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We ran the sequences of 2126 E. coli and phage proteins through CF-random. In total 3237 sequences were attempted, but in 1111 cases, MSAs deep enough for coevolutionary inference could not be generated. Seashell-like image represents these 3237 proteins by length; the inner circle represents 1111 rejected candidates, and outer, the 2126 proteins that were then run through CF-random. If two or more distinct conformations were identified, such as in the case of the successfully identified fold-switching E. coli protein, RfaH, we tested for dual-fold coevolution using ACE. If coevolutionary evidence for both folds was found, the protein was considered a putative fold switcher. Light gray/black contacts on upper/lower diagonals are unique to CF-random predicted dominant/alternative conformations. Teal contacts are from coevolutionary inference. Medium gray contacts are unique to both folds.
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