Header list of 2d8m.pdb file
Complete list - r 9 2 Bytes
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
Complete list - r 9 2 Bytes