BMRB: 1104

Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy

Authors

Oldfield, E., Norton, R.S., Allerhand, A.

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: 1.6 %, Completeness: 0.5 %, Completeness (bb): 0.8 % Detail

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Polymer type: polypeptide(L)

	Total	13C
All	0.5 % (3 of 548)	0.5 % (3 of 548)
Backbone	0.8 % (3 of 375)	0.8 % (3 of 375)
Sidechain	0.3 % (1 of 290)	0.3 % (1 of 290)
Aromatic	0.0 % (0 of 59)	0.0 % (0 of 59)
Methyl	0.0 % (0 of 61)	0.0 % (0 of 61)

1. lysozyme

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

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Sample

Temperature 315 K, pH 3.05

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Release date

1995-07-30

Citation

Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Strategies for assignments
Oldfield, E., Norton, R.S., Allerhand, A.
J. Biol. Chem. (1975), 250, 6381-6402, PubMed 169240 , 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