Figure
1: Superposition of a large protein target, T1154, a 1040 residue
archaeal S-layer protein (green) and the closest calculated structure
(blue). Misalignment of the lower right-hand domain likely reflects
interdomain flexibility. For the assessment, the structure was divided
into two evaluation units: the lower right-hand domain, and the rest of
the structure. Corresponding highest GDT_TS values are 88 and 90%.
There are no detectable templates for either unit.
Figure 2 shows performance in terms of the agreement between the best
CASP models and the corresponding experimental structures. The Cα RMSD
is below 3Å for over 90% of CASP15 targets, and less than 1Å for 40%
of the targets. These are impressive results, even though only modest
increases over the CASP14 (2020) performance.