Header list of 1pft.pdb file
Complete list - v 29 2 Bytes
HEADER TRANSCRIPTION INITIATION 27-MAR-96 1PFT
TITLE N-TERMINAL DOMAIN OF TFIIB, NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TFIIB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: PFTFIIBN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 GENE: PYROCOCCUS FURIOSUS TFIIB GENE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQZNTD;
SOURCE 9 EXPRESSION_SYSTEM_GENE: PYROCOCCUS FURIOSUS TFIIB GENE
KEYWDS N-TERMINAL DOMAIN, TFIIB, TRANSCRIPTION INITIATION FACTOR,
KEYWDS 2 TRANSCRIPTION INITIATION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR W.ZHU,Q.ZENG,C.M.COLANGELO,L.M.LEWIS,M.F.SUMMERS,R.A.SCOTT
REVDAT 3 29-NOV-17 1PFT 1 REMARK HELIX
REVDAT 2 24-FEB-09 1PFT 1 VERSN
REVDAT 1 17-AUG-96 1PFT 0
JRNL AUTH W.ZHU,Q.ZENG,C.M.COLANGELO,M.LEWIS,M.F.SUMMERS,R.A.SCOTT
JRNL TITL THE N-TERMINAL DOMAIN OF TFIIB FROM PYROCOCCUS FURIOSUS
JRNL TITL 2 FORMS A ZINC RIBBON.
JRNL REF NAT.STRUCT.BIOL. V. 3 122 1996
JRNL REFN ISSN 1072-8368
JRNL PMID 8564536
JRNL DOI 10.1038/NSB0296-122
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DSPACE
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PFT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175649.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DSPACE
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 ASN A 3 -155.46 70.15
REMARK 500 1 GLN A 5 86.80 68.11
REMARK 500 1 VAL A 7 -163.38 59.53
REMARK 500 1 ALA A 10 -74.48 -82.43
REMARK 500 1 GLU A 12 68.68 60.16
REMARK 500 1 LYS A 29 -69.13 -128.00
REMARK 500 1 ILE A 34 -75.92 -118.25
REMARK 500 1 GLU A 36 48.74 -151.51
REMARK 500 1 ASN A 37 56.90 -158.90
REMARK 500 1 ASP A 40 74.45 -162.09
REMARK 500 1 MET A 41 -55.64 -130.34
REMARK 500 1 GLU A 44 78.14 -157.29
REMARK 500 1 TRP A 45 -40.59 -151.33
REMARK 500 1 ALA A 47 132.08 61.61
REMARK 500 2 ASN A 3 -163.57 61.11
REMARK 500 2 LYS A 4 25.74 -175.75
REMARK 500 2 LYS A 29 -69.66 -127.70
REMARK 500 2 ILE A 34 -71.67 -118.57
REMARK 500 2 ILE A 39 -54.61 76.86
REMARK 500 2 TRP A 45 -75.49 -88.38
REMARK 500 2 PHE A 48 -72.37 -92.64
REMARK 500 3 VAL A 2 -177.08 59.04
REMARK 500 3 ASN A 3 116.42 -160.35
REMARK 500 3 GLN A 5 -76.34 -116.76
REMARK 500 3 ALA A 10 -75.62 -84.34
REMARK 500 3 ILE A 34 -74.46 -114.44
REMARK 500 3 GLU A 36 49.29 -141.81
REMARK 500 3 ASP A 40 99.13 -167.49
REMARK 500 3 PRO A 43 -85.18 -51.44
REMARK 500 3 TRP A 45 108.73 62.16
REMARK 500 3 ARG A 46 -80.85 -164.90
REMARK 500 3 ALA A 47 177.96 61.60
REMARK 500 3 ASP A 49 -52.52 -174.14
REMARK 500 4 ASN A 3 101.71 -165.06
REMARK 500 4 GLN A 5 24.31 -142.22
REMARK 500 4 ALA A 10 -76.78 -89.09
REMARK 500 4 LYS A 29 -79.89 -128.61
REMARK 500 4 ILE A 34 -74.96 -126.25
REMARK 500 4 ASN A 37 155.15 70.27
REMARK 500 4 ASP A 40 -96.59 -145.21
REMARK 500 4 GLU A 44 -66.11 -143.72
REMARK 500 4 TRP A 45 38.01 -176.03
REMARK 500 4 ASP A 49 -68.13 -130.07
REMARK 500 5 ASN A 3 -98.68 -62.45
REMARK 500 5 GLN A 5 -168.10 61.38
REMARK 500 5 LYS A 6 -168.94 -113.72
REMARK 500 5 VAL A 7 -165.35 60.41
REMARK 500 5 LYS A 29 -71.30 -126.40
REMARK 500 5 ILE A 34 -71.83 -118.01
REMARK 500 5 ASN A 37 44.23 -103.68
REMARK 500
REMARK 500 THIS ENTRY HAS 309 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 CYS A 8 -11.16
REMARK 500 3 CYS A 8 -11.08
REMARK 500 3 VAL A 33 -11.61
REMARK 500 4 CYS A 11 12.87
REMARK 500 4 GLY A 31 -11.30
REMARK 500 5 CYS A 8 -10.88
REMARK 500 6 CYS A 8 -11.02
REMARK 500 6 CYS A 11 12.25
REMARK 500 6 GLY A 31 10.10
REMARK 500 7 GLY A 31 10.65
REMARK 500 7 GLU A 44 10.69
REMARK 500 8 CYS A 8 -10.62
REMARK 500 8 GLY A 31 10.34
REMARK 500 8 ILE A 38 11.58
REMARK 500 9 CYS A 8 -10.15
REMARK 500 9 GLY A 31 11.27
REMARK 500 9 TYR A 32 -10.40
REMARK 500 10 CYS A 8 -10.18
REMARK 500 10 GLY A 31 10.15
REMARK 500 11 CYS A 8 -10.41
REMARK 500 12 GLY A 31 10.10
REMARK 500 12 VAL A 33 -10.52
REMARK 500 13 CYS A 8 -11.21
REMARK 500 13 ILE A 38 10.57
REMARK 500 14 CYS A 8 -11.54
REMARK 500 15 CYS A 11 12.72
REMARK 500 15 CYS A 27 -12.45
REMARK 500 15 ILE A 39 10.35
REMARK 500 16 CYS A 11 12.66
REMARK 500 16 VAL A 26 -10.86
REMARK 500 16 CYS A 27 -10.38
REMARK 500 17 GLN A 5 13.23
REMARK 500 17 CYS A 27 -10.44
REMARK 500 18 CYS A 27 -10.35
REMARK 500 19 CYS A 8 -10.46
REMARK 500 19 CYS A 27 -10.72
REMARK 500 20 CYS A 8 -10.81
REMARK 500 20 GLY A 31 10.51
REMARK 500 21 CYS A 8 -10.81
REMARK 500 21 GLY A 31 10.51
REMARK 500 22 CYS A 8 -10.94
REMARK 500 22 CYS A 27 -11.16
REMARK 500 23 CYS A 8 -11.36
REMARK 500 23 CYS A 27 -11.02
REMARK 500 23 GLY A 31 10.29
REMARK 500 23 TYR A 32 -10.14
REMARK 500 23 VAL A 33 -10.07
REMARK 500 24 CYS A 27 -12.89
REMARK 500 25 CYS A 8 -11.27
REMARK 500 25 CYS A 27 -14.38
REMARK 500
REMARK 500 THIS ENTRY HAS 51 MAIN CHAIN PLANARITY DEVIATIONS.
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 51 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 CYS A 11 SG 121.6
REMARK 620 3 CYS A 27 SG 103.6 114.1
REMARK 620 4 CYS A 30 SG 106.7 105.2 104.2
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 51
DBREF 1PFT A 1 50 UNP P61998 TF2B_PYRFU 1 49
SEQADV 1PFT VAL A 2 UNP P61998 INSERTION
SEQRES 1 A 50 MET VAL ASN LYS GLN LYS VAL CYS PRO ALA CYS GLU SER
SEQRES 2 A 50 ALA GLU LEU ILE TYR ASP PRO GLU ARG GLY GLU ILE VAL
SEQRES 3 A 50 CYS ALA LYS CYS GLY TYR VAL ILE GLU GLU ASN ILE ILE
SEQRES 4 A 50 ASP MET GLY PRO GLU TRP ARG ALA PHE ASP ALA
HET ZN A 51 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
SHEET 1 A 3 LEU A 16 ASP A 19 0
SHEET 2 A 3 GLU A 24 CYS A 27 -1 N VAL A 26 O ILE A 17
SHEET 3 A 3 TYR A 32 GLU A 36 -1
LINK ZN ZN A 51 SG CYS A 8 1555 1555 2.35
LINK ZN ZN A 51 SG CYS A 11 1555 1555 2.33
LINK ZN ZN A 51 SG CYS A 27 1555 1555 2.35
LINK ZN ZN A 51 SG CYS A 30 1555 1555 2.33
SITE 1 AC1 4 CYS A 8 CYS A 11 CYS A 27 CYS A 30
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 - v 29 2 Bytes