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

Prediction of FliN C-terminal homodimer

Prediction of FliN C-terminal homodimer through simulations with structure-based models driven by coevolution signals. The final model presented a RMSD of 0.81Å when compared to experimental X-ray structure (1O6A). This prediction was used as a validation step to support subsequent models

Recurring Chemical Cross-Links in FliN/FliM C-terminal homodimerization

Chemical Cross-Links in FliN/FliM C-terminal dimerization that are present in both rotational states of flagellar motor. This dataset from literature was used to support predicted model for FliN/FliM C-terminal heterodimer

MSA of FliM middle domain family

multiple sequence alignment used to compute coevolution signals in the middle domain of FliM protein from T. maritm

predicted FliM homodimer model I

Predicted homodimerization interface of FliM middle domain in a parallel configuration that is compatible to the interaction mode of one rotational state suggested by cryo-EM data fitting and chemical cross-linking experiments

predicted FliM homodimer model II

Predicted homodimerization interface of FliM middle domain in a twisted configuration that is supported by chemical cross-linking experiments and can be related to an alternative conformational state of flagellum rotation

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 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

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