Structural characterization of the serine protease function on Natterin-like 2 from Thalassophryne maculosa venom

Data obtained from fragments analyzed by mass spectrometry are presented here. These fragments correspond to proteins previously separated using electrophoretic techniques. For this purpose, conventional one and two dimensional SDS-PAGE gels were employed. Following the electrophoretic runs, protein bands and/or spots of interest were manually excised from the gels and subjected to enzymatic digestion protocols. The resulting peptides were then analyzed by mass spectrometry. The results for each spectrum of interest are presented and identified as follows: SDS-97 corresponds to a 97-kDa band extracted from a conventional SDS-PAGE gel, whereas 2D_38bandNatt2-4, 2D_32bandNatt_1, and 2D_31spotNat_3 correspond to bands and a spot excised from a two-dimensional gel with approximate molecular weights of 38, 32, and 31 kDa, respectively. Details of the bands can be see in Vásquez-Suárez et al., 2026.