Header list of 2sob.pdb file
Complete list - v 3 2 Bytes
HEADER HYDROLASE (PHOSPHORIC DIESTER) 15-SEP-95 2SOB TITLE SN-OB, OB-FOLD SUB-DOMAIN OF STAPHYLOCOCCAL NUCLEASE, NMR, 10 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: STAPHYLOCOCCAL NUCLEASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SN-OB, STAPHYLOCOCCAL NUCLEASE OB-SUBDOMAIN; COMPND 5 EC: 3.1.31.1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: 1 - 103 FRAGMENT OF THE 149 AMINO ACID STAPHYLOCOCCAL COMPND 9 NUCLEASE CONTAINING THE "GLOBAL SUPPRESSOR" MUTATIONS V66L AND G88V SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 STRAIN: FOGGI; SOURCE 5 ATCC: 27355; SOURCE 6 GENE: STAPHYLOCOCCAL NUCLEASE; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A T7; SOURCE 10 EXPRESSION_SYSTEM_GENE: STAPHYLOCOCCAL NUCLEASE MUTANT/FRAGMENT KEYWDS HYDROLASE (PHOSPHORIC DIESTER) EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR A.T.ALEXANDRESCU,A.G.GITTIS,C.ABEYGUNAWARDANA,D.SHORTLE REVDAT 4 03-NOV-21 2SOB 1 REMARK SEQADV REVDAT 3 24-FEB-09 2SOB 1 VERSN REVDAT 2 01-APR-03 2SOB 1 JRNL REVDAT 1 07-DEC-95 2SOB 0 SPRSDE 07-DEC-95 2SOB 1SOB JRNL AUTH A.T.ALEXANDRESCU,A.G.GITTIS,C.ABEYGUNAWARDANA,D.SHORTLE JRNL TITL NMR STRUCTURE OF A STABLE "OB-FOLD" SUB-DOMAIN ISOLATED FROM JRNL TITL 2 STAPHYLOCOCCAL NUCLEASE. JRNL REF J.MOL.BIOL. V. 250 134 1995 JRNL REFN ISSN 0022-2836 JRNL PMID 7608966 JRNL DOI 10.1006/JMBI.1995.0365 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.SHORTLE,C.ABEYGUNAWARDANA REMARK 1 TITL NMR ANALYSIS OF THE RESIDUAL STRUCTURE IN THE DENATURED REMARK 1 TITL 2 STATE OF AN UNUSUAL MUTANT OF STAPHYLOCOCCAL NUCLEASE REMARK 1 REF STRUCTURE V. 1 121 1993 REMARK 1 REFN ISSN 0969-2126 REMARK 1 REFERENCE 2 REMARK 1 AUTH D.SHORTLE,A.K.MEEKER REMARK 1 TITL RESIDUAL STRUCTURE IN LARGE FRAGMENTS OF STAPHYLOCOCCAL REMARK 1 TITL 2 NUCLEASE: EFFECTS OF AMINO ACID SUBSTITUTION REMARK 1 REF BIOCHEMISTRY V. 28 936 1989 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2SOB 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_1000178640. 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 : 10 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: 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 LYS A 6 -37.97 -174.98 REMARK 500 1 LEU A 7 125.64 75.28 REMARK 500 1 HIS A 8 -133.13 -81.47 REMARK 500 1 LYS A 9 133.57 -176.38 REMARK 500 1 ALA A 12 -156.17 -142.50 REMARK 500 1 LYS A 16 109.32 -175.39 REMARK 500 1 ASP A 19 -158.84 -146.64 REMARK 500 1 MET A 32 -159.92 -141.15 REMARK 500 1 LEU A 36 -82.71 67.24 REMARK 500 1 LEU A 38 126.57 71.34 REMARK 500 1 VAL A 39 -156.65 -63.48 REMARK 500 1 ASP A 40 54.08 -151.72 REMARK 500 1 THR A 44 111.95 65.32 REMARK 500 1 PRO A 56 -157.89 -63.45 REMARK 500 1 GLU A 57 -80.71 -78.00 REMARK 500 1 LEU A 66 -28.96 178.15 REMARK 500 1 GLU A 73 59.94 -147.74 REMARK 500 1 VAL A 74 105.79 -42.34 REMARK 500 1 ASP A 83 -94.04 -166.65 REMARK 500 1 ASP A 95 82.52 47.91 REMARK 500 1 LYS A 97 126.11 71.87 REMARK 500 1 VAL A 99 4.18 59.97 REMARK 500 2 SER A 3 35.71 -160.36 REMARK 500 2 LYS A 5 30.90 75.11 REMARK 500 2 LYS A 6 -82.52 -154.14 REMARK 500 2 GLU A 10 113.31 -160.65 REMARK 500 2 ALA A 12 -152.66 -110.58 REMARK 500 2 LYS A 16 161.83 177.83 REMARK 500 2 ASP A 19 144.64 76.50 REMARK 500 2 MET A 32 -167.53 -110.83 REMARK 500 2 LEU A 36 -54.97 160.32 REMARK 500 2 LEU A 38 -70.63 -76.73 REMARK 500 2 ASP A 40 35.70 -99.11 REMARK 500 2 GLU A 43 32.97 -167.86 REMARK 500 2 THR A 44 58.00 -153.14 REMARK 500 2 PRO A 47 39.40 -74.20 REMARK 500 2 LYS A 48 -170.31 57.68 REMARK 500 2 LYS A 53 110.11 -160.43 REMARK 500 2 PRO A 56 -163.40 -71.18 REMARK 500 2 ASN A 68 -32.60 -155.02 REMARK 500 2 ASP A 77 -50.58 -155.96 REMARK 500 2 LYS A 78 94.55 -53.36 REMARK 500 2 GLN A 80 48.58 -82.28 REMARK 500 2 ASP A 83 49.37 -162.50 REMARK 500 2 LYS A 84 63.29 -152.81 REMARK 500 2 TYR A 85 -33.58 87.97 REMARK 500 2 ARG A 87 146.73 74.49 REMARK 500 2 LEU A 89 88.98 -50.38 REMARK 500 2 LYS A 97 -91.78 56.52 REMARK 500 2 MET A 98 -40.25 170.94 REMARK 500 REMARK 500 THIS ENTRY HAS 266 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 ARG A 35 0.26 SIDE CHAIN REMARK 500 1 ARG A 81 0.32 SIDE CHAIN REMARK 500 1 ARG A 87 0.21 SIDE CHAIN REMARK 500 2 ARG A 35 0.27 SIDE CHAIN REMARK 500 2 ARG A 81 0.32 SIDE CHAIN REMARK 500 2 ARG A 87 0.31 SIDE CHAIN REMARK 500 3 ARG A 35 0.30 SIDE CHAIN REMARK 500 3 ARG A 81 0.31 SIDE CHAIN REMARK 500 3 ARG A 87 0.30 SIDE CHAIN REMARK 500 4 ARG A 35 0.28 SIDE CHAIN REMARK 500 4 ARG A 81 0.30 SIDE CHAIN REMARK 500 4 ARG A 87 0.23 SIDE CHAIN REMARK 500 5 ARG A 35 0.17 SIDE CHAIN REMARK 500 5 ARG A 81 0.31 SIDE CHAIN REMARK 500 5 ARG A 87 0.28 SIDE CHAIN REMARK 500 6 ARG A 35 0.30 SIDE CHAIN REMARK 500 6 ARG A 81 0.32 SIDE CHAIN REMARK 500 6 ARG A 87 0.32 SIDE CHAIN REMARK 500 7 ARG A 35 0.29 SIDE CHAIN REMARK 500 7 ARG A 81 0.31 SIDE CHAIN REMARK 500 7 ARG A 87 0.31 SIDE CHAIN REMARK 500 8 ARG A 35 0.32 SIDE CHAIN REMARK 500 8 ARG A 81 0.32 SIDE CHAIN REMARK 500 8 ARG A 87 0.28 SIDE CHAIN REMARK 500 9 ARG A 35 0.18 SIDE CHAIN REMARK 500 9 ARG A 81 0.31 SIDE CHAIN REMARK 500 9 ARG A 87 0.28 SIDE CHAIN REMARK 500 10 ARG A 35 0.27 SIDE CHAIN REMARK 500 10 ARG A 81 0.32 SIDE CHAIN REMARK 500 10 ARG A 87 0.24 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 2SOB A 1 103 UNP P00644 NUC_STAAU 83 185 SEQADV 2SOB LEU A 66 UNP P00644 VAL 148 ENGINEERED MUTATION SEQADV 2SOB VAL A 88 UNP P00644 GLY 170 ENGINEERED MUTATION SEQRES 1 A 103 ALA THR SER THR LYS LYS LEU HIS LYS GLU PRO ALA THR SEQRES 2 A 103 LEU ILE LYS ALA ILE ASP GLY ASP THR VAL LYS LEU MET SEQRES 3 A 103 TYR LYS GLY GLN PRO MET THR PHE ARG LEU LEU LEU VAL SEQRES 4 A 103 ASP THR PRO GLU THR LYS HIS PRO LYS LYS GLY VAL GLU SEQRES 5 A 103 LYS TYR GLY PRO GLU ALA SER ALA PHE THR LYS LYS MET SEQRES 6 A 103 LEU GLU ASN ALA LYS LYS ILE GLU VAL GLU PHE ASP LYS SEQRES 7 A 103 GLY GLN ARG THR ASP LYS TYR GLY ARG VAL LEU ALA TYR SEQRES 8 A 103 ILE TYR ALA ASP GLY LYS MET VAL ASN GLU ALA LEU HELIX 1 1 ALA A 58 GLU A 67 1 10 SHEET 1 A 2 VAL A 23 MET A 26 0 SHEET 2 A 2 PRO A 31 PHE A 34 -1 N PHE A 34 O VAL A 23 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 - v 3 2 Bytes