Header list of 1dl6.pdb file
Complete list - b 16 2 Bytes
HEADER GENE REGULATION 08-DEC-99 1DL6
TITLE SOLUTION STRUCTURE OF HUMAN TFIIB N-TERMINAL DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR II B (TFIIB);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL 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: PET21B
KEYWDS ZINC RIBBON, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR H.-T.CHEN,P.LEGAULT,J.GLUSHKA,J.G.OMICHINSKI,R.A.SCOTT
REVDAT 4 16-FEB-22 1DL6 1 REMARK LINK
REVDAT 3 24-FEB-09 1DL6 1 VERSN
REVDAT 2 01-APR-03 1DL6 1 JRNL
REVDAT 1 18-OCT-00 1DL6 0
JRNL AUTH H.T.CHEN,P.LEGAULT,J.GLUSHKA,J.G.OMICHINSKI,R.A.SCOTT
JRNL TITL STRUCTURE OF A (CYS3HIS) ZINC RIBBON, A UBIQUITOUS MOTIF IN
JRNL TITL 2 ARCHAEAL AND EUCARYAL TRANSCRIPTION.
JRNL REF PROTEIN SCI. V. 9 1743 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 11045620
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, CNS 0.4
REMARK 3 AUTHORS : VARIAN ASSOCIATES, INC. (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 443 RESTRAINTS, 431 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 12 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1DL6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010177.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM HTFIIB N-TERMINAL DOMAIN U
REMARK 210 -15N; 50MM PHOSPHATE; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, NMRDRAW 1.7
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 29
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 2 LYS A 59 C LYS A 59 OXT 0.200
REMARK 500 3 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 4 LYS A 59 C LYS A 59 OXT 0.202
REMARK 500 5 LYS A 59 C LYS A 59 OXT 0.202
REMARK 500 6 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 7 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 8 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 9 LYS A 59 C LYS A 59 OXT 0.200
REMARK 500 10 LYS A 59 C LYS A 59 OXT 0.202
REMARK 500 11 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 12 LYS A 59 C LYS A 59 OXT 0.202
REMARK 500 13 LYS A 59 C LYS A 59 OXT 0.200
REMARK 500 14 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 15 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 16 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 17 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 18 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 19 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 20 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 21 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 22 LYS A 59 C LYS A 59 OXT 0.201
REMARK 500 23 LYS A 59 C LYS A 59 OXT 0.200
REMARK 500 24 LYS A 59 C LYS A 59 OXT 0.200
REMARK 500 25 LYS A 59 C LYS A 59 OXT 0.201
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 ALA A 9 80.76 -63.93
REMARK 500 1 THR A 14 177.91 61.67
REMARK 500 1 HIS A 18 89.15 -153.09
REMARK 500 1 ARG A 28 122.04 172.04
REMARK 500 1 ASP A 31 -173.05 67.48
REMARK 500 1 GLU A 36 -77.77 -115.09
REMARK 500 1 ILE A 46 93.44 -59.64
REMARK 500 1 SER A 50 33.23 -162.54
REMARK 500 1 TRP A 52 -66.26 66.96
REMARK 500 1 ARG A 53 86.67 68.26
REMARK 500 1 PHE A 55 59.71 -90.12
REMARK 500 1 SER A 56 148.54 62.62
REMARK 500 2 SER A 5 96.26 60.74
REMARK 500 2 ARG A 6 133.04 63.53
REMARK 500 2 LEU A 7 47.37 -171.69
REMARK 500 2 ASP A 8 -42.06 -169.97
REMARK 500 2 ALA A 9 -172.12 62.27
REMARK 500 2 VAL A 13 48.14 -92.36
REMARK 500 2 ASP A 20 40.47 -92.26
REMARK 500 2 ALA A 21 63.56 -155.08
REMARK 500 2 GLU A 36 -83.04 -79.54
REMARK 500 2 ARG A 44 96.68 -66.38
REMARK 500 2 ARG A 53 132.05 63.80
REMARK 500 2 PHE A 55 -171.88 60.85
REMARK 500 2 SER A 56 149.38 62.21
REMARK 500 2 ASN A 57 98.43 59.45
REMARK 500 2 ASP A 58 -55.93 -138.45
REMARK 500 3 THR A 4 -66.23 -131.04
REMARK 500 3 SER A 5 -66.68 -162.84
REMARK 500 3 ARG A 6 -62.07 -148.94
REMARK 500 3 ALA A 9 35.45 -97.85
REMARK 500 3 PRO A 11 79.77 -67.47
REMARK 500 3 ARG A 12 59.59 -101.62
REMARK 500 3 VAL A 13 81.32 -63.67
REMARK 500 3 ASP A 20 31.03 -99.56
REMARK 500 3 ALA A 21 80.76 -152.92
REMARK 500 3 ASP A 26 93.29 42.68
REMARK 500 3 ALA A 29 -44.71 -152.40
REMARK 500 3 GLU A 36 -83.30 -87.99
REMARK 500 3 ASP A 43 83.84 -170.70
REMARK 500 3 ILE A 46 59.21 -93.95
REMARK 500 3 VAL A 48 30.80 -97.48
REMARK 500 3 GLU A 51 -46.81 -141.47
REMARK 500 3 SER A 56 169.01 60.52
REMARK 500 4 SER A 3 33.91 -167.23
REMARK 500 4 SER A 5 79.82 60.84
REMARK 500 4 ASP A 8 79.62 60.65
REMARK 500 4 LEU A 10 147.88 61.96
REMARK 500 4 THR A 14 175.31 72.04
REMARK 500 4 LEU A 23 -178.28 -55.05
REMARK 500
REMARK 500 THIS ENTRY HAS 321 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 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 HIS A 18 ND1 106.3
REMARK 620 3 CYS A 34 SG 111.1 108.9
REMARK 620 4 CYS A 37 SG 112.3 112.9 105.3
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 60
DBREF 1DL6 A 2 59 UNP Q00403 TF2B_HUMAN 2 59
SEQRES 1 A 58 ALA SER THR SER ARG LEU ASP ALA LEU PRO ARG VAL THR
SEQRES 2 A 58 CYS PRO ASN HIS PRO ASP ALA ILE LEU VAL GLU ASP TYR
SEQRES 3 A 58 ARG ALA GLY ASP MET ILE CYS PRO GLU CYS GLY LEU VAL
SEQRES 4 A 58 VAL GLY ASP ARG VAL ILE ASP VAL GLY SER GLU TRP ARG
SEQRES 5 A 58 THR PHE SER ASN ASP LYS
HET ZN A 60 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
SHEET 1 A 3 VAL A 24 GLU A 25 0
SHEET 2 A 3 MET A 32 ILE A 33 -1 O ILE A 33 N VAL A 24
SHEET 3 A 3 VAL A 40 VAL A 41 -1 N VAL A 41 O MET A 32
LINK SG CYS A 15 ZN ZN A 60 1555 1555 2.30
LINK ND1 HIS A 18 ZN ZN A 60 1555 1555 2.02
LINK SG CYS A 34 ZN ZN A 60 1555 1555 2.29
LINK SG CYS A 37 ZN ZN A 60 1555 1555 2.30
SITE 1 AC1 4 CYS A 15 HIS A 18 CYS A 34 CYS A 37
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