ProScan Structure-Based Proline Design Tool

Run Successful

Save this page to return to results

Show Guide For Output and Color Scheme

ProScan Output Summary

  • (Top Left) All residues are displayed on a Ramachandran plot with the contour graph constructed from proline angle preferences defined by Lovell et al.
  • (Top Right) A 3d model of the input protein is displayed in cartoon format. Residues with proline ProteinMPNN probability >= 0.1 and preferable or acceptable Ramachandran angle classification are also represented with a ball and stick model
  • (Bottom) A table summary of the ProScan output. The table includes Ramachandran classification, ProteinMPNN probability predictions, and potential disruptions of certain bonding interactions including hydrogen bonding ("H-bond"), disulfide bonds ("Disulfide"), and glycans ("Glycan"). The chain and ID of the other residue participating in the interaction or the bound glycan type are listed after the interaction type

Color Scheme (Same for All Output Sections)

  • (Green) Residues classified as highest confidence candidates for mutation to proline. These residues have preferable Ramachandran backbone angles for proline and a ProteinMPNN proline probability greater than or equal to 0.2
  • (Light Green) Residues classified as medium confidence candidates for mutation to proline. These residues have preferable or acceptable Ramachandran backbone angle for proline and ProteinMPNN proline probability between 0.01 and 0.2
  • (Grey/Uncolored) Residues predicted to be unsuitable candidates for mutation to proline. These residues either have questionable Ramachandran backbone angles or ProteinMPNN proline probability < 0.01
  • (Dark Blue) Wild-type proline residues