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. Author manuscript; available in PMC: 2019 Mar 12.
Published in final edited form as: Nature. 2018 Sep 12;561(7724):485–491. doi: 10.1038/s41586-018-0509-0

Figure 6: Comparison of structures of GFP and mFAP1.

Figure 6:

a, Surface mesh and ribbon representations of structures of GFP (left, PDB ID: 1EMA) and the computationally designed mFAP1 (right) with the chromophores embedded in the protein (green spheres). GFP, a product of natural evolution, has more than twice the number of residues, and a taller (top panel) and wider (bottom panel) barrel. Resolved water molecules in the crystal structures are shown as light purple spheres. b, Close-up of chromophore binding interactions in GFP (left) and mFAP1 (right).