Header list of 2d8u.pdb file
Complete list - r 9 2 Bytes
HEADER LIGASE 08-DEC-05 2D8U
TITLE SOLUTION STRUCTURE OF THE B-BOX DOMAIN OF THE HUMAN TRIPARTITE MOTIF-
TITLE 2 CONTAINING 63 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN LIGASE TRIM63;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-B BOX;
COMPND 5 SYNONYM: TRIPARTITE MOTIF-CONTAINING 63, MUSCLE-SPECIFIC RING FINGER
COMPND 6 PROTEIN 1, MURF1, MURF-1, RING FINGER PROTEIN 28, STRIATED MUSCLE
COMPND 7 RING ZINC FINGER PROTEIN, IRIS RING FINGER PROTEIN;
COMPND 8 EC: 6.3.2.-;
COMPND 9 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: TRIM63;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050302-45;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS TRIPARTITE MOTIF-CONTAINING 63, TRIM63, MUSCLE-SPECIFIC RING FINGER
KEYWDS 2 PROTEIN 1, MURF1, RING FINGER PROTEIN 28, STRIATED MUSCLE RING ZINC
KEYWDS 3 FINGER PROTEIN, IRIS RING FINGER PROTEIN, ZF-B_BOX, STRUCTURAL
KEYWDS 4 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 5 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 6 INITIATIVE, RSGI, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.MIYAMOTO,T.KIGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D8U 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2D8U 1 VERSN
REVDAT 1 08-JUN-06 2D8U 0
JRNL AUTH K.MIYAMOTO,T.KIGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE B-BOX DOMAIN OF THE HUMAN
JRNL TITL 2 TRIPARTITE MOTIF-CONTAINING 63 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D8U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025131.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.09MM ZF-B_BOX U-13C, 15N; 20MM
REMARK 210 D-TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 0.05MM
REMARK 210 ZNCL2; 1.0MM IDA; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9321, 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 : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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 SER A 2 -48.18 -131.05
REMARK 500 1 LEU A 24 -61.03 -108.26
REMARK 500 1 THR A 25 -70.02 -33.05
REMARK 500 1 GLU A 27 53.48 70.77
REMARK 500 1 PRO A 29 88.54 -69.73
REMARK 500 1 CYS A 31 -176.63 -68.62
REMARK 500 1 CYS A 43 -178.03 -65.59
REMARK 500 1 PRO A 47 89.78 -69.76
REMARK 500 1 LEU A 48 -32.95 -36.56
REMARK 500 1 GLN A 53 150.67 -44.79
REMARK 500 2 GLU A 17 92.21 -60.00
REMARK 500 2 LEU A 24 -61.43 -104.71
REMARK 500 2 PRO A 29 95.69 -69.78
REMARK 500 2 CYS A 31 171.42 -57.04
REMARK 500 2 ALA A 42 34.28 -82.31
REMARK 500 2 PRO A 47 85.24 -69.74
REMARK 500 2 PHE A 52 105.12 -169.93
REMARK 500 2 GLN A 53 42.55 36.59
REMARK 500 3 LEU A 24 -62.79 -104.05
REMARK 500 3 THR A 25 -73.86 -32.62
REMARK 500 3 HIS A 40 69.94 -69.33
REMARK 500 3 ALA A 42 34.20 -82.91
REMARK 500 3 GLN A 49 -72.91 -32.60
REMARK 500 3 VAL A 51 53.28 33.02
REMARK 500 3 GLN A 55 45.39 35.50
REMARK 500 3 GLU A 58 112.35 -37.22
REMARK 500 3 SER A 59 42.42 -80.84
REMARK 500 3 PRO A 61 86.90 -69.78
REMARK 500 4 LEU A 24 -64.17 -97.32
REMARK 500 4 THR A 25 -72.39 -29.90
REMARK 500 4 PRO A 29 91.74 -69.74
REMARK 500 4 HIS A 40 69.38 -69.35
REMARK 500 4 ALA A 42 32.00 -83.17
REMARK 500 4 PRO A 47 91.00 -69.78
REMARK 500 4 LEU A 48 -39.81 -39.33
REMARK 500 4 GLN A 53 126.80 -39.06
REMARK 500 4 GLN A 55 148.87 -39.57
REMARK 500 4 THR A 57 43.80 -108.93
REMARK 500 5 PRO A 29 83.89 -69.76
REMARK 500 5 CYS A 31 -174.88 -52.70
REMARK 500 5 PHE A 37 -58.61 -125.98
REMARK 500 5 HIS A 40 45.13 -74.91
REMARK 500 5 CYS A 43 -177.88 -65.04
REMARK 500 5 PRO A 47 95.06 -69.76
REMARK 500 5 LEU A 48 -36.73 -31.96
REMARK 500 5 GLN A 49 88.71 -68.11
REMARK 500 5 VAL A 51 98.89 -57.90
REMARK 500 5 GLN A 55 41.35 36.62
REMARK 500 5 LYS A 56 106.22 -170.76
REMARK 500 6 SER A 2 45.61 -79.46
REMARK 500
REMARK 500 THIS ENTRY HAS 196 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 HIS A 14 ND1 115.2
REMARK 620 3 CYS A 31 SG 119.8 109.4
REMARK 620 4 CYS A 34 SG 107.4 102.7 99.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 23 SG
REMARK 620 2 CYS A 26 SG 87.8
REMARK 620 3 HIS A 40 ND1 119.7 118.6
REMARK 620 4 CYS A 43 SG 98.7 120.0 109.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002010152.1 RELATED DB: TARGETDB
DBREF 2D8U A 8 58 UNP Q969Q1 TRI63_HUMAN 119 169
SEQADV 2D8U GLY A 1 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U SER A 2 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U SER A 3 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U GLY A 4 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U SER A 5 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U SER A 6 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U GLY A 7 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U SER A 59 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U GLY A 60 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U PRO A 61 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U SER A 62 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U SER A 63 UNP Q969Q1 CLONING ARTIFACT
SEQADV 2D8U GLY A 64 UNP Q969Q1 CLONING ARTIFACT
SEQRES 1 A 64 GLY SER SER GLY SER SER GLY HIS PRO MET CYS LYS GLU
SEQRES 2 A 64 HIS GLU ASP GLU LYS ILE ASN ILE TYR CYS LEU THR CYS
SEQRES 3 A 64 GLU VAL PRO THR CYS SER MET CYS LYS VAL PHE GLY ILE
SEQRES 4 A 64 HIS LYS ALA CYS GLU VAL ALA PRO LEU GLN SER VAL PHE
SEQRES 5 A 64 GLN GLY GLN LYS THR GLU SER GLY PRO SER SER GLY
HET ZN A 201 1
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 SER A 32 PHE A 37 1 6
SHEET 1 A 2 TYR A 22 CYS A 23 0
SHEET 2 A 2 VAL A 45 ALA A 46 -1 O ALA A 46 N TYR A 22
LINK SG CYS A 11 ZN ZN A 201 1555 1555 2.32
LINK ND1 HIS A 14 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 23 ZN ZN A 401 1555 1555 2.31
LINK SG CYS A 26 ZN ZN A 401 1555 1555 2.27
LINK SG CYS A 31 ZN ZN A 201 1555 1555 2.32
LINK SG CYS A 34 ZN ZN A 201 1555 1555 2.32
LINK ND1 HIS A 40 ZN ZN A 401 1555 1555 2.33
LINK SG CYS A 43 ZN ZN A 401 1555 1555 2.40
SITE 1 AC1 5 CYS A 11 HIS A 14 GLU A 17 CYS A 31
SITE 2 AC1 5 CYS A 34
SITE 1 AC2 4 CYS A 23 CYS A 26 HIS A 40 CYS A 43
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 - r 9 2 Bytes