Protein side chains do not move freely; instead, they adopt specific stable conformations known as rotamers . Rotamer libraries provide a compact representation of these conformational preferences by reporting the frequency and the favored χ-angle positions of each side chain. Such libraries are usually built from large datasets of crystal structures, refined through quality filters and statistical methods to correct for underrepresented regions.

In this work, we developed a backbone-independent rotamer library using 298K molecular dynamics simulations of 188 proteins from the Dynameomics database. Compared to experimental structures, molecular dynamics offers two key advantages: complete and unambiguous structural information, free from uncertainties caused by weak electron density especially for large surface residues, and sampling in solution, which avoids crystallographic artifacts.

For each amino acid, we provide our rotamer library, rotamer definitions, and dihedral angle parameters, alongside comparisons with Dynameomics simulations, GGXGG peptide models, Astral 40, and the Dunbrack Rotamer Library. A detailed description of our Dynamic Rotamer Library is available in Scouras and Daggett .