Fig. 4: Time-resolved structures of TPQamr and TPQsq with bound ligands.
a Stick models of the active site residues and PAA/2-PEA in the refined structures at Δtm = 100 ms (for TPQamr, PAA, Tyr296b, Asp298, Asn381, His431, and His433) and 1000 ms (for TPQsq, 2-PEA, Tyr296a, Asp298, Asn381, His431, and His433) are shown along with the Fo–Fc polder omit maps (gray mesh) contoured at 6.0 σ for PAA, TPQamr/TPQsq, and conformers a/b of Tyr296. b B-factor values averaged for the nine atoms of bound 2-PEA molecules in the dimer structure (black square) and occupancies of TPQsq (green square) and Tyr296a (orange square) are plotted against the delay time with SE obtained in the structure refinement. Dotted line indicates the curve fitting of TPQsq formation to first-order kinetics. Notably, B-factor values of 2-PEA did not change significantly upon structure refinement with the PAA model (39.69 ± 3.96 Å2 in the refined structure at Δtm = 100 ms). Source data are provided as a Source Data file.
