BMRB Entry 21099

Title:
Solution structure of U3-MYRTX-Tb1a peptide from Ant venom.
Deposition date:
2022-06-17
Original release date:
2022-12-24
Authors:
PAQUET, Francoise; TREILHOU, Michel; BARASSE, Valentine
Citation:

Citation: Barasse, Valentine; Tene, Nathan; Klopp, Christophe; Paquet, Francoise; Tysklind, Niklas; Troispoux, Valerie; Lalague, Hadrien; Orivel, Jerome; Lefranc, Benjamin; Leprince, Jerome; Kenne, Martin; Tindo, Maurice; Treilhou, Michel; Touchard, Axel; Bonnafe, Elsa. "Venomics survey of six myrmicine ants provides insights into the molecular and structural diversity of their peptide toxins."  Insect Biochem. Mol. Biol. 151, 103876-. (2022).
PubMed: 36410579

Assembly members:

Assembly members:
U3-MYRTX-Tb1a, polymer, 23 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: ants   Taxonomy ID: 219812   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Tetramorium bicarinatum

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
U3-MYRTX-Tb1a: VLPALPLLAGLMSLPFLQHK LTN

Data sets:
Data typeCount
13C chemical shifts90
15N chemical shifts21
1H chemical shifts185

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 23 residues - Formula weight is not available

1   VALLEUPROALALEUPROLEULEUALAGLY
2   LEUMETSERLEUPROPHELEUGLNHISLYS
3   LEUTHRASN

Samples:

sample_1: U3-MYRTX-Tb1a 0.8 ± 0.03 mM; TFE-d2, [U-2H], 100%

sample_conditions_1: pH: 4.6; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_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 peaks
SPARKY: Backbone or all simulated peaks