BMRB Entry 34793

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34793
MolProbity Validation Chart

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Title:
JzTx-34 toxin peptide W25A mutant
Deposition date:
2023-02-13
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, 4048.676 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 CRKKAPYHCVWDWTV

Data sets:
Data typeCount
15N chemical shifts32
1H chemical shifts228

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 35 residues - 4048.676 Da.

1   ALACYSARGGLUTRPLEUGLYGLYCYSSER
2   LYSASPALAASPCYSCYSALAHISLEUGLU
3   CYSARGLYSLYSALAPROTYRHISCYSVAL
4   TRPASPTRPTHRVAL

Samples:

sample_1: JzTx-34 W25A mutant (Jingzhaotoxin-34) 0.1 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1anisotropicsample_conditions_1
2D 1H-1H NOESYsample_1anisotropicsample_conditions_1
2D 1H-1H COSYsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
2D 1H-13C HSQCsample_1anisotropicsample_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

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