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.

In "cln025traj_dihedrals.npy" the frames are represented using the 32 dihedral angles of the peptide, given in the following order

phi1 phi2 phi3 phi4 phi5 phi6 phi7 phi8 phi9
psi1 psi2 psi3 psi4 psi5 psi6 psi7 psi8 psi9
chi1_1 chi1_2 chi1_3 chi1_5 chi1_6 chi1_8 chi1_9 chi1_10
chi2_1 chi2_2 chi2_3 chi2_5 chi2_9 chi2_10.

In "cln025traj_distances.npy" the frames are represented using the set of all the 4278 distances between heavy atoms of the molecule.

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:].

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 \& Francis}
}