DynaPIN: A Tool for Characterizing Dynamic Protein Interfaces

Abstract

Static structural models often fail to capture the dynamic mechanisms of protein interactions. To address this, we introduce DynaPIN, an open-source pipeline for extracting dynamic interface fingerprints from molecular simulations. DynaPIN unifies quality control metrics, interface prediction accuracy assessment, and atomistic interaction analysis into a single automated workflow, accessible at https://github.com/CSB-KaracaLab/DynaPIN. A key feature is our interface-specific analysis centered on a Dynamic Interface definition, which classifies residues based on the persistence of their interaction status over the simulation. We applied DynaPIN to representative rigid, medium, and difficult targets from the DynaBench dataset, an MD simulation resource for Docking Benchmark 5.5. Our results show that interface flexibility diverges from static accuracy classifications established in Docking Benchmark 5.5, as explored before. All in all, by providing standardized, frame-resolved outputs, DynaPINs aim is to facilitate mechanistic studies and generate standardized unbiased data for future dynamics-aware artificial intelligence models.