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Nuclear magnetic resonance study of the globular domain of chicken histone H5: Resonance assignment and secondary structure
Authors
Zarbock, J., Clore, G.MARIUS., Gronenborn, A.M.
Assembly
histone H5
Entity
1. histone H5 (polymer), 79 monomers, 8512.682 Da Detail

SASHPTYSEM IAAAIRAEKS RGGSSRQSIQ KYIKSHYKVG HNADLQIKLS IRRLLAAGVL KQTKGVGASG SFRLAKSDK


Formula weight
8512.682 Da
Source organism
Gallus gallus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.2 %, Completeness: 81.2 %, Completeness (bb): 95.1 % Detail

Polymer type: polypeptide(L)

Total1H
All81.2 % (384 of 473)81.2 % (384 of 473)
Backbone95.1 % (156 of 164)95.1 % (156 of 164)
Sidechain73.8 % (228 of 309)73.8 % (228 of 309)
Aromatic100.0 % (23 of 23)100.0 % (23 of 23)
Methyl73.8 % (31 of 42)73.8 % (31 of 42)

1. histone H5

SASHPTYSEM IAAAIRAEKS RGGSSRQSIQ KYIKSHYKVG HNADLQIKLS IRRLLAAGVL KQTKGVGASG SFRLAKSDK

Sample

Temperature 298 K, pH 3.7



Release date
1995-07-30
Citation
Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure
Zarbock, J., Clore, G.MARIUS., Gronenborn, A.M.
Proc. Natl. Acad. Sci. U. S. A. (1986), 83, 7628-7632, PubMed 3463990 , DOI: ,
Related entities 1. histone H5, : 1 : 1 : 2 : 201 entities Detail
Interaction partners 1. histone H5, : 53 interactors Detail
Experiments performed 1 experiments Detail
Chemical shift validation 3 contents Detail