BMRB Entry 5922

Name: Solution Structure of the HERG K+ channel S5-P extracellular linker
Published: 2003-12-19

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PDB ID: 1ujl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5922
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of the HERG K+ channel S5-P extracellular linker

Deposition date:

2003-08-27

Original release date:

2003-12-19

Authors:

Torres, A.; Bansal, P.; Sunde, M.; Clarke, C.; Bursill, J.; Smith, D.; Bauskin, A.; Breit, S.; Campbell, T.; Alewood, P.; Kuchel, P.; Vandenberg, J.

Citation:

Citation: Torres, A.; Bansal, P.; Sunde, M.; Clarke, C.; Bursill, J.; Smith, D.; Bauskin, A.; Breit, S.; Campbell, T.; Alewood, P.; Kuchel, P.; Vandenberg, J.. "Structure of the HERG K+ channel S5P extracellular linker: Role of an amphipathic alpha-helix in c-type inactivation" J. Biol. Chem. 278, 42136-42148 (2003).
PubMed: 12902341

Assembly members:

Assembly members:
HERG S5-P linker, polymer, 42 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HERG S5-P linker: AIGNXEQPHXDSRIGWLHNL GDQIGKPYNSSGLGGPSIKD KY

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	250

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Potassium voltage-gated channel subfamily H member 2	1

Entities:

Entity 1, Potassium voltage-gated channel subfamily H member 2 42 residues - Formula weight is not available

1

ALA

ILE

GLY

ASN

NLE

GLU

GLN

PRO

HIS

NLE

2

ASP

SER

ARG

ILE

GLY

TRP

LEU

HIS

ASN

LEU

3

GLY

ASP

GLN

ILE

GLY

LYS

PRO

TYR

ASN

SER

4

SER

GLY

LEU

GLY

PRO

SER

ILE

LYS

ASP

5

LYS

TYR

Samples:

sample_1: HERG S5-P linker 1.4 mM; SDS 100 mM; D2O 10%; H2O 90%

sample_cond_1: pH: 3.3; temperature: 303 K; ionic strength: 0 M; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_1	not available	sample_cond_1

Software:

XWINNMR v3.1 - processing

XEASY v1.3.13 - data analysis

DYANA v1.5 - structure solution

CNS v1.1 - refinement

NMR spectrometers:

Bruker AVANCE 600 MHz