BMRB: 1779

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), 103 monomers, 12420.66 Da Detail

XDVAKGKKTF VQKXAQXHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD ANKSKGIVWN ENTLMEYLEN PKKYIPGTKM IFAGIKKKGE RQDLVAYLKS ATS

Formula weight

12420.66 Da

Source organism

Equus caballus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 7.8 %, Completeness: 3.7 %, Completeness (bb): 3.8 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	3.7 % (23 of 629)	3.7 % (23 of 629)
Backbone	3.8 % (8 of 209)	3.8 % (8 of 209)
Sidechain	3.6 % (15 of 420)	3.6 % (15 of 420)
Aromatic	0.0 % (0 of 51)	0.0 % (0 of 51)
Methyl	10.9 % (5 of 46)	10.9 % (5 of 46)

1. cytochrome c

XDVAKGKKTF VQKXAQXHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD ANKSKGIVWN ENTLMEYLEN PKKYIPGTKM IFAGIKKKGE RQDLVAYLKS ATS

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Sample

Temperature 298 K, pH 4.6

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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: , Abstract

Related entities 1. cytochrome c, : 1 : 1 : 234 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail