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. 2016 Jan 20;11(1):e0146496. doi: 10.1371/journal.pone.0146496

Fig 3. Estimate of the secondary structure in MALT1Casp-Ig3(338–719).

Fig 3

Secondary chemical shifts (Δδ) were calculated by subtracting random coil chemical shifts corrected for nearest-neighbour effects from 13C’, 13Cα and 13Cβ chemical shifts corrected for deuterium isotope shifts. Consecutive values above 0.7 indicates alpha helix, while consecutive values below -0.7 indicates beta strand for Δδ13C’ and Δδ13Cα. The opposite is true for Δδ13Cβ. The CSI for the three nuclei were averaged and reported as a “consensus” CSI. β3, β3A and β3B are denoted β3 AB in the Fig. The star (*) indicates that the secondary structure is part of the Ig3 domain.