BMRB Entry 18316
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18316
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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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 264 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 190 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C-terminal domain of the MgtC protein | 1 |
Entities:
Entity 1, C-terminal domain of the MgtC protein 94 residues - 10414.866 Da.
| 1 | VAL | GLU | ASP | GLU | GLY | LEU | GLN | PRO | TYR | GLN | ||||
| 2 | VAL | ARG | VAL | ILE | CYS | ARG | PRO | LYS | ALA | GLU | ||||
| 3 | THR | TYR | VAL | ARG | ALA | HIS | ILE | VAL | GLN | ARG | ||||
| 4 | THR | SER | SER | ASN | ASP | ILE | THR | LEU | ARG | GLY | ||||
| 5 | ILE | ARG | THR | GLY | PRO | ALA | GLY | ASP | ASP | ASN | ||||
| 6 | ILE | THR | LEU | THR | ALA | HIS | LEU | LEU | MET | VAL | ||||
| 7 | GLY | HIS | THR | PRO | ALA | LYS | LEU | GLU | ARG | LEU | ||||
| 8 | VAL | ALA | GLU | LEU | SER | LEU | GLN | PRO | GLY | VAL | ||||
| 9 | TYR | ALA | VAL | HIS | TRP | TYR | ALA | GLY | GLU | HIS | ||||
| 10 | ALA | GLN | ALA | GLU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_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