BMRB: 1650

Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme

Authors

Evans, P.A., Topping, K.D., Woolfson, D.N., Dobson, C.M.

Assembly

lysozyme

Entity

1. lysozyme (polymer), 129 monomers, 14297.99 Da Detail

KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNT QATNRNTDGS TDYGILQINS RWWCNDGRTP GSRNLCNIPC SALLSSDITA SVNCALKIVS DGNGMNAWVA WRNRCKGTDV QAWIRGCRL

Formula weight

14297.99 Da

Source organism

Gallus gallus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 35.7 %, Completeness: 10.5 %, Completeness (bb): 13.4 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	10.5 % (79 of 749)	10.5 % (79 of 749)
Backbone	13.4 % (36 of 268)	13.4 % (36 of 268)
Sidechain	8.9 % (43 of 481)	8.9 % (43 of 481)
Aromatic	29.2 % (19 of 65)	29.2 % (19 of 65)
Methyl	27.9 % (17 of 61)	27.9 % (17 of 61)

1. lysozyme

KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNT QATNRNTDGS TDYGILQINS RWWCNDGRTP GSRNLCNIPC SALLSSDITA SVNCALKIVS DGNGMNAWVA WRNRCKGTDV QAWIRGCRL

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Sample

Temperature 348 K, pH 3.8

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Release date

1995-07-30

Citation

Hydrophobic clustering in nonnative states of a protein: interpretation of chemical shifts in NMR spectra of denatured states of lysozyme
Evans, P.A., Topping, K.D., Woolfson, D.N., Dobson, C.M.
Proteins (1991), 9, 248-266, PubMed 1650946 , DOI 10.1002/prot.340090404 , Abstract

Related entities 1. lysozyme, : 1 : 105 : 142 entities Detail

Interaction partners 1. lysozyme, : 7 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail