BMRB Entry 25774

Title:
Chemical Shift Assignments and Structure Determination for spider toxin, U4-agatoxin-Ao1a
Deposition date:
2015-08-27
Original release date:
2016-08-25
Authors:
Pineda, Sandy; Chin, Yanni; Mobli, Mehdi; King, Glenn
Citation:

Citation: Pineda, Sandy; Chin, Yanni K-Y; Undheim, Eivind; Senff, Sebastian; Mobli, Mehdi; Dauly, Claire; Escoubas, Pierre; Nicholson, Graham; Kaas, Quentin; Guo, Shaodong; Herzig, Volker; Mattick, John; King, Glenn. "Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene"  Proc. Natl. Acad. Sci. U. S. A. 117, 11399-11408 (2020).
PubMed: 32398368

Assembly members:

Assembly members:
U4-agatoxin-Ao1a, polymer, 32 residues, 3429.153 Da.

Natural source:

Natural source:   Common Name: spiders   Taxonomy ID: 293813   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Agelena orientalis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pLICC vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
U4-agatoxin-Ao1a: GYCAEKGIKCHNIHCCSGLT CKCKGSSCVCRK

Data sets:
Data typeCount
13C chemical shifts124
15N chemical shifts31
1H chemical shifts191

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1spider toxin, U4-agatoxin-Ao1a1

Entities:

Entity 1, spider toxin, U4-agatoxin-Ao1a 32 residues - 3429.153 Da.

1   GLYTYRCYSALAGLULYSGLYILELYSCYS
2   HISASNILEHISCYSCYSSERGLYLEUTHR
3   CYSLYSCYSLYSGLYSERSERCYSVALCYS
4   ARGLYS

Samples:

sample_1: SF23, [U-99% 13C; U-99% 15N], 300 uM; D2O 5%; MES 20 mM; DSS 10 uM; sodium azide 5%; H2O 90%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

TALOS vtalos+, Cornilescu, Delaglio and Bax - Obtain dihedral angle restraints

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Rowland_NMR_Toolkit, Hoch JC - processing NUS data

NMR spectrometers:

  • Bruker Avance II+ 900 MHz

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