Header list of 1p9d.pdb file
Complete list - b 23 2 Bytes
HEADER REPLICATION 10-MAY-03 1P9D
TITLE HIGH-RESOLUTION STRUCTURE OF THE COMPLEX OF HHR23A UBIQUITIN-LIKE
TITLE 2 DOMAIN AND THE C-TERMINAL UBIQUITIN-INTERACTING MOTIF OF PROTEASOME
TITLE 3 SUBUNIT S5A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 4;
COMPND 3 CHAIN: S;
COMPND 4 FRAGMENT: C-TERMINAL UBIQUITIN-INTERACTING MOTIF, PUBS2;
COMPND 5 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT S5A, RPN10, MULTIUBIQUITIN
COMPND 6 CHAIN BINDING PROTEIN, ANTISECRETORY FACTOR-1, AF, ASF;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A;
COMPND 10 CHAIN: U;
COMPND 11 FRAGMENT: UBIQUITIN-LIKE DOMAIN;
COMPND 12 SYNONYM: HHR23A;
COMPND 13 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: PSMD4 OR MCB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: RAD23A;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-PEPTIDE COMPLEX, REPLICATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.D.MUELLER,J.FEIGON
REVDAT 3 23-FEB-22 1P9D 1 REMARK
REVDAT 2 24-FEB-09 1P9D 1 VERSN
REVDAT 1 07-OCT-03 1P9D 0
JRNL AUTH T.D.MUELLER,J.FEIGON
JRNL TITL STRUCTURAL DETERMINANTS FOR THE BINDING OF UBIQUITIN-LIKE
JRNL TITL 2 DOMAINS TO THE PROTEASOME.
JRNL REF EMBO J. V. 22 4634 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12970176
JRNL DOI 10.1093/EMBOJ/CDG467
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER KARLSRUHE (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2066 RESTRAINTS, 1999 ARE
REMARK 3 NOE-DERIVED DISTANCE RESTRAINTS, OF WHICH 58 ARE INTERMOLECULAR.
REMARK 3 FOR THE S5A UBIQUITIN-INTERACTING MOTIF ONLY THE RESIDUES 270 TO
REMARK 3 301 WERE INCLUDED IN THE STRUCTURE CALCULATIONS DUE TO DISORDER OF
REMARK 3 THE FLEXIBLE N- AND C-TERMINI.
REMARK 4
REMARK 4 1P9D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019171.
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 : 150MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM S5A PEPTIDE UNLABELED, 2MM
REMARK 210 UBIQUITIN-LIKE DOMAIN OF HHR23A
REMARK 210 U-15N,13C; 2MM S5A PEPTIDE U-15N,
REMARK 210 13C, 2MM UBIQUITIN-LIKE DOMAIN
REMARK 210 OF HHR23A UNLABELED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 15N-,13C
REMARK 210 -FILTERED/EDITED 2D-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.8.9, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, U
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET S 263
REMARK 465 THR S 264
REMARK 465 ILE S 265
REMARK 465 SER S 266
REMARK 465 GLN S 267
REMARK 465 GLN S 268
REMARK 465 GLU S 269
REMARK 465 GLN S 302
REMARK 465 ALA S 303
REMARK 465 GLU S 304
REMARK 465 SER S 305
REMARK 465 ALA S 306
REMARK 465 ASP S 307
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
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 THR S 273 45.55 -84.98
REMARK 500 1 PRO S 276 -77.48 -80.89
REMARK 500 1 ASP S 277 -15.32 84.14
REMARK 500 1 SER S 280 29.84 90.68
REMARK 500 1 THR S 282 -70.82 14.02
REMARK 500 1 LEU S 295 34.61 -87.28
REMARK 500 1 GLN S 296 -31.69 -34.62
REMARK 500 1 ALA S 298 35.41 -155.18
REMARK 500 1 GLU S 299 36.78 -161.51
REMARK 500 1 PHE S 300 64.21 38.07
REMARK 500 1 LEU U 10 -46.37 -5.85
REMARK 500 1 GLN U 11 -5.52 -54.98
REMARK 500 1 GLN U 12 -4.29 96.12
REMARK 500 1 ARG U 18 65.28 -109.61
REMARK 500 1 GLU U 23 174.67 -49.46
REMARK 500 1 VAL U 25 -6.34 58.17
REMARK 500 1 PHE U 41 36.71 -150.21
REMARK 500 1 VAL U 43 -37.75 -28.72
REMARK 500 1 ASP U 57 -16.59 -47.78
REMARK 500 1 ARG U 65 62.15 29.58
REMARK 500 2 ASP S 277 86.52 22.36
REMARK 500 2 SER S 279 35.34 104.78
REMARK 500 2 SER S 280 10.91 88.99
REMARK 500 2 THR S 282 -126.92 29.79
REMARK 500 2 GLU S 283 -68.51 -29.47
REMARK 500 2 PHE S 300 -76.52 77.75
REMARK 500 2 THR U 9 48.22 -85.73
REMARK 500 2 LEU U 10 -30.73 73.09
REMARK 500 2 GLN U 12 -9.27 95.45
REMARK 500 2 GLN U 13 99.75 -56.55
REMARK 500 2 PHE U 15 -165.34 -104.25
REMARK 500 2 ARG U 18 67.79 -110.17
REMARK 500 2 GLU U 23 -176.68 -49.56
REMARK 500 2 VAL U 25 -0.86 52.35
REMARK 500 2 PHE U 41 42.47 -150.75
REMARK 500 2 VAL U 43 -38.03 -28.82
REMARK 500 2 ALA U 44 -73.60 -60.12
REMARK 500 2 ARG U 65 57.15 32.76
REMARK 500 3 PRO S 276 -95.73 -75.69
REMARK 500 3 ASP S 277 -93.37 -125.66
REMARK 500 3 LEU S 278 -26.31 82.98
REMARK 500 3 SER S 279 47.87 -89.34
REMARK 500 3 SER S 280 -28.47 163.02
REMARK 500 3 MET S 281 -62.61 -5.49
REMARK 500 3 THR S 282 -165.59 77.11
REMARK 500 3 LEU S 295 37.50 -81.22
REMARK 500 3 GLN S 296 -30.64 -34.82
REMARK 500 3 ALA S 298 -63.06 87.60
REMARK 500 3 GLU S 299 -92.90 -127.75
REMARK 500 3 ILE U 5 171.34 -50.19
REMARK 500
REMARK 500 THIS ENTRY HAS 206 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P98 RELATED DB: PDB
REMARK 900 HIGH-RESOLUTION STRUCTURE OF THE UBIQUITIN-LIKE DOMAIN OF HHR23A
REMARK 900 RELATED ID: 1P9C RELATED DB: PDB
REMARK 900 STRUCTURE OF THE C-TERMINAL UBIQUITIN-INTERACTING MOTIF OF THE
REMARK 900 PROEASOME SUBUNIT S5A IN ITS UNBOUND CONFORMATION
DBREF 1P9D U 1 78 UNP P54725 RD23A_HUMAN 1 78
DBREF 1P9D S 263 307 UNP P55036 PSD4_HUMAN 263 307
SEQRES 1 S 45 MET THR ILE SER GLN GLN GLU PHE GLY ARG THR GLY LEU
SEQRES 2 S 45 PRO ASP LEU SER SER MET THR GLU GLU GLU GLN ILE ALA
SEQRES 3 S 45 TYR ALA MET GLN MET SER LEU GLN GLY ALA GLU PHE GLY
SEQRES 4 S 45 GLN ALA GLU SER ALA ASP
SEQRES 1 U 78 MET ALA VAL THR ILE THR LEU LYS THR LEU GLN GLN GLN
SEQRES 2 U 78 THR PHE LYS ILE ARG MET GLU PRO ASP GLU THR VAL LYS
SEQRES 3 U 78 VAL LEU LYS GLU LYS ILE GLU ALA GLU LYS GLY ARG ASP
SEQRES 4 U 78 ALA PHE PRO VAL ALA GLY GLN LYS LEU ILE TYR ALA GLY
SEQRES 5 U 78 LYS ILE LEU SER ASP ASP VAL PRO ILE ARG ASP TYR ARG
SEQRES 6 U 78 ILE ASP GLU LYS ASN PHE VAL VAL VAL MET VAL THR LYS
HELIX 1 1 PRO S 276 SER S 280 5 5
HELIX 2 2 MET S 281 LEU S 295 1 15
HELIX 3 3 VAL U 25 GLY U 37 1 13
HELIX 4 4 PRO U 60 ARG U 65 5 6
SHEET 1 A 5 GLN U 13 ILE U 17 0
SHEET 2 A 5 ILE U 5 THR U 9 -1 N THR U 9 O GLN U 13
SHEET 3 A 5 VAL U 72 MET U 75 1 O VAL U 74 N LYS U 8
SHEET 4 A 5 LYS U 47 TYR U 50 -1 N LYS U 47 O MET U 75
SHEET 5 A 5 LYS U 53 SER U 56 -1 O LEU U 55 N LEU U 48
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 - b 23 2 Bytes