HEADER DNA BINDING PROTEIN 06-DEC-05 2D8M
TITLE SOLUTION STRUCTURE OF THE FIRST BRCT DOMAIN OF DNA-REPAIR PROTEIN
TITLE 2 XRCC1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-REPAIR PROTEIN XRCC1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BRCT DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: XRCC1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050322-07;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PARALLEL BETA-SHEET, DNA LIGASE III, POLY(ADP-RIBOSE) POLYMERASE-1,
KEYWDS 2 DNA POLYMERASE BETA, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS 3 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D8M 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D8M 1 VERSN
REVDAT 1 06-JUN-06 2D8M 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST BRCT DOMAIN OF DNA-REPAIR
JRNL TITL 2 PROTEIN XRCC1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D8M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025123.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.89MM BRCT DOMAIN U-15N,13C;
REMARK 210 20MM TRISHCL, 100MM NACL, 1MM
REMARK 210 DTT, 0.02% NAN3; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.901, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 1 ARG A 13 164.40 -45.88
REMARK 500 1 PRO A 16 0.58 -69.74
REMARK 500 1 ALA A 68 -177.04 -66.44
REMARK 500 1 SER A 112 48.50 -87.89
REMARK 500 1 SER A 124 44.11 -81.49
REMARK 500 1 PRO A 126 2.80 -69.77
REMARK 500 1 SER A 128 87.65 -59.63
REMARK 500 2 GLU A 8 66.18 -117.88
REMARK 500 2 ALA A 14 43.69 -80.80
REMARK 500 2 LEU A 23 41.49 -104.87
REMARK 500 2 GLU A 87 -32.07 -35.93
REMARK 500 2 PRO A 109 86.93 -69.76
REMARK 500 2 ASP A 116 137.20 -39.29
REMARK 500 2 HIS A 120 -35.15 -37.20
REMARK 500 3 SER A 3 41.07 -98.14
REMARK 500 3 PRO A 12 0.12 -69.71
REMARK 500 3 ARG A 13 113.87 -38.54
REMARK 500 3 CYS A 92 -36.78 -35.08
REMARK 500 3 SER A 113 42.44 -100.78
REMARK 500 4 TRP A 56 107.59 -53.68
REMARK 500 4 ALA A 68 -179.89 -69.83
REMARK 500 4 PRO A 100 99.03 -69.77
REMARK 500 4 SER A 119 127.90 -35.81
REMARK 500 4 SER A 128 135.08 -34.74
REMARK 500 5 ALA A 14 40.87 -102.11
REMARK 500 5 TRP A 56 89.40 -62.44
REMARK 500 5 ALA A 68 -175.56 -68.27
REMARK 500 5 GLU A 87 -26.47 -38.65
REMARK 500 5 CYS A 92 -33.64 -34.57
REMARK 500 5 ARG A 96 35.61 70.89
REMARK 500 5 SER A 111 73.49 -108.33
REMARK 500 5 GLU A 114 78.37 -113.90
REMARK 500 5 ALA A 118 106.83 -163.12
REMARK 500 6 PRO A 16 2.51 -69.71
REMARK 500 6 ALA A 68 -175.07 -64.50
REMARK 500 6 SER A 112 -60.72 -100.17
REMARK 500 7 SER A 2 139.19 -170.74
REMARK 500 7 ARG A 11 139.21 -34.57
REMARK 500 7 LEU A 23 40.97 -105.08
REMARK 500 7 ALA A 68 -178.94 -57.05
REMARK 500 7 SER A 119 89.24 -68.22
REMARK 500 7 PRO A 126 -174.31 -69.77
REMARK 500 8 PRO A 16 2.03 -69.75
REMARK 500 8 LEU A 23 56.37 -106.23
REMARK 500 8 PRO A 109 89.24 -69.76
REMARK 500 8 SER A 113 49.55 36.52
REMARK 500 8 ALA A 118 43.02 -108.47
REMARK 500 8 SER A 128 42.26 -96.08
REMARK 500 9 ARG A 13 173.45 -47.22
REMARK 500 9 ALA A 14 33.21 -85.05
REMARK 500
REMARK 500 THIS ENTRY HAS 141 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003000003.1 RELATED DB: TARGETDB
DBREF 2D8M A 8 123 UNP P18887 XRCC1_HUMAN 305 420
SEQADV 2D8M GLY A 1 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M SER A 2 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M SER A 3 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M GLY A 4 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M SER A 5 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M SER A 6 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M GLY A 7 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M GLN A 102 UNP P18887 ARG 399 SEE REMARK 999
SEQADV 2D8M SER A 124 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M GLY A 125 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M PRO A 126 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M SER A 127 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M SER A 128 UNP P18887 CLONING ARTIFACT
SEQADV 2D8M GLY A 129 UNP P18887 CLONING ARTIFACT
SEQRES 1 A 129 GLY SER SER GLY SER SER GLY GLU PRO ARG ARG PRO ARG
SEQRES 2 A 129 ALA GLY PRO GLU GLU LEU GLY LYS ILE LEU GLN GLY VAL
SEQRES 3 A 129 VAL VAL VAL LEU SER GLY PHE GLN ASN PRO PHE ARG SER
SEQRES 4 A 129 GLU LEU ARG ASP LYS ALA LEU GLU LEU GLY ALA LYS TYR
SEQRES 5 A 129 ARG PRO ASP TRP THR ARG ASP SER THR HIS LEU ILE CYS
SEQRES 6 A 129 ALA PHE ALA ASN THR PRO LYS TYR SER GLN VAL LEU GLY
SEQRES 7 A 129 LEU GLY GLY ARG ILE VAL ARG LYS GLU TRP VAL LEU ASP
SEQRES 8 A 129 CYS HIS ARG MET ARG ARG ARG LEU PRO SER GLN ARG TYR
SEQRES 9 A 129 LEU MET ALA GLY PRO GLY SER SER SER GLU GLU ASP GLU
SEQRES 10 A 129 ALA SER HIS SER GLY GLY SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 15 GLY A 20 1 6
HELIX 2 2 PRO A 36 LEU A 48 1 13
HELIX 3 3 THR A 70 GLY A 80 1 11
HELIX 4 4 LYS A 86 MET A 95 1 10
HELIX 5 5 PRO A 100 LEU A 105 5 6
SHEET 1 A 4 ALA A 50 ARG A 53 0
SHEET 2 A 4 VAL A 26 SER A 31 1 N VAL A 26 O LYS A 51
SHEET 3 A 4 HIS A 62 CYS A 65 1 O ILE A 64 N VAL A 29
SHEET 4 A 4 ARG A 82 ARG A 85 1 O ARG A 82 N LEU A 63
CISPEP 1 ASN A 35 PRO A 36 1 -0.06
CISPEP 2 ASN A 35 PRO A 36 2 -0.06
CISPEP 3 ASN A 35 PRO A 36 3 -0.08
CISPEP 4 ASN A 35 PRO A 36 4 -0.07
CISPEP 5 ASN A 35 PRO A 36 5 -0.16
CISPEP 6 ASN A 35 PRO A 36 6 -0.07
CISPEP 7 ASN A 35 PRO A 36 7 -0.02
CISPEP 8 ASN A 35 PRO A 36 8 -0.05
CISPEP 9 ASN A 35 PRO A 36 9 -0.04
CISPEP 10 ASN A 35 PRO A 36 10 -0.01
CISPEP 11 ASN A 35 PRO A 36 11 -0.07
CISPEP 12 ASN A 35 PRO A 36 12 -0.10
CISPEP 13 ASN A 35 PRO A 36 13 -0.07
CISPEP 14 ASN A 35 PRO A 36 14 0.01
CISPEP 15 ASN A 35 PRO A 36 15 -0.05
CISPEP 16 ASN A 35 PRO A 36 16 -0.02
CISPEP 17 ASN A 35 PRO A 36 17 -0.10
CISPEP 18 ASN A 35 PRO A 36 18 -0.06
CISPEP 19 ASN A 35 PRO A 36 19 -0.10
CISPEP 20 ASN A 35 PRO A 36 20 -0.05
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
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
