BMRB Entry 19300
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19300
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Title: Solution structure of protoxin-1 PubMed: 24530065
Deposition date: 2013-06-13 Original release date: 2014-04-28
Authors: Daly, Norelle
Citation: Gui, Junhong; Liu, Boyi; Cao, Guan; Lipchik, Andrew; Perez, Minervo; Dekan, Zoltan; Mobli, Mehdi; Daly, Norelle; Alewood, Paul; Parker, Laurie; King, Glenn; Zhou, Yufeng; Jordt, Sven-Eric; Nitabach, Michael. "A tarantula-venom peptide antagonizes the TRPA1 nociceptor ion channel by binding to the S1-S4 gating domain" Curr. Biol. 24, 473-483 (2014).
Assembly members:
entity, polymer, 35 residues, 3999.598 Da.
Natural source: Common Name: green velvet Taxonomy ID: 213387 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Thrixopelma pruriens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity: ECRYWLGGCSAGQTCCKHLV
CSRRHGWCVWDGTFS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 81 |
| 15N chemical shifts | 32 |
| 1H chemical shifts | 212 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protoxin-1 | 1 |
Entities:
Entity 1, protoxin-1 35 residues - 3999.598 Da.
| 1 | GLU | CYS | ARG | TYR | TRP | LEU | GLY | GLY | CYS | SER | ||||
| 2 | ALA | GLY | GLN | THR | CYS | CYS | LYS | HIS | LEU | VAL | ||||
| 3 | CYS | SER | ARG | ARG | HIS | GLY | TRP | CYS | VAL | TRP | ||||
| 4 | ASP | GLY | THR | PHE | SER |
Samples:
sample_1: protoxin-1 0.5 mM
sample_2: protoxin-1 0.5 mM
sample_conditions_1: ionic strength: 0 M; pH: 5; 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 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | 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:
TOPSPIN, Bruker Biospin - collection
CcpNMR, CCPN - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts