HEADER CELL CYCLE 29-MAR-07 2EP8
TITLE SOLUTION STRUCTURE OF THE BRCT DOMAIN FROM HUMAN PESCADILLO HOMOLOG 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PESCADILLO HOMOLOG 1;
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: PES1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P060821-06;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS A/B/A 3 LAYERS, NUCLEOLUS, RIBOSOME BIOGENESIS, DNA DAMAGE,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, CELL CYCLE
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 2EP8 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EP8 1 VERSN
REVDAT 1 02-OCT-07 2EP8 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE BRCT DOMAIN FROM HUMAN PESCADILLO
JRNL TITL 2 HOMOLOG 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 2EP8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000026937.
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 : 0.46MM 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 LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 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 HIS A 323 52.07 -102.73
REMARK 500 1 LEU A 330 129.72 -35.41
REMARK 500 1 ILE A 346 -72.42 -66.41
REMARK 500 1 THR A 385 -179.85 -63.10
REMARK 500 2 SER A 316 133.60 -170.31
REMARK 500 2 GLU A 341 -39.58 -36.84
REMARK 500 2 THR A 365 -70.51 -117.32
REMARK 500 2 THR A 385 175.81 -50.49
REMARK 500 2 ILE A 388 103.97 -51.21
REMARK 500 2 ARG A 405 42.64 34.42
REMARK 500 3 PHE A 327 41.86 -96.75
REMARK 500 3 GLU A 341 -39.57 -38.07
REMARK 500 3 ALA A 364 171.25 -46.66
REMARK 500 3 THR A 365 -69.81 -101.04
REMARK 500 3 GLN A 383 30.56 -89.19
REMARK 500 3 THR A 385 87.04 -58.33
REMARK 500 3 ARG A 405 37.52 36.56
REMARK 500 3 TYR A 413 49.66 -106.05
REMARK 500 4 PHE A 327 31.31 -87.49
REMARK 500 4 ILE A 346 -70.50 -57.74
REMARK 500 4 GLN A 383 -73.90 -52.93
REMARK 500 4 ILE A 388 104.44 -36.17
REMARK 500 4 ARG A 405 31.45 36.95
REMARK 500 4 LEU A 407 85.66 -66.67
REMARK 500 4 TYR A 413 33.34 -96.06
REMARK 500 5 SER A 316 42.07 -99.29
REMARK 500 5 PHE A 327 37.50 -95.18
REMARK 500 5 ALA A 364 152.11 -44.63
REMARK 500 5 THR A 385 -70.70 -97.36
REMARK 500 5 ILE A 388 99.41 -68.66
REMARK 500 6 PHE A 327 39.37 -91.50
REMARK 500 6 ILE A 346 -72.58 -63.64
REMARK 500 6 ALA A 364 158.32 -38.72
REMARK 500 6 ASP A 370 99.30 -65.70
REMARK 500 6 ILE A 373 120.79 -34.45
REMARK 500 6 PRO A 381 94.46 -69.81
REMARK 500 6 GLN A 383 76.75 -118.26
REMARK 500 6 GLN A 384 105.05 -171.49
REMARK 500 6 THR A 385 46.68 32.90
REMARK 500 6 ILE A 388 100.35 -50.00
REMARK 500 6 LEU A 407 93.94 -69.60
REMARK 500 7 SER A 319 113.31 -162.05
REMARK 500 7 PHE A 327 36.78 -98.00
REMARK 500 7 LEU A 330 125.94 -37.31
REMARK 500 7 THR A 365 -64.82 -108.76
REMARK 500 7 GLN A 384 163.65 -44.82
REMARK 500 7 ILE A 388 116.87 -38.08
REMARK 500 7 ARG A 405 44.24 38.11
REMARK 500 7 LEU A 408 156.45 -46.04
REMARK 500 7 TYR A 413 36.03 -95.30
REMARK 500
REMARK 500 THIS ENTRY HAS 148 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003833.2 RELATED DB: TARGETDB
DBREF 2EP8 A 322 414 UNP O00541 PESC_HUMAN 322 414
SEQADV 2EP8 GLY A 315 UNP O00541 EXPRESSION TAG
SEQADV 2EP8 SER A 316 UNP O00541 EXPRESSION TAG
SEQADV 2EP8 SER A 317 UNP O00541 EXPRESSION TAG
SEQADV 2EP8 GLY A 318 UNP O00541 EXPRESSION TAG
SEQADV 2EP8 SER A 319 UNP O00541 EXPRESSION TAG
SEQADV 2EP8 SER A 320 UNP O00541 EXPRESSION TAG
SEQADV 2EP8 GLY A 321 UNP O00541 EXPRESSION TAG
SEQRES 1 A 100 GLY SER SER GLY SER SER GLY LYS HIS LYS LYS LEU PHE
SEQRES 2 A 100 GLU GLY LEU LYS PHE PHE LEU ASN ARG GLU VAL PRO ARG
SEQRES 3 A 100 GLU ALA LEU ALA PHE ILE ILE ARG SER PHE GLY GLY GLU
SEQRES 4 A 100 VAL SER TRP ASP LYS SER LEU CYS ILE GLY ALA THR TYR
SEQRES 5 A 100 ASP VAL THR ASP SER ARG ILE THR HIS GLN ILE VAL ASP
SEQRES 6 A 100 ARG PRO GLY GLN GLN THR SER VAL ILE GLY ARG CYS TYR
SEQRES 7 A 100 VAL GLN PRO GLN TRP VAL PHE ASP SER VAL ASN ALA ARG
SEQRES 8 A 100 LEU LEU LEU PRO VAL ALA GLU TYR PHE
HELIX 1 1 PRO A 339 PHE A 350 1 12
HELIX 2 2 PRO A 395 ARG A 405 1 11
SHEET 1 A 2 LYS A 331 PHE A 333 0
SHEET 2 A 2 GLU A 353 SER A 355 1 O GLU A 353 N PHE A 332
SHEET 1 B 2 HIS A 375 ILE A 377 0
SHEET 2 B 2 CYS A 391 VAL A 393 1 O VAL A 393 N GLN A 376
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
