Thermodynamic and Dynamics Data for Coarse-grained Intrinsically Disordered Proteins Generated by Active Learning

This distribution compiles thermodynamic and (where available) dynamic
properties of short protein sequences as obtained from coarse-grained
molecular dynamics simulations. The dataset features 2114 protein
sequences with sequence lengths ranging from N=20 up to N=50 amino acids.
The simulation and analysis of these sequences is described in
"Active learning of the thermodynamics--dynamics tradeoff in protein
condensates'' by Yaxin An, Michael A. Webb*, and William M.
Jacobs* (https://doi.org/10.48550/arXiv.2306.03696). Of the 2114 protein
sequences, 80 are homomeric polypeptides (replicating a single amino acid
for N = 20, 30, 40, and 50), 1266 are sourced from version 9.0 of the
DisProt database, and the remaining 768 sequences are novel sequences
generated during an active learning campaign described in the
aforementioned manuscript. The simulations were performed using the LAMMPS
molecular dynamics engine. The interactions used for simulation are
obtained from R. M. Regy , J. Thompson , Y. C. Kim and J. Mittal ,
Improved coarse-grained model for studying sequence dependent phase
separation of disordered proteins, Protein Sci., 2021, 1371 —1379.
Properties included in this distribution include second virial
coefficients, pressure-density data, expectation for phase behavior at 300
K, estimated condensed-phase densities at 300 K (if exist), and
condensed-phase self-diffusion coefficients at 300 K (if exist).