BMRB: 6802

Chemical shifts of the selected resonances in calmodulin alone and in complex with various sk-MLCK target peptides

Authors

Findlay, W.A., Gradwell, M.J., Bayley, P.M.

Assembly

CaM

Entity

1. CaM (polymer, Thiol state: unknown), 148 monomers, 16725.22 Da Detail

ADQLTEEQIA EFYEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGFI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

Formula weight

16725.22 Da

Source organism

Drosophila melanogaster

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 6.1 %, Completeness: 2.2 %, Completeness (bb): 1.3 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	2.2 % (19 of 866)	2.2 % (19 of 866)
Backbone	1.3 % (4 of 305)	1.3 % (4 of 305)
Sidechain	2.9 % (16 of 561)	2.9 % (16 of 561)
Aromatic	14.5 % (8 of 55)	14.5 % (8 of 55)
Methyl	0.0 % (0 of 71)	0.0 % (0 of 71)

1. calmodulin

ADQLTEEQIA EFYEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGFI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

Show sample condition

Sample

Temperature 303 (±0) K

#	Name	Isotope labeling	Type	Concentration
1	calmodulin			1 mM
2	Tris			10 mM
3	KCl			100 mM
4	CaCl2			10 mM

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Release date

2013-02-14

Citation

Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin
Findlay, W.A., Gradwell, M.J., Bayley, P.M.
Protein Sci. (1995), 4, 2375-2382, PubMed 8563635 , DOI 10.1002/pro.5560041116 , Abstract

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. CaM, : 2 : 293 entities Detail

Interaction partners 1. CaM, : 1 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail