Header list of 1doq.pdb file
Complete list - 16 20 Bytes
HEADER TRANSFERASE 21-DEC-99 1DOQ TITLE THE C-TERMINAL DOMAIN OF THE RNA POLYMERASE ALPHA SUBUNIT FROM THERMUS TITLE 2 THERMOPHILUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: RNA POLYMERASE ALPHA SUBUNIT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN; COMPND 5 EC: 2.7.7.-; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS; SOURCE 3 ORGANISM_TAXID: 274; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET15 KEYWDS TRANSCRIPTION, RNA POLYMERASE, THERMUS THERMOPHILUS, TRANSFERASE EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR T.WADA,T.YAMAZAKI,Y.KYOGOKU REVDAT 4 16-FEB-22 1DOQ 1 REMARK REVDAT 3 24-FEB-09 1DOQ 1 VERSN REVDAT 2 14-JUN-00 1DOQ 1 JRNL REVDAT 1 05-JAN-00 1DOQ 0 JRNL AUTH T.WADA,T.YAMAZAKI,Y.KYOGOKU JRNL TITL THE STRUCTURE AND THE CHARACTERISTIC DNA BINDING PROPERTY OF JRNL TITL 2 THE C-TERMINAL DOMAIN OF THE RNA POLYMERASE ALPHA SUBUNIT JRNL TITL 3 FROM THERMUS THERMOPHILUS. JRNL REF J.BIOL.CHEM. V. 275 16057 2000 JRNL REFN ISSN 0021-9258 JRNL PMID 10821859 JRNL DOI 10.1074/JBC.275.21.16057 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE REMARK 3 AUTHORS : BAX, A REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON 734 NOE-DERIVED DISTANCE CONSTRAINTS, REMARK 3 43 DIHEDRAL REMARK 3 ANGLE RESTRAINTS AND 38 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1DOQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-99. REMARK 100 THE DEPOSITION ID IS D_1000010251. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 30MM KCL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2MM C-TERMINAL DOMAIN OF RNA REMARK 210 POLYMERASE ALPHA SUBUNIT-15N, REMARK 210 13C; 20MM PHOSPHATE BUFFER, 30MM REMARK 210 KCL; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 GLU A 249 31.29 -177.55 REMARK 500 LEU A 252 111.98 59.57 REMARK 500 ASP A 253 62.21 -160.11 REMARK 500 SER A 268 -70.61 -52.07 REMARK 500 LYS A 270 -77.38 -48.21 REMARK 500 LEU A 283 89.86 -59.05 REMARK 500 ASN A 284 -172.00 -63.87 REMARK 500 ASP A 287 -57.60 -132.75 REMARK 500 THR A 312 -142.38 -106.23 REMARK 500 LEU A 313 -3.53 78.58 REMARK 500 LYS A 314 43.94 -150.48 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 ARG A 264 0.26 SIDE CHAIN REMARK 500 ARG A 278 0.17 SIDE CHAIN REMARK 500 ARG A 297 0.28 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1DOQ A 247 315 UNP Q9Z9H6 RPOA_THETH 247 315 SEQRES 1 A 69 GLU GLN GLU GLU GLU LEU ASP LEU PRO LEU GLU GLU LEU SEQRES 2 A 69 GLY LEU SER THR ARG VAL LEU HIS SER LEU LYS GLU GLU SEQRES 3 A 69 GLY ILE GLU SER VAL ARG ALA LEU LEU ALA LEU ASN LEU SEQRES 4 A 69 LYS ASP LEU LYS ASN ILE PRO GLY ILE GLY GLU ARG SER SEQRES 5 A 69 LEU GLU GLU ILE LYS GLU ALA LEU GLU LYS LYS GLY PHE SEQRES 6 A 69 THR LEU LYS GLU HELIX 1 1 PRO A 255 GLY A 260 1 6 HELIX 2 2 SER A 262 GLU A 272 1 11 HELIX 3 3 SER A 276 LEU A 283 1 8 HELIX 4 4 ASN A 284 LYS A 289 1 6 HELIX 5 5 GLY A 295 GLY A 310 1 16 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 - 16 20 Bytes