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 16468

Title: High-resolution solution structure of the ASIC1a blocker PcTX1

Deposition date: 2009-08-25 Original release date: 2012-08-03

Authors: King, Glenn; Mobli, Mehdi; Saez, Natalie

Citation: Saez, Natalie; Mobli, Mehdi; Rash, Lachlan; King, Glenn. "High-resolution solution structure of the ASIC1a blocker PcTx1"  To be Published ., .-..

Assembly members:
PcTx1, polymer, 41 residues, 4792.611 Da.

Natural source:   Common Name: Trinidad chevron tarantula   Taxonomy ID: 179874   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Psalmopoeus cambridgei

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

Entity Sequences (FASTA):
PcTx1: SEDCIPKWKGCVNRHGDCCE GLECWKRRRSFEVCVPKTPK T

Data sets:
Data typeCount
13C chemical shifts161
15N chemical shifts42
1H chemical shifts273

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PcTx11

Entities:

Entity 1, PcTx1 41 residues - 4792.611 Da.

Residue 1 is a vestige of the TEV cleavage site used for recombinant production of the protein.

1   SERGLUASPCYSILEPROLYSTRPLYSGLY
2   CYSVALASNARGHISGLYASPCYSCYSGLU
3   GLYLEUGLUCYSTRPLYSARGARGARGSER
4   PHEGLUVALCYSVALPROLYSTHRPROLYS
5   THR

Samples:

sample_1: PcTx1, [U-99% 13C; U-99% 15N], 0.3 mM; sodium phosphate buffer, pH 6.0 10 mM; D2O 7%; H2O 93%

sample_2: PcTx1, [U-99% 13C; U-99% 15N], 0.3 mM; sodium phosphate buffer, pH 6.0 10 mM; D2O 100%

sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
4D HC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement, structure solution

XEASY, Bartels et al. - chemical shift assignment

Rowland NMR Toolkit, Hoch, Stern et al. - processing

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

PDB
UNP P60514
BMRB 26504
SP P60514

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