BMRB Entry 6740
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6740
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Title: NMR solution structure of the Crisp domain of Tpx-1 PubMed: 16339766
Deposition date: 2005-07-21 Original release date: 2007-02-06
Authors: Gibbs, G.; Scanlon, M.; Swarbrick, J.; Curtis, S.; Dulhunty, A.; O'Bryan, M.
Citation: Gibbs, G.; Scanlon, M.; Swarbrick, J.; Curtis, S.; Gallant, E.; Dulhunty, A.; O'Bryan, M.. "The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signalling" J. Biol. Chem. 281, 4156-4163 (2006).
Assembly members:
Cysteine-rich secretory protein-2, polymer, 57 residues, Formula weight is not available
Natural source: Common Name: House mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Cysteine-rich secretory protein-2: GSCASCPNNCENGLCTNSCD
FEDLLSNCESLKTSAGCKHE
LLKTKCQATCLCEDKIH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 78 |
15N chemical shifts | 58 |
1H chemical shifts | 293 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Cysteine-rich secretory protein-2 | 1 |
Entities:
Entity 1, Cysteine-rich secretory protein-2 57 residues - Formula weight is not available
1 | GLY | SER | CYS | ALA | SER | CYS | PRO | ASN | ASN | CYS | ||||
2 | GLU | ASN | GLY | LEU | CYS | THR | ASN | SER | CYS | ASP | ||||
3 | PHE | GLU | ASP | LEU | LEU | SER | ASN | CYS | GLU | SER | ||||
4 | LEU | LYS | THR | SER | ALA | GLY | CYS | LYS | HIS | GLU | ||||
5 | LEU | LEU | LYS | THR | LYS | CYS | GLN | ALA | THR | CYS | ||||
6 | LEU | CYS | GLU | ASP | LYS | ILE | HIS |
Samples:
sample_1: Cysteine-rich secretory protein-2, [U-13C; U-15], 1 mM; H2O 90%; D2O 10%
sample_2: Cysteine-rich secretory protein-2 1 mM; H2O 90%; D2O 10%
sample_3: Cysteine-rich secretory protein-2, [U-13C; U-15], 1 mM; D2O 100%
sample_cond_1: ionic strength: 1 mM; pH: 5.8; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D_15N-separated_NOESY | not available | not available | not available |
3D_15N-separated TOCSY | not available | not available | not available |
2D NOESY | not available | not available | not available |
2D TOCSY | not available | not available | not available |
DQF-COSY | not available | not available | not available |
Software:
XWINNMR v1, Bruker - collection, processing
SPARKY v3.101, Goddard Keller - data analysis
CYANA v1.06, Guntert - refinement
XPLOR-NIH v2.9.9, Clore Schwieters Kuszewski Tjandra - refinement
NMR spectrometers:
- Bruker DRX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts