BMRB Entry 16928

Name: 1H, 13C and 15N chemical shift assignment of the N-terminal domain of the voltage-gated potassium channel-hERG
Published: 2010-07-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16928

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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:

1H, 13C and 15N chemical shift assignment of the N-terminal domain of the voltage-gated potassium channel-hERG

Deposition date:

2010-05-14

Original release date:

2010-07-16

Authors:

Li, Qingxin; Kang, Congbao

Citation:

Citation: Li, Qingxin; Raida, Manfred; Kang, CongBao. "1H, 13C and 15N chemical shift assignments for the N-terminal domain of the voltage-gated potassium channel-hERG." Biomol. NMR Assignments 4, 211-213 (2010).
PubMed: 20607461

Assembly members:

Assembly members:
hERG_NTD, polymer, 136 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: recombinant technology Host organism: Escherichia coli Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hERG_NTD: HMPVRRGHVAPQNTFLDTII RKFEGQSRKFIIANARVENC AVIYCNDGFCELCGYSRAEV MQRPCTCDFLHGPRTQRRAA AQIAQALLGAEERKVEIAFY RKDGSCFLCLVDVVPVKNED GAVIMFILNFEVVMEK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	516
15N chemical shifts	139
1H chemical shifts	610

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hERG N-terminal 135 residues	1

Entities:

Entity 1, hERG N-terminal 135 residues 136 residues - Formula weight is not available

Residue 0 H was from Factor Xa cleavage. This residue is not included in the assignment.

1

HIS

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1

BMRB	16946 17066
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

BMRB Entry 16928

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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