Header list of 1hks.pdb file
Complete list - 23 20 Bytes
HEADER TRANSCRIPTION REGULATION 18-JUL-94 1HKS
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK
TITLE 2 TRANSCRIPTION FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT-SHOCK TRANSCRIPTION FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227
KEYWDS TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
AUTHOR G.W.VUISTER,S.-J.KIM,A.OROSZ,J.L.MARQUARDT,C.WU,A.BAX
REVDAT 3 23-FEB-22 1HKS 1 REMARK
REVDAT 2 24-FEB-09 1HKS 1 VERSN
REVDAT 1 30-SEP-94 1HKS 0
JRNL AUTH G.W.VUISTER,S.J.KIM,A.OROSZ,J.MARQUARDT,C.WU,A.BAX
JRNL TITL SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA
JRNL TITL 2 HEAT SHOCK TRANSCRIPTION FACTOR.
JRNL REF NAT.STRUCT.BIOL. V. 1 605 1994
JRNL REFN ISSN 1072-8368
JRNL PMID 7634100
JRNL DOI 10.1038/NSB0994-605
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.W.VUISTER,S.-J.KIM,C.WU,A.BAX
REMARK 1 TITL NMR EVIDENCE FOR SIMILARITIES BETWEEN THE DNA-BINDING
REMARK 1 TITL 2 REGIONS OF DROSOPHILA MELANOGASTER HEAT SHOCK FACTOR AND THE
REMARK 1 TITL 3 HELIX-TURN-HELIX AND HNF-3(SLASH)FORKHEAD FAMILIES OF
REMARK 1 TITL 4 TRANSCRIPTION FACTORS
REMARK 1 REF BIOCHEMISTRY V. 33 10 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HKS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173889.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
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 VAL A 46 108.25 -44.57
REMARK 500 ASP A 58 -128.42 -84.32
REMARK 500 ASP A 59 171.11 53.24
REMARK 500 THR A 62 31.72 -99.69
REMARK 500 ASN A 63 44.11 -87.09
REMARK 500 ARG A 64 -37.58 -170.26
REMARK 500 LYS A 70 -105.54 46.15
REMARK 500 ASP A 71 -90.67 -81.42
REMARK 500 SER A 74 -133.84 -171.13
REMARK 500 ALA A 81 -88.78 -82.54
REMARK 500 LYS A 85 34.85 -82.22
REMARK 500 GLU A 86 7.48 -157.67
REMARK 500 LEU A 87 -31.58 -146.26
REMARK 500 LEU A 90 26.22 -79.89
REMARK 500 ASN A 91 -77.39 -150.28
REMARK 500 LYS A 93 -60.68 74.10
REMARK 500 HIS A 94 -177.65 -52.07
REMARK 500 ASN A 95 -15.50 -144.54
REMARK 500 ALA A 98 -17.96 -45.62
REMARK 500 HIS A 110 82.39 -150.47
REMARK 500 SER A 114 94.20 48.01
REMARK 500 ILE A 115 92.23 -172.67
REMARK 500 LEU A 120 179.18 -50.55
REMARK 500 PHE A 122 98.06 -171.19
REMARK 500 ARG A 124 -12.16 -153.54
REMARK 500 GLU A 126 137.37 -39.57
REMARK 500 ILE A 127 83.21 -30.56
REMARK 500 PRO A 132 23.08 -64.24
REMARK 500 PHE A 133 30.99 -140.96
REMARK 500 PHE A 134 43.38 -150.37
REMARK 500 ARG A 136 -70.84 -85.40
REMARK 500 ASN A 137 -159.80 -58.35
REMARK 500 SER A 138 72.31 50.81
REMARK 500 PRO A 139 44.34 -71.90
REMARK 500 GLN A 144 -36.91 -160.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HKT RELATED DB: PDB
DBREF 1HKS A 43 148 UNP P22813 HSF_DROME 43 148
SEQRES 1 A 106 GLY SER GLY VAL PRO ALA PHE LEU ALA LYS LEU TRP ARG
SEQRES 2 A 106 LEU VAL ASP ASP ALA ASP THR ASN ARG LEU ILE CYS TRP
SEQRES 3 A 106 THR LYS ASP GLY GLN SER PHE VAL ILE GLN ASN GLN ALA
SEQRES 4 A 106 GLN PHE ALA LYS GLU LEU LEU PRO LEU ASN TYR LYS HIS
SEQRES 5 A 106 ASN ASN MET ALA SER PHE ILE ARG GLN LEU ASN MET TYR
SEQRES 6 A 106 GLY PHE HIS LYS ILE THR SER ILE ASP ASN GLY GLY LEU
SEQRES 7 A 106 ARG PHE ASP ARG ASP GLU ILE GLU PHE SER HIS PRO PHE
SEQRES 8 A 106 PHE LYS ARG ASN SER PRO PHE LEU LEU ASP GLN ILE LYS
SEQRES 9 A 106 ARG LYS
HELIX 1 H1 ALA A 48 VAL A 57 1 10
HELIX 2 H2 GLN A 80 PRO A 89 1DISTORTED HELIX 10
HELIX 3 H3 MET A 97 TYR A 107 1 11
SHEET 1 SB 4 ILE A 66 THR A 69 0
SHEET 2 SB 4 SER A 74 ILE A 77 -1
SHEET 3 SB 4 HIS A 110 ILE A 112 1
SHEET 4 SB 4 GLU A 126 SER A 130 -1
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
Complete list - 23 20 Bytes