Data describing the solution structure of the WW3* domain from human Nedd4-1

Panwalkar, Vineet; Schulte, Marianne; Lecher, Justin; Willbold, Dieter; Dingley, Andrew; Stoldt, Matthias

doi:10.1016/j.dib.2016.06.024

Journal Article

FZJ-2018-00425

Data describing the solution structure of the WW3* domain from human Nedd4-1

Panwalkar, V. (Corresponding author)FZJ* ; Schulte, M.FZJ* ; Lecher, J. ; Stoldt, M.FZJ* ; Willbold, D.FZJ* ; Dingley, A.FZJ*

2016
Elsevier Amsterdam [u.a.]

Data in Brief 8, 605 - 612 (2016) [10.1016/j.dib.2016.06.024]

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Please use a persistent id in citations: http://hdl.handle.net/2128/17603 doi:10.1016/j.dib.2016.06.024

Abstract: The third WW domain (WW3*) of human Nedd4-1 (Neuronal precursor cell expressed developmentally down-regulated gene 4-1) interacts with the poly-proline (PY) motifs of the human epithelial Na+ channel (hENaC) subunits at micromolar affinity. This data supplements the article (Panwalkar et al., 2015) [1]. We describe the NMR experiments used to solve the solution structure of the WW3* domain. We also present NOE network data for defining the rotameric state of side chains of peptide binding residues, and complement this data with χ1 dihedral angles derived from 3J couplings and molecular dynamics simulations data.

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