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 15312

Title: Solution structure of NusB from Aquifex Aeolicus   PubMed: 18177898

Authors: Das, Ranabir; Loss, Sandra; Li, Jess; Tarasov, Sergey; Wingfield, Paul; Waugh, David; Byrd, Robert; Altieri, Amanda

Citation: Das, Ranabir; Loss, Sandra; Li, Jess; Waugh, David; Tarasov, Sergey; Wingfield, Paul; Byrd, Robert; Altieri, Amanda. "Structural biophysics of the NusB:NusE antitermination complex"  J. Mol. Biol. 376, 705-720 (2008).

Assembly members:
NusB, polymer, 148 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: 63363   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Aquifex aeolicus

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

Entity Sequences (FASTA):
NusB: MRYRKGARDTAFLVLYRWDL RGENPGELFKEVVEEKNIKN KDAYEYAKKLVDTAVRHIEE IDSIIEKHLKGWSIDRLGYV ERNALRLGVAELIFLKSKEP GRVFIDIVDLVKKYADEKAG KFVNGVLSAIYKAYITSSKE EKPSLKSE

Data sets:
Data typeCount
13C chemical shifts656
15N chemical shifts143
1H chemical shifts1030

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Aquifex NusB monomer1

Entities:

Entity 1, Aquifex NusB monomer 148 residues - Formula weight is not available

1   METARGTYRARGLYSGLYALAARGASPTHR
2   ALAPHELEUVALLEUTYRARGTRPASPLEU
3   ARGGLYGLUASNPROGLYGLULEUPHELYS
4   GLUVALVALGLUGLULYSASNILELYSASN
5   LYSASPALATYRGLUTYRALALYSLYSLEU
6   VALASPTHRALAVALARGHISILEGLUGLU
7   ILEASPSERILEILEGLULYSHISLEULYS
8   GLYTRPSERILEASPARGLEUGLYTYRVAL
9   GLUARGASNALALEUARGLEUGLYVALALA
10   GLULEUILEPHELEULYSSERLYSGLUPRO
11   GLYARGVALPHEILEASPILEVALASPLEU
12   VALLYSLYSTYRALAASPGLULYSALAGLY
13   LYSPHEVALASNGLYVALLEUSERALAILE
14   TYRLYSALATYRILETHRSERSERLYSGLU
15   GLULYSPROSERLEULYSSERGLU

Samples:

sample_1: Aquifex NusB monomer, [U-13C; U-15N], 0.7 mM; potassium phosphate 50 mM; potassium chloride 200 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
4D 15N/13C NOESYsample_1isotropicsample_conditions_1
4D 13C/13C NOESYsample_1isotropicsample_conditions_1

Software:

ANSIG, Kraulis - chemical shift assignment

SPARKY, Goddard - peak picking

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

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