File S1 - Integrating Structure to Protein-Protein Interaction Networks That Drive Metastasis to Brain and Lung in Breast Cancer

Supporting figures and tables.
Figure S1, Structural enrichment of PPI networks with protein-protein interface predictions. FN1 and LTBP1 are predicted to be interacting via 1ywkAC template. This template is the interaction between A and C chains PDB ID: 1ywk complex. Figure S2, The increase in the number of interactions, as the number of GUILD score gets smaller. Figure S3, The increase in the number of interactions, as the number of nodes gets bigger. Table S1, Host-pathogen knowledge on proteins that use pathogenic interface architectures in BMSN. Table S2, Host-pathogen knowledge on proteins that use pathogenic interface architectures in LMSN. Table S3, The evidence for the presence of the genes of LMSN in different databases. Table S4, The evidence for the presence of the genes of BMSN in different databases. Table S5, The KEGG pathways enriched (P<0.05) in BMSN with respect to ClueGO p-value. Table S6, The KEGG pathways enriched (P<0.05) in LMSN with respect to ClueGO p-value. Table S7, The frequency of interfaces in both metastasis networks. Table S8, Proteins in BMSN that have PRISM interface predictions. Table S9, Proteins in LMSN that have PRISM interface predictions. Table S10, Distribution of the residue numbers and the mutation numbers per protein. Table S11, The total residues numbers/genetic variations observed in different locations and the odds ratio, 95% confidence interval, and the P-value for a two tailed test that OR is different from 1.0. Table S12, Interface residues (Sequence IDs) of HBEGF-EGFR model. The binding site residues of HBEGF protein’s complexes available in PDB and the binding site residues of EGFR protein’s complexes available in PDB. The interface residues that are overlaping with available binding site residues are in italic, bold fonts. Table S13, Interface residues (Sequence IDs) of EREG-EGFR model. The binding site residues of EGFR protein’s complexes available in PDB. The interface residues that are overlaping with available binding site residues are in italic, bold fonts. Table S14, Interface residues (Sequence IDs) of HBEGF-ERBB4 model. The binding site residues of HBEGF protein’s complexes available in PDB and the binding site residues of ERBB4 protein’s complexes available in PDB. The interface residues that are overlaping with available binding site residues are in italic, bold fonts. Table S15, Interface residues (Sequence IDs) of EREG-ERBB4 model. the binding site residues of ERBB4 protein’s complexes available in PDB. The interface residues that are overlaping with available binding site residues are in italic, bold fonts. Table S16, The interfaces in the 1jogCD PRINT cluster. Table S17, The biological processes of the proteins utilizing the most frequent interfaces of LMSN. Table S18, The molecular functions of the proteins utilizing the most frequent interfaces of LMSN. Table S19, The biological processes of the proteins utilizing the most frequent interfaces of BMSN. Table S20, The molecular functions of the proteins utilizing the most frequent interfaces of BMSN.
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