BMRB Entry 50735
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50735
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Title: Molecular insights into substrate recognition and discrimination by the N-terminal domain of Lon AAA+ protease PubMed: 33929321
Deposition date: 2021-01-25 Original release date: 2021-05-18
Authors: Tzeng, Shiou-Ru
Citation: Tzeng, Shiou-Ru; Tseng, Yin-Chu; Lin, Chien-Chu; Hsu, Chia-Ying; Huang, Shing-Jong; Kuo, Yi-Ting; Chang, Chung-I. "Molecular insights into substrate recognition and discrimination by the N-terminal domain of Lon AAA+ protease" elife 10, e64056-e64056 (2021).
Assembly members:
entity_1, polymer, 206 residues, Formula weight is not available
Natural source: Common Name: Meiothermus taiwanensis Taxonomy ID: 172827 Superkingdom: Bacteria Kingdom: not available Genus/species: Meiothermus taiwanensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-NN206
Entity Sequences (FASTA):
entity_1: MRLELPVIPLRNTVILPHTT
TPVDVGRAKSKRAVEEAMGA
DRLIFLVAQRDPEVDDPAPD
DLYTWGVQAVVKQAMRLPDG
TLQVMVEARARAQVTDYIPG
PYLRARGEVFSEIFPIDEAV
VRVLVEELKEAFEKYVANHK
SLRLDRYQLEAVKGTSDPAM
LADTIAYHATWTVAEKQEIL
ELTDLEARLKKVLGLLSRDL
ERFELD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 338 |
| 15N chemical shifts | 173 |
| 1H chemical shifts | 173 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NN206 in sul20-bound state | 1 |
Entities:
Entity 1, NN206 in sul20-bound state 206 residues - Formula weight is not available
| 1 | MET | ARG | LEU | GLU | LEU | PRO | VAL | ILE | PRO | LEU | ||||
| 2 | ARG | ASN | THR | VAL | ILE | LEU | PRO | HIS | THR | THR | ||||
| 3 | THR | PRO | VAL | ASP | VAL | GLY | ARG | ALA | LYS | SER | ||||
| 4 | LYS | ARG | ALA | VAL | GLU | GLU | ALA | MET | GLY | ALA | ||||
| 5 | ASP | ARG | LEU | ILE | PHE | LEU | VAL | ALA | GLN | ARG | ||||
| 6 | ASP | PRO | GLU | VAL | ASP | ASP | PRO | ALA | PRO | ASP | ||||
| 7 | ASP | LEU | TYR | THR | TRP | GLY | VAL | GLN | ALA | VAL | ||||
| 8 | VAL | LYS | GLN | ALA | MET | ARG | LEU | PRO | ASP | GLY | ||||
| 9 | THR | LEU | GLN | VAL | MET | VAL | GLU | ALA | ARG | ALA | ||||
| 10 | ARG | ALA | GLN | VAL | THR | ASP | TYR | ILE | PRO | GLY | ||||
| 11 | PRO | TYR | LEU | ARG | ALA | ARG | GLY | GLU | VAL | PHE | ||||
| 12 | SER | GLU | ILE | PHE | PRO | ILE | ASP | GLU | ALA | VAL | ||||
| 13 | VAL | ARG | VAL | LEU | VAL | GLU | GLU | LEU | LYS | GLU | ||||
| 14 | ALA | PHE | GLU | LYS | TYR | VAL | ALA | ASN | HIS | LYS | ||||
| 15 | SER | LEU | ARG | LEU | ASP | ARG | TYR | GLN | LEU | GLU | ||||
| 16 | ALA | VAL | LYS | GLY | THR | SER | ASP | PRO | ALA | MET | ||||
| 17 | LEU | ALA | ASP | THR | ILE | ALA | TYR | HIS | ALA | THR | ||||
| 18 | TRP | THR | VAL | ALA | GLU | LYS | GLN | GLU | ILE | LEU | ||||
| 19 | GLU | LEU | THR | ASP | LEU | GLU | ALA | ARG | LEU | LYS | ||||
| 20 | LYS | VAL | LEU | GLY | LEU | LEU | SER | ARG | ASP | LEU | ||||
| 21 | GLU | ARG | PHE | GLU | LEU | ASP |
Samples:
sample_1: NN206 in sul20-bound state, [U-100% 15N], 0.05 mM; NN206 in sul20-bound state, [U-98% 13C; U-98% 15N], 0.3 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 328 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA - chemical shift assignment
NMR spectrometers:
- Bruker Bruker AVIII-800 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts