The CCW-biased model is shown from the (A) outside, and (B) side with FliGNM in aqua, FliGc in blue, ARMM in green, ARMC in orange, FliM in light blue, and FliN in green. The FliG glycine, G214, involved in the CCW-biased model, is shown as a yellow sphere. The CW-locked model (C) from front (D) side view, FliG in purple, ARMM in green, ARMC in orange, FliM in gray blue, and FliN in green. The glycine that was mutated for the CW-locked variant, G215 is shown as a yellow sphere. In both models the charged residues, Lys 284, Arg 301, Asp 308, and Asp 309 (Nishikino et al., 2016), that interact with the stator are shown as red spheres. The EHPQR residues, EHPQ144-147, R179 (green spheres), retain the FliGMC and FliMM interface (Park et al., 2006; Sakai et al., 2019). The FliMM are residues that have been shown to interact with neighboring FliM molecules in E. coli or Salmonella, are shown in magenta. The residues in our model are located on the sides of FliM such that they would be able to interact with a neighboring C-ring subunit. FliM is orientated such that the N-terminus of FliM (teal, asterisk) would be able to extend from FliM to interact with CheY-P. (D) The CW-locked FliMM, is depicted in cartoon with CheY-P (1F4V [Lee et al., 2001a]) placed in the extra density around the C-ring (white). This shows that FliM could interact with CheY-P if the extra density is in fact CheY-P.