Additional file 2: of PEPstrMOD: structure prediction of peptides containing natural, non-natural and modified residues

Performance of PEPstrMOD on CyclicPep, ModPep and ModPep16 datasets. Table S5. Performance comparison of PEPstrMODpc with PEP-FOLDc and ab initio model on CyclicPep dataset in vacuum environment. Table S6. Performance comparison of PEPstrMODpc and ab initio model on CyclicPep dataset in hydrophilic environment. Table S7. Performance of PEPstrMOD, PEP-FOLD and PepLook on 28 cyclic peptides. Table S8. Performance of PEPstrMOD on ModPep dataset. Table S9. Comparison of the performance of initial structures of PEPstrMOD, ab initio and DSSP models on ModPep16 dataset. Table S10. Comparison of the performance of minimized structures of PEPstrMOD, ab initio and DSSP models on ModPep16 dataset in vacuum environment. Table S11. Comparison of the performance of structures of PEPstrMOD, ab initio and DSSP models on ModPep16 dataset in vacuum environment after 100 ps MD. Table S12. Comparison of the performance of structures of PEPstrMOD, ab initio and DSSP models on ModPep16 dataset in vacuum environment after 1 ns MD. Table S13. Comparison of the performance of minimized structures of PEPstrMOD, ab initio and DSSP models on ModPep16 dataset in hydrophilic environment. Table S14. Comparison of the performance of structures of PEPstrMOD, ab initio and DSSP models on ModPep16 dataset in hydrophilic environment after 100 ps MD. Table S15. Comparison of the performance of structures of PEPstrMOD, ab initio and DSSP models on ModPep16 dataset in hydrophilic environment after 1 ns MD. (XLSX 176 kb)