febs12704-sup-0001-FigS1-S8-TableS1-S3.zipZip archive5005K

Fig. S1. Mass spectrometry from ExoT–SpcS crystal.

Fig. S2. Chaperone–chaperone and chaperone–effector interactions.

Fig. S3. Overview of in silico alanine scanning mutagenesis binding data.

Fig. S4. Root mean square deviation and superposition of time-averaged structures of SpcS wild-type and mutants obtained from molecular dynamics simulation.

Fig. S5. Root mean square fluctuations for Cα atoms of the chaperone backbone, averaged over the time course of the simulation.

Fig. S6. Sensograms from surface plasmon resonance assay of ExoT–SpcS interaction.

Fig. S7. Far UV and near UV CD spectroscopy of wild-type and double SpcS mutants.

Fig. S8. Superimposition of chaperones SycE and SpcS, in the absence and presence of YopE and ExoT effectors, respectively.

Table S1. Details of residue contact existing between two dimeric chaperones.

Table S2. Details of residue contact existing between dimeric chaperone and effector.

Table S3. Summary of in silico alanine scanning mutations with their corresponding ΔΔGbind values.

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