Header list of 3hsf.pdb file
Complete list - r 16 2 Bytes
HEADER TRANSCRIPTION REGULATION 07-AUG-95 3HSF
TITLE HEAT SHOCK TRANSCRIPTION FACTOR (HSF)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK TRANSCRIPTION FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HSF;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 3 ORGANISM_TAXID: 28985;
SOURCE 4 CELL_LINE: BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PHN212
KEYWDS TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR F.F.DAMBERGER,J.G.PELTON,C.LIU,H.CHO,C.J.HARRISON,H.C.M.NELSON,
AUTHOR 2 D.E.WEMMER
REVDAT 3 16-MAR-22 3HSF 1 REMARK
REVDAT 2 24-FEB-09 3HSF 1 VERSN
REVDAT 1 14-NOV-95 3HSF 0
SPRSDE 14-NOV-95 3HSF 2HSF
JRNL AUTH F.F.DAMBERGER,J.G.PELTON,C.LIU,H.CHO,C.J.HARRISON,
JRNL AUTH 2 H.C.NELSON,D.E.WEMMER
JRNL TITL REFINED SOLUTION STRUCTURE AND DYNAMICS OF THE DNA-BINDING
JRNL TITL 2 DOMAIN OF THE HEAT SHOCK FACTOR FROM KLUYVEROMYCES LACTIS.
JRNL REF J.MOL.BIOL. V. 254 704 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7500344
JRNL DOI 10.1006/JMBI.1995.0649
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.HARRISON,A.A.BOHM,H.C.M.NELSON
REMARK 1 TITL CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF THE HEAT
REMARK 1 TITL 2 SHOCK TRANSCRIPTION FACTOR
REMARK 1 REF SCIENCE V. 263 224 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.F.DAMBERGER,J.G.PELTON,C.J.HARRISON,H.C.M.NELSON,
REMARK 1 AUTH 2 D.E.WEMMER
REMARK 1 TITL SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF THE HEAT
REMARK 1 TITL 2 SHOCK TRANSCRIPTION FACTOR DETERMINED BY MULTIDIMENSIONAL
REMARK 1 TITL 3 HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF PROTEIN SCI. V. 3 1806 1994
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HSF 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_1000179007.
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 : 30
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 ARG A 2 75.96 61.13
REMARK 500 1 ASN A 14 -98.66 -59.82
REMARK 500 1 ASP A 15 40.97 170.36
REMARK 500 1 LYS A 16 -68.78 -90.16
REMARK 500 1 LYS A 20 36.00 97.17
REMARK 500 1 PHE A 21 -43.56 -137.66
REMARK 500 1 THR A 26 -54.85 -151.30
REMARK 500 1 SER A 27 24.32 -149.36
REMARK 500 1 GLU A 29 18.82 58.88
REMARK 500 1 SER A 30 140.67 172.76
REMARK 500 1 PHE A 39 -73.91 -63.53
REMARK 500 1 VAL A 43 -41.07 -153.62
REMARK 500 1 TYR A 47 -44.49 -157.31
REMARK 500 1 LYS A 49 -96.49 42.67
REMARK 500 1 LYS A 72 -79.63 -83.38
REMARK 500 1 SER A 73 -79.66 -90.94
REMARK 500 1 MET A 76 31.16 -149.81
REMARK 500 1 LEU A 77 -166.98 -78.99
REMARK 500 1 ASN A 79 29.94 -151.76
REMARK 500 1 ASP A 81 36.17 -142.27
REMARK 500 1 SER A 82 32.53 -149.58
REMARK 500 1 ARG A 83 94.70 -177.42
REMARK 500 1 GLU A 89 99.90 -169.85
REMARK 500 2 ARG A 2 71.52 -165.78
REMARK 500 2 ASN A 14 -94.46 -57.40
REMARK 500 2 ASP A 15 39.35 165.96
REMARK 500 2 LYS A 16 -67.60 -91.97
REMARK 500 2 PHE A 21 -77.83 -151.62
REMARK 500 2 HIS A 23 137.96 -176.37
REMARK 500 2 SER A 25 -158.23 -89.67
REMARK 500 2 SER A 27 26.49 47.51
REMARK 500 2 GLU A 29 -68.31 -137.17
REMARK 500 2 VAL A 43 -34.43 -151.17
REMARK 500 2 TYR A 47 -44.20 -136.75
REMARK 500 2 PHE A 48 -64.04 -97.97
REMARK 500 2 LYS A 49 -50.68 85.93
REMARK 500 2 HIS A 50 59.78 -102.36
REMARK 500 2 ASP A 70 -64.51 82.77
REMARK 500 2 VAL A 71 90.19 66.26
REMARK 500 2 LYS A 72 -65.99 -172.68
REMARK 500 2 SER A 75 -40.96 -131.28
REMARK 500 2 MET A 76 -63.54 -131.25
REMARK 500 2 LEU A 77 -173.03 -60.11
REMARK 500 2 SER A 78 105.88 64.76
REMARK 500 2 ASN A 79 -52.77 83.96
REMARK 500 2 SER A 82 78.13 -114.49
REMARK 500 2 GLU A 89 113.17 64.04
REMARK 500 2 HIS A 91 -168.78 -111.04
REMARK 500 3 ARG A 2 -59.91 177.21
REMARK 500 3 PHE A 21 -86.23 -151.76
REMARK 500
REMARK 500 THIS ENTRY HAS 520 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 1 ARG A 2 0.32 SIDE CHAIN
REMARK 500 1 ARG A 36 0.24 SIDE CHAIN
REMARK 500 1 ARG A 38 0.32 SIDE CHAIN
REMARK 500 1 ARG A 58 0.28 SIDE CHAIN
REMARK 500 1 ARG A 83 0.20 SIDE CHAIN
REMARK 500 1 ARG A 90 0.30 SIDE CHAIN
REMARK 500 2 ARG A 2 0.28 SIDE CHAIN
REMARK 500 2 ARG A 36 0.32 SIDE CHAIN
REMARK 500 2 ARG A 38 0.27 SIDE CHAIN
REMARK 500 2 ARG A 58 0.28 SIDE CHAIN
REMARK 500 2 ARG A 83 0.32 SIDE CHAIN
REMARK 500 2 ARG A 90 0.31 SIDE CHAIN
REMARK 500 3 ARG A 2 0.31 SIDE CHAIN
REMARK 500 3 ARG A 36 0.26 SIDE CHAIN
REMARK 500 3 ARG A 38 0.29 SIDE CHAIN
REMARK 500 3 ARG A 58 0.25 SIDE CHAIN
REMARK 500 3 ARG A 83 0.28 SIDE CHAIN
REMARK 500 3 ARG A 90 0.30 SIDE CHAIN
REMARK 500 4 ARG A 2 0.22 SIDE CHAIN
REMARK 500 4 ARG A 36 0.29 SIDE CHAIN
REMARK 500 4 ARG A 38 0.29 SIDE CHAIN
REMARK 500 4 ARG A 58 0.25 SIDE CHAIN
REMARK 500 4 ARG A 83 0.26 SIDE CHAIN
REMARK 500 4 ARG A 90 0.21 SIDE CHAIN
REMARK 500 5 ARG A 2 0.24 SIDE CHAIN
REMARK 500 5 ARG A 36 0.28 SIDE CHAIN
REMARK 500 5 ARG A 38 0.30 SIDE CHAIN
REMARK 500 5 ARG A 58 0.32 SIDE CHAIN
REMARK 500 5 ARG A 83 0.31 SIDE CHAIN
REMARK 500 5 ARG A 90 0.24 SIDE CHAIN
REMARK 500 6 ARG A 2 0.28 SIDE CHAIN
REMARK 500 6 ARG A 36 0.30 SIDE CHAIN
REMARK 500 6 ARG A 38 0.32 SIDE CHAIN
REMARK 500 6 ARG A 58 0.31 SIDE CHAIN
REMARK 500 6 ARG A 83 0.26 SIDE CHAIN
REMARK 500 6 ARG A 90 0.27 SIDE CHAIN
REMARK 500 7 ARG A 2 0.31 SIDE CHAIN
REMARK 500 7 ARG A 36 0.30 SIDE CHAIN
REMARK 500 7 ARG A 38 0.23 SIDE CHAIN
REMARK 500 7 ARG A 58 0.23 SIDE CHAIN
REMARK 500 7 ARG A 83 0.22 SIDE CHAIN
REMARK 500 7 ARG A 90 0.23 SIDE CHAIN
REMARK 500 8 ARG A 2 0.32 SIDE CHAIN
REMARK 500 8 ARG A 36 0.23 SIDE CHAIN
REMARK 500 8 ARG A 38 0.21 SIDE CHAIN
REMARK 500 8 ARG A 58 0.23 SIDE CHAIN
REMARK 500 8 ARG A 83 0.24 SIDE CHAIN
REMARK 500 8 ARG A 90 0.31 SIDE CHAIN
REMARK 500 9 ARG A 2 0.22 SIDE CHAIN
REMARK 500 9 ARG A 36 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 180 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3HSF A 1 89 UNP P22121 HSF_KLULA 193 281
SEQRES 1 A 92 ALA ARG PRO ALA PHE VAL ASN LYS LEU TRP SER MET VAL
SEQRES 2 A 92 ASN ASP LYS SER ASN GLU LYS PHE ILE HIS TRP SER THR
SEQRES 3 A 92 SER GLY GLU SER ILE VAL VAL PRO ASN ARG GLU ARG PHE
SEQRES 4 A 92 VAL GLN GLU VAL LEU PRO LYS TYR PHE LYS HIS SER ASN
SEQRES 5 A 92 PHE ALA SER PHE VAL ARG GLN LEU ASN MET TYR GLY TRP
SEQRES 6 A 92 HIS LYS VAL GLN ASP VAL LYS SER GLY SER MET LEU SER
SEQRES 7 A 92 ASN ASN ASP SER ARG TRP GLU PHE GLU ASN GLU ARG HIS
SEQRES 8 A 92 ALA
HELIX 1 H1 ALA A 4 ASN A 14 1 11
HELIX 2 H2 ARG A 36 PHE A 48 1CONTAINS IRREGULAR BULGE 13
HELIX 3 H3 ALA A 54 TYR A 63 1H2 & H3 FORM HELIX-TURN-HELIX 10
SHEET 1 B 4 ILE A 22 TRP A 24 0
SHEET 2 B 4 ILE A 31 PRO A 34 -1 N VAL A 32 O HIS A 23
SHEET 3 B 4 TRP A 84 PHE A 86 -1 O PHE A 86 N ILE A 31
SHEET 4 B 4 TRP A 65 VAL A 68 -1 N VAL A 68 O GLU A 85
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 16 2 Bytes