Header list of 1p98.pdb file
Complete list - b 23 2 Bytes
HEADER REPLICATION 09-MAY-03 1P98
TITLE HIGH-RESOLUTION NMR STRUCTURE OF THE UBL-DOMAIN OF HHR23A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBIQUITIN-LIKE 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 GENE: RAD23A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS UBIQUITIN-LIKE DOMAIN, REPLICATION
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR T.D.MUELLER,J.FEIGON
REVDAT 3 23-FEB-22 1P98 1 REMARK
REVDAT 2 24-FEB-09 1P98 1 VERSN
REVDAT 1 07-OCT-03 1P98 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 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.D.MUELLER,J.FEIGON
REMARK 1 TITL SOLUTION STRUCTURES OF UBA DOMAINS REVEAL A CONSERVED
REMARK 1 TITL 2 HYDROPHOBIC SURFACE FOR PROTEIN-PROTEIN INTERACTIONS
REMARK 1 REF J.MOL.BIOL. V. 319 1243 2002
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1016/S0022-2836(02)00302-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AURELIA 2.8.9, X-PLOR 3.1
REMARK 3 AUTHORS : NEIDIG, P. (AURELIA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P98 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_1000019166.
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 UBIQUITIN-LIKE DOMAIN OF
REMARK 210 HHR23A U-15N,13C; 2MM UBIQUITIN-
REMARK 210 LIKE DOMAIN OF HHR23A, UNLABELED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C-SEPARATED_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 : XWINNMR 2.5, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
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: 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 THR A 9 -127.57 -62.08
REMARK 500 1 LEU A 10 36.25 -91.36
REMARK 500 1 GLN A 11 -22.19 91.14
REMARK 500 1 ARG A 18 -76.09 -24.47
REMARK 500 1 MET A 19 -157.00 38.28
REMARK 500 1 VAL A 25 -32.96 78.50
REMARK 500 1 LYS A 36 -65.35 -100.54
REMARK 500 1 VAL A 43 -32.74 -38.74
REMARK 500 2 ALA A 2 -160.93 80.72
REMARK 500 2 VAL A 3 -159.42 -131.40
REMARK 500 2 LEU A 10 -29.72 86.31
REMARK 500 2 GLN A 12 -18.28 124.10
REMARK 500 2 PHE A 15 -163.34 -126.76
REMARK 500 2 ARG A 18 -82.34 -62.06
REMARK 500 2 MET A 19 -165.72 44.96
REMARK 500 2 VAL A 25 -27.04 77.65
REMARK 500 2 LYS A 36 -67.09 -97.45
REMARK 500 2 ARG A 65 56.50 34.70
REMARK 500 2 ASN A 70 -155.29 -110.62
REMARK 500 2 PHE A 71 139.17 -171.51
REMARK 500 3 VAL A 3 -161.67 -72.82
REMARK 500 3 LEU A 10 -30.67 76.85
REMARK 500 3 GLN A 11 -51.66 161.49
REMARK 500 3 ARG A 18 69.50 -101.18
REMARK 500 3 VAL A 25 -25.92 76.06
REMARK 500 3 LYS A 36 -64.79 -96.89
REMARK 500 3 ALA A 44 -74.35 -51.70
REMARK 500 3 ARG A 65 41.92 37.32
REMARK 500 4 ALA A 2 174.16 58.84
REMARK 500 4 THR A 9 -127.44 -62.18
REMARK 500 4 LEU A 10 35.73 -90.17
REMARK 500 4 GLN A 11 -18.77 88.53
REMARK 500 4 PHE A 15 -158.39 -158.43
REMARK 500 4 ARG A 18 -78.82 -28.30
REMARK 500 4 MET A 19 -160.56 41.16
REMARK 500 4 VAL A 25 -29.59 77.30
REMARK 500 4 LYS A 36 -65.08 -96.97
REMARK 500 4 VAL A 43 -33.27 -38.18
REMARK 500 4 THR A 77 128.17 70.02
REMARK 500 5 VAL A 3 -159.79 -82.05
REMARK 500 5 LEU A 10 -40.52 78.25
REMARK 500 5 GLN A 11 -47.90 168.49
REMARK 500 5 ARG A 18 69.06 -100.12
REMARK 500 5 VAL A 25 -27.74 76.96
REMARK 500 5 LYS A 36 -65.73 -96.89
REMARK 500 5 ARG A 65 46.23 38.10
REMARK 500 5 ASN A 70 -153.88 -108.21
REMARK 500 5 PHE A 71 141.35 -174.71
REMARK 500 6 ALA A 2 174.64 58.71
REMARK 500 6 LEU A 10 -32.35 86.88
REMARK 500
REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DV0 RELATED DB: PDB
REMARK 900 C-TERMINAL UBA DOMAIN OF HHR23A
REMARK 900 RELATED ID: 1IFY RELATED DB: PDB
REMARK 900 N-TERMINAL UBA DOMAIN OF HHR23A
REMARK 900 RELATED ID: 1F4I RELATED DB: PDB
REMARK 900 MUTANT OF C-TERMINAL UBA 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
REMARK 900 RELATED ID: 1P9D RELATED DB: PDB
REMARK 900 HIGH-RESOLUTION STRUCTURE OF THE COMPLEX OF HHR23A UBIQUITIN-LIKE
REMARK 900 DOMAIN AND THE C-TERMINAL UBIQUITIN-INTERACTING MOTIF OF PROTEASOME
REMARK 900 SUBUNIT S5A
DBREF 1P98 A 1 78 UNP P54725 RD23A_HUMAN 1 78
SEQRES 1 A 78 MET ALA VAL THR ILE THR LEU LYS THR LEU GLN GLN GLN
SEQRES 2 A 78 THR PHE LYS ILE ARG MET GLU PRO ASP GLU THR VAL LYS
SEQRES 3 A 78 VAL LEU LYS GLU LYS ILE GLU ALA GLU LYS GLY ARG ASP
SEQRES 4 A 78 ALA PHE PRO VAL ALA GLY GLN LYS LEU ILE TYR ALA GLY
SEQRES 5 A 78 LYS ILE LEU SER ASP ASP VAL PRO ILE ARG ASP TYR ARG
SEQRES 6 A 78 ILE ASP GLU LYS ASN PHE VAL VAL VAL MET VAL THR LYS
HELIX 1 1 VAL A 25 LYS A 36 1 12
HELIX 2 2 ILE A 61 ARG A 65 5 5
SHEET 1 A 5 THR A 14 ILE A 17 0
SHEET 2 A 5 ILE A 5 LYS A 8 -1 N LEU A 7 O PHE A 15
SHEET 3 A 5 VAL A 72 MET A 75 1 O VAL A 72 N LYS A 8
SHEET 4 A 5 LYS A 47 TYR A 50 -1 N ILE A 49 O VAL A 73
SHEET 5 A 5 LYS A 53 LEU A 55 -1 O LEU A 55 N LEU A 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