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 18316

Title: Solution structure of the C-terminal domain of the MgtC protein from Mycobacterium tuberculosis   PubMed: 22984256

Deposition date: 2012-03-07 Original release date: 2012-04-11

Authors: Yang, Martin; Yang, Yishan; Labesse, Gilles; Blanc-Potard, Anne

Citation: Yang, Yinshan; Labesse, Gilles; Carrere-Kremer, Severine; Esteves, Kevin; Kremer, Laurent; Cohen-Gonsaud, Martin; Blanc-Potard, Anne-Beatrice. "The C-terminal domain of the virulence factor MgtC is a divergent ACT domain."  J. Bacteriol. 194, 6255-6263 (2012).

Assembly members:
entity, polymer, 94 residues, 10414.866 Da.

Natural source:   Common Name: High GC Gram +   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

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

Entity Sequences (FASTA):
entity: VEDEGLQPYQVRVICRPKAE TYVRAHIVQRTSSNDITLRG IRTGPAGDDNITLTAHLLMV GHTPAKLERLVAELSLQPGV YAVHWYAGEHAQAE

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts89
1H chemical shifts190

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal domain of the MgtC protein1

Entities:

Entity 1, C-terminal domain of the MgtC protein 94 residues - 10414.866 Da.

1   VALGLUASPGLUGLYLEUGLNPROTYRGLN
2   VALARGVALILECYSARGPROLYSALAGLU
3   THRTYRVALARGALAHISILEVALGLNARG
4   THRSERSERASNASPILETHRLEUARGGLY
5   ILEARGTHRGLYPROALAGLYASPASPASN
6   ILETHRLEUTHRALAHISLEULEUMETVAL
7   GLYHISTHRPROALALYSLEUGLUARGLEU
8   VALALAGLULEUSERLEUGLNPROGLYVAL
9   TYRALAVALHISTRPTYRALAGLYGLUHIS
10   ALAGLNALAGLU

Samples:

sample_1: entity, [U-100% 15N], 0.3 mM; H20 90%; D20 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 0.3 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 0.11 M; pH: 4.6; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAH26116 BAL65794 BAQ05835 GAA45520
EMBL CAL71832 CCC26903 CCC44159 CCC64414 CCE37295
GB AAK46132 ABQ73578 ABR06176 ACT25251 AEB04323
REF NP_216327 NP_855493 WP_003409190 WP_003899032 WP_003900414

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts