BMRB: 1785

Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c

Authors

Moench, S.J., Shi, T., Satterlee, J.D.

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: 9.6 %, Completeness: 4.3 %, Completeness (bb): 4.8 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	4.3 % (28 of 656)	4.3 % (28 of 656)
Backbone	4.8 % (10 of 209)	4.8 % (10 of 209)
Sidechain	4.0 % (18 of 447)	4.0 % (18 of 447)
Aromatic	10.4 % (5 of 48)	10.4 % (5 of 48)
Methyl	4.3 % (2 of 46)	4.3 % (2 of 46)

1. cytochrome c

XDVEKGKKIF VQKXAQXHTV EKGGKHKTGP NLHGLFGRKT GQAPGFTYTD ANKNKGITWK EETLMEYLEN PKKYIPGTKM IFAGIKKKTE REDLIAYLKK ATNE

Show sample condition

Sample

Temperature 298 K, pH 6.4

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Release date

1995-07-30

Citation

Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
Moench, S.J., Shi, T., Satterlee, J.D.
Eur. J. Biochem. (1991), 197, 631-641, PubMed 1851480 , DOI 10.1111/j.1432-1033.1991.tb15953.x , 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