Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modelling

This dataset contains essential molecular dynamics (MD) and steered molecular dynamics (SMD) simulation data for the kinesin-5/Cut7 protein, focusing on the role of C-terminal tail phosphorylation in motor regulation. The dataset includes: MD simulation data for the unphosphorylated kinesin-5 homotetramer system MD simulation data for unphosphorylated (UP) and phosphorylated (P) kinesin-5/Cut7 tail systems across three independent replicas MD simulation data for unphosphorylated (UP) and phosphorylated (P) kinesin-5/Cut7 tail–motor complexes across three independent replicas Steered MD (SMD) datasets, including force–time (pullf.xvg) and extension–time (pullx.xvg) data for all replicates from both all-atom and coarse-grained simulations To facilitate public data sharing, trajectories were processed to reduce file size while preserving the conformational dynamics relevant to the analyses presented in the associated manuscript. Specifically, processed trajectories (XTC format) were aligned to the motor domain, stripped of solvent and ions, and downsampled at 200 ps intervals. Corresponding topology/input files (TPR) and representative structure files (GRO) are included. Representative SMD trajectories and simulation parameter files (MDP) are also provided to ensure reproducibility of the simulations and analyses. Additional raw trajectories, intermediate files, and extended datasets are available from the corresponding author upon reasonable request.