BMRB Entry 51063

Name: NaKd18 in 100 mM K+
Published: 2021-11-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51063

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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:

NaKd18 in 100 mM K+

Deposition date:

2021-08-24

Original release date:

2021-11-01

Authors:

Lewis, Adam; Kurauskas, Vilius; Tonelli, Marco; Henzler-Wildman, Katherine

Citation:

Citation: Lewis, Adam; Kurauskas, Vilius; Tonelli, Marco; Henzler-Wildman, Katherine. "Ion-dependent structure, dynamics, and allosteric coupling in a non-selective cation channel" Nat. Commun. 12, 6225-6225 (2021).
PubMed: 34711838

Assembly members:

Assembly members:
entity_1, polymer, 92 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: WKDKEFQVLFVLTILTLISG TIFYSTVEGLRPIDALYFSV VTLTTVGDGNFSPQTDFGKI FTILYIFIGIGLVFGFIHKL AVNVQLPSILSN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	235
15N chemical shifts	84
1H chemical shifts	207

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NaKd18, monomer 1	1
2	NaKd18, monomer 2	1
3	NaKd18, monomer 3	1
4	NaKd18, monomer 4	1

Entities:

Entity 1, NaKd18, monomer 1 92 residues - Formula weight is not available

1

TRP

LYS

ASP

LYS

GLU

PHE

GLN

VAL

LEU

PHE

2

VAL

LEU

THR

ILE

LEU

THR

LEU

ILE

SER

GLY

3

THR

ILE

PHE

TYR

SER

THR

VAL

GLU

GLY

LEU

4

ARG

PRO

ILE

ASP

ALA

LEU

TYR

PHE

SER

VAL

5

VAL

THR

LEU

THR

VAL

GLY

ASP

GLY

ASN

6

PHE

SER

PRO

GLN

THR

ASP

PHE

GLY

LYS

ILE

7

PHE

THR

ILE

LEU

TYR

ILE

PHE

ILE

GLY

ILE

8

GLY

LEU

VAL

PHE

GLY

PHE

ILE

HIS

LYS

LEU

9

ALA

VAL

ASN

VAL

GLN

LEU

PRO

SER

ILE

LEU

10

SER

ASN

Samples:

sample_1: NaKd18, [U-100% 13C; U-100% 15N; U-80% 2H], 550 uM; H2O 55 M; D2O 7%; MOPS 100 mM; KCl 100 mM

sample_2: NaKd18, [U-15N; U-2H], 550 uM; H2O 55 M; D2O 7%; MOPS 100 mM; KCl 100 mM

sample_3: NaKd18, [U-15N; U-2H, ILV 13C, 1H], 550 uM; H2O 55 M; D2O 7%; MOPS 100 mM; KCl 100 mM; DSS 50 uM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HMQC	sample_3	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_3	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 750 MHz
Bruker AVANCE III 600 MHz
Varian VNMRS 800 MHz

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