BMRB Entry 5922
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5922
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Title: Solution Structure of the HERG K+ channel S5-P extracellular linker PubMed: 12902341
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: 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).
Assembly members:
HERG S5-P linker, polymer, 42 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
HERG S5-P linker: AIGNXEQPHXDSRIGWLHNL
GDQIGKPYNSSGLGGPSIKD
KY
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 250 |