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. 2005 Oct 7;90(1):164–172. doi: 10.1529/biophysj.105.063503

FIGURE 3.

FIGURE 3

Manual docking of FKBP12.6 atomic structure (68) into the 3D density difference map. To the left, a reconstruction of the RyR2 (−FKBP) complex is shown with the difference density map (blue), attributed to FKBP12.6, superimposed (blue; also see Fig. 1). To the right is an enlargement of one of the four FKBP12.6 difference masses with a ribbon representation of the FKBP12.6 atomic structure (68) docked inside it. To obtain an optimal fitting, the difference map density is displayed at a slightly lower threshold as that shown in Fig. 1 B, keeping the maximum limit of the difference density close to the known molecular mass of FKBP12.6. Side chains of residues of interest (Ala-63, Phe-59, Ile-90, Gln-31, and Asn-32) are shown in dark blue (see text).