BMRB Entry 4476
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4476
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Title: Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate PubMed: 9000078
Deposition date: 1998-12-22 Original release date: 2002-06-11
Authors: Antz, C.; Bauer, T.; Kalbacher, H.; Frank, R.; Covarrubias, M.; Kalbitzer, H.; Ruppersberg, J.; Baukrowitz, T.; Fakler, B.
Citation: Antz, C.; Geyer, M.; Fakler, B.; Schott, M.; Guy, H.; Frank, R.; Ruppersberg, J.; Kalbitzer, H.. "NMR structure of inactivation gates from mammalian voltage-dependent potassium channels" Nature 385, 272-275 (1997).
Assembly members:
Potassium channel, polymer, 30 residues, 185.072 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
Potassium channel: MISSVCVXSYRGRKSGNKPP
SKTCLKEEMA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 217 |