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Database: PDB
Entry: 4NEH
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Original site: 4NEH 
HEADER    CELL ADHESION                           29-OCT-13   4NEH              
TITLE     AN INTERNAL LIGAND-BOUND, METASTABLE STATE OF A LEUKOCYTE INTEGRIN,   
TITLE    2 AXB2                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-X;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CD11C;                                                     
COMPND   5 SYNONYM: CD11 ANTIGEN-LIKE FAMILY MEMBER C, LEU M5, LEUKOCYTE        
COMPND   6 ADHESION GLYCOPROTEIN P150,95 ALPHA CHAIN, LEUKOCYTE ADHESION        
COMPND   7 RECEPTOR P150,95;                                                    
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: INTEGRIN BETA-2;                                           
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: CD18;                                                      
COMPND  14 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-1/CR3/P150,95       
COMPND  15 SUBUNIT BETA, COMPLEMENT RECEPTOR C3 SUBUNIT BETA;                   
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGAX, CD11C;                                                  
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-293S GNTI -/-;                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE CELL LINES;                    
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: ET10;                                     
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: ITGB2, CD18, MFI7;                                             
SOURCE  17 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  18 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: HEK-293S GNTI -/-;                      
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PEF-PURO                              
KEYWDS    ROSSMANN FOLD, COMPLEMENT RECEPTOR, IC3B, ICAM-1, FIBRINOGEN,         
KEYWDS   2 DENATURATED PROTEINS, HEPARIN, N-LINKED GLYCOSYLATION, MEMBRANE,     
KEYWDS   3 CELL ADHESION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SEN,K.YUKI,T.A.SPRINGER                                             
REVDAT   4   02-JUN-21 4NEH    1       SOURCE HETSYN                            
REVDAT   3   29-JUL-20 4NEH    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   03-JUN-20 4NEH    1       SEQADV LINK   ATOM                       
REVDAT   1   15-JAN-14 4NEH    0                                                
JRNL        AUTH   M.SEN,K.YUKI,T.A.SPRINGER                                    
JRNL        TITL   AN INTERNAL LIGAND-BOUND, METASTABLE STATE OF A LEUKOCYTE    
JRNL        TITL 2 INTEGRIN, ALPHA X BETA 2.                                    
JRNL        REF    J.CELL BIOL.                  V. 203   629 2013              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   24385486                                                     
JRNL        DOI    10.1083/JCB.201308083                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 81427                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4044                            
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 45.6700 -  5.9219    0.97     7950   459  0.1712 0.1855        
REMARK   3     2  5.9219 -  4.7019    0.98     7879   399  0.1383 0.1733        
REMARK   3     3  4.7019 -  4.1080    0.99     7862   406  0.1357 0.1753        
REMARK   3     4  4.1080 -  3.7326    0.99     7892   378  0.1747 0.2126        
REMARK   3     5  3.7326 -  3.4652    1.00     7861   417  0.2132 0.2568        
REMARK   3     6  3.4652 -  3.2609    1.00     7811   419  0.2293 0.2804        
REMARK   3     7  3.2609 -  3.0977    1.00     7842   416  0.2632 0.2951        
REMARK   3     8  3.0977 -  2.9629    1.00     7818   431  0.3125 0.3727        
REMARK   3     9  2.9629 -  2.8488    0.97     7681   391  0.3424 0.3822        
REMARK   3    10  2.8488 -  2.7505    0.87     6787   328  0.3754 0.3606        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 1.00                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.004          14265                                  
REMARK   3   ANGLE     :  0.779          19273                                  
REMARK   3   CHIRALITY :  0.032           2177                                  
REMARK   3   PLANARITY :  0.004           2518                                  
REMARK   3   DIHEDRAL  : 11.375           5267                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 144 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -44.8601   5.5416  52.1725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6100 T22:   0.5612                                     
REMARK   3      T33:   0.5744 T12:   0.0800                                     
REMARK   3      T13:  -0.0093 T23:   0.0660                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2725 L22:  -0.1219                                     
REMARK   3      L33:   0.1486 L12:  -0.0179                                     
REMARK   3      L13:  -0.0385 L23:  -0.2061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0614 S12:  -0.1931 S13:  -0.1855                       
REMARK   3      S21:   0.1787 S22:  -0.1075 S23:  -0.1029                       
REMARK   3      S31:   0.0466 S32:   0.1475 S33:  -0.0004                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 249 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.0719  20.0952  26.0784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4793 T22:   0.6092                                     
REMARK   3      T33:   0.5889 T12:   0.0397                                     
REMARK   3      T13:  -0.0666 T23:   0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1278 L22:   0.0745                                     
REMARK   3      L33:   0.4500 L12:  -0.0765                                     
REMARK   3      L13:  -0.0385 L23:  -0.1287                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2036 S12:   0.0446 S13:  -0.1665                       
REMARK   3      S21:   0.1936 S22:  -0.2779 S23:  -0.1671                       
REMARK   3      S31:  -0.3957 S32:  -0.1549 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 250 THROUGH 316 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1396  25.0345  39.5080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8595 T22:   0.6972                                     
REMARK   3      T33:   0.6040 T12:  -0.1561                                     
REMARK   3      T13:  -0.1791 T23:   0.1206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0271 L22:   0.2410                                     
REMARK   3      L33:   0.1358 L12:   0.0629                                     
REMARK   3      L13:  -0.1108 L23:  -0.1153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2055 S12:  -0.5807 S13:  -0.2266                       
REMARK   3      S21:   0.5685 S22:  -0.2062 S23:  -0.1868                       
REMARK   3      S31:  -0.7229 S32:   0.2458 S33:   0.0001                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 501 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -61.5745  18.1256  42.9233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5711 T22:   0.5653                                     
REMARK   3      T33:   0.5159 T12:   0.0942                                     
REMARK   3      T13:   0.0368 T23:   0.0700                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5989 L22:   0.5269                                     
REMARK   3      L33:   0.3641 L12:   0.1485                                     
REMARK   3      L13:  -0.2253 L23:   0.0116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0255 S12:   0.2393 S13:   0.0264                       
REMARK   3      S21:  -0.1347 S22:   0.0146 S23:   0.0274                       
REMARK   3      S31:  -0.0364 S32:  -0.0785 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 502 THROUGH 727 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -91.3829  -6.8029  61.2899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4996 T22:   0.4777                                     
REMARK   3      T33:   0.5992 T12:   0.0451                                     
REMARK   3      T13:   0.0848 T23:   0.0893                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4664 L22:  -0.1065                                     
REMARK   3      L33:   0.0814 L12:   0.2627                                     
REMARK   3      L13:  -0.2848 L23:  -0.4292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0796 S12:   0.0300 S13:  -0.0023                       
REMARK   3      S21:   0.2186 S22:   0.1227 S23:   0.0807                       
REMARK   3      S31:   0.0336 S32:  -0.0271 S33:   0.0099                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 728 THROUGH 805 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):-110.2537  -0.2547  45.2113              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5448 T22:   0.8229                                     
REMARK   3      T33:   0.7265 T12:  -0.0395                                     
REMARK   3      T13:   0.0410 T23:   0.2741                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0319 L22:   0.1840                                     
REMARK   3      L33:   0.2257 L12:   0.1138                                     
REMARK   3      L13:  -0.2255 L23:  -0.1930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1077 S12:   0.0853 S13:  -0.0143                       
REMARK   3      S21:  -0.0862 S22:   0.2174 S23:  -0.0015                       
REMARK   3      S31:   0.0606 S32:  -0.3463 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 806 THROUGH 1083 )                
REMARK   3    ORIGIN FOR THE GROUP (A): -90.2581  21.1104  15.8485              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7210 T22:   0.7194                                     
REMARK   3      T33:   0.5113 T12:  -0.1593                                     
REMARK   3      T13:   0.0711 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5185 L22:  -0.0907                                     
REMARK   3      L33:   0.2561 L12:  -0.0994                                     
REMARK   3      L13:  -0.2721 L23:  -0.8008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2606 S12:  -0.0022 S13:  -0.1265                       
REMARK   3      S21:  -0.1865 S22:   0.1738 S23:  -0.0922                       
REMARK   3      S31:   0.2175 S32:  -0.0761 S33:   0.0140                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 138 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -92.0744  38.8652  69.2034              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4748 T22:   0.2743                                     
REMARK   3      T33:   0.7913 T12:   0.1469                                     
REMARK   3      T13:   0.5212 T23:  -0.1698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2122 L22:   0.4256                                     
REMARK   3      L33:   0.2594 L12:  -0.1572                                     
REMARK   3      L13:   0.1654 L23:   0.1145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1567 S12:  -0.1724 S13:   0.1935                       
REMARK   3      S21:   0.5092 S22:  -0.0791 S23:   0.3433                       
REMARK   3      S31:  -0.3191 S32:   0.0462 S33:  -0.5362                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 139 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -48.1158  39.7272  65.2431              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5508 T22:   0.5038                                     
REMARK   3      T33:   0.4849 T12:  -0.0486                                     
REMARK   3      T13:   0.0079 T23:  -0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0236 L22:   0.1893                                     
REMARK   3      L33:  -0.0288 L12:  -0.0542                                     
REMARK   3      L13:  -0.0179 L23:  -0.0211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0065 S12:  -0.2534 S13:  -0.0212                       
REMARK   3      S21:   0.3526 S22:  -0.0438 S23:  -0.1317                       
REMARK   3      S31:  -0.1961 S32:   0.3675 S33:  -0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 234 THROUGH 460 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -78.9881  35.7921  66.6304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6682 T22:   0.3715                                     
REMARK   3      T33:   0.5937 T12:   0.0387                                     
REMARK   3      T13:   0.1917 T23:   0.0497                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4498 L22:   0.1309                                     
REMARK   3      L33:   0.2285 L12:   0.3576                                     
REMARK   3      L13:   0.0756 L23:   0.0719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0815 S12:  -0.0882 S13:   0.2005                       
REMARK   3      S21:   0.3240 S22:  -0.0083 S23:   0.1441                       
REMARK   3      S31:  -0.0293 S32:   0.1514 S33:  -0.0003                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 461 THROUGH 575 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):-107.1585  17.0074  58.1990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5368 T22:   0.7506                                     
REMARK   3      T33:   1.0487 T12:  -0.0452                                     
REMARK   3      T13:   0.1408 T23:   0.1076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0119 L22:   0.2186                                     
REMARK   3      L33:   0.0563 L12:   0.0553                                     
REMARK   3      L13:   0.0106 L23:   0.0707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1958 S12:   0.0440 S13:   0.1669                       
REMARK   3      S21:  -0.1082 S22:   0.1035 S23:   0.1743                       
REMARK   3      S31:  -0.3041 S32:   0.1472 S33:  -0.0102                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 576 THROUGH 675 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -79.9716  46.4133  21.6110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6438 T22:   0.6813                                     
REMARK   3      T33:   0.6577 T12:  -0.0008                                     
REMARK   3      T13:  -0.0961 T23:  -0.1468                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2615 L22:   0.0579                                     
REMARK   3      L33:   0.0601 L12:  -0.0903                                     
REMARK   3      L13:   0.1433 L23:  -0.0350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1734 S12:   0.0310 S13:  -0.2328                       
REMARK   3      S21:  -0.0037 S22:  -0.1136 S23:   0.1744                       
REMARK   3      S31:  -0.5348 S32:  -0.2775 S33:   0.0001                       
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 4NEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000083100.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-10                          
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-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR AND   
REMARK 200                                   K-B PAIR OF BIOMORPH MIRRORS FOR   
REMARK 200                                   VERTICAL AND HORIZONTAL FOCUSING   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81493                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.11060                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 3K6S, 1N3Y, 2IUE                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 8000, 0.2 M MG ACETATE, 0.1 M     
REMARK 280  NA CACODYLATE, PH 7.2, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 297K                                                    
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       63.48350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.23850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.72200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.23850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       63.48350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.72200            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 81620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
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     PRO A  1085                                                      
REMARK 465     ALA A  1086                                                      
REMARK 465     ALA A  1087                                                      
REMARK 465     LEU A  1088                                                      
REMARK 465     GLN A  1089                                                      
REMARK 465     THR A  1090                                                      
REMARK 465     LEU A  1091                                                      
REMARK 465     PHE A  1092                                                      
REMARK 465     GLN A  1093                                                      
REMARK 465     GLY A  1094                                                      
REMARK 465     HIS B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     GLY B    71                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     ASP B   429                                                      
REMARK 465     GLN B   430                                                      
REMARK 465     SER B   431                                                      
REMARK 465     ARG B   432                                                      
REMARK 465     PRO B   677                                                      
REMARK 465     ALA B   678                                                      
REMARK 465     ALA B   679                                                      
REMARK 465     LEU B   680                                                      
REMARK 465     GLN B   681                                                      
REMARK 465     THR B   682                                                      
REMARK 465     LEU B   683                                                      
REMARK 465     PHE B   684                                                      
REMARK 465     GLN B   685                                                      
REMARK 465     GLY B   686                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A 888    CG   CD                                             
REMARK 470     ARG A 889    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 890    OG1  CG2                                            
REMARK 470     SER A 891    OG                                                  
REMARK 470     GLY A1084    C    O                                              
REMARK 470     ARG B 428    C    O    CB   CG   CD   NE   CZ                    
REMARK 470     ARG B 428    NH1  NH2                                            
REMARK 470     GLY B 676    C    O                                              
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   OD1  ASP B   120     O    GLU B   325              1.73            
REMARK 500   OD2  ASP B   120     O    HOH B   812              2.00            
REMARK 500   CG   ASN B   620     C1   NAG H     1              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  83   C   -  N   -  CA  ANGL. DEV. = -18.8 DEGREES          
REMARK 500    PRO A 543   C   -  N   -  CA  ANGL. DEV. =  11.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A   6      -66.73    -98.68                                   
REMARK 500    SER A  28      -43.35   -134.88                                   
REMARK 500    SER A  82      -78.24    -67.75                                   
REMARK 500    SER A  82      -74.18    -72.00                                   
REMARK 500    THR A 104     -168.75   -111.94                                   
REMARK 500    SER A 145      -91.51     44.03                                   
REMARK 500    SER A 175     -109.65   -155.02                                   
REMARK 500    GLN A 204     -149.68     55.34                                   
REMARK 500    ARG A 219      -64.46   -126.62                                   
REMARK 500    THR A 322     -176.59    -63.84                                   
REMARK 500    GLU A 329      -86.92   -121.56                                   
REMARK 500    PHE A 354       73.14     54.04                                   
REMARK 500    LYS A 396      -81.04   -153.22                                   
REMARK 500    HIS A 410        2.45     59.06                                   
REMARK 500    SER A 421     -119.90     58.67                                   
REMARK 500    PRO A 543      103.87    -15.38                                   
REMARK 500    SER A 570      113.23   -170.77                                   
REMARK 500    GLU A 622     -149.84     71.02                                   
REMARK 500    GLN A 623       67.35     34.06                                   
REMARK 500    LYS A 677       18.40     59.87                                   
REMARK 500    LYS A 690     -143.58     63.99                                   
REMARK 500    VAL A 708      -63.31    -97.44                                   
REMARK 500    CYS A 752      -75.54    -99.46                                   
REMARK 500    ASP A 791       71.62   -102.98                                   
REMARK 500    GLN A 837      142.06   -177.04                                   
REMARK 500    HIS A 848      -12.22     67.70                                   
REMARK 500    ARG A 889     -155.84     58.84                                   
REMARK 500    THR A 890       19.90     55.38                                   
REMARK 500    LYS A 892     -131.38     54.16                                   
REMARK 500    ASN A 974       64.03     33.72                                   
REMARK 500    SER A 976       26.76   -152.40                                   
REMARK 500    PRO A 999       73.32    -61.07                                   
REMARK 500    PHE B   6      -67.27   -106.58                                   
REMARK 500    LYS B  74      -47.02   -143.43                                   
REMARK 500    MET B 117       33.53    -95.27                                   
REMARK 500    VAL B 150      -81.01   -131.31                                   
REMARK 500    SER B 205     -161.28   -118.75                                   
REMARK 500    LEU B 208      -60.12    -95.90                                   
REMARK 500    VAL B 233     -169.85   -104.63                                   
REMARK 500    ASN B 350     -158.56    -82.75                                   
REMARK 500    ASN B 384       -3.12     63.36                                   
REMARK 500    ARG B 426       70.49     55.53                                   
REMARK 500    SER B 435      -17.43     63.64                                   
REMARK 500    HIS B 438       43.08     35.66                                   
REMARK 500    GLU B 470      -23.69     63.79                                   
REMARK 500    PRO B 503      107.95    -51.53                                   
REMARK 500    ASN B 523      -96.97     55.75                                   
REMARK 500    GLU B 567       80.23     61.43                                   
REMARK 500    SER B 569     -131.09     52.82                                   
REMARK 500    SER B 583     -134.50     56.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
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 A   82     PRO A   83                  149.89                    
REMARK 500 SER A   82     PRO A   83                  149.11                    
REMARK 500 GLU A  622     GLN A  623                 -146.12                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 140   OG                                                     
REMARK 620 2 SER A 142   OG   76.3                                              
REMARK 620 3 THR A 207   OG1  89.4 157.0                                        
REMARK 620 4 HOH A1245   O    73.3  72.6  86.2                                  
REMARK 620 5 HOH A1268   O   149.3 105.2  78.1  77.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 703  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 318   OE1                                                    
REMARK 620 2 SER B 114   OG   87.4                                              
REMARK 620 3 SER B 116   OG   80.1  92.6                                        
REMARK 620 4 GLU B 212   OE1  89.0  90.4 168.6                                  
REMARK 620 5 HOH B 801   O   157.8  72.8  90.9 100.6                            
REMARK 620 6 HOH B 821   O    99.8 172.9  88.5  89.9 100.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1104  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 447   OD1                                                    
REMARK 620 2 ASP A 449   OD1  84.4                                              
REMARK 620 3 ASP A 451   OD1  85.6 108.1                                        
REMARK 620 4 ASP A 451   OD2 128.3  78.0  55.8                                  
REMARK 620 5 SER A 453   O    68.5 151.2  80.0 126.2                            
REMARK 620 6 ASP A 455   OD1 117.2 106.6 140.0 114.4  79.1                      
REMARK 620 7 ASP A 455   OD2  88.6  66.2 172.3 125.5 102.5  47.5                
REMARK 620 8 HOH A1311   O   130.6  57.4 132.6  76.8 136.2  57.0  49.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1103  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 511   OD1                                                    
REMARK 620 2 ASN A 513   OD1  79.6                                              
REMARK 620 3 ASP A 515   OD1  65.8  84.3                                        
REMARK 620 4 LEU A 517   O    80.5 159.3  92.8                                  
REMARK 620 5 ASP A 519   OD1 141.0  96.4 153.0  95.4                            
REMARK 620 6 ASP A 519   OD2  85.8  81.0 150.0  91.9  55.4                      
REMARK 620 7 HOH A1261   O   147.0  98.4  81.2 101.5  72.0 126.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 574   OD1                                                    
REMARK 620 2 THR A 576   OG1  90.6                                              
REMARK 620 3 ASP A 578   OD1  78.8  85.3                                        
REMARK 620 4 ASP A 578   OD2 114.4  58.4  46.0                                  
REMARK 620 5 LEU A 580   O    78.0 165.2  83.2 117.7                            
REMARK 620 6 ASP A 582   OD1 132.2  98.2 148.4 110.1  96.4                      
REMARK 620 7 ASP A 582   OD2  77.5  90.8 155.9 145.6  95.9  55.7                
REMARK 620 8 HOH A1204   O   158.6  90.9  80.1  50.0  96.2  68.5 123.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 702  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 120   OD1                                                    
REMARK 620 2 ASP B 120   OD2  54.7                                              
REMARK 620 3 GLU B 325   O    42.6  89.1                                        
REMARK 620 4 HOH B 809   O   119.0 165.3  92.3                                  
REMARK 620 5 HOH B 812   O    72.0  49.8  73.6 144.3                            
REMARK 620 6 HOH B 860   O   132.9 120.4  96.0  74.1  75.1                      
REMARK 620 7 HOH B 861   O   138.6  88.1 172.0  92.2  99.0  78.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 701  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 151   OD2                                                    
REMARK 620 2 ASN B 207   OD1  94.5                                              
REMARK 620 3 ASP B 209   OD1  92.1  90.8                                        
REMARK 620 4 ASP B 209   O   162.9  83.4  71.0                                  
REMARK 620 5 PRO B 211   O    89.2 166.9 101.6  96.7                            
REMARK 620 6 GLU B 212   OE2 100.6  80.4 165.1  95.8  86.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K6S   RELATED DB: PDB                                   
REMARK 900 THE BEND AND CLOSED STRUCTURE OF AXB2                                
REMARK 900 RELATED ID: 3K71   RELATED DB: PDB                                   
REMARK 900 THE BEND AND CLOSED STRUCTURE OF AXB2                                
REMARK 900 RELATED ID: 3K7S   RELATED DB: PDB                                   
REMARK 900 THE BEND AND CLOSED STRUCTURE OF AXB2                                
REMARK 900 RELATED ID: 2IUE   RELATED DB: PDB                                   
REMARK 900 THE HOMOLOG                                                          
DBREF  4NEH A    1  1082  UNP    P20702   ITAX_HUMAN      20   1101             
DBREF  4NEH B    1   674  UNP    P05107   ITB2_HUMAN      23    696             
SEQADV 4NEH ASP A   42  UNP  P20702    ASN    61 CONFLICT                       
SEQADV 4NEH ASP A  368  UNP  P20702    SER   387 CONFLICT                       
SEQADV 4NEH THR A  678  UNP  P20702    ASN   697 CONFLICT                       
SEQADV 4NEH SER A  885  UNP  P20702    ASN   904 CONFLICT                       
SEQADV 4NEH CYS A  920  UNP  P20702    ASN   939 CONFLICT                       
SEQADV 4NEH PRO A 1083  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH GLY A 1084  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH PRO A 1085  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH ALA A 1086  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH ALA A 1087  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH LEU A 1088  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH GLN A 1089  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH THR A 1090  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH LEU A 1091  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH PHE A 1092  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH GLN A 1093  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH GLY A 1094  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEH ASP B  190  UNP  P05107    ASN   212 CONFLICT                       
SEQADV 4NEH LYS B  232  UNP  P05107    ASN   254 CONFLICT                       
SEQADV 4NEH CYS B  674  UNP  P05107    VAL   696 CONFLICT                       
SEQADV 4NEH GLY B  675  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH GLY B  676  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH PRO B  677  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH ALA B  678  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH ALA B  679  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH LEU B  680  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH GLN B  681  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH THR B  682  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH LEU B  683  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH PHE B  684  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH GLN B  685  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEH GLY B  686  UNP  P05107              EXPRESSION TAG                 
SEQRES   1 A 1094  PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL          
SEQRES   2 A 1094  ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA          
SEQRES   3 A 1094  ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR          
SEQRES   4 A 1094  ALA ALA ASP GLN THR GLY GLY LEU TYR GLN CYS GLY TYR          
SEQRES   5 A 1094  SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO          
SEQRES   6 A 1094  PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA          
SEQRES   7 A 1094  SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO          
SEQRES   8 A 1094  THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR          
SEQRES   9 A 1094  GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN          
SEQRES  10 A 1094  ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU          
SEQRES  11 A 1094  GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE          
SEQRES  12 A 1094  SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG          
SEQRES  13 A 1094  ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE          
SEQRES  14 A 1094  SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE          
SEQRES  15 A 1094  THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER          
SEQRES  16 A 1094  LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR          
SEQRES  17 A 1094  THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE          
SEQRES  18 A 1094  HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE          
SEQRES  19 A 1094  LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER          
SEQRES  20 A 1094  LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA          
SEQRES  21 A 1094  GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE          
SEQRES  22 A 1094  GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA          
SEQRES  23 A 1094  SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP          
SEQRES  24 A 1094  PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU          
SEQRES  25 A 1094  LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER          
SEQRES  26 A 1094  SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER          
SEQRES  27 A 1094  ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL          
SEQRES  28 A 1094  GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO          
SEQRES  29 A 1094  PRO ASN MET ASP PRO THR PHE ILE ASN MET SER GLN GLU          
SEQRES  30 A 1094  ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR          
SEQRES  31 A 1094  GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU          
SEQRES  32 A 1094  GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE          
SEQRES  33 A 1094  PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU          
SEQRES  34 A 1094  VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER          
SEQRES  35 A 1094  LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP          
SEQRES  36 A 1094  LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR          
SEQRES  37 A 1094  ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY          
SEQRES  38 A 1094  TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU          
SEQRES  39 A 1094  GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR          
SEQRES  40 A 1094  VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL          
SEQRES  41 A 1094  VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA          
SEQRES  42 A 1094  VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER          
SEQRES  43 A 1094  PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER          
SEQRES  44 A 1094  SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY          
SEQRES  45 A 1094  GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL          
SEQRES  46 A 1094  GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO          
SEQRES  47 A 1094  VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA          
SEQRES  48 A 1094  GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL          
SEQRES  49 A 1094  VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU          
SEQRES  50 A 1094  TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG          
SEQRES  51 A 1094  ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP          
SEQRES  52 A 1094  PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR          
SEQRES  53 A 1094  LYS THR ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU          
SEQRES  54 A 1094  LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER          
SEQRES  55 A 1094  CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU          
SEQRES  56 A 1094  ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG          
SEQRES  57 A 1094  ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR          
SEQRES  58 A 1094  PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA          
SEQRES  59 A 1094  ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER          
SEQRES  60 A 1094  PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU          
SEQRES  61 A 1094  GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU          
SEQRES  62 A 1094  ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA          
SEQRES  63 A 1094  GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN          
SEQRES  64 A 1094  GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA          
SEQRES  65 A 1094  PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG          
SEQRES  66 A 1094  ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR          
SEQRES  67 A 1094  PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU          
SEQRES  68 A 1094  GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU          
SEQRES  69 A 1094  SER ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU          
SEQRES  70 A 1094  GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER          
SEQRES  71 A 1094  SER HIS GLU GLN PHE THR LYS TYR LEU CYS PHE SER GLU          
SEQRES  72 A 1094  SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR          
SEQRES  73 A 1094  GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER          
SEQRES  74 A 1094  ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA          
SEQRES  75 A 1094  VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO          
SEQRES  76 A 1094  SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA          
SEQRES  77 A 1094  SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU          
SEQRES  78 A 1094  ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP          
SEQRES  79 A 1094  VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR          
SEQRES  80 A 1094  LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE          
SEQRES  81 A 1094  LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE          
SEQRES  82 A 1094  THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN          
SEQRES  83 A 1094  GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU          
SEQRES  84 A 1094  LYS TYR LYS PRO GLY PRO ALA ALA LEU GLN THR LEU PHE          
SEQRES  85 A 1094  GLN GLY                                                      
SEQRES   1 B  686  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 B  686  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 B  686  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 B  686  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 B  686  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 B  686  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 B  686  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 B  686  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO          
SEQRES   9 B  686  ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET          
SEQRES  10 B  686  LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP          
SEQRES  11 B  686  LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG          
SEQRES  12 B  686  ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO          
SEQRES  13 B  686  PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS          
SEQRES  14 B  686  PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE          
SEQRES  15 B  686  ARG HIS VAL LEU LYS LEU THR ASP ASN SER ASN GLN PHE          
SEQRES  16 B  686  GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU          
SEQRES  17 B  686  ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL          
SEQRES  18 B  686  ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG LYS VAL THR          
SEQRES  19 B  686  ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE          
SEQRES  20 B  686  ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN          
SEQRES  21 B  686  ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG          
SEQRES  22 B  686  SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA          
SEQRES  23 B  686  HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA          
SEQRES  24 B  686  VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR          
SEQRES  25 B  686  GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU          
SEQRES  26 B  686  ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR          
SEQRES  27 B  686  ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA          
SEQRES  28 B  686  LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS          
SEQRES  29 B  686  SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP          
SEQRES  30 B  686  CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN          
SEQRES  31 B  686  VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER          
SEQRES  32 B  686  PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR          
SEQRES  33 B  686  VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP          
SEQRES  34 B  686  GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE          
SEQRES  35 B  686  LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE          
SEQRES  36 B  686  GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER          
SEQRES  37 B  686  GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER          
SEQRES  38 B  686  ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN          
SEQRES  39 B  686  CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE          
SEQRES  40 B  686  TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU          
SEQRES  41 B  686  ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY          
SEQRES  42 B  686  LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE          
SEQRES  43 B  686  GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY          
SEQRES  44 B  686  CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY          
SEQRES  45 B  686  ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR          
SEQRES  46 B  686  GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER          
SEQRES  47 B  686  PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS          
SEQRES  48 B  686  PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA          
SEQRES  49 B  686  CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY          
SEQRES  50 B  686  ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL          
SEQRES  51 B  686  ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR          
SEQRES  52 B  686  LEU ILE TYR VAL ASP GLU SER ARG GLU CYS CYS GLY GLY          
SEQRES  53 B  686  PRO ALA ALA LEU GLN THR LEU PHE GLN GLY                      
MODRES 4NEH ASN A  880  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEH ASN A   70  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEH ASN A  373  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEH ASN B   94  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEH ASN A  716  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEH ASN A 1031  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEH ASN B  620  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    BMA  D   3      11                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    MAN  E   5      11                                                       
HET    MAN  E   6      11                                                       
HET    MAN  E   7      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET     CA  A1101       1                                                       
HET     MG  A1102       1                                                       
HET     CA  A1103       1                                                       
HET     CA  A1104       1                                                       
HET    NAG  A1119      14                                                       
HET     CL  A1120       1                                                       
HET     NA  A1121       1                                                       
HET     CA  B 701       1                                                       
HET     CA  B 702       1                                                       
HET     MG  B 703       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
FORMUL   3  NAG    13(C8 H15 N O6)                                              
FORMUL   4  BMA    2(C6 H12 O6)                                                 
FORMUL   5  MAN    4(C6 H12 O6)                                                 
FORMUL   9   CA    5(CA 2+)                                                     
FORMUL  10   MG    2(MG 2+)                                                     
FORMUL  14   CL    CL 1-                                                        
FORMUL  15   NA    NA 1+                                                        
FORMUL  19  HOH   *308(H2 O)                                                    
HELIX    1   1 SER A  145  GLN A  161  1                                  17    
HELIX    2   2 THR A  183  ARG A  189  1                                   7    
HELIX    3   3 ASN A  192  LEU A  196  5                                   5    
HELIX    4   4 TYR A  208  LEU A  220  1                                  13    
HELIX    5   5 HIS A  222  GLY A  226  5                                   5    
HELIX    6   6 ASP A  249  ALA A  260  1                                  12    
HELIX    7   7 GLY A  270  PHE A  273  5                                   4    
HELIX    8   8 ASN A  275  ALA A  286  1                                  12    
HELIX    9   9 PRO A  289  GLU A  292  5                                   4    
HELIX   10  10 ASP A  301  GLN A  307  1                                   7    
HELIX   11  11 ALA A  316  THR A  320  5                                   5    
HELIX   12  12 GLY A  352  SER A  357  1                                   6    
HELIX   13  13 ASN A  378  ARG A  382  5                                   5    
HELIX   14  14 ARG A  407  THR A  411  5                                   5    
HELIX   15  15 GLY A  526  ARG A  531  1                                   6    
HELIX   16  16 GLY A  555  SER A  559  1                                   5    
HELIX   17  17 ASP A  990  ASN A  998  1                                   9    
HELIX   18  18 GLY A 1035  ILE A 1040  5                                   6    
HELIX   19  19 GLN A 1066  PHE A 1069  5                                   4    
HELIX   20  20 CYS B   11  GLY B   18  1                                   8    
HELIX   21  21 ASP B   36  ILE B   38  5                                   3    
HELIX   22  22 LEU B   46  GLY B   50  5                                   5    
HELIX   23  23 SER B  114  LEU B  118  5                                   5    
HELIX   24  24 ASN B  123  THR B  139  1                                  17    
HELIX   25  25 HIS B  161  ASN B  167  1                                   7    
HELIX   26  26 ASN B  191  LYS B  201  1                                  11    
HELIX   27  27 GLY B  213  CYS B  224  1                                  12    
HELIX   28  28 CYS B  224  GLY B  229  1                                   6    
HELIX   29  29 GLY B  249  ALA B  255  5                                   7    
HELIX   30  30 TYR B  271  GLU B  276  5                                   6    
HELIX   31  31 SER B  281  ASN B  292  1                                  12    
HELIX   32  32 MET B  304  LYS B  310  1                                   7    
HELIX   33  33 LYS B  310  ILE B  315  1                                   6    
HELIX   34  34 ASN B  329  SER B  343  1                                  15    
HELIX   35  35 ILE B  482  GLY B  486  5                                   5    
HELIX   36  36 GLY B  528  ARG B  532  1                                   5    
HELIX   37  37 PRO B  599  LYS B  602  5                                   4    
HELIX   38  38 TYR B  603  GLU B  613  1                                  11    
HELIX   39  39 LYS B  614  GLY B  618  5                                   5    
HELIX   40  40 ASN B  620  CYS B  625  1                                   6    
SHEET    1   A 4 THR A   9  ARG A  12  0                                        
SHEET    2   A 4 GLN A 590  ARG A 595 -1  O  VAL A 591   N  PHE A  11           
SHEET    3   A 4 ASP A 582  ALA A 587 -1  N  VAL A 585   O  LEU A 592           
SHEET    4   A 4 LEU A 569  GLN A 573 -1  N  GLN A 573   O  ASP A 582           
SHEET    1   B 4 VAL A  22  TYR A  25  0                                        
SHEET    2   B 4 TRP A  29  ALA A  40 -1  O  VAL A  31   N  VAL A  23           
SHEET    3   B 4 GLN A  43  CYS A  50 -1  O  TYR A  48   N  VAL A  32           
SHEET    4   B 4 CYS A  57  PRO A  59 -1  O  GLU A  58   N  GLN A  49           
SHEET    1   C 4 SER A  76  THR A  80  0                                        
SHEET    2   C 4 GLN A  85  CYS A  97 -1  O  LEU A  87   N  ALA A  78           
SHEET    3   C 4 ASN A 100  LEU A 110 -1  O  TYR A 102   N  HIS A  95           
SHEET    4   C 4 GLN A 117  LEU A 119 -1  O  GLN A 117   N  LEU A 109           
SHEET    1   D 6 PHE A 178  PHE A 182  0                                        
SHEET    2   D 6 THR A 167  PHE A 174 -1  N  GLN A 173   O  GLN A 179           
SHEET    3   D 6 GLN A 131  ASP A 138  1  N  PHE A 135   O  SER A 170           
SHEET    4   D 6 ALA A 232  THR A 239  1  O  ILE A 238   N  ASP A 138           
SHEET    5   D 6 ILE A 262  GLY A 268  1  O  ILE A 263   N  LEU A 235           
SHEET    6   D 6 ILE A 294  LYS A 296  1  O  PHE A 295   N  GLY A 268           
SHEET    1   E 4 GLU A 335  THR A 342  0                                        
SHEET    2   E 4 GLY A 345  ALA A 350 -1  O  VAL A 347   N  VAL A 340           
SHEET    3   E 4 ALA A 360  LEU A 362 -1  O  PHE A 361   N  LEU A 348           
SHEET    4   E 4 THR A 370  ILE A 372 -1  O  ILE A 372   N  ALA A 360           
SHEET    1   F 4 THR A 390  LEU A 394  0                                        
SHEET    2   F 4 GLN A 399  ALA A 405 -1  O  SER A 400   N  ALA A 393           
SHEET    3   F 4 LYS A 413  VAL A 420 -1  O  VAL A 415   N  LEU A 403           
SHEET    4   F 4 GLN A 423  THR A 431 -1  O  GLN A 423   N  VAL A 420           
SHEET    1   G 4 LEU A 443  VAL A 446  0                                        
SHEET    2   G 4 LEU A 456  TYR A 465 -1  O  LEU A 458   N  CYS A 444           
SHEET    3   G 4 GLY A 470  PRO A 477 -1  O  GLN A 472   N  ALA A 461           
SHEET    4   G 4 ALA A 489  LEU A 491 -1  O  LEU A 491   N  VAL A 473           
SHEET    1   H 4 LEU A 506  GLY A 510  0                                        
SHEET    2   H 4 ASP A 519  ALA A 524 -1  O  VAL A 521   N  THR A 507           
SHEET    3   H 4 ALA A 533  PHE A 537 -1  O  ALA A 533   N  ALA A 524           
SHEET    4   H 4 GLN A 551  ALA A 554 -1  O  ILE A 553   N  VAL A 534           
SHEET    1   I 2 GLY A 539  VAL A 540  0                                        
SHEET    2   I 2 SER A 544  ILE A 545 -1  O  SER A 544   N  VAL A 540           
SHEET    1   J 5 THR A 672  PHE A 673  0                                        
SHEET    2   J 5 LYS A 690  LEU A 700 -1  O  LEU A 699   N  THR A 672           
SHEET    3   J 5 THR A 629  LYS A 641 -1  N  ILE A 639   O  LYS A 690           
SHEET    4   J 5 VAL A 599  ILE A 609 -1  N  ILE A 609   O  GLN A 632           
SHEET    5   J 5 MET A 733  LEU A 734  1  O  MET A 733   N  LEU A 600           
SHEET    1   K 4 SER A 680  LEU A 687  0                                        
SHEET    2   K 4 SER A 654  LEU A 662 -1  N  LEU A 658   O  ARG A 683           
SHEET    3   K 4 ILE A 711  GLY A 721 -1  O  ARG A 714   N  ALA A 661           
SHEET    4   K 4 TYR A 741  LEU A 746 -1  O  LEU A 746   N  ILE A 711           
SHEET    1   L 4 GLY A 763  SER A 767  0                                        
SHEET    2   L 4 GLU A 781  TRP A 789 -1  O  MET A 787   N  SER A 765           
SHEET    3   L 4 GLN A 856  VAL A 865 -1  O  PHE A 863   N  LEU A 782           
SHEET    4   L 4 LEU A 808  TYR A 810 -1  N  SER A 809   O  ASP A 864           
SHEET    1   M 6 LEU A 774  VAL A 776  0                                        
SHEET    2   M 6 PHE A 895  VAL A 905  1  O  PRO A 900   N  LEU A 774           
SHEET    3   M 6 ARG A 874  SER A 882 -1  N  ALA A 879   O  PHE A 895           
SHEET    4   M 6 SER A 795  PRO A 805 -1  N  THR A 801   O  ASN A 880           
SHEET    5   M 6 THR A 839  PHE A 851 -1  O  CYS A 844   N  ILE A 800           
SHEET    6   M 6 THR A 828  VAL A 834 -1  N  ALA A 832   O  SER A 841           
SHEET    1   N 3 LEU A 774  VAL A 776  0                                        
SHEET    2   N 3 PHE A 895  VAL A 905  1  O  PRO A 900   N  LEU A 774           
SHEET    3   N 3 TYR A1060  GLN A1062  1  O  SER A1061   N  VAL A 905           
SHEET    1   O 4 THR A 907  SER A 911  0                                        
SHEET    2   O 4 SER A 929  ASN A 940 -1  O  ASN A 939   N  VAL A 908           
SHEET    3   O 4 GLU A1023  SER A1033 -1  O  LEU A1028   N  HIS A 934           
SHEET    4   O 4 TRP A 964  SER A 970 -1  N  MET A 965   O  ASN A1031           
SHEET    1   P 6 TYR A 918  SER A 922  0                                        
SHEET    2   P 6 ARG A1071  TYR A1081  1  O  VAL A1077   N  LEU A 919           
SHEET    3   P 6 LYS A1044  THR A1054 -1  N  ALA A1051   O  ALA A1072           
SHEET    4   P 6 LEU A 946  LEU A 958 -1  N  ASN A 951   O  GLU A1052           
SHEET    5   P 6 GLY A1007  PHE A1018 -1  O  VAL A1015   N  VAL A 948           
SHEET    6   P 6 SER A 980  ILE A 984 -1  N  ILE A 984   O  CYS A1008           
SHEET    1   Q 4 GLU A 961  ALA A 962  0                                        
SHEET    2   Q 4 LEU A 946  LEU A 958 -1  N  LEU A 958   O  GLU A 961           
SHEET    3   Q 4 LYS A1044  THR A1054 -1  O  GLU A1052   N  ASN A 951           
SHEET    4   Q 4 VAL A1000  LEU A1001  1  N  LEU A1001   O  SER A1046           
SHEET    1   R 3 CYS B  40  ASP B  41  0                                        
SHEET    2   R 3 THR B  22  CYS B  24 -1  N  THR B  22   O  ASP B  41           
SHEET    3   R 3 ILE B  56  MET B  57 -1  O  MET B  57   N  TRP B  23           
SHEET    1   S 6 LEU B  62  THR B  65  0                                        
SHEET    2   S 6 LYS B  80  LEU B  85 -1  O  TYR B  84   N  LEU B  62           
SHEET    3   S 6 ILE B 414  PRO B 421  1  O  GLN B 418   N  LEU B  83           
SHEET    4   S 6 GLN B 402  ALA B 408 -1  N  GLN B 402   O  VAL B 419           
SHEET    5   S 6 VAL B 345  HIS B 349 -1  N  ASP B 348   O  ARG B 407           
SHEET    6   S 6 GLY B 376  CYS B 378 -1  O  GLY B 376   N  LEU B 347           
SHEET    1   T 5 LEU B  76  SER B  77  0                                        
SHEET    2   T 5 ALA B  91  PHE B  97 -1  O  THR B  96   N  SER B  77           
SHEET    3   T 5 ILE B 387  ALA B 395 -1  O  PHE B 389   N  VAL B  95           
SHEET    4   T 5 LEU B 356  PHE B 363 -1  N  THR B 359   O  LYS B 392           
SHEET    5   T 5 THR B 369  GLN B 373 -1  O  GLN B 373   N  TYR B 360           
SHEET    1   U 6 PHE B 182  THR B 189  0                                        
SHEET    2   U 6 GLY B 142  PHE B 149 -1  N  ILE B 144   O  THR B 189           
SHEET    3   U 6 ILE B 105  ASP B 112  1  N  MET B 111   O  GLY B 147           
SHEET    4   U 6 THR B 234  THR B 241  1  O  LEU B 236   N  ASP B 106           
SHEET    5   U 6 ILE B 294  THR B 301  1  O  ILE B 297   N  LEU B 237           
SHEET    6   U 6 ALA B 319  LEU B 323  1  O  LEU B 323   N  VAL B 300           
SHEET    1   V 2 PHE B 442  GLU B 444  0                                        
SHEET    2   V 2 ILE B 447  ARG B 449 -1  O  ILE B 447   N  GLU B 444           
SHEET    1   W 2 TYR B 454  ILE B 455  0                                        
SHEET    2   W 2 CYS B 461  GLN B 462 -1  O  CYS B 461   N  ILE B 455           
SHEET    1   X 2 GLY B 488  VAL B 491  0                                        
SHEET    2   X 2 GLN B 494  CYS B 497 -1  O  LEU B 496   N  ASP B 489           
SHEET    1   Y 2 ARG B 521  TYR B 522  0                                        
SHEET    2   Y 2 GLN B 525  VAL B 526 -1  O  GLN B 525   N  TYR B 522           
SHEET    1   Z 2 GLY B 533  PHE B 536  0                                        
SHEET    2   Z 2 LYS B 539  CYS B 542 -1  O  LYS B 539   N  PHE B 536           
SHEET    1  AA 2 PHE B 546  GLU B 547  0                                        
SHEET    2  AA 2 CYS B 553  GLU B 554 -1  O  CYS B 553   N  GLU B 547           
SHEET    1  AB 2 GLY B 572  ARG B 575  0                                        
SHEET    2  AB 2 VAL B 578  CYS B 581 -1  O  GLU B 580   N  ARG B 573           
SHEET    1  AC 4 LEU B 628  SER B 631  0                                        
SHEET    2  AC 4 ARG B 662  VAL B 667  1  O  ILE B 665   N  SER B 631           
SHEET    3  AC 4 TRP B 649  GLN B 657 -1  N  GLN B 657   O  ARG B 662           
SHEET    4  AC 4 ARG B 638  ARG B 643 -1  N  GLU B 642   O  VAL B 650           
SSBOND   1 CYS A   50    CYS A   57                          1555   1555  2.04  
SSBOND   2 CYS A   89    CYS A  107                          1555   1555  2.02  
SSBOND   3 CYS A   97    CYS A  126                          1555   1555  2.03  
SSBOND   4 CYS A  476    CYS A  487                          1555   1555  2.03  
SSBOND   5 CYS A  620    CYS A  703                          1555   1555  2.03  
SSBOND   6 CYS A  636    CYS A  693                          1555   1555  2.03  
SSBOND   7 CYS A  752    CYS A  758                          1555   1555  2.04  
SSBOND   8 CYS A  829    CYS A  844                          1555   1555  2.03  
SSBOND   9 CYS A  920    CYS B  674                          1555   1555  2.03  
SSBOND  10 CYS A  979    CYS A 1013                          1555   1555  2.03  
SSBOND  11 CYS A 1003    CYS A 1008                          1555   1555  2.03  
SSBOND  12 CYS B    3    CYS B   21                          1555   1555  2.03  
SSBOND  13 CYS B   11    CYS B  425                          1555   1555  2.03  
SSBOND  14 CYS B   14    CYS B   40                          1555   1555  2.03  
SSBOND  15 CYS B   24    CYS B   51                          1555   1555  2.03  
SSBOND  16 CYS B  169    CYS B  176                          1555   1555  2.03  
SSBOND  17 CYS B  224    CYS B  264                          1555   1555  2.03  
SSBOND  18 CYS B  364    CYS B  378                          1555   1555  2.03  
SSBOND  19 CYS B  398    CYS B  423                          1555   1555  2.03  
SSBOND  20 CYS B  427    CYS B  445                          1555   1555  2.03  
SSBOND  21 CYS B  437    CYS B  448                          1555   1555  2.02  
SSBOND  22 CYS B  450    CYS B  459                          1555   1555  2.03  
SSBOND  23 CYS B  461    CYS B  492                          1555   1555  2.03  
SSBOND  24 CYS B  475    CYS B  490                          1555   1555  2.03  
SSBOND  25 CYS B  484    CYS B  495                          1555   1555  2.03  
SSBOND  26 CYS B  497    CYS B  512                          1555   1555  2.03  
SSBOND  27 CYS B  514    CYS B  537                          1555   1555  2.03  
SSBOND  28 CYS B  519    CYS B  535                          1555   1555  2.03  
SSBOND  29 CYS B  527    CYS B  540                          1555   1555  2.03  
SSBOND  30 CYS B  542    CYS B  551                          1555   1555  2.03  
SSBOND  31 CYS B  553    CYS B  576                          1555   1555  2.03  
SSBOND  32 CYS B  560    CYS B  574                          1555   1555  2.03  
SSBOND  33 CYS B  568    CYS B  579                          1555   1555  2.03  
SSBOND  34 CYS B  581    CYS B  590                          1555   1555  2.03  
SSBOND  35 CYS B  593    CYS B  596                          1555   1555  2.03  
SSBOND  36 CYS B  600    CYS B  640                          1555   1555  2.03  
SSBOND  37 CYS B  606    CYS B  625                          1555   1555  2.03  
SSBOND  38 CYS B  609    CYS B  621                          1555   1555  2.03  
SSBOND  39 CYS B  648    CYS B  673                          1555   1555  2.03  
LINK         ND2 ASN A  70                 C1  NAG D   1     1555   1555  1.43  
LINK         ND2 ASN A 373                 C1  NAG E   1     1555   1555  1.43  
LINK         ND2 ASN A 716                 C1  NAG F   1     1555   1555  1.44  
LINK         ND2 ASN A 880                 C1  NAG A1119     1555   1555  1.43  
LINK         ND2 ASN A1031                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN B  94                 C1  NAG G   1     1555   1555  1.44  
LINK         ND2 ASN B 620                 C1  NAG H   1     1555   1555  1.45  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.44  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.44  
LINK         O3  BMA E   3                 C1  MAN E   4     1555   1555  1.43  
LINK         O6  BMA E   3                 C1  MAN E   6     1555   1555  1.44  
LINK         O2  MAN E   4                 C1  MAN E   5     1555   1555  1.44  
LINK         O3  MAN E   6                 C1  MAN E   7     1555   1555  1.45  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.45  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.44  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.44  
LINK         OG  SER A 140                MG    MG A1102     1555   1555  2.12  
LINK         OG  SER A 142                MG    MG A1102     1555   1555  2.10  
LINK         OG1 THR A 207                MG    MG A1102     1555   1555  2.08  
LINK         OE1 GLU A 318                MG    MG B 703     1555   1555  2.02  
LINK         O   GLY A 352                NA    NA A1121     1555   1555  2.40  
LINK         OD1 ASP A 447                CA    CA A1104     1555   1555  2.35  
LINK         OD1 ASP A 449                CA    CA A1104     1555   1555  2.37  
LINK         OD1 ASP A 451                CA    CA A1104     1555   1555  2.29  
LINK         OD2 ASP A 451                CA    CA A1104     1555   1555  2.39  
LINK         O   SER A 453                CA    CA A1104     1555   1555  2.48  
LINK         OD1 ASP A 455                CA    CA A1104     1555   1555  2.34  
LINK         OD2 ASP A 455                CA    CA A1104     1555   1555  2.94  
LINK         OD1 ASP A 511                CA    CA A1103     1555   1555  2.38  
LINK         OD1 ASN A 513                CA    CA A1103     1555   1555  2.35  
LINK         OD1 ASP A 515                CA    CA A1103     1555   1555  2.36  
LINK         O   LEU A 517                CA    CA A1103     1555   1555  2.11  
LINK         OD1 ASP A 519                CA    CA A1103     1555   1555  2.34  
LINK         OD2 ASP A 519                CA    CA A1103     1555   1555  2.38  
LINK         OD1 ASP A 574                CA    CA A1101     1555   1555  2.36  
LINK         OG1 THR A 576                CA    CA A1101     1555   1555  2.35  
LINK         OD1 ASP A 578                CA    CA A1101     1555   1555  2.32  
LINK         OD2 ASP A 578                CA    CA A1101     1555   1555  3.03  
LINK         O   LEU A 580                CA    CA A1101     1555   1555  2.32  
LINK         OD1 ASP A 582                CA    CA A1101     1555   1555  2.31  
LINK         OD2 ASP A 582                CA    CA A1101     1555   1555  2.39  
LINK        CA    CA A1101                 O   HOH A1204     1555   1555  2.38  
LINK        MG    MG A1102                 O   HOH A1245     1555   1555  2.07  
LINK        MG    MG A1102                 O   HOH A1268     1555   1555  2.07  
LINK        CA    CA A1103                 O   HOH A1261     1555   1555  2.43  
LINK        CA    CA A1104                 O   HOH A1311     1555   1555  2.42  
LINK         OG  SER B 114                MG    MG B 703     1555   1555  2.09  
LINK         OG  SER B 116                MG    MG B 703     1555   1555  2.09  
LINK         OD1 ASP B 120                CA    CA B 702     1555   1555  2.38  
LINK         OD2 ASP B 120                CA    CA B 702     1555   1555  2.40  
LINK         OD2 ASP B 151                CA    CA B 701     1555   1555  2.39  
LINK         OD1 ASN B 207                CA    CA B 701     1555   1555  2.34  
LINK         OD1 ASP B 209                CA    CA B 701     1555   1555  2.33  
LINK         O   ASP B 209                CA    CA B 701     1555   1555  2.44  
LINK         O   PRO B 211                CA    CA B 701     1555   1555  2.19  
LINK         OE2 GLU B 212                CA    CA B 701     1555   1555  2.37  
LINK         OE1 GLU B 212                MG    MG B 703     1555   1555  2.05  
LINK         O   GLU B 325                CA    CA B 702     1555   1555  2.38  
LINK        CA    CA B 702                 O   HOH B 809     1555   1555  2.42  
LINK        CA    CA B 702                 O   HOH B 812     1555   1555  2.36  
LINK        CA    CA B 702                 O   HOH B 860     1555   1555  2.38  
LINK        CA    CA B 702                 O   HOH B 861     1555   1555  2.34  
LINK        MG    MG B 703                 O   HOH B 801     1555   1555  2.06  
LINK        MG    MG B 703                 O   HOH B 821     1555   1555  2.08  
CISPEP   1 LEU A  119    PRO A  120          0        -3.41                     
CISPEP   2 ARG A  164    PRO A  165          0        -1.41                     
CISPEP   3 LYS A  288    PRO A  289          0        -0.65                     
CISPEP   4 ILE A  609    PRO A  610          0         3.11                     
CISPEP   5 SER B   77    PRO B   78          0        -0.66                     
CISPEP   6 LEU B  155    PRO B  156          0         0.91                     
CISPEP   7 LEU B  587    PRO B  588          0         2.48                     
CRYST1  126.967  131.444  190.477  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      0.007876  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007608  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005250        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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