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Figure 3
Difference electron-density maps of PK (a) and A2AAR [(b) and (c)] structures to illustrate the absence of model bias. Residue fragment Val226–Tyr236 of PK structure (a), Ile100–Leu110 of A2AAR (b) and ligand ZM241385 (c) were deleted from models and simulated-annealing OMIT maps 2mFoDFc (gray) and mFoDFc (green) were calculated. In all cases [(a) and (b)], OMIT maps 2mFoDFc are contoured at 1.5σ and mFoDFc are contoured at 2.5σ. Omitted residues are shown for clarity. The positive electron density, where original residues were, is in good agreement with the final structural model of PK and A2AAR.

Volume 6| Part 3| May 2019| Pages 412-425
ISSN: 2052-2525