BMRB Entry 25151

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25151
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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:

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"  .

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pLic-MBP

Entity Sequences (FASTA):

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
  • Hide all

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