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Table 1 Overview of the prediction software used

From: Online biophysical predictions for SARS-CoV-2 proteins

Software Type Color Description
DynaMine Backbone dynamics Black Rigidity of the backbone, higher values mean backbone movements are more likely to be limited; values > 1.0 indicate membrane spanning regions, > 0.8 rigid conformations, < 0.69 flexible regions. Residues with 0.80–0.69 values are ‘context’ dependent and capable of being either rigid or flexible.
  Sidechain dynamics Grey Rigidity of the sidechain, higher values mean the sidechain is more likely to be conformationally restricted. These values are highly dependent on the amino acid type (i.e. a Trp will be rigid, an Asp flexible).
  Sheet, helix, coil propen-sities Blue, red, purple The propensity of the residue, based on local amino acid context, to adopt helix, sheet or coil conformations. Higher values indicate higher propensities.
EFoldMine Early folding propensity Green Likelihood that this residue will adopt a persistent conformation based on only local interactions with other amino acids. Values > 0.169 indicate residues most likely to start the protein folding process.
DisoMine Disorder Yellow Likelihood that this residue will be disordered (highly dynamic, many conformations). Values > 0.5 indicate that this is most likely a disordered residue.
Agmata Aggregation propensity Dark green Residues with higher values indicate residues likely to be involved in β-sheet aggregation. The values displayed in the plots are divided by a factor 20 from the original.
SeRenDIP Protein-protein interactions Cyan Indicates residues likely to participate in protein-protein interactions (PPIs). Values > 0.5 indicate residues that are most likely involved in PPIs.
SeRenDIP-CE Conformat-ional epitope regions Sea-green Indicates residues likely to be part of a conformational (discontinuous) epitope (CE) region. Values > 0.5 indicate residues that are most likely involved in CEs.