To improve the quality of the full-length CsTegu20.6 model, we then used combined 3D modeling methods and refinement as described in Section 3.2. (Figure 2). It should be noted that the disordered region was placed between Thr61 and Asp90 (Figure S3). This region can decrease the quality of the overall model, as it requires additional simulation time, and it interferes with the structural clustering process . These regions have been predicted representing tegumental protein linkers because they lack secondary structure in Schistosoma mansoni  and Fasciola hepatica . To address this issue, we split the whole sequence into two domains, domain 1 (aa1–74) and domain 2 (aa75–175), based on the disordered region rather than removing the region. The model of each domain was constructed using I-TASSER  based on iterative fragment assembly simulations. Then, the structures of the unaligned regions, as for the disordered region, were constructed by ab initio modeling based on replica-exchange Monte Carlo simulations . The structures of the two domains were finally combined into a full-length model using the C1 fragment aa50–99 as a bridge using TM-Scores . The initial model of CsTegu20.6 was obtained by refining the combined model using ModRefiner  (Figure S4). This program is designed to improve the physical realism and structural quality of protein models via two-step atomic-level energy minimization. Because ModRefiner can build the coordinates of the unfolded regions, the program has been employed as a key method of the combined approach .