BMRB Entry 21100
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR21100
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of M-MYRTX-Tb1a peptide (Bicarinalin) from Ant peptide venom. PubMed: 36879819
Deposition date: 2022-07-12 Original release date: 2022-12-24
Authors: PAQUET, Francoise; JOUVENSAL, Laurence; LOTH, Karine
Citation: Ascoet, Steven; Touchard, Axel; Tene, Nathan; Lefranc, Benjamin; Leprince, Jerome; Paquet, Francoise; Jouvensal, Laurence; Barasse, Valentine; Treilhou, Michel; Billet, Arnaud; Bonnafe, Elsa. "The mechanism underlying toxicity of a venom peptide against insects reveals how ants are master at disrupting membranes." iScience 26, 106157-106157 (2023).
Assembly members:
M-MYRTX-Tb1a, polymer, 20 residues, 2235.839 Da.
Natural source: Common Name: ants Taxonomy ID: 219812 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Tetramorium bicarinatum
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
M-MYRTX-Tb1a: KIKIPWGKVKDFLVGGMKAV
X
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 80 |
15N chemical shifts | 18 |
1H chemical shifts | 164 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | M-MYRTX-Tb1a | 1 |
Entities:
Entity 1, M-MYRTX-Tb1a 20 residues - 2235.839 Da.
1 | LYS | ILE | LYS | ILE | PRO | TRP | GLY | LYS | VAL | LYS | ||||
2 | ASP | PHE | LEU | VAL | GLY | GLY | MET | LYS | ALA | VAL | ||||
3 | NH2 |
Samples:
sample_1: M-MYRTX-Tb1a 1.2 ± 0.05 mM; TFE-d2, [U-2H], 100%
sample_conditions_1: pH: 4.6; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | 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 |
Software:
ARIA v2.3.1, Linge, O'Donoghue and Nilges - structure solution
CCPNMR v2.1, CCPN - chemical shift assignment, data analysis, peak picking
TOPSPIN v3.6.2, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance III HD 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts