Header list of 1d8j.pdb file
Complete list - b 16 2 Bytes
HEADER GENE REGULATION 25-OCT-99 1D8J
TITLE SOLUTION STRUCTURE OF THE CENTRAL CORE DOMAIN OF TFIIE BETA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENERAL TRANSCRIPTION FACTOR TFIIE-BETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CENTRAL CORE DOMAIN;
COMPND 5 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_PLASMID: PET3A
KEYWDS WINGED HELIX-TURN-HELIX, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 2 INITIATIVE, RSGI, STRUCTURAL GENOMICS, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.OKUDA,Y.WATANABE,H.OKAMURA,F.HANAOKA,Y.OHKUMA,Y.NISHIMURA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 16-FEB-22 1D8J 1 REMARK
REVDAT 2 24-FEB-09 1D8J 1 VERSN
REVDAT 1 26-APR-00 1D8J 0
JRNL AUTH M.OKUDA,Y.WATANABE,H.OKAMURA,F.HANAOKA,Y.OHKUMA,Y.NISHIMURA
JRNL TITL STRUCTURE OF THE CENTRAL CORE DOMAIN OF TFIIEBETA WITH A
JRNL TITL 2 NOVEL DOUBLE-STRANDED DNA-BINDING SURFACE.
JRNL REF EMBO J. V. 19 1346 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10716934
JRNL DOI 10.1093/EMBOJ/19.6.1346
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.6, EMBOSS 5
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER, BAX
REMARK 3 (NMRPIPE), NAKAI, KIDERA, NAKAMURA (EMBOSS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1224 RESTRAINTS, 1184 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 38
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 40 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1D8J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009887.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 500MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-2MM PROTEIN U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER, 500MM NACL; 1-
REMARK 210 2MM PROTEIN ; 20MM PHOSPHATE
REMARK 210 BUFFER, 500MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP, CAPP, STAPP 3.9, EMBOSS 5
REMARK 210 METHOD USED : 4D SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
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: 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 LYS A 9 -59.90 74.93
REMARK 500 1 ILE A 46 -105.72 26.28
REMARK 500 1 GLU A 57 -67.39 -165.45
REMARK 500 1 LEU A 59 27.93 -79.71
REMARK 500 1 VAL A 60 -38.80 -134.88
REMARK 500 1 ILE A 68 -98.66 -115.96
REMARK 500 1 TYR A 78 49.22 36.15
REMARK 500 1 ASN A 79 -49.69 -164.60
REMARK 500 2 LEU A 2 -64.79 -155.68
REMARK 500 2 SER A 5 -173.10 61.26
REMARK 500 2 LYS A 9 -47.36 82.62
REMARK 500 2 ASP A 28 46.38 -82.06
REMARK 500 2 GLN A 42 72.71 -26.47
REMARK 500 2 HIS A 43 58.12 -178.58
REMARK 500 2 ASP A 45 -45.06 -162.21
REMARK 500 2 ILE A 46 -89.57 40.88
REMARK 500 2 GLU A 57 -54.21 -138.84
REMARK 500 2 LYS A 77 -72.25 71.60
REMARK 500 2 TYR A 78 46.28 -146.02
REMARK 500 3 LYS A 9 -47.87 -166.34
REMARK 500 3 ARG A 26 -51.71 -163.87
REMARK 500 3 LEU A 44 -52.59 166.26
REMARK 500 3 GLU A 57 -68.89 -160.32
REMARK 500 3 ASN A 61 58.35 -101.78
REMARK 500 3 ILE A 68 -96.65 -131.79
REMARK 500 3 LYS A 77 -103.56 55.73
REMARK 500 3 ASN A 79 173.76 73.99
REMARK 500 4 SER A 3 -36.58 -153.82
REMARK 500 4 SER A 6 34.23 -83.79
REMARK 500 4 TYR A 8 -126.81 51.95
REMARK 500 4 ASP A 28 53.96 -140.46
REMARK 500 4 ASP A 45 -40.65 -163.54
REMARK 500 4 ILE A 46 -88.30 18.18
REMARK 500 4 GLU A 57 -66.86 -162.29
REMARK 500 4 VAL A 60 -41.78 -133.22
REMARK 500 5 LEU A 2 -81.73 62.08
REMARK 500 5 SER A 5 81.04 56.92
REMARK 500 5 LYS A 9 -67.88 69.56
REMARK 500 5 GLU A 57 -74.43 -138.77
REMARK 500 5 ASN A 61 -15.78 -145.81
REMARK 500 5 ILE A 68 -108.09 -116.94
REMARK 500 5 PRO A 76 -81.86 -73.65
REMARK 500 5 LYS A 77 41.10 -161.42
REMARK 500 5 ASN A 79 105.39 -167.52
REMARK 500 6 LYS A 9 -47.68 175.27
REMARK 500 6 ARG A 26 -47.09 -136.81
REMARK 500 6 ILE A 46 -102.46 22.47
REMARK 500 6 GLU A 57 -55.16 -167.58
REMARK 500 6 LYS A 77 -44.47 -164.35
REMARK 500 6 TYR A 78 -64.24 -147.08
REMARK 500
REMARK 500 THIS ENTRY HAS 180 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 4 ARG A 23 0.08 SIDE CHAIN
REMARK 500 8 ARG A 23 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D8K RELATED DB: PDB
REMARK 900 RELATED ID: TRT001000205.1 RELATED DB: TARGETDB
DBREF 1D8J A 1 81 UNP P29084 T2EB_HUMAN 66 146
SEQRES 1 A 81 ALA LEU SER GLY SER SER GLY TYR LYS PHE GLY VAL LEU
SEQRES 2 A 81 ALA LYS ILE VAL ASN TYR MET LYS THR ARG HIS GLN ARG
SEQRES 3 A 81 GLY ASP THR HIS PRO LEU THR LEU ASP GLU ILE LEU ASP
SEQRES 4 A 81 GLU THR GLN HIS LEU ASP ILE GLY LEU LYS GLN LYS GLN
SEQRES 5 A 81 TRP LEU MET THR GLU ALA LEU VAL ASN ASN PRO LYS ILE
SEQRES 6 A 81 GLU VAL ILE ASP GLY LYS TYR ALA PHE LYS PRO LYS TYR
SEQRES 7 A 81 ASN VAL ARG
HELIX 1 1 PHE A 10 GLN A 25 1 16
HELIX 2 2 LEU A 34 GLU A 40 1 7
HELIX 3 3 LEU A 48 MET A 55 1 8
SHEET 1 A 3 LEU A 32 LEU A 32 0
SHEET 2 A 3 ILE A 65 ILE A 68 0
SHEET 3 A 3 LYS A 71 PHE A 74 0
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 16 2 Bytes