BMRB Entry 21099

Name: Solution structure of U3-MYRTX-Tb1a peptide from Ant venom.
Published: 2022-12-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR21099

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of U3-MYRTX-Tb1a peptide from Ant venom. PubMed: 36410579

Deposition date: 2022-06-17 Original release date: 2022-12-24

Authors: PAQUET, Francoise; TREILHOU, Michel; BARASSE, Valentine

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).

Assembly members:
U3-MYRTX-Tb1a, polymer, 23 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):
U3-MYRTX-Tb1a: VLPALPLLAGLMSLPFLQHK LTN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- 1

Data type	Count
13C chemical shifts	90
15N chemical shifts	21
1H chemical shifts	185

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit 1	1

Entities:

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

1

VAL

LEU

PRO

ALA

LEU

PRO

LEU

ALA

GLY

2

LEU

MET

SER

LEU

PRO

PHE

LEU

GLN

HIS

LYS

3

LEU

THR

ASN

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:

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