BMRB Entry 34790

Name: JzTx-34 toxin peptide
Published: 2023-07-17

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PDB ID: 8ciq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34790
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:

JzTx-34 toxin peptide

Deposition date:

2023-02-10

Original release date:

2023-07-17

Authors:

Landon, C.; Meudal, H.

Citation:

Citation: Lopez, Ludivine; De Waard, Stephan; Meudal, Herve; Caumes, Cecile; Khakh, Kuldip; Peigneur, Steve; Oliveira-Mendes, Barbara; Lin, Sophia; De Waele, Jolien; Montnach, Jerome; Cestele, Sandrine; Tessier, Agnes; Johnson, J.; Mantegazza, Massimo; Tytgat, Jan; Cohen, Charles; Beroud, Remy; Bosmans, Frank; Landon, Celine; De Waard, Michel. "Structure-function relationship of new peptides activating human Nav1.1" Biomed. Pharmacother. 165, 115173-115173 (2023).
PubMed: 37453200

Assembly members:

Assembly members:
entity_1, polymer, 35 residues, 4163.808 Da.

Natural source:

Natural source: Common Name: spiders Taxonomy ID: 278059 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Chilobrachys not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ACREWLGGCSKDADCCAHLE CRKKWPYHCVWDWTV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	232

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 35 residues - 4163.808 Da.

1

ALA

CYS

ARG

GLU

TRP

LEU

GLY

CYS

SER

2

LYS

ASP

ALA

ASP

CYS

ALA

HIS

LEU

GLU

3

CYS

ARG

LYS

TRP

PRO

TYR

HIS

CYS

VAL

4

TRP

ASP

TRP

THR

VAL

Samples:

sample_1: JzTx-34 wild type 0.1 mM

sample_conditions_1: ionic strength: 0 Not defined; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	anisotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	anisotropic	sample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement, structure calculation

CcpNmr Analysis v2.1, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III HD 700 MHz