BMRB Entry 30555

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30555
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Title:
Solution structure of AcaTx1, a potassium channel inhibitor from the sea anemone Antopleura cascaia
Deposition date:
2019-01-05
Original release date:
2020-01-10
Authors:
Amorim, G.; Madio, B.; Almeida, F.
Citation:

Citation: Amorim, G.; Almeida, F.; Madio, B.. "Structural Features of Potassium Channel Inhibition By Acatx1, A Novel Sea Anemone Neurotoxin."  .

Assembly members:

Assembly members:
entity_1, polymer, 32 residues, 3348.779 Da.

Natural source:

Natural source:   Common Name: Anthopleura   Taxonomy ID: 6109   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Anthopleura not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: CGGAGAKCSTKSDCCSGLWC SGSGHCYHRRYT

Data sets:
Data typeCount
13C chemical shifts82
15N chemical shifts25
1H chemical shifts159

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 32 residues - 3348.779 Da.

1   CYSGLYGLYALAGLYALALYSCYSSERTHR
2   LYSSERASPCYSCYSSERGLYLEUTRPCYS
3   SERGLYSERGLYHISCYSTYRHISARGARG
4   TYRTHR

Samples:

sample_1: AcaTx1, [U-99% 13C; U-99% 15N], 150 uM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_2: AcaTx1, [U-99% 15N], 150 uM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_2
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBCBCGCDHDsample_1isotropicsample_conditions_1
3D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

Analysis, Vranken et al., 2005 - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker AvanceIII 800 MHz

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