BMRB Entry 25247
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25247
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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).
PubMed: 28089452
Assembly members:
FliFc, polymer, 38 residues, Formula weight is not available
FliG, polymer, 342 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: obtained from a vendor
Entity Sequences (FASTA):
FliFc: VSPEEKELLELLEELENIFS
RSPSDIAEIVRLWFFERG
FliG: MHHHQHHMPEKKIDGRRKAA
VLLVALGPEKAAQVMKHLDE
ETVEQLVVEIANIGRVTPEE
KKQVLEEFLSLAKAKEMISE
GGIEYAKKVLEKAFGPERAR
KIIERLTSSLQVKPFSFVRD
TDPVQLVNFLQSEHPQTIAV
VLSYLDPPVAAQILGALPEE
LQTEVLKRIALLERTSPEVV
KEIERNLEKKISGFVSRTFS
KVGGIDTAAEIMNNLDRTTE
KKIMDKLVQENPELADEIRR
RMFVFEDILKLDDRSIQLVL
REVDTRDLALALKGASDELK
EKIFKNMSKRAAALLKDELE
YMGPVRLKDVEEAQQKIINI
IRRLEEAGEIVIARGGGEEL
IM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 557 |
| 15N chemical shifts | 273 |
| 1H chemical shifts | 273 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FliFc | 1 |
| 2 | FliG | 2 |
Entities:
Entity 1, FliFc 38 residues - Formula weight is not available
Corresponds to cytoplasmic C-terminal region of FliF
| 1 | VAL | SER | PRO | GLU | GLU | LYS | GLU | LEU | LEU | GLU | ||||
| 2 | LEU | LEU | GLU | GLU | LEU | GLU | ASN | ILE | PHE | SER | ||||
| 3 | ARG | SER | PRO | SER | ASP | ILE | ALA | GLU | ILE | VAL | ||||
| 4 | ARG | LEU | TRP | PHE | PHE | GLU | ARG | GLY |
Entity 2, FliG 342 residues - Formula weight is not available
N-terminal His-tagged FliG construct.
| 1 | MET | HIS | HIS | HIS | GLN | HIS | HIS | MET | PRO | GLU | ||||
| 2 | LYS | LYS | ILE | ASP | GLY | ARG | ARG | LYS | ALA | ALA | ||||
| 3 | VAL | LEU | LEU | VAL | ALA | LEU | GLY | PRO | GLU | LYS | ||||
| 4 | ALA | ALA | GLN | VAL | MET | LYS | HIS | LEU | ASP | GLU | ||||
| 5 | GLU | THR | VAL | GLU | GLN | LEU | VAL | VAL | GLU | ILE | ||||
| 6 | ALA | ASN | ILE | GLY | ARG | VAL | THR | PRO | GLU | GLU | ||||
| 7 | LYS | LYS | GLN | VAL | LEU | GLU | GLU | PHE | LEU | SER | ||||
| 8 | LEU | ALA | LYS | ALA | LYS | GLU | MET | ILE | SER | GLU | ||||
| 9 | GLY | GLY | ILE | GLU | TYR | ALA | LYS | LYS | VAL | LEU | ||||
| 10 | GLU | LYS | ALA | PHE | GLY | PRO | GLU | ARG | ALA | ARG | ||||
| 11 | LYS | ILE | ILE | GLU | ARG | LEU | THR | SER | SER | LEU | ||||
| 12 | GLN | VAL | LYS | PRO | PHE | SER | PHE | VAL | ARG | ASP | ||||
| 13 | THR | ASP | PRO | VAL | GLN | LEU | VAL | ASN | PHE | LEU | ||||
| 14 | GLN | SER | GLU | HIS | PRO | GLN | THR | ILE | ALA | VAL | ||||
| 15 | VAL | LEU | SER | TYR | LEU | ASP | PRO | PRO | VAL | ALA | ||||
| 16 | ALA | GLN | ILE | LEU | GLY | ALA | LEU | PRO | GLU | GLU | ||||
| 17 | LEU | GLN | THR | GLU | VAL | LEU | LYS | ARG | ILE | ALA | ||||
| 18 | LEU | LEU | GLU | ARG | THR | SER | PRO | GLU | VAL | VAL | ||||
| 19 | LYS | GLU | ILE | GLU | ARG | ASN | LEU | GLU | LYS | LYS | ||||
| 20 | ILE | SER | GLY | PHE | VAL | SER | ARG | THR | PHE | SER | ||||
| 21 | LYS | VAL | GLY | GLY | ILE | ASP | THR | ALA | ALA | GLU | ||||
| 22 | ILE | MET | ASN | ASN | LEU | ASP | ARG | THR | THR | GLU | ||||
| 23 | LYS | LYS | ILE | MET | ASP | LYS | LEU | VAL | GLN | GLU | ||||
| 24 | ASN | PRO | GLU | LEU | ALA | ASP | GLU | ILE | ARG | ARG | ||||
| 25 | ARG | MET | PHE | VAL | PHE | GLU | ASP | ILE | LEU | LYS | ||||
| 26 | LEU | ASP | ASP | ARG | SER | ILE | GLN | LEU | VAL | LEU | ||||
| 27 | ARG | GLU | VAL | ASP | THR | ARG | ASP | LEU | ALA | LEU | ||||
| 28 | ALA | LEU | LYS | GLY | ALA | SER | ASP | GLU | LEU | LYS | ||||
| 29 | GLU | LYS | ILE | PHE | LYS | ASN | MET | SER | LYS | ARG | ||||
| 30 | ALA | ALA | ALA | LEU | LEU | LYS | ASP | GLU | LEU | GLU | ||||
| 31 | TYR | MET | GLY | PRO | VAL | ARG | LEU | LYS | ASP | VAL | ||||
| 32 | GLU | GLU | ALA | GLN | GLN | LYS | ILE | ILE | ASN | ILE | ||||
| 33 | ILE | ARG | ARG | LEU | GLU | GLU | ALA | GLY | GLU | ILE | ||||
| 34 | VAL | ILE | ALA | ARG | GLY | GLY | GLY | GLU | GLU | LEU | ||||
| 35 | ILE | MET |
Samples:
FliG-FliFc: FliFc 350 ± 50 mM; FliG, [U-13C; U-15N; U-2H], 350 ± 50 mM; Sodium phosphate 50 mM; NaCl 100 mM; EDTA 1 mM
Sodium_Phosphate: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | FliG-FliFc | isotropic | Sodium_Phosphate |
| 3D HNCA | FliG-FliFc | isotropic | Sodium_Phosphate |
| 3D HNCACB | FliG-FliFc | isotropic | Sodium_Phosphate |
| 3D HN(CO)CA | FliG-FliFc | isotropic | Sodium_Phosphate |
| 3D HN(COCA)CB | FliG-FliFc | isotropic | Sodium_Phosphate |
Software:
ANSIG, Kraulis - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks