BMRB Entry 26592
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26592
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Title: The LcrG tip chaperone protein of the Yersinia pestis type III secretion system is partially folded PubMed: 26259880
Deposition date: 2015-06-22 Original release date: 2015-12-18
Authors: De Guzman, Roberto; Chaudhury, Sukanya
Citation: Chaudhury, Sukanya; Souza, Clarice; Plano, Gregory; De Guzman, Roberto. "The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded" J. Mol. Biol. 427, 3096-3109 (2015).
Assembly members:
LcrG, polymer, 67 residues, Formula weight is not available
Natural source: Common Name: enterobacteria Taxonomy ID: 632 Superkingdom: Bacteria Kingdom: not available Genus/species: Yersinia pestis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
LcrG: DEYDKTLKQAELAIADSDHR
AKLLQEMSADIGLTPEAVMK
IFAGRSAEEIKPAERELLDE
IKRQRER
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 163 |
15N chemical shifts | 78 |
1H chemical shifts | 78 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | LcrG 7-73 | 1 |
Entities:
Entity 1, LcrG 7-73 67 residues - Formula weight is not available
The sequence corresponds to LcrG residues 7-73
1 | ASP | GLU | TYR | ASP | LYS | THR | LEU | LYS | GLN | ALA | ||||
2 | GLU | LEU | ALA | ILE | ALA | ASP | SER | ASP | HIS | ARG | ||||
3 | ALA | LYS | LEU | LEU | GLN | GLU | MET | SER | ALA | ASP | ||||
4 | ILE | GLY | LEU | THR | PRO | GLU | ALA | VAL | MET | LYS | ||||
5 | ILE | PHE | ALA | GLY | ARG | SER | ALA | GLU | GLU | ILE | ||||
6 | LYS | PRO | ALA | GLU | ARG | GLU | LEU | LEU | ASP | GLU | ||||
7 | ILE | LYS | ARG | GLN | ARG | GLU | ARG |
Samples:
sample_1: LcrG, [U-99% 13C; U-99% 15N], 0.9 mM; sodium phosphate mM; sodium chloride mM; H2O 90%; D2O 10%
sample_2: LcrG in complex with LcrV, U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate mM; sodium chloride mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K
sample_conditions_2: ionic strength: 10 mM; pH: 7.0; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
3D HNCA | sample_2 | isotropic | sample_conditions_2 |
3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts