TABLE 1.
Best model evaluation |
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Round | Target. interface # | Complex name | Challenge | Method(s) used | fnat | Lrmsd (Å) |
Irmsd (Å) |
Quality |
37 | 110 | Fiber head domain of raptor adenovirus 1 | Symmetric docking based on homolog | SymDock local refinement | 0.67 | 2.35 | 1.73 | ** |
111 | Fiber head domain of lizard adenovirus 2 | Symmetric docking based on homolog | SymDock local refinement | 0.75 | 0.98 | 0.73 | *** | |
112 | Fiber head domain of goose adenovirus 4 | Symmetric docking based on homolog | SymDock local refinement | 0.38 | 5.81 | 2.90 | * | |
118.1 | Fructose bisphosphatase | Symmetric docking based on homolog | SymDock local refinement | 0.41 | 1.72 | 1.07 | ** | |
119 | Alcohol dehydrogenase | pH-dependent symmetric docking based on homolog | SymDock local refinement, pHDock | 0.61 | 9.92 | 2.99 | * | |
120 | Group 1 dockerin-cohesin complex | Local docking based on homomer | RosettaDock with ensembles | 0.25 | 4.96 | 3.80 | * | |
39 | 122 | IL-23-receptor complex | Multibody docking, global docking | RosettaDock with ensembles | 0.22 | 16.86 | 0.70 | * |
40 | 125.1 | NKR-P1-LLT1 complex | Multibody docking, symmetric global docking | ClusPro, RosettaDock with ensembles, SymDock | 0.40 | 1.97 | 0.97 | ** |
41 | 127 | 1,5-α-L-arabinopentose bound to AbnE | Oligosaccharide docking | GlycanDock | 0.11 | 6.78 | 2.99 | * |
128 | 1,5-α-L-arabinotetrose bound to AbnE | Oligosaccharide docking | GlycanDock | 0.15 | 7.79 | 2.94 | * | |
129 | 1,5-α-L-arabinotriose bound to AbnE | Oligosaccharide docking | GlycanDock | 0.48 | 2.78 | 1.84 | ** | |
130 | 1,5-α-L-arabinopentose bound to AbnBE201A | Oligosaccharide docking | GlycanDock | 0.63 | 4.22 | 1.58 | ** | |
43 | 133 | Designed colicin E2-Im2 complex | Loop modeling, docking based on homolog | KIC, RosettaDock with ensembles | 0.45 | 5.58 | 4.26 | * |
45 | 136.1 | Lysine decarboxylase | Symmetric docking based on homolog, complex size | Constrained relax, SymDock local refinement | 0.58 | 2.70 | 1.68 | ** |
Notes: The table lists the round, target number, name of the complex, the nature of the challenge, the methods used to model the complex, and the evaluation metrics for the best model that we submitted. The metrics are fnat: the fraction of native contacts recovered, Lrmsd: root-mean-square deviation of the backbone atoms from the native ligand after superimposing the receptor, Irmsd: root-mean-square deviation of the backbone atoms of the interface after superposition to the bound interface, and quality: high quality (***), medium quality (**), acceptable (*), or incorrect (−) as evaluated by the CAPRI organizers.