CASP 15 Target ID Description Alternate conformations Ensemble class Experimental clarity Performance
T1109, T1110 (section 2.1)
Wild type and interface mutant for isocyanide hydratase
20-residue long domain swap induced by a single-point mutation
Environment difference: mutation
High: 1.0 & 0.7 Å resolution, X-ray
Conformational change reproduced by groups from 7 labs
T1158, v0-4 (section 2.2)
Multidrug- resistant ABC transporter
Apo and complexed with each of four ligands, 3 distinct conformations
Environment difference: ligands
Medium: 2.7 -3.5 Å, cryo-EM
Individual conformations reproduced by a few groups
T1160, T1161 (section 2.3)
Two 48-residue ‘ancient’ sequences, differing by five mutations
Crystallization condition and mutation-induced conformational differences
Environment difference: mutations, crystal conditions
High: 1.3 Å, X-ray
Individual conformations reproduced by one and three groups, respectively
T1195-T1197 (section 2.4)
Three kinases
1 or 2 low occupancy alternative conformations each
Low population conformations
Low: NMR CEST data, implied coordinates
Appropriate functional motifs sampled
R1156 (section 2.5)
135-base RNA
4 independent electron density maps, 10 map-derived models each
Experimental uncertainty: ensemble
Medium: 5.8 Å best resolution, cryo-EM
One model more accurate than experimental uncertainty
R1138 (section 2.6)
720-base designed RNA
Mature and folding intermediate
Folding intermediate
Medium: 4.8 & 5.2 Å, cryo-EM
Intermediate not reproduced
T1189/R1189T1190/R1190 (section 2.7)
Protein/RNA complex
RNA with three (1189) or two (1190) protein dimers bound.
Two alternative oligomeric states
Medium: 3.8 & 4.6 Å, cryo-EM, two particle sets
Neither complex reproduced
T1170, H1171 (v1,2), H1172 (v1-4) (section 2.7)
Holliday junction complex in different states
Components include DNA, and/or organic ligands. Interdomain differences
Time dependent differences: protein binding partners, ATP/ADP
Medium: 3 Å best resolution, cryo-EM
Not reproduced