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Figure 9
Electron-density maps for fragment 2. (a) Fragment 2 modelled as two alternate binding modes (yellow and orange) at the interface of chains A (cyan) and B (beige) showing the 2mFoDFc map at 0.8 r.m.s.d. in blue. The two modelled copies of the fragment are almost perfectly rotationally symmetric, and were modelled as alternate conformations of the same molecule. Similarly, Arg74 of chains A and B was built with alternate conformations. The two alternate copies of the fragment were refined to partial occupancies of 0.43 for conformation A (interacting with chain A of the protein) and 0.31 for conformation B (interacting with chain B). (b) 2mFoDFc maps at 0.8 r.m.s.d. for fragment 2 modelled at the interface of chains C (forest green) and D (purple); the methoxy group of 2 is not well resolved but its position was confirmed by reference to the polder map. (c) Polder map (green) at a contour of 3.5 r.m.s.d. indicating the presence of the fragment. The bound model of fragment 2 binding to chain D was refined to a final occupancy of 0.88. All maps were calculated to a resolution of 2.3 Å. Residues are shown in stick format and labelled; other protein chains are shown in cartoon representation.

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ISSN: 2059-7983
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