Header list of 1tof.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 30-MAY-96 1TOF TITLE THIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: THIOREDOXIN H; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HTRX, HCH1, CH1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII; SOURCE 3 ORGANISM_TAXID: 3055; SOURCE 4 STRAIN: CW15; SOURCE 5 CELLULAR_LOCATION: CYTOPLASM; SOURCE 6 GENE: THIOREDOXIN H CDNA (X78822 EMB; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-3D; SOURCE 11 EXPRESSION_SYSTEM_GENE: THIOREDOXIN H CDNA (X78822,EMBL) KEYWDS OXIDOREDUCTASE, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 23 AUTHOR V.MITTARD,M.J.BLACKLEDGE,M.STEIN,J.-P.JACQUOT,D.MARION,J.-M.LANCELIN REVDAT 5 02-MAR-22 1TOF 1 REMARK REVDAT 4 24-FEB-09 1TOF 1 VERSN REVDAT 3 01-APR-03 1TOF 1 JRNL REVDAT 2 09-JUL-99 1TOF 1 JRNL REVDAT 1 07-DEC-96 1TOF 0 JRNL AUTH V.MITTARD,M.J.BLACKLEDGE,M.STEIN,J.P.JACQUOT,D.MARION, JRNL AUTH 2 J.M.LANCELIN JRNL TITL NMR SOLUTION STRUCTURE OF AN OXIDISED THIOREDOXIN H FROM THE JRNL TITL 2 EUKARYOTIC GREEN ALGA CHLAMYDOMONAS REINHARDTII. JRNL REF EUR.J.BIOCHEM. V. 243 374 1997 JRNL REFN ISSN 0014-2956 JRNL PMID 9030762 JRNL DOI 10.1111/J.1432-1033.1997.0374A.X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.STEIN,J.P.JACQUOT,E.JEANNETTE,P.DECOTTIGNIES,M.HODGES, REMARK 1 AUTH 2 J.M.LANCELIN,V.MITTARD,J.M.SCHMITTER,M.MIGINIAC-MASLOW REMARK 1 TITL CHLAMYDOMONAS REINHARDTII THIOREDOXINS: STRUCTURE OF THE REMARK 1 TITL 2 GENES CODING FOR THE CHLOROPLASTIC M AND CYTOSOLIC H REMARK 1 TITL 3 ISOFORMS; EXPRESSION IN ESCHERICHIA COLI OF THE RECOMBINANT REMARK 1 TITL 4 PROTEINS, PURIFICATION AND BIOCHEMICAL PROPERTIES REMARK 1 REF PLANT MOL.BIOL. V. 28 487 1995 REMARK 1 REFN ISSN 0167-4412 REMARK 1 REFERENCE 2 REMARK 1 AUTH V.MITTARD,N.MORELLE,B.BRUTSCHER,J.P.SIMORRE,D.MARION, REMARK 1 AUTH 2 M.STEIN,J.P.JACQUOT,P.N.LIRSAC,J.M.LANCELIN REMARK 1 TITL 1H, 13C, 15N-NMR RESONANCE ASSIGNMENTS OF OXIDIZED REMARK 1 TITL 2 THIOREDOXIN H FROM THE EUKARYOTIC GREEN ALGA CHLAMYDOMONAS REMARK 1 TITL 3 REINHARDTII USING NEW METHODS BASED ON TWO-DIMENSIONAL REMARK 1 TITL 4 TRIPLE-RESONANCE NMR SPECTROSCOPY AND COMPUTER-ASSISTED REMARK 1 TITL 5 BACKBONE ASSIGNMENT REMARK 1 REF EUR.J.BIOCHEM. V. 229 473 1995 REMARK 1 REFN ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TOF 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_1000176768. 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 : 23 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 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 5 CYS A 36 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 12 CYS A 36 CA - CB - SG ANGL. DEV. = 7.4 DEGREES REMARK 500 17 PRO A 38 C - N - CD ANGL. DEV. = -13.2 DEGREES REMARK 500 17 PRO A 38 CA - N - CD ANGL. DEV. = -10.0 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 1 VAL A 4 35.98 -78.60 REMARK 500 1 GLU A 23 -59.79 -15.05 REMARK 500 1 THR A 34 -70.11 -71.25 REMARK 500 1 PRO A 38 -39.44 -39.81 REMARK 500 1 ALA A 66 -62.31 -92.80 REMARK 500 1 THR A 77 -83.72 -136.00 REMARK 500 1 ASP A 87 -54.84 72.98 REMARK 500 1 LYS A 90 91.07 -46.73 REMARK 500 1 LEU A 94 114.83 -162.11 REMARK 500 1 SER A 98 50.41 35.11 REMARK 500 2 LYS A 21 63.10 62.92 REMARK 500 2 HIS A 24 19.23 -154.16 REMARK 500 2 ALA A 54 -125.44 36.05 REMARK 500 2 THR A 77 -74.92 -113.51 REMARK 500 2 LYS A 90 103.01 -60.00 REMARK 500 2 ALA A 97 46.16 -76.89 REMARK 500 3 ASP A 8 -38.33 -134.32 REMARK 500 3 GLU A 22 64.15 -67.91 REMARK 500 3 HIS A 24 72.81 68.04 REMARK 500 3 THR A 77 -78.95 -139.84 REMARK 500 3 ASP A 87 -59.81 67.00 REMARK 500 3 LYS A 90 98.64 -62.96 REMARK 500 3 ALA A 97 42.79 -78.62 REMARK 500 4 SER A 9 110.81 -14.13 REMARK 500 4 ALA A 18 -60.23 -106.19 REMARK 500 4 GLU A 22 43.36 -73.55 REMARK 500 4 THR A 32 -165.11 -116.14 REMARK 500 4 LYS A 56 38.45 -71.81 REMARK 500 4 ALA A 66 -61.42 -96.00 REMARK 500 4 THR A 77 -82.25 -136.75 REMARK 500 4 ASP A 87 -64.02 62.46 REMARK 500 4 LYS A 90 106.08 -57.51 REMARK 500 4 SER A 98 80.27 -157.59 REMARK 500 5 SER A 3 78.47 -68.06 REMARK 500 5 SER A 9 105.71 -37.12 REMARK 500 5 GLU A 23 -66.63 -22.57 REMARK 500 5 THR A 34 -47.99 -25.67 REMARK 500 5 ASP A 63 86.20 -69.90 REMARK 500 5 ALA A 66 -70.80 -84.78 REMARK 500 5 THR A 77 -71.41 -101.34 REMARK 500 5 ASP A 87 -63.12 67.26 REMARK 500 5 SER A 98 108.13 -163.85 REMARK 500 5 ALA A 111 -105.32 -91.31 REMARK 500 6 ASP A 8 56.13 -145.01 REMARK 500 6 LYS A 21 73.75 66.08 REMARK 500 6 GLU A 22 49.44 -71.06 REMARK 500 6 HIS A 24 24.61 -152.96 REMARK 500 6 PRO A 38 -37.82 -39.58 REMARK 500 6 ALA A 66 -75.32 -91.18 REMARK 500 6 THR A 77 -75.98 -93.21 REMARK 500 REMARK 500 THIS ENTRY HAS 240 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 PHE A 46 0.11 SIDE CHAIN REMARK 500 1 TYR A 85 0.08 SIDE CHAIN REMARK 500 2 PHE A 31 0.11 SIDE CHAIN REMARK 500 2 TYR A 85 0.08 SIDE CHAIN REMARK 500 3 PHE A 31 0.08 SIDE CHAIN REMARK 500 3 TYR A 53 0.11 SIDE CHAIN REMARK 500 3 TYR A 85 0.09 SIDE CHAIN REMARK 500 4 TYR A 53 0.14 SIDE CHAIN REMARK 500 5 PHE A 46 0.08 SIDE CHAIN REMARK 500 5 PHE A 59 0.09 SIDE CHAIN REMARK 500 6 PHE A 31 0.12 SIDE CHAIN REMARK 500 7 PHE A 31 0.07 SIDE CHAIN REMARK 500 7 PHE A 46 0.10 SIDE CHAIN REMARK 500 7 TYR A 53 0.14 SIDE CHAIN REMARK 500 7 TYR A 85 0.08 SIDE CHAIN REMARK 500 8 PHE A 59 0.13 SIDE CHAIN REMARK 500 9 PHE A 31 0.09 SIDE CHAIN REMARK 500 9 TYR A 53 0.08 SIDE CHAIN REMARK 500 9 PHE A 59 0.10 SIDE CHAIN REMARK 500 10 PHE A 31 0.12 SIDE CHAIN REMARK 500 10 PHE A 59 0.09 SIDE CHAIN REMARK 500 10 TYR A 85 0.08 SIDE CHAIN REMARK 500 11 PHE A 31 0.11 SIDE CHAIN REMARK 500 11 PHE A 46 0.08 SIDE CHAIN REMARK 500 11 TYR A 53 0.10 SIDE CHAIN REMARK 500 11 TYR A 85 0.07 SIDE CHAIN REMARK 500 12 PHE A 31 0.11 SIDE CHAIN REMARK 500 12 TYR A 53 0.16 SIDE CHAIN REMARK 500 12 PHE A 59 0.10 SIDE CHAIN REMARK 500 12 TYR A 85 0.10 SIDE CHAIN REMARK 500 13 PHE A 46 0.08 SIDE CHAIN REMARK 500 13 PHE A 82 0.08 SIDE CHAIN REMARK 500 14 PHE A 31 0.10 SIDE CHAIN REMARK 500 14 TYR A 53 0.12 SIDE CHAIN REMARK 500 14 TYR A 85 0.07 SIDE CHAIN REMARK 500 15 PHE A 31 0.09 SIDE CHAIN REMARK 500 15 TYR A 53 0.13 SIDE CHAIN REMARK 500 15 TYR A 85 0.09 SIDE CHAIN REMARK 500 16 PHE A 31 0.11 SIDE CHAIN REMARK 500 16 PHE A 46 0.10 SIDE CHAIN REMARK 500 16 PHE A 59 0.11 SIDE CHAIN REMARK 500 17 PHE A 59 0.09 SIDE CHAIN REMARK 500 17 TYR A 85 0.06 SIDE CHAIN REMARK 500 18 TYR A 85 0.07 SIDE CHAIN REMARK 500 19 PHE A 31 0.09 SIDE CHAIN REMARK 500 19 TYR A 53 0.09 SIDE CHAIN REMARK 500 20 PHE A 46 0.09 SIDE CHAIN REMARK 500 20 TYR A 85 0.09 SIDE CHAIN REMARK 500 21 PHE A 31 0.09 SIDE CHAIN REMARK 500 22 PHE A 31 0.11 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 53 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: ACT REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: SSBOND AT REDOX-ACTIVE CENTER. DBREF 1TOF A 1 112 UNP P80028 TRXH_CHLRE 1 112 SEQRES 1 A 112 GLY GLY SER VAL ILE VAL ILE ASP SER LYS ALA ALA TRP SEQRES 2 A 112 ASP ALA GLN LEU ALA LYS GLY LYS GLU GLU HIS LYS PRO SEQRES 3 A 112 ILE VAL VAL ASP PHE THR ALA THR TRP CYS GLY PRO CYS SEQRES 4 A 112 LYS MET ILE ALA PRO LEU PHE GLU THR LEU SER ASN ASP SEQRES 5 A 112 TYR ALA GLY LYS VAL ILE PHE LEU LYS VAL ASP VAL ASP SEQRES 6 A 112 ALA VAL ALA ALA VAL ALA GLU ALA ALA GLY ILE THR ALA SEQRES 7 A 112 MET PRO THR PHE HIS VAL TYR LYS ASP GLY VAL LYS ALA SEQRES 8 A 112 ASP ASP LEU VAL GLY ALA SER GLN ASP LYS LEU LYS ALA SEQRES 9 A 112 LEU VAL ALA LYS HIS ALA ALA ALA HELIX 1 1 LYS A 10 LYS A 19 1 10 HELIX 2 2 GLU A 22 HIS A 24 5 3 HELIX 3 3 GLY A 37 ASP A 52 5 16 HELIX 4 4 ALA A 68 ALA A 74 1 7 HELIX 5 5 GLN A 99 ALA A 110 1 12 SHEET 1 A 4 ILE A 58 ASP A 63 0 SHEET 2 A 4 ILE A 27 THR A 32 1 N VAL A 28 O ILE A 58 SHEET 3 A 4 THR A 81 VAL A 84 -1 N HIS A 83 O VAL A 29 SHEET 4 A 4 ASP A 92 VAL A 95 -1 N LEU A 94 O PHE A 82 SSBOND 1 CYS A 36 CYS A 39 1555 1555 2.08 CISPEP 1 MET A 79 PRO A 80 1 -0.41 CISPEP 2 MET A 79 PRO A 80 2 -0.54 CISPEP 3 MET A 79 PRO A 80 3 -1.30 CISPEP 4 MET A 79 PRO A 80 4 -1.10 CISPEP 5 MET A 79 PRO A 80 5 1.92 CISPEP 6 MET A 79 PRO A 80 6 0.82 CISPEP 7 MET A 79 PRO A 80 7 -2.15 CISPEP 8 MET A 79 PRO A 80 8 -3.33 CISPEP 9 MET A 79 PRO A 80 9 0.58 CISPEP 10 MET A 79 PRO A 80 10 -2.05 CISPEP 11 MET A 79 PRO A 80 11 -1.26 CISPEP 12 MET A 79 PRO A 80 12 -1.92 CISPEP 13 MET A 79 PRO A 80 13 0.01 CISPEP 14 MET A 79 PRO A 80 14 -3.60 CISPEP 15 MET A 79 PRO A 80 15 -0.85 CISPEP 16 MET A 79 PRO A 80 16 -2.02 CISPEP 17 MET A 79 PRO A 80 17 -1.14 CISPEP 18 MET A 79 PRO A 80 18 -1.07 CISPEP 19 MET A 79 PRO A 80 19 -2.71 CISPEP 20 MET A 79 PRO A 80 20 -1.79 CISPEP 21 MET A 79 PRO A 80 21 -0.61 CISPEP 22 MET A 79 PRO A 80 22 -1.66 CISPEP 23 MET A 79 PRO A 80 23 -1.01 SITE 1 ACT 5 TRP A 35 CYS A 36 GLY A 37 PRO A 38 SITE 2 ACT 5 CYS A 39 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