BMRB Entry 18652
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18652
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Citation: Lee, Alan Yueh-Luen; Chen, Yu-Da; Chang, Yu-Yung; Lin, Yu-Ching; Chang, Chi-Fon; Huang, Shing-Jong; Wu, Shih-Hsiung; Hsu, Chun-Hua. "Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease." Acta Crystallogr. D Biol. Crystallogr. 70, 218-230 (2014).
PubMed: 24531457
Assembly members:
alpha_sub-domain, polymer, 124 residues, Formula weight is not available
Natural source: Common Name: Brevibacillus thermoruber Taxonomy ID: 33942 Superkingdom: Bacteria Kingdom: not available Genus/species: Brevibacillus thermoruber
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21a
Entity Sequences (FASTA):
alpha_sub-domain: MAGYTELEKLHIMRDYLLPK
QMEEHGLGRDKLQMNEEAML
KVIRQYTREAGVRNLNREAA
NICRKAARLIVSGEKKRVVV
TPKTVESLLGKPRYRYGLAE
REDQVGAVTGLAWTQALEHH
HHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 214 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 205 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alpha sub-domain | 1 |
Entities:
Entity 1, alpha sub-domain 124 residues - Formula weight is not available
N-terminal M (490), and C-termianl LEHHHHHH (606-613) are artifacts sequencing and tag.
| 1 | MET | ALA | GLY | TYR | THR | GLU | LEU | GLU | LYS | LEU | ||||
| 2 | HIS | ILE | MET | ARG | ASP | TYR | LEU | LEU | PRO | LYS | ||||
| 3 | GLN | MET | GLU | GLU | HIS | GLY | LEU | GLY | ARG | ASP | ||||
| 4 | LYS | LEU | GLN | MET | ASN | GLU | GLU | ALA | MET | LEU | ||||
| 5 | LYS | VAL | ILE | ARG | GLN | TYR | THR | ARG | GLU | ALA | ||||
| 6 | GLY | VAL | ARG | ASN | LEU | ASN | ARG | GLU | ALA | ALA | ||||
| 7 | ASN | ILE | CYS | ARG | LYS | ALA | ALA | ARG | LEU | ILE | ||||
| 8 | VAL | SER | GLY | GLU | LYS | LYS | ARG | VAL | VAL | VAL | ||||
| 9 | THR | PRO | LYS | THR | VAL | GLU | SER | LEU | LEU | GLY | ||||
| 10 | LYS | PRO | ARG | TYR | ARG | TYR | GLY | LEU | ALA | GLU | ||||
| 11 | ARG | GLU | ASP | GLN | VAL | GLY | ALA | VAL | THR | GLY | ||||
| 12 | LEU | ALA | TRP | THR | GLN | ALA | LEU | GLU | HIS | HIS | ||||
| 13 | HIS | HIS | HIS | HIS |
Samples:
sample_1: alpha sub-domain, [U-98% 13C; U-98% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 5 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- 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