Header list of 1f4i.pdb file
Complete list - v 3 2 Bytes
HEADER DNA BINDING PROTEIN,TRANSCRIPTION 07-JUN-00 1F4I
TITLE SOLUTION STRUCTURE OF THE HHR23A UBA(2) MUTANT P333E, DEFICIENT IN
TITLE 2 BINDING THE HIV-1 ACCESSORY PROTEIN VPR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UV EXCISION REPAIR PROTEIN PROTEIN RAD23 HOMOLOG A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL UBA DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PEPTIDE NATURALLY OCCURS IN HUMANS (HOMO SAPIENS).
KEYWDS ALPHA HELICAL BUNDLE, DNA BINDING PROTEIN, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR E.S.WITHERS-WARD,T.D.MUELLER,I.S.CHEN,J.FEIGON
REVDAT 3 03-NOV-21 1F4I 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1F4I 1 VERSN
REVDAT 1 20-DEC-00 1F4I 0
JRNL AUTH E.S.WITHERS-WARD,T.D.MUELLER,I.S.CHEN,J.FEIGON
JRNL TITL BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE INTERACTION
JRNL TITL 2 BETWEEN THE UBA(2) DOMAIN OF THE DNA REPAIR PROTEIN HHR23A
JRNL TITL 3 AND HIV-1 VPR.
JRNL REF BIOCHEMISTRY V. 39 14103 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11087358
JRNL DOI 10.1021/BI0017071
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.DIECKMANN,E.S.WITHERS-WARD,M.A.JAROSINSKI,C.F.LIU,
REMARK 1 AUTH 2 I.S.Y.CHEN,J.FEIGON
REMARK 1 TITL STRUCTURE OF A HUMAN DNA REPAIR PROTEIN UBA DOMAIN THAT
REMARK 1 TITL 2 INTERACTS WITH HIV-1 VPR
REMARK 1 REF NAT.STRUCT.BIOL. V. 5 1042 1998
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/4220
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER, KARLSRUHE (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TOTAL NUMBER OF RESTRAINTS 826,
REMARK 3 204 INTRARESIDUAL,
REMARK 3 182 SEQUENTIAL,
REMARK 3 226 MEDIUM RANGE (|I-J|<5),
REMARK 3 214 LONG RANGE (|I-J|>=5)
REMARK 4
REMARK 4 1F4I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011232.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE, 150MM
REMARK 210 SODIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM UBA(2) DOMAIN MUTANT P333E;
REMARK 210 50MM PHOSPHATE BUFFER, 150MM
REMARK 210 SODIUM CHLORIDE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.10, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING, DISTANCE
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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 PHE A 14 -140.68 -109.15
REMARK 500 1 GLU A 16 -19.30 -48.10
REMARK 500 1 LYS A 28 58.56 37.86
REMARK 500 1 ASN A 29 -146.95 -106.85
REMARK 500 1 GLU A 30 -76.46 -135.23
REMARK 500 1 PHE A 42 110.46 -173.71
REMARK 500 1 ASP A 43 -149.65 -110.69
REMARK 500 2 PHE A 14 -144.82 -108.42
REMARK 500 2 LYS A 28 59.14 33.88
REMARK 500 2 ASN A 29 -143.12 -104.87
REMARK 500 2 GLU A 30 -75.59 -140.61
REMARK 500 2 GLN A 40 100.77 -57.95
REMARK 500 2 PHE A 42 123.18 -173.96
REMARK 500 2 ASP A 44 -89.46 174.05
REMARK 500 3 PHE A 14 -146.33 -107.56
REMARK 500 3 LYS A 28 60.38 29.21
REMARK 500 3 ASN A 29 -142.71 -104.66
REMARK 500 3 GLU A 30 -75.89 -140.50
REMARK 500 3 PHE A 42 81.86 177.50
REMARK 500 3 ASP A 43 -80.69 177.73
REMARK 500 3 ASP A 44 105.21 -172.12
REMARK 500 4 PHE A 14 -144.79 -106.61
REMARK 500 4 LYS A 28 60.36 31.76
REMARK 500 4 ASN A 29 -147.69 -106.05
REMARK 500 4 GLU A 30 -76.22 -134.28
REMARK 500 4 PHE A 42 51.24 -176.63
REMARK 500 4 ASP A 43 -74.97 -170.83
REMARK 500 4 ASP A 44 -73.35 -142.75
REMARK 500 5 GLU A 2 5.73 85.84
REMARK 500 5 PHE A 14 -146.19 -108.01
REMARK 500 5 LYS A 28 63.22 27.86
REMARK 500 5 ASN A 29 -148.17 -109.80
REMARK 500 5 GLU A 30 -71.01 -142.98
REMARK 500 5 ASP A 43 -148.86 55.06
REMARK 500 5 ASP A 44 59.43 34.09
REMARK 500 6 PHE A 14 -147.16 -108.23
REMARK 500 6 LYS A 28 60.69 32.00
REMARK 500 6 ASN A 29 -148.91 -105.53
REMARK 500 6 GLU A 30 -72.62 -141.88
REMARK 500 6 PHE A 42 111.52 -174.06
REMARK 500 6 ASP A 43 -44.49 -174.92
REMARK 500 7 PHE A 14 -147.37 -107.03
REMARK 500 7 LYS A 28 55.19 32.64
REMARK 500 7 ASN A 29 -142.03 -100.20
REMARK 500 7 GLU A 30 -78.56 -143.60
REMARK 500 7 GLN A 40 101.01 -43.29
REMARK 500 7 PHE A 42 139.86 179.50
REMARK 500 7 ASP A 43 79.92 49.15
REMARK 500 7 ASP A 44 32.79 -148.09
REMARK 500 8 PHE A 14 -145.17 -107.25
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: 1DV0 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF WILD TYPE HHR23A UBA(2) DOMAIN
DBREF 1F4I A 1 45 UNP P54725 RD23A_HUMAN 319 363
SEQADV 1F4I GLU A 15 UNP P54725 PRO 333 ENGINEERED MUTATION
SEQRES 1 A 45 GLN GLU LYS GLU ALA ILE GLU ARG LEU LYS ALA LEU GLY
SEQRES 2 A 45 PHE GLU GLU SER LEU VAL ILE GLN ALA TYR PHE ALA CYS
SEQRES 3 A 45 GLU LYS ASN GLU ASN LEU ALA ALA ASN PHE LEU LEU SER
SEQRES 4 A 45 GLN ASN PHE ASP ASP GLU
HELIX 1 1 GLU A 2 LEU A 12 1 11
HELIX 2 2 LEU A 18 ALA A 25 1 8
HELIX 3 3 LEU A 32 SER A 39 1 8
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
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