Here, we present the PG-1 dimer structures in different environments. In the bulk water environment, PG-1 dimers are partially folded β-sheets, while both the antiparallel and parallel β-sheet conformations of the PG-1 dimer are well preserved at the amphipathic interface of the lipid bilayer. Our simulation results provide important guidelines for how the environment supports the β-sheets of the PG-1 dimer and how the dimer activity depends on the β-sheet arrangements. We conducted four simulations starting at different initial configurations, two for antiparallel dimers and two for parallel dimers (page 4). As expected, these simulations do not converge to the same point, since molecules should have conformational and energetic distributions in nature, especially when embedded in the complex membrane environment. Similarly, a recent PG-1 monomer simulation work observed a "kick-shaped" conformation only in one of the two simulations . In the work reported here, while the simulations do not converge to the same conformation, nevertheless the essential features converged: consistently, in both simulations of parallel dimers, the membrane disruption was larger than in the two antiparallel dimer simulations. The parallel β-sheets of the PG-1 dimer induce the membrane disruption effect at the amphipathic interface of the lipid bilayer. Comparing with the recent experimental observation that the parallel PG-1 dimer inserts into POPC lipids , our simulations unified experimental observations by revealing that the parallel PG-1 dimer is biologically more active to insert into POPC membrane.