HEADER LIGASE 17-NOV-06 2E2W
TITLE SOLUTION STRUCTURE OF THE FIRST BRCT DOMAIN OF HUMAN DNA
TITLE 2 LIGASE IV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA LIGASE 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BRCT DOMAIN;
COMPND 5 SYNONYM: DNA LIGASE IV, POLYDEOXYRIBONUCLEOTIDE SYNTHASE
COMPND 6 [ATP] 4;
COMPND 7 EC: 6.5.1.1;
COMPND 8 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: LIG4;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P060731-14;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS 3LAYERS A/B/A, PARALLEL BETA-SHEET OF 4 STRANDS, XRCC4, NON-
KEYWDS 2 HOMOLOGOUS END JOINTING, V(D)J RECOMBINATION, STRUCTURAL
KEYWDS 3 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 4 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 5 GENOMICS/PROTEOMICS INITIATIVE, RSGI, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 2 24-FEB-09 2E2W 1 VERSN
REVDAT 1 05-DEC-06 2E2W 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST BRCT DOMAIN OF
JRNL TITL 2 HUMAN DNA LIGASE IV
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2E2W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB026156.
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 : 1.23MM UNIFORMLY 13C AND 15N
REMARK 210 LABELLED PROTEIN; 20MM
REMARK 210 TRISHCL, 100MM NACL, 1MM DTT,
REMARK 210 0.02% NAN3, 10% D2O, 90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY, 3D_
REMARK 210 15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, NMRPIPE 20020425,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.9816,
REMARK 210 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 : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY,TARGET FUNCTION
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 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 PRO A 30 17.27 -69.74
REMARK 500 1 ASP A 50 44.29 -109.70
REMARK 500 1 CYS A 101 161.00 -42.87
REMARK 500 2 PRO A 28 -179.26 -69.75
REMARK 500 2 PRO A 30 8.02 -69.82
REMARK 500 2 ASP A 50 44.24 -109.25
REMARK 500 2 TRP A 79 -35.99 -39.16
REMARK 500 3 SER A 3 107.98 -54.06
REMARK 500 3 SER A 5 149.15 -38.20
REMARK 500 3 PRO A 28 -178.46 -69.79
REMARK 500 3 PRO A 30 6.64 -69.77
REMARK 500 3 ASP A 50 42.31 -104.55
REMARK 500 3 TRP A 79 -39.05 -39.24
REMARK 500 3 CYS A 101 159.12 -49.07
REMARK 500 4 SER A 5 135.24 -171.39
REMARK 500 4 PRO A 28 -178.78 -69.76
REMARK 500 4 PRO A 30 8.46 -69.79
REMARK 500 4 ASP A 50 42.12 -104.26
REMARK 500 4 PRO A 77 2.85 -69.71
REMARK 500 4 PRO A 91 -164.33 -69.78
REMARK 500 4 CYS A 101 162.91 -44.00
REMARK 500 5 SER A 5 94.99 -44.36
REMARK 500 5 PRO A 30 15.03 -69.80
REMARK 500 5 ASP A 50 43.68 -107.16
REMARK 500 5 LYS A 71 -53.31 -120.75
REMARK 500 5 PRO A 77 0.55 -69.74
REMARK 500 5 PRO A 91 -175.80 -69.78
REMARK 500 5 CYS A 101 161.40 -48.56
REMARK 500 6 PRO A 30 14.73 -69.72
REMARK 500 6 ASP A 50 44.98 -109.94
REMARK 500 6 ASN A 70 44.71 35.98
REMARK 500 6 HIS A 99 105.03 -163.34
REMARK 500 7 PRO A 30 15.57 -69.76
REMARK 500 7 PHE A 89 101.57 -48.97
REMARK 500 7 CYS A 101 159.26 -44.59
REMARK 500 8 ASP A 15 33.59 71.82
REMARK 500 8 PRO A 30 17.03 -69.70
REMARK 500 8 ASP A 50 43.22 -107.73
REMARK 500 8 TYR A 52 -64.15 -91.50
REMARK 500 8 LYS A 87 43.78 37.82
REMARK 500 8 PRO A 91 -178.28 -69.82
REMARK 500 8 CYS A 101 160.61 -44.53
REMARK 500 9 SER A 2 147.80 -172.78
REMARK 500 9 ASN A 11 48.11 -102.11
REMARK 500 9 ASP A 15 31.89 72.70
REMARK 500 9 PRO A 30 18.16 -69.72
REMARK 500 9 ASP A 50 42.60 -103.94
REMARK 500 9 GLU A 59 91.72 -60.39
REMARK 500 9 MET A 100 -174.88 -52.87
REMARK 500 10 ASN A 11 37.87 -85.09
REMARK 500 10 PRO A 30 17.79 -69.79
REMARK 500 10 ASP A 50 38.70 -98.80
REMARK 500 10 PHE A 89 97.84 -66.43
REMARK 500 10 LYS A 105 -33.99 -33.85
REMARK 500 11 PRO A 30 17.32 -69.75
REMARK 500 11 ASP A 50 40.37 -101.90
REMARK 500 11 LYS A 87 41.49 39.85
REMARK 500 11 CYS A 101 160.87 -40.09
REMARK 500 12 PRO A 30 17.95 -69.73
REMARK 500 12 CYS A 101 161.16 -40.58
REMARK 500 13 PRO A 28 -167.38 -69.75
REMARK 500 13 PRO A 30 14.06 -69.78
REMARK 500 13 ASP A 50 42.85 -106.48
REMARK 500 13 PRO A 77 1.17 -69.72
REMARK 500 13 LYS A 87 43.10 34.68
REMARK 500 14 SER A 2 41.70 37.93
REMARK 500 14 PRO A 28 -169.95 -69.72
REMARK 500 14 PRO A 30 17.86 -69.78
REMARK 500 14 ASP A 50 40.77 -103.00
REMARK 500 14 PRO A 77 0.59 -69.76
REMARK 500 14 PHE A 89 98.55 -67.86
REMARK 500 14 CYS A 101 158.85 -40.58
REMARK 500 15 PRO A 30 14.01 -69.75
REMARK 500 15 ASN A 34 -70.80 -63.96
REMARK 500 15 ASP A 50 39.89 -99.65
REMARK 500 15 SER A 69 -29.55 -39.31
REMARK 500 15 HIS A 99 112.00 -160.98
REMARK 500 16 ASN A 11 42.12 -103.78
REMARK 500 16 PRO A 30 17.00 -69.78
REMARK 500 16 ASN A 65 -38.57 -39.31
REMARK 500 16 PHE A 89 96.17 -60.35
REMARK 500 16 LYS A 105 -36.77 -36.23
REMARK 500 17 PRO A 30 18.96 -69.76
REMARK 500 17 ASP A 50 42.26 -106.10
REMARK 500 17 CYS A 101 160.14 -48.65
REMARK 500 18 PRO A 30 13.52 -69.78
REMARK 500 18 THR A 51 129.31 -33.92
REMARK 500 18 ASP A 73 156.65 -40.36
REMARK 500 18 CYS A 101 161.12 -43.16
REMARK 500 19 PRO A 30 17.82 -69.75
REMARK 500 19 ASP A 50 46.85 -109.14
REMARK 500 19 PRO A 77 2.94 -69.78
REMARK 500 20 SER A 5 83.40 -68.45
REMARK 500 20 SER A 6 43.94 -89.24
REMARK 500 20 SER A 10 119.78 -164.91
REMARK 500 20 ASP A 15 34.52 70.95
REMARK 500 20 PRO A 30 12.43 -69.73
REMARK 500 20 ASP A 50 44.39 -105.96
REMARK 500 20 SER A 69 -36.19 -38.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002000250.1 RELATED DB: TARGETDB
DBREF 2E2W A 8 113 UNP P49917 DNL4_HUMAN 654 759
SEQADV 2E2W GLY A 1 UNP P49917 CLONING ARTIFACT
SEQADV 2E2W SER A 2 UNP P49917 CLONING ARTIFACT
SEQADV 2E2W SER A 3 UNP P49917 CLONING ARTIFACT
SEQADV 2E2W GLY A 4 UNP P49917 CLONING ARTIFACT
SEQADV 2E2W SER A 5 UNP P49917 CLONING ARTIFACT
SEQADV 2E2W SER A 6 UNP P49917 CLONING ARTIFACT
SEQADV 2E2W GLY A 7 UNP P49917 CLONING ARTIFACT
SEQRES 1 A 113 GLY SER SER GLY SER SER GLY LYS ILE SER ASN ILE PHE
SEQRES 2 A 113 GLU ASP VAL GLU PHE CYS VAL MET SER GLY THR ASP SER
SEQRES 3 A 113 GLN PRO LYS PRO ASP LEU GLU ASN ARG ILE ALA GLU PHE
SEQRES 4 A 113 GLY GLY TYR ILE VAL GLN ASN PRO GLY PRO ASP THR TYR
SEQRES 5 A 113 CYS VAL ILE ALA GLY SER GLU ASN ILE ARG VAL LYS ASN
SEQRES 6 A 113 ILE ILE LEU SER ASN LYS HIS ASP VAL VAL LYS PRO ALA
SEQRES 7 A 113 TRP LEU LEU GLU CYS PHE LYS THR LYS SER PHE VAL PRO
SEQRES 8 A 113 TRP GLN PRO ARG PHE MET ILE HIS MET CYS PRO SER THR
SEQRES 9 A 113 LYS GLU HIS PHE ALA ARG GLU TYR ASP
HELIX 1 1 PRO A 28 PHE A 39 1 12
HELIX 2 2 ASN A 60 ASN A 70 1 11
HELIX 3 3 LYS A 76 LYS A 87 1 12
HELIX 4 4 THR A 104 ASP A 113 1 10
SHEET 1 A 5 GLY A 41 VAL A 44 0
SHEET 2 A 5 VAL A 16 SER A 22 1 N VAL A 16 O TYR A 42
SHEET 3 A 5 VAL A 54 ALA A 56 1 O ILE A 55 N CYS A 19
SHEET 4 A 5 VAL A 74 VAL A 75 1 O VAL A 75 N ALA A 56
SHEET 5 A 5 MET A 97 HIS A 99 -1 O ILE A 98 N VAL A 74
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
