Hi everybody, I'm trying to perform some analysis about residue variability on some cell division proteins, looking for conserved sites which might be involved in protein-protein interactions. In order to do this, I'm using methods like evolutionary trace and the methods implemented on the Consurf server. My first round of analysis seems to indicate that such methods are very sensible to differences in input multiple sequence alignments, since they use the variation in an alignment column to identify highly conserved residues. Therefore, hoping to improve the matching of homologous residues to alignment columns, I'm looking for a tool that is able to build multiple protein sequence alignments using strutural information, which is available for some of my sequences in PDB. Do you know if there is any alignment program that multiply aligns a set of homologous sequences while respecting the best "fit" of those sequences to a 3D structure? Thanks for any help. Best, Robson