BMRB Entry 26908
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26908
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Title: Backbone 1H, 13C, 15N chemical shift assignments of portions of Thermotoga maritima flagellar motor proteins FliG (N-terminal domain; FliGN) and FliF (C-terminal domain; FliFC) in complex PubMed: 28089452
Deposition date: 2016-09-23 Original release date: 2017-02-15
Authors: Levenson, Robert; Dahlquist, Frederick
Citation: Lynch, Michael; Levenson, Robert; Kim, Eun; Sircar, Ria; Blair, David; Dahlquist, Frederick; Crane, Brian. "Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor" Structure 25, 317-328 (2017).
Assembly members:
FliGn, polymer, 104 residues, Formula weight is not available
FliFc, polymer, 58 residues, Formula weight is not available
Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FliGn: GHMPEKKIDGRRKAAVLLVA
LGPEKAAQVMKHLDEETVEQ
LVVEIANIGRVTPEEKKQVL
EEFLSLAKAKEMISEGGIEY
AKKVLEKAFGPERARKIIER
LTSS
FliFc: MVSPEEKELLELLEELENIF
SRSPSDIAEIVRLWFFERGL
EDHHHHHHHHASENLYFQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 267 |
15N chemical shifts | 131 |
1H chemical shifts | 131 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | FliGn | 1 |
2 | FliFc | 2 |
Entities:
Entity 1, FliGn 104 residues - Formula weight is not available
1 | GLY | HIS | MET | PRO | GLU | LYS | LYS | ILE | ASP | GLY | ||||
2 | ARG | ARG | LYS | ALA | ALA | VAL | LEU | LEU | VAL | ALA | ||||
3 | LEU | GLY | PRO | GLU | LYS | ALA | ALA | GLN | VAL | MET | ||||
4 | LYS | HIS | LEU | ASP | GLU | GLU | THR | VAL | GLU | GLN | ||||
5 | LEU | VAL | VAL | GLU | ILE | ALA | ASN | ILE | GLY | ARG | ||||
6 | VAL | THR | PRO | GLU | GLU | LYS | LYS | GLN | VAL | LEU | ||||
7 | GLU | GLU | PHE | LEU | SER | LEU | ALA | LYS | ALA | LYS | ||||
8 | GLU | MET | ILE | SER | GLU | GLY | GLY | ILE | GLU | TYR | ||||
9 | ALA | LYS | LYS | VAL | LEU | GLU | LYS | ALA | PHE | GLY | ||||
10 | PRO | GLU | ARG | ALA | ARG | LYS | ILE | ILE | GLU | ARG | ||||
11 | LEU | THR | SER | SER |
Entity 2, FliFc 58 residues - Formula weight is not available
1 | MET | VAL | SER | PRO | GLU | GLU | LYS | GLU | LEU | LEU | ||||
2 | GLU | LEU | LEU | GLU | GLU | LEU | GLU | ASN | ILE | PHE | ||||
3 | SER | ARG | SER | PRO | SER | ASP | ILE | ALA | GLU | ILE | ||||
4 | VAL | ARG | LEU | TRP | PHE | PHE | GLU | ARG | GLY | LEU | ||||
5 | GLU | ASP | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | ||||
6 | ALA | SER | GLU | ASN | LEU | TYR | PHE | GLN |
Samples:
sample_1: FliGn, [U-13C; U-15N; U-2H], 400 ± 100 uM; FliFc, [U-13C; U-15N; U-2H], 400 ± 100 uM; Sodium Phosphate 50 mM; NaCl 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 125 mM; pH: 6.5; pressure: 1 atm; temperature: 313 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
Software:
ANSIG, Kraulis - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts