Although the 3D structure of CsTegu20.6 was modeled using Swiss-Model  and I-TASSER , the optimal 3D structure was not constructed because of the unavailability of appropriate templates. Therefore, we used a modified method to obtain the full-length and refined structures of the CsTegu20.6 protein (Figure 1) as follows: (1) the CsTegu20.6 protein sequence was split into D1 and D2 domains based on the disordered region predicted by DisoPred3  (Figure 1A); the C1 fragment was selected as a bridge in order to later combine the two domains; (2) the 3D structures of D1, D2 and C1 were modeled using I-TASSER  (Figure 1B); (3) the residue numbers of the D2 domain and the C1 fragment were readjusted to the original numbers in the sequence, renaming them as D2′ and C1′, respectively. Each domain and C1′ fragment was superposed using the TM-Score . Both D1 and D2′ were aligned to the C1′ fragment using the TM-Score so that D1 and D2′ were correctly oriented 5′ to 3′ with respect to each other. Then, the full-length structure was obtained by combining each superposed structure, from which the C1′ fragment was removed manually (Figure 1C); (4) The low free-energy conformations of the combined full-length structure were refined by full-atomic simulations using ModRefiner  (Figure 1D). The additional refinement process was performed in two stages. First, the loop regions aa13–20, aa74–88 and aa145–154 were refined by GalaxyLoop  using the ‘PS1tbm protocol’ scoring method. Then, both the backbone and side chain of the structure were refined using GalaxyRefine  incorporating the “both mild and aggressive relaxation” method.