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. Author manuscript; available in PMC: 2013 May 1.
Published in final edited form as: Chem Biol Drug Des. 2012 Feb 9;79(5):703–718. doi: 10.1111/j.1747-0285.2012.01324.x

Figure 3.

Figure 3

Residue intermolecular interaction energy differences between the complex W4A9:hC3 [15] and selected compstatin simulations of the present work. Compstatin and C3 results are shown in the left and right panel. Data are averaged over all respective runs. The colored code used is: blue – polar; red – nonpolar; and green – total. The uncertainties (error bars) are computed as described in methods. (A) W4A9:hC3 – R1:H difference; (B) W4A9:hC3 – W1:H difference; (C) W4A9:hC3 – S-1S0:H difference. Positive/negative values indicate, respectively, gained/lost interactions in the new complexes, relative to the W4A9:hC3 complex [15]. C3 regions interacting with compstatin analogs are enclosed in boxes in (A) and (C), colored as follows: red – sector 344–349; green – sector 388–393; blue – sector 454–462; purple – sector 488–492; and orange – sector 371–376.