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@ARTICLE{Panwalkar:842151,
      author       = {Panwalkar, Vineet and Schulte, Marianne and Lecher, Justin
                      and Stoldt, Matthias and Willbold, Dieter and Dingley,
                      Andrew},
      title        = {{D}ata describing the solution structure of the {WW}3*
                      domain from human {N}edd4-1},
      journal      = {Data in Brief},
      volume       = {8},
      issn         = {2352-3409},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2018-00425},
      pages        = {605 - 612},
      year         = {2016},
      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.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27419198},
      UT           = {WOS:000453168700097},
      doi          = {10.1016/j.dib.2016.06.024},
      url          = {https://juser.fz-juelich.de/record/842151},
}