BMRB Entry 19300

Title:
Solution structure of protoxin-1
Deposition date:
2013-06-13
Original release date:
2014-04-28
Authors:
Daly, Norelle
Citation:

Citation: Gui, Junhong; Liu, Boyi; Cao, Guan; Lipchik, Andrew; Perez, Minervo; Dekan, Zoltan; Mobli, Mehdi; Daly, Norelle; Alewood, Paul; Parker, Laurie; King, Glenn; Zhou, Yufeng; Jordt, Sven-Eric; Nitabach, Michael. "A tarantula-venom peptide antagonizes the TRPA1 nociceptor ion channel by binding to the S1-S4 gating domain"  Curr. Biol. 24, 473-483 (2014).
PubMed: 24530065

Assembly members:

Assembly members:
entity, polymer, 35 residues, 3999.598 Da.

Natural source:

Natural source:   Common Name: green velvet   Taxonomy ID: 213387   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Thrixopelma pruriens

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: ECRYWLGGCSAGQTCCKHLV CSRRHGWCVWDGTFS

Data sets:
Data typeCount
13C chemical shifts81
15N chemical shifts32
1H chemical shifts212

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protoxin-11

Entities:

Entity 1, protoxin-1 35 residues - 3999.598 Da.

1   GLUCYSARGTYRTRPLEUGLYGLYCYSSER
2   ALAGLYGLNTHRCYSCYSLYSHISLEUVAL
3   CYSSERARGARGHISGLYTRPCYSVALTRP
4   ASPGLYTHRPHESER

Samples:

sample_1: protoxin-1 0.5 mM

sample_2: protoxin-1 0.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CcpNMR, CCPN - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

PDB
SP P83480
AlphaFold P83480

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