BMRB Entry 27220

Name: ssNMR assignment of membrane embedded NaK channel (ion-favored conformer)
Published: 2018-02-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27220

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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:

ssNMR assignment of membrane embedded NaK channel (ion-favored conformer)

Deposition date:

2017-08-15

Original release date:

2018-02-19

Authors:

Shi, Chaowei; He, Yao; Hendriks, Kitty; de Groot, Bert L.; Tian, Changlin; Lange, Adam; Sun, Han

Citation:

Citation: Shi, Chaowei; He, Yao; Hendriks, Kitty; de Groot, Bert; Cai, Xiaoying; Tian, Changlin; Lange, Adam; Sun, Han. "A single NaK channel conformation is not enough for non-selective ion conduction" Nat. Commun. 9, 717-717 (2018).
PubMed: 29459730

Assembly members:

Assembly members:
NaK_Channel, polymer, 106 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NaK_Channel: MGHHHHHHMAWKDKEFQVLF VLTILTLISGTIFYSTVEGL RPIDALYFSVVTLTTVGDGN FSPQTDFGKIFTILYIFIGI GLVFGFIHKLAVNVQLPSIL SNRKKE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	231
15N chemical shifts	55

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NaK channel	1

Entities:

Entity 1, NaK channel 106 residues - Formula weight is not available

1

MET

GLY

HIS

MET

ALA

2

TRP

LYS

ASP

LYS

GLU

PHE

GLN

VAL

LEU

PHE

3

VAL

LEU

THR

ILE

LEU

THR

LEU

ILE

SER

GLY

4

THR

ILE

PHE

TYR

SER

THR

VAL

GLU

GLY

LEU

5

ARG

PRO

ILE

ASP

ALA

LEU

TYR

PHE

SER

VAL

6

VAL

THR

LEU

THR

VAL

GLY

ASP

GLY

ASN

7

PHE

SER

PRO

GLN

THR

ASP

PHE

GLY

LYS

ILE

8

PHE

THR

ILE

LEU

TYR

ILE

PHE

ILE

GLY

ILE

9

GLY

LEU

VAL

PHE

GLY

PHE

ILE

HIS

LYS

LEU

10

ALA

VAL

ASN

VAL

GLN

LEU

PRO

SER

ILE

LEU

11

SER

ASN

ARG

LYS

GLU

Samples:

sample_1: NaK Channel, [U-99% 13C; U-99% 15N], 10 mg; TRIS 20 mM; sodium chloride 50 mM; Asolectin 5 mg

sample_conditions_1: ionic strength: 50 mM; pH: 8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D PDSD	sample_1	solid	sample_conditions_1
2D NCA	sample_1	solid	sample_conditions_1
2D NCO	sample_1	solid	sample_conditions_1
3D CANCO	sample_1	solid	sample_conditions_1
3D NCOCA	sample_1	solid	sample_conditions_1
3D NCOCACB	sample_1	solid	sample_conditions_1
2D CANCOCA	sample_1	solid	sample_conditions_1
3D NCACX	sample_1	solid	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 700 MHz

UniProt	Q81HW2
AlphaFold	Q81HW2