Header list of 2b6f.pdb file
Complete list - b 26 2 Bytes
HEADER OXIDOREDUCTASE 01-OCT-05 2B6F TITLE SOLUTION STRUCTURE OF HUMAN SULFIREDOXIN (SRX) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SULFIREDOXIN; COMPND 3 CHAIN: A; COMPND 4 EC: 1.18.-.-; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SRX, C20ORF139; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS PARB DOMAIN FOLD, OXIDOREDUCTASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.M.GRUSCHUS,D.-Y.LEE,J.A.FERRETTI,S.G.RHEE REVDAT 4 26-FEB-20 2B6F 1 REMARK LINK REVDAT 3 24-FEB-09 2B6F 1 VERSN REVDAT 2 13-FEB-07 2B6F 1 JRNL REVDAT 1 19-SEP-06 2B6F 0 JRNL AUTH D.-Y.LEE,S.J.PARK,W.JEONG,H.J.SUNG,T.OHO,X.WU,S.G.RHEE, JRNL AUTH 2 J.M.GRUSCHUS JRNL TITL MUTAGENESIS AND MODELING OF THE PEROXIREDOXIN (PRX) COMPLEX JRNL TITL 2 WITH THE NMR STRUCTURE OF ATP-BOUND HUMAN SULFIREDOXIN JRNL TITL 3 IMPLICATE ASPARTATE 187 OF PRX I AS THE CATALYTIC RESIDUE IN JRNL TITL 4 ATP HYDROLYSIS JRNL REF BIOCHEMISTRY V. 45 15301 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 17176052 JRNL DOI 10.1021/BI061824H REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.1, XPLOR-NIH 2.9.7, MACROMODEL 9.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), SCHWIETERS, KUSZEWSKI, TJANDRA, REMARK 3 CLORE, BRUNGER (XPLOR-NIH), SCHROEDINGER REMARK 3 (MACROMODEL) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2B6F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-05. REMARK 100 THE DEPOSITION ID IS D_1000034732. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 7.3 REMARK 210 IONIC STRENGTH : 50 MM PHOSPHATE; 100 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7MM SULFIREDOXIN U-15N,13C; REMARK 210 10MM ATP; 50MM PHOSPHATE, 100MM REMARK 210 NACL, 2MM DTT REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_SHORTCT_ALIPHATIC_NOESY; 3D_13C-SEPARATED_AROMATIC_ REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.3 REV 2004.184.22.03, REMARK 210 NMRDRAW 2.3 REV 2004.184.22.03 REMARK 210 METHOD USED : DISTANCE GEOMETRY FOLLOWED BY REMARK 210 SIMULATED ANNEALING; DOCKING REMARK 210 WITH RESTRAINED MD REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 HG SER A 64 HN61 ATP A 1 1.11 REMARK 500 OG SER A 64 HN61 ATP A 1 1.36 REMARK 500 O ASP A 135 HE21 GLN A 137 1.45 REMARK 500 H HIS A 100 O1G ATP A 1 1.48 REMARK 500 OD1 ASP A 58 H LYS A 61 1.49 REMARK 500 O LEU A 129 HG1 THR A 133 1.51 REMARK 500 O LEU A 129 H ALA A 131 1.54 REMARK 500 O THR A 68 H ASP A 72 1.57 REMARK 500 HE22 GLN A 119 O SER A 120 1.58 REMARK 500 H GLY A 98 O3G ATP A 1 1.59 REMARK 500 N GLY A 98 O3G ATP A 1 1.82 REMARK 500 OG SER A 64 N6 ATP A 1 2.14 REMARK 500 OG SER A 64 N1 ATP A 1 2.15 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 ALA A 18 60.38 -160.76 REMARK 500 1 PRO A 19 33.95 -75.69 REMARK 500 1 PRO A 22 -93.89 -75.38 REMARK 500 1 SER A 25 27.26 -161.30 REMARK 500 1 HIS A 34 -7.50 -169.50 REMARK 500 1 SER A 35 -94.65 -71.39 REMARK 500 1 PRO A 54 169.38 -49.11 REMARK 500 1 ALA A 131 -53.77 -154.86 REMARK 500 1 SER A 132 36.17 -99.12 REMARK 500 2 PRO A 22 175.77 -46.14 REMARK 500 2 GLN A 29 2.23 -153.20 REMARK 500 2 ARG A 37 148.18 -170.06 REMARK 500 2 PRO A 54 169.52 -48.02 REMARK 500 2 SER A 75 22.53 -71.85 REMARK 500 2 ALA A 131 -53.76 -155.37 REMARK 500 3 GLU A 20 -103.74 -166.49 REMARK 500 3 PRO A 54 169.19 -48.01 REMARK 500 3 LEU A 108 7.77 -67.61 REMARK 500 3 ALA A 131 -54.83 -153.62 REMARK 500 3 SER A 132 35.26 -99.86 REMARK 500 4 PRO A 19 127.09 -36.83 REMARK 500 4 SER A 25 37.37 -72.64 REMARK 500 4 GLN A 29 -105.14 -143.20 REMARK 500 4 HIS A 34 78.55 -170.02 REMARK 500 4 SER A 35 -22.40 -170.01 REMARK 500 4 ARG A 37 162.11 -49.65 REMARK 500 4 SER A 75 24.45 -71.96 REMARK 500 4 LEU A 108 9.31 -66.83 REMARK 500 4 ALA A 131 -58.05 -153.54 REMARK 500 4 SER A 132 36.94 -98.95 REMARK 500 5 PRO A 19 -161.98 -72.76 REMARK 500 5 PRO A 24 161.86 -46.11 REMARK 500 5 SER A 25 -165.48 -78.85 REMARK 500 5 SER A 35 -103.51 -74.22 REMARK 500 5 ARG A 37 96.17 -68.31 REMARK 500 5 PRO A 52 30.53 -97.43 REMARK 500 5 SER A 75 21.27 -77.90 REMARK 500 5 ALA A 131 -57.77 -153.60 REMARK 500 5 SER A 132 36.55 -98.72 REMARK 500 6 SER A 32 177.82 -50.60 REMARK 500 6 ILE A 33 -40.14 -169.84 REMARK 500 6 SER A 35 117.12 -170.03 REMARK 500 6 ARG A 37 146.70 -170.05 REMARK 500 6 PRO A 54 169.51 -48.64 REMARK 500 6 ALA A 131 -55.88 -154.65 REMARK 500 6 SER A 132 36.04 -99.84 REMARK 500 7 GLU A 20 37.17 -75.04 REMARK 500 7 SER A 25 -22.37 -169.09 REMARK 500 7 ALA A 131 -54.93 -155.39 REMARK 500 8 PRO A 19 159.97 -36.79 REMARK 500 REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1YZS RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF HUMAN SULFIREDOXIN (SRX) DBREF 2B6F A 17 137 UNP Q9BYN0 SRXN1_HUMAN 17 137 SEQRES 1 A 121 GLY ALA PRO GLU GLY PRO GLY PRO SER GLY GLY ALA GLN SEQRES 2 A 121 GLY GLY SER ILE HIS SER GLY ARG ILE ALA ALA VAL HIS SEQRES 3 A 121 ASN VAL PRO LEU SER VAL LEU ILE ARG PRO LEU PRO SER SEQRES 4 A 121 VAL LEU ASP PRO ALA LYS VAL GLN SER LEU VAL ASP THR SEQRES 5 A 121 ILE ARG GLU ASP PRO ASP SER VAL PRO PRO ILE ASP VAL SEQRES 6 A 121 LEU TRP ILE LYS GLY ALA GLN GLY GLY ASP TYR PHE TYR SEQRES 7 A 121 SER PHE GLY GLY CYS HIS ARG TYR ALA ALA TYR GLN GLN SEQRES 8 A 121 LEU GLN ARG GLU THR ILE PRO ALA LYS LEU VAL GLN SER SEQRES 9 A 121 THR LEU SER ASP LEU ARG VAL TYR LEU GLY ALA SER THR SEQRES 10 A 121 PRO ASP LEU GLN HET MG A 2 1 HET ATP A 1 43 HETNAM MG MAGNESIUM ION HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE FORMUL 2 MG MG 2+ FORMUL 3 ATP C10 H16 N5 O13 P3 HELIX 1 1 ASP A 58 ASP A 72 1 15 HELIX 2 2 GLY A 98 LEU A 108 1 11 HELIX 3 3 THR A 121 GLY A 130 1 10 SHEET 1 A 5 VAL A 41 PRO A 45 0 SHEET 2 A 5 THR A 112 GLN A 119 -1 O ALA A 115 N HIS A 42 SHEET 3 A 5 ILE A 79 LYS A 85 1 N ILE A 79 O LYS A 116 SHEET 4 A 5 ASP A 91 SER A 95 -1 O TYR A 92 N ILE A 84 SHEET 5 A 5 LEU A 49 ILE A 50 1 N ILE A 50 O SER A 95 SITE 1 AC1 8 LYS A 61 SER A 64 THR A 68 GLY A 97 SITE 2 AC1 8 GLY A 98 CYS A 99 HIS A 100 ARG A 101 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 - b 26 2 Bytes