Estimate of the secondary structure in MALT1_Casp-Ig3(338–719).

<p>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.</p

Peak appearance progress during the course of the TA procedure for the MALT1 sample.

<p>The horizontal axis shows the total measurement time excluding the HNCO experiment, which was recorded prior to the TA. The spectral processing and analysis was done automatically during the course of the data acquisition.</p

¹H-¹⁵N TROSY spectrum of MALT1_Casp-Ig3(338–719) with the assigned amino acid residue number annotated.

<p>¹H-¹⁵N TROSY spectrum of MALT1_Casp-Ig3(338–719) with the assigned amino acid residue number annotated.</p

Estimated secondary structure from NMR experiments (in black) compared to secondary structure from the in-house X-ray structure (in dark grey) and from the published X-ray structure of <i>apo</i> MALT1_Casp-Ig3, PDB ID: 3V55 (in light grey).

<p>Alpha helices are indicated with a greater symbol size than the beta-sheets. β3, β3A and β3B are denoted β3 AB in the Fig. The star (*) indicates that the secondary structure is part of the Ig3 domain.</p