BMRB Entry 51644

Name: ILV chemical shifts of NaK2K d18
Published: 2022-11-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51644

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

ILV chemical shifts of NaK2K d18

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, 100 residues, 11240.2117 Da.

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 YFSVVTLTTVGYGDFSPQTD FGKIFTILYIFIGIGLVFGF IHKLAVNVQLPSILSNRKKE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	52
1H chemical shifts	156

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NaK2K, 1	1
2	NaK2K, 2	1
3	NaK2K, 3	1
4	NaK2K, 4	1

Entities:

Entity 1, NaK2K, 1 100 residues - 11240.2117 Da.

Residues 15-18 represents remainder after cleavage with thrombin protease

1	GLY	SER	HIS	MET	TRP	LYS	ASP	LYS	GLU	PHE
2	GLN	VAL	LEU	PHE	VAL	LEU	THR	ILE	LEU	THR
3	LEU	ILE	SER	GLY	THR	ILE	PHE	TYR	SER	THR
4	VAL	GLU	GLY	LEU	ARG	PRO	ILE	ASP	ALA	LEU
5	TYR	PHE	SER	VAL	VAL	THR	LEU	THR	THR	VAL
6	GLY	TYR	GLY	ASP	PHE	SER	PRO	GLN	THR	ASP
7	PHE	GLY	LYS	ILE	PHE	THR	ILE	LEU	TYR	ILE
8	PHE	ILE	GLY	ILE	GLY	LEU	VAL	PHE	GLY	PHE
9	ILE	HIS	LYS	LEU	ALA	VAL	ASN	VAL	GLN	LEU
10	PRO	SER	ILE	LEU	SER	ASN	ARG	LYS	LYS	GLU

Name	Sample	Sample state	Sample conditions
2D 1H-13C HMQC	sample_1	isotropic	sample_conditions_1
3D 13C,13C NOESY HSQC	sample_1	isotropic	sample_conditions_1

BMRB Entry 51644

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	GLY	SER	HIS	MET	TRP	LYS	ASP	LYS	GLU	PHE
2	GLN	VAL	LEU	PHE	VAL	LEU	THR	ILE	LEU	THR
3	LEU	ILE	SER	GLY	THR	ILE	PHE	TYR	SER	THR
4	VAL	GLU	GLY	LEU	ARG	PRO	ILE	ASP	ALA	LEU
5	TYR	PHE	SER	VAL	VAL	THR	LEU	THR	THR	VAL
6	GLY	TYR	GLY	ASP	PHE	SER	PRO	GLN	THR	ASP
7	PHE	GLY	LYS	ILE	PHE	THR	ILE	LEU	TYR	ILE
8	PHE	ILE	GLY	ILE	GLY	LEU	VAL	PHE	GLY	PHE
9	ILE	HIS	LYS	LEU	ALA	VAL	ASN	VAL	GLN	LEU
10	PRO	SER	ILE	LEU	SER	ASN	ARG	LYS	LYS	GLU

1	GLY	SER	HIS	MET	TRP	LYS	ASP	LYS	GLU	PHE
2	GLN	VAL	LEU	PHE	VAL	LEU	THR	ILE	LEU	THR
3	LEU	ILE	SER	GLY	THR	ILE	PHE	TYR	SER	THR
4	VAL	GLU	GLY	LEU	ARG	PRO	ILE	ASP	ALA	LEU
5	TYR	PHE	SER	VAL	VAL	THR	LEU	THR	THR	VAL
6	GLY	TYR	GLY	ASP	PHE	SER	PRO	GLN	THR	ASP
7	PHE	GLY	LYS	ILE	PHE	THR	ILE	LEU	TYR	ILE
8	PHE	ILE	GLY	ILE	GLY	LEU	VAL	PHE	GLY	PHE
9	ILE	HIS	LYS	LEU	ALA	VAL	ASN	VAL	GLN	LEU
10	PRO	SER	ILE	LEU	SER	ASN	ARG	LYS	LYS	GLU

1	GLY	SER	HIS	MET	TRP	LYS	ASP	LYS	GLU	PHE
2	GLN	VAL	LEU	PHE	VAL	LEU	THR	ILE	LEU	THR
3	LEU	ILE	SER	GLY	THR	ILE	PHE	TYR	SER	THR
4	VAL	GLU	GLY	LEU	ARG	PRO	ILE	ASP	ALA	LEU
5	TYR	PHE	SER	VAL	VAL	THR	LEU	THR	THR	VAL
6	GLY	TYR	GLY	ASP	PHE	SER	PRO	GLN	THR	ASP
7	PHE	GLY	LYS	ILE	PHE	THR	ILE	LEU	TYR	ILE
8	PHE	ILE	GLY	ILE	GLY	LEU	VAL	PHE	GLY	PHE
9	ILE	HIS	LYS	LEU	ALA	VAL	ASN	VAL	GLN	LEU
10	PRO	SER	ILE	LEU	SER	ASN	ARG	LYS	LYS	GLU