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Database: PDB
Entry: 3LQC
LinkDB: 3LQC
Original site: 3LQC 
HEADER    DNA-BINDING PROTEIN                     09-FEB-10   3LQC              
TITLE     X-RAY CRYSTAL STRUCTURE OF OXIDIZED XRCC1 BOUND TO DNA POL BETA PALM  
TITLE    2 THUMB DOMAIN                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA REPAIR PROTEIN XRCC1;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 1;                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA POLYMERASE BETA;                                       
COMPND   8 CHAIN: B;                                                            
COMPND   9 EC: 2.7.7.7, 4.2.99.-;                                               
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 STRAIN: HOMO SAPIENS;                                                
SOURCE   6 GENE: XRCC1;                                                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 RIL;                                  
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET21A;                                   
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  14 ORGANISM_COMMON: RAT;                                                
SOURCE  15 ORGANISM_TAXID: 10116;                                               
SOURCE  16 GENE: POLB;                                                          
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21 RIL;                                  
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ALLOSTERIC DISULFIDE, SCAFFOLDING PROTEIN, DNA REPAIR, DNA DAMAGE,    
KEYWDS   2 NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, DNA REPLICATION, DNA          
KEYWDS   3 SYNTHESIS, DNA-BINDING, DNA-DIRECTED DNA POLYMERASE, LYASE,          
KEYWDS   4 MAGNESIUM, METAL-BINDING, NUCLEOTIDYLTRANSFERASE, SODIUM,            
KEYWDS   5 TRANSFERASE, DNA-BINDING PROTEIN                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.CUNEO,J.M.KRAHN,R.E.LONDON                                        
REVDAT   1   28-APR-10 3LQC    0                                                
JRNL        AUTH   M.J.CUNEO,R.E.LONDON                                         
JRNL        TITL   OXIDATION STATE OF THE XRCC1 N-TERMINAL DOMAIN REGULATES     
JRNL        TITL 2 DNA POLYMERASE BETA BINDING AFFINITY.                        
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107  6805 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20351257                                                     
JRNL        DOI    10.1073/PNAS.0914077107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17764                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 889                             
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 24.6290 -  4.2630    1.00     2962   156  0.1600 0.2050        
REMARK   3     2  4.2630 -  3.3860    1.00     2836   150  0.1540 0.2070        
REMARK   3     3  3.3860 -  2.9590    1.00     2792   147  0.1850 0.2770        
REMARK   3     4  2.9590 -  2.6890    1.00     2762   145  0.2030 0.2860        
REMARK   3     5  2.6890 -  2.4970    1.00     2772   146  0.2240 0.2770        
REMARK   3     6  2.4970 -  2.3490    1.00     2751   145  0.2360 0.3250        
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              : 0.34                                          
REMARK   3   B_SOL              : 26.94                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.56700                                              
REMARK   3    B22 (A**2) : 2.56700                                              
REMARK   3    B33 (A**2) : -5.13300                                             
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      :  0.006           2795                                  
REMARK   3   ANGLE     :  0.920           3772                                  
REMARK   3   CHIRALITY :  0.059            409                                  
REMARK   3   PLANARITY :  0.004            498                                  
REMARK   3   DIHEDRAL  : 15.895           1044                                  
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 3LQC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057597.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 92                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17765                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 10.300                             
REMARK 200  R MERGE                    (I) : 0.12200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1XNA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG 3350, 0.2-0.3M TRI-           
REMARK 280  POTASSIUM CITRATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.05333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       84.10667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       84.10667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       42.05333            
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: 1610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     PRO A   153                                                      
REMARK 465     ASP A   154                                                      
REMARK 465     LYS A   155                                                      
REMARK 465     ASP A   156                                                      
REMARK 465     GLU A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     ALA A   160                                                      
REMARK 465     PRO A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     GLN A   163                                                      
REMARK 465     LYS A   164                                                      
REMARK 465     VAL A   165                                                      
REMARK 465     THR A   166                                                      
REMARK 465     VAL A   167                                                      
REMARK 465     THR A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     LEU A   170                                                      
REMARK 465     GLY A   171                                                      
REMARK 465     GLN A   172                                                      
REMARK 465     PHE A   173                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     VAL A   175                                                      
REMARK 465     LYS A   176                                                      
REMARK 465     GLU A   177                                                      
REMARK 465     GLU A   178                                                      
REMARK 465     ASP A   179                                                      
REMARK 465     GLU A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     ALA A   182                                                      
REMARK 465     ASN A   183                                                      
REMARK 465     HIS A   184                                                      
REMARK 465     HIS A   185                                                      
REMARK 465     HIS A   186                                                      
REMARK 465     HIS A   187                                                      
REMARK 465     HIS A   188                                                      
REMARK 465     HIS A   189                                                      
REMARK 465     HIS B   336                                                      
REMARK 465     HIS B   337                                                      
REMARK 465     HIS B   338                                                      
REMARK 465     HIS B   339                                                      
REMARK 465     HIS B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  31    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     ARG A 118    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 138    CE   NZ                                             
REMARK 470     TYR B 142    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE B 143    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 209    CG   CD   CE   NZ                                   
REMARK 470     ASN B 245    CG   OD1  ND2                                       
REMARK 470     GLU B 335    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    PRO A     2     O1   CO3 A   190              2.10            
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    CYS A  12       72.48   -107.09                                   
REMARK 500    SER A  13      -77.25    -63.76                                   
REMARK 500    SER A  14       50.42   -100.85                                   
REMARK 500    ALA A  79       96.92   -163.92                                   
REMARK 500    GLN A 134       75.09   -151.24                                   
REMARK 500    SER A 137       55.35   -142.18                                   
REMARK 500    PRO A 141       49.01    -84.80                                   
REMARK 500    PHE B 143      -60.86    -94.67                                   
REMARK 500    ASP B 170      114.31   -171.23                                   
REMARK 500    CYS B 178     -145.50   -108.99                                   
REMARK 500    ASN B 294     -165.29   -123.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     CO3 A  190                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 278  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  74   O                                                      
REMARK 620 2 ALA A  76   O    79.3                                              
REMARK 620 3 GLY A  78   O    73.9  86.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 278                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 190                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K75   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF REDUCED XRCC1 BOUND TO DNA POL            
REMARK 900 BETA CATALYTIC DOMAIN                                                
REMARK 900 RELATED ID: 3K77   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF XRCC1                                     
DBREF  3LQC A    1   183  UNP    P18887   XRCC1_HUMAN      1    183             
DBREF  3LQC B  142   335  UNP    P06766   DPOLB_RAT      142    335             
SEQADV 3LQC HIS A  184  UNP  P18887              EXPRESSION TAG                 
SEQADV 3LQC HIS A  185  UNP  P18887              EXPRESSION TAG                 
SEQADV 3LQC HIS A  186  UNP  P18887              EXPRESSION TAG                 
SEQADV 3LQC HIS A  187  UNP  P18887              EXPRESSION TAG                 
SEQADV 3LQC HIS A  188  UNP  P18887              EXPRESSION TAG                 
SEQADV 3LQC HIS A  189  UNP  P18887              EXPRESSION TAG                 
SEQADV 3LQC HIS B  336  UNP  P06766              EXPRESSION TAG                 
SEQADV 3LQC HIS B  337  UNP  P06766              EXPRESSION TAG                 
SEQADV 3LQC HIS B  338  UNP  P06766              EXPRESSION TAG                 
SEQADV 3LQC HIS B  339  UNP  P06766              EXPRESSION TAG                 
SEQADV 3LQC HIS B  340  UNP  P06766              EXPRESSION TAG                 
SEQADV 3LQC HIS B  341  UNP  P06766              EXPRESSION TAG                 
SEQRES   1 A  189  MET PRO GLU ILE ARG LEU ARG HIS VAL VAL SER CYS SER          
SEQRES   2 A  189  SER GLN ASP SER THR HIS CYS ALA GLU ASN LEU LEU LYS          
SEQRES   3 A  189  ALA ASP THR TYR ARG LYS TRP ARG ALA ALA LYS ALA GLY          
SEQRES   4 A  189  GLU LYS THR ILE SER VAL VAL LEU GLN LEU GLU LYS GLU          
SEQRES   5 A  189  GLU GLN ILE HIS SER VAL ASP ILE GLY ASN ASP GLY SER          
SEQRES   6 A  189  ALA PHE VAL GLU VAL LEU VAL GLY SER SER ALA GLY GLY          
SEQRES   7 A  189  ALA GLY GLU GLN ASP TYR GLU VAL LEU LEU VAL THR SER          
SEQRES   8 A  189  SER PHE MET SER PRO SER GLU SER ARG SER GLY SER ASN          
SEQRES   9 A  189  PRO ASN ARG VAL ARG MET PHE GLY PRO ASP LYS LEU VAL          
SEQRES  10 A  189  ARG ALA ALA ALA GLU LYS ARG TRP ASP ARG VAL LYS ILE          
SEQRES  11 A  189  VAL CYS SER GLN PRO TYR SER LYS ASP SER PRO PHE GLY          
SEQRES  12 A  189  LEU SER PHE VAL ARG PHE HIS SER PRO PRO ASP LYS ASP          
SEQRES  13 A  189  GLU ALA GLU ALA PRO SER GLN LYS VAL THR VAL THR LYS          
SEQRES  14 A  189  LEU GLY GLN PHE ARG VAL LYS GLU GLU ASP GLU SER ALA          
SEQRES  15 A  189  ASN HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  200  TYR PHE GLU ASP PHE GLU LYS ARG ILE PRO ARG GLU GLU          
SEQRES   2 B  200  MET LEU GLN MET GLN ASP ILE VAL LEU ASN GLU VAL LYS          
SEQRES   3 B  200  LYS LEU ASP PRO GLU TYR ILE ALA THR VAL CYS GLY SER          
SEQRES   4 B  200  PHE ARG ARG GLY ALA GLU SER SER GLY ASP MET ASP VAL          
SEQRES   5 B  200  LEU LEU THR HIS PRO ASN PHE THR SER GLU SER SER LYS          
SEQRES   6 B  200  GLN PRO LYS LEU LEU HIS ARG VAL VAL GLU GLN LEU GLN          
SEQRES   7 B  200  LYS VAL ARG PHE ILE THR ASP THR LEU SER LYS GLY GLU          
SEQRES   8 B  200  THR LYS PHE MET GLY VAL CYS GLN LEU PRO SER GLU ASN          
SEQRES   9 B  200  ASP GLU ASN GLU TYR PRO HIS ARG ARG ILE ASP ILE ARG          
SEQRES  10 B  200  LEU ILE PRO LYS ASP GLN TYR TYR CYS GLY VAL LEU TYR          
SEQRES  11 B  200  PHE THR GLY SER ASP ILE PHE ASN LYS ASN MET ARG ALA          
SEQRES  12 B  200  HIS ALA LEU GLU LYS GLY PHE THR ILE ASN GLU TYR THR          
SEQRES  13 B  200  ILE ARG PRO LEU GLY VAL THR GLY VAL ALA GLY GLU PRO          
SEQRES  14 B  200  LEU PRO VAL ASP SER GLU GLN ASP ILE PHE ASP TYR ILE          
SEQRES  15 B  200  GLN TRP ARG TYR ARG GLU PRO LYS ASP ARG SER GLU HIS          
SEQRES  16 B  200  HIS HIS HIS HIS HIS                                          
HET     NA  A 278       1                                                       
HET    CO3  A 190       3                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     CO3 CARBONATE ION                                                    
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  CO3    C O3 2-                                                      
FORMUL   5  HOH   *234(H2 O)                                                    
HELIX    1   1 GLU A    3  ARG A    5  5                                   3    
HELIX    2   2 ASP A   16  LYS A   26  1                                  11    
HELIX    3   3 ALA A   27  LYS A   37  1                                  11    
HELIX    4   4 GLY A   80  TYR A   84  5                                   5    
HELIX    5   5 SER A   95  GLY A  102  1                                   8    
HELIX    6   6 GLY A  112  LEU A  116  5                                   5    
HELIX    7   7 VAL A  117  GLU A  122  1                                   6    
HELIX    8   8 ARG B  152  ASP B  170  1                                  19    
HELIX    9   9 CYS B  178  ARG B  183  1                                   6    
HELIX   10  10 PRO B  208  VAL B  221  1                                  14    
HELIX   11  11 PRO B  261  ASP B  263  5                                   3    
HELIX   12  12 GLN B  264  GLY B  274  1                                  11    
HELIX   13  13 SER B  275  LYS B  289  1                                  15    
HELIX   14  14 SER B  315  ILE B  323  1                                   9    
HELIX   15  15 GLU B  329  ARG B  333  5                                   5    
SHEET    1   A 5 ARG A   7  CYS A  12  0                                        
SHEET    2   A 5 THR A  42  GLU A  53  1  O  GLN A  48   N  VAL A  10           
SHEET    3   A 5 TRP A 125  SER A 133 -1  O  VAL A 128   N  LEU A  47           
SHEET    4   A 5 PHE A  67  GLY A  73 -1  N  GLU A  69   O  VAL A 131           
SHEET    5   A 5 GLU A  85  SER A  92 -1  O  GLU A  85   N  VAL A  72           
SHEET    1   B 3 VAL A 108  PHE A 111  0                                        
SHEET    2   B 3 SER A  57  ASP A  63 -1  N  ILE A  60   O  ARG A 109           
SHEET    3   B 3 GLY A 143  HIS A 150 -1  O  SER A 145   N  GLY A  61           
SHEET    1   C 2 ILE B 150  PRO B 151  0                                        
SHEET    2   C 2 SER B 187  SER B 188 -1  O  SER B 188   N  ILE B 150           
SHEET    1   D 5 ILE B 174  VAL B 177  0                                        
SHEET    2   D 5 MET B 191  THR B 196 -1  O  LEU B 194   N  THR B 176           
SHEET    3   D 5 ARG B 253  LEU B 259  1  O  ARG B 258   N  LEU B 195           
SHEET    4   D 5 LYS B 234  CYS B 239 -1  N  PHE B 235   O  ILE B 257           
SHEET    5   D 5 ILE B 224  LYS B 230 -1  N  SER B 229   O  MET B 236           
SHEET    1   E 2 PHE B 291  ILE B 293  0                                        
SHEET    2   E 2 ILE B 298  PRO B 300 -1  O  ARG B 299   N  THR B 292           
SSBOND   1 CYS A   12    CYS A   20                          1555   1555  2.03  
LINK         O   SER A  74                NA    NA A 278     1555   1555  2.82  
LINK         O   ALA A  76                NA    NA A 278     1555   1555  2.86  
LINK         O   GLY A  78                NA    NA A 278     1555   1555  2.96  
LINK         N   PRO A   2                 C   CO3 A 190     1555   1555  1.36  
CISPEP   1 GLY B  274    SER B  275          0         6.11                     
SITE     1 AC1  3 SER A  74  ALA A  76  GLY A  78                               
SITE     1 AC2  6 PRO A   2  GLU A   3  ARG A   7  SER A  44                    
SITE     2 AC2  6 LYS A 129  HOH A 193                                          
CRYST1   75.240   75.240  126.160  90.00  90.00 120.00 P 31 2 1      6          
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      0.013291  0.007673  0.000000        0.00000                         
SCALE2      0.000000  0.015347  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007926        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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