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![[Figure 7]](rr5233fig7mag.jpg)
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Figure 7
Modelling of full-length TtCWBD-GH184. (a) Superposition of the top five AlphaFold2 models coloured ice blue (1), gold (2), coral (3), grey (4) and pink (5). The GH184 domain predictions superpose closely, with r.m.s.d.s of ∼0.5 Å. The CWBDs also superpose with one another with a similar r.m.s.d. and all in a similar position with respect to the GH184 domain. The AlphaFold2 model available from the AlphaFold2 database (A0A5M3Z971) for a protein from A. terreus superposed with the same set of models is shown in black. (b) Superposition of the top five RosettaCM models. Here, the relative orientation of the two domains differs widely in the five models, reflecting the long flexible linker. In both cases the superposition is based on the residues in the GH184 domain. |
![[Figure 7]](rr5233fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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