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Figure 4.
Fig. 4. NMR structure ensembles for (A) Z38 and (B) Z34C. In
each case, 24 models are shown aligned using the backbone atoms
of residues 10-36. Shown also are the coordinates for residues
7-38 from the^ crystal structure of the B-domain/Fc complex
(red) (6). The^ disordered N-terminal residues 1-5 from Z38 are
colored gray. Side chains from the hydrophobic core of Z34C are
shown (Phe-6, Cys-10, Phe-14, Ala-17, Leu-18, Leu-23, Ile-32,
Ile-35, and Cys-39). (C) The minimized mean structure of Z34C
showing all side chains colored by amino acid type: hydrophobic
(yellow), positively charged^ (blue), negatively charged (red),
and polar (green); only those^ that are labeled are well defined
in the NMR ensemble with  1^angular
order parameters >0.9. Note that only the 1 =  60°
orientation for Phe-14 is shown, but this side chain also exists
in the 1^ = 180°
conformation in solution. (D) Same as C, but rotated 90°
with the Fc binding surface on top.
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