Header list of 3trx.pdb file
Complete list - 16 20 Bytes
HEADER ELECTRON TRANSPORT 17-DEC-90 3TRX
TITLE HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF REDUCED RECOMBINANT
TITLE 2 HUMAN THIOREDOXIN IN SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR J.D.FORMAN-KAY,G.M.CLORE,A.M.GRONENBORN
REVDAT 4 16-MAR-22 3TRX 1 REMARK SEQADV
REVDAT 3 24-FEB-09 3TRX 1 VERSN
REVDAT 2 15-JAN-93 3TRX 1 HEADER COMPND
REVDAT 1 15-JAN-92 3TRX 0
JRNL AUTH J.D.FORMAN-KAY,G.M.CLORE,P.T.WINGFIELD,A.M.GRONENBORN
JRNL TITL HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF REDUCED
JRNL TITL 2 RECOMBINANT HUMAN THIOREDOXIN IN SOLUTION.
JRNL REF BIOCHEMISTRY V. 30 2685 1991
JRNL REFN ISSN 0006-2960
JRNL PMID 2001356
JRNL DOI 10.1021/BI00224A017
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.D.FORMAN-KAY,A.M.GRONENBORN,L.E.KAY,P.T.WINGFIELD,
REMARK 1 AUTH 2 G.M.CLORE
REMARK 1 TITL STUDIES ON THE SOLUTION CONFORMATION OF HUMAN THIOREDOXIN
REMARK 1 TITL 2 USING HETERONUCLEAR 15N-1H NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 29 1566 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.D.FORMAN-KAY,G.M.CLORE,P.C.DRISCOLL,P.WINGFIELD,
REMARK 1 AUTH 2 F.M.RICHARDS,A.M.GRONENBORN
REMARK 1 TITL A PROTON NUCLEAR MAGNETIC RESONANCE ASSIGNMENT AND SECONDARY
REMARK 1 TITL 2 STRUCTURE DETERMINATION OF RECOMBINANT HUMAN THIOREDOXIN
REMARK 1 REF BIOCHEMISTRY V. 28 7088 1989
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:
REMARK 3 STRUCTURES DETERMINED BY THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD OF M. NILGES, G. M. CLORE, AND A. M. GRONENBORN
REMARK 3 (FEBS LETT. 229, 317 (1988)). THE STRUCTURES ARE BASED
REMARK 3 ON 1983 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE
REMARK 3 MEASUREMENTS; 52 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR
REMARK 3 26 HYDROGEN-BONDS IDENTIFIED ON THE BASIS OF THE NOE AND
REMARK 3 AMIDE PROTON EXCHANGE DATA, AS WELL AS THE INITIAL
REMARK 3 STRUCTURE CALCULATIONS; AND 98 PHI AND 71 PSI BACKBONE
REMARK 3 TORSION ANGLE RESTRAINTS AND 72 CHI1 SIDE-CHAIN TORSION
REMARK 3 ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS AND NOE
REMARK 3 DATA.
REMARK 3
REMARK 3 A TOTAL OF 33 STRUCTURES WERE CALCULATED. THIS STRUCTURE
REMARK 3 REPRESENTS THE MINIMIZED AVERAGE STRUCTURE. THIS IS
REMARK 3 OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL
REMARK 3 STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO
REMARK 3 RESTRAINED MINIMIZATION. THE ENTIRE SET OF 33 STRUCTURES
REMARK 3 CAN BE FOUND IN PDB ENTRY 4TRX.
REMARK 3
REMARK 3 THE LAST COLUMN IN THIS COORDINATE FILE REPRESENTS THE
REMARK 3 ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT
REMARK 3 THE MEAN COORDINATE POSITIONS.
REMARK 4
REMARK 4 3TRX 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_1000179177.
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: 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 TRP A 31 CG TRP A 31 CD2 -0.106
REMARK 500 HIS A 43 CG HIS A 43 ND1 -0.115
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.7 DEGREES
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 GLU A 6 -19.36 -143.93
REMARK 500 LYS A 21 160.40 -45.37
REMARK 500 PRO A 40 0.91 -62.13
REMARK 500 LYS A 48 -71.28 -59.08
REMARK 500 VAL A 59 17.60 -68.77
REMARK 500 LYS A 72 22.71 -145.56
REMARK 500 CYS A 73 126.42 -176.26
REMARK 500 LYS A 82 11.14 57.37
REMARK 500 GLU A 95 -18.39 -46.46
REMARK 500 GLU A 98 -72.77 -50.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TRX RELATED DB: PDB
DBREF 3TRX A 2 105 UNP P10599 THIO_HUMAN 1 104
SEQADV 3TRX THR A 74 UNP P10599 MET 73 CONFLICT
SEQRES 1 A 105 MET VAL LYS GLN ILE GLU SER LYS THR ALA PHE GLN GLU
SEQRES 2 A 105 ALA LEU ASP ALA ALA GLY ASP LYS LEU VAL VAL VAL ASP
SEQRES 3 A 105 PHE SER ALA THR TRP CYS GLY PRO CYS LYS MET ILE LYS
SEQRES 4 A 105 PRO PHE PHE HIS SER LEU SER GLU LYS TYR SER ASN VAL
SEQRES 5 A 105 ILE PHE LEU GLU VAL ASP VAL ASP ASP CYS GLN ASP VAL
SEQRES 6 A 105 ALA SER GLU CYS GLU VAL LYS CYS THR PRO THR PHE GLN
SEQRES 7 A 105 PHE PHE LYS LYS GLY GLN LYS VAL GLY GLU PHE SER GLY
SEQRES 8 A 105 ALA ASN LYS GLU LYS LEU GLU ALA THR ILE ASN GLU LEU
SEQRES 9 A 105 VAL
HELIX 1 1 SER A 7 ALA A 18 1 12
HELIX 2 2 CYS A 35 MET A 37 5 3
HELIX 3 3 ILE A 38 HIS A 43 1 6
HELIX 4 4 SER A 44 TYR A 49 1 6
HELIX 5 5 CYS A 62 SER A 67 1 6
HELIX 6 6 LYS A 94 VAL A 105 1 12
SHEET 1 A 5 LYS A 3 GLN A 4 0
SHEET 2 A 5 ILE A 53 ASP A 58 1 O PHE A 54 N LYS A 3
SHEET 3 A 5 VAL A 23 SER A 28 1 O VAL A 24 N LEU A 55
SHEET 4 A 5 THR A 76 LYS A 81 -1 O THR A 76 N PHE A 27
SHEET 5 A 5 GLN A 84 SER A 90 -1 O GLN A 84 N LYS A 81
CISPEP 1 THR A 74 PRO A 75 0 -0.90
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 - 16 20 Bytes