Science Advances

Supplementary Materials

This PDF file includes:

  • Fig. S1. Electron density evidence for a reliable residue adopting a conformation in the +110° < ϕ < +160° range.
  • Fig. S2. ϕ,ψ angles describing the local conformational context of the mountain pass residues.
  • Fig. S3. Four diverse examples showing the contexts of residues adopting a ϕ ~ 0° conformation.
  • Fig. S4. How the average bond angle variations obtained by treating the ψ ≤ 0° and ψ ≥ 0° transitions separately compare with each other and with those based on the combined data.
  • Fig. S5. AMBER minimizations of alanine dipeptides distort bond angles to alleviate the O−1 … C steric clash in ϕ ~ 0 conformations.
  • Table S1. Complete list of analyzed ϕ ~ 0 mountain pass residues.
  • Table S2. Frequency of amino acid types in the mountain pass transition region.
  • Table S3. Equations governing ϕ-dependent changes in geometry during transition through the mountain pass.
  • Table S4. Further details of data plotted in Fig. 3 including the ranges for and numbers of observations in each ϕ bin and the average distances and angles.
  • References (34, 35)
  • Legend for movie S1

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Other Supplementary Material for this manuscript includes the following:

  • Movie S1 (.mov format). An alanine dipeptide animation generated according to the “general” model of the ψ ~ +90° conformational transition described in this paper.

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