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Database: PDB
Entry: 1XNA
LinkDB: 1XNA
Original site: 1XNA 
HEADER    DNA BINDING PROTEIN                     27-FEB-99   1XNA              
TITLE     NMR SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR              
TITLE    2 PROTEIN XRCC1-N-TERMINAL DOMAIN                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (DNA-REPAIR PROTEIN XRCC1);                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-183. RESIDUES 152-           
COMPND   5 183 ARE DISORDERED AND NOT SHOWN.;                                   
COMPND   6 SYNONYM: XRCC1-NTD;                                                  
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELLULAR_LOCATION: NUCLEUS;                                          
SOURCE   6 GENE: XRCC1;                                                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21[DE3]PLYSS;                            
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET23A                                    
KEYWDS    XRCC1, 3D NMR, DNA REPAIR, SINGLE-STRAND BREAK DNA BINDING,           
KEYWDS   2 DNA POLYMERASE-BETA BINDING, BETA SANDWICH, DNA BINDING              
KEYWDS   3 PROTEIN                                                              
EXPDTA    SOLUTION NMR                                                          
AUTHOR    A.MARINTCHEV,G.P.MULLEN                                               
REVDAT   3   24-FEB-09 1XNA    1       VERSN                                    
REVDAT   2   01-APR-03 1XNA    1       JRNL                                     
REVDAT   1   01-SEP-99 1XNA    0                                                
JRNL        AUTH   A.MARINTCHEV,M.A.MULLEN,M.W.MACIEJEWSKI,B.PAN,               
JRNL        AUTH 2 M.R.GRYK,G.P.MULLEN                                          
JRNL        TITL   SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK                
JRNL        TITL 2 REPAIR PROTEIN XRCC1 N-TERMINAL DOMAIN.                      
JRNL        REF    NAT.STRUCT.BIOL.              V.   6   884 1999              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   10467102                                                     
JRNL        DOI    10.1038/12347                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN        
REMARK   3  THE JOURNAL CITATION ABOVE.                                         
REMARK   4                                                                      
REMARK   4 1XNA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000558.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 6.8                                
REMARK 210  IONIC STRENGTH                 : 0.4                                
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : H2O AND D2O                        
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D HNCACB, CBCA(CO)NH, HN(CO)      
REMARK 210                                   CA, 15N-EDITED TOCSY, HCC(CO)      
REMARK 210                                   NH, HCCH TOCSY, HNCO, HNHA,        
REMARK 210                                   HNHB, 2D (HB)CB(CGCD)HD, 1H-       
REMARK 210                                   15N-HSQC, 1H-13C-HSQC, 1H-         
REMARK 210                                   TOCSY, AROMATIC 1H-13C-HSQC,       
REMARK 210                                   HMQC-J, 3D 15N-NOESY, 3D 13C-      
REMARK 210                                   NOESY                              
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ                            
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : DYANA 1.5                          
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS             
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : MINIMIZED AVERAGE STRUCTURE        
REMARK 210                                   OF 23 CONFORMERS                   
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-AND DOUBLE-        
REMARK 210  RESONANCE NMR SPECTROSCOPY ON 13C-, 15N-LABELED XRCC1-N-            
REMARK 210  TERMINAL DOMAIN                                                     
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465     RES C SSSEQI                                                     
REMARK 465     PRO A   152                                                      
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     GLU A   179                                                      
REMARK 465     GLU A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     ALA A   182                                                      
REMARK 465     ASN A   183                                                      
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    SER A  14       90.04    153.86                                   
REMARK 500    LYS A  26       65.33   -114.99                                   
REMARK 500    THR A  29      -87.95   -155.53                                   
REMARK 500    TYR A  30       35.06   -178.04                                   
REMARK 500    LYS A  32     -164.08   -127.33                                   
REMARK 500    GLU A  40       88.26    -52.12                                   
REMARK 500    GLU A  50       -9.96    -51.35                                   
REMARK 500    ASP A  63       77.29   -113.31                                   
REMARK 500    ALA A  66      -51.61   -139.29                                   
REMARK 500    ASP A  83       34.16    -97.05                                   
REMARK 500    VAL A  86       89.37    -58.65                                   
REMARK 500    VAL A  89      179.10    -53.03                                   
REMARK 500    SER A  97      -51.73   -120.18                                   
REMARK 500    ARG A 100      -82.28    -82.36                                   
REMARK 500    SER A 101       38.83   -161.66                                   
REMARK 500    SER A 103     -154.17   -150.98                                   
REMARK 500    ASN A 104      109.48    -54.27                                   
REMARK 500    GLN A 134      128.33    149.70                                   
REMARK 500    LYS A 138      -40.47   -170.66                                   
REMARK 500    PHE A 142     -165.90   -167.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1XNA A    1   183  UNP    P18887   XRCC1_HUMAN      1    183             
SEQADV 1XNA GLU A  179  UNP  P18887    ASP   179 CLONING ARTIFACT               
SEQRES   1 A  183  MET PRO GLU ILE ARG LEU ARG HIS VAL VAL SER CYS SER          
SEQRES   2 A  183  SER GLN ASP SER THR HIS CYS ALA GLU ASN LEU LEU LYS          
SEQRES   3 A  183  ALA ASP THR TYR ARG LYS TRP ARG ALA ALA LYS ALA GLY          
SEQRES   4 A  183  GLU LYS THR ILE SER VAL VAL LEU GLN LEU GLU LYS GLU          
SEQRES   5 A  183  GLU GLN ILE HIS SER VAL ASP ILE GLY ASN ASP GLY SER          
SEQRES   6 A  183  ALA PHE VAL GLU VAL LEU VAL GLY SER SER ALA GLY GLY          
SEQRES   7 A  183  ALA GLY GLU GLN ASP TYR GLU VAL LEU LEU VAL THR SER          
SEQRES   8 A  183  SER PHE MET SER PRO SER GLU SER ARG SER GLY SER ASN          
SEQRES   9 A  183  PRO ASN ARG VAL ARG MET PHE GLY PRO ASP LYS LEU VAL          
SEQRES  10 A  183  ARG ALA ALA ALA GLU LYS ARG TRP ASP ARG VAL LYS ILE          
SEQRES  11 A  183  VAL CYS SER GLN PRO TYR SER LYS ASP SER PRO PHE GLY          
SEQRES  12 A  183  LEU SER PHE VAL ARG PHE HIS SER PRO PRO ASP LYS ASP          
SEQRES  13 A  183  GLU ALA GLU ALA PRO SER GLN LYS VAL THR VAL THR LYS          
SEQRES  14 A  183  LEU GLY GLN PHE ARG VAL LYS GLU GLU GLU GLU SER ALA          
SEQRES  15 A  183  ASN                                                          
HELIX    1   1 ALA A   21  LEU A   25  5                                   5    
HELIX    2   2 PRO A   96  ARG A  100  1                                   5    
HELIX    3   3 ARG A  118  GLU A  122  1                                   5    
SHEET    1   1 5 HIS A   8  SER A  13  0                                        
SHEET    2   1 5 THR A  42  LEU A  49 -1  N  VAL A  46   O  SER A  11           
SHEET    3   1 5 ARG A 127  SER A 133 -1  N  CYS A 132   O  ILE A  43           
SHEET    4   1 5 PHE A  67  SER A  74 -1  N  GLY A  73   O  ARG A 127           
SHEET    5   1 5 TYR A  84  SER A  92 -1  N  LEU A  88   O  VAL A  72           
SHEET    1   2 3 ARG A 107  GLY A 112  0                                        
SHEET    2   2 3 SER A  57  ASN A  62 -1  N  ASN A  62   O  ARG A 107           
SHEET    3   2 3 PHE A 146  HIS A 150 -1  N  HIS A 150   O  SER A  57           
SHEET    1   3 2 TRP A  33  ALA A  35  0                                        
SHEET    2   3 2 PHE A 142  LEU A 144 -1  N  LEU A 144   O  TRP A  33           
SHEET    1   4 2 GLU A  52  ILE A  55  0                                        
SHEET    2   4 2 ARG A 124  TRP A 125 -1  N  TRP A 125   O  GLU A  53           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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