BMRB Entry 19430
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19430
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Structure of Salmonella MgtR PubMed: 24140750
Deposition date: 2013-08-15 Original release date: 2013-10-28
Authors: Jean-Francois, Frantz; Dai, Jian; Yu, Lu; Myrick, Alissa; Rubin, Eric; Fajer, Piotr; Song, Likai; Zhou, Huan-Xiang; Cross, Timothy
Citation: Jean-Francois, Frantz; Dai, Jian; Yu, Lu; Myrick, Alissa; Rubin, Eric; Fajer, Piotr; Song, Likai; Zhou, Huan-Xiang; Cross, Timothy. "Binding of MgtR, a Salmonella Transmembrane Regulatory Peptide, to MgtC, a Mycobacterium tuberculosis Virulence Factor: A Structural Study." J. Mol. Biol. 426, 436-446 (2014).
Assembly members:
entity, polymer, 30 residues, 3459.372 Da.
Natural source: Common Name: Salmonella enterica Taxonomy ID: 28901 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella enterica
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity: MNRSPDKIIALIFLLISLLV
LCLALWQIVF
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 15N chemical shifts | 8 |
| residual dipolar couplings | 8 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Salmonella MgtR | 1 |
Entities:
Entity 1, Salmonella MgtR 30 residues - 3459.372 Da.
| 1 | MET | ASN | ARG | SER | PRO | ASP | LYS | ILE | ILE | ALA | |
| 2 | LEU | ILE | PHE | LEU | LEU | ILE | SER | LEU | LEU | VAL | |
| 3 | LEU | CYS | LEU | ALA | LEU | TRP | GLN | ILE | VAL | PHE |
Samples:
sample_1: H20 54 % w/w; DMPC % w/w; MgtR, specific AA labels, % w/w
sample_conditions_1: pH: 8; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| PISEMA | sample_1 | anisotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.29, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 400 MHz