Header list of 1xfl.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 15-SEP-04 1XFL TITLE SOLUTION STRUCTURE OF THIOREDOXIN H1 FROM ARABIDOPSIS THALIANA COMPND MOL_ID: 1; COMPND 2 MOLECULE: THIOREDOXIN H1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: TRXH1, TRX-H-1, THIOREDOXIN H-TYPE 1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: AT3G51030; SOURCE 6 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEU(N)HIS6-AT3G51030; SOURCE 9 OTHER_DETAILS: WHEAT GERM CELL-FREE, IN VITRO EXPRESSION KEYWDS AT3G51030, THIOREDOXIN, STRUCTURAL GENOMICS, PROTEIN STRUCTURE KEYWDS 2 INITIATIVE, CESG, PSI, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, KEYWDS 3 ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.C.PETERSON,B.L.LYTLE,S.SAMPATH,D.VINAROV,E.TYLER,M.SHAHAN, AUTHOR 2 J.L.MARKLEY,B.F.VOLKMAN,CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS AUTHOR 3 (CESG) REVDAT 10 02-MAR-22 1XFL 1 REMARK SEQADV REVDAT 9 24-FEB-09 1XFL 1 VERSN REVDAT 8 29-APR-08 1XFL 1 SOURCE REVDAT 7 12-FEB-08 1XFL 1 REMARK REVDAT 6 09-AUG-05 1XFL 1 JRNL REVDAT 5 01-FEB-05 1XFL 1 AUTHOR KEYWDS REMARK REVDAT 4 09-NOV-04 1XFL 1 AUTHOR REVDAT 3 26-OCT-04 1XFL 1 JRNL REVDAT 2 19-OCT-04 1XFL 1 JRNL REVDAT 1 28-SEP-04 1XFL 0 JRNL AUTH F.C.PETERSON,B.L.LYTLE,S.SAMPATH,D.VINAROV,E.TYLER,M.SHAHAN, JRNL AUTH 2 J.L.MARKLEY,B.F.VOLKMAN JRNL TITL SOLUTION STRUCTURE OF THIOREDOXIN H1 FROM ARABIDOPSIS JRNL TITL 2 THALIANA. JRNL REF PROTEIN SCI. V. 14 2195 2005 JRNL REFN ISSN 0961-8368 JRNL PMID 15987893 JRNL DOI 10.1110/PS.051477905 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 1.0.6, XPLOR-NIH 2.0.6 REMARK 3 AUTHORS : GUENTERT (CYANA), CLORE (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: INITIAL STRUCTURES WERE GENERATED USING REMARK 3 THE CANDID MODULE OF CYANA. ADDITIONAL NOE ASSIGNMENTS WERE REMARK 3 DETERMINED MANUALLY. PHI AND PSI TORSION ANGLE CONSTRAINTS WERE REMARK 3 GENERATED FROM CHEMICAL SHIFT DATABASE SEARCHING USING THE REMARK 3 PROGRAM TALOS (G. CORNILESCU). REMARK 4 REMARK 4 1XFL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-04. REMARK 100 THE DEPOSITION ID IS D_1000030306. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : 50 MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM U-15N,13C AT3G51030;10MM REMARK 210 PHOSPHATE BUFFER; 50MM KCL; 90% REMARK 210 H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_ 13C REMARK 210 -SEPARATED_NOESY; 3D 13C- REMARK 210 SEPARATED NOESY-AROMATIC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.1, NMRPIPE 2.1, XEASY REMARK 210 1.3.1, SPSCAN 1.1.0 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED REMARK 210 BY CARTESIAN MOLECULAR DYNAMICS REMARK 210 IN EXPLICIT SOLVENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: CHEMICAL SHIFT ASSIGNMENTS WERE OBTAINED FROM STANDARD 3D REMARK 210 TRIPLE-RESONANCE EXPERIMENTS, USING THE AUTOMATED METHOD OF REMARK 210 GARANT (CHRISTIAN BARTELS). 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A -9 REMARK 465 GLY A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 LEU A -1 REMARK 465 GLU A 0 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 OD2 ASP A 34 HZ2 LYS A 64 1.53 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 LEU A 70 62.45 -105.55 REMARK 500 1 ALA A 78 64.20 62.14 REMARK 500 2 LEU A 70 46.09 -94.51 REMARK 500 2 GLN A 80 -31.26 -132.48 REMARK 500 2 LEU A 94 -64.29 -106.95 REMARK 500 3 SER A 3 -169.59 -113.13 REMARK 500 3 LEU A 94 -70.44 -96.37 REMARK 500 5 ASN A 59 73.12 -170.50 REMARK 500 5 GLN A 80 -41.25 -137.71 REMARK 500 5 LEU A 94 -65.18 -106.40 REMARK 500 6 ALA A 2 -157.89 -91.45 REMARK 500 6 SER A 3 159.45 78.82 REMARK 500 6 GLU A 5 -168.12 -79.30 REMARK 500 6 LEU A 70 50.04 -95.62 REMARK 500 7 LEU A 70 49.10 -80.62 REMARK 500 7 LEU A 94 -67.76 -101.55 REMARK 500 8 GLU A 4 14.42 -142.04 REMARK 500 8 ASN A 59 84.60 -166.35 REMARK 500 8 ALA A 78 86.66 61.20 REMARK 500 9 SER A 3 -170.15 72.03 REMARK 500 10 ALA A 2 91.60 76.27 REMARK 500 10 LEU A 70 47.46 -84.15 REMARK 500 10 LEU A 94 -66.99 -104.16 REMARK 500 11 GLU A 5 -173.84 62.90 REMARK 500 11 ALA A 78 71.57 64.47 REMARK 500 12 GLU A 4 -79.68 -97.35 REMARK 500 12 GLU A 5 -169.47 53.66 REMARK 500 12 LEU A 70 69.11 -106.40 REMARK 500 12 LEU A 94 -61.46 -104.69 REMARK 500 13 LEU A 94 -64.72 -104.68 REMARK 500 14 ALA A 78 72.93 56.22 REMARK 500 14 LEU A 94 -64.32 -107.48 REMARK 500 15 SER A 3 -165.08 62.88 REMARK 500 15 GLU A 4 -82.65 -105.25 REMARK 500 15 GLU A 5 -166.22 52.27 REMARK 500 16 LEU A 70 58.77 -93.58 REMARK 500 17 SER A 3 103.08 -52.61 REMARK 500 17 LEU A 70 66.30 -108.68 REMARK 500 17 ALA A 78 74.43 53.12 REMARK 500 18 GLU A 4 -74.36 -121.96 REMARK 500 18 GLU A 5 140.96 63.96 REMARK 500 19 SER A 3 84.45 -68.97 REMARK 500 19 GLU A 5 159.77 55.24 REMARK 500 19 LEU A 70 46.25 -98.26 REMARK 500 19 LEU A 94 -61.00 -103.63 REMARK 500 20 LEU A 70 58.13 -96.89 REMARK 500 20 GLN A 80 -28.33 -149.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GO.14751 RELATED DB: TARGETDB DBREF 1XFL A 1 114 UNP P29448 TRXH1_ARATH 1 114 SEQADV 1XFL MET A -9 UNP P29448 INITIATING METHIONINE SEQADV 1XFL GLY A -8 UNP P29448 EXPRESSION TAG SEQADV 1XFL HIS A -7 UNP P29448 EXPRESSION TAG SEQADV 1XFL HIS A -6 UNP P29448 EXPRESSION TAG SEQADV 1XFL HIS A -5 UNP P29448 EXPRESSION TAG SEQADV 1XFL HIS A -4 UNP P29448 EXPRESSION TAG SEQADV 1XFL HIS A -3 UNP P29448 EXPRESSION TAG SEQADV 1XFL HIS A -2 UNP P29448 EXPRESSION TAG SEQADV 1XFL LEU A -1 UNP P29448 EXPRESSION TAG SEQADV 1XFL GLU A 0 UNP P29448 EXPRESSION TAG SEQRES 1 A 124 MET GLY HIS HIS HIS HIS HIS HIS LEU GLU MET ALA SER SEQRES 2 A 124 GLU GLU GLY GLN VAL ILE ALA CYS HIS THR VAL GLU THR SEQRES 3 A 124 TRP ASN GLU GLN LEU GLN LYS ALA ASN GLU SER LYS THR SEQRES 4 A 124 LEU VAL VAL VAL ASP PHE THR ALA SER TRP CYS GLY PRO SEQRES 5 A 124 CYS ARG PHE ILE ALA PRO PHE PHE ALA ASP LEU ALA LYS SEQRES 6 A 124 LYS LEU PRO ASN VAL LEU PHE LEU LYS VAL ASP THR ASP SEQRES 7 A 124 GLU LEU LYS SER VAL ALA SER ASP TRP ALA ILE GLN ALA SEQRES 8 A 124 MET PRO THR PHE MET PHE LEU LYS GLU GLY LYS ILE LEU SEQRES 9 A 124 ASP LYS VAL VAL GLY ALA LYS LYS ASP GLU LEU GLN SER SEQRES 10 A 124 THR ILE ALA LYS HIS LEU ALA HELIX 1 1 THR A 13 SER A 27 1 15 HELIX 2 2 CYS A 40 LEU A 57 1 18 HELIX 3 3 LEU A 70 TRP A 77 1 8 HELIX 4 4 LYS A 101 LEU A 113 1 13 SHEET 1 A 5 ILE A 9 CYS A 11 0 SHEET 2 A 5 VAL A 60 ASP A 66 1 O PHE A 62 N ILE A 9 SHEET 3 A 5 LEU A 30 THR A 36 1 N ASP A 34 O VAL A 65 SHEET 4 A 5 THR A 84 LYS A 89 -1 O MET A 86 N VAL A 33 SHEET 5 A 5 LYS A 92 VAL A 98 -1 O LYS A 92 N LYS A 89 SSBOND 1 CYS A 40 CYS A 43 1555 1555 2.04 CISPEP 1 MET A 82 PRO A 83 1 -1.76 CISPEP 2 MET A 82 PRO A 83 2 -1.35 CISPEP 3 MET A 82 PRO A 83 3 0.87 CISPEP 4 MET A 82 PRO A 83 4 -3.21 CISPEP 5 MET A 82 PRO A 83 5 -3.96 CISPEP 6 MET A 82 PRO A 83 6 -4.90 CISPEP 7 MET A 82 PRO A 83 7 -3.17 CISPEP 8 MET A 82 PRO A 83 8 -0.83 CISPEP 9 MET A 82 PRO A 83 9 -0.36 CISPEP 10 MET A 82 PRO A 83 10 -2.18 CISPEP 11 MET A 82 PRO A 83 11 -0.87 CISPEP 12 MET A 82 PRO A 83 12 -2.51 CISPEP 13 MET A 82 PRO A 83 13 0.62 CISPEP 14 MET A 82 PRO A 83 14 -0.97 CISPEP 15 MET A 82 PRO A 83 15 -3.42 CISPEP 16 MET A 82 PRO A 83 16 -4.03 CISPEP 17 MET A 82 PRO A 83 17 -0.12 CISPEP 18 MET A 82 PRO A 83 18 -4.00 CISPEP 19 MET A 82 PRO A 83 19 -0.49 CISPEP 20 MET A 82 PRO A 83 20 -2.03 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