BMRB Entry 21101
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR21101
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Title: Solution structure of U9-MYRTX-Tb1a 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:
U9-MYRTX-Tb1a, polymer, 19 residues, Formula weight is not available
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):
U9-MYRTX-Tb1a: GIVTKLIKKGVKLGLKMAL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 75 |
15N chemical shifts | 17 |
1H chemical shifts | 161 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | U9-MYRTX-Tb1a | 1 |
Entities:
Entity 1, U9-MYRTX-Tb1a 19 residues - Formula weight is not available
1 | GLY | ILE | VAL | THR | LYS | LEU | ILE | LYS | LYS | GLY | ||||
2 | VAL | LYS | LEU | GLY | LEU | LYS | MET | ALA | LEU |
Samples:
sample_1: U9-MYRTX-Tb1a 0.8 ± 0.03 mM; TFE-d2, [U-2H], 100%
sample_conditions_1: pH: 5.2; 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