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The homologous models were calculated using the Web-based modeling programs; I-TASSER (red), IntFOLD2 (green), Phyre2 (blue), RaptorX (purple).
The homologous models of Ube2g1 were generated by various modeling programs, and then their CSs were predicted by using the SHIFTX2 program.
Therefore, we generated four different homologous models of Ube2g1 using the Web-based modeling programs, I-TASSER (Yang et al. 2015), IntFOLD2 (McGuffin et al. 2015), Phyre2 (Kelley et al. 2015), RaptorX (Kallberg et al. 2014), to take account of the effects from wrong CS references during the RASPnmr analyses.
The homologous models of Ube2g1 seem to be accurate for the E2-core domain, but those of the unstructured parts vary with the algorisms of the modeling program (Fig. 2).
The reference bCSs calculated from various homologous models of Ube2g1 enabled the automatic bCSs assignment process by the RASPnmr program, and a similar application will be possible for the bCS assignments of other proteins.
The presence of the flexible parts in these homologous models of Ube2g1 was also confirmed by the measured 15N-relaxation data (T1, T2, and 1H,15N-heteronuclear NOE values) (Fig. 3).
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Homologous modeling of the predicted mature enzyme with a ligand (inhibitor) was with Modeller [ 32].
In addition, the predicted start of the T. molitor and T. castaneum mature enzyme sequence was identified by sequence homology through alignment with mature human cathepsin L and cathepsin B. The simulation of 3D structures of cysteine cathepsin proteins was obtained by two different approaches: Homologous modeling of the predicted mature enzyme with a ligand (inhibitor) was with Modeller [ 32 ].
The structure model of BAHBAHD1 was obtained by homologous modelling.
There are many programs to predict the homologous model of protein structure, and they utilize their own specific algorism.
The known crystal structure of human IFN α2b (PDB ID: 1RH2), which is closely homologous to IFN-CSP, was used to establish the homologous model.
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