Header list of 1r1b.pdb file
Complete list - 2 202 Bytes
HEADER LIGASE 15-DEC-98 1R1B TITLE EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRNA SYNTHETASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1 - 59; COMPND 5 SYNONYM: TRNA LIGASE; COMPND 6 EC: 6.1.1.-; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS; SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER; SOURCE 4 ORGANISM_TAXID: 10029; SOURCE 5 ORGAN: OVARY CELLS; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS TRNA SYNTHETASE (LIGASE), PROTEIN TRANSCRIPTION, LIGASE EXPDTA SOLUTION NMR AUTHOR B.CAHUZAC,E.BERTHONNEAU,N.BIRLIRAKIS,M.MIRANDE,E.GUITTET REVDAT 4 02-MAR-22 1R1B 1 REMARK REVDAT 3 24-FEB-09 1R1B 1 VERSN REVDAT 2 24-MAY-00 1R1B 1 JRNL REVDAT 1 15-DEC-99 1R1B 0 JRNL AUTH B.CAHUZAC,E.BERTHONNEAU,N.BIRLIRAKIS,E.GUITTET,M.MIRANDE JRNL TITL A RECURRENT RNA-BINDING DOMAIN IS APPENDED TO EUKARYOTIC JRNL TITL 2 AMINOACYL-TRNA SYNTHETASES. JRNL REF EMBO J. V. 19 445 2000 JRNL REFN ISSN 0261-4189 JRNL PMID 10654942 JRNL DOI 10.1093/EMBOJ/19.3.445 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 1R1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-98. REMARK 100 THE DEPOSITION ID IS D_1000000291. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293.0 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA, X-PLOR 3.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: MINIMIZED AVERAGE STRUCTURE. THE STRUCTURE WAS DETERMINED REMARK 210 USING DOUBLE-- RESONANCE NMR SPECTROSCOPY ON A 15N-LABELED SAMPLE 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 RES C SSSEQI REMARK 465 HIS A 57 REMARK 465 HIS A 58 REMARK 465 HIS A 59 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 ASP A 4 -104.76 -69.28 REMARK 500 ALA A 8 -71.08 -36.68 REMARK 500 LYS A 20 100.67 75.02 REMARK 500 TYR A 40 -89.09 -53.47 REMARK 500 LYS A 41 48.33 31.10 REMARK 500 GLU A 42 -73.41 -75.10 REMARK 500 LYS A 43 41.44 -171.31 REMARK 500 THR A 44 -68.01 -135.30 REMARK 500 LYS A 46 102.94 62.62 REMARK 500 TYR A 48 145.95 -39.54 REMARK 500 LEU A 52 -76.12 -90.06 REMARK 500 HIS A 54 53.11 79.72 REMARK 500 REMARK 500 REMARK: NULL DBREF 1R1B A 3 51 UNP Q7SIA2 SYEP_CRIGR 1 49 SEQRES 1 A 59 MET VAL TYR ASP LYS ILE ALA ALA GLN GLY GLU VAL VAL SEQRES 2 A 59 ARG LYS LEU LYS ALA GLU LYS ALA PRO LYS ALA LYS VAL SEQRES 3 A 59 THR GLU ALA VAL GLU CYS LEU LEU SER LEU LYS ALA GLU SEQRES 4 A 59 TYR LYS GLU LYS THR GLY LYS GLU TYR VAL PRO GLY LEU SEQRES 5 A 59 GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 ASP A 4 GLU A 19 1 16 HELIX 2 2 LYS A 23 TYR A 40 1 18 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
Complete list - 2 202 Bytes