BMRB Entry 51156
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51156
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Title: Backbone NMR resonance assignments of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the ADP-bound state PubMed: 34988902
Deposition date: 2021-10-26 Original release date: 2022-01-07
Authors: Perez Carrillo, Victor Hugo; Rose-Sperling, Dania; Tran, Mai Ahn; Wiedemann, Christoph; Hellmich, Ute
Citation: Perez Carrillo, Victor Hugo; Rose-Sperling, Dania; Tran, Mai Ahn; Wiedemann, Christoph; Hellmich, Ute. "Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state" Biomol. NMR Assignments 16, 81-86 (2022).
Assembly members:
entity_1, polymer, 259 residues, Formula weight is not available
entity_ADP, non-polymer, 427.201 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 11a
Entity Sequences (FASTA):
entity_1: GKQIENAHLPIQLDRVSFGY
KPDQLILKEVSAVIEAGKVT
AIVGPSGGGKTTLFKLLERF
YSPTAGTIRLGDEPVDTYSL
ESWREHIGYVSQESPLMSGT
IRENICYGLERDVTDAEIEK
AAEMAYALNFIKELPNQFDT
EVGERGIMLSGGQRQRIAIA
RALLRNPSILMLDEATSSLD
SQSEKSVQQALEVLMEGRTT
IVIAHRLSTVVDADQLLFVE
KGEITGRGTHHELMASHGLY
RDFAEQQLKMNADLENKAG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 711 |
| 15N chemical shifts | 244 |
| 1H chemical shifts | 244 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BmrA NBD | 1 |
| 2 | ADP | 2 |
Entities:
Entity 1, BmrA NBD 259 residues - Formula weight is not available
| 1 | GLY | LYS | GLN | ILE | GLU | ASN | ALA | HIS | LEU | PRO | ||||
| 2 | ILE | GLN | LEU | ASP | ARG | VAL | SER | PHE | GLY | TYR | ||||
| 3 | LYS | PRO | ASP | GLN | LEU | ILE | LEU | LYS | GLU | VAL | ||||
| 4 | SER | ALA | VAL | ILE | GLU | ALA | GLY | LYS | VAL | THR | ||||
| 5 | ALA | ILE | VAL | GLY | PRO | SER | GLY | GLY | GLY | LYS | ||||
| 6 | THR | THR | LEU | PHE | LYS | LEU | LEU | GLU | ARG | PHE | ||||
| 7 | TYR | SER | PRO | THR | ALA | GLY | THR | ILE | ARG | LEU | ||||
| 8 | GLY | ASP | GLU | PRO | VAL | ASP | THR | TYR | SER | LEU | ||||
| 9 | GLU | SER | TRP | ARG | GLU | HIS | ILE | GLY | TYR | VAL | ||||
| 10 | SER | GLN | GLU | SER | PRO | LEU | MET | SER | GLY | THR | ||||
| 11 | ILE | ARG | GLU | ASN | ILE | CYS | TYR | GLY | LEU | GLU | ||||
| 12 | ARG | ASP | VAL | THR | ASP | ALA | GLU | ILE | GLU | LYS | ||||
| 13 | ALA | ALA | GLU | MET | ALA | TYR | ALA | LEU | ASN | PHE | ||||
| 14 | ILE | LYS | GLU | LEU | PRO | ASN | GLN | PHE | ASP | THR | ||||
| 15 | GLU | VAL | GLY | GLU | ARG | GLY | ILE | MET | LEU | SER | ||||
| 16 | GLY | GLY | GLN | ARG | GLN | ARG | ILE | ALA | ILE | ALA | ||||
| 17 | ARG | ALA | LEU | LEU | ARG | ASN | PRO | SER | ILE | LEU | ||||
| 18 | MET | LEU | ASP | GLU | ALA | THR | SER | SER | LEU | ASP | ||||
| 19 | SER | GLN | SER | GLU | LYS | SER | VAL | GLN | GLN | ALA | ||||
| 20 | LEU | GLU | VAL | LEU | MET | GLU | GLY | ARG | THR | THR | ||||
| 21 | ILE | VAL | ILE | ALA | HIS | ARG | LEU | SER | THR | VAL | ||||
| 22 | VAL | ASP | ALA | ASP | GLN | LEU | LEU | PHE | VAL | GLU | ||||
| 23 | LYS | GLY | GLU | ILE | THR | GLY | ARG | GLY | THR | HIS | ||||
| 24 | HIS | GLU | LEU | MET | ALA | SER | HIS | GLY | LEU | TYR | ||||
| 25 | ARG | ASP | PHE | ALA | GLU | GLN | GLN | LEU | LYS | MET | ||||
| 26 | ASN | ALA | ASP | LEU | GLU | ASN | LYS | ALA | GLY |
Entity 2, ADP - C10 H15 N5 O10 P2 - 427.201 Da.
| 1 | ADP |
Samples:
sample_1: BmrA NBD, [U-13C; U-15N; U-2H], 441 uM; DSS 0.15 mM; ADP 10 mM; BisTris 50 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA - chemical shift assignment
TOPSPIN - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts