Fig. 5. Molecular surface of CpOsm. Mapping of the electrostatic potentials on the molecular surfaces of the front (A) and back (B) sides of CpOsm. The negative potentials (colored red) and the positive potentials (colored blue) are displayed at —10 kT/e level and +10 kT/e level, respectively. Neutral surfaces are white. Mapping of the surface hydrophobicity on the front (C) and back (D) faces of CpOsm. The protein surface is colored according to the Eisenberg hydrophobicity scale (Eisenberg et al., 1984), from red (hydrophobic) to white (hydrophilic). (E) CpOsm structure shown as a cartoon (colored in orange) depicting the location and shape of the main surface cleft, which is represented as a green colored triangulated mesh. The cleft was calculated using the SURFNET program (Laskowski, 1995), available at the PDBsum web server (http://www. ebi.ac.uk/pdbsum/). (F) Molecular surface of the front side of CpOsm. The acidic (red), basic (blue) and aromatic (yellow) residues located inside and around the central cleft are colored and labeled. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)