Report Maker

Warning! The site is being updated and for now only contains analysis for structures up to 2009. In the meantime, we suggest the use of these alternative ET portals

About Evolutionary Trace Report Maker

Evolutionary trace is a method that uses a sequence similarity tree of a family of homologous proteins to highlight residues which are statistically likely to be under evolutionary pressure, and therefore of certain functional or structural importance for the family. This enables researchers looking for residues responsible for a detectable phenotype change to focus their search on the individual residues or regions of proteins most likely to produce such a change. Real-valued ET is particularly robust and suitable for making blind predictions about the evolutionary behavior of protein residues. ET ranks residues according to the estimated evolutionary pressure they experience. When the structure is available, ET results may be mapped onto the structure, thus clearly outlining known as well as putative functional parts of the protein surface.

Evolutionary trace report maker pools from different sources information about protein sequence, structure and elementary annotation, and to that background superimposes inference about evolutionary behavior of individual residues, using real-valued evolutionary trace method. As its only input it takes Protein Data Bank identifier or UniProt accession number, and returns a human-readable document in PDF format, supplemented by the original data needed to reproduce the results quoted in the report.

Questions and comments:

If you intend to use the Evolutionary Trace Server and viewer as part of a published work, please cite the following papers:

  • Mihalek I., I. Res and O. Lichtarge. "Evolutionary Trace Report Maker: a new type of service for comparative analysis of proteins." Bioinformatics. 2006 Jul 1;22(13):1656-7. Epub 2006 Apr 27.
  • Mihalek, I., I. Res, O. Lichtarge. (2004). "A Family of Evolution-Entropy Hybrid Methods for Ranking of Protein Residues by Importance" J. Mol. Bio. 336(5): 1265-82.
  • Lichtarge, O., H.R. Bourne and F.E. Cohen (1996). "An evolutionary trace method defines binding surfaces common to protein families." J. Mol. Biol. 257(2): 342-58.

The Evolutionary Trace report_maker is freely available for non-profit use.
For profit use of the Evolutionary Trace report_maker may be arranged by contacting
Mrs. Lisa Beveridge (, 713-798-6821) to request a license from Baylor College of Medicine.