Patch analysis distributions: rank ordering of observed interface patches relative to
High ASA other patches on the surface of the protein. For each protein, the interface patch is ranked, relative to all other surface patches, as being in the top 10%, 10-20% etc. (see Fig. 7). The observations (one for each homodimer) are combined for each parameter separately. The distributionsshown are rms deviation of atoms from the least-squares plane through the atoms (0-
10% are the most planar interfaces) (a), interface residue propensities (b), protrusion index (c),hydrophobicity [based on the scale of Janin et al.(9)] (d), and ASA (e). A mean ASA for residues 90' 100 in each patch was calculated and used in the rank ordering.