BMRB Entry 31124
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31124
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Title: NMR structure of the funnel-web spider toxin Hc3a
Deposition date: 2023-11-06 Original release date: 2024-03-08
Authors: Budusan, E.; Payne, C.; Gonzalez, T.; Clark, R.; Rosengren, K.; Rash, L.; Cristofori-Armstrong, B.
Citation: Budusan, E.; Payne, C.; Gonzalez, T.; Obergrussberger, A.; Becker, N.; Clark, R.; Rosengren, K.; Rash, L.; Cristofori-Armstrong, B.. "The funnel-web spider venom derived single knot peptide Hc3a modulates acid-sensing ion channel 1a desensitisation" .
Assembly members:
entity_1, polymer, 39 residues, 4495.241 Da.
Natural source: Common Name: Hadronyche cerberea Taxonomy ID: 1107879 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hadronyche cerberea
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GNECIRKWLSCVDRKNDCCE
GLECWKRRGNKSSVCVPIT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 116 |
| 15N chemical shifts | 40 |
| 1H chemical shifts | 269 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 39 residues - 4495.241 Da.
| 1 | GLY | ASN | GLU | CYS | ILE | ARG | LYS | TRP | LEU | SER | ||||
| 2 | CYS | VAL | ASP | ARG | LYS | ASN | ASP | CYS | CYS | GLU | ||||
| 3 | GLY | LEU | GLU | CYS | TRP | LYS | ARG | ARG | GLY | ASN | ||||
| 4 | LYS | SER | SER | VAL | CYS | VAL | PRO | ILE | THR |
Samples:
sample_1: Hc3a 4 ± 0.1 mg/mL
sample_conditions_1: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 288 K
sample_conditions_3: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 293 K
sample_conditions_4: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 303 K
sample_conditions_5: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 308 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-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_3 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_4 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_5 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
MolProbity, Richardson - data analysis
NMR spectrometers:
- Bruker AVANCE 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts