BMRB Entry 21100

Name: Solution structure of M-MYRTX-Tb1a peptide (Bicarinalin) from Ant peptide venom.
Published: 2022-12-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR21100

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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 M-MYRTX-Tb1a peptide (Bicarinalin) from Ant peptide venom.

Deposition date:

2022-07-12

Original release date:

2022-12-24

Authors:

PAQUET, Francoise; JOUVENSAL, Laurence; LOTH, Karine

Citation:

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).
PubMed: 36879819

Assembly members:

Assembly members:
M-MYRTX-Tb1a, polymer, 20 residues, 2235.839 Da.

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):
M-MYRTX-Tb1a: KIKIPWGKVKDFLVGGMKAV X

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	80
15N chemical shifts	18
1H chemical shifts	164

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

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 peaks
SPARKY: Backbone or all simulated peaks