BMRB Entry 30190
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30190
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Title: Solution NMR structure of gHwTx-IV PubMed: 28115115
Deposition date: 2016-10-11 Original release date: 2017-02-16
Authors: Agwa, A.; Schroeder, C.
Citation: Agwa, A.; Lawrence, N.; Deplazes, E.; Cheneval, O.; Chen, R.; Craik, D.; Schroeder, C.; Henriques, S.. "Spider peptide toxin HwTx-IV engineered to bind to lipid membranes has an increased inhibitory potency at human voltage-gated sodium channel hNaV1.7." Biochim. Biophys. Acta 1859, 835-844 (2017).
Assembly members:
entity_1, polymer, 36 residues, 4036.820 Da.
Natural source: Common Name: Chinese bird spider Taxonomy ID: 29017 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Haplopelma schmidti
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: GCLGIWKACNPSNDQCCKSS
KLVCSRKTRWCKWQIX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 89 |
| 15N chemical shifts | 31 |
| 1H chemical shifts | 229 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 36 residues - 4036.820 Da.
| 1 | GLY | CYS | LEU | GLY | ILE | TRP | LYS | ALA | CYS | ASN | ||||
| 2 | PRO | SER | ASN | ASP | GLN | CYS | CYS | LYS | SER | SER | ||||
| 3 | LYS | LEU | VAL | CYS | SER | ARG | LYS | THR | ARG | TRP | ||||
| 4 | CYS | LYS | TRP | GLN | ILE | NH2 |
Samples:
sample_1: entity_1 mM; D2O, [U-2H], 10%; H2O 90%
sample_2: entity_1 mM; D2O, [U-2H], 100%
sample_conditions_1: pH: 4.0; pressure: 1 atm; temperature: 298 K
sample_conditions_2: pH: 4.0; pressure: 1 atm; temperature: 298 K
sample_conditions_3: pH: 4.0; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | 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-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 1D 1H | sample_1 | isotropic | sample_conditions_3 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_3 |
| 1D 1H | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 2D E.COSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
CcpNMR, CCPN - chemical shift assignment
MOLPROBITY, Richardson - data analysis
TALOS-N, Cornilescu, Delaglio and Bax - data analysis
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts