BMRB Entry 18491
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18491
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Citation: Rico, Manuel; Jimenez, M Angeles; Gonzalez, Carlos; de Filippis, Vincenzo; Fontana, Angelo. "NMR solution structure of the C-terminal fragment 255-316 of Thermolysin: A dimer formed by subunits having native structure" Biochemistry 33, 14834-14847 (1994).
PubMed: 7993910
Assembly members:
Th255-316, polymer, 62 residues, 6624.5 Da.
Natural source: Common Name: Bacillus thermoproteolyticus Taxonomy ID: 1427 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus thermoproteolyticus
Experimental source: Production method: Subtilisin limited proteolysis
Entity Sequences (FASTA):
Th255-316: VVGIGRDKLGKIFYRALTQY
LTPTSNFSQLRAAAVQSATD
LYGSTSQEVASVKQAFDAVG
VK
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 448 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Th255-316, chain 1 | 1 |
| 2 | Th255-316, chain 2 | 1 |
Entities:
Entity 1, Th255-316, chain 1 62 residues - 6624.5 Da.
| 1 | VAL | VAL | GLY | ILE | GLY | ARG | ASP | LYS | LEU | GLY | ||||
| 2 | LYS | ILE | PHE | TYR | ARG | ALA | LEU | THR | GLN | TYR | ||||
| 3 | LEU | THR | PRO | THR | SER | ASN | PHE | SER | GLN | LEU | ||||
| 4 | ARG | ALA | ALA | ALA | VAL | GLN | SER | ALA | THR | ASP | ||||
| 5 | LEU | TYR | GLY | SER | THR | SER | GLN | GLU | VAL | ALA | ||||
| 6 | SER | VAL | LYS | GLN | ALA | PHE | ASP | ALA | VAL | GLY | ||||
| 7 | VAL | LYS |
Samples:
sample_1: Th255-316 1 mM; TSP 0.1 mM; H2O 90%; D2P 10%
sample_2: Th255-316 1 mM; TSP 0.1 mM; D2O 100%
sample_conditions_1: ionic strength: 0 M; pH: 4.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
UXNMR, Bruker Biospin - processing
NMR spectrometers:
- Bruker AMX 600 MHz