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Database: PDB
Entry: 4NEN
LinkDB: 4NEN
Original site: 4NEN 
HEADER    CELL ADHESION                           29-OCT-13   4NEN              
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_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK-293;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE CELL LINES;                    
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: ET10;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ITGB2, CD18, MFI7;                                             
SOURCE  16 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK-293;                                
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE CELL LINES;                    
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PEF-PURO                                  
KEYWDS    COMPLEMENT RECEPTOR, IC3B, FIBRINOGEN, DENATURATED PROTEINS, HEPARIN, 
KEYWDS   2 ICAM, N-LINKED GLYCOSYLATION, MEMBRANE, CELL ADHESION                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SEN,K.YUKI,T.A.SPRINGER                                             
REVDAT   2   29-JUL-20 4NEN    1       COMPND REMARK SEQADV HETNAM              
REVDAT   2 2                   1       LINK   SITE   ATOM                       
REVDAT   1   15-JAN-14 4NEN    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.    2.90 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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 61856                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3117                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.8151 -  8.1167    0.95     2752   136  0.1823 0.2136        
REMARK   3     2  8.1167 -  6.4475    0.99     2733   134  0.1974 0.2314        
REMARK   3     3  6.4475 -  5.6339    0.99     2698   151  0.1951 0.2356        
REMARK   3     4  5.6339 -  5.1194    0.99     2724   132  0.1698 0.2128        
REMARK   3     5  5.1194 -  4.7529    0.99     2699   128  0.1536 0.1985        
REMARK   3     6  4.7529 -  4.4729    0.99     2667   159  0.1570 0.1927        
REMARK   3     7  4.4729 -  4.2490    1.00     2666   153  0.1675 0.2121        
REMARK   3     8  4.2490 -  4.0641    1.00     2672   143  0.1892 0.2252        
REMARK   3     9  4.0641 -  3.9078    1.00     2670   152  0.2089 0.2760        
REMARK   3    10  3.9078 -  3.7730    1.00     2668   139  0.2318 0.2664        
REMARK   3    11  3.7730 -  3.6550    0.99     2672   128  0.2426 0.2670        
REMARK   3    12  3.6550 -  3.5506    1.00     2656   132  0.2562 0.2831        
REMARK   3    13  3.5506 -  3.4571    1.00     2673   143  0.2727 0.3231        
REMARK   3    14  3.4571 -  3.3728    1.00     2669   155  0.2840 0.3592        
REMARK   3    15  3.3728 -  3.2962    1.00     2647   150  0.2927 0.3217        
REMARK   3    16  3.2962 -  3.2260    1.00     2634   138  0.3214 0.3536        
REMARK   3    17  3.2260 -  3.1615    1.00     2645   143  0.3388 0.3746        
REMARK   3    18  3.1615 -  3.1019    1.00     2664   149  0.3501 0.3922        
REMARK   3    19  3.1019 -  3.0465    1.00     2659   127  0.3552 0.4428        
REMARK   3    20  3.0465 -  2.9948    1.00     2646   141  0.3688 0.3894        
REMARK   3    21  2.9948 -  2.9465    1.00     2635   160  0.3961 0.3914        
REMARK   3    22  2.9465 -  2.9012    0.97     2590   124  0.4081 0.4362        
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)     : 0.580            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.020           
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      :  0.005          13983                                  
REMARK   3   ANGLE     :  0.765          18982                                  
REMARK   3   CHIRALITY :  0.030           2135                                  
REMARK   3   PLANARITY :  0.003           2466                                  
REMARK   3   DIHEDRAL  : 10.968           5133                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 1:124)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -48.6651  11.1890  55.7419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5029 T22:   0.4477                                     
REMARK   3      T33:   0.8230 T12:   0.0921                                     
REMARK   3      T13:   0.0747 T23:   0.0746                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6706 L22:   0.4962                                     
REMARK   3      L33:   0.8477 L12:  -0.2069                                     
REMARK   3      L13:  -0.6384 L23:   0.3908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1680 S12:   0.0671 S13:  -0.5592                       
REMARK   3      S21:   0.2935 S22:   0.2023 S23:  -0.5526                       
REMARK   3      S31:   0.1570 S32:   0.1482 S33:   0.0050                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 129:310)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2032  25.5222  31.8371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4858 T22:   0.7564                                     
REMARK   3      T33:   0.8495 T12:   0.0588                                     
REMARK   3      T13:   0.1025 T23:   0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0206 L22:   1.4446                                     
REMARK   3      L33:   1.7227 L12:  -0.2480                                     
REMARK   3      L13:  -0.5296 L23:  -0.7918                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1928 S12:  -0.0136 S13:   0.1396                       
REMARK   3      S21:   0.1376 S22:  -0.1427 S23:  -0.3341                       
REMARK   3      S31:  -0.3018 S32:  -0.0667 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 311:334)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -39.1405  37.8084  44.3347              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6066 T22:   0.5404                                     
REMARK   3      T33:   0.5343 T12:   0.0066                                     
REMARK   3      T13:   0.0441 T23:   0.0839                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0207 L22:   0.0540                                     
REMARK   3      L33:   0.0079 L12:  -0.0282                                     
REMARK   3      L13:  -0.0352 L23:   0.0493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2222 S12:  -0.3612 S13:  -0.2302                       
REMARK   3      S21:  -0.2265 S22:  -0.5705 S23:  -0.5429                       
REMARK   3      S31:  -0.4627 S32:   0.2605 S33:  -0.0009                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 336:596)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -65.1225  20.6850  49.0056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4351 T22:   0.4203                                     
REMARK   3      T33:   0.4403 T12:   0.0340                                     
REMARK   3      T13:   0.0355 T23:   0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0060 L22:   1.2395                                     
REMARK   3      L33:   0.6784 L12:   0.2192                                     
REMARK   3      L13:  -0.3918 L23:  -0.2518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1873 S12:   0.1402 S13:  -0.1401                       
REMARK   3      S21:   0.0323 S22:   0.2072 S23:   0.2716                       
REMARK   3      S31:  -0.0724 S32:  -0.0904 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 600:750)                         
REMARK   3    ORIGIN FOR THE GROUP (A):-101.5483  -5.2158  66.5308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7678 T22:   0.7750                                     
REMARK   3      T33:   1.0910 T12:  -0.0241                                     
REMARK   3      T13:   0.2759 T23:   0.3915                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5845 L22:   0.4614                                     
REMARK   3      L33:   1.0306 L12:  -0.0958                                     
REMARK   3      L13:   0.1672 L23:  -0.1838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0408 S12:  -0.3879 S13:  -1.2382                       
REMARK   3      S21:   0.2423 S22:   0.0398 S23:  -0.1332                       
REMARK   3      S31:   0.0836 S32:  -0.2835 S33:   0.1861                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 758:902)                         
REMARK   3    ORIGIN FOR THE GROUP (A):-109.6672   8.3221  42.3506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4864 T22:   0.9435                                     
REMARK   3      T33:   0.7155 T12:  -0.0545                                     
REMARK   3      T13:   0.0453 T23:   0.3342                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8039 L22:   0.0481                                     
REMARK   3      L33:   1.4273 L12:  -0.1288                                     
REMARK   3      L13:  -0.2501 L23:  -0.3022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6272 S12:  -0.2222 S13:  -0.2904                       
REMARK   3      S21:  -0.6039 S22:   0.4126 S23:   0.1340                       
REMARK   3      S31:   0.5572 S32:  -0.3923 S33:  -0.0224                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 903:1082)                        
REMARK   3    ORIGIN FOR THE GROUP (A): -79.1300  26.0549   4.8586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6645 T22:   0.6149                                     
REMARK   3      T33:   0.5411 T12:  -0.1468                                     
REMARK   3      T13:  -0.0670 T23:   0.0989                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0295 L22:   0.1473                                     
REMARK   3      L33:   1.5354 L12:   0.3450                                     
REMARK   3      L13:  -0.4763 L23:  -0.6520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1819 S12:   0.0629 S13:  -0.1372                       
REMARK   3      S21:   0.0169 S22:   0.1312 S23:   0.1198                       
REMARK   3      S31:   0.0103 S32:  -0.0677 S33:  -0.0001                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 1:56)                            
REMARK   3    ORIGIN FOR THE GROUP (A):-116.6914  35.1904  73.1277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9992 T22:   1.2462                                     
REMARK   3      T33:   1.4729 T12:  -0.0048                                     
REMARK   3      T13:   0.3228 T23:   0.1384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1704 L22:   0.4089                                     
REMARK   3      L33:   0.3533 L12:   0.1491                                     
REMARK   3      L13:   0.0615 L23:   0.0334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3562 S12:   0.2328 S13:   1.0734                       
REMARK   3      S21:  -0.0518 S22:  -0.3098 S23:   0.1796                       
REMARK   3      S31:   0.4399 S32:   0.2267 S33:  -0.4500                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 57:123)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -76.0252  52.6564  71.7441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6681 T22:   0.5179                                     
REMARK   3      T33:   0.5343 T12:   0.0803                                     
REMARK   3      T13:   0.3894 T23:  -0.0465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4129 L22:   0.6960                                     
REMARK   3      L33:   0.2076 L12:  -0.3226                                     
REMARK   3      L13:   0.2582 L23:  -0.0410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3272 S12:  -0.4129 S13:   0.9208                       
REMARK   3      S21:   0.6436 S22:   0.3780 S23:   0.2046                       
REMARK   3      S31:   0.1428 S32:   0.0323 S33:  -0.0995                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 128:329)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -51.9771  46.3828  64.5496              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5016 T22:   0.4311                                     
REMARK   3      T33:   0.2857 T12:   0.0844                                     
REMARK   3      T13:  -0.0213 T23:  -0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0598 L22:   1.4752                                     
REMARK   3      L33:   0.6778 L12:  -0.5696                                     
REMARK   3      L13:  -0.1434 L23:   0.9402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1055 S12:  -0.0991 S13:   0.1645                       
REMARK   3      S21:   0.4729 S22:   0.2228 S23:  -0.2405                       
REMARK   3      S31:   0.0237 S32:   0.0678 S33:   0.0001                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 330:423)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -82.3341  50.1403  68.6158              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6397 T22:   0.5129                                     
REMARK   3      T33:   0.6309 T12:   0.1457                                     
REMARK   3      T13:   0.1728 T23:   0.1004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4648 L22:   0.0324                                     
REMARK   3      L33:   0.0679 L12:   0.4972                                     
REMARK   3      L13:  -0.0477 L23:   0.4033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0493 S12:   0.2386 S13:   0.4958                       
REMARK   3      S21:   0.5410 S22:   0.1962 S23:   0.5573                       
REMARK   3      S31:  -0.2264 S32:  -0.1151 S33:  -0.0012                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 426:460)                         
REMARK   3    ORIGIN FOR THE GROUP (A):-118.8440  25.2744  86.4337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3482 T22:   1.6314                                     
REMARK   3      T33:   1.0232 T12:   0.0029                                     
REMARK   3      T13:   0.7060 T23:  -0.1651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2436 L22:   0.0629                                     
REMARK   3      L33:   0.1228 L12:  -0.0815                                     
REMARK   3      L13:  -0.1624 L23:   0.0476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1488 S12:  -0.4083 S13:   0.2939                       
REMARK   3      S21:   0.5196 S22:  -0.3620 S23:   0.3548                       
REMARK   3      S31:   0.0401 S32:  -0.3936 S33:  -0.0496                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 461:513)                         
REMARK   3    ORIGIN FOR THE GROUP (A):-119.2369  14.7018  70.1683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8814 T22:   1.2036                                     
REMARK   3      T33:   1.3064 T12:   0.1367                                     
REMARK   3      T13:   0.3517 T23:   0.2580                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5033 L22:   0.2377                                     
REMARK   3      L33:   1.4717 L12:   0.0323                                     
REMARK   3      L13:   0.2477 L23:   0.1934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0287 S12:  -0.1619 S13:   0.1569                       
REMARK   3      S21:  -0.3635 S22:   0.1069 S23:  -0.0828                       
REMARK   3      S31:   0.2340 S32:  -0.8230 S33:   0.1297                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 514:552)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -99.1013  25.4648  57.6280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2009 T22:   1.6062                                     
REMARK   3      T33:   1.3052 T12:  -0.1533                                     
REMARK   3      T13:   0.4886 T23:   0.2736                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0912 L22:   0.0798                                     
REMARK   3      L33:   0.0117 L12:  -0.0863                                     
REMARK   3      L13:   0.0567 L23:  -0.0226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4590 S12:  -0.3173 S13:   0.5063                       
REMARK   3      S21:  -0.2410 S22:   0.4489 S23:   0.4131                       
REMARK   3      S31:  -0.2770 S32:   0.5366 S33:   0.0018                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 553:592)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -86.5225  38.0808  39.5186              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2711 T22:   0.9579                                     
REMARK   3      T33:   1.6260 T12:  -0.4293                                     
REMARK   3      T13:   0.3814 T23:   0.0596                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0199 L22:  -0.0255                                     
REMARK   3      L33:   0.2169 L12:  -0.0007                                     
REMARK   3      L13:   0.0274 L23:  -0.0388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4400 S12:  -0.7324 S13:  -0.2535                       
REMARK   3      S21:   0.7990 S22:  -1.0091 S23:  -0.6355                       
REMARK   3      S31:   0.4020 S32:   0.5414 S33:  -0.0205                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 593:597)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -83.8442  33.5021  22.9114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2318 T22:   0.7597                                     
REMARK   3      T33:   1.5947 T12:  -0.1590                                     
REMARK   3      T13:  -0.0748 T23:  -0.1892                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0139 L22:   0.0198                                     
REMARK   3      L33:   0.0905 L12:  -0.0051                                     
REMARK   3      L13:   0.0326 L23:  -0.0101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0684 S12:   0.3019 S13:   0.2144                       
REMARK   3      S21:   0.2669 S22:   0.0070 S23:   0.0108                       
REMARK   3      S31:   0.1550 S32:   0.0065 S33:   0.0003                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 598:674)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -78.8313  50.2070  14.7896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8399 T22:   0.7137                                     
REMARK   3      T33:   1.1877 T12:  -0.0609                                     
REMARK   3      T13:  -0.0226 T23:  -0.1713                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3824 L22:   0.4508                                     
REMARK   3      L33:   0.4039 L12:   0.0127                                     
REMARK   3      L13:  -0.1472 L23:   0.5011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0805 S12:   0.0383 S13:  -0.1900                       
REMARK   3      S21:   0.0664 S22:  -0.0546 S23:   0.5526                       
REMARK   3      S31:  -0.1632 S32:  -0.3174 S33:   0.0002                       
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 4NEN 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_1000083106.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03329                            
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   : 61864                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
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     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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 ENTRY 3K6S                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61                     
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       63.54350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       91.19950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.92550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       91.19950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       63.54350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.92550            
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: 11630 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 79650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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     LYS A   750                                                      
REMARK 465     ASN A   751                                                      
REMARK 465     CYS A   752                                                      
REMARK 465     GLY A   753                                                      
REMARK 465     ALA A   754                                                      
REMARK 465     ASP A   755                                                      
REMARK 465     HIS A   756                                                      
REMARK 465     ILE A   757                                                      
REMARK 465     CYS A   758                                                      
REMARK 465     GLN A   759                                                      
REMARK 465     GLU A   815                                                      
REMARK 465     GLY A   816                                                      
REMARK 465     GLN A   817                                                      
REMARK 465     LYS A   818                                                      
REMARK 465     GLN A   819                                                      
REMARK 465     GLY A   820                                                      
REMARK 465     GLN A   821                                                      
REMARK 465     LEU A   822                                                      
REMARK 465     ARG A   823                                                      
REMARK 465     SER A   824                                                      
REMARK 465     GLY A  1084                                                      
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     ASP B   433                                                      
REMARK 465     ARG B   434                                                      
REMARK 465     SER B   435                                                      
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     ARG B 426    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 428    O    CB   CG   CD   NE   CZ   NH1                   
REMARK 470     ARG B 428    NH2                                                 
REMARK 470     GLY B 676    C    O                                              
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 543   C   -  N   -  CA  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    PRO A 888   N   -  CA  -  CB  ANGL. DEV. =   7.4 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    SER A  28      -49.98   -135.81                                   
REMARK 500    SER A  82       70.75     52.31                                   
REMARK 500    SER A 145     -101.53     47.37                                   
REMARK 500    PRO A 165       37.08    -93.07                                   
REMARK 500    SER A 175     -104.63   -155.87                                   
REMARK 500    GLN A 204     -150.86     54.99                                   
REMARK 500    ARG A 219      -69.09   -130.51                                   
REMARK 500    PHE A 221       77.95   -103.55                                   
REMARK 500    GLU A 329      -81.34   -123.08                                   
REMARK 500    PHE A 354       72.47     51.89                                   
REMARK 500    TYR A 363       76.01   -117.11                                   
REMARK 500    LYS A 396     -119.82     56.74                                   
REMARK 500    PRO A 479       60.47    -69.22                                   
REMARK 500    GLU A 528       73.68     27.46                                   
REMARK 500    PRO A 543      105.24     -6.72                                   
REMARK 500    ARG A 561       -0.07     62.22                                   
REMARK 500    GLU A 619      116.48   -164.53                                   
REMARK 500    LYS A 677       -9.33     85.32                                   
REMARK 500    THR A 678     -140.33   -128.15                                   
REMARK 500    LEU A 689     -166.81    -74.08                                   
REMARK 500    LYS A 690     -123.35     55.07                                   
REMARK 500    LEU A 725      -37.86     64.12                                   
REMARK 500    PRO A 805      173.28    -58.74                                   
REMARK 500    ASN A 847     -157.94   -133.64                                   
REMARK 500    HIS A 848       -1.73     74.30                                   
REMARK 500    ARG A 889     -160.98     57.35                                   
REMARK 500    LYS A 892     -137.08     52.04                                   
REMARK 500    ASN A 974       65.00     34.46                                   
REMARK 500    PRO A 975       45.17    -89.02                                   
REMARK 500    PRO A 999       70.99    -65.40                                   
REMARK 500    GLN A1021       -1.55     65.56                                   
REMARK 500    PHE B   6      -80.66   -137.95                                   
REMARK 500    GLN B  75      -60.47   -109.20                                   
REMARK 500    VAL B 150      -80.18   -128.96                                   
REMARK 500    SER B 205     -164.12   -123.33                                   
REMARK 500    ASN B 207     -169.44   -161.79                                   
REMARK 500    ASN B 384       -0.66     63.95                                   
REMARK 500    CYS B 427      140.30    -38.42                                   
REMARK 500    SER B 467       81.66     50.23                                   
REMARK 500    GLU B 470        2.05     59.62                                   
REMARK 500    ASN B 523     -135.65     56.42                                   
REMARK 500    PRO B 530       41.11    -75.03                                   
REMARK 500    ARG B 555     -118.31     29.92                                   
REMARK 500    THR B 556     -159.39   -138.38                                   
REMARK 500    GLU B 567       90.64     62.58                                   
REMARK 500    SER B 569     -135.15     54.05                                   
REMARK 500    ASN B 577       -4.75     63.62                                   
REMARK 500    SER B 583     -145.35     57.77                                   
REMARK 500    GLU B 613       -8.53     61.82                                   
REMARK 500    LYS B 619      -10.10     93.67                                   
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 A1116  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 140   OG                                                     
REMARK 620 2 SER A 142   OG   92.8                                              
REMARK 620 3 THR A 207   OG1  80.3 170.6                                        
REMARK 620 4 HOH A1205   O    90.7  86.5  87.2                                  
REMARK 620 5 HOH A1218   O   156.1 108.0  77.6  79.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 707  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 318   OE1                                                    
REMARK 620 2 SER B 114   OG   68.3                                              
REMARK 620 3 SER B 116   OG   77.6  84.0                                        
REMARK 620 4 GLU B 212   OE2  78.5  79.0 154.6                                  
REMARK 620 5 HOH B 806   O   153.7  88.0 112.1  86.2                            
REMARK 620 6 HOH B 807   O   101.1 148.4 123.9  69.6  93.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1115  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 447   OD1                                                    
REMARK 620 2 ASP A 449   OD1  87.2                                              
REMARK 620 3 ASP A 451   OD1  85.5  71.8                                        
REMARK 620 4 SER A 453   O    69.8 152.0  90.0                                  
REMARK 620 5 ASP A 455   OD1 124.1 126.7 142.2  80.7                            
REMARK 620 6 ASP A 455   OD2  90.5  83.5 155.1 111.6  57.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1113  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 511   OD1                                                    
REMARK 620 2 ASN A 513   OD1  74.8                                              
REMARK 620 3 ASP A 515   OD1  78.3  79.1                                        
REMARK 620 4 LEU A 517   O    94.6 157.8  79.7                                  
REMARK 620 5 ASP A 519   OD2  95.4  93.9 171.5 106.7                            
REMARK 620 6 ASP A 519   OD1 151.0 104.4 130.6  94.3  55.6                      
REMARK 620 7 HOH A1219   O   137.4  99.2  59.4  75.1 127.1  71.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1114  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 574   OD1                                                    
REMARK 620 2 THR A 576   OG1  99.1                                              
REMARK 620 3 ASP A 578   OD1 103.5  82.6                                        
REMARK 620 4 LEU A 580   O    97.1 153.6 113.5                                  
REMARK 620 5 ASP A 582   OD2  80.6  79.6 162.2  82.7                            
REMARK 620 6 ASP A 582   OD1 126.8  67.1 123.4  86.6  47.1                      
REMARK 620 7 HOH A1225   O   175.1  78.2  72.2  86.9 102.7  55.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 706  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 116   O                                                      
REMARK 620 2 ASP B 242   OD2  72.0                                              
REMARK 620 3 HOH B 809   O   130.9 110.7                                        
REMARK 620 4 HOH B 810   O   122.7 138.2  88.9                                  
REMARK 620 5 HOH B 834   O    80.0  80.2  53.8 137.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 705  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 151   OD2                                                    
REMARK 620 2 ASN B 207   OD1  89.8                                              
REMARK 620 3 ASP B 209   OD1  91.0 102.0                                        
REMARK 620 4 ASP B 209   O   159.2 100.1  69.2                                  
REMARK 620 5 PRO B 211   O    82.5 171.0  83.0  88.7                            
REMARK 620 6 GLU B 212   OE1 100.1  82.7 168.1  99.3  93.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4NEH   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN CRYSTAL BUT DEHYDRATED                              
REMARK 900 RELATED ID: 3K6S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3K71   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3K72   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2IUE   RELATED DB: PDB                                   
REMARK 900 HOMOLOG                                                              
DBREF  4NEN A    1  1082  UNP    P20702   ITAX_HUMAN      20   1101             
DBREF  4NEN B    1   674  UNP    P05107   ITB2_HUMAN      23    696             
SEQADV 4NEN ASP A   42  UNP  P20702    ASN    61 ENGINEERED MUTATION            
SEQADV 4NEN ASP A  368  UNP  P20702    SER   387 ENGINEERED MUTATION            
SEQADV 4NEN THR A  678  UNP  P20702    ASN   697 ENGINEERED MUTATION            
SEQADV 4NEN SER A  885  UNP  P20702    ASN   904 ENGINEERED MUTATION            
SEQADV 4NEN CYS A  920  UNP  P20702    ASN   939 ENGINEERED MUTATION            
SEQADV 4NEN PRO A 1083  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN GLY A 1084  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN PRO A 1085  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN ALA A 1086  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN ALA A 1087  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN LEU A 1088  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN GLN A 1089  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN THR A 1090  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN LEU A 1091  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN PHE A 1092  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN GLN A 1093  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN GLY A 1094  UNP  P20702              EXPRESSION TAG                 
SEQADV 4NEN ASP B  190  UNP  P05107    ASN   212 ENGINEERED MUTATION            
SEQADV 4NEN LYS B  232  UNP  P05107    ASN   254 ENGINEERED MUTATION            
SEQADV 4NEN CYS B  674  UNP  P05107    VAL   696 ENGINEERED MUTATION            
SEQADV 4NEN GLY B  675  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN GLY B  676  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN PRO B  677  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN ALA B  678  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN ALA B  679  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN LEU B  680  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN GLN B  681  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN THR B  682  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN LEU B  683  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN PHE B  684  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN GLN B  685  UNP  P05107              EXPRESSION TAG                 
SEQADV 4NEN 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 4NEN ASN A  716  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEN ASN B   94  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEN ASN B  620  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEN ASN A  373  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEN ASN A   70  ASN  GLYCOSYLATION SITE                                 
MODRES 4NEN ASN A 1031  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
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    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  A1113       1                                                       
HET     CA  A1114       1                                                       
HET     CA  A1115       1                                                       
HET     MG  A1116       1                                                       
HET     CL  A1117       1                                                       
HET     CA  B 705       1                                                       
HET     CA  B 706       1                                                       
HET     MG  B 707       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                                                     
FORMUL   3  NAG    12(C8 H15 N O6)                                              
FORMUL   5  BMA    C6 H12 O6                                                    
FORMUL   5  MAN    3(C6 H12 O6)                                                 
FORMUL   9   CA    5(CA 2+)                                                     
FORMUL  12   MG    2(MG 2+)                                                     
FORMUL  13   CL    CL 1-                                                        
FORMUL  17  HOH   *128(H2 O)                                                    
HELIX    1   1 SER A  145  SER A  160  1                                  16    
HELIX    2   2 THR A  183  SER A  190  1                                   8    
HELIX    3   3 ASN A  192  VAL A  200  5                                   9    
HELIX    4   4 TYR A  208  HIS A  218  1                                  11    
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 PHE A  300  GLN A  307  1                                   8    
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 SER B   10  GLY B   18  1                                   9    
HELIX   21  21 PRO B   35  ILE B   38  5                                   4    
HELIX   22  22 THR B   42  MET B   48  1                                   7    
HELIX   23  23 SER B  114  SER B  116  5                                   3    
HELIX   24  24 MET B  117  THR B  139  1                                  23    
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  ARG B  344  1                                  16    
HELIX   35  35 LEU B  471  CYS B  475  5                                   5    
HELIX   36  36 ILE B  482  GLY B  486  5                                   5    
HELIX   37  37 SER B  598  LYS B  602  5                                   5    
HELIX   38  38 TYR B  603  GLU B  613  1                                  11    
HELIX   39  39 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  LEU A 583   O  LEU A 594           
SHEET    4   A 4 LEU A 569  GLN A 573 -1  N  SER A 570   O  ALA A 584           
SHEET    1   B 4 VAL A  22  TYR A  25  0                                        
SHEET    2   B 4 TRP A  29  ALA A  40 -1  O  TRP A  29   N  TYR A  25           
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 LEU A  77  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  LEU A 110   N  LEU A  86           
SHEET    4   C 4 GLN A 117  LEU A 119 -1  O  LEU A 119   N  CYS A 107           
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  LEU A 136           
SHEET    5   D 6 ILE A 263  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  GLY A 349   N  SER A 338           
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  TRP A 395  0                                        
SHEET    2   F 4 VAL A 398  ALA A 405 -1  O  SER A 400   N  ALA A 393           
SHEET    3   F 4 LYS A 413  GLN A 419 -1  O  PHE A 417   N  LEU A 401           
SHEET    4   F 4 TRP A 424  THR A 431 -1  O  LYS A 427   N  ILE A 416           
SHEET    1   G 4 LEU A 443  VAL A 446  0                                        
SHEET    2   G 4 LEU A 456  GLY A 460 -1  O  LEU A 458   N  CYS A 444           
SHEET    3   G 4 VAL A 473  PRO A 477 -1  O  CYS A 476   N  VAL A 457           
SHEET    4   G 4 ALA A 489  LEU A 491 -1  O  LEU A 491   N  VAL A 473           
SHEET    1   H 2 ARG A 469  GLY A 471  0                                        
SHEET    2   H 2 HIS A 497  PHE A 502  1  O  HIS A 497   N  GLY A 470           
SHEET    1   I 4 LEU A 506  VAL A 508  0                                        
SHEET    2   I 4 VAL A 520  GLY A 523 -1  O  VAL A 521   N  THR A 507           
SHEET    3   I 4 ALA A 533  PHE A 537 -1  O  TYR A 535   N  ILE A 522           
SHEET    4   I 4 GLN A 551  ALA A 554 -1  O  ILE A 553   N  VAL A 534           
SHEET    1   J 2 GLY A 539  VAL A 540  0                                        
SHEET    2   J 2 SER A 544  ILE A 545 -1  O  SER A 544   N  VAL A 540           
SHEET    1   K 5 THR A 672  PHE A 673  0                                        
SHEET    2   K 5 LYS A 690  LEU A 700 -1  O  LEU A 699   N  THR A 672           
SHEET    3   K 5 THR A 629  LYS A 641 -1  N  VAL A 631   O  LEU A 698           
SHEET    4   K 5 VAL A 599  ILE A 609 -1  N  ILE A 609   O  GLN A 632           
SHEET    5   K 5 MET A 733  LEU A 734  1  O  MET A 733   N  LEU A 600           
SHEET    1   L 4 SER A 680  LEU A 687  0                                        
SHEET    2   L 4 SER A 654  LEU A 662 -1  N  SER A 654   O  LEU A 687           
SHEET    3   L 4 ILE A 711  GLY A 721 -1  O  VAL A 720   N  SER A 655           
SHEET    4   L 4 PHE A 742  LEU A 746 -1  O  LEU A 746   N  ILE A 711           
SHEET    1   M 4 LEU A 762  SER A 767  0                                        
SHEET    2   M 4 GLU A 781  ASN A 790 -1  O  MET A 787   N  SER A 765           
SHEET    3   M 4 GLN A 856  VAL A 865 -1  O  PHE A 863   N  LEU A 782           
SHEET    4   M 4 LEU A 808  ARG A 811 -1  N  SER A 809   O  ASP A 864           
SHEET    1   N 6 LEU A 774  VAL A 776  0                                        
SHEET    2   N 6 PHE A 895  VAL A 905  1  O  PRO A 900   N  LEU A 774           
SHEET    3   N 6 ARG A 874  ALA A 879 -1  N  ALA A 879   O  PHE A 895           
SHEET    4   N 6 THR A 798  PRO A 805 -1  N  SER A 803   O  THR A 878           
SHEET    5   N 6 THR A 839  ILE A 846 -1  O  TRP A 840   N  HIS A 804           
SHEET    6   N 6 THR A 828  PRO A 833 -1  N  ALA A 832   O  SER A 841           
SHEET    1   O 3 LEU A 774  VAL A 776  0                                        
SHEET    2   O 3 PHE A 895  VAL A 905  1  O  PRO A 900   N  LEU A 774           
SHEET    3   O 3 TYR A1060  GLN A1062  1  O  SER A1061   N  TYR A 903           
SHEET    1   P 4 THR A 907  SER A 911  0                                        
SHEET    2   P 4 SER A 929  ASN A 940 -1  O  ASN A 939   N  VAL A 908           
SHEET    3   P 4 GLU A1023  SER A1033 -1  O  LEU A1028   N  HIS A 934           
SHEET    4   P 4 TRP A 964  SER A 970 -1  N  MET A 965   O  ASN A1031           
SHEET    1   Q 6 TYR A 918  PHE A 921  0                                        
SHEET    2   Q 6 ARG A1071  LYS A1080  1  O  VAL A1077   N  LEU A 919           
SHEET    3   Q 6 LYS A1044  PHE A1055 -1  N  VAL A1045   O  LEU A1078           
SHEET    4   Q 6 LEU A 946  LEU A 958 -1  N  TRP A 953   O  VAL A1050           
SHEET    5   Q 6 GLY A1007  PHE A1018 -1  O  CYS A1013   N  ILE A 950           
SHEET    6   Q 6 CYS A 979  ILE A 984 -1  N  GLU A 982   O  ARG A1010           
SHEET    1   R 4 GLU A 961  ALA A 962  0                                        
SHEET    2   R 4 LEU A 946  LEU A 958 -1  N  LEU A 958   O  GLU A 961           
SHEET    3   R 4 LYS A1044  PHE A1055 -1  O  VAL A1050   N  TRP A 953           
SHEET    4   R 4 VAL A1000  LEU A1001  1  N  LEU A1001   O  SER A1046           
SHEET    1   S 3 CYS B  40  ASP B  41  0                                        
SHEET    2   S 3 THR B  22  CYS B  24 -1  N  THR B  22   O  ASP B  41           
SHEET    3   S 3 ILE B  56  MET B  57 -1  O  MET B  57   N  TRP B  23           
SHEET    1   T 6 LEU B  62  THR B  65  0                                        
SHEET    2   T 6 LYS B  80  LEU B  85 -1  O  TYR B  84   N  LEU B  62           
SHEET    3   T 6 ILE B 414  PRO B 421  1  O  GLN B 418   N  VAL B  81           
SHEET    4   T 6 GLN B 402  ALA B 408 -1  N  ILE B 406   O  VAL B 415           
SHEET    5   T 6 VAL B 345  HIS B 349 -1  N  ASP B 348   O  ARG B 407           
SHEET    6   T 6 GLY B 376  CYS B 378 -1  O  CYS B 378   N  VAL B 345           
SHEET    1   U 5 LEU B  76  SER B  77  0                                        
SHEET    2   U 5 ALA B  91  PHE B  97 -1  O  THR B  96   N  SER B  77           
SHEET    3   U 5 ILE B 387  ALA B 395 -1  O  ILE B 387   N  PHE B  97           
SHEET    4   U 5 LEU B 356  PHE B 363 -1  N  ASP B 361   O  GLN B 390           
SHEET    5   U 5 THR B 369  GLN B 373 -1  O  GLN B 373   N  TYR B 360           
SHEET    1   V 6 PHE B 182  THR B 189  0                                        
SHEET    2   V 6 ARG B 143  PHE B 149 -1  N  SER B 148   O  ARG B 183           
SHEET    3   V 6 ILE B 105  ASP B 112  1  N  LEU B 107   O  ARG B 143           
SHEET    4   V 6 THR B 234  THR B 241  1  O  LEU B 236   N  ASP B 106           
SHEET    5   V 6 ILE B 294  VAL B 300  1  O  ILE B 297   N  LEU B 237           
SHEET    6   V 6 ALA B 319  GLU B 322  1  O  ALA B 319   N  PHE B 298           
SHEET    1   W 2 GLY B 441  GLU B 444  0                                        
SHEET    2   W 2 ILE B 447  CYS B 450 -1  O  ILE B 447   N  GLU B 444           
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 ILE B 507  TYR B 508  0                                        
SHEET    2   Y 2 CYS B 514  ASP B 515 -1  O  CYS B 514   N  TYR B 508           
SHEET    1   Z 2 ARG B 521  TYR B 522  0                                        
SHEET    2   Z 2 GLN B 525  VAL B 526 -1  O  GLN B 525   N  TYR B 522           
SHEET    1  AA 2 GLY B 533  PHE B 536  0                                        
SHEET    2  AA 2 LYS B 539  CYS B 542 -1  O  LYS B 539   N  PHE B 536           
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 TYR B 663  VAL B 667  1  O  ILE B 665   N  SER B 631           
SHEET    3  AC 4 TRP B 649  GLN B 656 -1  N  GLU B 655   O  LEU B 664           
SHEET    4  AC 4 ARG B 638  ARG B 643 -1  N  GLU B 642   O  VAL B 650           
SSBOND   1 CYS A   89    CYS A  107                          1555   1555  2.04  
SSBOND   2 CYS A   97    CYS A  126                          1555   1555  2.03  
SSBOND   3 CYS A  476    CYS A  487                          1555   1555  2.03  
SSBOND   4 CYS A  620    CYS A  703                          1555   1555  2.02  
SSBOND   5 CYS A  636    CYS A  693                          1555   1555  2.03  
SSBOND   6 CYS A  829    CYS A  844                          1555   1555  2.03  
SSBOND   7 CYS A  920    CYS B  674                          1555   1555  2.03  
SSBOND   8 CYS A  979    CYS A 1013                          1555   1555  2.03  
SSBOND   9 CYS A 1003    CYS A 1008                          1555   1555  2.03  
SSBOND  10 CYS B    3    CYS B   21                          1555   1555  2.03  
SSBOND  11 CYS B   11    CYS B  425                          1555   1555  2.04  
SSBOND  12 CYS B   14    CYS B   40                          1555   1555  2.03  
SSBOND  13 CYS B   24    CYS B   51                          1555   1555  2.03  
SSBOND  14 CYS B  169    CYS B  176                          1555   1555  2.03  
SSBOND  15 CYS B  224    CYS B  264                          1555   1555  2.03  
SSBOND  16 CYS B  364    CYS B  378                          1555   1555  2.03  
SSBOND  17 CYS B  398    CYS B  423                          1555   1555  2.03  
SSBOND  18 CYS B  427    CYS B  445                          1555   1555  2.05  
SSBOND  19 CYS B  437    CYS B  448                          1555   1555  2.03  
SSBOND  20 CYS B  450    CYS B  459                          1555   1555  2.03  
SSBOND  21 CYS B  461    CYS B  492                          1555   1555  2.03  
SSBOND  22 CYS B  475    CYS B  490                          1555   1555  2.03  
SSBOND  23 CYS B  484    CYS B  495                          1555   1555  2.03  
SSBOND  24 CYS B  497    CYS B  512                          1555   1555  2.03  
SSBOND  25 CYS B  514    CYS B  537                          1555   1555  2.03  
SSBOND  26 CYS B  519    CYS B  535                          1555   1555  2.03  
SSBOND  27 CYS B  527    CYS B  540                          1555   1555  2.03  
SSBOND  28 CYS B  542    CYS B  551                          1555   1555  2.03  
SSBOND  29 CYS B  553    CYS B  576                          1555   1555  2.04  
SSBOND  30 CYS B  560    CYS B  574                          1555   1555  2.03  
SSBOND  31 CYS B  568    CYS B  579                          1555   1555  2.03  
SSBOND  32 CYS B  581    CYS B  590                          1555   1555  2.03  
SSBOND  33 CYS B  593    CYS B  596                          1555   1555  2.03  
SSBOND  34 CYS B  600    CYS B  640                          1555   1555  2.03  
SSBOND  35 CYS B  606    CYS B  625                          1555   1555  2.03  
SSBOND  36 CYS B  609    CYS B  621                          1555   1555  2.03  
SSBOND  37 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  1.42  
LINK         ND2 ASN A1031                 C1  NAG C   1     1555   1555  1.44  
LINK         ND2 ASN B  94                 C1  NAG G   1     1555   1555  1.43  
LINK         ND2 ASN B 620                 C1  NAG H   1     1555   1555  1.43  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.45  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.45  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.44  
LINK         O6  BMA E   3                 C1  MAN E   4     1555   1555  1.44  
LINK         O3  BMA E   3                 C1  MAN E   6     1555   1555  1.44  
LINK         O3  MAN E   4                 C1  MAN E   5     1555   1555  1.44  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.44  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.44  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.43  
LINK         OG  SER A 140                MG    MG A1116     1555   1555  2.30  
LINK         OG  SER A 142                MG    MG A1116     1555   1555  2.03  
LINK         OG1 THR A 207                MG    MG A1116     1555   1555  2.09  
LINK         OE1 GLU A 318                MG    MG B 707     1555   1555  2.09  
LINK         OD1 ASP A 447                CA    CA A1115     1555   1555  2.32  
LINK         OD1 ASP A 449                CA    CA A1115     1555   1555  2.31  
LINK         OD1 ASP A 451                CA    CA A1115     1555   1555  2.29  
LINK         O   SER A 453                CA    CA A1115     1555   1555  2.34  
LINK         OD1 ASP A 455                CA    CA A1115     1555   1555  2.29  
LINK         OD2 ASP A 455                CA    CA A1115     1555   1555  2.30  
LINK         OD1 ASP A 511                CA    CA A1113     1555   1555  2.32  
LINK         OD1 ASN A 513                CA    CA A1113     1555   1555  2.29  
LINK         OD1 ASP A 515                CA    CA A1113     1555   1555  2.38  
LINK         O   LEU A 517                CA    CA A1113     1555   1555  2.21  
LINK         OD2 ASP A 519                CA    CA A1113     1555   1555  2.33  
LINK         OD1 ASP A 519                CA    CA A1113     1555   1555  2.36  
LINK         OD1 ASP A 574                CA    CA A1114     1555   1555  2.30  
LINK         OG1 THR A 576                CA    CA A1114     1555   1555  2.36  
LINK         OD1 ASP A 578                CA    CA A1114     1555   1555  2.25  
LINK         O   LEU A 580                CA    CA A1114     1555   1555  2.04  
LINK         OD2 ASP A 582                CA    CA A1114     1555   1555  2.46  
LINK         OD1 ASP A 582                CA    CA A1114     1555   1555  2.92  
LINK        CA    CA A1113                 O   HOH A1219     1555   1555  2.37  
LINK        CA    CA A1114                 O   HOH A1225     1555   1555  2.38  
LINK        MG    MG A1116                 O   HOH A1205     1555   1555  2.09  
LINK        MG    MG A1116                 O   HOH A1218     1555   1555  2.08  
LINK         OG  SER B 114                MG    MG B 707     1555   1555  2.16  
LINK         O   SER B 116                CA    CA B 706     1555   1555  2.42  
LINK         OG  SER B 116                MG    MG B 707     1555   1555  2.03  
LINK         OD2 ASP B 151                CA    CA B 705     1555   1555  2.38  
LINK         OD1 ASN B 207                CA    CA B 705     1555   1555  2.27  
LINK         OD1 ASP B 209                CA    CA B 705     1555   1555  2.29  
LINK         O   ASP B 209                CA    CA B 705     1555   1555  2.34  
LINK         O   PRO B 211                CA    CA B 705     1555   1555  2.34  
LINK         OE1 GLU B 212                CA    CA B 705     1555   1555  2.40  
LINK         OE2 GLU B 212                MG    MG B 707     1555   1555  2.20  
LINK         OD2 ASP B 242                CA    CA B 706     1555   1555  2.40  
LINK        CA    CA B 706                 O   HOH B 809     1555   1555  2.56  
LINK        CA    CA B 706                 O   HOH B 810     1555   1555  2.53  
LINK        CA    CA B 706                 O   HOH B 834     1555   1555  2.92  
LINK        MG    MG B 707                 O   HOH B 806     1555   1555  2.06  
LINK        MG    MG B 707                 O   HOH B 807     1555   1555  2.07  
CISPEP   1 SER A   82    PRO A   83          0        -2.97                     
CISPEP   2 LEU A  119    PRO A  120          0        -1.69                     
CISPEP   3 ARG A  164    PRO A  165          0        -3.65                     
CISPEP   4 LYS A  288    PRO A  289          0         0.79                     
CISPEP   5 ILE A  609    PRO A  610          0         1.71                     
CISPEP   6 SER B   77    PRO B   78          0        -1.39                     
CISPEP   7 LEU B  155    PRO B  156          0         3.09                     
CISPEP   8 LEU B  587    PRO B  588          0         3.27                     
CRYST1  127.087  119.851  182.399  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      0.007869  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008344  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005482        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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