BMRB Entry 51645

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51645

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Title:
Full-length NaK ILV chemical shifts
Deposition date:
2022-09-29
Original release date:
2022-11-21
Authors:
Henzler-Wildman, Katherine
Citation:

Citation: Kurauskas, Vilius; Tonelli, Marco; Henzler-Wildman, Katherine. "Full opening of helix bundle does not lead to NaK channel activation"  J. Gen. Physiol. 154, e202213196-e202213196 (2022).
PubMed: 36326620

Assembly members:

Assembly members:
entity_1, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacillus cereus   Taxonomy ID: 1396   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus cereus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMALSFLLTLKRMLRACL RAWKDKEFQVLFVLTILTLI SGTIFYSTVEGLRPIDALYF SVVTLTTVGDGNFSPQTDFG KIFTILYIFIGIGLVFGFIH KLAVNVQLPSILSNRKKE

Data sets:
Data typeCount
13C chemical shifts51
15N chemical shifts21
1H chemical shifts174

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1NaK1

Entities:

Entity 1, NaK 118 residues - Formula weight is not available

Residues -3 to 1 - residual after cleavage with thrombin

1   GLYSERHISMETALALEUSERPHELEULEU
2   THRLEULYSARGMETLEUARGALACYSLEU
3   ARGALATRPLYSASPLYSGLUPHEGLNVAL
4   LEUPHEVALLEUTHRILELEUTHRLEUILE
5   SERGLYTHRILEPHETYRSERTHRVALGLU
6   GLYLEUARGPROILEASPALALEUTYRPHE
7   SERVALVALTHRLEUTHRTHRVALGLYASP
8   GLYASNPHESERPROGLNTHRASPPHEGLY
9   LYSILEPHETHRILELEUTYRILEPHEILE
10   GLYILEGLYLEUVALPHEGLYPHEILEHIS
11   LYSLEUALAVALASNVALGLNLEUPROSER
12   ILELEUSERASNARGLYSLYSGLU

Related Database Links:

UNP Q81HW2
AlphaFold Q81HW2

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