BMRB Entry 30598
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30598
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Title: Solution structure of scorpion Hottentotta jayakari venom toxin Hj1a PubMed: 32259093
Deposition date: 2019-04-08 Original release date: 2020-02-07
Authors: Chin, Y.; Chow, C.; King, G.
Citation: Chow, Chun Yuen; Chin, Yanni K-Y; Walker, Andrew; Guo, Shaodong; Blomster, Linda; Ward, Micaiah; Herzig, Volker; Rokyta, Darin; King, Glenn. "Venom Peptides with Dual Modulatory Activity on the Voltage-Gated Sodium Channel Na V 1.1 Provide Novel Leads for Development of Antiepileptic Drugs" ACS Pharmacol. Transl. Sci. 3, 119-134 (2020).
Assembly members:
entity_1, polymer, 67 residues, 7559.603 Da.
Natural source: Common Name: scorpions Taxonomy ID: 224597 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hottentotta jayakari
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GEEVRDAYIAQPHNCVYHCF
RDSYCNDLCIKHGAESGECK
WFTSSGNACWCVKLPKSEPI
KVPGKCH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 262 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 419 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 67 residues - 7559.603 Da.
| 1 | GLY | GLU | GLU | VAL | ARG | ASP | ALA | TYR | ILE | ALA | ||||
| 2 | GLN | PRO | HIS | ASN | CYS | VAL | TYR | HIS | CYS | PHE | ||||
| 3 | ARG | ASP | SER | TYR | CYS | ASN | ASP | LEU | CYS | ILE | ||||
| 4 | LYS | HIS | GLY | ALA | GLU | SER | GLY | GLU | CYS | LYS | ||||
| 5 | TRP | PHE | THR | SER | SER | GLY | ASN | ALA | CYS | TRP | ||||
| 6 | CYS | VAL | LYS | LEU | PRO | LYS | SER | GLU | PRO | ILE | ||||
| 7 | LYS | VAL | PRO | GLY | LYS | CYS | HIS |
Samples:
sample_1: Hj1a, [U-13C; U-15N], 663 uM; MES 20 mM; D2O 5%
sample_conditions_1: ionic strength: 0 mM; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
Analysis, CCPN - chemical shift assignment
CcpNMR, CCPN - peak picking
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
Rowland NMR Toolkit, Gregory P. Mullen - processing
NMR spectrometers:
- Bruker AvanceIII 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts