Header list of 1rip.pdb file
Complete list - 2 20 Bytes
HEADER RIBOSOMAL PROTEIN 17-AUG-93 1RIP TITLE RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL TITLE 2 STRUCTURE BY 1H-AND 15N-NMR COMPND MOL_ID: 1; COMPND 2 MOLECULE: RIBOSOMAL PROTEIN S17; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS; SOURCE 3 ORGANISM_TAXID: 1422 KEYWDS RIBOSOMAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 6 AUTHOR B.L.GOLDEN,D.W.HOFFMAN,V.RAMAKRISHNAN,S.W.WHITE REVDAT 3 02-MAR-22 1RIP 1 REMARK REVDAT 2 24-FEB-09 1RIP 1 VERSN REVDAT 1 31-OCT-93 1RIP 0 JRNL AUTH B.L.GOLDEN,D.W.HOFFMAN,V.RAMAKRISHNAN,S.W.WHITE JRNL TITL RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE JRNL TITL 2 THREE-DIMENSIONAL STRUCTURE BY 1H AND 15N NMR. JRNL REF BIOCHEMISTRY V. 32 12812 1993 JRNL REFN ISSN 0006-2960 JRNL PMID 8251502 JRNL DOI 10.1021/BI00210A033 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.HERZOG,M.YAGUCHI,T.CABEZON,M.-C.CORCHUELO,J.PETRE,A.BOLLEN REMARK 1 TITL A MISSENSE MUTATION IN THE GENE CODING FOR RIBOSOMAL PROTEIN REMARK 1 TITL 2 S17 (RPSQ) LEADING TO RIBOSOMAL ASSEMBLY DEFECTIVITY IN REMARK 1 TITL 3 ESCHERICHIA COLI REMARK 1 REF MOL.GEN.GENET. V. 171 15 1979 REMARK 1 REFN ISSN 0026-8925 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.YAGUCHI,H.G.WITTMANN,T.CABEZON,M.DEWILDE,R.VILLARROEL, REMARK 1 AUTH 2 A.HERZOG,A.BOLLEN REMARK 1 TITL ALTERATION OF RIBOSOMAL PROTEIN S17 BY MUTATION LINKED TO REMARK 1 TITL 2 NEAMINE RESISTANCE IN ESCHERICHIA COLI. II. LOCALIZATION OF REMARK 1 TITL 3 THE AMINO ACID REPLACEMENT IN PROTEIN S17 FROM A NEAA MUTANT REMARK 1 REF J.MOL.BIOL. V. 104 617 1976 REMARK 1 REFN ISSN 0022-2836 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: NULL REMARK 4 REMARK 4 1RIP 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_1000176100. 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 : 6 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 DBREF 1RIP A 5 84 UNP P23828 RS17_BACST 5 84 SEQRES 1 A 81 GLN ARG LYS VAL TYR VAL GLY ARG VAL VAL SER ASP LYS SEQRES 2 A 81 MET ASP LYS THR ILE THR VAL LEU VAL GLU THR TYR LYS SEQRES 3 A 81 LYS HIS PRO LEU TYR GLY LYS ARG VAL LYS TYR SER LYS SEQRES 4 A 81 LYS TYR LYS ALA HIS ASP GLU HIS ASN GLU ALA LYS VAL SEQRES 5 A 81 GLY ASP ILE VAL LYS ILE MET GLU THR ARG PRO LEU SER SEQRES 6 A 81 ALA THR LYS ARG PHE ARG LEU VAL GLU ILE VAL GLU LYS SEQRES 7 A 81 ALA VAL ARG SHEET 1 1 5 SER A 42 ASP A 49 0 SHEET 2 1 5 THR A 21 GLU A 27 -1 N VAL A 26 O LYS A 43 SHEET 3 1 5 VAL A 8 SER A 15 -1 O ARG A 12 N LEU A 25 SHEET 4 1 5 GLY A 57 THR A 65 -1 N ILE A 62 O TYR A 9 SHEET 5 1 5 PHE A 74 VAL A 80 -1 O ARG A 75 N MET A 63 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 - 2 20 Bytes