BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 4476

Title: Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate   PubMed: 9000078

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

Data sets:
Data typeCount
1H chemical shifts217

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Potassium channel1

Entities:

Entity 1, Potassium channel 30 residues - 185.072 Da.

1   METILESERSERVALCYSVALSEPSERTYR
2   ARGGLYARGLYSSERGLYASNLYSPROPRO
3   SERLYSTHRCYSLEULYSGLUGLUMETALA

Samples:

sample_1: Potassium channel mM

sample_cond_1: pH: 3.51; temperature: 283 K

sample_cond_2: pH: 6.8; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
not availablesample_1not availablenot available

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz

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