BMRB Entry 19708

Name: Voltage Sensor Domain of human KCNQ1 (VSD-Q1)
Published: 2014-04-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19708

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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:

Voltage Sensor Domain of human KCNQ1 (VSD-Q1)

Deposition date:

2013-12-26

Original release date:

2014-04-11

Authors:

Peng, Dungeng; Law, Cheryl

Citation:

Citation: Peng, Dungeng; Kim, Ji-Hun; Kroncke, Brett; Law, Cheryl; Xia, Yan; Droege, Kristin; Van Horn, Wade; Vanoye, Carlos; Sanders, Charles. "Purification and Structural Study of the Voltage-Sensor Domain of the Human KCNQ1 Potassium Ion Channel." Biochemistry 53, 2032-2042 (2014).
PubMed: 24606221

Assembly members:

Assembly members:
VSD-Q1, polymer, 153 residues, 17473 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VSD-Q1: MGHHHHHHGVLARTHVQGRV YNFLERPTGWKCFVYHFAVF LIVLVCLIFSVLSTIEQYAA LATGTLFWMEIVLVVFFGTE YVVRLWSAGCRSKYVGLWGR LRFARKPISIIDLIVVVASM VVLCVGSKGQVFATSAIRGI RFLQILRMLHVDR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	278
15N chemical shifts	137
1H chemical shifts	137

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Voltage Sensor Domain	1

Entities:

Entity 1, Voltage Sensor Domain 153 residues - 17473 Da.

Residues 1-9 are non-native hexa histidine-6 tag; Sequence number counts from the valine after the His-tag.

1

MET

GLY

HIS

GLY

VAL

2

LEU

ALA

ARG

THR

HIS

VAL

GLN

GLY

ARG

VAL

3

TYR

ASN

PHE

LEU

GLU

ARG

PRO

THR

GLY

TRP

4

LYS

CYS

PHE

VAL

TYR

HIS

PHE

ALA

VAL

PHE

5

LEU

ILE

VAL

LEU

VAL

CYS

LEU

ILE

PHE

SER

6

VAL

LEU

SER

THR

ILE

GLU

GLN

TYR

ALA

7

LEU

ALA

THR

GLY

THR

LEU

PHE

TRP

MET

GLU

8

ILE

VAL

LEU

VAL

PHE

GLY

THR

GLU

9

TYR

VAL

ARG

LEU

TRP

SER

ALA

GLY

CYS

10

ARG

SER

LYS

TYR

VAL

GLY

LEU

TRP

GLY

ARG

11

LEU

ARG

PHE

ALA

ARG

LYS

PRO

ILE

SER

ILE

12

ILE

ASP

LEU

ILE

VAL

ALA

SER

MET

13

VAL

LEU

CYS

VAL

GLY

SER

LYS

GLY

GLN

14

VAL

PHE

ALA

THR

SER

ALA

ILE

ARG

GLY

ILE

15

ARG

PHE

LEU

GLN

ILE

LEU

ARG

MET

LEU

HIS

16

VAL

ASP

ARG

Samples:

sample_1: VSD-Q1, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; MES buffer 50 mM; EDTA 0.5 mM; TCEP 2 mM

sample_2: VSD-Q1, [U-100% 15N], 0.5 mM; MES buffer 50 mM; EDTA 0.5 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.50; pressure: 1 atm; temperature: 323 K

Experiments:

Name	Sample	Sample state	Sample conditions
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 HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.106, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 900 MHz
Bruker Avance 600 MHz

DBJ	BAA34738 BAC15571 BAE32460 BAF83307 BAG73570
EMBL	CAB38863 CAB44649 CAB44650
GB	AAB36518 AAC05498 AAC05705 AAC51776 AAC51781
REF	NP_000209 NP_001166292 NP_001192370 NP_032460 NP_114462
SP	O70344 P51787 P97414 Q9MYS6 Q9Z0N7
TPG	DAA13511
AlphaFold	O70344 P51787 P97414 Q9MYS6 Q9Z0N7