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Database: PDB
Entry: 3THX
LinkDB: 3THX
Original site: 3THX 
HEADER    DNA BINDING PROTEIN/DNA                 19-AUG-11   3THX              
TITLE     HUMAN MUTSBETA COMPLEXED WITH AN IDL OF 3 BASES (LOOP3) AND ADP       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA MISMATCH REPAIR PROTEIN MSH2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HMSH2, MUTS PROTEIN HOMOLOG 2;                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA MISMATCH REPAIR PROTEIN MSH3;                          
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 219-1137;                                     
COMPND  10 SYNONYM: HMSH3, DIVERGENT UPSTREAM PROTEIN, DUP, MISMATCH REPAIR     
COMPND  11 PROTEIN 1, MRP1;                                                     
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA LOOP3 MINUS STRAND;                                    
COMPND  15 CHAIN: D;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: DNA LOOP3 PLUS STRAND;                                     
COMPND  19 CHAIN: E;                                                            
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MSH2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HI5;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: DUC1, DUG, MSH3;                                               
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: HI5;                                    
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 SYNTHETIC: YES;                                                      
SOURCE  19 OTHER_DETAILS: CHEMICALLY SYNTHESIZED;                               
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 SYNTHETIC: YES;                                                      
SOURCE  22 OTHER_DETAILS: CHEMICALLY SYNTHESIZED                                
KEYWDS    ABC FAMILY ATPASE, MISMATCH RECOGNITION, MISMATCHED UNPAIRED IDL DNA, 
KEYWDS   2 DNA BINDING PROTEIN-DNA COMPLEX                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.YANG                                                                
REVDAT   3   17-JUL-19 3THX    1       REMARK DBREF                             
REVDAT   2   26-JUN-13 3THX    1       JRNL                                     
REVDAT   1   21-DEC-11 3THX    0                                                
JRNL        AUTH   S.GUPTA,M.GELLERT,W.YANG                                     
JRNL        TITL   MECHANISM OF MISMATCH RECOGNITION REVEALED BY HUMAN MUTSBETA 
JRNL        TITL 2 BOUND TO UNPAIRED DNA LOOPS                                  
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  19    72 2012              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   22179786                                                     
JRNL        DOI    10.1038/NSMB.2175                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 49511                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.770                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1315                            
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 27.0202 -  5.6004    0.98     5791   174  0.1666 0.2281        
REMARK   3     2  5.6004 -  4.4517    0.97     5828   144  0.1663 0.2264        
REMARK   3     3  4.4517 -  3.8908    0.96     5718   160  0.1753 0.2499        
REMARK   3     4  3.8908 -  3.5359    0.94     5597   173  0.2201 0.2665        
REMARK   3     5  3.5359 -  3.2830    0.93     5580   182  0.2494 0.2941        
REMARK   3     6  3.2830 -  3.0897    0.90     5363   147  0.2718 0.3271        
REMARK   3     7  3.0897 -  2.9351    0.84     5039   152  0.3067 0.3944        
REMARK   3     8  2.9351 -  2.8075    0.73     4345   117  0.3380 0.3836        
REMARK   3     9  2.8075 -  2.6995    0.48     2915    66  0.3544 0.4280        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.30                                          
REMARK   3   B_SOL              : 43.35                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.35970                                              
REMARK   3    B22 (A**2) : 1.11400                                              
REMARK   3    B33 (A**2) : -6.47370                                             
REMARK   3    B12 (A**2) : -0.08190                                             
REMARK   3    B13 (A**2) : 3.51020                                              
REMARK   3    B23 (A**2) : 1.66950                                              
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      :  0.002          14985                                  
REMARK   3   ANGLE     :  0.558          20474                                  
REMARK   3   CHIRALITY :  0.037           2359                                  
REMARK   3   PLANARITY :  0.002           2446                                  
REMARK   3   DIHEDRAL  : 15.555           5669                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 12:145                                
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0727  -3.3289  27.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3203 T22:   0.1721                                     
REMARK   3      T33:   0.3298 T12:  -0.0459                                     
REMARK   3      T13:  -0.1128 T23:  -0.0795                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8183 L22:   0.7440                                     
REMARK   3      L33:   1.2859 L12:  -0.6521                                     
REMARK   3      L13:   0.1999 L23:   0.3475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0143 S12:  -0.0710 S13:   0.2083                       
REMARK   3      S21:   0.2817 S22:   0.0298 S23:  -0.3844                       
REMARK   3      S31:   0.1412 S32:  -0.2013 S33:  -0.0208                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 146:250                               
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6219 -21.0726   5.1843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4047 T22:   0.2834                                     
REMARK   3      T33:   0.3060 T12:  -0.0208                                     
REMARK   3      T13:   0.0505 T23:   0.0550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3001 L22:   0.9364                                     
REMARK   3      L33:   2.7821 L12:   0.2522                                     
REMARK   3      L13:  -0.5122 L23:  -1.6241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1636 S12:   0.0359 S13:  -0.0354                       
REMARK   3      S21:  -0.4107 S22:  -0.2174 S23:  -0.3183                       
REMARK   3      S31:   0.4645 S32:   0.3262 S33:   0.2660                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 251:380                               
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8765 -23.8206  -1.4278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4870 T22:   0.3679                                     
REMARK   3      T33:   0.1470 T12:  -0.2007                                     
REMARK   3      T13:   0.0442 T23:  -0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6547 L22:   0.6948                                     
REMARK   3      L33:   1.3271 L12:   0.6428                                     
REMARK   3      L13:  -0.6799 L23:  -0.8180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3838 S12:   0.3514 S13:  -0.1092                       
REMARK   3      S21:  -0.1660 S22:   0.2715 S23:  -0.0204                       
REMARK   3      S31:   0.5927 S32:  -0.5055 S33:   0.1197                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 381:501                               
REMARK   3    ORIGIN FOR THE GROUP (A): -27.3323 -29.4715  17.1540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5445 T22:   0.5889                                     
REMARK   3      T33:   0.4383 T12:  -0.2844                                     
REMARK   3      T13:   0.0984 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5392 L22:   1.0559                                     
REMARK   3      L33:   1.0156 L12:   0.0055                                     
REMARK   3      L13:  -0.7994 L23:   0.8026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7033 S12:   0.3031 S13:   0.1317                       
REMARK   3      S21:   0.3426 S22:   0.3287 S23:   0.3668                       
REMARK   3      S31:   0.4844 S32:  -0.1940 S33:   0.2827                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 502:580                               
REMARK   3    ORIGIN FOR THE GROUP (A): -36.1115 -16.3754  48.4112              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1977 T22:   1.0372                                     
REMARK   3      T33:   0.9519 T12:  -0.1119                                     
REMARK   3      T13:   0.3243 T23:  -0.2435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6997 L22:   0.2964                                     
REMARK   3      L33:   0.9324 L12:  -0.3494                                     
REMARK   3      L13:  -0.5443 L23:  -0.0026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5791 S12:  -0.2991 S13:   0.0619                       
REMARK   3      S21:   0.0634 S22:  -0.1030 S23:   0.0198                       
REMARK   3      S31:  -0.5403 S32:   0.1628 S33:  -0.3752                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 581:850                               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9343  -6.9536 -22.1079              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3486 T22:   0.5811                                     
REMARK   3      T33:   0.1444 T12:  -0.1232                                     
REMARK   3      T13:  -0.0316 T23:   0.1079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5350 L22:   0.6459                                     
REMARK   3      L33:   1.4565 L12:   0.4170                                     
REMARK   3      L13:  -0.8878 L23:  -0.3855                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1797 S12:   0.5528 S13:   0.0767                       
REMARK   3      S21:  -0.3636 S22:   0.2841 S23:   0.0877                       
REMARK   3      S31:   0.2974 S32:  -0.8077 S33:  -0.0926                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 852:950                               
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5694  19.4576 -52.9723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5634 T22:   0.4299                                     
REMARK   3      T33:   0.2492 T12:  -0.1548                                     
REMARK   3      T13:   0.0540 T23:   0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7588 L22:   0.7756                                     
REMARK   3      L33:   0.3624 L12:   0.1991                                     
REMARK   3      L13:  -0.6535 L23:   0.0341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6267 S12:   0.0549 S13:  -0.1089                       
REMARK   3      S21:  -0.1726 S22:   0.2558 S23:  -0.0164                       
REMARK   3      S31:   0.4137 S32:   0.2239 S33:   0.3220                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 217:351                               
REMARK   3    ORIGIN FOR THE GROUP (A): -23.7749  12.3329  23.3579              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1486 T22:   0.4099                                     
REMARK   3      T33:   0.3616 T12:   0.0311                                     
REMARK   3      T13:  -0.0451 T23:  -0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6847 L22:   1.1190                                     
REMARK   3      L33:   1.8656 L12:  -0.8134                                     
REMARK   3      L13:  -0.9648 L23:   0.7338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0809 S12:   0.4147 S13:  -0.0555                       
REMARK   3      S21:   0.0778 S22:  -0.1687 S23:   0.1749                       
REMARK   3      S31:  -0.0362 S32:  -0.6343 S33:   0.0835                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 352:471                               
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0523  25.3828  -0.1066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4568 T22:   0.7146                                     
REMARK   3      T33:   0.2718 T12:   0.3138                                     
REMARK   3      T13:   0.0201 T23:   0.1072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0473 L22:   1.0362                                     
REMARK   3      L33:   0.5160 L12:  -0.6497                                     
REMARK   3      L13:  -1.0080 L23:   0.4037                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4699 S12:   1.0104 S13:   0.0389                       
REMARK   3      S21:  -0.4740 S22:  -0.3399 S23:   0.1049                       
REMARK   3      S31:  -0.2640 S32:  -0.5919 S33:  -0.1254                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND RESI 472:591                               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4852  29.7557   6.2233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4170 T22:   0.2215                                     
REMARK   3      T33:   0.2982 T12:   0.1243                                     
REMARK   3      T13:   0.1404 T23:   0.0857                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0327 L22:   0.4635                                     
REMARK   3      L33:   1.0600 L12:  -0.1243                                     
REMARK   3      L13:  -0.5916 L23:   0.6995                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3930 S12:   0.1793 S13:   0.0708                       
REMARK   3      S21:  -0.1513 S22:  -0.0456 S23:  -0.1642                       
REMARK   3      S31:  -0.5136 S32:  -0.2171 S33:  -0.3098                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND RESI 592:791                               
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7414  26.5308  42.8282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2112 T22:   0.1651                                     
REMARK   3      T33:   0.2008 T12:  -0.0192                                     
REMARK   3      T13:   0.0716 T23:  -0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6308 L22:   0.3165                                     
REMARK   3      L33:   1.1357 L12:   0.4652                                     
REMARK   3      L13:  -1.3421 L23:  -0.3124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2072 S12:  -0.2629 S13:   0.1397                       
REMARK   3      S21:   0.0866 S22:  -0.0012 S23:  -0.0017                       
REMARK   3      S31:  -0.2582 S32:   0.2037 S33:  -0.0772                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN B AND RESI 792:991                               
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7398  26.1262  -1.9586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3046 T22:   0.1052                                     
REMARK   3      T33:   0.2549 T12:   0.0890                                     
REMARK   3      T13:   0.1622 T23:   0.0786                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8545 L22:   0.3761                                     
REMARK   3      L33:   1.7718 L12:  -0.1997                                     
REMARK   3      L13:  -1.1428 L23:   0.7072                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4328 S12:   0.1023 S13:   0.3794                       
REMARK   3      S21:  -0.2527 S22:   0.0694 S23:  -0.1954                       
REMARK   3      S31:  -0.5548 S32:  -0.1169 S33:  -0.4191                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN B AND RESI 992:1120                              
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3318  15.5792 -27.7790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4263 T22:   0.2864                                     
REMARK   3      T33:   0.2793 T12:  -0.0137                                     
REMARK   3      T13:   0.1465 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0791 L22:   0.8849                                     
REMARK   3      L33:   1.3143 L12:   0.3809                                     
REMARK   3      L13:  -0.1637 L23:  -0.7598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0041 S12:   0.0107 S13:   0.0093                       
REMARK   3      S21:  -0.1698 S22:   0.2623 S23:   0.0970                       
REMARK   3      S31:  -0.1036 S32:   0.0343 S33:  -0.1918                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN D AND RESI 3:14                                  
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6469  -3.1854  53.6857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1477 T22:   0.9747                                     
REMARK   3      T33:   0.9685 T12:   0.4590                                     
REMARK   3      T13:  -0.1318 T23:   0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5146 L22:   1.8309                                     
REMARK   3      L33:   3.0918 L12:   0.7864                                     
REMARK   3      L13:  -0.5842 L23:   0.2143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0120 S12:  -0.2875 S13:  -0.2974                       
REMARK   3      S21:  -0.2904 S22:   0.1271 S23:   0.3009                       
REMARK   3      S31:  -0.4770 S32:   0.3335 S33:  -0.1193                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN D AND RESI 15:23                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.2756   5.4098  37.9549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3030 T22:   0.7338                                     
REMARK   3      T33:   0.7429 T12:  -0.0657                                     
REMARK   3      T13:   0.1111 T23:  -0.1128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0337 L22:   1.0130                                     
REMARK   3      L33:   0.9729 L12:   1.7028                                     
REMARK   3      L13:  -0.4966 L23:  -0.5925                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1806 S12:   0.7222 S13:  -1.2214                       
REMARK   3      S21:   0.0298 S22:   0.5941 S23:  -0.6643                       
REMARK   3      S31:   0.0759 S32:  -0.4589 S33:   0.5515                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN E AND RESI 26:35                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -42.2013   5.9565  39.0474              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5590 T22:   0.9178                                     
REMARK   3      T33:   0.7152 T12:  -0.2044                                     
REMARK   3      T13:   0.2157 T23:  -0.1129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0650 L22:   1.6118                                     
REMARK   3      L33:   5.5857 L12:   2.1914                                     
REMARK   3      L13:   1.3700 L23:   0.6721                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0233 S12:   0.3892 S13:   0.7885                       
REMARK   3      S21:   0.0575 S22:  -0.1876 S23:  -0.3211                       
REMARK   3      S31:   0.6031 S32:  -1.6683 S33:   1.0104                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN E AND RESI 36:38                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.7778   0.8705  31.1023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1864 T22:   0.6046                                     
REMARK   3      T33:   0.8216 T12:  -0.1744                                     
REMARK   3      T13:   0.0558 T23:  -0.3444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2539 L22:   1.9344                                     
REMARK   3      L33:   8.2199 L12:   0.3198                                     
REMARK   3      L13:   1.2076 L23:   0.5520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7194 S12:  -0.4255 S13:  -0.0923                       
REMARK   3      S21:   0.0725 S22:  -1.0375 S23:   0.5970                       
REMARK   3      S31:  -0.0597 S32:  -0.0811 S33:   1.6645                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN E AND RESI 39                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7089   3.5145  34.9226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2723 T22:   0.8763                                     
REMARK   3      T33:   1.0080 T12:   0.4480                                     
REMARK   3      T13:  -0.0180 T23:   0.0906                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7640 L22:   0.9593                                     
REMARK   3      L33:   0.5812 L12:  -0.8244                                     
REMARK   3      L13:  -0.4345 L23:   0.3148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2314 S12:   0.0759 S13:  -0.5350                       
REMARK   3      S21:   0.1385 S22:   0.5154 S23:  -0.0516                       
REMARK   3      S31:  -0.0072 S32:  -0.0969 S33:  -0.6546                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN E AND RESI 40:50                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4705  -2.9736  53.1995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8781 T22:   0.6472                                     
REMARK   3      T33:   0.4984 T12:   0.4373                                     
REMARK   3      T13:   0.0634 T23:  -0.1278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4810 L22:   7.0395                                     
REMARK   3      L33:   4.7312 L12:  -0.0388                                     
REMARK   3      L13:  -1.9605 L23:  -4.5923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1265 S12:  -0.7657 S13:  -0.0410                       
REMARK   3      S21:   1.2098 S22:   0.7310 S23:   0.3734                       
REMARK   3      S31:   0.2143 S32:   0.8179 S33:  -0.3947                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN G                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0569   2.1047 -21.8621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6220 T22:   1.2649                                     
REMARK   3      T33:   0.8631 T12:   0.0010                                     
REMARK   3      T13:  -0.0618 T23:   0.2333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9875 L22:   1.1620                                     
REMARK   3      L33:   1.3135 L12:   1.1831                                     
REMARK   3      L13:   1.4256 L23:   1.1986                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3032 S12:  -0.6856 S13:   0.6138                       
REMARK   3      S21:  -0.0623 S22:   0.3902 S23:   0.4058                       
REMARK   3      S31:   0.1245 S32:  -0.4425 S33:  -0.0460                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3THX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000067498.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5-7.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN A200                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 43.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.440                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 20-25% PEG3350    
REMARK 280  (W/V) AND 0.1M MES PH 6.5-7.5, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 14930 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 78240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E                            
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     ASN A   109                                                      
REMARK 465     LYS A   110                                                      
REMARK 465     ALA A   111                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     ASN A   138                                                      
REMARK 465     ASN A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     MET A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     ALA A   143                                                      
REMARK 465     SER A   144                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     SER A   316                                                      
REMARK 465     VAL A   317                                                      
REMARK 465     GLU A   318                                                      
REMARK 465     ASP A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     THR A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     SER A   323                                                      
REMARK 465     GLN A   518                                                      
REMARK 465     PHE A   519                                                      
REMARK 465     LYS A   546                                                      
REMARK 465     ASN A   547                                                      
REMARK 465     ASP A   646                                                      
REMARK 465     GLU A   647                                                      
REMARK 465     ALA A   714                                                      
REMARK 465     GLY A   715                                                      
REMARK 465     ASP A   716                                                      
REMARK 465     SER A   717                                                      
REMARK 465     GLN A   718                                                      
REMARK 465     LEU A   719                                                      
REMARK 465     LYS A   720                                                      
REMARK 465     GLY A   721                                                      
REMARK 465     VAL A   722                                                      
REMARK 465     ILE A   857                                                      
REMARK 465     GLY A   858                                                      
REMARK 465     GLU A   859                                                      
REMARK 465     SER A   860                                                      
REMARK 465     GLN A   861                                                      
REMARK 465     GLY A   862                                                      
REMARK 465     TYR A   863                                                      
REMARK 465     ASP A   864                                                      
REMARK 465     ILE A   865                                                      
REMARK 465     MET A   866                                                      
REMARK 465     GLU A   867                                                      
REMARK 465     PRO A   868                                                      
REMARK 465     ALA A   869                                                      
REMARK 465     ALA A   870                                                      
REMARK 465     LYS A   871                                                      
REMARK 465     LYS A   931                                                      
REMARK 465     VAL A   932                                                      
REMARK 465     THR A   933                                                      
REMARK 465     THR A   934                                                      
REMARK 465     GLY B   208                                                      
REMARK 465     PRO B   209                                                      
REMARK 465     LYS B   210                                                      
REMARK 465     SER B   211                                                      
REMARK 465     ALA B   212                                                      
REMARK 465     ASN B   213                                                      
REMARK 465     LYS B   214                                                      
REMARK 465     ARG B   215                                                      
REMARK 465     SER B   216                                                      
REMARK 465     ASP B   342                                                      
REMARK 465     ASP B   343                                                      
REMARK 465     GLU B   367                                                      
REMARK 465     ASN B   368                                                      
REMARK 465     VAL B   369                                                      
REMARK 465     ARG B   370                                                      
REMARK 465     ASP B   371                                                      
REMARK 465     LYS B   372                                                      
REMARK 465     LYS B   373                                                      
REMARK 465     LYS B   374                                                      
REMARK 465     GLY B   375                                                      
REMARK 465     LYS B   469                                                      
REMARK 465     ASP B   470                                                      
REMARK 465     THR B   471                                                      
REMARK 465     VAL B   472                                                      
REMARK 465     ASP B   473                                                      
REMARK 465     ILE B   474                                                      
REMARK 465     LYS B   475                                                      
REMARK 465     GLY B   476                                                      
REMARK 465     SER B   477                                                      
REMARK 465     GLN B   478                                                      
REMARK 465     ILE B   479                                                      
REMARK 465     ILE B   480                                                      
REMARK 465     SER B   481                                                      
REMARK 465     GLY B   482                                                      
REMARK 465     GLY B   931                                                      
REMARK 465     ALA B   932                                                      
REMARK 465     ALA B   933                                                      
REMARK 465     ASP B   934                                                      
REMARK 465     ASN B   935                                                      
REMARK 465     ILE B   936                                                      
REMARK 465     TYR B   937                                                      
REMARK 465     LYS B   938                                                      
REMARK 465     GLY B   939                                                      
REMARK 465     ARG B   940                                                      
REMARK 465     GLU B  1027                                                      
REMARK 465     ASP B  1028                                                      
REMARK 465     GLU B  1029                                                      
REMARK 465     SER B  1030                                                      
REMARK 465     LYS B  1031                                                      
REMARK 465     LEU B  1032                                                      
REMARK 465     ASP B  1033                                                      
REMARK 465     PRO B  1034                                                      
REMARK 465     GLY B  1035                                                      
REMARK 465     ALA B  1036                                                      
REMARK 465     ALA B  1037                                                      
REMARK 465     GLU B  1038                                                      
REMARK 465     GLN B  1039                                                      
REMARK 465     VAL B  1040                                                      
REMARK 465     PRO B  1041                                                      
REMARK 465     ASP B  1042                                                      
REMARK 465     PHE B  1043                                                      
REMARK 465     GLU B  1121                                                      
REMARK 465     THR B  1122                                                      
REMARK 465     GLN B  1123                                                      
REMARK 465     THR B  1124                                                      
REMARK 465     SER B  1125                                                      
REMARK 465      DC D     1                                                      
REMARK 465      DC D     2                                                      
REMARK 465      DG D    24                                                      
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     GLU A  12    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 205    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 264    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 314    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 324    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 397    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 423    CG   CD   CE   NZ                                   
REMARK 470     HIS A 424    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 425    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 431    CG   CD1  CD2                                       
REMARK 470     LYS A 509    CG   CD   CE   NZ                                   
REMARK 470     GLN A 510    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 512    CG   CD   CE   NZ                                   
REMARK 470     ARG A 524    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 526    OG1  CG2                                            
REMARK 470     ILE A 544    CG1  CG2  CD1                                       
REMARK 470     ASN A 835    CG   OD1  ND2                                       
REMARK 470     LYS A 838    CG   CD   CE   NZ                                   
REMARK 470     TYR A 856    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 872    CG   CD   CE   NZ                                   
REMARK 470     CYS A 873    SG                                                  
REMARK 470     TYR A 874    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 875    CG   CD1  CD2                                       
REMARK 470     GLU A 878    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 882    CG   CD   CE   NZ                                   
REMARK 470     GLN A 893    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 902    CG   CD   OE1  OE2                                  
REMARK 470     SER A 921    OG                                                  
REMARK 470     LYS B 217    CG   CD   CE   NZ                                   
REMARK 470     GLU B 252    CG   CD   OE1  OE2                                  
REMARK 470     SER B 355    OG                                                  
REMARK 470     LYS B 366    CG   CD   CE   NZ                                   
REMARK 470     ARG B 402    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 440    CB   CG   CD   OE1  NE2                             
REMARK 470     LYS B 522    CG   CD   CE   NZ                                   
REMARK 470     MET B 523    CG   SD   CE                                        
REMARK 470     LYS B 608    CG   CD   CE   NZ                                   
REMARK 470     GLU B 668    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 683    CG   CD   OE1  NE2                                  
REMARK 470     PHE B 700    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B 941    OG                                                  
REMARK 470     VAL B1025    CG1  CG2                                            
REMARK 470     SER B1026    OG                                                  
REMARK 470     VAL B1044    CG1  CG2                                            
REMARK 470     PHE B1046    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B1047    CG   CD1  CD2                                       
REMARK 470     ARG B1057    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B1111    CG   CD   OE1  NE2                                  
REMARK 470      DT D   3    P    OP1  OP2                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG B  607   CA                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DG D  10   C3' -  C2' -  C1' ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DC E  40   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  57      -60.45    -91.87                                   
REMARK 500    ALA A  70      -36.60    -38.08                                   
REMARK 500    VAL A  95      -68.51   -101.77                                   
REMARK 500    SER A 153      124.72   -172.82                                   
REMARK 500    VAL A 155      -72.71    -76.67                                   
REMARK 500    CYS A 176      111.52   -164.96                                   
REMARK 500    GLU A 205     -153.74   -137.13                                   
REMARK 500    ALA A 207     -176.49    -60.60                                   
REMARK 500    LYS A 235      -70.10    -59.01                                   
REMARK 500    LYS A 249       19.72     54.93                                   
REMARK 500    GLN A 288      -29.56   -141.25                                   
REMARK 500    GLU A 378       -3.79   -142.74                                   
REMARK 500    ARG A 396       29.55    -79.87                                   
REMARK 500    LYS A 427     -154.00   -167.59                                   
REMARK 500    GLN A 429       -3.66     68.18                                   
REMARK 500    LEU A 433        7.69    -66.61                                   
REMARK 500    THR A 457      -48.48   -138.71                                   
REMARK 500    ASP A 506      128.64    -34.89                                   
REMARK 500    VAL A 525      147.88   -172.40                                   
REMARK 500    ASN A 536       47.23     35.66                                   
REMARK 500    ALA A 636       73.73     44.97                                   
REMARK 500    VAL A 644      -83.11    -67.24                                   
REMARK 500    LYS A 661      -76.60   -131.37                                   
REMARK 500    ASP A 706      -70.08    -53.55                                   
REMARK 500    GLU A 749       78.88     47.70                                   
REMARK 500    THR A 772      -67.58    -95.05                                   
REMARK 500    PHE A 854       83.87    -65.44                                   
REMARK 500    GLN A 855      -26.19   -148.98                                   
REMARK 500    PRO A 895       48.09    -75.24                                   
REMARK 500    GLU A 898       45.34   -151.54                                   
REMARK 500    TYR B 245       40.54   -101.58                                   
REMARK 500    HIS B 269      -74.14     66.40                                   
REMARK 500    SER B 314       69.13   -101.16                                   
REMARK 500    SER B 355       -4.10     68.38                                   
REMARK 500    ILE B 377      143.58   -170.86                                   
REMARK 500    ASN B 485       72.68   -111.50                                   
REMARK 500    LYS B 512       63.65     65.87                                   
REMARK 500    GLN B 542       49.83    -82.29                                   
REMARK 500    THR B 543       -2.30   -145.94                                   
REMARK 500    ASP B 544      -17.82   -156.38                                   
REMARK 500    LEU B 592      -76.10    -59.72                                   
REMARK 500    SER B 594      126.17   -174.71                                   
REMARK 500    PRO B 756      177.80    -55.57                                   
REMARK 500    LYS B 847      138.65   -178.64                                   
REMARK 500    LEU B 862      -86.87   -139.96                                   
REMARK 500    GLN B 867      -73.70    -78.57                                   
REMARK 500    PRO B 870      151.68    -48.72                                   
REMARK 500    ASP B 878       43.56    -78.95                                   
REMARK 500    SER B 879     -153.45   -174.43                                   
REMARK 500    PHE B1117      -76.18    -53.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 935                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3THW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3THY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3THZ   RELATED DB: PDB                                   
DBREF  3THX A    1   934  UNP    P43246   MSH2_HUMAN       1    934             
DBREF1 3THX B  210  1125  GB                   EAW95862                         
DBREF2 3THX B     119616268                         210        1125             
DBREF  3THX D    1    24  PDB    3THX     3THX             1     24             
DBREF  3THX E   26    50  PDB    3THX     3THX            26     50             
SEQADV 3THX GLY B  208  GB   119616268           EXPRESSION TAG                 
SEQADV 3THX PRO B  209  GB   119616268           EXPRESSION TAG                 
SEQRES   1 A  934  MET ALA VAL GLN PRO LYS GLU THR LEU GLN LEU GLU SER          
SEQRES   2 A  934  ALA ALA GLU VAL GLY PHE VAL ARG PHE PHE GLN GLY MET          
SEQRES   3 A  934  PRO GLU LYS PRO THR THR THR VAL ARG LEU PHE ASP ARG          
SEQRES   4 A  934  GLY ASP PHE TYR THR ALA HIS GLY GLU ASP ALA LEU LEU          
SEQRES   5 A  934  ALA ALA ARG GLU VAL PHE LYS THR GLN GLY VAL ILE LYS          
SEQRES   6 A  934  TYR MET GLY PRO ALA GLY ALA LYS ASN LEU GLN SER VAL          
SEQRES   7 A  934  VAL LEU SER LYS MET ASN PHE GLU SER PHE VAL LYS ASP          
SEQRES   8 A  934  LEU LEU LEU VAL ARG GLN TYR ARG VAL GLU VAL TYR LYS          
SEQRES   9 A  934  ASN ARG ALA GLY ASN LYS ALA SER LYS GLU ASN ASP TRP          
SEQRES  10 A  934  TYR LEU ALA TYR LYS ALA SER PRO GLY ASN LEU SER GLN          
SEQRES  11 A  934  PHE GLU ASP ILE LEU PHE GLY ASN ASN ASP MET SER ALA          
SEQRES  12 A  934  SER ILE GLY VAL VAL GLY VAL LYS MET SER ALA VAL ASP          
SEQRES  13 A  934  GLY GLN ARG GLN VAL GLY VAL GLY TYR VAL ASP SER ILE          
SEQRES  14 A  934  GLN ARG LYS LEU GLY LEU CYS GLU PHE PRO ASP ASN ASP          
SEQRES  15 A  934  GLN PHE SER ASN LEU GLU ALA LEU LEU ILE GLN ILE GLY          
SEQRES  16 A  934  PRO LYS GLU CYS VAL LEU PRO GLY GLY GLU THR ALA GLY          
SEQRES  17 A  934  ASP MET GLY LYS LEU ARG GLN ILE ILE GLN ARG GLY GLY          
SEQRES  18 A  934  ILE LEU ILE THR GLU ARG LYS LYS ALA ASP PHE SER THR          
SEQRES  19 A  934  LYS ASP ILE TYR GLN ASP LEU ASN ARG LEU LEU LYS GLY          
SEQRES  20 A  934  LYS LYS GLY GLU GLN MET ASN SER ALA VAL LEU PRO GLU          
SEQRES  21 A  934  MET GLU ASN GLN VAL ALA VAL SER SER LEU SER ALA VAL          
SEQRES  22 A  934  ILE LYS PHE LEU GLU LEU LEU SER ASP ASP SER ASN PHE          
SEQRES  23 A  934  GLY GLN PHE GLU LEU THR THR PHE ASP PHE SER GLN TYR          
SEQRES  24 A  934  MET LYS LEU ASP ILE ALA ALA VAL ARG ALA LEU ASN LEU          
SEQRES  25 A  934  PHE GLN GLY SER VAL GLU ASP THR THR GLY SER GLN SER          
SEQRES  26 A  934  LEU ALA ALA LEU LEU ASN LYS CYS LYS THR PRO GLN GLY          
SEQRES  27 A  934  GLN ARG LEU VAL ASN GLN TRP ILE LYS GLN PRO LEU MET          
SEQRES  28 A  934  ASP LYS ASN ARG ILE GLU GLU ARG LEU ASN LEU VAL GLU          
SEQRES  29 A  934  ALA PHE VAL GLU ASP ALA GLU LEU ARG GLN THR LEU GLN          
SEQRES  30 A  934  GLU ASP LEU LEU ARG ARG PHE PRO ASP LEU ASN ARG LEU          
SEQRES  31 A  934  ALA LYS LYS PHE GLN ARG GLN ALA ALA ASN LEU GLN ASP          
SEQRES  32 A  934  CYS TYR ARG LEU TYR GLN GLY ILE ASN GLN LEU PRO ASN          
SEQRES  33 A  934  VAL ILE GLN ALA LEU GLU LYS HIS GLU GLY LYS HIS GLN          
SEQRES  34 A  934  LYS LEU LEU LEU ALA VAL PHE VAL THR PRO LEU THR ASP          
SEQRES  35 A  934  LEU ARG SER ASP PHE SER LYS PHE GLN GLU MET ILE GLU          
SEQRES  36 A  934  THR THR LEU ASP MET ASP GLN VAL GLU ASN HIS GLU PHE          
SEQRES  37 A  934  LEU VAL LYS PRO SER PHE ASP PRO ASN LEU SER GLU LEU          
SEQRES  38 A  934  ARG GLU ILE MET ASN ASP LEU GLU LYS LYS MET GLN SER          
SEQRES  39 A  934  THR LEU ILE SER ALA ALA ARG ASP LEU GLY LEU ASP PRO          
SEQRES  40 A  934  GLY LYS GLN ILE LYS LEU ASP SER SER ALA GLN PHE GLY          
SEQRES  41 A  934  TYR TYR PHE ARG VAL THR CYS LYS GLU GLU LYS VAL LEU          
SEQRES  42 A  934  ARG ASN ASN LYS ASN PHE SER THR VAL ASP ILE GLN LYS          
SEQRES  43 A  934  ASN GLY VAL LYS PHE THR ASN SER LYS LEU THR SER LEU          
SEQRES  44 A  934  ASN GLU GLU TYR THR LYS ASN LYS THR GLU TYR GLU GLU          
SEQRES  45 A  934  ALA GLN ASP ALA ILE VAL LYS GLU ILE VAL ASN ILE SER          
SEQRES  46 A  934  SER GLY TYR VAL GLU PRO MET GLN THR LEU ASN ASP VAL          
SEQRES  47 A  934  LEU ALA GLN LEU ASP ALA VAL VAL SER PHE ALA HIS VAL          
SEQRES  48 A  934  SER ASN GLY ALA PRO VAL PRO TYR VAL ARG PRO ALA ILE          
SEQRES  49 A  934  LEU GLU LYS GLY GLN GLY ARG ILE ILE LEU LYS ALA SER          
SEQRES  50 A  934  ARG HIS ALA CYS VAL GLU VAL GLN ASP GLU ILE ALA PHE          
SEQRES  51 A  934  ILE PRO ASN ASP VAL TYR PHE GLU LYS ASP LYS GLN MET          
SEQRES  52 A  934  PHE HIS ILE ILE THR GLY PRO ASN MET GLY GLY LYS SER          
SEQRES  53 A  934  THR TYR ILE ARG GLN THR GLY VAL ILE VAL LEU MET ALA          
SEQRES  54 A  934  GLN ILE GLY CYS PHE VAL PRO CYS GLU SER ALA GLU VAL          
SEQRES  55 A  934  SER ILE VAL ASP CYS ILE LEU ALA ARG VAL GLY ALA GLY          
SEQRES  56 A  934  ASP SER GLN LEU LYS GLY VAL SER THR PHE MET ALA GLU          
SEQRES  57 A  934  MET LEU GLU THR ALA SER ILE LEU ARG SER ALA THR LYS          
SEQRES  58 A  934  ASP SER LEU ILE ILE ILE ASP GLU LEU GLY ARG GLY THR          
SEQRES  59 A  934  SER THR TYR ASP GLY PHE GLY LEU ALA TRP ALA ILE SER          
SEQRES  60 A  934  GLU TYR ILE ALA THR LYS ILE GLY ALA PHE CYS MET PHE          
SEQRES  61 A  934  ALA THR HIS PHE HIS GLU LEU THR ALA LEU ALA ASN GLN          
SEQRES  62 A  934  ILE PRO THR VAL ASN ASN LEU HIS VAL THR ALA LEU THR          
SEQRES  63 A  934  THR GLU GLU THR LEU THR MET LEU TYR GLN VAL LYS LYS          
SEQRES  64 A  934  GLY VAL CYS ASP GLN SER PHE GLY ILE HIS VAL ALA GLU          
SEQRES  65 A  934  LEU ALA ASN PHE PRO LYS HIS VAL ILE GLU CYS ALA LYS          
SEQRES  66 A  934  GLN LYS ALA LEU GLU LEU GLU GLU PHE GLN TYR ILE GLY          
SEQRES  67 A  934  GLU SER GLN GLY TYR ASP ILE MET GLU PRO ALA ALA LYS          
SEQRES  68 A  934  LYS CYS TYR LEU GLU ARG GLU GLN GLY GLU LYS ILE ILE          
SEQRES  69 A  934  GLN GLU PHE LEU SER LYS VAL LYS GLN MET PRO PHE THR          
SEQRES  70 A  934  GLU MET SER GLU GLU ASN ILE THR ILE LYS LEU LYS GLN          
SEQRES  71 A  934  LEU LYS ALA GLU VAL ILE ALA LYS ASN ASN SER PHE VAL          
SEQRES  72 A  934  ASN GLU ILE ILE SER ARG ILE LYS VAL THR THR                  
SEQRES   1 B  918  GLY PRO LYS SER ALA ASN LYS ARG SER LYS SER ILE TYR          
SEQRES   2 B  918  THR PRO LEU GLU LEU GLN TYR ILE GLU MET LYS GLN GLN          
SEQRES   3 B  918  HIS LYS ASP ALA VAL LEU CYS VAL GLU CYS GLY TYR LYS          
SEQRES   4 B  918  TYR ARG PHE PHE GLY GLU ASP ALA GLU ILE ALA ALA ARG          
SEQRES   5 B  918  GLU LEU ASN ILE TYR CYS HIS LEU ASP HIS ASN PHE MET          
SEQRES   6 B  918  THR ALA SER ILE PRO THR HIS ARG LEU PHE VAL HIS VAL          
SEQRES   7 B  918  ARG ARG LEU VAL ALA LYS GLY TYR LYS VAL GLY VAL VAL          
SEQRES   8 B  918  LYS GLN THR GLU THR ALA ALA LEU LYS ALA ILE GLY ASP          
SEQRES   9 B  918  ASN ARG SER SER LEU PHE SER ARG LYS LEU THR ALA LEU          
SEQRES  10 B  918  TYR THR LYS SER THR LEU ILE GLY GLU ASP VAL ASN PRO          
SEQRES  11 B  918  LEU ILE LYS LEU ASP ASP ALA VAL ASN VAL ASP GLU ILE          
SEQRES  12 B  918  MET THR ASP THR SER THR SER TYR LEU LEU CYS ILE SER          
SEQRES  13 B  918  GLU ASN LYS GLU ASN VAL ARG ASP LYS LYS LYS GLY ASN          
SEQRES  14 B  918  ILE PHE ILE GLY ILE VAL GLY VAL GLN PRO ALA THR GLY          
SEQRES  15 B  918  GLU VAL VAL PHE ASP SER PHE GLN ASP SER ALA SER ARG          
SEQRES  16 B  918  SER GLU LEU GLU THR ARG MET SER SER LEU GLN PRO VAL          
SEQRES  17 B  918  GLU LEU LEU LEU PRO SER ALA LEU SER GLU GLN THR GLU          
SEQRES  18 B  918  ALA LEU ILE HIS ARG ALA THR SER VAL SER VAL GLN ASP          
SEQRES  19 B  918  ASP ARG ILE ARG VAL GLU ARG MET ASP ASN ILE TYR PHE          
SEQRES  20 B  918  GLU TYR SER HIS ALA PHE GLN ALA VAL THR GLU PHE TYR          
SEQRES  21 B  918  ALA LYS ASP THR VAL ASP ILE LYS GLY SER GLN ILE ILE          
SEQRES  22 B  918  SER GLY ILE VAL ASN LEU GLU LYS PRO VAL ILE CYS SER          
SEQRES  23 B  918  LEU ALA ALA ILE ILE LYS TYR LEU LYS GLU PHE ASN LEU          
SEQRES  24 B  918  GLU LYS MET LEU SER LYS PRO GLU ASN PHE LYS GLN LEU          
SEQRES  25 B  918  SER SER LYS MET GLU PHE MET THR ILE ASN GLY THR THR          
SEQRES  26 B  918  LEU ARG ASN LEU GLU ILE LEU GLN ASN GLN THR ASP MET          
SEQRES  27 B  918  LYS THR LYS GLY SER LEU LEU TRP VAL LEU ASP HIS THR          
SEQRES  28 B  918  LYS THR SER PHE GLY ARG ARG LYS LEU LYS LYS TRP VAL          
SEQRES  29 B  918  THR GLN PRO LEU LEU LYS LEU ARG GLU ILE ASN ALA ARG          
SEQRES  30 B  918  LEU ASP ALA VAL SER GLU VAL LEU HIS SER GLU SER SER          
SEQRES  31 B  918  VAL PHE GLY GLN ILE GLU ASN HIS LEU ARG LYS LEU PRO          
SEQRES  32 B  918  ASP ILE GLU ARG GLY LEU CYS SER ILE TYR HIS LYS LYS          
SEQRES  33 B  918  CYS SER THR GLN GLU PHE PHE LEU ILE VAL LYS THR LEU          
SEQRES  34 B  918  TYR HIS LEU LYS SER GLU PHE GLN ALA ILE ILE PRO ALA          
SEQRES  35 B  918  VAL ASN SER HIS ILE GLN SER ASP LEU LEU ARG THR VAL          
SEQRES  36 B  918  ILE LEU GLU ILE PRO GLU LEU LEU SER PRO VAL GLU HIS          
SEQRES  37 B  918  TYR LEU LYS ILE LEU ASN GLU GLN ALA ALA LYS VAL GLY          
SEQRES  38 B  918  ASP LYS THR GLU LEU PHE LYS ASP LEU SER ASP PHE PRO          
SEQRES  39 B  918  LEU ILE LYS LYS ARG LYS ASP GLU ILE GLN GLY VAL ILE          
SEQRES  40 B  918  ASP GLU ILE ARG MET HIS LEU GLN GLU ILE ARG LYS ILE          
SEQRES  41 B  918  LEU LYS ASN PRO SER ALA GLN TYR VAL THR VAL SER GLY          
SEQRES  42 B  918  GLN GLU PHE MET ILE GLU ILE LYS ASN SER ALA VAL SER          
SEQRES  43 B  918  CYS ILE PRO THR ASP TRP VAL LYS VAL GLY SER THR LYS          
SEQRES  44 B  918  ALA VAL SER ARG PHE HIS SER PRO PHE ILE VAL GLU ASN          
SEQRES  45 B  918  TYR ARG HIS LEU ASN GLN LEU ARG GLU GLN LEU VAL LEU          
SEQRES  46 B  918  ASP CYS SER ALA GLU TRP LEU ASP PHE LEU GLU LYS PHE          
SEQRES  47 B  918  SER GLU HIS TYR HIS SER LEU CYS LYS ALA VAL HIS HIS          
SEQRES  48 B  918  LEU ALA THR VAL ASP CYS ILE PHE SER LEU ALA LYS VAL          
SEQRES  49 B  918  ALA LYS GLN GLY ASP TYR CYS ARG PRO THR VAL GLN GLU          
SEQRES  50 B  918  GLU ARG LYS ILE VAL ILE LYS ASN GLY ARG HIS PRO VAL          
SEQRES  51 B  918  ILE ASP VAL LEU LEU GLY GLU GLN ASP GLN TYR VAL PRO          
SEQRES  52 B  918  ASN ASN THR ASP LEU SER GLU ASP SER GLU ARG VAL MET          
SEQRES  53 B  918  ILE ILE THR GLY PRO ASN MET GLY GLY LYS SER SER TYR          
SEQRES  54 B  918  ILE LYS GLN VAL ALA LEU ILE THR ILE MET ALA GLN ILE          
SEQRES  55 B  918  GLY SER TYR VAL PRO ALA GLU GLU ALA THR ILE GLY ILE          
SEQRES  56 B  918  VAL ASP GLY ILE PHE THR ARG MET GLY ALA ALA ASP ASN          
SEQRES  57 B  918  ILE TYR LYS GLY ARG SER THR PHE MET GLU GLU LEU THR          
SEQRES  58 B  918  ASP THR ALA GLU ILE ILE ARG LYS ALA THR SER GLN SER          
SEQRES  59 B  918  LEU VAL ILE LEU ASP GLU LEU GLY ARG GLY THR SER THR          
SEQRES  60 B  918  HIS ASP GLY ILE ALA ILE ALA TYR ALA THR LEU GLU TYR          
SEQRES  61 B  918  PHE ILE ARG ASP VAL LYS SER LEU THR LEU PHE VAL THR          
SEQRES  62 B  918  HIS TYR PRO PRO VAL CYS GLU LEU GLU LYS ASN TYR SER          
SEQRES  63 B  918  HIS GLN VAL GLY ASN TYR HIS MET GLY PHE LEU VAL SER          
SEQRES  64 B  918  GLU ASP GLU SER LYS LEU ASP PRO GLY ALA ALA GLU GLN          
SEQRES  65 B  918  VAL PRO ASP PHE VAL THR PHE LEU TYR GLN ILE THR ARG          
SEQRES  66 B  918  GLY ILE ALA ALA ARG SER TYR GLY LEU ASN VAL ALA LYS          
SEQRES  67 B  918  LEU ALA ASP VAL PRO GLY GLU ILE LEU LYS LYS ALA ALA          
SEQRES  68 B  918  HIS LYS SER LYS GLU LEU GLU GLY LEU ILE ASN THR LYS          
SEQRES  69 B  918  ARG LYS ARG LEU LYS TYR PHE ALA LYS LEU TRP THR MET          
SEQRES  70 B  918  HIS ASN ALA GLN ASP LEU GLN LYS TRP THR GLU GLU PHE          
SEQRES  71 B  918  ASN MET GLU GLU THR GLN THR SER                              
SEQRES   1 D   24   DC  DC  DT  DC  DT  DA  DT  DC  DT  DG  DA  DA  DG          
SEQRES   2 D   24   DC  DC  DG  DA  DT  DC  DG  DA  DT  DG  DG                  
SEQRES   1 E   25   DT  DC  DA  DT  DC  DG  DA  DT  DC  DG  DA  DC  DA          
SEQRES   2 E   25   DG  DC  DT  DT  DC  DA  DG  DA  DT  DA  DG  DG              
HET    ADP  A 935      27                                                       
HET     NA  B   1       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      NA SODIUM ION                                                       
FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6   NA    NA 1+                                                        
FORMUL   7  HOH   *27(H2 O)                                                     
HELIX    1   1 SER A   13  GLY A   25  1                                  13    
HELIX    2   2 GLY A   47  VAL A   57  1                                  11    
HELIX    3   3 LYS A   82  VAL A   95  1                                  14    
HELIX    4   4 PHE A  131  PHE A  136  1                                   6    
HELIX    5   5 PHE A  184  GLY A  195  1                                  12    
HELIX    6   6 ALA A  207  GLY A  221  1                                  15    
HELIX    7   7 LYS A  228  SER A  233  5                                   6    
HELIX    8   8 ASP A  236  LEU A  245  1                                  10    
HELIX    9   9 ASN A  254  GLU A  262  5                                   9    
HELIX   10  10 ASN A  263  GLU A  278  1                                  16    
HELIX   11  11 LEU A  279  PHE A  286  5                                   8    
HELIX   12  12 ASP A  295  TYR A  299  5                                   5    
HELIX   13  13 ASP A  303  LEU A  310  1                                   8    
HELIX   14  14 SER A  325  ASN A  331  1                                   7    
HELIX   15  15 THR A  335  GLN A  348  1                                  14    
HELIX   16  16 ASP A  352  GLU A  368  1                                  17    
HELIX   17  17 ASP A  369  GLU A  378  1                                  10    
HELIX   18  18 LEU A  380  PHE A  384  5                                   5    
HELIX   19  19 ASP A  386  ARG A  396  1                                  11    
HELIX   20  20 ASN A  400  ASN A  412  1                                  13    
HELIX   21  21 GLN A  413  HIS A  424  1                                  12    
HELIX   22  22 LEU A  431  VAL A  435  5                                   5    
HELIX   23  23 PHE A  436  THR A  456  1                                  21    
HELIX   24  24 ASP A  461  ASN A  465  5                                   5    
HELIX   25  25 ASP A  475  LEU A  503  1                                  29    
HELIX   26  26 THR A  526  LYS A  531  1                                   6    
HELIX   27  27 LYS A  555  THR A  564  1                                  10    
HELIX   28  28 LYS A  567  SER A  586  1                                  20    
HELIX   29  29 TYR A  588  GLY A  614  1                                  27    
HELIX   30  30 GLY A  674  GLY A  692  1                                  19    
HELIX   31  31 THR A  724  ALA A  739  1                                  16    
HELIX   32  32 SER A  755  LYS A  773  1                                  19    
HELIX   33  33 PHE A  784  GLN A  793  5                                  10    
HELIX   34  34 PHE A  826  ALA A  834  1                                   9    
HELIX   35  35 PRO A  837  LEU A  851  1                                  15    
HELIX   36  36 TYR A  874  GLN A  893  1                                  20    
HELIX   37  37 MET A  894  MET A  899  5                                   6    
HELIX   38  38 SER A  900  LYS A  918  1                                  19    
HELIX   39  39 ASN A  920  ARG A  929  1                                  10    
HELIX   40  40 THR B  221  GLN B  232  1                                  12    
HELIX   41  41 GLY B  251  ASN B  262  1                                  12    
HELIX   42  42 ARG B  280  GLY B  292  1                                  13    
HELIX   43  43 THR B  303  ALA B  308  1                                   6    
HELIX   44  44 ARG B  402  GLN B  413  1                                  12    
HELIX   45  45 SER B  424  VAL B  437  1                                  14    
HELIX   46  46 ASP B  450  PHE B  454  5                                   5    
HELIX   47  47 GLU B  455  TYR B  467  1                                  13    
HELIX   48  48 GLU B  487  PHE B  504  1                                  18    
HELIX   49  49 ASN B  505  SER B  511  5                                   7    
HELIX   50  50 LYS B  512  GLU B  514  5                                   3    
HELIX   51  51 ASN B  529  LEU B  536  1                                   8    
HELIX   52  52 SER B  550  ASP B  556  1                                   7    
HELIX   53  53 THR B  560  GLN B  573  1                                  14    
HELIX   54  54 LYS B  577  HIS B  593  1                                  17    
HELIX   55  55 SER B  597  HIS B  605  1                                   9    
HELIX   56  56 ASP B  611  HIS B  621  1                                  11    
HELIX   57  57 SER B  625  HIS B  653  1                                  29    
HELIX   58  58 SER B  656  LEU B  664  1                                   9    
HELIX   59  59 LEU B  664  LEU B  670  1                                   7    
HELIX   60  60 VAL B  673  LYS B  678  1                                   6    
HELIX   61  61 ASN B  681  GLY B  688  1                                   8    
HELIX   62  62 ASP B  696  ASP B  699  5                                   4    
HELIX   63  63 PHE B  700  LYS B  729  1                                  30    
HELIX   64  64 ALA B  751  ILE B  755  5                                   5    
HELIX   65  65 SER B  773  SER B  806  1                                  34    
HELIX   66  66 HIS B  808  LYS B  833  1                                  26    
HELIX   67  67 HIS B  855  LEU B  862  1                                   8    
HELIX   68  68 MET B  890  ILE B  909  1                                  20    
HELIX   69  69 THR B  942  ALA B  957  1                                  16    
HELIX   70  70 SER B  973  ASP B  991  1                                  19    
HELIX   71  71 TYR B 1002  CYS B 1006  5                                   5    
HELIX   72  72 GLU B 1007  TYR B 1012  1                                   6    
HELIX   73  73 GLY B 1060  LYS B 1065  1                                   6    
HELIX   74  74 PRO B 1070  THR B 1103  1                                  34    
HELIX   75  75 ASN B 1106  GLU B 1120  1                                  15    
SHEET    1   A 6 LYS A  65  MET A  67  0                                        
SHEET    2   A 6 LEU A  75  SER A  81 -1  O  SER A  77   N  LYS A  65           
SHEET    3   A 6 PHE A  42  HIS A  46 -1  N  TYR A  43   O  LEU A  80           
SHEET    4   A 6 THR A  33  ASP A  38 -1  N  PHE A  37   O  THR A  44           
SHEET    5   A 6 ARG A  99  ASN A 105  1  O  GLU A 101   N  LEU A  36           
SHEET    6   A 6 TRP A 117  ALA A 123 -1  O  ALA A 123   N  VAL A 100           
SHEET    1   B 6 LEU A 223  ARG A 227  0                                        
SHEET    2   B 6 GLU A 198  PRO A 202  1  N  CYS A 199   O  THR A 225           
SHEET    3   B 6 VAL A 147  MET A 152  1  N  VAL A 148   O  VAL A 200           
SHEET    4   B 6 GLN A 160  ASP A 167 -1  O  GLY A 164   N  GLY A 149           
SHEET    5   B 6 LYS A 172  PRO A 179 -1  O  PHE A 178   N  VAL A 161           
SHEET    6   B 6 GLU A 290  THR A 293  1  O  THR A 292   N  LEU A 175           
SHEET    1   C 7 LYS A 301  LEU A 302  0                                        
SHEET    2   C 7 CYS A 707  ARG A 711  1  O  ILE A 708   N  LYS A 301           
SHEET    3   C 7 LEU A 744  ASP A 748  1  O  LEU A 744   N  CYS A 707           
SHEET    4   C 7 PHE A 777  THR A 782  1  O  PHE A 777   N  ILE A 745           
SHEET    5   C 7 PHE A 664  THR A 668  1  N  HIS A 665   O  PHE A 780           
SHEET    6   C 7 VAL A 797  THR A 807  1  O  ASN A 798   N  ILE A 666           
SHEET    7   C 7 THR A 810  LYS A 819 -1  O  THR A 810   N  THR A 807           
SHEET    1   D 4 LYS A 512  SER A 515  0                                        
SHEET    2   D 4 TYR A 521  VAL A 525 -1  O  ARG A 524   N  LYS A 512           
SHEET    3   D 4 VAL A 549  THR A 552 -1  O  PHE A 551   N  PHE A 523           
SHEET    4   D 4 SER A 540  ASP A 543 -1  N  ASP A 543   O  LYS A 550           
SHEET    1   E 4 ALA A 623  LEU A 625  0                                        
SHEET    2   E 4 CYS A 697  SER A 703  1  O  VAL A 702   N  ALA A 623           
SHEET    3   E 4 ARG A 631  SER A 637 -1  N  LYS A 635   O  GLU A 698           
SHEET    4   E 4 ASN A 653  GLU A 658 -1  O  ASN A 653   N  SER A 637           
SHEET    1   F 6 HIS B 266  ASP B 268  0                                        
SHEET    2   F 6 PHE B 271  PRO B 277 -1  O  PHE B 271   N  ASP B 268           
SHEET    3   F 6 LYS B 246  PHE B 250 -1  N  TYR B 247   O  ILE B 276           
SHEET    4   F 6 VAL B 238  GLU B 242 -1  N  VAL B 241   O  ARG B 248           
SHEET    5   F 6 VAL B 295  GLN B 300  1  O  VAL B 298   N  CYS B 240           
SHEET    6   F 6 ARG B 319  TYR B 325 -1  O  THR B 322   N  VAL B 297           
SHEET    1   G 2 LEU B 338  ILE B 339  0                                        
SHEET    2   G 2 ASN B 346  VAL B 347 -1  O  ASN B 346   N  ILE B 339           
SHEET    1   H 6 ARG B 445  MET B 449  0                                        
SHEET    2   H 6 GLU B 416  PRO B 420  1  N  LEU B 417   O  GLU B 447           
SHEET    3   H 6 LEU B 359  ASN B 365  1  N  LEU B 360   O  GLU B 416           
SHEET    4   H 6 ILE B 377  VAL B 384 -1  O  VAL B 382   N  CYS B 361           
SHEET    5   H 6 VAL B 391  ASP B 398 -1  O  VAL B 392   N  GLY B 383           
SHEET    6   H 6 PHE B 516  GLN B 518  1  O  LYS B 517   N  PHE B 393           
SHEET    1   I 7 THR B 527  ILE B 528  0                                        
SHEET    2   I 7 GLY B 925  ARG B 929  1  O  ILE B 926   N  THR B 527           
SHEET    3   I 7 LEU B 962  ASP B 966  1  O  ILE B 964   N  PHE B 927           
SHEET    4   I 7 LEU B 995  VAL B 999  1  O  LEU B 995   N  VAL B 963           
SHEET    5   I 7 VAL B 882  THR B 886  1  N  MET B 883   O  PHE B 998           
SHEET    6   I 7 VAL B1016  LEU B1024  1  O  TYR B1019   N  ILE B 884           
SHEET    7   I 7 PHE B1046  ARG B1052 -1  O  THR B1051   N  HIS B1020           
SHEET    1   J 4 VAL B 736  VAL B 738  0                                        
SHEET    2   J 4 GLN B 741  LYS B 748 -1  O  GLN B 741   N  VAL B 738           
SHEET    3   J 4 VAL B 768  HIS B 772 -1  O  SER B 769   N  ILE B 747           
SHEET    4   J 4 VAL B 760  SER B 764 -1  N  VAL B 760   O  HIS B 772           
SHEET    1   K 4 THR B 841  GLN B 843  0                                        
SHEET    2   K 4 GLU B 917  GLY B 921  1  O  ILE B 920   N  THR B 841           
SHEET    3   K 4 LYS B 847  GLY B 853 -1  N  LYS B 847   O  GLY B 921           
SHEET    4   K 4 ASN B 871  LEU B 875 -1  O  THR B 873   N  ILE B 850           
CISPEP   1 GLY A  204    GLU A  205          0         0.88                     
SITE     1 AC1 13 ILE A 648  ALA A 649  PHE A 650  ILE A 651                    
SITE     2 AC1 13 ASN A 653  PRO A 670  MET A 672  GLY A 673                    
SITE     3 AC1 13 GLY A 674  LYS A 675  SER A 676  THR A 677                    
SITE     4 AC1 13 TYR A 815                                                     
SITE     1 AC2  3 GLU B 844  ILE B 922  GLN B 960                               
CRYST1   67.120   91.540   95.580  67.88  86.51  72.86 P 1           1          
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      0.014899 -0.004595  0.000884        0.00000                         
SCALE2      0.000000  0.011432 -0.004638        0.00000                         
SCALE3      0.000000  0.000000  0.011312        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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