CLN025 folding represented via dihedrals or heavy atom distances

41580 frames from a replica-exchange molecular dynamics simulation (400 ns, 340 K replica, dt = 2 fs) of the 10-residue peptide CLN025, which folds into a beta hairpin.<br><br>In "cln025traj_dihedrals.npy" the frames are represented using the 32 dihedral angles of the peptide, given in the following order<br>phi1 phi2 phi3 phi4 phi5 phi6 phi7 phi8 phi9psi1 psi2 psi3 psi4 psi5 psi6 psi7 psi8 psi9chi1_1 chi1_2 chi1_3 chi1_5 chi1_6 chi1_8 chi1_9 chi1_10chi2_1 chi2_2 chi2_3 chi2_5 chi2_9 chi2_10.<br><br>In "cln025traj_distances.npy" the frames are represented using the set of all the 4278 distances between heavy atoms of the molecule.<br><br>The additional files ending with "_decimated_equilibrated" are smaller trajectories generated from the original ones by:- first, taking 1 element every 10 via numpy command array[::10].- then, removing the first 400 elements via array[400:].<br>If you find this dataset useful for your research, please cite the following publication@article{carli2021statistically,title={Statistically unbiased free energy estimates from biased simulations},author={Carli, Matteo and Laio, Alessandro},journal={Molecular Physics},volume={119},number={19-20},pages={e1899323},year={2021},publisher={Taylor \&amp; Francis}}<br><br>