BMRB Entry 16946

Name: 15N, 13C and 1H Resonance Assignments of the PAS domain of hERG (KV11.1)
Published: 2010-08-18

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16946

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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:

15N, 13C and 1H Resonance Assignments of the PAS domain of hERG (KV11.1)

Deposition date:

2010-05-24

Original release date:

2010-08-18

Authors:

Muskett, Frederick; Mitcheson, John

Citation:

Citation: Muskett, Frederick; Mitcheson, John. "Resonance assignment and secondary structure prediction of the N-terminal domain of hERG (Kv11.1)." Biomol. NMR Assignments 5, 15-17 (2011).
PubMed: 20711762

Assembly members:

Assembly members:
hERG1-135, polymer, 150 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: pET-21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hERG1-135: MPVRRGHVAPQNTFLDTIIR KFEGQSRKFIIANARVENCA VIYCNDGFCELCGYSRAEVM QRPCTCDFLHGPRTQRRAAA QIAQALLGAEERKVEIAFYR KDGSCFLCLVDVVPVKNEDG AVIMFILNFEVVMEKENLYF QSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	522
15N chemical shifts	141
1H chemical shifts	873

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hERG1-135	1

Entities:

Entity 1, hERG1-135 150 residues - Formula weight is not available

1	MET	PRO	VAL	ARG	ARG	GLY	HIS	VAL	ALA	PRO
2	GLN	ASN	THR	PHE	LEU	ASP	THR	ILE	ILE	ARG
3	LYS	PHE	GLU	GLY	GLN	SER	ARG	LYS	PHE	ILE
4	ILE	ALA	ASN	ALA	ARG	VAL	GLU	ASN	CYS	ALA
5	VAL	ILE	TYR	CYS	ASN	ASP	GLY	PHE	CYS	GLU
6	LEU	CYS	GLY	TYR	SER	ARG	ALA	GLU	VAL	MET
7	GLN	ARG	PRO	CYS	THR	CYS	ASP	PHE	LEU	HIS
8	GLY	PRO	ARG	THR	GLN	ARG	ARG	ALA	ALA	ALA
9	GLN	ILE	ALA	GLN	ALA	LEU	LEU	GLY	ALA	GLU
10	GLU	ARG	LYS	VAL	GLU	ILE	ALA	PHE	TYR	ARG
11	LYS	ASP	GLY	SER	CYS	PHE	LEU	CYS	LEU	VAL
12	ASP	VAL	VAL	PRO	VAL	LYS	ASN	GLU	ASP	GLY
13	ALA	VAL	ILE	MET	PHE	ILE	LEU	ASN	PHE	GLU
14	VAL	VAL	MET	GLU	LYS	GLU	ASN	LEU	TYR	PHE
15	GLN	SER	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

Samples:

sample_1: hERG1-135, [U-100% 13C; U-100% 15N], 0.2 mM; H20 90%; D20 10%; EDTA 500 uM; AEBSF 200 uM; DTT 200 uM; Sodium_Azide 0.02 % w/v; acetate buffer 20 mM

sample_2: hERG1-135, [U-100% 15N], 0.2 mM; H20 90%; D20 10%; EDTA 500 uM; AEBSF 200 uM; DTT 200 uM; Sodium_Azide 0.02 % w/v; acetate buffer 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

TALOS v1.2, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 800 MHz

BMRB	16928 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

1	MET	PRO	VAL	ARG	ARG	GLY	HIS	VAL	ALA	PRO
2	GLN	ASN	THR	PHE	LEU	ASP	THR	ILE	ILE	ARG
3	LYS	PHE	GLU	GLY	GLN	SER	ARG	LYS	PHE	ILE
4	ILE	ALA	ASN	ALA	ARG	VAL	GLU	ASN	CYS	ALA
5	VAL	ILE	TYR	CYS	ASN	ASP	GLY	PHE	CYS	GLU
6	LEU	CYS	GLY	TYR	SER	ARG	ALA	GLU	VAL	MET
7	GLN	ARG	PRO	CYS	THR	CYS	ASP	PHE	LEU	HIS
8	GLY	PRO	ARG	THR	GLN	ARG	ARG	ALA	ALA	ALA
9	GLN	ILE	ALA	GLN	ALA	LEU	LEU	GLY	ALA	GLU
10	GLU	ARG	LYS	VAL	GLU	ILE	ALA	PHE	TYR	ARG
11	LYS	ASP	GLY	SER	CYS	PHE	LEU	CYS	LEU	VAL
12	ASP	VAL	VAL	PRO	VAL	LYS	ASN	GLU	ASP	GLY
13	ALA	VAL	ILE	MET	PHE	ILE	LEU	ASN	PHE	GLU
14	VAL	VAL	MET	GLU	LYS	GLU	ASN	LEU	TYR	PHE
15	GLN	SER	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	PRO	VAL	ARG	ARG	GLY	HIS	VAL	ALA	PRO
2	GLN	ASN	THR	PHE	LEU	ASP	THR	ILE	ILE	ARG
3	LYS	PHE	GLU	GLY	GLN	SER	ARG	LYS	PHE	ILE
4	ILE	ALA	ASN	ALA	ARG	VAL	GLU	ASN	CYS	ALA
5	VAL	ILE	TYR	CYS	ASN	ASP	GLY	PHE	CYS	GLU
6	LEU	CYS	GLY	TYR	SER	ARG	ALA	GLU	VAL	MET
7	GLN	ARG	PRO	CYS	THR	CYS	ASP	PHE	LEU	HIS
8	GLY	PRO	ARG	THR	GLN	ARG	ARG	ALA	ALA	ALA
9	GLN	ILE	ALA	GLN	ALA	LEU	LEU	GLY	ALA	GLU
10	GLU	ARG	LYS	VAL	GLU	ILE	ALA	PHE	TYR	ARG
11	LYS	ASP	GLY	SER	CYS	PHE	LEU	CYS	LEU	VAL
12	ASP	VAL	VAL	PRO	VAL	LYS	ASN	GLU	ASP	GLY
13	ALA	VAL	ILE	MET	PHE	ILE	LEU	ASN	PHE	GLU
14	VAL	VAL	MET	GLU	LYS	GLU	ASN	LEU	TYR	PHE
15	GLN	SER	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS