Fig. 1: Molecular dynamics simulations of the disordered Tau-5_{R2_R3} region of the androgen receptor N-terminal transactivation domain.

A Comparison of the helical propensity observed in the 300 K replica of a 74 μs explicit solvent REST2 MD simulation of Tau-5_{R2_R3} in its apo form (red), the helical propensity obtained after maximum-entropy reweighting of the MD ensemble using NMR Cα chemical shifts as restraints (discontinuous line, dark red) and helical propensity predictions derived from experimental NMR chemical shifts (blue and black). Helical propensities were calculated with the DSSP algorithm. Simulated helical propensities are presented as mean values ± statistical error estimates from blocking. B Illustrative snapshots from an MD simulation of the Tau-5_{R2_R3}. The R2 and R3 regions of Tau-5_{R2_R3} are colored red and blue, respectively. C Comparison of experimental NMR Cα chemical shifts with shifts calculated from MD simulations using SPARTA+ before (red) and after maximum-entropy reweighting (discontinuous line, dark red). Black lines indicate the average Cα chemical shift prediction error of SPARTA+ on its training database of folded protein structures. Source data are provided as a Source Data file.