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. Author manuscript; available in PMC: 2010 Dec 1.
Published in final edited form as: Nat Struct Mol Biol. 2010 May 30;17(6):768–774. doi: 10.1038/nsmb.1807

Figure 2.

Figure 2

Solution-NMR structure of pSRII in DHPC micelles. (a) An ensemble of 30 low-energy structures derived from NMR restraints. The backbone r.m.s. deviation for residues 1–221 is 0.48 Å. Loop and strand regions are indicated in green and purple, respectively. The 20 unstructured C-terminal residues are omitted from this figure. (b) Ribbon diagram of the structure closest to the mean. (c) Superposition of the NMR structure shown in b in red and the X-ray crystal structure 1H6823 in blue. The r.m.s. deviation of the best backbone superposition of the two structures for residues 1–219 is 1.23 Å. (d) All-trans retinal binding pocket viewed side-on showing the chromophore attached via a Schiff base to Lys205. The closest to the mean NMR structure is shown in pink superimposed on the X-ray structure displayed in blue. Selected side chains of residues contacting the retinal are shown for the NMR structure in purple. The two potential counter ions to the Schiff base Asp75 and Asp201 as well as Arg72 are displayed in brown.