HEADER ELECTRON TRANSPORT 10-MAY-94 1TRV
TITLE THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE
TITLE 2 OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN
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
NUMMDL 40
AUTHOR G.M.CLORE,J.QIN,A.M.GRONENBORN
REVDAT 3 02-MAR-22 1TRV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1TRV 1 VERSN
REVDAT 1 30-SEP-94 1TRV 0
JRNL AUTH J.QIN,G.M.CLORE,A.M.GRONENBORN
JRNL TITL THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF
JRNL TITL 2 THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN.
JRNL REF STRUCTURE V. 2 503 1994
JRNL REFN ISSN 0969-2126
JRNL PMID 7922028
JRNL DOI 10.1016/S0969-2126(00)00051-4
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 THE 3D STRUCTURE OF REDUCED HUMAN THIOREDOXIN IN SOLUTION
REMARK 3 BY NMR IS BASED ON 2933 EXPERIMENTAL RESTRAINTS COMPRISING:
REMARK 3 2571 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS; 28
REMARK 3 RESTRAINTS FOR 14 H-BONDS INVOLVING 6 TIGHTLY BOUND WATER
REMARK 3 MOLECULES; 60 RESTRAINTS FOR 30 BACKBONE HYDROGEN BONDS
REMARK 3 INVOLVING SLOWLY EXCHANGING AMIDE PROTONS; 273 TORSION
REMARK 3 ANGLE RESTRAINTS (104 PHI, 71 PSI, 78 CHI1 AND 20 CHI2);
REMARK 3 AND 89 HN-HALPHA THREE-BOND COUPLING CONSTANTS. A
REMARK 3 COMPLETE LIST OF EXPERIMENTAL RESTRAINTS AND 1H, 13C AND
REMARK 3 15N ASSIGNMENTS HAVE BEEN DEPOSITED WITH THE PROTEIN DATA
REMARK 3 BANK.
REMARK 3
REMARK 3 THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. &
REMARK 3 GRONENBORN, A.M. (1988) FEBS LETT 229, 317 - 324. ALL
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN THE REFERENCE.
REMARK 3
REMARK 3 THE RESTRAINED MINIMIZED AVERAGE STRUCTURE (SA)R IS
REMARK 3 PRESENTED IN PROTEIN DATA BANK ENTRY 1TRW. THIS IS
REMARK 3 OBTAINED BY FIRST AVERAGING THE COORDINATES OF THE
REMARK 3 INDIVIDUAL 40 DYNAMICAL SIMULATED ANNEALING SA STRUCTURES
REMARK 3 BEST FITTED TO RESIDUES 1 - 105, AND SUBJECTING THE
REMARK 3 RESULTING COORDINATES TO RESTRAINED MINIMIZATION.
REMARK 3
REMARK 3 COLUMNS 61 - 65 OF THE COORDINATE RECORDS (THE B VALUE
REMARK 3 FIELD IN X-RAY STRUCTURES) IN THE MINIMIZED STRUCTURE
REMARK 3 (ENTRY 1TRW) GIVE THE AVERAGE RMS DIFFERENCE BETWEEN THE
REMARK 3 INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE. THE
REMARK 3 NUMBERS IN THIS FIELD OF THE INDIVIDUAL STRUCTURES (ENTRY
REMARK 3 1TRV) HAVE NO MEANING.
REMARK 4
REMARK 4 1TRV 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_1000176817.
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 : 40
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
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 1 SER A 7 -159.21 -159.55
REMARK 500 1 SER A 28 -165.98 -119.79
REMARK 500 1 ALA A 92 36.78 -79.71
REMARK 500 1 ASN A 93 75.88 -101.69
REMARK 500 2 VAL A 59 9.98 -65.73
REMARK 500 2 LYS A 82 19.22 51.95
REMARK 500 2 ALA A 92 38.62 -80.03
REMARK 500 2 ASN A 93 75.78 -101.35
REMARK 500 3 SER A 50 0.94 -68.21
REMARK 500 3 LYS A 82 19.97 52.23
REMARK 500 3 ALA A 92 40.72 -80.01
REMARK 500 4 CYS A 35 36.44 -74.27
REMARK 500 4 LYS A 36 -34.34 -140.64
REMARK 500 4 SER A 50 1.32 -68.80
REMARK 500 4 VAL A 59 10.12 -65.85
REMARK 500 4 LYS A 82 19.32 52.05
REMARK 500 4 ALA A 92 40.87 -80.25
REMARK 500 5 SER A 28 -167.06 -120.12
REMARK 500 5 LYS A 82 19.63 52.54
REMARK 500 5 ALA A 92 41.24 -80.13
REMARK 500 6 SER A 28 -166.26 -118.39
REMARK 500 6 SER A 50 1.66 -68.35
REMARK 500 6 ALA A 92 40.14 -80.33
REMARK 500 6 ASN A 93 78.64 -100.98
REMARK 500 7 CYS A 35 33.26 -73.02
REMARK 500 7 LYS A 36 -32.64 -140.63
REMARK 500 7 VAL A 59 8.22 -65.18
REMARK 500 7 LYS A 82 18.53 51.75
REMARK 500 7 ALA A 92 37.49 -80.19
REMARK 500 7 ASN A 93 78.66 -100.99
REMARK 500 8 SER A 28 -168.14 -119.83
REMARK 500 8 CYS A 35 35.12 -73.97
REMARK 500 8 LYS A 36 -28.62 -140.47
REMARK 500 8 SER A 50 3.15 -67.98
REMARK 500 8 LYS A 82 18.74 52.04
REMARK 500 8 ALA A 92 41.53 -80.34
REMARK 500 9 CYS A 35 34.03 -73.44
REMARK 500 9 LYS A 36 -29.84 -140.42
REMARK 500 9 SER A 50 1.61 -68.88
REMARK 500 9 LYS A 82 19.94 52.30
REMARK 500 9 ALA A 92 35.27 -79.71
REMARK 500 9 ASN A 93 77.65 -101.73
REMARK 500 10 SER A 28 -167.40 -115.95
REMARK 500 10 SER A 50 0.89 -68.27
REMARK 500 10 LYS A 82 17.51 52.53
REMARK 500 10 ALA A 92 42.91 -80.18
REMARK 500 11 SER A 28 -166.84 -122.19
REMARK 500 11 CYS A 35 34.04 -73.77
REMARK 500 11 LYS A 36 -30.92 -140.58
REMARK 500 11 SER A 50 1.15 -69.08
REMARK 500
REMARK 500 THIS ENTRY HAS 189 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TRW RELATED DB: PDB
DBREF 1TRV A 2 105 UNP P10599 THIO_HUMAN 1 104
SEQADV 1TRV ALA A 62 UNP P10599 CYS 61 CONFLICT
SEQADV 1TRV ALA A 69 UNP P10599 CYS 68 CONFLICT
SEQADV 1TRV ALA A 73 UNP P10599 CYS 72 CONFLICT
SEQADV 1TRV 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 ALA GLN ASP VAL
SEQRES 6 A 105 ALA SER GLU ALA GLU VAL LYS ALA 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
FORMUL 2 HOH *6(H2 O)
HELIX 1 1 SER A 7 GLY A 19 1 13
HELIX 2 2 GLY A 33 ILE A 38 1 6
HELIX 3 3 ILE A 38 TYR A 49 1 12
HELIX 4 4 ALA A 62 GLU A 70 1 9
HELIX 5 5 GLU A 95 ASN A 102 1 8
SHEET 1 A 5 VAL A 2 ILE A 5 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 N VAL A 24 O ILE A 53
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 N GLN A 84 O LYS A 81
CISPEP 1 THR A 74 PRO A 75 1 -1.17
CISPEP 2 THR A 74 PRO A 75 2 -1.31
CISPEP 3 THR A 74 PRO A 75 3 -1.24
CISPEP 4 THR A 74 PRO A 75 4 -1.29
CISPEP 5 THR A 74 PRO A 75 5 -1.25
CISPEP 6 THR A 74 PRO A 75 6 -1.27
CISPEP 7 THR A 74 PRO A 75 7 -1.23
CISPEP 8 THR A 74 PRO A 75 8 -1.26
CISPEP 9 THR A 74 PRO A 75 9 -1.18
CISPEP 10 THR A 74 PRO A 75 10 -1.30
CISPEP 11 THR A 74 PRO A 75 11 -1.27
CISPEP 12 THR A 74 PRO A 75 12 -1.33
CISPEP 13 THR A 74 PRO A 75 13 -1.19
CISPEP 14 THR A 74 PRO A 75 14 -1.53
CISPEP 15 THR A 74 PRO A 75 15 -1.23
CISPEP 16 THR A 74 PRO A 75 16 -1.31
CISPEP 17 THR A 74 PRO A 75 17 -1.18
CISPEP 18 THR A 74 PRO A 75 18 -1.25
CISPEP 19 THR A 74 PRO A 75 19 -1.31
CISPEP 20 THR A 74 PRO A 75 20 -1.16
CISPEP 21 THR A 74 PRO A 75 21 -1.15
CISPEP 22 THR A 74 PRO A 75 22 -1.19
CISPEP 23 THR A 74 PRO A 75 23 -1.16
CISPEP 24 THR A 74 PRO A 75 24 -1.26
CISPEP 25 THR A 74 PRO A 75 25 -1.24
CISPEP 26 THR A 74 PRO A 75 26 -1.24
CISPEP 27 THR A 74 PRO A 75 27 -1.26
CISPEP 28 THR A 74 PRO A 75 28 -1.19
CISPEP 29 THR A 74 PRO A 75 29 -1.19
CISPEP 30 THR A 74 PRO A 75 30 -1.28
CISPEP 31 THR A 74 PRO A 75 31 -1.22
CISPEP 32 THR A 74 PRO A 75 32 -1.14
CISPEP 33 THR A 74 PRO A 75 33 -1.31
CISPEP 34 THR A 74 PRO A 75 34 -1.15
CISPEP 35 THR A 74 PRO A 75 35 -1.22
CISPEP 36 THR A 74 PRO A 75 36 -1.29
CISPEP 37 THR A 74 PRO A 75 37 -1.05
CISPEP 38 THR A 74 PRO A 75 38 -1.05
CISPEP 39 THR A 74 PRO A 75 39 -1.22
CISPEP 40 THR A 74 PRO A 75 40 -1.26
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
(ATOM LINES ARE NOT SHOWN.)
END
