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. Author manuscript; available in PMC: 2015 Oct 7.
Published in final edited form as: Structure. 2014 Oct 7;22(10):1467–1477. doi: 10.1016/j.str.2014.08.014

Figure 2.

Figure 2

Residue-level conformational heterogeneity. (a) Examples of heterogeneity in C domain. Lys42 and Glu24 sidechains are solvent-exposed, and Ile34 is in the interior. The maximum distance between equivalent sidechain atoms (see text) is depicted for each residue. (b) Putty-sausage diagram of C domain where the relative diameter represents the maximum distance between equivalent atoms of alternative conformations (if present) within each residue. The color coding reflects the type of heterogeneity. (c) Comparison of residue-level conformational heterogeneity of single domains in C domain and B–B structures. B–B chain and domain designations are indicated as a suffix to the protein name. For example, “X1” indicates domain1 of chain X. See also Figures S3 and S4.