Fig. 5. AlphaFold2 successfully predicts two conformations of a candidate sequence without experimentally determined structures.

a A NusG N-terminal (NGN) fold (light gray) and a C-terminal β-roll fold (lavender) are predicted from a deep input MSA (region corresponding to the CTD shown). Predicted β-sheets in the C-terminal domain that agree closely with the β-sheets predicted from nuclear magnetic resonance experiments are shown with black boxes surrounding lavender bars. b A NusG N-terminal (NGN) fold (light gray) and a C-terminal α-helical hairpin fold (teal) are predicted from a modified input MSA in which columns predicted to form only β-roll contacts are changed to alanine. Predicted α-helices in the C-terminal domain that agree with the α-helices predicted from nuclear magnetic resonance experiments are shown with black boxes surrounding teal bars. Protein structures were generated with PyMOL⁸⁰. Source data are provided as a Source Data file.