HEADER TRANSFERASE 09-FEB-07 2EBW
TITLE SOLUTION STRUCTURE OF THE BRCT DOMAIN FROM HUMAN DNA REPAIR PROTEIN
TITLE 2 REV1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA REPAIR PROTEIN REV1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BRCT DOMAIN;
COMPND 5 SYNONYM: REV1-LIKE TERMINAL DEOXYCYTIDYL TRANSFERASE, ALPHA INTEGRIN-
COMPND 6 BINDING PROTEIN 80, AIBP80;
COMPND 7 EC: 2.7.7.-;
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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P060821-10;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS A/B/A 3 LAYERS, PARALLEL BETA-SHEET, DNA REPLICATION, TRANSLESSION
KEYWDS 2 SYNTHESIS, TLS, DNA POLYMERASE ZETA, PCNA, STRUCTURAL GENOMICS,
KEYWDS 3 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 4 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 5 TRANSFERASE
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 2EBW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EBW 1 VERSN
REVDAT 1 14-AUG-07 2EBW 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE BRCT DOMAIN FROM HUMAN DNA REPAIR
JRNL TITL 2 PROTEIN REV1
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 2EBW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000026478.
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 : 0.76MM UNIFORMLY 13C/15N-LABELED
REMARK 210 PROTEIN, 20MM TRISHCL, 100MM
REMARK 210 NACL, 1MM DTT, 0.02% NAN3, 10%
REMARK 210 D2O, 90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 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 0.9822, 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 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 THR A 47 44.17 -106.02
REMARK 500 1 PRO A 62 -176.29 -69.75
REMARK 500 1 LEU A 70 -34.01 -34.74
REMARK 500 1 LYS A 86 -71.89 -66.91
REMARK 500 1 PRO A 111 1.99 -69.74
REMARK 500 1 LEU A 131 -74.77 -62.99
REMARK 500 2 PRO A 62 -178.38 -69.79
REMARK 500 2 LYS A 86 -71.05 -71.39
REMARK 500 2 LYS A 101 -70.10 -59.84
REMARK 500 2 GLU A 102 -27.25 -38.68
REMARK 500 2 LEU A 103 40.44 -102.75
REMARK 500 2 PRO A 111 0.04 -69.78
REMARK 500 2 PRO A 128 1.03 -69.81
REMARK 500 2 TYR A 132 38.85 37.10
REMARK 500 3 LEU A 70 -39.45 -37.17
REMARK 500 3 LYS A 86 -72.10 -60.94
REMARK 500 3 LEU A 103 32.81 -85.59
REMARK 500 3 GLU A 106 163.16 -41.47
REMARK 500 3 PRO A 128 0.41 -69.79
REMARK 500 4 THR A 47 49.42 -106.52
REMARK 500 4 LEU A 70 -32.91 -34.57
REMARK 500 4 LYS A 86 -74.10 -77.90
REMARK 500 4 LEU A 103 41.17 -98.16
REMARK 500 4 PRO A 111 3.09 -69.78
REMARK 500 4 PRO A 128 1.51 -69.76
REMARK 500 5 SER A 38 44.26 39.61
REMARK 500 5 SER A 39 101.83 -40.48
REMARK 500 5 THR A 47 49.55 -101.43
REMARK 500 5 LEU A 103 39.39 -86.04
REMARK 500 5 TYR A 132 44.36 37.59
REMARK 500 6 THR A 44 49.07 38.05
REMARK 500 6 PRO A 62 -179.79 -69.78
REMARK 500 6 LEU A 103 35.22 -96.41
REMARK 500 6 GLU A 106 -178.96 -51.44
REMARK 500 6 PRO A 111 0.00 -69.77
REMARK 500 6 PRO A 128 2.91 -69.80
REMARK 500 7 THR A 47 53.61 -101.38
REMARK 500 7 SER A 63 170.03 -52.27
REMARK 500 7 MET A 71 -70.79 -78.86
REMARK 500 7 TYR A 82 126.60 -38.20
REMARK 500 7 LYS A 86 -65.12 -97.67
REMARK 500 7 ASN A 97 -33.91 -38.79
REMARK 500 7 GLU A 106 172.49 -50.30
REMARK 500 7 TYR A 132 52.98 37.37
REMARK 500 8 THR A 47 27.74 43.30
REMARK 500 8 TYR A 82 125.30 -35.86
REMARK 500 8 LYS A 86 -73.93 -78.67
REMARK 500 8 GLU A 106 163.10 -49.10
REMARK 500 8 PRO A 111 2.94 -69.77
REMARK 500 8 LEU A 124 -75.14 -92.87
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO003006822.1 RELATED DB: TARGETDB
DBREF 2EBW A 44 133 UNP Q9UBZ9 REV1_HUMAN 44 133
SEQADV 2EBW GLY A 37 UNP Q9UBZ9 CLONING ARTIFACT
SEQADV 2EBW SER A 38 UNP Q9UBZ9 CLONING ARTIFACT
SEQADV 2EBW SER A 39 UNP Q9UBZ9 CLONING ARTIFACT
SEQADV 2EBW GLY A 40 UNP Q9UBZ9 CLONING ARTIFACT
SEQADV 2EBW SER A 41 UNP Q9UBZ9 CLONING ARTIFACT
SEQADV 2EBW SER A 42 UNP Q9UBZ9 CLONING ARTIFACT
SEQADV 2EBW GLY A 43 UNP Q9UBZ9 CLONING ARTIFACT
SEQRES 1 A 97 GLY SER SER GLY SER SER GLY THR SER SER THR ILE PHE
SEQRES 2 A 97 SER GLY VAL ALA ILE TYR VAL ASN GLY TYR THR ASP PRO
SEQRES 3 A 97 SER ALA GLU GLU LEU ARG LYS LEU MET MET LEU HIS GLY
SEQRES 4 A 97 GLY GLN TYR HIS VAL TYR TYR SER ARG SER LYS THR THR
SEQRES 5 A 97 HIS ILE ILE ALA THR ASN LEU PRO ASN ALA LYS ILE LYS
SEQRES 6 A 97 GLU LEU LYS GLY GLU LYS VAL ILE ARG PRO GLU TRP ILE
SEQRES 7 A 97 VAL GLU SER ILE LYS ALA GLY ARG LEU LEU SER TYR ILE
SEQRES 8 A 97 PRO TYR GLN LEU TYR THR
HELIX 1 1 SER A 63 HIS A 74 1 12
HELIX 2 2 ALA A 98 LEU A 103 1 6
HELIX 3 3 PRO A 111 GLY A 121 1 11
HELIX 4 4 TYR A 126 GLN A 130 5 5
SHEET 1 A 3 GLN A 77 TYR A 78 0
SHEET 2 A 3 ALA A 53 VAL A 56 1 N ILE A 54 O GLN A 77
SHEET 3 A 3 HIS A 89 ILE A 91 1 O HIS A 89 N ALA A 53
CISPEP 1 ASP A 61 PRO A 62 1 0.05
CISPEP 2 ASP A 61 PRO A 62 2 0.06
CISPEP 3 ASP A 61 PRO A 62 3 0.09
CISPEP 4 ASP A 61 PRO A 62 4 0.05
CISPEP 5 ASP A 61 PRO A 62 5 -0.01
CISPEP 6 ASP A 61 PRO A 62 6 0.06
CISPEP 7 ASP A 61 PRO A 62 7 0.09
CISPEP 8 ASP A 61 PRO A 62 8 0.04
CISPEP 9 ASP A 61 PRO A 62 9 -0.03
CISPEP 10 ASP A 61 PRO A 62 10 0.00
CISPEP 11 ASP A 61 PRO A 62 11 -0.06
CISPEP 12 ASP A 61 PRO A 62 12 -0.03
CISPEP 13 ASP A 61 PRO A 62 13 0.08
CISPEP 14 ASP A 61 PRO A 62 14 -0.02
CISPEP 15 ASP A 61 PRO A 62 15 -0.01
CISPEP 16 ASP A 61 PRO A 62 16 0.09
CISPEP 17 ASP A 61 PRO A 62 17 0.03
CISPEP 18 ASP A 61 PRO A 62 18 0.02
CISPEP 19 ASP A 61 PRO A 62 19 0.03
CISPEP 20 ASP A 61 PRO A 62 20 0.03
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