Structure properties calculated for protein complexes formed by disordered proteins

Table S2.
Structural parameter abbreviations:
SSa: fraction of residues in helical conformation
SSb: fraction of residues in extended conformation
SSc: fraction of residues in coil conformation
SASA/H: Hydrophobic fraction of solvent accessible surface area (SASA)
SASA/P: Polar fraction of SASA
INT/H: Hydrophobic fraction of interface area
INT/P: Polar fraction of interface area
BUR/H: Hydrophobic fraction of buried surface area
BUR/P: Polar fraction of buried surface area
INT/TOT: Interface area / (interface area+SASA)
BUR/TOT: Buried surface area / (interface area+SASA)
interHH: Fraction of atomic level intermolecular interactions between two hydrophobic atoms
interHP: Fraction of atomic level intermolecular interactions between a hydrophobic and a polar atom
interPP: Fraction of atomic level intermolecular interactions between two polar atoms
interBB: Fraction of atomic level intermolecular interactions between two backbone atoms
interBS: Fraction of atomic level intermolecular interactions between a backbone and a sidechain atom
interSS: Fraction of atomic level intermolecular interactions between two sidechain atoms
intraHH: Fraction of atomic level intramolecular interactions between two hydrophobic atoms
intraHP: Fraction of atomic level intramolecular interactions between a hydrophobic and a polar atom
intraPP: Fraction of atomic level intramolecular interactions between two polar atoms
intraBB: Fraction of atomic level intramolecular interactions between two backbone atoms
intraBS: Fraction of atomic level intramolecular interactions between a backbone and a sidechain atom
intraSS: Fraction of atomic level intramolecular interactions between two sidechain atoms
inter/intra: number of atomic level interchain interactions / number of atomic level intrachain interactions
Etot/res: Sum of interchain and intrachain pairwise interaction energies / number of residues in chain
Eint/Etot: Sum of interchain pairwise interaction energies / sum of interchain and intrachain pairwise interaction energies (maximized at 1).
Calc. averages & correlations: Mean, Standard error and Relative standard error of normalized or proportional structural parameters in all groups and correlations between them. Grey background highlights those weakly correlation parameters that were selected for further calculations.
Calculated averages for 3 group: Mean normalized or proportional structural parameters in the 3 structural classes.
Auton. folding & ind. binding: normalized or proportional structural properties of each protein belonging to ’autonomous folding & independent binding’
Coupled folding & binding: normalized or proportional structural properties of each protein belonging to ’coupled folding & binding’
Mutual synergistic folding: normalized or proportional structural properties of each protein belonging to ’mutual synergistic folding’