BMRB Entry 25917
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25917
MolProbity Validation Chart
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Title: ProTx-II PubMed: 27311819
Deposition date: 2015-12-08 Original release date: 2016-07-05
Authors: Schroeder, Christina
Citation: Henriques, Sonia; Deplazes, Evelyn; Lawrence, Nicole; Chenval, Olivier; Inserra, Marco; Thongyoo, Panumart; Marks, Alan; Vetter, Irina; Craik, David; Schroeder, Christina. "Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes is a Prerequisite for its Inhibition of Human Voltage-gated Sodium Channel NaV1.7" J. Biol. Chem. 291, 17049-17065 (2016).
Assembly members:
entity, polymer, 30 residues, 3839.690 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity: YCQKWMWTCDSERKCCEGMV
CRLWCKKKLW
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 84 |
| 15N chemical shifts | 33 |
| 1H chemical shifts | 218 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 30 residues - 3839.690 Da.
| 1 | TYR | CYS | GLN | LYS | TRP | MET | TRP | THR | CYS | ASP | |
| 2 | SER | GLU | ARG | LYS | CYS | CYS | GLU | GLY | MET | VAL | |
| 3 | CYS | ARG | LEU | TRP | CYS | LYS | LYS | LYS | LEU | TRP |
Samples:
sample_1: entity 2 mg; H2O 90%; D2O 10%
sample_2: entity 2 mg; D2O 100%
sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 298 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 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis
TOPSPIN, Bruker Biospin - collection, processing
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
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SPARKY: Backbone
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