Header list of 1xob.pdb file
Complete list - v 29 2 Bytes
HEADER ELECTRON TRANSPORT 28-NOV-95 1XOB
TITLE THIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRX-SH2;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: REDUCED DITHIO FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: C1A;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PBHK8
KEYWDS ELECTRON TRANSPORT, REDOX-ACTIVE CENTER
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.-F.JENG,A.P.CAMPBELL,T.BEGLEY,A.HOLMGREN,D.A.CASE,P.E.WRIGHT,
AUTHOR 2 H.J.DYSON
REVDAT 3 29-NOV-17 1XOB 1 REMARK HELIX
REVDAT 2 24-FEB-09 1XOB 1 VERSN
REVDAT 1 10-JUN-96 1XOB 0
SPRSDE 10-JUN-96 1XOB 1TRX
JRNL AUTH M.F.JENG,A.P.CAMPBELL,T.BEGLEY,A.HOLMGREN,D.A.CASE,
JRNL AUTH 2 P.E.WRIGHT,H.J.DYSON
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURES OF OXIDIZED AND REDUCED
JRNL TITL 2 ESCHERICHIA COLI THIOREDOXIN.
JRNL REF STRUCTURE V. 2 853 1994
JRNL REFN ISSN 0969-2126
JRNL PMID 7812718
JRNL DOI 10.1016/S0969-2126(94)00086-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.CHANDRASEKHAR,A.P.CAMPBELL,M.F.JENG,A.HOLMGREN,H.J.DYSON
REMARK 1 TITL EFFECT OF DISULFIDE BRIDGE FORMATION ON THE NMR SPECTRUM OF
REMARK 1 TITL 2 A PROTEIN: STUDIES ON OXIDIZED AND REDUCED ESCHERICHIA COLI
REMARK 1 TITL 3 THIOREDOXIN
REMARK 1 REF J.BIOMOL.NMR V. 4 411 1994
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.CHANDRASEKHAR,G.KRAUSE,A.HOLMGREN,H.J.DYSON
REMARK 1 TITL ASSIGNMENT OF THE 15N NMR SPECTRA OF REDUCED AND OXIDIZED
REMARK 1 TITL 2 ESCHERICHIA COLI THIOREDOXIN
REMARK 1 REF FEBS LETT. V. 284 178 1991
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.J.DYSON,G.P.GIPPERT,D.A.CASE,A.HOLMGREN,P.E.WRIGHT
REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED FORM OF
REMARK 1 TITL 2 ESCHERICHIA COLI THIOREDOXIN DETERMINED BY NUCLEAR MAGNETIC
REMARK 1 TITL 3 RESONANCE SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 29 4129 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH H.J.DYSON,A.HOLMGREN,P.E.WRIGHT
REMARK 1 TITL ASSIGNMENT OF THE PROTON NMR SPECTRUM OF REDUCED AND
REMARK 1 TITL 2 OXIDIZED THIOREDOXIN: SEQUENCE-SPECIFIC ASSIGNMENTS,
REMARK 1 TITL 3 SECONDARY STRUCTURE, AND GLOBAL FOLD
REMARK 1 REF BIOCHEMISTRY V. 28 7074 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XOB 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_1000177299.
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 : 20
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 VAL A 16 -60.42 -108.99
REMARK 500 1 ASN A 63 67.36 -117.15
REMARK 500 2 ASP A 2 -136.88 -166.87
REMARK 500 2 VAL A 16 -62.86 -120.77
REMARK 500 3 ASP A 2 -73.53 60.79
REMARK 500 3 LYS A 18 30.67 -93.00
REMARK 500 3 ASN A 63 67.11 -119.26
REMARK 500 4 ASP A 2 -71.79 58.60
REMARK 500 4 LYS A 18 31.72 -91.98
REMARK 500 4 ASP A 20 54.33 -108.70
REMARK 500 4 ASN A 63 68.91 -119.83
REMARK 500 8 TYR A 49 30.50 -98.86
REMARK 500 9 LYS A 3 46.10 -140.28
REMARK 500 9 ASN A 83 71.52 55.42
REMARK 500 10 LYS A 18 42.33 -91.36
REMARK 500 10 ASN A 63 67.00 -118.11
REMARK 500 12 ASP A 2 -56.33 -23.95
REMARK 500 12 LYS A 18 33.54 -93.68
REMARK 500 12 ALA A 19 81.47 -68.94
REMARK 500 13 VAL A 16 -61.37 -120.48
REMARK 500 13 ASN A 63 72.31 -119.87
REMARK 500 15 ASP A 2 -70.81 63.89
REMARK 500 15 ASN A 83 70.81 51.01
REMARK 500 16 LYS A 18 35.32 -91.64
REMARK 500 18 VAL A 16 -60.29 -94.14
REMARK 500 18 ASP A 20 36.25 -99.52
REMARK 500 18 ASN A 63 70.79 -119.76
REMARK 500 19 LYS A 18 30.13 -96.83
REMARK 500 19 ASN A 63 71.83 -118.39
REMARK 500 20 ASP A 2 -104.66 48.16
REMARK 500 20 LYS A 18 32.06 -96.22
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 TYR A 70 0.18 SIDE CHAIN
REMARK 500 2 TYR A 49 0.08 SIDE CHAIN
REMARK 500 2 TYR A 70 0.14 SIDE CHAIN
REMARK 500 2 ARG A 73 0.10 SIDE CHAIN
REMARK 500 3 TYR A 49 0.09 SIDE CHAIN
REMARK 500 3 TYR A 70 0.17 SIDE CHAIN
REMARK 500 4 TYR A 70 0.15 SIDE CHAIN
REMARK 500 5 PHE A 12 0.08 SIDE CHAIN
REMARK 500 5 TYR A 49 0.12 SIDE CHAIN
REMARK 500 5 TYR A 70 0.08 SIDE CHAIN
REMARK 500 5 PHE A 102 0.08 SIDE CHAIN
REMARK 500 6 TYR A 70 0.12 SIDE CHAIN
REMARK 500 6 PHE A 102 0.09 SIDE CHAIN
REMARK 500 7 TYR A 70 0.14 SIDE CHAIN
REMARK 500 7 ARG A 73 0.10 SIDE CHAIN
REMARK 500 7 PHE A 102 0.08 SIDE CHAIN
REMARK 500 8 TYR A 70 0.14 SIDE CHAIN
REMARK 500 9 TYR A 49 0.08 SIDE CHAIN
REMARK 500 9 TYR A 70 0.07 SIDE CHAIN
REMARK 500 9 ARG A 73 0.10 SIDE CHAIN
REMARK 500 10 TYR A 49 0.08 SIDE CHAIN
REMARK 500 10 TYR A 70 0.13 SIDE CHAIN
REMARK 500 11 TYR A 49 0.07 SIDE CHAIN
REMARK 500 11 TYR A 70 0.09 SIDE CHAIN
REMARK 500 12 TYR A 70 0.20 SIDE CHAIN
REMARK 500 13 TYR A 70 0.14 SIDE CHAIN
REMARK 500 13 ARG A 73 0.10 SIDE CHAIN
REMARK 500 14 TYR A 70 0.17 SIDE CHAIN
REMARK 500 15 TYR A 70 0.17 SIDE CHAIN
REMARK 500 16 TYR A 49 0.10 SIDE CHAIN
REMARK 500 16 TYR A 70 0.14 SIDE CHAIN
REMARK 500 17 TYR A 70 0.10 SIDE CHAIN
REMARK 500 17 ARG A 73 0.10 SIDE CHAIN
REMARK 500 18 TYR A 70 0.17 SIDE CHAIN
REMARK 500 19 TYR A 70 0.17 SIDE CHAIN
REMARK 500 19 ARG A 73 0.11 SIDE CHAIN
REMARK 500 20 TYR A 70 0.16 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XOB A 1 108 UNP P0AA25 THIO_ECOLI 1 108
SEQRES 1 A 108 SER ASP LYS ILE ILE HIS LEU THR ASP ASP SER PHE ASP
SEQRES 2 A 108 THR ASP VAL LEU LYS ALA ASP GLY ALA ILE LEU VAL ASP
SEQRES 3 A 108 PHE TRP ALA GLU TRP CYS GLY PRO CYS LYS MET ILE ALA
SEQRES 4 A 108 PRO ILE LEU ASP GLU ILE ALA ASP GLU TYR GLN GLY LYS
SEQRES 5 A 108 LEU THR VAL ALA LYS LEU ASN ILE ASP GLN ASN PRO GLY
SEQRES 6 A 108 THR ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU
SEQRES 7 A 108 LEU LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL
SEQRES 8 A 108 GLY ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP
SEQRES 9 A 108 ALA ASN LEU ALA
HELIX 1 H1 SER A 11 LYS A 18 1 8
HELIX 2 H2 GLY A 33 GLU A 48 1 16
HELIX 3 H3 ILE A 60 LYS A 69 5DISTORTED 10
HELIX 4 H4 LYS A 96 LEU A 107 1 12
SHEET 1 B1 5 ILE A 4 THR A 8 0
SHEET 2 B1 5 LEU A 53 ASN A 59 1 N LYS A 57 O ILE A 5
SHEET 3 B1 5 ALA A 22 ALA A 29 1 N ASP A 26 O ALA A 56
SHEET 4 B1 5 PRO A 76 LYS A 82 -1 N LEU A 79 O VAL A 25
SHEET 5 B1 5 ALA A 88 GLY A 92 -1 N LYS A 90 O LEU A 78
CISPEP 1 ILE A 75 PRO A 76 1 -1.14
CISPEP 2 ILE A 75 PRO A 76 2 -0.46
CISPEP 3 ILE A 75 PRO A 76 3 -1.34
CISPEP 4 ILE A 75 PRO A 76 4 -0.37
CISPEP 5 ILE A 75 PRO A 76 5 -1.62
CISPEP 6 ILE A 75 PRO A 76 6 -1.37
CISPEP 7 ILE A 75 PRO A 76 7 -1.80
CISPEP 8 ILE A 75 PRO A 76 8 0.07
CISPEP 9 ILE A 75 PRO A 76 9 -1.53
CISPEP 10 ILE A 75 PRO A 76 10 -0.31
CISPEP 11 ILE A 75 PRO A 76 11 -0.86
CISPEP 12 ILE A 75 PRO A 76 12 -1.09
CISPEP 13 ILE A 75 PRO A 76 13 -1.92
CISPEP 14 ILE A 75 PRO A 76 14 -1.68
CISPEP 15 ILE A 75 PRO A 76 15 -1.47
CISPEP 16 ILE A 75 PRO A 76 16 0.13
CISPEP 17 ILE A 75 PRO A 76 17 -0.44
CISPEP 18 ILE A 75 PRO A 76 18 -0.18
CISPEP 19 ILE A 75 PRO A 76 19 -0.96
CISPEP 20 ILE A 75 PRO A 76 20 -1.12
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