Structure and Asn-Pro-Phe Binding Pocket of the Eps15 Homology Domain

epidermal growth factor receptor pathway substrate clone 15

eps15 plays a critical role in endocytosis

The notation in the NMR chemical shift
table corresponds to that of eps15,
residues 121-215

A considerable degree of variability exists in the way that 1H, 13C and 15N
chemical shifts are reported and referenced for biomolecules. In this article
we explore some of the reasons for this situation and propose guidelines for
future chemical shift referencing and for conversion from many common 1H, 13C
and 15N chemical shift standards, now used in biomolecular NMR, to those
proposed here.

Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J.,
Oldfield, E., Markley, J. L., and Sykes, B. D.
J. Biomol. NMR 6, 135-140 (1995).

1H, 13C and 15N chemical shift referencing in biomolecular NMR.

Structure Of The Second Eps15 Homology Domain Of Human Eps15, Nmr, 20 Structures

Structure Of The Second Eps15 Homology Domain Of Human Eps15 In Complex With Ptgssstnpfr

Structure Of The Second Eps15 Homology Domain Of Human Eps15 In Complex With Ptgssstnpfl

Structure Of The Eps15-eh2 Stonin2 Complex

Epidermal growth factor receptor substrate 15 [Myotis davidii]

PREDICTED: epidermal growth factor receptor substrate 15-like [Gorilla gorilla gorilla]

homonuclear EH2 and U-98% 15N-labelled
EH2 samples were measured under similar
conditions.
DTT is essential for prevention of
Cys oxidation

generating peak-picked list, which was the basis of the chemical shift tables