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 25151

Title: Solution structure of spider-venom peptide Hs1a

Deposition date: 2014-08-14 Original release date: 2015-08-17

Authors: Klint, Julie; King, Glenn; Mobli, Mehdi

Citation: Klint, Julie; Castro, Joel; Vetter, Irina; Er, Sing; Cardoso, Fernanda; Liu, Yi; Hagan, Rebecca; Neff, Robert; Minassian, Natali; Huang, Johnny; Cooper, Matt; Wickenden, Alan; Mobli, Mehdi; Jin, Lian; Nicolazzo, Joseph; Lewis, Richard; Bosmans, Frank; Brierley, Stuart; King, Glenn. "Nav1.7 inhibitors normalise mechanical responses in chronic visceral hypersensitivity"  Not known ., .-..

Assembly members:
Hs1a, polymer, 35 residues, 3866.550 Da.

Natural source:   Common Name: Tarantula   Taxonomy ID: 118971   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Hysterocrates spec

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

Entity Sequences (FASTA):
Hs1a: GNDCLGFWSACNPKNDKCCA NLVCSSKHKWCKGKL

Data sets:
Data typeCount
13C chemical shifts111
15N chemical shifts39
1H chemical shifts228

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Hs1a1

Entities:

Entity 1, Hs1a 35 residues - 3866.550 Da.

1   GLYASNASPCYSLEUGLYPHETRPSERALA
2   CYSASNPROLYSASNASPLYSCYSCYSALA
3   ASNLEUVALCYSSERSERLYSHISLYSTRP
4   CYSLYSGLYLYSLEU

Samples:

sample_1: Hs1a, [U-98% 13C; U-98% 15N], 0.5 mM; sodium acetate 20 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 20 mM; pH: 4.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
4D HCC(CO)NH TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection

Rowland_NMR_Toolkit v3, Jeffrey C. Hoch & Alan Stern - processing

XEASY, Bartels et al. - data analysis, peak picking

Talos+, Cornilescu, Delaglio and Bax - data analysis

CYANA v3, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts