BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16153

Title: Structure of the transcription repressor SvtR08 (gp08) from the hyperthermophilic archaeal virus SIRV1   PubMed: 19535331

Authors: Guilliere, Florence; Kessler, Alexandra; Peixeiro, Nuno; Sezonov, Guennadi; Prangishvili, David; Delepierre, Muriel; Guijarro, J. Inaki

Citation: Guilliere, Florence; Peixeiro, Nuno; Kessler, Alexandra; Raynal, Bertrand; Desnoues, Nicole; Keller, Jenny; Delepierre, Muriel; Prangishvili, David; Sezonov, Guennadi; Guijarro, J. Inaki. "Structure, function and targets of the transcriptional regulator SvtR from the hyperthermophilic archaeal virus SIRV1."  J. Biol. Chem. 284, 22222-22237 (2009).

Assembly members:
svtr08, polymer, 56 residues, 6620.74 Da.

Natural source:   Common Name: Sulfolobus virus SIRV1   Taxonomy ID: 157898   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
svtr08: MQTQEQSQKKKQKAVFGIYM DKDLKTRLKVYCAKNNLQLT QAIEEAIKEYLQKRNG

Data sets:
Data typeCount
13C chemical shifts261
15N chemical shifts64
1H chemical shifts425

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 56 residues - 6620.74 Da.

Residues 1-12 are disordered. Only coordinates for residues 11-56 are included. Final structures were calculated with data for residues 11-56

1   METGLNTHRGLNGLUGLNSERGLNLYSLYS
2   LYSGLNLYSALAVALPHEGLYILETYRMET
3   ASPLYSASPLEULYSTHRARGLEULYSVAL
4   TYRCYSALALYSASNASNLEUGLNLEUTHR
5   GLNALAILEGLUGLUALAILELYSGLUTYR
6   LEUGLNLYSARGASNGLY

Samples:

sample_1: svtr08 1.6 mM; sodium acetate, [U-2H], 20 mM; D2O 10%; H2O 90%

sample_2: svtr08 1.2 mM; sodium acetate, [U-2H], 20 mM; D2O 100%

sample_3: svtr08, [U-98% 13C; U-98% 15N], 1.5 mM; sodium acetate, [U-2H], 20 mM; D2O 12%; H2O 88%

sample_4: svtr08, 50%[U-98% 13C; U-98% 15N]; 50% natural abundance, 2.9 mM; sodium acetate, [U-2H], 20 mM; D2O 12%; H2O 88%

sample_5: svtr08, [U-98% 15N], 1.7 mM; sodium acetate, [U-2H], 20 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 5.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D DOUBLY-FILTERED 1H-13C NOESYsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_5isotropicsample_conditions_1

Software:

ARIA v2.2, Linge, O, . - nOe assignment, structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

VNMRJ v2.1B, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

ProcheckNMR v3.4, Laskowski and MacArthur - data analysis

WhatIF, Vriend - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
EMBL CAC93963 CAG38828
REF NP_666596
SP Q8QL46