Raw data for "Mapping of dynamic allostery within p38 alpha kinase via network analyses and NMR spectroscopy"

By integrating NMR spectroscopy, activity assays, and in silico analyses of the wild-type protein and selected mutants, both in the presence and absence of an active-site inhibitor, we experimentally validate the contribution of these residues to global protein motions and long-range allosteric regulation. Notably, the resulting network reveals communication pathways that couple the lipid-binding domain to an embedded cryptic pocket.

Together, these findings provide mechanistic insight into p38α allostery and highlight new avenues for the rational design of selective allosteric modulators targeting MAP kinases. Dataset Description: This dataset contains files to reproduce the data to be published for the above project. The files in folders for simulation ensembles as well as NMR raw data systems are provided in zip files.

The version 2 has the initial starting structures for MD run. Raw NMR spectra for assignment and relaxation is also provided. Simulation scripts are also provided for reproduction.