Table 1 Overview of the prediction software used

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.