -0.2848                                     
REMARK   3      L13:   0.0927 L23:   0.0170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0614 S12:   0.0729 S13:   0.0165                       
REMARK   3      S21:   0.0516 S22:   0.0065 S23:   0.0023                       
REMARK   3      S31:   0.0667 S32:  -0.1355 S33:  -0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND RESSEQ 1216-1249                           
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7599 -13.9738  55.6634              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1835 T22:   0.1915                                     
REMARK   3      T33:   0.2050 T12:  -0.0510                                     
REMARK   3      T13:   0.0246 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2710 L22:   0.1935                                     
REMARK   3      L33:   0.5629 L12:  -0.1537                                     
REMARK   3      L13:   0.4433 L23:  -0.2601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0198 S12:   0.1458 S13:  -0.0136                       
REMARK   3      S21:  -0.0254 S22:   0.0112 S23:   0.0554                       
REMARK   3      S31:   0.1949 S32:  -0.2238 S33:  -0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND RESSEQ 1250-1277                           
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3549  -4.5087  60.4161              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1878 T22:   0.1785                                     
REMARK   3      T33:   0.1625 T12:  -0.0147                                     
REMARK   3      T13:  -0.0116 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1898 L22:   0.1382                                     
REMARK   3      L33:   0.5624 L12:   0.1179                                     
REMARK   3      L13:   0.0764 L23:   0.2807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0327 S12:  -0.0386 S13:   0.0462                       
REMARK   3      S21:  -0.2314 S22:   0.0300 S23:  -0.1110                       
REMARK   3      S31:  -0.0743 S32:  -0.0288 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND RESSEQ 1278-1301                           
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8647  -6.0406  63.3346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1790 T22:   0.1795                                     
REMARK   3      T33:   0.1752 T12:  -0.0052                                     
REMARK   3      T13:   0.0160 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2503 L22:   0.1003                                     
REMARK   3      L33:   0.4059 L12:   0.1777                                     
REMARK   3      L13:  -0.3265 L23:  -0.3493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:  -0.0647 S13:   0.0418                       
REMARK   3      S21:   0.1403 S22:   0.1162 S23:   0.0073                       
REMARK   3      S31:   0.0373 S32:  -0.0825 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN B AND RESSEQ 1302-1339                           
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0904  -8.7685  64.3113              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1743 T22:   0.1941                                     
REMARK   3      T33:   0.1964 T12:   0.0043                                     
REMARK   3      T13:   0.0014 T23:  -0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5510 L22:  -0.0533                                     
REMARK   3      L33:   0.0780 L12:  -0.3855                                     
REMARK   3      L13:  -0.2026 L23:  -0.1887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0853 S12:  -0.0440 S13:  -0.0440                       
REMARK   3      S21:   0.0559 S22:   0.0842 S23:   0.0049                       
REMARK   3      S31:   0.0748 S32:  -0.0165 S33:   0.0000                       
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 3F7Q COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050251.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50835                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1QG3                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.3M NACL, 24% PEG        
REMARK 280  200, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 298K                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE MONOMERIC FORM IS BELIEVED TO BE THE BIOLOGICAL UNIT.    
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  1122                                                      
REMARK 465     SER A  1123                                                      
REMARK 465     HIS A  1124                                                      
REMARK 465     MET A  1125                                                      
REMARK 465     GLY A  1340                                                      
REMARK 465     GLU A  1341                                                      
REMARK 465     ASP A  1342                                                      
REMARK 465     TYR A  1343                                                      
REMARK 465     ASP A  1344                                                      
REMARK 465     SER A  1345                                                      
REMARK 465     PHE A  1346                                                      
REMARK 465     LEU A  1347                                                      
REMARK 465     MET A  1348                                                      
REMARK 465     TYR A  1349                                                      
REMARK 465     SER A  1350                                                      
REMARK 465     ASP A  1351                                                      
REMARK 465     ASP A  1352                                                      
REMARK 465     VAL A  1353                                                      
REMARK 465     LEU A  1354                                                      
REMARK 465     ARG A  1355                                                      
REMARK 465     GLY B  1122                                                      
REMARK 465     SER B  1123                                                      
REMARK 465     HIS B  1124                                                      
REMARK 465     MET B  1125                                                      
REMARK 465     GLY B  1340                                                      
REMARK 465     GLU B  1341                                                      
REMARK 465     ASP B  1342                                                      
REMARK 465     TYR B  1343                                                      
REMARK 465     ASP B  1344                                                      
REMARK 465     SER B  1345                                                      
REMARK 465     PHE B  1346                                                      
REMARK 465     LEU B  1347                                                      
REMARK 465     MET B  1348                                                      
REMARK 465     TYR B  1349                                                      
REMARK 465     SER B  1350                                                      
REMARK 465     ASP B  1351                                                      
REMARK 465     ASP B  1352                                                      
REMARK 465     VAL B  1353                                                      
REMARK 465     LEU B  1354                                                      
REMARK 465     ARG B  1355                                                      
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 A1166     -133.01    -93.64                                   
REMARK 500    PRO A1179       45.98    -83.62                                   
REMARK 500    ASN A1261     -155.58    -83.81                                   
REMARK 500    GLU B1168       -7.37    -52.06                                   
REMARK 500    PRO B1179       43.55    -83.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER B 1169     GLU B 1170                  146.36                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 601                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 701                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 703                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 706                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 707                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 602                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 702                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 704                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 705                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QG3   RELATED DB: PDB                                   
REMARK 900 SIMILAR FRAGMENT LACKING THE CONNECTING SEGMENT                      
REMARK 900 RELATED ID: 3F7P   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF A SIMILAR FRAGMENT OF INTEGRIN BETA4 IN                 
REMARK 900 COMPLEX WITH PLECTIN                                                 
REMARK 900 RELATED ID: 3F7R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE AT 2.04A OF AN EQUIVALENT FRAGMENT OF INTEGRIN             
REMARK 900 BETA4                                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE IS BASED ON REFERENCE 2 IN THE DATABASE, ITB4_HUMAN.    
DBREF  3F7Q A 1126  1355  UNP    P16144   ITB4_HUMAN    1126   1355             
DBREF  3F7Q B 1126  1355  UNP    P16144   ITB4_HUMAN    1126   1355             
SEQADV 3F7Q GLY A 1122  UNP  P16144              EXPRESSION TAG                 
SEQADV 3F7Q SER A 1123  UNP  P16144              EXPRESSION TAG                 
SEQADV 3F7Q HIS A 1124  UNP  P16144              EXPRESSION TAG                 
SEQADV 3F7Q MET A 1125  UNP  P16144              EXPRESSION TAG                 
SEQADV 3F7Q GLY B 1122  UNP  P16144              EXPRESSION TAG                 
SEQADV 3F7Q SER B 1123  UNP  P16144              EXPRESSION TAG                 
SEQADV 3F7Q HIS B 1124  UNP  P16144              EXPRESSION TAG                 
SEQADV 3F7Q MET B 1125  UNP  P16144              EXPRESSION TAG                 
SEQRES   1 A  234  GLY SER HIS MET ASP LEU GLY ALA PRO GLN ASN PRO ASN          
SEQRES   2 A  234  ALA LYS ALA ALA GLY SER ARG LYS ILE HIS PHE ASN TRP          
SEQRES   3 A  234  LEU PRO PRO SER GLY LYS PRO MET GLY TYR ARG VAL LYS          
SEQRES   4 A  234  TYR TRP ILE GLN GLY ASP SER GLU SER GLU ALA HIS LEU          
SEQRES   5 A  234  LEU ASP SER LYS VAL PRO SER VAL GLU LEU THR ASN LEU          
SEQRES   6 A  234  TYR PRO TYR CYS ASP TYR GLU MET LYS VAL CYS ALA TYR          
SEQRES   7 A  234  GLY ALA GLN GLY GLU GLY PRO TYR SER SER LEU VAL SER          
SEQRES   8 A  234  CYS ARG THR HIS GLN GLU VAL PRO SER GLU PRO GLY ARG          
SEQRES   9 A  234  LEU ALA PHE ASN VAL VAL SER SER THR VAL THR GLN LEU          
SEQRES  10 A  234  SER TRP ALA GLU PRO ALA GLU THR ASN GLY GLU ILE THR          
SEQRES  11 A  234  ALA TYR GLU VAL CYS TYR GLY LEU VAL ASN ASP ASP ASN          
SEQRES  12 A  234  ARG PRO ILE GLY PRO MET LYS LYS VAL LEU VAL ASP ASN          
SEQRES  13 A  234  PRO LYS ASN ARG MET LEU LEU ILE GLU ASN LEU ARG GLU          
SEQRES  14 A  234  SER GLN PRO TYR ARG TYR THR VAL LYS ALA ARG ASN GLY          
SEQRES  15 A  234  ALA GLY TRP GLY PRO GLU ARG GLU ALA ILE ILE ASN LEU          
SEQRES  16 A  234  ALA THR GLN PRO LYS ARG PRO MET SER ILE PRO ILE ILE          
SEQRES  17 A  234  PRO ASP ILE PRO ILE VAL ASP ALA GLN SER GLY GLU ASP          
SEQRES  18 A  234  TYR ASP SER PHE LEU MET TYR SER ASP ASP VAL LEU ARG          
SEQRES   1 B  234  GLY SER HIS MET ASP LEU GLY ALA PRO GLN ASN PRO ASN          
SEQRES   2 B  234  ALA LYS ALA ALA GLY SER ARG LYS ILE HIS PHE ASN TRP          
SEQRES   3 B  234  LEU PRO PRO SER GLY LYS PRO MET GLY TYR ARG VAL LYS          
SEQRES   4 B  234  TYR TRP ILE GLN GLY ASP SER GLU SER GLU ALA HIS LEU          
SEQRES   5 B  234  LEU ASP SER LYS VAL PRO SER VAL GLU LEU THR ASN LEU          
SEQRES   6 B  234  TYR PRO TYR CYS ASP TYR GLU MET LYS VAL CYS ALA TYR          
SEQRES   7 B  234  GLY ALA GLN GLY GLU GLY PRO TYR SER SER LEU VAL SER          
SEQRES   8 B  234  CYS ARG THR HIS GLN GLU VAL PRO SER GLU PRO GLY ARG          
SEQRES   9 B  234  LEU ALA PHE ASN VAL VAL SER SER THR VAL THR GLN LEU          
SEQRES  10 B  234  SER TRP ALA GLU PRO ALA GLU THR ASN GLY GLU ILE THR          
SEQRES  11 B  234  ALA TYR GLU VAL CYS TYR GLY LEU VAL ASN ASP ASP ASN          
SEQRES  12 B  234  ARG PRO ILE GLY PRO MET LYS LYS VAL LEU VAL ASP ASN          
SEQRES  13 B  234  PRO LYS ASN ARG MET LEU LEU ILE GLU ASN LEU ARG GLU          
SEQRES  14 B  234  SER GLN PRO TYR ARG TYR THR VAL LYS ALA ARG ASN GLY          
SEQRES  15 B  234  ALA GLY TRP GLY PRO GLU ARG GLU ALA ILE ILE ASN LEU          
SEQRES  16 B  234  ALA THR GLN PRO LYS ARG PRO MET SER ILE PRO ILE ILE          
SEQRES  17 B  234  PRO ASP ILE PRO ILE VAL ASP ALA GLN SER GLY GLU ASP          
SEQRES  18 B  234  TYR ASP SER PHE LEU MET TYR SER ASP ASP VAL LEU ARG          
HET     CL  A 601       1                                                       
HET    PEG  A 701       7                                                       
HET    1PE  A 703      16                                                       
HET    EDO  A 706       4                                                       
HET    EDO  A 707       4                                                       
HET     CL  B 602       1                                                       
HET    PEG  B 702       7                                                       
HET    PG4  B 704      13                                                       
HET    EDO  B 705       4                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4  PEG    2(C4 H10 O3)                                                 
FORMUL   5  1PE    C10 H22 O6                                                   
FORMUL   6  EDO    3(C2 H6 O2)                                                  
FORMUL  10  PG4    C8 H18 O5                                                    
FORMUL  12  HOH   *502(H2 O)                                                    
HELIX    1   1 SER A 1167  ALA A 1171  5                                   5    
HELIX    2   2 ASN A 1315  GLN A 1319  5                                   5    
HELIX    3   3 SER B 1167  ALA B 1171  5                                   5    
HELIX    4   4 ASN B 1315  GLN B 1319  5                                   5    
SHEET    1   A 3 GLN A1131  ALA A1137  0                                        
SHEET    2   A 3 ILE A1143  LEU A1148 -1  O  HIS A1144   N  LYS A1136           
SHEET    3   A 3 SER A1180  LEU A1183 -1  O  LEU A1183   N  ILE A1143           
SHEET    1   B 4 HIS A1172  SER A1176  0                                        
SHEET    2   B 4 GLY A1156  ILE A1163 -1  N  TYR A1157   O  SER A1176           
SHEET    3   B 4 ASP A1191  GLY A1200 -1  O  GLU A1193   N  TRP A1162           
SHEET    4   B 4 GLY A1203  GLU A1204 -1  O  GLY A1203   N  GLY A1200           
SHEET    1   C 4 HIS A1172  SER A1176  0                                        
SHEET    2   C 4 GLY A1156  ILE A1163 -1  N  TYR A1157   O  SER A1176           
SHEET    3   C 4 ASP A1191  GLY A1200 -1  O  GLU A1193   N  TRP A1162           
SHEET    4   C 4 VAL A1211  ARG A1214 -1  O  CYS A1213   N  TYR A1192           
SHEET    1   D 4 ALA A1227  VAL A1230  0                                        
SHEET    2   D 4 THR A1236  SER A1239 -1  O  SER A1239   N  ALA A1227           
SHEET    3   D 4 MET A1282  GLU A1286 -1  O  LEU A1283   N  LEU A1238           
SHEET    4   D 4 ILE A1334  ASP A1336  1  O  VAL A1335   N  GLU A1286           
SHEET    1   E 4 LYS A1271  LYS A1272  0                                        
SHEET    2   E 4 ALA A1252  LEU A1259 -1  N  TYR A1257   O  LYS A1271           
SHEET    3   E 4 TYR A1294  ASN A1302 -1  O  ARG A1301   N  ALA A1252           
SHEET    4   E 4 GLY A1305  TRP A1306 -1  O  GLY A1305   N  ASN A1302           
SHEET    1   F 4 LYS A1271  LYS A1272  0                                        
SHEET    2   F 4 ALA A1252  LEU A1259 -1  N  TYR A1257   O  LYS A1271           
SHEET    3   F 4 TYR A1294  ASN A1302 -1  O  ARG A1301   N  ALA A1252           
SHEET    4   F 4 ARG A1310  ILE A1314 -1  O  ALA A1312   N  TYR A1296           
SHEET    1   G 3 GLN B1131  ALA B1137  0                                        
SHEET    2   G 3 ILE B1143  LEU B1148 -1  O  LEU B1148   N  GLN B1131           
SHEET    3   G 3 SER B1180  LEU B1183 -1  O  LEU B1183   N  ILE B1143           
SHEET    1   H 4 HIS B1172  SER B1176  0                                        
SHEET    2   H 4 GLY B1156  ILE B1163 -1  N  TYR B1161   O  HIS B1172           
SHEET    3   H 4 ASP B1191  GLY B1200 -1  O  GLU B1193   N  TRP B1162           
SHEET    4   H 4 GLY B1203  GLU B1204 -1  O  GLY B1203   N  GLY B1200           
SHEET    1   I 4 HIS B1172  SER B1176  0                                        
SHEET    2   I 4 GLY B1156  ILE B1163 -1  N  TYR B1161   O  HIS B1172           
SHEET    3   I 4 ASP B1191  GLY B1200 -1  O  GLU B1193   N  TRP B1162           
SHEET    4   I 4 VAL B1211  ARG B1214 -1  O  CYS B1213   N  TYR B1192           
SHEET    1   J 4 ALA B1227  SER B1232  0                                        
SHEET    2   J 4 VAL B1235  SER B1239 -1  O  SER B1239   N  ALA B1227           
SHEET    3   J 4 MET B1282  GLU B1286 -1  O  ILE B1285   N  THR B1236           
SHEET    4   J 4 ILE B1334  ASP B1336  1  O  VAL B1335   N  GLU B1286           
SHEET    1   K 4 LYS B1271  LYS B1272  0                                        
SHEET    2   K 4 ALA B1252  LEU B1259 -1  N  TYR B1257   O  LYS B1271           
SHEET    3   K 4 TYR B1294  ASN B1302 -1  O  ARG B1301   N  ALA B1252           
SHEET    4   K 4 GLY B1305  TRP B1306 -1  O  GLY B1305   N  ASN B1302           
SHEET    1   L 4 LYS B1271  LYS B1272  0                                        
SHEET    2   L 4 ALA B1252  LEU B1259 -1  N  TYR B1257   O  LYS B1271           
SHEET    3   L 4 TYR B1294  ASN B1302 -1  O  ARG B1301   N  ALA B1252           
SHEET    4   L 4 ARG B1310  ILE B1314 -1  O  ALA B1312   N  TYR B1296           
SITE     1 AC1  6 HOH A 238  GLY A1139  SER A1140  ARG A1141                    
SITE     2 AC1  6 LYS A1142  LYS B1142                                          
SITE     1 AC2  3 ASN A1185  TYR A1187  GLU B1245                               
SITE     1 AC3  5 HOH A 201  GLU A1254  LYS A1272  GLU B1286                    
SITE     2 AC3  5 ILE B1334                                                     
SITE     1 AC4  2 GLU A1170  HIS A1172                                          
SITE     1 AC5  2 GLU A1222  GLU B1170                                          
SITE     1 AC6  5 LYS A1142  GLY B1139  SER B1140  ARG B1141                    
SITE     2 AC6  5 LYS B1142                                                     
SITE     1 AC7  4 HOH B 365  HOH B 418  ASN B1185  TYR B1187                    
SITE     1 AC8  5 GLU A1286  ILE A1326  HOH B 410  LYS B1272                    
SITE     2 AC8  5 LEU B1274                                                     
SITE     1 AC9  6 HOH B 252  TYR B1161  LEU B1174  GLU B1182                    
SITE     2 AC9  6 LEU B1183  THR B1184                                          
CRYST1   43.110   49.470   74.360 107.22  96.06 106.60 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023196  0.006915  0.005141        0.00000                         
SCALE2      0.000000  0.021093  0.007686        0.00000                         
SCALE3      0.000000  0.000000  0.014394        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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