BMRB Entry 26992

Name: Isolated voltage-sensing domain from second subunit of human sodium channel Nav1.4 in the LPPG micelles, N-formilated form
Published: 2017-01-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26992

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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:

Isolated voltage-sensing domain from second subunit of human sodium channel Nav1.4 in the LPPG micelles, N-formilated form

Deposition date:

2017-01-09

Original release date:

2017-01-19

Authors:

Myshkin, Mikhail; Paramonov, Alexander; Arseniev, Alexander; Shenkarev, Zakhar

Citation:

Citation: Paramonov, Alexander; Lyukmanova, Ekaterina; Myshkin, Mikhail; Shulepko, Mikhail; Kulbatskii, Dmitrii; Petrosian, Nikolay; Chugunov, Anton; Dolgikh, Dmitrii; Kirpichnikov, Mikhail; Arseniev, Alexander; Shenkarev, Zakhar. "NMR investigation of the isolated second voltage-sensing domain of human Nav1.4 channel" Biochim. Biophys. Acta 1859, 493-506 (2017).
PubMed: 28065835

Assembly members:

Assembly members:
Nav1.4-II, polymer, 153 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: pIVEX2.3d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nav1.4-II: XGKVLIWNSSAPWLKFKNII HLIVMDPFVDLGITISIVLN TLFMAMEHYPMTEHFDNVLT VGNLVFTGIFTAEMVLKLIA MDPYEYFQQGWNIFDSIIVT LSLVELGLANVQGLSVLRSF RLLRVFKLAKSWPTLNMLIK IIGNSGSHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1_formil

Data type	Count
13C chemical shifts	503
15N chemical shifts	149
1H chemical shifts	887

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NavIIform	1

Entities:

Entity 1, NavIIform 153 residues - Formula weight is not available

N-terminal formyl group. 6-His tag at the C-terminus.

1

FME

GLY

LYS

VAL

LEU

ILE

TRP

ASN

SER

2

ALA

PRO

TRP

LEU

LYS

PHE

LYS

ASN

ILE

3

HIS

LEU

ILE

VAL

MET

ASP

PRO

PHE

VAL

ASP

4

LEU

GLY

ILE

THR

ILE

SER

ILE

VAL

LEU

ASN

5

THR

LEU

PHE

MET

ALA

MET

GLU

HIS

TYR

PRO

6

MET

THR

GLU

HIS

PHE

ASP

ASN

VAL

LEU

THR

7

VAL

GLY

ASN

LEU

VAL

PHE

THR

GLY

ILE

PHE

8

THR

ALA

GLU

MET

VAL

LEU

LYS

LEU

ILE

ALA

9

MET

ASP

PRO

TYR

GLU

TYR

PHE

GLN

GLY

10

TRP

ASN

ILE

PHE

ASP

SER

ILE

VAL

THR

11

LEU

SER

LEU

VAL

GLU

LEU

GLY

LEU

ALA

ASN

12

VAL

GLN

GLY

LEU

SER

VAL

LEU

ARG

SER

PHE

13

ARG

LEU

ARG

VAL

PHE

LYS

LEU

ALA

LYS

14

SER

TRP

PRO

THR

LEU

ASN

MET

LEU

ILE

LYS

15

ILE

GLY

ASN

SER

GLY

SER

HIS

16

HIS

Samples:

sample_1: Nav1.4-II, [U-99% 13C; U-99% 15N], 0.6 mM; LPPG 5%

Sel1_CN-Ile: Nav1.4-II, [U-13C; U-15N]-Ile, 0.1 mM; LPPG 5%

Sel2_Leu_Val: Nav1.4-II, [U-15N]-Leu; [13C(1)]-Val, 0.1 mM; LPPG 5%

Sel3_TIFW: Nav1.4-II, [U-15N]-Thr; [13C(1)]-Ile; [13C(1)]-Phe; [U-13C; U-15N]-Trp], 0.1 mM; LPPG 5%

sample_conditions_1: ionic strength: 0.02 M; pH: 6.0; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	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
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	Sel1_CN-Ile	isotropic	sample_conditions_1
2D HNCO 1H-15N	Sel1_CN-Ile	isotropic	sample_conditions_1
2D HNCA 1H-15N	Sel1_CN-Ile	isotropic	sample_conditions_1
3D 1H-15N NOESY	Sel1_CN-Ile	isotropic	sample_conditions_1
2D 1H-15N HSQC	Sel2_Leu_Val	isotropic	sample_conditions_1
2D HNCO 1H-15N	Sel2_Leu_Val	isotropic	sample_conditions_1
2D HNCA 1H-15N	Sel2_Leu_Val	isotropic	sample_conditions_1
2D 1H-15N HSQC	Sel3_TIFW	isotropic	sample_conditions_1
2D HNCO 1H-15N	Sel3_TIFW	isotropic	sample_conditions_1
2D HNCA 1H-15N	Sel3_TIFW	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

MDDNMR, Vladislav Orekhov, Maxim Mayzel - processing

CARA, Rochus Keller - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

UNP	P35499
AlphaFold	Q7Z6B1