BMRB: 5922

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

Authors

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

Assembly

Potassium voltage-gated channel subfamily H member 2

Entity

1. Potassium voltage-gated channel subfamily H member 2 (polymer, Thiol state: not present), 42 monomers, 4547.008 Da Detail

AIGNXEQPHX DSRIGWLHNL GDQIGKPYNS SGLGGPSIKD KY

Formula weight

4547.008 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.2 %, Completeness: 85.8 %, Completeness (bb): 94.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	85.8 % (205 of 239)	85.8 % (205 of 239)
Backbone	94.0 % (79 of 84)	94.0 % (79 of 84)
Sidechain	81.3 % (126 of 155)	81.3 % (126 of 155)
Aromatic	77.8 % (14 of 18)	77.8 % (14 of 18)
Methyl	93.3 % (14 of 15)	93.3 % (14 of 15)

1. HERG S5-P linker

AIGNXEQPHX DSRIGWLHNL GDQIGKPYNS SGLGGPSIKD KY

Show sample condition

Sample

Pressure 1 atm, Temperature 303 (±1) K, pH 3.3 (±0.2), Details SDS micelles

#	Name	Isotope labeling	Type	Concentration
1	HERG S5-P linker			1.4 mM
2	SDS			100 mM
3	D2O			10 %
4	H2O			90 %

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Release date

2003-12-18

Citation

Structure of the HERG K+ channel S5P extracellular linker: role of an amphipathic alpha-helix in C-type inactivation
Torres, A.M., Bansal, P.S., Sunde, M., Clarke, C.E., Bursill, J.A., Smith, D.J., Bauskin, A., Breit, S.N., Campbell, T.J., Alewood, P.F., Kuchel, P.W., Vandenberg, J.I.
J. Biol. Chem. (2003), 278, 42136-42148, PubMed 12902341 , DOI 10.1074/jbc.M212824200 , Abstract

Related entities 1. Potassium voltage-gated channel subfamily H member 2, : 1 : 10 : 25 entities Detail

Interaction partners 1. Potassium voltage-gated channel subfamily H member 2, : 7 interactors Detail

Experiments performed 1 experiments Detail