BMRB: 1648

Triple-Resonance Multidimensional NMR Study of Calmodulin Complexed with the Binding Domain of Skeletal Muscle Myosin Light-Chain Kinase: Indication of a Conformational Change in the Central Helix

Authors

Ikura, M., Kay, L.E., Krinks, M., Bax, A.

Assembly

calmodulin

Entity

1. calmodulin (polymer), 148 monomers, 16678.20 Da Detail

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGFI SAAELRHVMT NLGEKLTDEE VDEMIREANI DGDGQVNYEE FVTMMTSK

Formula weight

16678.2 Da

Source organism

Drosophila melanogaster

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 3.4 %, Completeness: 1.5 %, Completeness (bb): 2.3 % Detail

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Polymer type: polypeptide(L)

	Total	13C
All	1.5 % (10 of 646)	1.5 % (10 of 646)
Backbone	2.3 % (10 of 433)	2.3 % (10 of 433)
Sidechain	0.9 % (3 of 350)	0.9 % (3 of 350)
Aromatic	0.0 % (0 of 51)	0.0 % (0 of 51)
Methyl	0.0 % (0 of 71)	0.0 % (0 of 71)

1. calmodulin

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGFI SAAELRHVMT NLGEKLTDEE VDEMIREANI DGDGQVNYEE FVTMMTSK

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Sample

Temperature 320 K, pH 6.3

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Release date

1995-07-30

Citation

Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix
Ikura, M., Kay, L.E., Krinks, M., Bax, A.
Biochemistry (1991), 30, 5498-5504, PubMed 2036419 , DOI: , Abstract

Related entities 1. calmodulin, : 1 : 24 : 270 entities Detail

Interaction partners 1. calmodulin, : 1 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail