Header list of 1tru.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 10-MAY-94 1TRU 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 1TRU 1 REMARK SEQADV REVDAT 2 24-FEB-09 1TRU 1 VERSN REVDAT 1 30-SEP-94 1TRU 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 OXIDIZED HUMAN THIOREDOXIN IN SOLUTION REMARK 3 BY NMR IS BASED ON 3018 EXPERIMENTAL RESTRAINTS COMPRISING: REMARK 3 2649 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS; 34 REMARK 3 RESTRAINTS FOR 17 H-BONDS INVOLVING 7 TIGHTLY BOUND WATER REMARK 3 MOLECULES; 42 RESTRAINTS FOR 21 BACKBONE HYDROGEN BONDS REMARK 3 INVOLVING SLOWLY EXCHANGING AMIDE PROTONS; 278 TORSION REMARK 3 ANGLE RESTRAINTS (104 PHI, 76 PSI, 78 CHI1 AND 20 CHI2); REMARK 3 AND 91 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 1TRS. 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 1TRS) 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 1TRU) HAVE NO MEANING. REMARK 4 REMARK 4 1TRU 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_1000176816. 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 H VAL A 52 H2 HOH A 207 1.27 REMARK 500 HD21 ASN A 93 H LYS A 96 1.29 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 PHE A 41 -70.63 -115.02 REMARK 500 1 VAL A 59 6.81 -63.32 REMARK 500 1 ALA A 62 53.37 -104.47 REMARK 500 1 LYS A 82 9.12 52.63 REMARK 500 1 ASN A 93 73.37 -103.22 REMARK 500 2 PHE A 41 -70.59 -115.35 REMARK 500 2 ASN A 51 31.09 -98.93 REMARK 500 2 VAL A 59 6.24 -63.53 REMARK 500 2 ALA A 62 53.31 -104.44 REMARK 500 3 ASN A 51 30.31 -99.42 REMARK 500 3 VAL A 59 4.98 -62.44 REMARK 500 3 ALA A 62 54.39 -105.02 REMARK 500 3 LYS A 82 11.75 51.60 REMARK 500 4 PHE A 41 -70.04 -115.17 REMARK 500 4 ASN A 51 32.08 -98.35 REMARK 500 4 VAL A 59 7.71 -63.35 REMARK 500 4 ALA A 62 54.40 -103.53 REMARK 500 4 LYS A 82 13.16 52.23 REMARK 500 5 PHE A 41 -71.16 -115.39 REMARK 500 5 VAL A 59 6.87 -63.01 REMARK 500 5 ALA A 62 50.45 -101.79 REMARK 500 5 LYS A 82 11.82 52.10 REMARK 500 5 GLU A 88 147.20 -172.06 REMARK 500 5 ASN A 93 79.37 -104.38 REMARK 500 6 PRO A 40 5.09 -69.24 REMARK 500 6 LEU A 45 -9.96 -59.92 REMARK 500 6 ASN A 51 33.18 -99.73 REMARK 500 6 VAL A 59 8.58 -63.48 REMARK 500 6 ALA A 62 52.30 -102.87 REMARK 500 6 ALA A 73 85.94 -151.79 REMARK 500 6 LYS A 82 9.16 52.66 REMARK 500 6 ASN A 93 79.16 -104.14 REMARK 500 7 PHE A 41 -71.49 -116.29 REMARK 500 7 HIS A 43 0.05 -65.94 REMARK 500 7 ASN A 51 32.67 -98.96 REMARK 500 7 VAL A 59 7.02 -63.43 REMARK 500 7 ALA A 62 52.21 -104.17 REMARK 500 7 LYS A 82 9.46 52.38 REMARK 500 8 VAL A 59 6.51 -63.44 REMARK 500 8 ALA A 62 52.91 -102.32 REMARK 500 8 LYS A 82 9.74 52.51 REMARK 500 9 PHE A 41 -72.39 -115.23 REMARK 500 9 ASN A 51 31.02 -99.33 REMARK 500 9 VAL A 59 8.26 -64.05 REMARK 500 9 ALA A 62 53.53 -104.95 REMARK 500 9 LYS A 82 9.40 52.29 REMARK 500 9 GLU A 88 144.75 -171.15 REMARK 500 9 ASN A 93 79.87 -105.92 REMARK 500 10 PHE A 41 -70.26 -115.67 REMARK 500 10 VAL A 59 6.78 -63.42 REMARK 500 REMARK 500 THIS ENTRY HAS 229 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1TRS RELATED DB: PDB DBREF 1TRU A 2 105 UNP P10599 THIO_HUMAN 1 104 SEQADV 1TRU ALA A 62 UNP P10599 CYS 61 CONFLICT SEQADV 1TRU ALA A 69 UNP P10599 CYS 68 CONFLICT SEQADV 1TRU ALA A 73 UNP P10599 CYS 72 CONFLICT SEQADV 1TRU 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 *7(H2 O) HELIX 1 1 SER A 7 GLY A 19 1 13 HELIX 2 2 CYS A 35 LYS A 39 5 5 HELIX 3 3 SER A 44 TYR A 49 1 6 HELIX 4 4 ALA A 62 ALA A 69 1 8 HELIX 5 5 ASN A 93 ASN A 102 1 10 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 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 N GLN A 84 O LYS A 81 SSBOND 1 CYS A 32 CYS A 35 1555 1555 2.02 CISPEP 1 THR A 74 PRO A 75 1 -1.03 CISPEP 2 THR A 74 PRO A 75 2 -1.07 CISPEP 3 THR A 74 PRO A 75 3 -1.06 CISPEP 4 THR A 74 PRO A 75 4 -1.27 CISPEP 5 THR A 74 PRO A 75 5 -1.16 CISPEP 6 THR A 74 PRO A 75 6 -1.20 CISPEP 7 THR A 74 PRO A 75 7 -1.11 CISPEP 8 THR A 74 PRO A 75 8 -1.02 CISPEP 9 THR A 74 PRO A 75 9 -1.18 CISPEP 10 THR A 74 PRO A 75 10 -1.08 CISPEP 11 THR A 74 PRO A 75 11 -1.09 CISPEP 12 THR A 74 PRO A 75 12 -1.07 CISPEP 13 THR A 74 PRO A 75 13 -1.07 CISPEP 14 THR A 74 PRO A 75 14 -1.08 CISPEP 15 THR A 74 PRO A 75 15 -1.05 CISPEP 16 THR A 74 PRO A 75 16 -1.01 CISPEP 17 THR A 74 PRO A 75 17 -1.11 CISPEP 18 THR A 74 PRO A 75 18 -1.11 CISPEP 19 THR A 74 PRO A 75 19 -0.98 CISPEP 20 THR A 74 PRO A 75 20 -1.02 CISPEP 21 THR A 74 PRO A 75 21 -1.14 CISPEP 22 THR A 74 PRO A 75 22 -1.03 CISPEP 23 THR A 74 PRO A 75 23 -1.12 CISPEP 24 THR A 74 PRO A 75 24 -1.11 CISPEP 25 THR A 74 PRO A 75 25 -1.06 CISPEP 26 THR A 74 PRO A 75 26 -1.06 CISPEP 27 THR A 74 PRO A 75 27 -1.05 CISPEP 28 THR A 74 PRO A 75 28 -1.10 CISPEP 29 THR A 74 PRO A 75 29 -1.12 CISPEP 30 THR A 74 PRO A 75 30 -1.03 CISPEP 31 THR A 74 PRO A 75 31 -1.10 CISPEP 32 THR A 74 PRO A 75 32 -1.08 CISPEP 33 THR A 74 PRO A 75 33 -0.91 CISPEP 34 THR A 74 PRO A 75 34 -0.97 CISPEP 35 THR A 74 PRO A 75 35 -1.17 CISPEP 36 THR A 74 PRO A 75 36 -1.07 CISPEP 37 THR A 74 PRO A 75 37 -1.09 CISPEP 38 THR A 74 PRO A 75 38 -0.99 CISPEP 39 THR A 74 PRO A 75 39 -1.17 CISPEP 40 THR A 74 PRO A 75 40 -1.16 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 2 2 Bytes