Olivieri, CristinaVeglia, GianluigiVeliparambil Subrahmanian, ManuWang, Yingjie2024-02-192024-02-192024-02-19https://hdl.handle.net/11299/261043• Proton and amide chemical shift list files of PKA-C PKA-C mutant F100A in the apo form, ATPgN-, ADP- and ATPgN/PKI-form. The list files were obtained using standard [1H, 15N]-WADE-TROSY-HSQC pulse sequence on uniformly 15N labeled-protein. • Raw data of the steady-state coupled enzyme assays of F100A mutant using standard PKA-C peptide substrates (Kempite)This investigation examines the cooperative modulation of Protein Kinase A (PKA) activity by ATP and substrates, with a specialized focus on the enzyme's catalytic subunit (PKA-C), utilizing NMR-restrained molecular dynamics simulations complemented by advanced Markov Model analysis. Herein, we deposit chemical shift datasets for the PKA-C mutant F100A, both in its apo form and in complex with nucleotides and inhibitors, and activity assay data providing a comprehensive insight into the enzyme's allosteric regulation mechanisms.CC0 1.0 UniversalProtein kinase AReplica-averaged metadynamics (RAM) simulationsMarkov State Model (MSM) analysisProtein cooperativityallosteric mutationDatasethttps://doi.org/10.13020/8f9s-qd79