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.