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Backbone 1H, 13C, 15N and sidechain 1H Chemical shift of CPI-17
Authors
Ohki, S., Eto, M., Kariya, E., Hayano, T., Hayashi, Y., Yazawa, M., Brautigan, D., Kainosho, M.
Assembly
CPI-17 (35-120) deletion mutant
Entity
1. CPI-17 (35-120) deletion mutant (polymer, Thiol state: all free), 86 monomers, 10295.55 Da Detail

ARVTVKYDRR ELQRRLDVEK WIDGRLEELY RGREADMPDE VNIDELLELE SEEERSRKIQ GLLKSCTNPT ENFVQELLVK LRGLHK


Formula weight
10295.55 Da
Source organism
Sus scrofa
Exptl. method
NMR
Refine. method
distance geometry
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 73.4 %, Completeness (bb): 84.4 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All73.4 % (771 of 1050)90.3 % (505 of 559)45.5 % (182 of 400)92.3 % (84 of 91)
Backbone84.4 % (432 of 512)100.0 % (174 of 174)68.5 % (174 of 254)100.0 % (84 of 84)
Sidechain67.9 % (421 of 620)86.0 % (331 of 385)39.5 % (90 of 228) 0.0 % (0 of 7)
Aromatic38.1 % (16 of 42)76.2 % (16 of 21) 0.0 % (0 of 20) 0.0 % (0 of 1)
Methyl58.2 % (57 of 98)100.0 % (49 of 49)16.3 % (8 of 49)

1. CPI-17

ARVTVKYDRR ELQRRLDVEK WIDGRLEELY RGREADMPDE VNIDELLELE SEEERSRKIQ GLLKSCTNPT ENFVQELLVK LRGLHK

Sample

Temperature 298 (±0.1) K, pH 6.8 (±0.05)


#NameIsotope labelingTypeConcentration
1CPI-170.8 ~ 1.3 mM

Protein Blocks Logo
Calculated from 1 models in PDB: 1K5O, Strand ID: A Detail


Release date
2002-05-05
Citation
Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation
Ohki, S., Eto, M., Kariya, E., Hayano, T., Hayashi, Y., Yazawa, M., Brautigan, D., Kainosho, M.
J. Mol. Biol. (2001), 314, 839-849, PubMed 11734001 , DOI 10.1006/jmbi.2001.5200 ,
Related entities 1. CPI-17 (35-120) deletion mutant, : 1 : 2 : 2 : 34 entities Detail
Interaction partners 1. CPI-17 (35-120) deletion mutant, : 1 interactors Detail
nullKeywords CPI-17