BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30190

Title: Solution NMR structure of gHwTx-IV   PubMed: 28115115

Authors: Agwa, A.; Schroeder, C.

Citation: Agwa, A.; Lawrence, N.; Deplazes, E.; Cheneval, O.; Chen, R.; Craik, D.; Schroeder, C.; Henriques, S.. "Spider peptide toxin HwTx-IV engineered to bind to lipid membranes has an increased inhibitory potency at human voltage-gated sodium channel hNaV1.7."  Biochim. Biophys. Acta 1859, 835-844 (2017).

Assembly members:
entity_1, polymer, 36 residues, 4036.820 Da.

Natural source:   Common Name: Chinese bird spider   Taxonomy ID: 29017   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Haplopelma schmidti

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: GCLGIWKACNPSNDQCCKSS KLVCSRKTRWCKWQIX

Data sets:
Data typeCount
13C chemical shifts89
15N chemical shifts31
1H chemical shifts229

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 36 residues - 4036.820 Da.

1   GLYCYSLEUGLYILETRPLYSALACYSASN
2   PROSERASNASPGLNCYSCYSLYSSERSER
3   LYSLEUVALCYSSERARGLYSTHRARGTRP
4   CYSLYSTRPGLNILENH2

Samples:

sample_1: entity_1 mM; D2O, [U-2H], 10%; H2O 90%

sample_2: entity_1 mM; D2O, [U-2H], 100%

sample_conditions_1: pH: 4.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 4.0; pressure: 1 atm; temperature: 298 K

sample_conditions_3: pH: 4.0; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_3
2D 1H-1H TOCSYsample_1isotropicsample_conditions_3
1D 1Hsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
2D 1H-1H TOCSYsample_2isotropicsample_conditions_2
2D E.COSYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR, CCPN - chemical shift assignment

MOLPROBITY, Richardson - data analysis

TALOS-N, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

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