BMRB Entry 18491
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18491
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H chemical shifts of Thermolysin 255-316 fragment PubMed: 7993910
Deposition date: 2012-05-30 Original release date: 2012-06-18
Authors: Rico, Manuel; Jimenez, M Angeles; Gonzalez, Carlos
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).
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