PKA targets transient states of RKIP: NMR and MD Data

Abstract

This repository provides molecular dynamics (MD) datasets and fast dynamic NMR data associated with the study “Protein Kinase A Phosphorylates a Conformationally High-Energy State of Raf Kinase Inhibitory Protein.” The stored datasets include replica-averaged restrained MD (RARMD) simulations of Raf Kinase Inhibitory Protein (RKIP) and experimental backbone relaxation data (T₁, T₂, and heteronuclear NOE) that capture the fast-timescale dynamics of the protein. RKIP, a member of the PEBP family, undergoes a conformational equilibrium between a compact fold and a more open, phosphorylation-competent state that facilitates recognition by Protein Kinase A (PKA). These datasets provide a resource for detailed analysis of high-energy conformational states, protein flexibility, and dynamic mechanisms of kinase-substrate recognition.