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Figure S1. Tv-PSP1 crystal packing. Crystal packing of the hexagonal space group P63 with cell dimensions a=81.9 Å, b=81.9 Å, c=129.3 Å, and γ=120°. A) Trimer A in Grey surface is around the threefold axis symbol. B) Trimer D in blue steel color, this trimer is under Trimer A on the same threefold axis. The trimer D on the final structure is not visible in a large part of the structure, only are visible the fragments in contact with monomer A, here was built a complete Trimer from previous refinement process to illustrate the position on the crystal. C)Trimer B in green color is around the threefold axis symbol in the symmetric object of the twofold screw axis of the cell. D)Trimer C in orange color is around the sixfold axis symbol. Figure was made in VMD program [39]. ID PDB: 7KGC. Figure S2. Tv-PSP1 secondary structure and general topology. A) Tv-PSP1 secondary structure of the asymmetric unit monomers obtained with VMD program [39]. Marginal differences are observed on the L1 and L7. B) General topology of the monomer A structure. Beta strands in yellow color, 3-10 helixes in blue color, alfa helixes in magenta color, turns and coil in green color.
The first four researchers are the authors of the PDB-coded structure 7KGC: Crystal structure of a perchloric acid-soluble protein (PSP) from Trichomonas vaginalis at 1.95 A, Tv-PSP1. Adelaida Díaz-Vilchis collected diffraction data with time donated by Dr. Lilian González Segura at the 19-ID beamline of the Advanced Photon Source, Argonne National Laboratory (Argonne, IL, USA) using a Pilatus 6 M detector.
{"references": ["https://www.mdpi.com/2076-0817/12/1/79", "https://doi.org/10.1016/j.parint.2016.09.004", "https://doi.org/10.1007/s00436-018-6065-6"]}
intrinsic fluorescence, Trichomonas vaginalis, molecular docking, stem-loops, REMSA, molecular dynamics, binding free energy, Tv-PSP1
intrinsic fluorescence, Trichomonas vaginalis, molecular docking, stem-loops, REMSA, molecular dynamics, binding free energy, Tv-PSP1
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