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Database: PDB
Entry: 5E6Q
LinkDB: 5E6Q
Original site: 5E6Q 
HEADER    PROTEIN BINDING                         10-OCT-15   5E6Q              
TITLE     IMPORTIN ALPHA BINDING TO XRCC1 NLS PEPTIDE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IMPORTIN SUBUNIT ALPHA-1;                                  
COMPND   3 CHAIN: B;                                                            
COMPND   4 SYNONYM: IMPORTIN ALPHA P1,KARYOPHERIN SUBUNIT ALPHA-2,PENDULIN,PORE 
COMPND   5 TARGETING COMPLEX 58 KDA SUBUNIT,PTAC58,RAG COHORT PROTEIN 1,SRP1-   
COMPND   6 ALPHA;                                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA REPAIR PROTEIN XRCC1 NLS PEPTIDE;                      
COMPND  10 CHAIN: A;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 241-276;                                      
COMPND  12 SYNONYM: X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 1;                 
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: KPNA2, RCH1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    XRCC1, IMPORTIN, NLS, BIPARTITE, PROTEIN BINDING                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.C.PEDERSEN,T.W.KIRBY,N.R.GASSMAN,C.E.SMITH,S.A.GABEL,M.SOBHANY,     
AUTHOR   2 S.H.WILSON,R.E.LONDON                                                
REVDAT   1   28-OCT-15 5E6Q    0                                                
JRNL        AUTH   T.W.KIRBY,N.R.GASSMAN,C.E.SMITH,L.C.PEDERSEN,S.A.GABEL,      
JRNL        AUTH 2 M.SOBHANY,S.H.WILSON,R.E.LONDON                              
JRNL        TITL   NUCLEAR LOCALIZATION OF THE DNA REPAIR SCAFFOLD XRCC1:       
JRNL        TITL 2 UNCOVERING THE FUNCTIONAL ROLE OF A BIPARTITE NLS.           
JRNL        REF    SCI REP                       V.   5 13405 2015              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   26304019                                                     
JRNL        DOI    10.1038/SREP13405                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.31 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.41                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 31075                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2852                            
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 42.4146 -  6.2495    0.94     2733   141  0.1624 0.1534        
REMARK   3     2  6.2495 -  4.9628    0.96     2783   141  0.1833 0.2053        
REMARK   3     3  4.9628 -  4.3362    0.96     2754   142  0.1391 0.1533        
REMARK   3     4  4.3362 -  3.9401    0.96     2801   146  0.1337 0.1612        
REMARK   3     5  3.9401 -  3.6578    0.96     2785   145  0.1429 0.1800        
REMARK   3     6  3.6578 -  3.4423    0.97     2781   163  0.1608 0.1923        
REMARK   3     7  3.4423 -  3.2699    0.97     2812   135  0.1801 0.2662        
REMARK   3     8  3.2699 -  3.1277    0.97     2788   148  0.1875 0.2067        
REMARK   3     9  3.1277 -  3.0073    0.97     2814   148  0.1925 0.2576        
REMARK   3    10  3.0073 -  2.9035    0.97     2845   150  0.1885 0.2738        
REMARK   3    11  2.9035 -  2.8128    0.97     2850   138  0.1939 0.2527        
REMARK   3    12  2.8128 -  2.7324    0.97     2774   160  0.1945 0.2263        
REMARK   3    13  2.7324 -  2.6605    0.97     2798   144  0.1998 0.2465        
REMARK   3    14  2.6605 -  2.5956    0.96     2804   159  0.2107 0.2921        
REMARK   3    15  2.5956 -  2.5366    0.96     2808   147  0.2178 0.3037        
REMARK   3    16  2.5366 -  2.4826    0.93     2697   148  0.2186 0.2420        
REMARK   3    17  2.4826 -  2.4329    0.90     2624   131  0.2222 0.2659        
REMARK   3    18  2.4329 -  2.3870    0.86     2473   133  0.2355 0.3486        
REMARK   3    19  2.3870 -  2.3444    0.78     2261   131  0.2534 0.3241        
REMARK   3    20  2.3444 -  2.3047    0.70     1999   102  0.2414 0.2956        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           3379                                  
REMARK   3   ANGLE     :  0.680           4620                                  
REMARK   3   CHIRALITY :  0.046            562                                  
REMARK   3   PLANARITY :  0.004            594                                  
REMARK   3   DIHEDRAL  : 10.683           1214                                  
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 5E6Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214449.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31129                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3UKY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE, 0.1M BIS-TRIS     
REMARK 280  PROPANE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
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       39.33400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.34950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.05600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.34950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.33400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.05600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
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 B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 465     HIS B    22                                                      
REMARK 465     HIS B    23                                                      
REMARK 465     HIS B    24                                                      
REMARK 465     HIS B    25                                                      
REMARK 465     HIS B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     LEU B    30                                                      
REMARK 465     VAL B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     GLY B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     MET B    37                                                      
REMARK 465     LYS B    38                                                      
REMARK 465     GLU B    39                                                      
REMARK 465     THR B    40                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     LYS B    44                                                      
REMARK 465     PHE B    45                                                      
REMARK 465     GLU B    46                                                      
REMARK 465     ARG B    47                                                      
REMARK 465     GLN B    48                                                      
REMARK 465     HIS B    49                                                      
REMARK 465     MET B    50                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     SER B    52                                                      
REMARK 465     PRO B    53                                                      
REMARK 465     ASP B    54                                                      
REMARK 465     LEU B    55                                                      
REMARK 465     GLY B    56                                                      
REMARK 465     THR B    57                                                      
REMARK 465     ASP B    58                                                      
REMARK 465     ASP B    59                                                      
REMARK 465     ASP B    60                                                      
REMARK 465     ASP B    61                                                      
REMARK 465     LYS B    62                                                      
REMARK 465     ALA B    63                                                      
REMARK 465     MET B    64                                                      
REMARK 465     ALA B    65                                                      
REMARK 465     ASP B    66                                                      
REMARK 465     ILE B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     GLN B    71                                                      
REMARK 465     SER B   497                                                      
REMARK 465     VAL B   498                                                      
REMARK 465     GLU B   499                                                      
REMARK 465     GLU B   500                                                      
REMARK 465     GLU B   501                                                      
REMARK 465     GLU B   502                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     GLN B   504                                                      
REMARK 465     ASN B   505                                                      
REMARK 465     VAL B   506                                                      
REMARK 465     VAL B   507                                                      
REMARK 465     PRO B   508                                                      
REMARK 465     GLU B   509                                                      
REMARK 465     THR B   510                                                      
REMARK 465     THR B   511                                                      
REMARK 465     SER B   512                                                      
REMARK 465     GLU B   513                                                      
REMARK 465     GLY B   514                                                      
REMARK 465     PHE B   515                                                      
REMARK 465     ALA B   516                                                      
REMARK 465     PHE B   517                                                      
REMARK 465     GLN B   518                                                      
REMARK 465     VAL B   519                                                      
REMARK 465     GLN B   520                                                      
REMARK 465     ASP B   521                                                      
REMARK 465     GLY B   522                                                      
REMARK 465     ALA B   523                                                      
REMARK 465     PRO B   524                                                      
REMARK 465     GLY B   525                                                      
REMARK 465     THR B   526                                                      
REMARK 465     PHE B   527                                                      
REMARK 465     ASN B   528                                                      
REMARK 465     PHE B   529                                                      
REMARK 465     SER A   241                                                      
REMARK 465     PRO A   242                                                      
REMARK 465     LYS A   243                                                      
REMARK 465     ASP A   249                                                      
REMARK 465     LEU A   250                                                      
REMARK 465     ASN A   251                                                      
REMARK 465     GLN A   252                                                      
REMARK 465     GLU A   253                                                      
REMARK 465     GLU A   254                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     THR A   257                                                      
REMARK 465     PRO A   258                                                      
REMARK 465     SER A   259                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     PRO A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     GLN A   264                                                      
REMARK 465     LEU A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     PRO A   267                                                      
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     ASN B  75    CG   OD1  ND2                                       
REMARK 470     GLN B  95    CD   OE1  NE2                                       
REMARK 470     GLU B 107    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 108    CG   CD   CE   NZ                                   
REMARK 470     GLN B 109    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 123    CE   NZ                                             
REMARK 470     LYS B 291    CE   NZ                                             
REMARK 470     LYS B 330    CE   NZ                                             
REMARK 470     LYS B 392    CD   CE   NZ                                        
REMARK 470     LYS B 432    CG   CD   CE   NZ                                   
REMARK 470     GLU B 458    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 459    CG   CD   CE   NZ                                   
REMARK 470     GLU B 465    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 474    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 477    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 478    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 480    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 482    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 485    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 486    CG   CD   CE   NZ                                   
REMARK 470     LEU B 489    CG   CD1  CD2                                       
REMARK 470     GLU B 493    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 494    CD   CE   NZ                                        
REMARK 470     SER A 268    CB   OG                                             
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    GLN B 109       74.77     49.69                                   
REMARK 500    ASN B 239      149.23     71.97                                   
REMARK 500    LYS B 432       42.37    -83.02                                   
REMARK 500    ARG B 478       59.15   -107.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 922        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH B 923        DISTANCE =  6.12 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 604                  
DBREF  5E6Q B   70   529  UNP    P52293   IMA1_MOUSE      70    529             
DBREF  5E6Q A  241   276  UNP    P18887   XRCC1_HUMAN    241    276             
SEQADV 5E6Q MET B   20  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q HIS B   21  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q HIS B   22  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q HIS B   23  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q HIS B   24  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q HIS B   25  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q HIS B   26  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q SER B   27  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q SER B   28  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q GLY B   29  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q LEU B   30  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q VAL B   31  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q PRO B   32  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ARG B   33  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q GLY B   34  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q SER B   35  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q GLY B   36  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q MET B   37  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q LYS B   38  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q GLU B   39  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q THR B   40  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ALA B   41  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ALA B   42  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ALA B   43  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q LYS B   44  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q PHE B   45  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q GLU B   46  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ARG B   47  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q GLN B   48  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q HIS B   49  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q MET B   50  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ASP B   51  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q SER B   52  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q PRO B   53  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ASP B   54  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q LEU B   55  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q GLY B   56  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q THR B   57  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ASP B   58  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ASP B   59  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ASP B   60  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ASP B   61  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q LYS B   62  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ALA B   63  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q MET B   64  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ALA B   65  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ASP B   66  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q ILE B   67  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q GLY B   68  UNP  P52293              EXPRESSION TAG                 
SEQADV 5E6Q SER B   69  UNP  P52293              EXPRESSION TAG                 
SEQRES   1 B  510  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 B  510  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 B  510  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 B  510  ASP ASP ASP LYS ALA MET ALA ASP ILE GLY SER ASN GLN          
SEQRES   5 B  510  GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL LYS GLY          
SEQRES   6 B  510  ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN ALA THR          
SEQRES   7 B  510  GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS GLN PRO          
SEQRES   8 B  510  PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE PRO LYS          
SEQRES   9 B  510  PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER PRO ILE          
SEQRES  10 B  510  GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE ALA SER          
SEQRES  11 B  510  GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP GLY GLY          
SEQRES  12 B  510  ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER PRO HIS          
SEQRES  13 B  510  ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU GLY ASN          
SEQRES  14 B  510  ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU VAL ILE          
SEQRES  15 B  510  LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU LEU ALA          
SEQRES  16 B  510  VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR LEU ARG          
SEQRES  17 B  510  ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG ASN LYS          
SEQRES  18 B  510  ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN ILE LEU          
SEQRES  19 B  510  PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP PRO GLU          
SEQRES  20 B  510  VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR LEU THR          
SEQRES  21 B  510  ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL LYS LYS          
SEQRES  22 B  510  GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY ALA THR          
SEQRES  23 B  510  GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA ILE GLY          
SEQRES  24 B  510  ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN LYS VAL          
SEQRES  25 B  510  ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER LEU LEU          
SEQRES  26 B  510  THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA THR TRP          
SEQRES  27 B  510  THR MET SER ASN ILE THR ALA GLY ARG GLN ASP GLN ILE          
SEQRES  28 B  510  GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE LEU VAL          
SEQRES  29 B  510  GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN LYS GLU          
SEQRES  30 B  510  ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY GLY THR          
SEQRES  31 B  510  VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY ILE ILE          
SEQRES  32 B  510  GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP THR LYS          
SEQRES  33 B  510  ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN ILE PHE          
SEQRES  34 B  510  GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS LEU SER          
SEQRES  35 B  510  ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS ILE GLU          
SEQRES  36 B  510  ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR LYS ALA          
SEQRES  37 B  510  SER LEU ASN LEU ILE GLU LYS TYR PHE SER VAL GLU GLU          
SEQRES  38 B  510  GLU GLU ASP GLN ASN VAL VAL PRO GLU THR THR SER GLU          
SEQRES  39 B  510  GLY PHE ALA PHE GLN VAL GLN ASP GLY ALA PRO GLY THR          
SEQRES  40 B  510  PHE ASN PHE                                                  
SEQRES   1 A   36  SER PRO LYS GLY LYS ARG LYS LEU ASP LEU ASN GLN GLU          
SEQRES   2 A   36  GLU LYS LYS THR PRO SER LYS PRO PRO ALA GLN LEU SER          
SEQRES   3 A   36  PRO SER VAL PRO LYS ARG PRO LYS LEU PRO                      
HET    SO4  B 601       5                                                       
HET    GOL  B 602       6                                                       
HET     CL  B 603       1                                                       
HET     CL  B 604       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   7  HOH   *228(H2 O)                                                    
HELIX    1 AA1 SER B   77  SER B   87  1                                  11    
HELIX    2 AA2 ASN B   89  LEU B  104  1                                  16    
HELIX    3 AA3 PRO B  111  ALA B  118  1                                   8    
HELIX    4 AA4 LEU B  120  LEU B  128  1                                   9    
HELIX    5 AA5 CYS B  133  SER B  149  1                                  17    
HELIX    6 AA6 THR B  151  GLY B  161  1                                  11    
HELIX    7 AA7 GLY B  162  LEU B  170  1                                   9    
HELIX    8 AA8 LEU B  171  SER B  173  5                                   3    
HELIX    9 AA9 HIS B  175  GLY B  191  1                                  17    
HELIX   10 AB1 GLY B  193  HIS B  203  1                                  11    
HELIX   11 AB2 ALA B  205  LEU B  212  1                                   8    
HELIX   12 AB3 ASP B  217  LEU B  221  5                                   5    
HELIX   13 AB4 ALA B  222  CYS B  237  1                                  16    
HELIX   14 AB5 PRO B  245  LEU B  260  1                                  16    
HELIX   15 AB6 ASP B  264  THR B  279  1                                  16    
HELIX   16 AB7 PRO B  282  LYS B  291  1                                  10    
HELIX   17 AB8 VAL B  294  GLY B  303  1                                  10    
HELIX   18 AB9 GLU B  306  VAL B  321  1                                  16    
HELIX   19 AC1 THR B  324  ALA B  334  1                                  11    
HELIX   20 AC2 GLY B  335  ALA B  338  5                                   4    
HELIX   21 AC3 VAL B  339  LEU B  344  1                                   6    
HELIX   22 AC4 LYS B  348  THR B  363  1                                  16    
HELIX   23 AC5 ARG B  366  HIS B  376  1                                  11    
HELIX   24 AC6 LEU B  378  LYS B  388  1                                  11    
HELIX   25 AC7 ASP B  390  GLY B  408  1                                  19    
HELIX   26 AC8 THR B  409  CYS B  419  1                                  11    
HELIX   27 AC9 ILE B  421  LEU B  428  1                                   8    
HELIX   28 AD1 LEU B  429  ALA B  431  5                                   3    
HELIX   29 AD2 ASP B  433  LYS B  453  1                                  21    
HELIX   30 AD3 GLU B  456  CYS B  467  1                                  12    
HELIX   31 AD4 GLY B  468  LEU B  476  1                                   9    
HELIX   32 AD5 GLN B  477  HIS B  479  5                                   3    
HELIX   33 AD6 ASN B  481  PHE B  496  1                                  16    
CISPEP   1 ASN B  241    PRO B  242          0        -1.85                     
SITE     1 AC1  7 LYS B 202  GLN B 352  LYS B 388  HOH B 705                    
SITE     2 AC1  7 HOH B 722  HOH B 730  HOH B 788                               
SITE     1 AC2  5 ILE B 332  ASP B 333  GLY B 335  HIS B 376                    
SITE     2 AC2  5 HOH B 703                                                     
SITE     1 AC3  1 THR B 349                                                     
SITE     1 AC4  2 SER B 194  ALA B 195                                          
CRYST1   78.668   90.112  100.699  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      0.012712  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011097  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009931        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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