HEADER REPLICATION 09-FEB-07 2EBU
TITLE SOLUTION STRUCTURE OF THE BRCT DOMAIN FROM HUMAN REPLICATION FACTOR C
TITLE 2 LARGE SUBUNIT 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REPLICATION FACTOR C SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BRCT DOMAIN;
COMPND 5 SYNONYM: REPLICATION FACTOR C LARGE SUBUNIT, RF-C 140 KDA SUBUNIT,
COMPND 6 ACTIVATOR 1 140 KDA SUBUNIT, ACTIVATOR 1 LARGE SUBUNIT, A1 140 KDA
COMPND 7 SUBUNIT, DNA-BINDING PROTEIN PO-GA;
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: P060403-02;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS A/B/A 3 LAYERS, PARALLEL BETA-SHEET, DNA REPLICATION, CLAMP LOADER,
KEYWDS 2 RFC1, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, REPLICATION
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 2EBU 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EBU 1 VERSN
REVDAT 1 14-AUG-07 2EBU 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE BRCT DOMAIN FROM HUMAN REPLICATION
JRNL TITL 2 FACTOR C LARGE SUBUNIT 1
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 2EBU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000026476.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.17MM 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 : 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 0.9822, 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 SER A 386 110.63 -166.74
REMARK 500 1 ALA A 393 47.00 36.87
REMARK 500 1 ARG A 423 -37.88 -39.84
REMARK 500 1 ASP A 453 38.00 34.54
REMARK 500 1 PRO A 483 -178.42 -69.81
REMARK 500 1 ALA A 492 -178.39 -61.51
REMARK 500 1 VAL A 493 39.70 34.17
REMARK 500 2 SER A 390 42.93 -86.08
REMARK 500 2 GLU A 419 -69.58 -94.73
REMARK 500 2 ASP A 453 39.01 34.75
REMARK 500 2 PRO A 483 -165.18 -69.74
REMARK 500 2 LYS A 488 43.50 -91.45
REMARK 500 3 SER A 420 -31.60 -39.74
REMARK 500 3 ASP A 424 -65.86 -92.56
REMARK 500 3 ASP A 453 39.04 34.56
REMARK 500 3 PRO A 483 -173.26 -69.71
REMARK 500 3 LYS A 486 47.59 33.15
REMARK 500 3 ALA A 492 48.04 34.43
REMARK 500 4 SER A 396 28.20 48.29
REMARK 500 4 ASP A 453 38.80 34.41
REMARK 500 4 GLN A 456 30.80 36.16
REMARK 500 4 GLU A 472 -32.79 -35.31
REMARK 500 4 PRO A 483 -166.39 -69.74
REMARK 500 4 SER A 487 142.38 -173.88
REMARK 500 4 ALA A 492 153.75 -45.54
REMARK 500 5 SER A 389 -49.81 -130.42
REMARK 500 5 ARG A 423 -31.75 -38.14
REMARK 500 5 ASN A 440 124.96 -170.96
REMARK 500 5 ASP A 453 36.34 34.08
REMARK 500 5 PRO A 483 -165.86 -69.76
REMARK 500 5 GLU A 490 139.71 -37.93
REMARK 500 6 ALA A 393 50.97 -114.72
REMARK 500 6 ASP A 453 36.95 34.42
REMARK 500 6 PRO A 483 -170.31 -69.84
REMARK 500 6 THR A 495 158.52 -48.37
REMARK 500 7 GLU A 419 -67.07 -102.74
REMARK 500 7 ASP A 453 44.89 36.39
REMARK 500 7 PRO A 483 -163.82 -69.74
REMARK 500 8 ASP A 453 53.46 35.68
REMARK 500 8 GLU A 472 -25.83 -39.80
REMARK 500 8 PRO A 483 -164.49 -69.80
REMARK 500 8 GLU A 494 167.23 -49.52
REMARK 500 9 SER A 387 118.20 -166.02
REMARK 500 9 SER A 389 43.50 35.41
REMARK 500 9 LYS A 392 44.21 34.62
REMARK 500 9 ASP A 453 48.17 34.37
REMARK 500 9 PRO A 483 -164.89 -69.73
REMARK 500 10 SER A 420 -39.25 -37.67
REMARK 500 10 ARG A 423 -35.23 -38.36
REMARK 500 10 ASP A 453 40.07 34.56
REMARK 500
REMARK 500 THIS ENTRY HAS 87 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003000047.2 RELATED DB: TARGETDB
DBREF 2EBU A 392 496 UNP P35251 RFC1_HUMAN 392 496
SEQADV 2EBU GLY A 385 UNP P35251 CLONING ARTIFACT
SEQADV 2EBU SER A 386 UNP P35251 CLONING ARTIFACT
SEQADV 2EBU SER A 387 UNP P35251 CLONING ARTIFACT
SEQADV 2EBU GLY A 388 UNP P35251 CLONING ARTIFACT
SEQADV 2EBU SER A 389 UNP P35251 CLONING ARTIFACT
SEQADV 2EBU SER A 390 UNP P35251 CLONING ARTIFACT
SEQADV 2EBU GLY A 391 UNP P35251 CLONING ARTIFACT
SEQRES 1 A 112 GLY SER SER GLY SER SER GLY LYS ALA LEU GLY SER LYS
SEQRES 2 A 112 GLU ILE PRO LYS GLY ALA GLU ASN CYS LEU GLU GLY LEU
SEQRES 3 A 112 ILE PHE VAL ILE THR GLY VAL LEU GLU SER ILE GLU ARG
SEQRES 4 A 112 ASP GLU ALA LYS SER LEU ILE GLU ARG TYR GLY GLY LYS
SEQRES 5 A 112 VAL THR GLY ASN VAL SER LYS LYS THR ASN TYR LEU VAL
SEQRES 6 A 112 MET GLY ARG ASP SER GLY GLN SER LYS SER ASP LYS ALA
SEQRES 7 A 112 ALA ALA LEU GLY THR LYS ILE ILE ASP GLU ASP GLY LEU
SEQRES 8 A 112 LEU ASN LEU ILE ARG THR MET PRO GLY LYS LYS SER LYS
SEQRES 9 A 112 TYR GLU ILE ALA VAL GLU THR GLU
HELIX 1 1 GLU A 422 TYR A 433 1 12
HELIX 2 2 GLN A 456 GLY A 466 1 11
HELIX 3 3 GLU A 472 MET A 482 1 11
SHEET 1 A 4 LYS A 436 VAL A 437 0
SHEET 2 A 4 ILE A 411 ILE A 414 1 N PHE A 412 O LYS A 436
SHEET 3 A 4 TYR A 447 MET A 450 1 O TYR A 447 N ILE A 411
SHEET 4 A 4 LYS A 468 ASP A 471 1 O ILE A 470 N MET A 450
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
