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Structure of Salmonella MgtR
Authors
Jean-Francois, F., Dai, J., Yu, L., Myrick, A., Rubin, E., Fajer, P., Song, L., Zhou, H., Cross, T.
Assembly
Salmonella MgtR
Entity
1. Salmonella MgtR (polymer), 30 monomers, 3457.325 Da Detail

MNRSPDKIIA LIFLLISLLV LCLALWQIVF


Formula weight
3457.325 Da
Source organism
Salmonella enterica
Exptl. method
solid-state NMR
Refine. method
molecular dynamics
Data set
assigned_chemical_shifts, RDCs
Chem. Shift Complete
Sequence coverage: 26.7 %, Completeness: 25.0 %, Completeness (bb): 27.6 % Detail

Polymer type: polypeptide(L)

Total15N
All25.0 % (8 of 32)25.0 % (8 of 32)
Backbone27.6 % (8 of 29)27.6 % (8 of 29)
Sidechain 0.0 % (0 of 3) 0.0 % (0 of 3)
Aromatic 0.0 % (0 of 1) 0.0 % (0 of 1)

1. entity

MNRSPDKIIA LIFLLISLLV LCLALWQIVF

Sample

Solvent system 54% by weight water, Pressure 1 atm, Temperature 310 K, pH 8, Details MgtR in DMPC liquid crystalline lipids for solid state NMR. 1:6 w/w ratio of MgtR/lipid.


#NameIsotope labelingTypeConcentration
1H20natural abundance
2DMPCnatural abundance
3MgtRspecific AA labels

Protein Blocks Logo
Calculated from 1 models in PDB: 2MC7, Strand ID: A Detail


RDC
8 RDC values in 1 lists
Field strength (1H) 400 MHz, Pressure 1 atm, Temperature 310 K, pH 8 Detail
Release date
2013-10-27
Citation
Binding of MgtR, a Salmonella transmembrane regulatory peptide, to MgtC, a Mycobacterium tuberculosis virulence factor: a structural study
Jean-Francois, F.L., Dai, J., Yu, L., Myrick, A., Rubin, E., Fajer, P.G., Song, L., Zhou, H., Cross, T.A.
J. Mol. Biol. (2014), 426, 436-446, PubMed 24140750 , DOI 10.1016/j.jmb.2013.10.014 ,
Related entities 1. Salmonella MgtR, : 1 : 11 entities Detail
Experiments performed 1 experiments Detail
nullKeywords Distance Restraints, MgtC/MgtR complex, Mycobacterium tuberculosis MgtC, Orientational Restraints, Restrained Molecular Dynamics, Salmonella Typhis MgtR, Torsional Restraints, Transmembrane helical complex