Header list of 1ify.pdb file
Complete list - 23 20 Bytes
HEADER DNA BINDING PROTEIN 13-APR-01 1IFY
TITLE SOLUTION STRUCTURE OF THE INTERNAL UBA DOMAIN OF HHR23A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: INTERNAL UBA DOMAIN;
COMPND 5 SYNONYM: HHR23A;
COMPND 6 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX2T
KEYWDS UBIQUITIN ASSOCIATED DOMAIN, UBA DOMAIN, UBIQUITIN PROTEOSOME
KEYWDS 2 PATHWAY, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.D.MUELLER,J.FEIGON
REVDAT 3 23-FEB-22 1IFY 1 REMARK
REVDAT 2 24-FEB-09 1IFY 1 VERSN
REVDAT 1 03-JUL-02 1IFY 0
JRNL AUTH T.D.MUELLER,J.FEIGON
JRNL TITL SOLUTION STRUCTURES OF UBA DOMAINS REVEAL A CONSERVED
JRNL TITL 2 HYDROPHOBIC SURFACE FOR PROTEIN-PROTEIN INTERACTIONS.
JRNL REF J.MOL.BIOL. V. 319 1243 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12079361
JRNL DOI 10.1016/S0022-2836(02)00302-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.S.WITHERS-WARD,T.D.MUELLER,I.S.CHEN,J.FEIGON
REMARK 1 TITL BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE INTERACTION
REMARK 1 TITL 2 BETWEEN THE UBA(2) DOMAIN OF THE DNA REPAIR PROTEIN HHR23A
REMARK 1 TITL 3 AND HIV-1 VPR
REMARK 1 REF BIOCHEMISTRY V. 39 14103 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI0017071
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 AG (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 1692 NOE-DERIVED DISTANCE RESTRAINTS,
REMARK 3 OF WHICH
REMARK 3 1055 DISTANCE RESTRAINTS ARE NON-REDUNDANT. 407 RESTRAINTS ARE
REMARK 3 INTRARESIDUE,
REMARK 3 212 ARE SEQUENTIAL, 226 ARE MEDIUMRANGE (I-J < 5) AND 210 ARE
REMARK 3 LONG-RANGE (I-J > 4)
REMARK 4
REMARK 4 1IFY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013237.
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, 100MM
REMARK 210 SODIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM UBA1 U-15N,13C; 2MM UBA1 U
REMARK 210 -15N; 2MM UBA1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, AURELIA 2.8.9, X
REMARK 210 -PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HG SER A 187 O ASN A 190 1.44
REMARK 500
REMARK 500 REMARK: NULL
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 161 -79.03 -36.15
REMARK 500 1 SER A 172 -30.26 -37.62
REMARK 500 1 MET A 173 35.49 -79.01
REMARK 500 1 GLU A 176 151.03 -39.41
REMARK 500 1 TYR A 188 13.18 86.25
REMARK 500 1 ASN A 189 -6.84 102.69
REMARK 500 1 PRO A 191 -60.67 -90.99
REMARK 500 1 LEU A 199 -81.13 -76.56
REMARK 500 1 THR A 200 -33.48 -32.03
REMARK 500 1 ILE A 202 106.42 -54.26
REMARK 500 2 LEU A 157 71.33 61.17
REMARK 500 2 VAL A 158 -153.82 -135.53
REMARK 500 2 THR A 159 -87.11 -80.85
REMARK 500 2 GLU A 169 -70.51 -66.71
REMARK 500 2 SER A 172 -29.98 -37.61
REMARK 500 2 MET A 173 38.12 -79.96
REMARK 500 2 GLU A 176 154.68 -36.92
REMARK 500 2 ASN A 189 -20.52 69.29
REMARK 500 2 PRO A 191 -63.44 -95.65
REMARK 500 2 LEU A 199 -83.50 -78.88
REMARK 500 3 VAL A 158 46.99 -84.47
REMARK 500 3 THR A 159 -72.73 79.81
REMARK 500 3 SER A 161 -71.71 -73.25
REMARK 500 3 GLU A 169 -71.64 -72.07
REMARK 500 3 SER A 172 -33.02 -33.51
REMARK 500 3 MET A 173 39.08 -84.38
REMARK 500 3 GLU A 176 156.26 -34.14
REMARK 500 3 TYR A 188 47.51 78.78
REMARK 500 3 ASN A 189 -28.43 75.40
REMARK 500 3 PRO A 191 -65.32 -97.27
REMARK 500 3 LEU A 199 -84.06 -78.61
REMARK 500 4 VAL A 158 101.70 -163.27
REMARK 500 4 GLU A 169 -70.60 -71.94
REMARK 500 4 SER A 172 -32.87 -33.49
REMARK 500 4 MET A 173 39.07 -84.56
REMARK 500 4 GLU A 176 155.57 -35.16
REMARK 500 4 TYR A 188 53.79 73.30
REMARK 500 4 ASN A 189 -16.40 66.92
REMARK 500 4 PRO A 191 -66.92 -96.39
REMARK 500 4 LEU A 199 -80.65 -76.22
REMARK 500 4 THR A 200 -32.59 -33.21
REMARK 500 4 ILE A 202 96.41 -36.09
REMARK 500 5 LEU A 157 118.72 -173.64
REMARK 500 5 VAL A 158 90.87 -34.83
REMARK 500 5 THR A 159 -76.77 -35.48
REMARK 500 5 SER A 161 -87.42 -68.11
REMARK 500 5 GLU A 169 -71.48 -70.12
REMARK 500 5 SER A 172 -29.73 -37.37
REMARK 500 5 MET A 173 38.10 -79.49
REMARK 500 5 GLU A 176 155.41 -36.82
REMARK 500
REMARK 500 THIS ENTRY HAS 106 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DV0 RELATED DB: PDB
REMARK 900 1DV0 IS THE C-TERMINAL UBA DOMAIN OF HHR23A
REMARK 900 RELATED ID: 1F4I RELATED DB: PDB
REMARK 900 1F4I IS THE P333E MUTANT OF C-TERMINAL UBA DOMAIN OF HHR23A
DBREF 1IFY A 156 204 UNP P54725 RD23A_HUMAN 156 204
SEQRES 1 A 49 THR LEU VAL THR GLY SER GLU TYR GLU THR MET LEU THR
SEQRES 2 A 49 GLU ILE MET SER MET GLY TYR GLU ARG GLU ARG VAL VAL
SEQRES 3 A 49 ALA ALA LEU ARG ALA SER TYR ASN ASN PRO HIS ARG ALA
SEQRES 4 A 49 VAL GLU TYR LEU LEU THR GLY ILE PRO GLY
HELIX 1 1 GLY A 160 MET A 173 1 14
HELIX 2 2 GLU A 176 ALA A 186 1 11
HELIX 3 3 PRO A 191 GLY A 201 1 11
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
Complete list - 23 20 Bytes