Fig. 5 |. In the nsp13_T-swiveled structure, the entire nsp13_T promoter is rotated.

A. 10 independent simulations of ADPMg²⁺-bound nsp13_T, starting from the 1B-open cryo-EM structure, in isolation (five simulations, left-hand plot) and as part of the nsp13₂-RTC complex (five simulations, right-hand plot). Values plotted represent the heavy-atom rmsd of the 1B domain (nsp13 residues 150–228) compared to the 1B domain in the 1B-open cryo-EM structure (aligned on the RecA1 domain). The rmsd histograms on the right of each plot represent aggregate values across all five simulations. Representative structures of the two major conformations from simulations are shown (right, colored according to the histogram labels).

B. Five independent simulations of ADPMg²⁺-bound nsp13_T, starting from the nsp13_T-engaged state. Values plotted represent the heavy-atom rmsd of the 1B domain compared to the 1B domain in the 1B-open cryo-EM state (aligned on the RecA1 domain). The rmsd histograms on the far right represent aggregate values across all five simulations. Representative structures of the two major conformations from the rmsd histogram from simulations are shown (right).

C. Front view of the nsp13_T-swiveled structure, highlighting nsp13_T. The position of the nsp13_T promoter in the nsp13_T-engaged structure is illustrated by the dashed black outline. The nsp13_T protomer of the nsp13_T-swiveled structure is rotated by 38° as shown.

See also Extended Data Fig. 7.