BMRB Entry 12011
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR12011
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Title: Backbone 1H, 13C, 15N chemical shift assignments for FliGc A282T mutated protein PubMed: 28919442
Deposition date: 2017-04-19 Original release date: 2018-12-11
Authors: Miyanoiri, Yohei; Hijikata, Atsushi; Nishino, Yuuki; Gohara, Mizuki; Onoue, Yasuhiro; Kojima, Seiji; Kojima, Chojiro; Shirai, Tsuyoshi; Kainosho, Masatsune; Homma, Michio
Citation: Miyanoiri, Yohei; Hijikata, Atsushi; Nishino, Yuuki; Gohara, Mizuki; Onoue, Yasuhiro; Kojima, Seiji; Kojima, Chojiro; Shirai, Tsuyoshi; Kainosho, Masatsune; Homma, Michio. "Structural and Functional Analysis of the C-Terminal Region of FliG, an Essential Motor Component of Vibrio Na+ -Driven Flagella." Structure 25, 1540-1548 (2017).
Assembly members:
flagellar_protein_FliGc_A282T, polymer, 116 residues, Formula weight is not available
Natural source: Common Name: Vibrio alginolyticus Taxonomy ID: 663 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio alginolyticus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pCold I
Entity Sequences (FASTA):
flagellar_protein_FliGc_A282T: MNHKVHHHHHHIEGRHMMFV
FENLVEVDDQGIQKLLRDVP
QDVLQKTLKGADDSLREKVF
KNMSKRAAEMMRDDIEAMPP
VRVADVEAAQKEILAIARRM
ADAGELMLSGGADEFL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 266 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 88 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | flagellar protein FliGc A282T | 1 |
Entities:
Entity 1, flagellar protein FliGc A282T 116 residues - Formula weight is not available
| 1 | MET | ASN | HIS | LYS | VAL | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | HIS | ILE | GLU | GLY | ARG | HIS | MET | MET | PHE | VAL | ||||
| 3 | PHE | GLU | ASN | LEU | VAL | GLU | VAL | ASP | ASP | GLN | ||||
| 4 | GLY | ILE | GLN | LYS | LEU | LEU | ARG | ASP | VAL | PRO | ||||
| 5 | GLN | ASP | VAL | LEU | GLN | LYS | THR | LEU | LYS | GLY | ||||
| 6 | ALA | ASP | ASP | SER | LEU | ARG | GLU | LYS | VAL | PHE | ||||
| 7 | LYS | ASN | MET | SER | LYS | ARG | ALA | ALA | GLU | MET | ||||
| 8 | MET | ARG | ASP | ASP | ILE | GLU | ALA | MET | PRO | PRO | ||||
| 9 | VAL | ARG | VAL | ALA | ASP | VAL | GLU | ALA | ALA | GLN | ||||
| 10 | LYS | GLU | ILE | LEU | ALA | ILE | ALA | ARG | ARG | MET | ||||
| 11 | ALA | ASP | ALA | GLY | GLU | LEU | MET | LEU | SER | GLY | ||||
| 12 | GLY | ALA | ASP | GLU | PHE | LEU |
Samples:
sample_1: FliGc A282T, [U-15N], 0.9 mM; Tris-HCl 50 mM; sodium chloride 150 mM; DSS 0.01 % w/v; H2O 95%; D2O, [U-2H], 5%
sample_2: FliGc A282T, [U-13C; U-15N], 0.9 mM; Tris-HCl 50 mM; sodium chloride 150 mM; DSS 0.01 % w/v; H2O 95%; D2O, [U-2H], 5%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2, Bruker Biospin - data analysis, processing
SPARKY, Goddard - chemical shift assignment, peak picking
TALOS vtalos-n, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts