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. Author manuscript; available in PMC: 2021 Nov 12.
Published in final edited form as: Proteins. 2019 Dec 3;88(8):973–985. doi: 10.1002/prot.25855

TABLE 1.

Summary of targets successfully modeled

Best model evaluation
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.