BMRB Entry 51645

Name: Full-length NaK ILV chemical shifts
Published: 2022-11-21

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

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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:

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:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	51
15N chemical shifts	21
1H chemical shifts	174

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NaK	1

Entities:

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

Residues -3 to 1 - residual after cleavage with thrombin

1

GLY

SER

HIS

MET

ALA

LEU

SER

PHE

LEU

2

THR

LEU

LYS

ARG

MET

LEU

ARG

ALA

CYS

LEU

3

ARG

ALA

TRP

LYS

ASP

LYS

GLU

PHE

GLN

VAL

4

LEU

PHE

VAL

LEU

THR

ILE

LEU

THR

LEU

ILE

5

SER

GLY

THR

ILE

PHE

TYR

SER

THR

VAL

GLU

6

GLY

LEU

ARG

PRO

ILE

ASP

ALA

LEU

TYR

PHE

7

SER

VAL

THR

LEU

THR

VAL

GLY

ASP

8

GLY

ASN

PHE

SER

PRO

GLN

THR

ASP

PHE

GLY

9

LYS

ILE

PHE

THR

ILE

LEU

TYR

ILE

PHE

ILE

10

GLY

ILE

GLY

LEU

VAL

PHE

GLY

PHE

ILE

HIS

11

LYS

LEU

ALA

VAL

ASN

VAL

GLN

LEU

PRO

SER

12

ILE

LEU

SER

ASN

ARG

LYS

GLU

Samples:

sample_1: Full-length NaK, [U-15N; U-2H, ILV 13C, 1H], 0.76 mM; MOPS 100 mM; KCl 100 mM; DMPC, [U-99% 2H], 44 mM; DHPC, [U-99% 2H], 113 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:

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

Software:

NMRPipe vVersion 9.0 - data analysis

TOPSPIN v3.6.2 - collection

NMR spectrometers:

Bruker AVANCE III 900 MHz

UNP	Q81HW2
AlphaFold	Q81HW2