Content This data set contains 1.5 million trp-cage protein conformations from a Molecular dynamics simulation. The conformations are described in dihedral space containing all 38 backbone dihedral angles of this protein. The data was obtained from a temperature replica exchange simulation scheme. Therefore, different conformations where sampled at different temperatures which are also given in the data set. For analysis purposes the data set also contains the C-alpha root mean square deviation (rmsd) of each conformation compared to the native folded structure and a completely alpha-helical structure. If you use this data in published work please cite: Lemke, Tobias, and Christine Peter. "EncoderMap: Dimensionality Reduction and Generation of Molecule Conformations." Journal of chemical theory and computation (2019). https://pubs.acs.org/doi/10.1021/acs.jctc.8b00975