Molecular dynamics descriptors for 1,079 post-translationally modified protein systems
Kaining LiuiD, Qiuting Qian, Jiahua Peng, Dongge Ma, Yifei Yao, Jingjing Zhao, Ying ChiiD
Abstract
Databases of post-translational modifications (PTMs) catalogue modified sites and increasingly add static structural context, but trajectory-derived descriptors remain scattered across specialised tools and general molecular dynamics archives. Dyna-MO PTM brings together 1,079 AlphaFold 3-seeded systems covering lysine acetylation, lysine and arginine monomethylation, and serine, threonine and tyrosine phosphorylation. Each system is linked to three completed 10 ns replicas generated with CHARMM36m and TIP3P, for 32.37 s of aggregate sampling. A 118-column table joins simulation and quality-control provenance with global relaxation measures, site solvent exposure, rotamers, secondary structure and ionic-contact proxies. Versioned identifiers connect the records to starting structures, trajectories, manifests and analysis scripts. Researchers can use the resource to filter PTM contexts, reproduce descriptors, prioritise longer simulations and evaluate trajectory-analysis or generative methods. The trajectories describe finite-window relaxation rather than equilibrium free energies, kinetics or matched PTM effects.
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