SI S1 Prediction of Noncompetitive Inhibitor Binding Mode Reveals Promising Site for Allosteric Modulation of Falcipain-2 Jorge Enrique Hernández González, † Lilian Hernández Alvarez, † Pedro Geraldo Pascutti, ‡ Vitor B. P. Leite †,§ † Departamento de Física, Instituto de Biociências, Letras e Ciências Exatas, Universidade Estadual Paulista Júlio de Mesquita Filho, Rua Cristóvão Colombo, 2265, Jardim Nazareth, São José do Rio Preto, São Paulo, CEP 15054-000, Brazil. ‡ Laboratório de Dinâmica e Modelagem Molecular, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Ave. Carlos Chagas Filho, 373, CCS-Bloco D sala 30, Cidade Universitária Ilha de Fundão, Rio de Janeiro, CEP 21941-902, Brazil. § Center for Theoretical Biological Physics, Rice University, Houston, Texas, 77005, United States. Figure S1. Allosteric inhibitors of FP-2 reported in literature. Three scaffolds of allosteric inhibitors of mature FP-2 have been described so far: i) suramin, ii) heme and iii) chalcone derivatives. Inhibitors of scaffolds i) and ii) trigger a substrate-excess inhibition of the enzyme, which requires the binding of a second substrate molecule that acts as modulator. On the other hand, the chalcone derivative (Cpd66) exerts a classical non-competitive inhibition on FP-2.