ntary Movie S2 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

Prediction of FliN_C-FliM_C heterodimerization using coevolutionary signals. This predicted complex is in agreement with reported cross-linking experiments

Supplementary Figure S7 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

(A) Predicted parallel conformation of FliM_M homodimerization in a side-to-side orientation (model I). (B) Predicted twisted conformation of FliM_M homodimerization in a perpendicular orientation (model II). Representative DCA contacts used to drive FliM_M association are represented in red

Supplementary Table S1 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

Comparison of predicted FliM_M complexes with reported cross-link signals

Supplementary Figure S5 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

Depiction of representative DCA contacts (in green) as Gaussian interaction potentials driving the association of FliN_C and FliM_C (depicted in red and blue, respectively) in MD simulation. These predicted physical interactions are fulfilled in final model

Supplementary Movie S3 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

Last step of MD simulation for the prediction of FliM_M homodimerization using coevolutionary signals. At this final stage, an oscillation between a parallel (mode I) and a twisted configuration (model II)

Supplementary Figure S2 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

Prediction of FliN_C homodimerization using random distributed interaction pairs in an equivalent number to DCA driven simulations. Simulation performed as a negative control for complex formation using DCA as interaction pairs

Supplementary Table S2 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

Parameters for complex predictions using SBM molecular simulations

Supplementary Figure S3 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

DCA contacts obtained for FliN_C considering the non-filtered FliMN_C Pfam domain (PF01052). DCA couplings related to FliN folding are highlighted with blue circles

Supplementary Movie S1 from Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

Prediction of FliN_C homodimerization using coevolutionary signals. MD simulation was able to recover the X-ray complex model reported (PDB ID: 1O6A) with a lowest RMSD of 0.81 Å