BMRB: 5092

1H chemical shift assignments for the cytoplasmic N-terminus of KCNMB2

Authors

Bentrop, D., Beyermann, M., Wissmann, R., Fakler, B.

Assembly

beta2 subunit of BK channels

Entity

1. beta2 subunit of BK channels (polymer, Thiol state: not present), 45 monomers, 5367.966 Da Detail

MFIWTSGRTS SSYRHDEKRN IYQKIRDHDL LDKRKTVTAL KAGED

Formula weight

5367.966 Da

Source organism

Homo sapiens

Exptl. method

NMR

Refine. method

simulated annealing, torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 99.3 %, Completeness (bb): 98.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	99.3 % (284 of 286)	99.3 % (284 of 286)
Backbone	98.9 % (91 of 92)	98.9 % (91 of 92)
Sidechain	99.5 % (193 of 194)	99.5 % (193 of 194)
Aromatic	100.0 % (23 of 23)	100.0 % (23 of 23)
Methyl	100.0 % (20 of 20)	100.0 % (20 of 20)

1. beta2 subunit of BK channels

MFIWTSGRTS SSYRHDEKRN IYQKIRDHDL LDKRKTVTAL KAGED

Show sample condition

Sample

Temperature 288 (±0.3) K, pH 3.0 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	beta2 subunit of BK channels			2.0 mM

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Protein Blocks Logo

Calculated from 24 models in PDB: 1JO6, Strand ID: A Detail

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Release date

2001-07-30

Citation

NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels
Bentrop, D., Beyermann, M., Wissmann, R., Fakler, B.
J. Biol. Chem. (2001), 276, 42116-42121, PubMed 11517232 , DOI 10.1074/jbc.M107118200 , Abstract

Entries sharing articles Swiss-Prot: 1 entries Detail

Related entities 1. beta2 subunit of BK channels, : 1 : 4 : 2 : 11 entities Detail

Interaction partners 1. beta2 subunit of BK channels, : 1 interactors Detail

Experiments performed 3 experiments Detail