BMRB: 7029

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-FFF

Entity

1. calmodulin (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

2. FFF peptide (polymer, Thiol state: not present), 18 monomers, 2181.586 Da Detail

KRRFKKNFIA VSAANRFK

Total weight

18906.807 Da

Max. entity weight

16725.22 Da

Source organism

Drosophila melanogaster

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 6.0 %, Completeness: 1.5 %, Completeness (bb): 2.1 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	1.5 % (15 of 997)	1.5 % (15 of 997)
Backbone	2.1 % (7 of 341)	2.1 % (7 of 341)
Sidechain	1.2 % (8 of 656)	1.2 % (8 of 656)
Aromatic	5.7 % (4 of 70)	5.7 % (4 of 70)
Methyl	0.0 % (0 of 78)	0.0 % (0 of 78)

1. calmodulin

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

2. FFF peptide

KRRFKKNFIA VSAANRFK

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
5	FFF peptide			1 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. calmodulin, : 1 : 94 entities Detail

Related entities 2. FFF peptide, : 1 : 20 : 6 entities Detail

Interaction partners 2. FFF peptide, : 3 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 4 contents Detail