Any changes made on the 3D structure can be downloaded by clicking on the "Save as Pymol File" link (on the “Protein Structure” panel), which will generate this exact state of the structure as a Pymol session. This will be useful for the users who want to investigate the structure with their preferred local structure visualization software.

The atomic level interaction information can be saved in a text file which has all the details such as which residue is contacting which residue and within these residues, which atoms are contacting which other atoms, the distance between the atoms, whether they are on main or side chains. The text files are accessible via the “List of contacts on atomic level (.zip)” link in the top right corner of the panel titled “Density of Residue Contacts” on the main interactions analysis page or on the "PFAM mappings" page.

The residue interactions can be downloaded in sif format (a network format) to be used later in Cytoscape to view the interactions which is accessible on “Density of Residue Contacts” panel.

Images of all plots (chord, asteroid, scatter) as well as the 3D structure can also be created and downloaded by taking a snapshot.

A full report of the whole analysis of the selected chain of the structure can be downloaded as an HTML file (accessible from the Structure Report link at the top of the interaction analysis page). The report contains a chord plot with the interaction between secondary structures, an asteroid plot of the current selected residue/ligand, the 3D screenshot of the structure and the scatter plot matrix shown by the Network Statistics page. The outlier residues are listed as six different tables. The first row of tables shows the top ten residues with the highest and bottom ten residues with the lowest solvent accessible areas; the second row of tables shows the top ten residues with the highest and bottom ten residues with the lowest degree values; the third row of tables shows the top ten residues with the highest and bottom ten residues with the lowest betweenness centrality measures; and finally, the last row shows the top ten residues with the highest and bottom ten residues with the lowest closeness centrality measures. Finally, if the structure has any ligands, the list of ligands are all shown in the report. The two tables shown are the top and bottom ten ligands sorted by the number of atomic contacts they have with other residues/ligands. The report is generated by clicking on the “Structure Report” button on the top of the analysis page. It takes around 30-40 seconds to generate the report. It will be generating the screenshots of the figures on the go as they were before clicking the button so that the users can personalize their reports by choosing which residues they want to display in the figures or the 3D structure. The report can be useful as a summary of the features of the structure and can be used in publications of the users.