BMRB Entry 17066

Name: SOLUTION NMR STRUCTURE OF THE N-TERMINAL PAS DOMAIN OF HERG POTASSIUM CHANNEL
Published: 2011-05-23

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PDB ID: 2l0w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17066
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

SOLUTION NMR STRUCTURE OF THE N-TERMINAL PAS DOMAIN OF HERG POTASSIUM CHANNEL

Deposition date:

2010-07-19

Original release date:

2011-05-23

Authors:

Vandenberg, Jamie; Ng, Chai; Hunter, Mark; Mobli, Mehdi; King, Glenn; Kuchel, Philip

Citation:

Citation: Ng, Chai Ann; Hunter, Mark; Perry, Matthew; Mobli, Mehdi; Ke, Ying; Kuchel, Philip; King, Glenn; Stock, Daniela; Vandenberg, Jamie. "The N-terminal tail of hERG contains an amphipathic -helix that regulates channel deactivation." PLoS ONE 6, .-. (2011).
PubMed: 21249148

Assembly members:

Assembly members:
Potassium_voltage-gated_channel_subfamily_H_member_2, polymer, 136 residues, 45860.719 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PGEXT2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Potassium_voltage-gated_channel_subfamily_H_member_2: SMPVRRGHVAPQNTFLDTII RKFEGQSRKFIIANARVENC AVIYCNDGFCELCGYSRAEV MQRPCTCDFLHGPRTQRRAA AQIAQALLGAEERKVEIAFY RKDGSCFLCLVDVVPVKNED GAVIMFILNFEVVMEK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	531
15N chemical shifts	146
1H chemical shifts	887

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H_member_2	1

Entities:

Entity 1, H_member_2 136 residues - 45860.719 Da.

Residue 1 is from TEV cleavage site. This polypeptide is the N-terminal PAS domain of hERG Potassium channel.

1

SER

MET

PRO

VAL

ARG

GLY

HIS

VAL

ALA

2

PRO

GLN

ASN

THR

PHE

LEU

ASP

THR

ILE

3

ARG

LYS

PHE

GLU

GLY

GLN

SER

ARG

LYS

PHE

4

ILE

ALA

ASN

ALA

ARG

VAL

GLU

ASN

CYS

5

ALA

VAL

ILE

TYR

CYS

ASN

ASP

GLY

PHE

CYS

6

GLU

LEU

CYS

GLY

TYR

SER

ARG

ALA

GLU

VAL

7

MET

GLN

ARG

PRO

CYS

THR

CYS

ASP

PHE

LEU

8

HIS

GLY

PRO

ARG

THR

GLN

ARG

ALA

9

ALA

GLN

ILE

ALA

GLN

ALA

LEU

GLY

ALA

10

GLU

ARG

LYS

VAL

GLU

ILE

ALA

PHE

TYR

11

ARG

LYS

ASP

GLY

SER

CYS

PHE

LEU

CYS

LEU

12

VAL

ASP

VAL

PRO

VAL

LYS

ASN

GLU

ASP

13

GLY

ALA

VAL

ILE

MET

PHE

ILE

LEU

ASN

PHE

14

GLU

VAL

MET

GLU

LYS

Samples:

sample: sodium chloride 150 mM; HEPES 10 mM; TCEP 3 mM; D2O, [U-100% 2H], 7%; Octyl Glucoside 5 mM; H2O 93%; N15 labeled PAS, [U-99% 15N], 99%

sample_1: sodium chloride 150 mM; HEPES 10 mM; TCEP 3 mM; D2O, [U-100% 2H], 100%; Octyl Glucoside 5 mM; N15/C13 labeled PAS, [U-99% 13C; U-99% 15N], 99%

sample_conditions_1: ionic strength: 150 mM; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample	isotropic	sample_conditions_1
3D HNCACB	sample	isotropic	sample_conditions_1
3D C(CO)NH	sample	isotropic	sample_conditions_1
3D H(CCO)NH	sample	isotropic	sample_conditions_1
3D HNCO	sample	isotropic	sample_conditions_1
3D HNCA	sample	isotropic	sample_conditions_1
3D HN(CO)CA	sample	isotropic	sample_conditions_1
3D HNCA	sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement

AMBER v10, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - Dihedral angles calculation

TOPSPIN v2, Bruker Biospin - collection, processing

NMR spectrometers:

BRUKER Avance II 900 MHz

BMRB	16928 16946
PDB	1BYW 2L0W 2L1M 2L4R 4HP9 4HQA
DBJ	BAA37096 BAB19682
EMBL	CAA09232 CAB09536 CAB64868
GB	AAA62473 AAC53418 AAC53420 AAC53422 AAC99425
REF	NP_000229 NP_001003145 NP_001092571 NP_001166444 NP_001180587
SP	O08962 O35219 Q12809 Q8WNY2 Q9TSZ3
TPG	DAA30311
AlphaFold	O08962 O35219 Q12809 Q8WNY2 Q9TSZ3