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Studies of Individual Carbon Sites of Hen Egg White Lysozyme by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy
Authors
Allerhand, A., Norton, R.S., Childers, R.F.
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

Polymer type: polypeptide(L)

Total13C
All 0.5 % (3 of 548) 0.5 % (3 of 548)
Backbone 0.8 % (3 of 375) 0.8 % (3 of 375)
Sidechain 0.0 % (0 of 290) 0.0 % (0 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

Sample

Temperature 317 K, pH 3.1



Release date
1995-07-30
Citation
Studies of individual carbon sites of hen egg white lysozyme by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Assignment of the nonprotonated aromatic carbon resonances to specific residues in the sequence
Allerhand, A., Norton, R.S., Childers, R.F.
J. Biol. Chem. (1977), 252, 1786-1794, PubMed 14162 ,
Related entities 1. lysozyme, : 1 : 103 : 99 entities Detail
Interaction partners 1. lysozyme, : 8 interactors Detail