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Database: PDB
Entry: 4W9U
LinkDB: 4W9U
Original site: 4W9U 
HEADER    OXIDOREDUCTASE                          27-AUG-14   4W9U              
TITLE     CRYSTAL STRUCTURE OF AN ACYL-COA DEHYDROGENASE FROM BRUCELLA          
TITLE    2 MELITENSIS                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYL-COA DEHYDROGENASE;                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BRUCELLA ABORTUS 2308;                          
SOURCE   3 ORGANISM_COMMON: BRUCELLA MELITENSIS BIOVAR ABORTUS 2308;            
SOURCE   4 ORGANISM_TAXID: 359391;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    SSGCID, NIAID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS       
KEYWDS   2 CENTER FOR INFECTIOUS DISEASE, OXIDOREDUCTASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   4   27-DEC-23 4W9U    1       REMARK                                   
REVDAT   3   22-NOV-17 4W9U    1       SOURCE REMARK                            
REVDAT   2   25-FEB-15 4W9U    1       REMARK                                   
REVDAT   1   10-SEP-14 4W9U    0                                                
JRNL        AUTH   D.M.DRANOW,T.E.EDWARDS,D.LORIMER,                            
JRNL        AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE    
JRNL        AUTH 3 (SSGCID)                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF AN ACYL-COA DEHYDROGENASE FROM BRUCELLA 
JRNL        TITL 2 MELITENSIS                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1769)                     
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 56423                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2806                            
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 47.2396 -  6.5094    1.00     3093   164  0.1616 0.1908        
REMARK   3     2  6.5094 -  5.1688    0.99     3009   162  0.1729 0.2166        
REMARK   3     3  5.1688 -  4.5160    0.99     3018   135  0.1370 0.1868        
REMARK   3     4  4.5160 -  4.1033    0.97     2958   154  0.1255 0.1830        
REMARK   3     5  4.1033 -  3.8094    0.95     2904   142  0.1434 0.1966        
REMARK   3     6  3.8094 -  3.5849    0.94     2814   173  0.1682 0.2418        
REMARK   3     7  3.5849 -  3.4054    0.96     2896   146  0.1866 0.2338        
REMARK   3     8  3.4054 -  3.2572    0.95     2879   140  0.1933 0.2603        
REMARK   3     9  3.2572 -  3.1318    0.93     2827   130  0.1962 0.2525        
REMARK   3    10  3.1318 -  3.0238    0.89     2703   144  0.2037 0.2685        
REMARK   3    11  3.0238 -  2.9292    0.87     2615   147  0.2051 0.2655        
REMARK   3    12  2.9292 -  2.8455    0.86     2606   132  0.2133 0.3510        
REMARK   3    13  2.8455 -  2.7706    0.83     2503   152  0.2239 0.2973        
REMARK   3    14  2.7706 -  2.7030    0.82     2461   133  0.2189 0.2754        
REMARK   3    15  2.7030 -  2.6416    0.82     2450   135  0.2213 0.3074        
REMARK   3    16  2.6416 -  2.5854    0.81     2458   132  0.2216 0.3004        
REMARK   3    17  2.5854 -  2.5337    0.80     2405   107  0.2303 0.2711        
REMARK   3    18  2.5337 -  2.4858    0.79     2375   137  0.2398 0.3253        
REMARK   3    19  2.4858 -  2.4414    0.77     2320   128  0.2614 0.3231        
REMARK   3    20  2.4414 -  2.4001    0.77     2323   113  0.2711 0.3501        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.730           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.31                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.97                          
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      :  0.009          11183                                  
REMARK   3   ANGLE     :  1.173          15107                                  
REMARK   3   CHIRALITY :  0.045           1664                                  
REMARK   3   PLANARITY :  0.006           1980                                  
REMARK   3   DIHEDRAL  : 12.181           3972                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 35 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0493  72.0982  49.8983              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3207 T22:   0.2345                                     
REMARK   3      T33:   0.3972 T12:   0.0572                                     
REMARK   3      T13:   0.0105 T23:  -0.0844                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2099 L22:   2.5247                                     
REMARK   3      L33:   3.8549 L12:   1.2890                                     
REMARK   3      L13:   0.8508 L23:   0.7782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2137 S12:  -0.3819 S13:   0.2184                       
REMARK   3      S21:   0.2584 S22:   0.1843 S23:  -0.3391                       
REMARK   3      S31:  -0.3066 S32:  -0.3493 S33:  -0.0723                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 90 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.1257  62.6882  59.3029              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4832 T22:   0.3604                                     
REMARK   3      T33:   0.5015 T12:   0.0739                                     
REMARK   3      T13:  -0.2176 T23:  -0.1402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6854 L22:   2.6381                                     
REMARK   3      L33:   3.6062 L12:   0.7424                                     
REMARK   3      L13:   0.0589 L23:  -0.3474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3048 S12:  -0.2842 S13:  -0.2497                       
REMARK   3      S21:   0.7425 S22:   0.0330 S23:  -0.5347                       
REMARK   3      S31:   0.2290 S32:   0.4286 S33:  -0.1904                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 116 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3027  54.2831  60.1929              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6125 T22:   0.4373                                     
REMARK   3      T33:   0.4650 T12:   0.0717                                     
REMARK   3      T13:  -0.2393 T23:  -0.0892                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9345 L22:   0.3444                                     
REMARK   3      L33:   1.6486 L12:  -0.5561                                     
REMARK   3      L13:   1.0875 L23:   0.0798                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2791 S12:  -0.3337 S13:  -0.5093                       
REMARK   3      S21:   0.6034 S22:   0.1753 S23:  -0.6029                       
REMARK   3      S31:   0.1521 S32:   0.0167 S33:  -0.2074                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 177 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0464  44.1850  68.0078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9512 T22:   0.5639                                     
REMARK   3      T33:   0.6877 T12:   0.0821                                     
REMARK   3      T13:  -0.4453 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4195 L22:   0.6867                                     
REMARK   3      L33:   1.8005 L12:   0.4293                                     
REMARK   3      L13:   0.6200 L23:   0.4064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2727 S12:  -0.5032 S13:  -0.8882                       
REMARK   3      S21:   0.4625 S22:  -0.1303 S23:  -0.8357                       
REMARK   3      S31:   0.3513 S32:   0.0424 S33:  -0.2620                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 198 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.9818  38.2526  70.4875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3362 T22:   0.4650                                     
REMARK   3      T33:   0.8512 T12:   0.1323                                     
REMARK   3      T13:  -0.6771 T23:   0.2384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4317 L22:   1.0282                                     
REMARK   3      L33:   0.7081 L12:  -0.6019                                     
REMARK   3      L13:  -0.1884 L23:   0.6040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0006 S12:  -0.5681 S13:  -0.5313                       
REMARK   3      S21:   0.3662 S22:   0.2026 S23:   0.2182                       
REMARK   3      S31:   0.9256 S32:  -0.1265 S33:  -0.2176                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 199 THROUGH 241 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.5043  40.9670  68.2798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9728 T22:   0.5556                                     
REMARK   3      T33:   0.8281 T12:   0.2075                                     
REMARK   3      T13:  -0.5521 T23:   0.1200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8799 L22:   0.2145                                     
REMARK   3      L33:   1.8253 L12:   0.7682                                     
REMARK   3      L13:  -0.1321 L23:  -0.2095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0104 S12:  -0.2752 S13:  -1.0301                       
REMARK   3      S21:   0.3658 S22:   0.2123 S23:  -0.7423                       
REMARK   3      S31:   0.9366 S32:  -0.0001 S33:  -0.2236                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 242 THROUGH 277 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8986  58.2290  46.1936              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3904 T22:   0.2693                                     
REMARK   3      T33:   0.4049 T12:   0.0264                                     
REMARK   3      T13:  -0.0758 T23:  -0.1200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3469 L22:   1.4405                                     
REMARK   3      L33:   3.1409 L12:   0.0225                                     
REMARK   3      L13:   0.3594 L23:  -1.0442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1557 S12:  -0.2011 S13:  -0.0798                       
REMARK   3      S21:   0.2387 S22:  -0.0204 S23:  -0.3279                       
REMARK   3      S31:   0.1432 S32:   0.5888 S33:  -0.1305                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 347 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5082  59.0005  39.6192              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2959 T22:   0.2788                                     
REMARK   3      T33:   0.3234 T12:   0.0095                                     
REMARK   3      T13:  -0.0656 T23:  -0.0728                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6295 L22:   1.3311                                     
REMARK   3      L33:   2.5253 L12:   0.0493                                     
REMARK   3      L13:  -0.6698 L23:  -0.0555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:  -0.0062 S13:  -0.0342                       
REMARK   3      S21:   0.0346 S22:   0.0856 S23:  -0.2333                       
REMARK   3      S31:   0.1298 S32:   0.0530 S33:  -0.1132                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 348 THROUGH 371 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7651  54.7053  39.3853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4183 T22:   0.6444                                     
REMARK   3      T33:   0.5117 T12:   0.1989                                     
REMARK   3      T13:  -0.1224 T23:  -0.2968                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8140 L22:   2.0975                                     
REMARK   3      L33:   7.3513 L12:   0.0037                                     
REMARK   3      L13:  -0.2927 L23:  -2.9437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4924 S12:   0.3949 S13:   0.0695                       
REMARK   3      S21:  -0.3733 S22:   0.3605 S23:  -0.3854                       
REMARK   3      S31:   1.2742 S32:   0.2002 S33:  -0.2951                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 372 THROUGH 394 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9931  38.8252  47.6213              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4544 T22:   0.2417                                     
REMARK   3      T33:   0.3165 T12:   0.0108                                     
REMARK   3      T13:  -0.0777 T23:   0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2720 L22:   7.8094                                     
REMARK   3      L33:   6.1574 L12:   1.2002                                     
REMARK   3      L13:  -2.4606 L23:  -0.6916                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0253 S12:  -0.1981 S13:  -0.4130                       
REMARK   3      S21:  -0.1327 S22:  -0.0823 S23:  -0.7296                       
REMARK   3      S31:  -0.3681 S32:   0.1223 S33:   0.0033                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 129 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1184  64.9080  40.6220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2657 T22:   0.3592                                     
REMARK   3      T33:   0.2919 T12:   0.0233                                     
REMARK   3      T13:   0.0845 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7348 L22:   1.5112                                     
REMARK   3      L33:   1.3976 L12:  -0.6569                                     
REMARK   3      L13:   0.6956 L23:  -0.7349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0578 S12:  -0.2405 S13:  -0.0530                       
REMARK   3      S21:   0.2718 S22:   0.1085 S23:   0.2321                       
REMARK   3      S31:  -0.1505 S32:  -0.2507 S33:  -0.0871                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 130 THROUGH 241 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4811  79.0499  20.5288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2749 T22:   0.3135                                     
REMARK   3      T33:   0.2908 T12:   0.0267                                     
REMARK   3      T13:   0.0540 T23:   0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7793 L22:   5.4314                                     
REMARK   3      L33:   3.4910 L12:   0.9999                                     
REMARK   3      L13:   0.1904 L23:  -0.0593                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0873 S12:   0.3042 S13:   0.2515                       
REMARK   3      S21:  -0.1581 S22:   0.1184 S23:  -0.1161                       
REMARK   3      S31:  -0.3772 S32:  -0.1425 S33:  -0.0157                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 242 THROUGH 371 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5724  53.8345  36.5533              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2116 T22:   0.2946                                     
REMARK   3      T33:   0.2418 T12:  -0.0027                                     
REMARK   3      T13:   0.0176 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1547 L22:   1.4062                                     
REMARK   3      L33:   0.3456 L12:  -0.3478                                     
REMARK   3      L13:  -0.0836 L23:  -0.3121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0491 S12:  -0.0023 S13:  -0.1047                       
REMARK   3      S21:  -0.0520 S22:   0.0431 S23:   0.1043                       
REMARK   3      S31:   0.0280 S32:  -0.1116 S33:  -0.0977                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 394 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2467  69.4220  25.2105              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4362 T22:   0.2189                                     
REMARK   3      T33:   0.3705 T12:   0.0300                                     
REMARK   3      T13:   0.0242 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1338 L22:   3.1800                                     
REMARK   3      L33:   2.4342 L12:  -0.1508                                     
REMARK   3      L13:   0.2063 L23:   0.8604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1169 S12:   0.0537 S13:  -0.0586                       
REMARK   3      S21:  -0.3783 S22:   0.1067 S23:   0.2065                       
REMARK   3      S31:  -0.1015 S32:   0.0387 S33:  -0.1372                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 90 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8151  33.6382   0.6855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4497 T22:   0.2738                                     
REMARK   3      T33:   0.3028 T12:   0.0090                                     
REMARK   3      T13:  -0.1463 T23:  -0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8629 L22:   3.2064                                     
REMARK   3      L33:   0.9151 L12:   2.1931                                     
REMARK   3      L13:   1.2846 L23:  -0.0373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1896 S12:   0.1530 S13:  -0.0518                       
REMARK   3      S21:  -0.4013 S22:  -0.0271 S23:   0.2807                       
REMARK   3      S31:   0.2298 S32:  -0.0610 S33:  -0.0398                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 91 THROUGH 177 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3446  18.7040  12.4992              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5176 T22:   0.4506                                     
REMARK   3      T33:   0.5921 T12:  -0.1784                                     
REMARK   3      T13:  -0.1780 T23:   0.0749                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8217 L22:   1.6732                                     
REMARK   3      L33:   0.9164 L12:   0.5728                                     
REMARK   3      L13:   0.6336 L23:   0.3074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2681 S12:  -0.3453 S13:  -0.4729                       
REMARK   3      S21:  -0.0742 S22:   0.0441 S23:   0.3006                       
REMARK   3      S31:   0.5876 S32:  -0.4658 S33:  -0.1265                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 178 THROUGH 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0281  13.8598  18.0505              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5853 T22:   0.5471                                     
REMARK   3      T33:   0.8197 T12:  -0.2638                                     
REMARK   3      T13:  -0.1768 T23:   0.3152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0409 L22:   3.3343                                     
REMARK   3      L33:   0.8844 L12:  -0.3464                                     
REMARK   3      L13:   0.0234 L23:  -0.4157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1713 S12:  -0.6511 S13:  -0.7531                       
REMARK   3      S21:   0.5933 S22:   0.0135 S23:   0.6357                       
REMARK   3      S31:   0.4059 S32:  -0.8281 S33:  -0.3206                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 219 THROUGH 242 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2104  11.9486  18.0567              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7191 T22:   0.6139                                     
REMARK   3      T33:   0.8148 T12:  -0.2669                                     
REMARK   3      T13:  -0.1418 T23:   0.2280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2753 L22:   3.1802                                     
REMARK   3      L33:   2.0562 L12:   0.3262                                     
REMARK   3      L13:   0.3228 L23:   0.2849                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1955 S12:  -0.5465 S13:  -0.7088                       
REMARK   3      S21:   0.6240 S22:  -0.0759 S23:   0.4375                       
REMARK   3      S31:   0.9532 S32:  -0.7308 S33:  -0.2858                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 243 THROUGH 347 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7855  42.0168  13.8030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2411 T22:   0.2528                                     
REMARK   3      T33:   0.2420 T12:   0.0036                                     
REMARK   3      T13:  -0.0294 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7128 L22:   2.6487                                     
REMARK   3      L33:   0.7449 L12:   0.3735                                     
REMARK   3      L13:   0.1060 L23:   0.2321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0934 S12:   0.0434 S13:   0.0367                       
REMARK   3      S21:  -0.1188 S22:  -0.0641 S23:   0.2169                       
REMARK   3      S31:  -0.0035 S32:  -0.1488 S33:  -0.0201                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 348 THROUGH 371 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2563  45.3612  17.0965              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3100 T22:   0.6196                                     
REMARK   3      T33:   0.4766 T12:  -0.0846                                     
REMARK   3      T13:   0.0203 T23:  -0.1640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7735 L22:   7.5774                                     
REMARK   3      L33:   5.0525 L12:  -0.2189                                     
REMARK   3      L13:  -0.1264 L23:  -2.4578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1686 S12:  -0.1480 S13:   0.1421                       
REMARK   3      S21:   0.0458 S22:  -0.3824 S23:   1.1294                       
REMARK   3      S31:   0.4555 S32:  -0.8375 S33:   0.4452                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 372 THROUGH 394 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8676  27.7747  30.3937              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2989 T22:   0.2090                                     
REMARK   3      T33:   0.3863 T12:  -0.0440                                     
REMARK   3      T13:  -0.0412 T23:   0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6294 L22:   4.5674                                     
REMARK   3      L33:   3.2975 L12:  -0.1669                                     
REMARK   3      L13:  -1.8446 L23:   1.2558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2066 S12:   0.0926 S13:   0.2232                       
REMARK   3      S21:  -0.0202 S22:  -0.1222 S23:   0.2607                       
REMARK   3      S31:   0.0325 S32:  -0.1954 S33:  -0.0875                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 4 THROUGH 129 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  44.4491  37.4386  13.1802              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2944 T22:   0.2643                                     
REMARK   3      T33:   0.3702 T12:   0.0782                                     
REMARK   3      T13:  -0.0125 T23:  -0.0617                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2808 L22:   1.4489                                     
REMARK   3      L33:   1.3783 L12:   0.9319                                     
REMARK   3      L13:  -0.7806 L23:  -0.6242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0317 S12:   0.0605 S13:  -0.4226                       
REMARK   3      S21:  -0.2477 S22:  -0.0073 S23:  -0.3215                       
REMARK   3      S31:   0.2632 S32:   0.1764 S33:  -0.0063                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 130 THROUGH 167 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  51.0952  63.4573   7.6022              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2810 T22:   0.2811                                     
REMARK   3      T33:   0.2829 T12:   0.0637                                     
REMARK   3      T13:   0.0260 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7144 L22:   4.4769                                     
REMARK   3      L33:   3.6900 L12:   1.2123                                     
REMARK   3      L13:  -1.2570 L23:  -3.3509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1548 S12:   0.0462 S13:   0.4983                       
REMARK   3      S21:  -0.0251 S22:   0.0815 S23:   0.3223                       
REMARK   3      S31:  -0.2443 S32:  -0.0287 S33:  -0.2169                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 168 THROUGH 198 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  50.5125  60.1044   7.4946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2418 T22:   0.3233                                     
REMARK   3      T33:   0.2781 T12:   0.0653                                     
REMARK   3      T13:   0.0492 T23:  -0.0418                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1641 L22:   3.2563                                     
REMARK   3      L33:   5.9811 L12:  -0.1910                                     
REMARK   3      L13:   1.8958 L23:  -1.9331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0951 S12:   0.1724 S13:   0.2158                       
REMARK   3      S21:  -0.0546 S22:   0.0894 S23:   0.1048                       
REMARK   3      S31:  -0.1395 S32:  -0.2034 S33:   0.1606                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 199 THROUGH 242 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  53.7192  59.1186  11.6907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2060 T22:   0.2660                                     
REMARK   3      T33:   0.3034 T12:   0.0547                                     
REMARK   3      T13:   0.0652 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4759 L22:   3.9731                                     
REMARK   3      L33:   3.9980 L12:   1.1883                                     
REMARK   3      L13:   0.5403 L23:  -0.4074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0153 S12:  -0.1351 S13:  -0.0515                       
REMARK   3      S21:   0.1023 S22:  -0.2044 S23:   0.0949                       
REMARK   3      S31:  -0.3256 S32:   0.0860 S33:   0.2054                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 243 THROUGH 347 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5704  39.5154  22.2499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2382 T22:   0.2198                                     
REMARK   3      T33:   0.3067 T12:   0.0115                                     
REMARK   3      T13:  -0.0326 T23:  -0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8180 L22:   1.0391                                     
REMARK   3      L33:   1.8598 L12:   0.1451                                     
REMARK   3      L13:  -0.2260 L23:  -0.7597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0925 S12:  -0.0262 S13:  -0.0549                       
REMARK   3      S21:  -0.0077 S22:   0.0213 S23:   0.0018                       
REMARK   3      S31:   0.1091 S32:   0.1845 S33:  -0.0388                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 348 THROUGH 371 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.4408  45.0376  31.4055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2709 T22:   0.3851                                     
REMARK   3      T33:   0.4532 T12:   0.0031                                     
REMARK   3      T13:  -0.0368 T23:  -0.1186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5538 L22:   3.9535                                     
REMARK   3      L33:   9.5368 L12:   1.5713                                     
REMARK   3      L13:  -4.3203 L23:   0.0633                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3129 S12:  -0.9945 S13:   0.4220                       
REMARK   3      S21:   0.3469 S22:   0.3406 S23:  -0.6428                       
REMARK   3      S31:  -0.1806 S32:   0.6655 S33:  -0.5771                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 372 THROUGH 394 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.9472  58.6274  12.3568              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3390 T22:   0.2926                                     
REMARK   3      T33:   0.3858 T12:   0.0140                                     
REMARK   3      T13:   0.0753 T23:  -0.0385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2503 L22:   6.3233                                     
REMARK   3      L33:   2.7005 L12:  -0.9153                                     
REMARK   3      L13:   4.0014 L23:  -0.5582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2916 S12:   0.2545 S13:   0.1710                       
REMARK   3      S21:  -0.5497 S22:   0.0102 S23:  -0.6021                       
REMARK   3      S31:   0.0200 S32:   0.7754 S33:  -0.1660                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 6561                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 6561                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 6561                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4W9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203446.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63306                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.510                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG(D2): 30% PEG-400, 100MM HEPES       
REMARK 280  FREE ACID/ NAOH, 200MM MGCL2, PH 7.5, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 289K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       53.33000            
REMARK 290   SMTRY3   2  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14550 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 51450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     TYR A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     GLU A    47                                                      
REMARK 465     GLU A    48                                                      
REMARK 465     THR A    49                                                      
REMARK 465     THR A    50                                                      
REMARK 465     ASP A   142                                                      
REMARK 465     ALA A   143                                                      
REMARK 465     GLY A   144                                                      
REMARK 465     SER A   145                                                      
REMARK 465     ASP A   146                                                      
REMARK 465     PRO A   147                                                      
REMARK 465     ALA A   148                                                      
REMARK 465     GLY A   149                                                      
REMARK 465     GLY A   210                                                      
REMARK 465     GLY A   211                                                      
REMARK 465     LYS A   212                                                      
REMARK 465     LEU A   213                                                      
REMARK 465     SER A   214                                                      
REMARK 465     LEU A   215                                                      
REMARK 465     ARG A   216                                                      
REMARK 465     GLY A   350                                                      
REMARK 465     ASN A   351                                                      
REMARK 465     GLY A   352                                                      
REMARK 465     ILE A   353                                                      
REMARK 465     GLN A   354                                                      
REMARK 465     ILE A   355                                                      
REMARK 465     GLU A   356                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     TYR B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     ALA B   143                                                      
REMARK 465     GLY B   144                                                      
REMARK 465     SER B   145                                                      
REMARK 465     ASP B   146                                                      
REMARK 465     LYS B   212                                                      
REMARK 465     LEU B   213                                                      
REMARK 465     SER B   214                                                      
REMARK 465     GLY B   350                                                      
REMARK 465     ASN B   351                                                      
REMARK 465     GLY B   352                                                      
REMARK 465     ILE B   353                                                      
REMARK 465     GLN B   354                                                      
REMARK 465     ILE B   355                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     ALA C    44                                                      
REMARK 465     TYR C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     GLU C    47                                                      
REMARK 465     GLU C    48                                                      
REMARK 465     THR C    49                                                      
REMARK 465     ASP C   142                                                      
REMARK 465     ALA C   143                                                      
REMARK 465     GLY C   144                                                      
REMARK 465     SER C   145                                                      
REMARK 465     ASP C   146                                                      
REMARK 465     PRO C   147                                                      
REMARK 465     ALA C   148                                                      
REMARK 465     GLY C   149                                                      
REMARK 465     GLY C   210                                                      
REMARK 465     GLY C   211                                                      
REMARK 465     LYS C   212                                                      
REMARK 465     LEU C   213                                                      
REMARK 465     SER C   214                                                      
REMARK 465     ASN C   351                                                      
REMARK 465     GLY C   352                                                      
REMARK 465     ILE C   353                                                      
REMARK 465     GLN C   354                                                      
REMARK 465     ILE C   355                                                      
REMARK 465     GLU C   356                                                      
REMARK 465     TYR C   357                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     LYS D    43                                                      
REMARK 465     ALA D    44                                                      
REMARK 465     TYR D    45                                                      
REMARK 465     LEU D    46                                                      
REMARK 465     GLU D    47                                                      
REMARK 465     GLU D    48                                                      
REMARK 465     THR D    49                                                      
REMARK 465     ASP D   146                                                      
REMARK 465     PRO D   147                                                      
REMARK 465     LEU D   213                                                      
REMARK 465     GLY D   350                                                      
REMARK 465     ASN D   351                                                      
REMARK 465     GLY D   352                                                      
REMARK 465     ILE D   353                                                      
REMARK 465     GLN D   354                                                      
REMARK 465     ILE D   355                                                      
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     ARG A   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A  41    CG1  CG2                                            
REMARK 470     GLU A  42    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  51    CG   OD1  OD2                                       
REMARK 470     GLU A  53    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  71    CG   OD1  OD2                                       
REMARK 470     ALA A  74    CB                                                  
REMARK 470     SER A 116    OG                                                  
REMARK 470     GLU A 118    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 121    CG   CD   CE   NZ                                   
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     SER A 129    OG                                                  
REMARK 470     GLU A 131    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 138    CG   CD1  CD2                                       
REMARK 470     LYS A 151    CG   CD   CE   NZ                                   
REMARK 470     ARG A 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 155    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 156    CG   CD   CE   NZ                                   
REMARK 470     ILE A 157    CG1  CG2  CD1                                       
REMARK 470     ASP A 158    CG   OD1  OD2                                       
REMARK 470     ARG A 162    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 163    CG   CD1  CD2                                       
REMARK 470     MET A 168    CG   SD   CE                                        
REMARK 470     TRP A 169    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 169    CZ3  CH2                                            
REMARK 470     ILE A 170    CG1  CG2  CD1                                       
REMARK 470     SER A 171    OG                                                  
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     ASP A 189    CG   OD1  OD2                                       
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     LEU A 204    CG   CD1  CD2                                       
REMARK 470     LYS A 208    CG   CD   CE   NZ                                   
REMARK 470     SER A 218    OG                                                  
REMARK 470     THR A 220    OG1  CG2                                            
REMARK 470     GLU A 222    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 223    CG1  CG2  CD1                                       
REMARK 470     VAL A 224    CG1  CG2                                            
REMARK 470     VAL A 228    CG1  CG2                                            
REMARK 470     GLU A 229    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 232    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 243    CG   CD   CE   NZ                                   
REMARK 470     ARG A 278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 279    CG   CD   CE   NZ                                   
REMARK 470     ASN A 282    CG   OD1  ND2                                       
REMARK 470     LYS A 283    CG   CD   CE   NZ                                   
REMARK 470     TYR A 357    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET A 360    CG   SD   CE                                        
REMARK 470     GLN A 364    CG   CD   OE1  NE2                                  
REMARK 470     TYR A 372    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 373    CG   CD   OE1  OE2                                  
REMARK 470     ARG B   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B   9    OE1  OE2                                            
REMARK 470     GLU B  20    CG   CD   OE1  OE2                                  
REMARK 470     MET B  24    CG   SD   CE                                        
REMARK 470     ASP B  35    CG   OD1  OD2                                       
REMARK 470     GLU B  42    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     GLU B  47    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     ALA B  74    CB                                                  
REMARK 470     GLU B 118    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 121    CG   CD   CE   NZ                                   
REMARK 470     ASP B 142    CG   OD1  OD2                                       
REMARK 470     LYS B 151    CG   CD   CE   NZ                                   
REMARK 470     ILE B 157    CG1  CG2  CD1                                       
REMARK 470     ASP B 158    CG   OD1  OD2                                       
REMARK 470     LYS B 184    CG   CD   CE   NZ                                   
REMARK 470     ASN B 190    CG   OD1  ND2                                       
REMARK 470     LYS B 202    CG   CD   CE   NZ                                   
REMARK 470     GLU B 232    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 243    CG   CD   CE   NZ                                   
REMARK 470     ARG B 278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 282    CG   OD1  ND2                                       
REMARK 470     LYS B 283    CG   CD   CE   NZ                                   
REMARK 470     GLU B 356    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 357    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B 372    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU C  42    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  43    CG   CD   CE   NZ                                   
REMARK 470     GLU C  53    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  60    CG   CD   OE1  NE2                                  
REMARK 470     ALA C  74    CB                                                  
REMARK 470     ASP C 117    CG   OD1  OD2                                       
REMARK 470     GLU C 118    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 131    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 132    CG   CD1  CD2                                       
REMARK 470     LYS C 151    CG   CD   CE   NZ                                   
REMARK 470     ARG C 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 156    CG   CD   CE   NZ                                   
REMARK 470     ILE C 157    CG1  CG2  CD1                                       
REMARK 470     ASP C 158    CG   OD1  OD2                                       
REMARK 470     ARG C 162    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 163    CG   CD1  CD2                                       
REMARK 470     SER C 164    OG                                                  
REMARK 470     SER C 166    OG                                                  
REMARK 470     LYS C 167    CG   CD   CE   NZ                                   
REMARK 470     MET C 168    CG   SD   CE                                        
REMARK 470     TRP C 169    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 169    CZ3  CH2                                            
REMARK 470     ILE C 170    CG1  CG2  CD1                                       
REMARK 470     SER C 171    OG                                                  
REMARK 470     VAL C 181    CG1  CG2                                            
REMARK 470     LYS C 184    CG   CD   CE   NZ                                   
REMARK 470     ASP C 189    CG   OD1  OD2                                       
REMARK 470     ASN C 190    CG   OD1  ND2                                       
REMARK 470     ILE C 192    CG1  CG2  CD1                                       
REMARK 470     LYS C 199    CG   CD   CE   NZ                                   
REMARK 470     LYS C 202    CG   CD   CE   NZ                                   
REMARK 470     LEU C 204    CG   CD1  CD2                                       
REMARK 470     LYS C 208    CG   CD   CE   NZ                                   
REMARK 470     ILE C 209    CG1  CG2  CD1                                       
REMARK 470     LEU C 215    CG   CD1  CD2                                       
REMARK 470     ARG C 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C 218    OG                                                  
REMARK 470     VAL C 228    CG1  CG2                                            
REMARK 470     GLU C 229    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 232    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 233    CG   OD1  OD2                                       
REMARK 470     ILE C 235    CG1  CG2  CD1                                       
REMARK 470     LYS C 279    CG   CD   CE   NZ                                   
REMARK 470     ASN C 282    CG   OD1  ND2                                       
REMARK 470     MET C 360    CG   SD   CE                                        
REMARK 470     GLU C 373    CG   CD   OE1  OE2                                  
REMARK 470     ASP D  21    CG   OD1  OD2                                       
REMARK 470     MET D  24    CG   SD   CE                                        
REMARK 470     GLU D  42    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  53    CG   CD   OE1  OE2                                  
REMARK 470     ALA D  74    CB                                                  
REMARK 470     GLU D 118    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 121    NZ                                                  
REMARK 470     ASP D 142    CG   OD1  OD2                                       
REMARK 470     LYS D 151    CG   CD   CE   NZ                                   
REMARK 470     LYS D 212    CG   CD   CE   NZ                                   
REMARK 470     SER D 214    CB   OG                                             
REMARK 470     ASN D 282    CB   CG   OD1  ND2                                  
REMARK 470     LYS D 283    CG   CD   CE   NZ                                   
REMARK 470     GLU D 356    CG   CD   OE1  OE2                                  
REMARK 470     TYR D 357    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR C    79     O1   EDO C   401              1.27            
REMARK 500   OG   SER C   105     O2   EDO C   401              1.27            
REMARK 500   CZ   TYR C    79     O1   EDO C   401              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 138      -54.59   -127.68                                   
REMARK 500    ASP A 158      107.07    -54.51                                   
REMARK 500    ALA A 187       -2.44     86.89                                   
REMARK 500    ASN A 190       17.39     58.56                                   
REMARK 500    ASP A 226       78.42   -100.79                                   
REMARK 500    ASN A 238       34.64    -95.35                                   
REMARK 500    HIS A 348       45.69    -90.14                                   
REMARK 500    LEU B 138      -53.64   -126.07                                   
REMARK 500    ASP B 189       65.77     29.37                                   
REMARK 500    ASN B 190       14.14     49.28                                   
REMARK 500    ASP B 226       78.79   -100.76                                   
REMARK 500    ASN B 238       34.48    -95.54                                   
REMARK 500    LEU C 138      -55.90   -126.80                                   
REMARK 500    ASP C 158      108.38    -53.71                                   
REMARK 500    ASP C 189       71.14    -69.87                                   
REMARK 500    ASN C 190       16.07     53.02                                   
REMARK 500    LYS C 202      -75.45    -63.54                                   
REMARK 500    ASN C 238       34.19    -95.63                                   
REMARK 500    HIS C 348       48.62    -91.03                                   
REMARK 500    GLU C 373       73.22     21.83                                   
REMARK 500    VAL D 107      -54.00   -120.09                                   
REMARK 500    LEU D 138      -55.51   -124.76                                   
REMARK 500    ALA D 143     -121.54   -173.44                                   
REMARK 500    ASP D 158      105.58    -50.40                                   
REMARK 500    ALA D 187      -12.62     92.17                                   
REMARK 500    ASN D 190       18.17     56.44                                   
REMARK 500    ASP D 226       79.07   -101.81                                   
REMARK 500    ASN D 238       32.56    -95.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 565        DISTANCE =  5.97 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: SSGCID-BRABA.00027.A   RELATED DB: TARGETTRACK           
DBREF  4W9U A    0   394  PDB    4W9U     4W9U             0    394             
DBREF  4W9U B    0   394  PDB    4W9U     4W9U             0    394             
DBREF  4W9U C    0   394  PDB    4W9U     4W9U             0    394             
DBREF  4W9U D    0   394  PDB    4W9U     4W9U             0    394             
SEQRES   1 A  395  SER MET SER ARG ALA ALA PHE ALA TRP GLU ASP PRO PHE          
SEQRES   2 A  395  LEU LEU GLU GLU GLN LEU THR GLU ASP GLU ARG MET ILE          
SEQRES   3 A  395  ARG ASP SER ALA LYS ALA PHE ALA SER ASP VAL LEU LEU          
SEQRES   4 A  395  PRO ARG VAL GLU LYS ALA TYR LEU GLU GLU THR THR ASP          
SEQRES   5 A  395  PRO GLU LEU PHE HIS LEU MET GLY GLN ALA GLY LEU LEU          
SEQRES   6 A  395  GLY VAL THR LEU PRO GLU ASP TYR GLY ALA ALA ASN ALA          
SEQRES   7 A  395  SER TYR VAL ALA TYR GLY LEU VAL ALA ARG GLU VAL GLU          
SEQRES   8 A  395  ARG ILE ASP SER GLY TYR ARG SER MET MET SER VAL GLN          
SEQRES   9 A  395  SER SER LEU VAL MET TYR PRO ILE TYR ALA TYR GLY SER          
SEQRES  10 A  395  ASP GLU GLN ARG LYS LYS TYR LEU PRO GLY LEU VAL SER          
SEQRES  11 A  395  GLY GLU LEU ILE GLY CYS PHE GLY LEU THR GLU PRO ASP          
SEQRES  12 A  395  ALA GLY SER ASP PRO ALA GLY MET LYS THR ARG ALA GLU          
SEQRES  13 A  395  LYS ILE ASP GLY GLY TYR ARG LEU SER GLY SER LYS MET          
SEQRES  14 A  395  TRP ILE SER ASN SER PRO ILE ALA ASP VAL PHE VAL VAL          
SEQRES  15 A  395  TRP ALA LYS SER ALA ALA HIS ASP ASN ALA ILE ARG GLY          
SEQRES  16 A  395  PHE ILE LEU GLU LYS GLY MET LYS GLY LEU SER ALA PRO          
SEQRES  17 A  395  LYS ILE GLY GLY LYS LEU SER LEU ARG ALA SER ILE THR          
SEQRES  18 A  395  GLY GLU ILE VAL MET ASP GLY VAL GLU VAL SER GLU ASP          
SEQRES  19 A  395  ALA ILE LEU PRO ASN VAL SER GLY LEU LYS GLY PRO PHE          
SEQRES  20 A  395  GLY CYS LEU ASN ARG ALA ARG TYR GLY ILE SER TRP GLY          
SEQRES  21 A  395  VAL LEU GLY ALA ALA GLU ASP CYS TRP PHE ARG ALA ARG          
SEQRES  22 A  395  GLN TYR GLY LEU ASP ARG LYS GLN PHE ASN LYS PRO LEU          
SEQRES  23 A  395  ALA GLY THR GLN LEU TYR GLN LYS LYS LEU ALA ASP MET          
SEQRES  24 A  395  GLN THR GLU ILE ALA LEU GLY ILE GLN ALA SER LEU ARG          
SEQRES  25 A  395  VAL GLY ARG LEU PHE ASP GLU GLY LYS MET ALA PRO GLU          
SEQRES  26 A  395  MET ILE SER ILE VAL LYS ARG ASN ASN CYS GLY LYS ALA          
SEQRES  27 A  395  LEU ASP ILE ALA ARG GLN ALA ARG ASP MET HIS GLY GLY          
SEQRES  28 A  395  ASN GLY ILE GLN ILE GLU TYR HIS VAL MET ARG HIS ALA          
SEQRES  29 A  395  GLN ASN LEU GLU THR VAL ASN THR TYR GLU GLY THR HIS          
SEQRES  30 A  395  ASP VAL HIS ALA LEU ILE LEU GLY ARG ALA GLN THR GLY          
SEQRES  31 A  395  ILE GLN ALA PHE PHE                                          
SEQRES   1 B  395  SER MET SER ARG ALA ALA PHE ALA TRP GLU ASP PRO PHE          
SEQRES   2 B  395  LEU LEU GLU GLU GLN LEU THR GLU ASP GLU ARG MET ILE          
SEQRES   3 B  395  ARG ASP SER ALA LYS ALA PHE ALA SER ASP VAL LEU LEU          
SEQRES   4 B  395  PRO ARG VAL GLU LYS ALA TYR LEU GLU GLU THR THR ASP          
SEQRES   5 B  395  PRO GLU LEU PHE HIS LEU MET GLY GLN ALA GLY LEU LEU          
SEQRES   6 B  395  GLY VAL THR LEU PRO GLU ASP TYR GLY ALA ALA ASN ALA          
SEQRES   7 B  395  SER TYR VAL ALA TYR GLY LEU VAL ALA ARG GLU VAL GLU          
SEQRES   8 B  395  ARG ILE ASP SER GLY TYR ARG SER MET MET SER VAL GLN          
SEQRES   9 B  395  SER SER LEU VAL MET TYR PRO ILE TYR ALA TYR GLY SER          
SEQRES  10 B  395  ASP GLU GLN ARG LYS LYS TYR LEU PRO GLY LEU VAL SER          
SEQRES  11 B  395  GLY GLU LEU ILE GLY CYS PHE GLY LEU THR GLU PRO ASP          
SEQRES  12 B  395  ALA GLY SER ASP PRO ALA GLY MET LYS THR ARG ALA GLU          
SEQRES  13 B  395  LYS ILE ASP GLY GLY TYR ARG LEU SER GLY SER LYS MET          
SEQRES  14 B  395  TRP ILE SER ASN SER PRO ILE ALA ASP VAL PHE VAL VAL          
SEQRES  15 B  395  TRP ALA LYS SER ALA ALA HIS ASP ASN ALA ILE ARG GLY          
SEQRES  16 B  395  PHE ILE LEU GLU LYS GLY MET LYS GLY LEU SER ALA PRO          
SEQRES  17 B  395  LYS ILE GLY GLY LYS LEU SER LEU ARG ALA SER ILE THR          
SEQRES  18 B  395  GLY GLU ILE VAL MET ASP GLY VAL GLU VAL SER GLU ASP          
SEQRES  19 B  395  ALA ILE LEU PRO ASN VAL SER GLY LEU LYS GLY PRO PHE          
SEQRES  20 B  395  GLY CYS LEU ASN ARG ALA ARG TYR GLY ILE SER TRP GLY          
SEQRES  21 B  395  VAL LEU GLY ALA ALA GLU ASP CYS TRP PHE ARG ALA ARG          
SEQRES  22 B  395  GLN TYR GLY LEU ASP ARG LYS GLN PHE ASN LYS PRO LEU          
SEQRES  23 B  395  ALA GLY THR GLN LEU TYR GLN LYS LYS LEU ALA ASP MET          
SEQRES  24 B  395  GLN THR GLU ILE ALA LEU GLY ILE GLN ALA SER LEU ARG          
SEQRES  25 B  395  VAL GLY ARG LEU PHE ASP GLU GLY LYS MET ALA PRO GLU          
SEQRES  26 B  395  MET ILE SER ILE VAL LYS ARG ASN ASN CYS GLY LYS ALA          
SEQRES  27 B  395  LEU ASP ILE ALA ARG GLN ALA ARG ASP MET HIS GLY GLY          
SEQRES  28 B  395  ASN GLY ILE GLN ILE GLU TYR HIS VAL MET ARG HIS ALA          
SEQRES  29 B  395  GLN ASN LEU GLU THR VAL ASN THR TYR GLU GLY THR HIS          
SEQRES  30 B  395  ASP VAL HIS ALA LEU ILE LEU GLY ARG ALA GLN THR GLY          
SEQRES  31 B  395  ILE GLN ALA PHE PHE                                          
SEQRES   1 C  395  SER MET SER ARG ALA ALA PHE ALA TRP GLU ASP PRO PHE          
SEQRES   2 C  395  LEU LEU GLU GLU GLN LEU THR GLU ASP GLU ARG MET ILE          
SEQRES   3 C  395  ARG ASP SER ALA LYS ALA PHE ALA SER ASP VAL LEU LEU          
SEQRES   4 C  395  PRO ARG VAL GLU LYS ALA TYR LEU GLU GLU THR THR ASP          
SEQRES   5 C  395  PRO GLU LEU PHE HIS LEU MET GLY GLN ALA GLY LEU LEU          
SEQRES   6 C  395  GLY VAL THR LEU PRO GLU ASP TYR GLY ALA ALA ASN ALA          
SEQRES   7 C  395  SER TYR VAL ALA TYR GLY LEU VAL ALA ARG GLU VAL GLU          
SEQRES   8 C  395  ARG ILE ASP SER GLY TYR ARG SER MET MET SER VAL GLN          
SEQRES   9 C  395  SER SER LEU VAL MET TYR PRO ILE TYR ALA TYR GLY SER          
SEQRES  10 C  395  ASP GLU GLN ARG LYS LYS TYR LEU PRO GLY LEU VAL SER          
SEQRES  11 C  395  GLY GLU LEU ILE GLY CYS PHE GLY LEU THR GLU PRO ASP          
SEQRES  12 C  395  ALA GLY SER ASP PRO ALA GLY MET LYS THR ARG ALA GLU          
SEQRES  13 C  395  LYS ILE ASP GLY GLY TYR ARG LEU SER GLY SER LYS MET          
SEQRES  14 C  395  TRP ILE SER ASN SER PRO ILE ALA ASP VAL PHE VAL VAL          
SEQRES  15 C  395  TRP ALA LYS SER ALA ALA HIS ASP ASN ALA ILE ARG GLY          
SEQRES  16 C  395  PHE ILE LEU GLU LYS GLY MET LYS GLY LEU SER ALA PRO          
SEQRES  17 C  395  LYS ILE GLY GLY LYS LEU SER LEU ARG ALA SER ILE THR          
SEQRES  18 C  395  GLY GLU ILE VAL MET ASP GLY VAL GLU VAL SER GLU ASP          
SEQRES  19 C  395  ALA ILE LEU PRO ASN VAL SER GLY LEU LYS GLY PRO PHE          
SEQRES  20 C  395  GLY CYS LEU ASN ARG ALA ARG TYR GLY ILE SER TRP GLY          
SEQRES  21 C  395  VAL LEU GLY ALA ALA GLU ASP CYS TRP PHE ARG ALA ARG          
SEQRES  22 C  395  GLN TYR GLY LEU ASP ARG LYS GLN PHE ASN LYS PRO LEU          
SEQRES  23 C  395  ALA GLY THR GLN LEU TYR GLN LYS LYS LEU ALA ASP MET          
SEQRES  24 C  395  GLN THR GLU ILE ALA LEU GLY ILE GLN ALA SER LEU ARG          
SEQRES  25 C  395  VAL GLY ARG LEU PHE ASP GLU GLY LYS MET ALA PRO GLU          
SEQRES  26 C  395  MET ILE SER ILE VAL LYS ARG ASN ASN CYS GLY LYS ALA          
SEQRES  27 C  395  LEU ASP ILE ALA ARG GLN ALA ARG ASP MET HIS GLY GLY          
SEQRES  28 C  395  ASN GLY ILE GLN ILE GLU TYR HIS VAL MET ARG HIS ALA          
SEQRES  29 C  395  GLN ASN LEU GLU THR VAL ASN THR TYR GLU GLY THR HIS          
SEQRES  30 C  395  ASP VAL HIS ALA LEU ILE LEU GLY ARG ALA GLN THR GLY          
SEQRES  31 C  395  ILE GLN ALA PHE PHE                                          
SEQRES   1 D  395  SER MET SER ARG ALA ALA PHE ALA TRP GLU ASP PRO PHE          
SEQRES   2 D  395  LEU LEU GLU GLU GLN LEU THR GLU ASP GLU ARG MET ILE          
SEQRES   3 D  395  ARG ASP SER ALA LYS ALA PHE ALA SER ASP VAL LEU LEU          
SEQRES   4 D  395  PRO ARG VAL GLU LYS ALA TYR LEU GLU GLU THR THR ASP          
SEQRES   5 D  395  PRO GLU LEU PHE HIS LEU MET GLY GLN ALA GLY LEU LEU          
SEQRES   6 D  395  GLY VAL THR LEU PRO GLU ASP TYR GLY ALA ALA ASN ALA          
SEQRES   7 D  395  SER TYR VAL ALA TYR GLY LEU VAL ALA ARG GLU VAL GLU          
SEQRES   8 D  395  ARG ILE ASP SER GLY TYR ARG SER MET MET SER VAL GLN          
SEQRES   9 D  395  SER SER LEU VAL MET TYR PRO ILE TYR ALA TYR GLY SER          
SEQRES  10 D  395  ASP GLU GLN ARG LYS LYS TYR LEU PRO GLY LEU VAL SER          
SEQRES  11 D  395  GLY GLU LEU ILE GLY CYS PHE GLY LEU THR GLU PRO ASP          
SEQRES  12 D  395  ALA GLY SER ASP PRO ALA GLY MET LYS THR ARG ALA GLU          
SEQRES  13 D  395  LYS ILE ASP GLY GLY TYR ARG LEU SER GLY SER LYS MET          
SEQRES  14 D  395  TRP ILE SER ASN SER PRO ILE ALA ASP VAL PHE VAL VAL          
SEQRES  15 D  395  TRP ALA LYS SER ALA ALA HIS ASP ASN ALA ILE ARG GLY          
SEQRES  16 D  395  PHE ILE LEU GLU LYS GLY MET LYS GLY LEU SER ALA PRO          
SEQRES  17 D  395  LYS ILE GLY GLY LYS LEU SER LEU ARG ALA SER ILE THR          
SEQRES  18 D  395  GLY GLU ILE VAL MET ASP GLY VAL GLU VAL SER GLU ASP          
SEQRES  19 D  395  ALA ILE LEU PRO ASN VAL SER GLY LEU LYS GLY PRO PHE          
SEQRES  20 D  395  GLY CYS LEU ASN ARG ALA ARG TYR GLY ILE SER TRP GLY          
SEQRES  21 D  395  VAL LEU GLY ALA ALA GLU ASP CYS TRP PHE ARG ALA ARG          
SEQRES  22 D  395  GLN TYR GLY LEU ASP ARG LYS GLN PHE ASN LYS PRO LEU          
SEQRES  23 D  395  ALA GLY THR GLN LEU TYR GLN LYS LYS LEU ALA ASP MET          
SEQRES  24 D  395  GLN THR GLU ILE ALA LEU GLY ILE GLN ALA SER LEU ARG          
SEQRES  25 D  395  VAL GLY ARG LEU PHE ASP GLU GLY LYS MET ALA PRO GLU          
SEQRES  26 D  395  MET ILE SER ILE VAL LYS ARG ASN ASN CYS GLY LYS ALA          
SEQRES  27 D  395  LEU ASP ILE ALA ARG GLN ALA ARG ASP MET HIS GLY GLY          
SEQRES  28 D  395  ASN GLY ILE GLN ILE GLU TYR HIS VAL MET ARG HIS ALA          
SEQRES  29 D  395  GLN ASN LEU GLU THR VAL ASN THR TYR GLU GLY THR HIS          
SEQRES  30 D  395  ASP VAL HIS ALA LEU ILE LEU GLY ARG ALA GLN THR GLY          
SEQRES  31 D  395  ILE GLN ALA PHE PHE                                          
HET    EDO  A 401       4                                                       
HET    EDO  A 402       4                                                       
HET    EDO  C 401       4                                                       
HET    EDO  D 401       4                                                       
HET    EDO  D 402       4                                                       
HET    EDO  D 403       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  EDO    6(C2 H6 O2)                                                  
FORMUL  11  HOH   *330(H2 O)                                                    
HELIX    1 AA1 LEU A   13  LEU A   18  5                                   6    
HELIX    2 AA2 THR A   19  VAL A   36  1                                  18    
HELIX    3 AA3 VAL A   36  GLU A   42  1                                   7    
HELIX    4 AA4 PRO A   52  ALA A   61  1                                  10    
HELIX    5 AA5 PRO A   69  GLY A   73  5                                   5    
HELIX    6 AA6 SER A   78  ARG A   91  1                                  14    
HELIX    7 AA7 ASP A   93  LEU A  106  1                                  14    
HELIX    8 AA8 VAL A  107  GLY A  115  1                                   9    
HELIX    9 AA9 SER A  116  GLY A  130  1                                  15    
HELIX   10 AB1 SER A  173  ALA A  176  5                                   4    
HELIX   11 AB2 LEU A  242  ARG A  278  1                                  37    
HELIX   12 AB3 THR A  288  GLU A  318  1                                  31    
HELIX   13 AB4 ALA A  322  MET A  347  1                                  26    
HELIX   14 AB5 HIS A  358  TYR A  372  1                                  15    
HELIX   15 AB6 THR A  375  GLY A  389  1                                  15    
HELIX   16 AB7 LEU B   13  GLN B   17  5                                   5    
HELIX   17 AB8 THR B   19  VAL B   36  1                                  18    
HELIX   18 AB9 VAL B   36  GLU B   42  1                                   7    
HELIX   19 AC1 PRO B   52  GLY B   62  1                                  11    
HELIX   20 AC2 PRO B   69  GLY B   73  5                                   5    
HELIX   21 AC3 SER B   78  ARG B   91  1                                  14    
HELIX   22 AC4 ASP B   93  LEU B  106  1                                  14    
HELIX   23 AC5 VAL B  107  GLY B  115  1                                   9    
HELIX   24 AC6 SER B  116  SER B  129  1                                  14    
HELIX   25 AC7 SER B  173  ALA B  176  5                                   4    
HELIX   26 AC8 ALA B  187  ASP B  189  5                                   3    
HELIX   27 AC9 ASP B  233  ILE B  235  5                                   3    
HELIX   28 AD1 LEU B  242  ARG B  278  1                                  37    
HELIX   29 AD2 THR B  288  GLU B  318  1                                  31    
HELIX   30 AD3 ALA B  322  HIS B  348  1                                  27    
HELIX   31 AD4 TYR B  357  TYR B  372  1                                  16    
HELIX   32 AD5 THR B  375  GLY B  389  1                                  15    
HELIX   33 AD6 LEU C   13  LEU C   18  5                                   6    
HELIX   34 AD7 THR C   19  VAL C   36  1                                  18    
HELIX   35 AD8 VAL C   36  GLU C   42  1                                   7    
HELIX   36 AD9 ASP C   51  ALA C   61  1                                  11    
HELIX   37 AE1 PRO C   69  GLY C   73  5                                   5    
HELIX   38 AE2 SER C   78  ARG C   91  1                                  14    
HELIX   39 AE3 ASP C   93  LEU C  106  1                                  14    
HELIX   40 AE4 VAL C  107  GLY C  115  1                                   9    
HELIX   41 AE5 SER C  116  SER C  129  1                                  14    
HELIX   42 AE6 SER C  173  ALA C  176  5                                   4    
HELIX   43 AE7 LEU C  242  ARG C  278  1                                  37    
HELIX   44 AE8 THR C  288  GLU C  318  1                                  31    
HELIX   45 AE9 ALA C  322  HIS C  348  1                                  27    
HELIX   46 AF1 VAL C  359  TYR C  372  1                                  14    
HELIX   47 AF2 THR C  375  GLY C  389  1                                  15    
HELIX   48 AF3 LEU D   13  LEU D   18  5                                   6    
HELIX   49 AF4 THR D   19  VAL D   36  1                                  18    
HELIX   50 AF5 VAL D   36  GLU D   42  1                                   7    
HELIX   51 AF6 ASP D   51  ALA D   61  1                                  11    
HELIX   52 AF7 PRO D   69  GLY D   73  5                                   5    
HELIX   53 AF8 SER D   78  ARG D   91  1                                  14    
HELIX   54 AF9 ASP D   93  LEU D  106  1                                  14    
HELIX   55 AG1 VAL D  107  GLY D  115  1                                   9    
HELIX   56 AG2 SER D  116  SER D  129  1                                  14    
HELIX   57 AG3 SER D  173  ALA D  176  5                                   4    
HELIX   58 AG4 ASP D  233  ILE D  235  5                                   3    
HELIX   59 AG5 LEU D  242  ARG D  278  1                                  37    
HELIX   60 AG6 THR D  288  GLU D  318  1                                  31    
HELIX   61 AG7 ALA D  322  HIS D  348  1                                  27    
HELIX   62 AG8 TYR D  357  TYR D  372  1                                  16    
HELIX   63 AG9 THR D  375  GLY D  389  1                                  15    
SHEET    1 AA1 6 GLY A 134  GLY A 137  0                                        
SHEET    2 AA1 6 VAL A 178  SER A 185  1  O  VAL A 180   N  GLY A 137           
SHEET    3 AA1 6 ARG A 153  ILE A 157  1  N  ALA A 154   O  LYS A 184           
SHEET    4 AA1 6 GLY A 160  SER A 171 -1  O  GLY A 160   N  ILE A 157           
SHEET    5 AA1 6 THR A 220  SER A 231 -1  O  VAL A 230   N  TYR A 161           
SHEET    6 AA1 6 LEU A 204  SER A 205 -1  N  SER A 205   O  VAL A 224           
SHEET    1 AA2 4 GLY A 134  GLY A 137  0                                        
SHEET    2 AA2 4 VAL A 178  SER A 185  1  O  VAL A 180   N  GLY A 137           
SHEET    3 AA2 4 ILE A 192  GLU A 198 -1  O  LEU A 197   N  PHE A 179           
SHEET    4 AA2 4 ILE A 235  LEU A 236 -1  O  LEU A 236   N  GLY A 194           
SHEET    1 AA3 2 LYS A 279  GLN A 280  0                                        
SHEET    2 AA3 2 LYS A 283  PRO A 284 -1  O  LYS A 283   N  GLN A 280           
SHEET    1 AA4 3 GLY B 134  GLY B 137  0                                        
SHEET    2 AA4 3 VAL B 178  SER B 185  1  O  VAL B 180   N  GLY B 137           
SHEET    3 AA4 3 ILE B 192  GLU B 198 -1  O  LEU B 197   N  PHE B 179           
SHEET    1 AA5 6 GLY B 134  GLY B 137  0                                        
SHEET    2 AA5 6 VAL B 178  SER B 185  1  O  VAL B 180   N  GLY B 137           
SHEET    3 AA5 6 ARG B 153  ILE B 157  1  N  ALA B 154   O  LYS B 184           
SHEET    4 AA5 6 GLY B 160  SER B 171 -1  O  GLY B 160   N  ILE B 157           
SHEET    5 AA5 6 THR B 220  SER B 231 -1  O  GLY B 221   N  ILE B 170           
SHEET    6 AA5 6 LEU B 204  SER B 205 -1  N  SER B 205   O  VAL B 224           
SHEET    1 AA6 2 LYS B 279  GLN B 280  0                                        
SHEET    2 AA6 2 LYS B 283  PRO B 284 -1  O  LYS B 283   N  GLN B 280           
SHEET    1 AA7 3 GLY C 134  GLY C 137  0                                        
SHEET    2 AA7 3 VAL C 178  SER C 185  1  O  VAL C 180   N  GLY C 137           
SHEET    3 AA7 3 ILE C 192  GLU C 198 -1  O  LEU C 197   N  PHE C 179           
SHEET    1 AA8 6 GLY C 134  GLY C 137  0                                        
SHEET    2 AA8 6 VAL C 178  SER C 185  1  O  VAL C 180   N  GLY C 137           
SHEET    3 AA8 6 ARG C 153  ILE C 157  1  N  ALA C 154   O  LYS C 184           
SHEET    4 AA8 6 GLY C 160  SER C 171 -1  O  GLY C 160   N  ILE C 157           
SHEET    5 AA8 6 THR C 220  SER C 231 -1  O  VAL C 228   N  LEU C 163           
SHEET    6 AA8 6 LEU C 204  SER C 205 -1  N  SER C 205   O  VAL C 224           
SHEET    1 AA9 2 LYS C 279  GLN C 280  0                                        
SHEET    2 AA9 2 LYS C 283  PRO C 284 -1  O  LYS C 283   N  GLN C 280           
SHEET    1 AB1 3 GLY D 134  GLY D 137  0                                        
SHEET    2 AB1 3 VAL D 178  SER D 185  1  O  VAL D 180   N  GLY D 137           
SHEET    3 AB1 3 ILE D 192  GLU D 198 -1  O  LEU D 197   N  PHE D 179           
SHEET    1 AB2 6 GLY D 134  GLY D 137  0                                        
SHEET    2 AB2 6 VAL D 178  SER D 185  1  O  VAL D 180   N  GLY D 137           
SHEET    3 AB2 6 ARG D 153  ILE D 157  1  N  ALA D 154   O  LYS D 184           
SHEET    4 AB2 6 GLY D 160  SER D 171 -1  O  GLY D 160   N  ILE D 157           
SHEET    5 AB2 6 THR D 220  SER D 231 -1  O  GLY D 221   N  ILE D 170           
SHEET    6 AB2 6 LEU D 204  SER D 205 -1  N  SER D 205   O  VAL D 224           
SHEET    1 AB3 2 LYS D 279  GLN D 280  0                                        
SHEET    2 AB3 2 LYS D 283  PRO D 284 -1  O  LYS D 283   N  GLN D 280           
CISPEP   1 HIS A  188    ASP A  189          0       -19.45                     
CISPEP   2 GLU C  373    GLY C  374          0       -15.10                     
SITE     1 AC1  2 GLN A 387  ARG B 272                                          
SITE     1 AC2  1 HOH A 545                                                     
SITE     1 AC3  7 THR C  67  TYR C  79  TYR C  82  SER C 104                    
SITE     2 AC3  7 SER C 105  TYR C 109  ARG C 251                               
SITE     1 AC4  2 ASP D  27  SER D  28                                          
SITE     1 AC5  3 ASP D 266  PHE D 269  ARG D 270                               
SITE     1 AC6  2 ARG C 272  HOH D 559                                          
CRYST1   82.020  106.660   99.390  90.00 108.12  90.00 P 1 21 1      8          
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      0.012192  0.000000  0.003990        0.00000                         
SCALE2      0.000000  0.009376  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010586        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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