BMRB Entry 30226
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30226
MolProbity Validation Chart
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: NMR SOLUTION STRUCTURE OF THE ALPHA-CONOTOXIN GID MUTANT V13Y PubMed: 28874590
Deposition date: 2017-01-06 Original release date: 2017-08-31
Authors: Hussein, A.; Leffler, A.; Kuryatov, A.; Zebroski, H.; Powell, S.; Filipenko, P.; Gorson, J.; Heizmann, A.; Lyskov, S.; Nicke, A.; Lindstrom, J.; Rudy, B.; Bonneau, R.; Holford, M.; Poget, S.
Citation: Leffler, Abba; Kuryatov, Alexander; Zebroski, Henry; Powell, Susan; Filipenko, Petr; Hussein, Adel; Gorson, Juliette; Heizmann, Anna; Lyskov, Sergey; Tsien, Richard; Poget, Sebastien; Nicke, Annette; Lindstrom, Jon; Rudy, Bernardo; Bonneau, Richard; Holford, Mande. "Discovery of peptide ligands through docking and virtual screening at nicotinic acetylcholine receptor homology models." Proc. Natl. Acad. Sci. U.S.A. 114, E8100-E8109 (2017).
Assembly members:
Alpha-conotoxin GID, polymer, 19 residues, 2213.479 Da.
Natural source: Common Name: Geography cone Taxonomy ID: 6491 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Conus geographus
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
Alpha-conotoxin GID: IRDECCSNPACRYNNPHVC
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 34 |
| 1H chemical shifts | 110 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 19 residues - 2213.479 Da.
| 1 | ILE | ARG | ASP | GLU | CYS | CYS | SER | ASN | PRO | ALA | ||||
| 2 | CYS | ARG | TYR | ASN | ASN | HYP | HIS | VAL | CYS |
Samples:
sample_1: design 8, none, 1.5 ± 0.3 mM; H2O 90%; D2O 10%
sample_2: design 8, none, 1.5 ± 0.3 mM; D2O 100%
sample_conditions_1: ionic strength: 0 mM; pH: 3; pressure: 1 atm; temperature: 280 K
sample_conditions_2: ionic strength: 0 mM; pH: 3; pressure: 1 atm; temperature: 280 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_2 |
Software:
ARIA, Linge, O'Donoghue and Nilges - structure calculation
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
CcpNMR, CCPN - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
TOPSPIN, Bruker Biospin - collection
VNMR, Varian - collection
NMR spectrometers:
- Varian UNITYPLUS 600 MHz
- Bruker Avance 800 MHz