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Fig. 4 in Structural characterization of the Pet c 1.0201 PR-10 protein isolated from roots of Petroselinum crispum (Mill.) Fuss

Fig. 4. Superpositions of optimized tertiary structures of the Pet c 1.0201 3D homology model and the Api g 1.0101 crystal structure (PDB accession 2BK0). A: blue – the template structure of Api g 1, red – the 3D model of Pet c 1.0201, both with annotated secondary structure elements: α – α-helix, β – β-sheet, L – loop, and N- and C-terminals. B: monomers of Api g 1.0101 and C: monomers of Pet c 1.0201 after 200 ns MD simulations. Red indicates the position of Glu45 responsible for IgE binding. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

ShareScore

32/100

Overall dataset sharing score

Score breakdown

These five areas show where the dataset supports — or may limit — practical reuse.

Stewardship
8
Harmonization
4
Access
12
Reuse readiness
8
Engagement
0

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