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 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. <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> The "cln025traj_distances.npy.gz" file is a compressed version of the file described above.

本数据集包含41580个轨迹帧，源于10残基肽CLN025的副本交换分子动力学（replica-exchange molecular dynamics）模拟，该模拟总时长为400 ns，对应340 K的温度副本，积分步长dt=2 fs，该肽可折叠为β发夹（beta hairpin）结构。

在文件"cln025traj_dihedrals.npy"中，每个轨迹帧通过该肽的32个二面角（dihedral angles）进行表征，其顺序依次为：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。

在文件"cln025traj_distances.npy"中，每个轨迹帧通过该分子所有重原子间的4278个原子间距进行表征。文件"cln025traj_distances.npy.gz"为上述文件的压缩版本。