BMRB Entry 30928

Name: Solution structure of peptide toxin MIITX2-Mg1a from the venom of the Australian giant red bull ant Myrmecia gulosa
Published: 2022-02-04

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PDB ID: 7r6p
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30928
MolProbity Validation Chart

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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 peptide toxin MIITX2-Mg1a from the venom of the Australian giant red bull ant Myrmecia gulosa

Deposition date:

2021-06-23

Original release date:

2022-02-04

Authors:

Chin, Y.; Eagle, D.; Bankala, K.; Robinson, S.

Citation:

Citation: Eagle, D.; Saez, N.; Bankala, K.; Bradford, J.; Chin, Y.; Starobova, H.; Mueller, A.; Deuis, J.; Reichelt, M.; Undheim, E.; Norton, R.; Thomas, W.; Vetter, I.; King, G.; Robinson, S.. "Solution structure of peptide toxin MIITX2-Mg1a from the venom of the Australian giant red bull ant Myrmecia gulosa" .

Assembly members:

Assembly members:
entity_1, polymer, 51 residues, 5861.392 Da.

Natural source:

Natural source: Common Name: Red bulldog ant Taxonomy ID: 36170 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Myrmecia gulosa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GDISDYGDPCSDDLKDYCIH GDCFFLKELNQPACRCYTGY YGSRCEHIDHN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	200
15N chemical shifts	50
1H chemical shifts	302

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 51 residues - 5861.392 Da.

1

GLY

ASP

ILE

SER

ASP

TYR

GLY

ASP

PRO

CYS

2

SER

ASP

LEU

LYS

ASP

TYR

CYS

ILE

HIS

3

GLY

ASP

CYS

PHE

LEU

LYS

GLU

LEU

ASN

4

GLN

PRO

ALA

CYS

ARG

CYS

TYR

THR

GLY

TYR

5

TYR

GLY

SER

ARG

CYS

GLU

HIS

ILE

ASP

HIS

6

ASN

Samples:

sample_1: MIITX2-Mg1a, [U-100% 13C; U-100% 15N], 350 uM; MES 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

TopSpin vv.3.2, Bruker Biospin - processing

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

TALOS-N, Yang Shen and Ad Bax - geometry optimization

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 900 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks