File S1 - Unfolding Simulations of Holomyoglobin from Four Mammals: Identification of Intermediates and β-Sheet Formation from Partially Unfolded States

File S1 contains information about the relation between helix character and ellipticity (Figure S1); figures showing the sensitivity to variation in parameters (Figure S2); Secondary Structure types at 310 K for all four proteins (Figure S3); correlation of structures to experimental structures (Figure S4); Time evolution of secondary structures (Figures S5–S19); 2D RMSD matrix for alpha carbon (Figure S20); Key average properties of the simulated proteins separated into helices (Tables S1–S8); Timings of heme loss from simulations at 500 K, first and second replicate (Table S9); clustering analysis for all four proteins (Figures S21–S24).
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