Figure 10.

Crystal structures and NSD analysis of the camphor-free and camphor-bound forms of the ferric heme of cytochrome P450_cam. The displacement along each of the low frequency normal mode unit vectors of Fe porphine is given in mass weighted coordinates (amu^1/2 Å). The color coding for the modes is pro: propellering (blue), ruf: ruffling (green), sad: saddling (red), wav(x): waving_x (light blue), wav(y): waving_y (yellow), dom: doming (purple), invdom: inverse doming (gray). The crystal structures are extracted from the protein data bank: 1PHC⁷⁹ for the camphor-free and 2CPP⁷² for the camphor-bound form. One of the major differences is that the camphor-bound form has a strong heme doming distortion, which is consistent with the appearance of the ~33 cm⁻¹ mode in the coherence spectra of camphor-bound P450_cam (Fig. 3)