eh, it still took ~56 real-world attempts to get two functional designs. That's not even quantifying how strongly they fluoresce, and other qualitative/quantitative aspects (eg, how good of a GFP were these proteins). It's very impressive, and the Baker lab has done amazing stuff, but we are a long ways off from rational design.

From the paper: "Synthetic genes encoding the 56 designs were obtained and the proteins were expressed in E. coli. Thirty-eight of the proteins were wellexpressed and soluble; SEC and far-ultraviolet CD spectroscopy showed that 20 were monomeric β-sheet proteins (Supplementary Table 3). Four of the oligomer-forming designs became monomeric upon incorporation of a disulfide bond between the N-terminal 3–10 helix and the barrel β-strands. The crystal structure of one of the monomeric designs (b10) was solved to 2.1 Å, and was found to be very close to the design model (0.57 Å backbone r.m.s.d., Fig. 3c)."

"Two of the 20 monomeric designs—b11 and b32—were found to activate DFHBI fluorescence by 12- and 8-fold with binding dissociation constants (KD) values of 12.8 and 49.8 μM, respectively (Extended Data Fig. 6f)"