Elucidating the mechanism of familial amyloidosis- Finnish type: NMR studies of human gelsolin domain 2 -- Data Supplement - Supplemental Figures -- Proceedings of the National Academy of Sciences

Supplementary material for Kazmirski et al., Proc. Natl. Acad. Sci. USA, 10.1073/pnas.180310097

Fig. 6.
The distance in Phi-Psi space was calculated for each residue between the backbone dihedral angles of the equine crystal structure of domain 2 and the angles predicted by TALOS for human WT (A) and D187N (B) gelsolin domain 2. The secondary structure for the crystal structure is shown above the values. The secondary structure regions had low values, suggesting that the crystal structure was a good model of the human protein.