BMRB Entry 51646

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51646

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Title:
NaK d18 F92A ILV shifts
Deposition date:
2022-09-29
Original release date:
2022-11-21
Authors:
kurauskas, Vilius
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, 100 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: GSHMWKDKEFQVLFVLTILT LISGTIFYSTVEGLRPIDAL YFSVVTLTTVGDGNFSPQTD FGKIFTILYIFIGIGLVAGF IHKLAVNVQLPSILSNRKKE

Data sets:
Data typeCount
13C chemical shifts50
15N chemical shifts49
1H chemical shifts199

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NaKd18 F92A, 11
2NaKd18 F92A, 21
3NaKd18 F92A, 31
4NaKd18 F92A, 41

Entities:

Entity 1, NaKd18 F92A, 1 100 residues - Formula weight is not available

1   GLYSERHISMETTRPLYSASPLYSGLUPHE
2   GLNVALLEUPHEVALLEUTHRILELEUTHR
3   LEUILESERGLYTHRILEPHETYRSERTHR
4   VALGLUGLYLEUARGPROILEASPALALEU
5   TYRPHESERVALVALTHRLEUTHRTHRVAL
6   GLYASPGLYASNPHESERPROGLNTHRASP
7   PHEGLYLYSILEPHETHRILELEUTYRILE
8   PHEILEGLYILEGLYLEUVALALAGLYPHE
9   ILEHISLYSLEUALAVALASNVALGLNLEU
10   PROSERILELEUSERASNARGLYSLYSGLU

Samples:

sample_1: NaKd18 F92A tetramer, [U-15N; U-2H, ILV 13C, 1H], 0.9 mM; MOPS 100 mM; KCl 100 mM; DMPC, [U-2H], 59 mM; DHPC, [U-2H], 150 mM; DSS 50 uM; NaN3 0.1 mg

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HMQCsample_1isotropicsample_conditions_1
3D 13C, 13C NOESY HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe vVersion 9.0 - processing

TOPSPIN v3.6.2 - collection

CcpNMR v2.4.2 - data analysis

NMR spectrometers:

  • Bruker AVANCE III 900 MHz

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