Header list of 1nz9.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 17-FEB-03 1NZ9 TITLE SOLUTION STRUCTURE OF THE N-UTILIZATION SUBSTANCE G (NUSG) C-TERMINAL TITLE 2 (NGC) DOMAIN FROM THERMUS THERMOPHILUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSCRIPTION ANTITERMINATION PROTEIN NUSG; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL (NGC) DOMAIN; COMPND 5 SYNONYM: N-UTILIZATION SUBSTANCE G; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS; SOURCE 3 ORGANISM_TAXID: 274; SOURCE 4 GENE: NUSG; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS TRANSCRIPTION ELONGATION, TERMINATION, ANTITERMINATION, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL KEYWDS 3 GENOMICS, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 31 AUTHOR P.REAY,K.YAMASAKI,T.TERADA,S.KURAMITSU,M.SHIROUZU,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 4 23-FEB-22 1NZ9 1 REMARK REVDAT 3 24-FEB-09 1NZ9 1 VERSN REVDAT 2 20-JUL-04 1NZ9 1 JRNL REVDAT 1 06-APR-04 1NZ9 0 JRNL AUTH P.REAY,K.YAMASAKI,T.TERADA,S.KURAMITSU,M.SHIROUZU,S.YOKOYAMA JRNL TITL STRUCTURAL AND SEQUENCE COMPARISONS ARISING FROM THE JRNL TITL 2 SOLUTION STRUCTURE OF THE TRANSCRIPTION ELONGATION FACTOR JRNL TITL 3 NUSG FROM THERMUS THERMOPHILUS JRNL REF PROTEINS V. 56 40 2004 JRNL REFN ISSN 0887-3585 JRNL PMID 15162485 JRNL DOI 10.1002/PROT.20054 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 566 UNAMBIGUOUS NOE DISTANCE REMARK 3 RESTRAINTS, 52 HYDROGEN BOND RESTRAINTS, 46 HN-N DIPOLAR REMARK 3 COUPLINGS, NO RESONANCES WERE ASSIGNED FOR ALA 127 REMARK 4 REMARK 4 1NZ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-FEB-03. REMARK 100 THE DEPOSITION ID IS D_1000018378. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 318 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : 50MM PHOSPAHTE, 100MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM NUSG C-DOMAIN, 50MM REMARK 210 PHOSPHATE BUFFER, 100MM KCL, 95% REMARK 210 H2O, 5% D2O; 2MM 15N NUSG C- REMARK 210 DOMAIN, 50MM PHOSPHATE BUFFER, REMARK 210 100MM KCL, 95% H2O, 5% D2O; 2MM REMARK 210 15N NUSG C-DOMAIN, 50MM REMARK 210 PHOSPHATE BUFFER, 100MM KCL, 100% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; HSQC; HMQC-J REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ANSIG 3.3, CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 90 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 31 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY, NONE WITH DISTANCE REMARK 210 VIOLATIONS > 0.2 ANGSTROMS, NONE REMARK 210 WITH DIHEDRAL ANGLE RESTRAINT REMARK 210 VIOLATIONS > 2 DEGREES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: MODEL 31 IS THE MINIMIZED AVERAGE STRUCTURE 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 O ASP A 177 H GLN A 180 1.59 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 SER A 141 -164.18 -160.43 REMARK 500 1 ALA A 145 39.69 -79.14 REMARK 500 1 ASP A 146 34.87 -160.70 REMARK 500 1 THR A 172 91.17 -160.02 REMARK 500 2 GLN A 128 158.81 60.51 REMARK 500 2 SER A 141 -164.69 -160.44 REMARK 500 2 ALA A 145 35.67 -82.38 REMARK 500 2 ASP A 146 35.63 -160.96 REMARK 500 2 THR A 152 -60.47 -105.22 REMARK 500 2 ARG A 158 -50.10 -160.08 REMARK 500 2 PHE A 168 79.43 43.52 REMARK 500 2 ARG A 170 109.21 -160.13 REMARK 500 3 SER A 141 -165.14 -160.11 REMARK 500 3 ALA A 145 36.87 -77.48 REMARK 500 3 ASP A 146 34.41 -161.05 REMARK 500 3 ARG A 158 -44.16 -160.07 REMARK 500 4 GLN A 128 74.57 60.07 REMARK 500 4 ALA A 145 50.71 -69.63 REMARK 500 4 ASP A 146 31.37 -160.61 REMARK 500 4 ARG A 158 -45.25 -159.96 REMARK 500 4 PHE A 168 -72.49 65.86 REMARK 500 4 THR A 172 81.30 -159.99 REMARK 500 4 LEU A 176 -158.96 -124.27 REMARK 500 5 ALA A 145 39.22 -80.42 REMARK 500 5 ASP A 146 31.57 -160.78 REMARK 500 5 THR A 152 -55.54 -137.55 REMARK 500 5 PHE A 168 76.86 -166.37 REMARK 500 5 THR A 172 84.21 -159.74 REMARK 500 6 GLN A 128 140.86 63.44 REMARK 500 6 SER A 141 -165.42 -160.22 REMARK 500 6 ALA A 145 38.44 -80.53 REMARK 500 6 ASP A 146 36.98 -161.03 REMARK 500 6 VAL A 151 105.95 -56.98 REMARK 500 7 VAL A 129 31.12 -98.64 REMARK 500 7 ASP A 135 -176.08 -57.91 REMARK 500 7 SER A 141 -163.50 -160.50 REMARK 500 7 ALA A 145 37.68 -79.53 REMARK 500 7 ASP A 146 32.05 -160.91 REMARK 500 7 ARG A 158 -45.17 -159.86 REMARK 500 7 LEU A 176 -159.18 -137.54 REMARK 500 8 ALA A 145 46.93 -69.82 REMARK 500 8 ASP A 146 32.19 -160.71 REMARK 500 8 ILE A 167 -66.83 -136.29 REMARK 500 8 PHE A 168 55.57 -91.46 REMARK 500 8 PRO A 173 83.37 -66.77 REMARK 500 9 ALA A 145 39.49 -67.82 REMARK 500 9 ASP A 146 31.23 -160.89 REMARK 500 9 ARG A 158 -60.16 -103.80 REMARK 500 10 GLN A 128 97.81 -166.32 REMARK 500 10 ALA A 145 47.63 -69.65 REMARK 500 REMARK 500 THIS ENTRY HAS 162 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1NZ8 RELATED DB: PDB REMARK 900 N-TERMINAL (NGN) DOMAIN REMARK 900 RELATED ID: TTK003000790.2 RELATED DB: TARGETDB DBREF 1NZ9 A 127 184 UNP P35872 NUSG_THET8 127 184 SEQRES 1 A 58 ALA GLN VAL ALA PHE ARG GLU GLY ASP GLN VAL ARG VAL SEQRES 2 A 58 VAL SER GLY PRO PHE ALA ASP PHE THR GLY THR VAL THR SEQRES 3 A 58 GLU ILE ASN PRO GLU ARG GLY LYS VAL LYS VAL MET VAL SEQRES 4 A 58 THR ILE PHE GLY ARG GLU THR PRO VAL GLU LEU ASP PHE SEQRES 5 A 58 SER GLN VAL VAL LYS ALA HELIX 1 1 PHE A 178 GLN A 180 5 3 SHEET 1 A 5 GLU A 171 LEU A 176 0 SHEET 2 A 5 LYS A 160 THR A 166 -1 N VAL A 161 O LEU A 176 SHEET 3 A 5 THR A 148 ASN A 155 -1 N GLU A 153 O LYS A 162 SHEET 4 A 5 GLN A 136 VAL A 139 -1 N VAL A 137 O GLY A 149 SHEET 5 A 5 VAL A 181 LYS A 183 -1 O VAL A 182 N ARG A 138 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 23 2 Bytes