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1H-NMR Study of the Intramolecular Interaction of a Substrate Analogue Covalently Attached to Aspartic Acid-101 in Lysozyme
Authors
Ueda, T., Isakari, Y., Aoki, H., Yasukochi, T., Masutomo, S., Kawano, K., Terada, Y., Yamada, H., Imoto, T.
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: 20.2 %, Completeness: 5.6 %, Completeness (bb): 5.2 % Detail

Polymer type: polypeptide(L)

Total1H
All 5.6 % (42 of 749) 5.6 % (42 of 749)
Backbone 5.2 % (14 of 268) 5.2 % (14 of 268)
Sidechain 6.0 % (29 of 481) 6.0 % (29 of 481)
Aromatic18.5 % (12 of 65)18.5 % (12 of 65)
Methyl16.4 % (10 of 61)16.4 % (10 of 61)

1. lysozyme

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

Sample

Temperature 329 K, pH 4.8



Release date
1995-07-30
Citation
1H-NMR study of the intramolecular interaction of a substrate analogue covalently attached to aspartic acid-101 in lysozyme
Ueda, T., Isakari, Y., Aoki, H., Yasukochi, T., Masutomo, S., Kawano, K., Terada, Y., Yamada, H., Imoto, T.
J. Biochem. (1991), 109, 690-698, PubMed 1917892 ,
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