BMRB: 216

1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange

Authors

Boswell, A.P., Eley, C.G.S., Moore, G.R., Robinson, M.N., Williams, G., Williams, R.J.P., Neupert, W.J., Hennig, B.

Assembly

cytochrome c

Entity

1. cytochrome c (polymer), 104 monomers, 12738.12 Da Detail

XDVEKGKKIF VQKXAQXHTV EKGGKHKTGP NLHGLFGRKT GQAPGFTYTD ANKNKGITWK EETLMEYLEN PKKYIPGTKM IFAGIKKKTE REDLIAYLKK ATNE

Formula weight

12738.12 Da

Source organism

Equus caballus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 7.7 %, Completeness: 4.7 %, Completeness (bb): 2.4 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	4.7 % (31 of 656)	4.7 % (31 of 656)
Backbone	2.4 % (5 of 209)	2.4 % (5 of 209)
Sidechain	5.8 % (26 of 447)	5.8 % (26 of 447)
Aromatic	14.6 % (7 of 48)	14.6 % (7 of 48)
Methyl	10.9 % (5 of 46)	10.9 % (5 of 46)

1. cytochrome c

XDVEKGKKIF VQKXAQXHTV EKGGKHKTGP NLHGLFGRKT GQAPGFTYTD ANKNKGITWK EETLMEYLEN PKKYIPGTKM IFAGIKKKTE REDLIAYLKK ATNE

Show sample condition

Sample

Temperature 298 K, pH 7

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Release date

1995-07-30

Citation

1H NMR studies of eukaryotic cytochrome c. Resonance assignments and iron-hexacyanide-mediated electron exchange
Boswell, A.P., Eley, C.G.S., Moore, G.R., Robinson, M.N., Williams, G., Williams, R.J.P., Neupert, W.J., Hennig, B.
Eur. J. Biochem. (1982), 124, 289-294, PubMed 6284503 , DOI: , Abstract

Related entities 1. cytochrome c, : 1 : 31 : 204 entities Detail

Interaction partners 1. cytochrome c, : 1 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail