(A) The C atoms of all residues involved in binding in any of the five peptide bound structures are shown (red) along with the rest of the backbone (light blue ribbon)

(B) The standard deviation in the area bound on complex formation is displayed by coloring the C atoms of peptide binding residues on a gradient, from a standard deviation of 0Å (blue) to 10Å and greater (red). (C) The backbone RMSF of the 14-3-3 domain calculated over C atoms displayed as a color and radius gradient, from an RMSF of 0Å (blue, 0.25Å) to an RMSF of 2.0Å and greater (red, 2.0Å). (D) The side chain RMSF is displayed by coloring the C atoms of peptide binding residues on a gradient, from a RMSF of 0Å (blue) to an RMSF of 0.50Å and greater (red). All parameters were calculated using all five of the peptide-14-3-3 complexes.<p><b>Copyright information:</b></p><p>Taken from "Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners"</p><p>http://www.biomedcentral.com/1471-2164/9/S1/S1</p><p>BMC Genomics 2008;9(Suppl 1):S1-S1.</p><p>Published online 20 Mar 2008</p><p>PMCID:PMC2386051.</p><p>