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Database: PDB
Entry: 3THW
LinkDB: 3THW
Original site: 3THW 
HEADER    DNA BINDING PROTEIN/DNA                 19-AUG-11   3THW              
TITLE     HUMAN MUTSBETA COMPLEXED WITH AN IDL OF 4 BASES (LOOP4) 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- 1134;                                    
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 LOOP4 HAIRPIN;                                         
COMPND  15 CHAIN: D;                                                            
COMPND  16 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                                                       
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   08-NOV-17 3THW    1       REMARK                                   
REVDAT   2   26-JUN-13 3THW    1       JRNL                                     
REVDAT   1   21-DEC-11 3THW    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.    3.09 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) : 3.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.53                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 38509                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1919                            
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 32.5317 -  6.6313    0.95     3949   218  0.1748 0.2063        
REMARK   3     2  6.6313 -  5.2707    0.97     3892   201  0.2228 0.3000        
REMARK   3     3  5.2707 -  4.6066    0.98     3878   208  0.1720 0.2511        
REMARK   3     4  4.6066 -  4.1864    0.98     3847   199  0.1756 0.2417        
REMARK   3     5  4.1864 -  3.8868    0.96     3754   224  0.2120 0.2729        
REMARK   3     6  3.8868 -  3.6580    0.94     3642   196  0.2404 0.3027        
REMARK   3     7  3.6580 -  3.4750    0.92     3614   153  0.2625 0.3460        
REMARK   3     8  3.4750 -  3.3239    0.89     3450   183  0.3218 0.3911        
REMARK   3     9  3.3239 -  3.1961    0.86     3357   167  0.3339 0.4243        
REMARK   3    10  3.1961 -  3.0859    0.82     3207   170  0.3759 0.4154        
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              : 0.28                                          
REMARK   3   B_SOL              : 30.88                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.160           
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) : -5.37420                                             
REMARK   3    B22 (A**2) : -14.19280                                            
REMARK   3    B33 (A**2) : 19.56700                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.003          15294                                  
REMARK   3   ANGLE     :  0.563          20903                                  
REMARK   3   CHIRALITY :  0.038           2404                                  
REMARK   3   PLANARITY :  0.002           2480                                  
REMARK   3   DIHEDRAL  : 16.587           5784                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3THW 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_1000067497.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-08                          
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) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : X-GEN                              
REMARK 200  DATA SCALING SOFTWARE          : X-GEN                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41282                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.09960                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2O8B                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
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 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       52.92000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.02000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.06500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.02000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       52.92000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.06500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 84340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     GLY A   108                                                      
REMARK 465     ASN A   109                                                      
REMARK 465     LYS A   110                                                      
REMARK 465     ALA A   111                                                      
REMARK 465     SER A   142                                                      
REMARK 465     ALA A   143                                                      
REMARK 465     SER A   144                                                      
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     GLN A   518                                                      
REMARK 465     PHE A   519                                                      
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     TYR A   856                                                      
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     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     ASP B   342                                                      
REMARK 465     ASP B   343                                                      
REMARK 465     VAL B   369                                                      
REMARK 465     ARG B   370                                                      
REMARK 465     ASP B   371                                                      
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     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     SER B  1026                                                      
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     GLU B  1115                                                      
REMARK 465     GLU B  1116                                                      
REMARK 465     PHE B  1117                                                      
REMARK 465     ASN B  1118                                                      
REMARK 465     MET B  1119                                                      
REMARK 465     GLU B  1120                                                      
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 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 205    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 264    CG   CD   OE1  NE2                                  
REMARK 470     SER A 316    OG                                                  
REMARK 470     SER A 323    OG                                                  
REMARK 470     LYS A 427    CG   CD   CE   NZ                                   
REMARK 470     GLN A 429    CB   CG   CD   OE1  NE2                             
REMARK 470     LYS A 430    CG   CD   CE   NZ                                   
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     CYS A 527    SG                                                  
REMARK 470     ASP A 543    CG   OD1  OD2                                       
REMARK 470     ILE A 544    CG1  CG2  CD1                                       
REMARK 470     LYS A 546    CG   CD   CE   NZ                                   
REMARK 470     ASP A 646    CG   OD1  OD2                                       
REMARK 470     LEU A 719    CG   CD1  CD2                                       
REMARK 470     ASN A 835    CG   OD1  ND2                                       
REMARK 470     LYS A 838    CG   CD   CE   NZ                                   
REMARK 470     MET A 866    CG   SD   CE                                        
REMARK 470     GLU A 867    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 871    CG   CD   CE   NZ                                   
REMARK 470     LYS A 872    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     SER B 216    OG                                                  
REMARK 470     GLU B 252    CG   CD   OE1  OE2                                  
REMARK 470     SER B 355    OG                                                  
REMARK 470     GLU B 367    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 372    CG   CD   CE   NZ                                   
REMARK 470     LYS B 373    CG   CD   CE   NZ                                   
REMARK 470     LYS B 374    CG   CD   CE   NZ                                   
REMARK 470     GLN B 440    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 469    CG   CD   CE   NZ                                   
REMARK 470     LYS B 522    CG   CD   CE   NZ                                   
REMARK 470     MET B 523    CG   SD   CE                                        
REMARK 470     GLN B 683    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 878    CG   OD1  OD2                                       
REMARK 470     ARG B 940    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 941    OG                                                  
REMARK 470     VAL B1025    CG1  CG2                                            
REMARK 470     PHE B1043    CG   CD1  CD2  CE1  CE2  CZ                         
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     DT D   3   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DG D  52   O4' -  C1' -  N9  ANGL. DEV. =   2.1 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  95      -76.25   -123.16                                   
REMARK 500    ASN A 115       77.58   -118.49                                   
REMARK 500    LEU A 119       93.65    -66.54                                   
REMARK 500    ALA A 123      118.14   -177.26                                   
REMARK 500    SER A 153      115.61   -165.64                                   
REMARK 500    VAL A 155      -81.20    -69.47                                   
REMARK 500    ASP A 156       56.57   -112.18                                   
REMARK 500    ALA A 207     -173.31    -61.60                                   
REMARK 500    ASP A 209      -61.49    -94.05                                   
REMARK 500    LYS A 235      -73.76    -42.46                                   
REMARK 500    LYS A 249       19.82     57.51                                   
REMARK 500    LEU A 258      139.65    -38.15                                   
REMARK 500    LEU A 310       24.16    -76.62                                   
REMARK 500    ASN A 311       56.73     23.96                                   
REMARK 500    GLN A 377      -81.86    -89.81                                   
REMARK 500    ASP A 379      -74.04   -130.27                                   
REMARK 500    ALA A 398       27.27   -151.77                                   
REMARK 500    ASN A 400     -156.26    -87.72                                   
REMARK 500    LYS A 423        0.29    -65.15                                   
REMARK 500    LYS A 430      -70.07    -90.13                                   
REMARK 500    THR A 457      -50.72   -122.35                                   
REMARK 500    ASP A 459       95.58    -64.99                                   
REMARK 500    SER A 473       49.29    -77.92                                   
REMARK 500    PHE A 474      -28.99   -145.08                                   
REMARK 500    LYS A 509      -76.21    -53.57                                   
REMARK 500    LYS A 512     -157.10   -134.18                                   
REMARK 500    VAL A 525     -145.81   -139.54                                   
REMARK 500    THR A 526     -148.33   -139.64                                   
REMARK 500    ASN A 536       74.79     47.49                                   
REMARK 500    LYS A 537      -74.43    -57.13                                   
REMARK 500    THR A 552     -150.64    -94.35                                   
REMARK 500    ASP A 575       23.78    -77.49                                   
REMARK 500    PRO A 618      141.37    -36.40                                   
REMARK 500    ALA A 636       71.63     51.76                                   
REMARK 500    VAL A 644       43.16   -102.73                                   
REMARK 500    ASP A 646      -73.16    -52.53                                   
REMARK 500    GLU A 647       49.61   -142.62                                   
REMARK 500    LYS A 661      -66.96   -129.85                                   
REMARK 500    GLU A 749       85.35     57.68                                   
REMARK 500    ILE A 774      -75.83    -79.96                                   
REMARK 500    GLU A 809       39.51   -145.81                                   
REMARK 500    ASP A 823      -69.26    -90.84                                   
REMARK 500    GLN A 879      -70.17    -62.60                                   
REMARK 500    GLN A 893       23.20    -78.15                                   
REMARK 500    SER B 218       58.89   -111.65                                   
REMARK 500    HIS B 234       62.03   -152.86                                   
REMARK 500    HIS B 269     -104.03     75.13                                   
REMARK 500    ALA B 308       26.38    -70.48                                   
REMARK 500    SER B 315     -141.38   -163.64                                   
REMARK 500    ASN B 336       78.86   -118.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      88 RAMACHANDRAN OUTLIERS.                        
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3THX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3THY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3THZ   RELATED DB: PDB                                   
DBREF  3THW A    1   934  UNP    P43246   MSH2_HUMAN       1    934             
DBREF1 3THW B  210  1125  GB                   EAW95862                         
DBREF2 3THW B     119616268                         210        1125             
DBREF  3THW D    1    53  PDB    3THW     3THW             1     53             
SEQADV 3THW GLY B  208  GB   119616268           EXPRESSION TAG                 
SEQADV 3THW 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   53   DC  DC  DT  DC  DT  DA  DT  DC  DT  DG  DA  DA  DG          
SEQRES   2 D   53   DC  DC  DG  DA  DT  DC  DG  DA  DT  DG  DA  DA  DG          
SEQRES   3 D   53   DC  DA  DT  DC  DG  DA  DT  DC  DG  DC  DA  DC  DA          
SEQRES   4 D   53   DG  DC  DT  DT  DC  DA  DG  DA  DT  DA  DG  DA  DG          
SEQRES   5 D   53   DG                                                          
HET    ADP  A 935      27                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   5  HOH   *4(H2 O)                                                      
HELIX    1   1 GLU A   12  GLY A   25  1                                  14    
HELIX    2   2 GLY A   47  VAL A   57  1                                  11    
HELIX    3   3 SER A   81  VAL A   95  1                                  15    
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 ASP A  209  GLY A  220  1                                  12    
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 LEU A  258  GLU A  262  5                                   5    
HELIX   10  10 ASN A  263  LEU A  277  1                                  15    
HELIX   11  11 GLU A  278  PHE A  286  5                                   9    
HELIX   12  12 ASP A  303  LEU A  310  1                                   8    
HELIX   13  13 SER A  325  ASN A  331  1                                   7    
HELIX   14  14 THR A  335  GLN A  348  1                                  14    
HELIX   15  15 ASP A  352  GLU A  368  1                                  17    
HELIX   16  16 ASP A  369  ASP A  379  1                                  11    
HELIX   17  17 LEU A  380  PHE A  384  5                                   5    
HELIX   18  18 ASP A  386  ARG A  396  1                                  11    
HELIX   19  19 LEU A  401  ASN A  412  1                                  12    
HELIX   20  20 GLN A  413  LYS A  423  1                                  11    
HELIX   21  21 LYS A  430  VAL A  435  1                                   6    
HELIX   22  22 PHE A  436  THR A  456  1                                  21    
HELIX   23  23 GLN A  462  HIS A  466  5                                   5    
HELIX   24  24 ASP A  475  MET A  492  1                                  18    
HELIX   25  25 GLN A  493  SER A  498  1                                   6    
HELIX   26  26 SER A  498  LEU A  503  1                                   6    
HELIX   27  27 LYS A  555  SER A  586  1                                  32    
HELIX   28  28 TYR A  588  GLY A  614  1                                  27    
HELIX   29  29 HIS A  639  VAL A  644  1                                   6    
HELIX   30  30 GLY A  674  GLY A  692  1                                  19    
HELIX   31  31 SER A  723  ARG A  737  1                                  15    
HELIX   32  32 SER A  755  ALA A  771  1                                  17    
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 HIS A  839  LEU A  851  1                                  13    
HELIX   36  36 GLU A  867  GLN A  893  1                                  27    
HELIX   37  37 SER A  900  ASN A  919  1                                  20    
HELIX   38  38 ASN A  920  ARG A  929  1                                  10    
HELIX   39  39 THR B  221  GLN B  232  1                                  12    
HELIX   40  40 GLY B  251  LEU B  261  1                                  11    
HELIX   41  41 ARG B  280  LYS B  291  1                                  12    
HELIX   42  42 THR B  303  ALA B  308  1                                   6    
HELIX   43  43 ARG B  402  GLN B  413  1                                  12    
HELIX   44  44 SER B  424  SER B  438  1                                  15    
HELIX   45  45 GLU B  455  TYR B  467  1                                  13    
HELIX   46  46 GLU B  487  LYS B  502  1                                  16    
HELIX   47  47 LEU B  506  GLU B  514  5                                   9    
HELIX   48  48 ASN B  529  LEU B  536  1                                   8    
HELIX   49  49 SER B  550  ASP B  556  1                                   7    
HELIX   50  50 THR B  560  GLN B  573  1                                  14    
HELIX   51  51 LYS B  577  SER B  594  1                                  18    
HELIX   52  52 SER B  596  LEU B  609  1                                  14    
HELIX   53  53 ASP B  611  HIS B  621  1                                  11    
HELIX   54  54 SER B  625  PHE B  643  1                                  19    
HELIX   55  55 ILE B  646  HIS B  653  1                                   8    
HELIX   56  56 LEU B  658  LEU B  670  1                                  13    
HELIX   57  57 PRO B  672  ILE B  679  1                                   8    
HELIX   58  58 ASN B  681  GLY B  688  1                                   8    
HELIX   59  59 PHE B  700  MET B  719  1                                  20    
HELIX   60  60 HIS B  720  LEU B  728  1                                   9    
HELIX   61  61 SER B  750  ILE B  755  5                                   6    
HELIX   62  62 SER B  773  SER B  806  1                                  34    
HELIX   63  63 HIS B  808  GLN B  834  1                                  27    
HELIX   64  64 VAL B  857  LEU B  862  1                                   6    
HELIX   65  65 MET B  890  GLY B  910  1                                  21    
HELIX   66  66 THR B  942  ALA B  957  1                                  16    
HELIX   67  67 SER B  973  ASP B  991  1                                  19    
HELIX   68  68 TYR B 1002  CYS B 1006  5                                   5    
HELIX   69  69 GLU B 1007  TYR B 1012  1                                   6    
HELIX   70  70 SER B 1058  LYS B 1065  1                                   8    
HELIX   71  71 PRO B 1070  THR B 1103  1                                  34    
SHEET    1   A 6 LYS A  65  MET A  67  0                                        
SHEET    2   A 6 LEU A  75  LEU A  80 -1  O  SER A  77   N  LYS A  65           
SHEET    3   A 6 TYR A  43  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  ARG A  99   N  VAL A  34           
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  LEU A 223           
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  LYS A 172   N  ASP A 167           
SHEET    6   B 6 GLU A 290  THR A 293  1  O  GLU A 290   N  LEU A 173           
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  ILE A 746   N  ARG A 711           
SHEET    4   C 7 PHE A 777  ALA A 781  1  O  MET A 779   N  ILE A 747           
SHEET    5   C 7 PHE A 664  THR A 668  1  N  ILE A 667   O  PHE A 780           
SHEET    6   C 7 VAL A 797  THR A 807  1  O  ASN A 798   N  PHE A 664           
SHEET    7   C 7 THR A 810  LYS A 819 -1  O  THR A 812   N  LEU A 805           
SHEET    1   D 2 LYS A 512  ASP A 514  0                                        
SHEET    2   D 2 TYR A 522  ARG A 524 -1  O  TYR A 522   N  ASP A 514           
SHEET    1   E 2 SER A 540  ILE A 544  0                                        
SHEET    2   E 2 VAL A 549  THR A 552 -1  O  LYS A 550   N  ASP A 543           
SHEET    1   F 4 ALA A 623  LEU A 625  0                                        
SHEET    2   F 4 SER A 699  SER A 703  1  O  ALA A 700   N  ALA A 623           
SHEET    3   F 4 ILE A 632  SER A 637 -1  N  ILE A 633   O  GLU A 701           
SHEET    4   F 4 ASN A 653  PHE A 657 -1  O  ASN A 653   N  SER A 637           
SHEET    1   G 6 HIS B 266  ASP B 268  0                                        
SHEET    2   G 6 PHE B 271  PRO B 277 -1  O  THR B 273   N  HIS B 266           
SHEET    3   G 6 LYS B 246  PHE B 250 -1  N  TYR B 247   O  ILE B 276           
SHEET    4   G 6 ALA B 237  CYS B 243 -1  N  CYS B 243   O  LYS B 246           
SHEET    5   G 6 LYS B 294  GLN B 300  1  O  GLY B 296   N  VAL B 238           
SHEET    6   G 6 ARG B 319  TYR B 325 -1  O  TYR B 325   N  VAL B 295           
SHEET    1   H 2 LEU B 338  ILE B 339  0                                        
SHEET    2   H 2 ASN B 346  VAL B 347 -1  O  ASN B 346   N  ILE B 339           
SHEET    1   I 6 ARG B 445  MET B 449  0                                        
SHEET    2   I 6 GLU B 416  PRO B 420  1  N  LEU B 417   O  ARG B 445           
SHEET    3   I 6 LEU B 359  ASN B 365  1  N  LEU B 360   O  LEU B 418           
SHEET    4   I 6 ILE B 377  GLN B 385 -1  O  GLY B 380   N  SER B 363           
SHEET    5   I 6 GLU B 390  ASP B 398 -1  O  VAL B 392   N  GLY B 383           
SHEET    6   I 6 PHE B 516  GLN B 518  1  O  LYS B 517   N  VAL B 391           
SHEET    1   J 7 THR B 527  ILE B 528  0                                        
SHEET    2   J 7 GLY B 925  ARG B 929  1  O  ILE B 926   N  THR B 527           
SHEET    3   J 7 LEU B 962  ASP B 966  1  O  ILE B 964   N  PHE B 927           
SHEET    4   J 7 LEU B 995  VAL B 999  1  O  LEU B 997   N  VAL B 963           
SHEET    5   J 7 VAL B 882  THR B 886  1  N  MET B 883   O  PHE B 998           
SHEET    6   J 7 VAL B1016  PHE B1023  1  O  TYR B1019   N  ILE B 884           
SHEET    7   J 7 TYR B1048  ARG B1052 -1  O  THR B1051   N  HIS B1020           
SHEET    1   K 4 VAL B 736  VAL B 738  0                                        
SHEET    2   K 4 GLN B 741  LYS B 748 -1  O  MET B 744   N  VAL B 736           
SHEET    3   K 4 VAL B 768  HIS B 772 -1  O  PHE B 771   N  ILE B 745           
SHEET    4   K 4 VAL B 760  SER B 764 -1  N  GLY B 763   O  ARG B 770           
SHEET    1   L 2 TYR B 837  CYS B 838  0                                        
SHEET    2   L 2 VAL B 913  PRO B 914 -1  O  VAL B 913   N  CYS B 838           
SHEET    1   M 4 THR B 841  GLN B 843  0                                        
SHEET    2   M 4 GLU B 917  GLY B 921  1  O  ILE B 920   N  GLN B 843           
SHEET    3   M 4 LYS B 847  GLY B 853 -1  N  LYS B 847   O  GLY B 921           
SHEET    4   M 4 ASN B 871  LEU B 875 -1  O  THR B 873   N  ILE B 850           
SITE     1 AC1 13 ALA A 649  PHE A 650  ILE A 651  PRO A 670                    
SITE     2 AC1 13 ASN A 671  MET A 672  GLY A 673  GLY A 674                    
SITE     3 AC1 13 LYS A 675  SER A 676  THR A 677  TYR A 815                    
SITE     4 AC1 13 HOH A 937                                                     
CRYST1  105.840  116.130  180.040  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009448  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008611  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005554        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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