Identification of similar regions of protein structures using integrated sequence and structure analysis tools-2

<p><b>Copyright information:</b></p><p>Taken from "Identification of similar regions of protein structures using integrated sequence and structure analysis tools"</p><p>BMC Structural Biology 2006;6():4-4.</p><p>Published online 9 Mar 2006</p><p>PMCID:PMC1435900.</p><p>Copyright © 2006 Peters et al; licensee BioMed Central Ltd.</p> random member was selected. Then each representative was run against the method using the database specified in the legend, with the HMMer results excluded. The same set was run against ASTRAL 95 v1.67, if the domain was not found in v1.67, another random member of that fold was chosen, if the fold was not found in v1.67, it was excluded. The sensitivity and precision were measured as (true positives/total positives) and (true positives/total hits), respectively. EC.3 is the first three numbers of the EC number and SCOP SF is the first three numbers of the SCOP ID (superfamily)

Identification of similar regions of protein structures using integrated sequence and structure analysis tools-0

<p><b>Copyright information:</b></p><p>Taken from "Identification of similar regions of protein structures using integrated sequence and structure analysis tools"</p><p>BMC Structural Biology 2006;6():4-4.</p><p>Published online 9 Mar 2006</p><p>PMCID:PMC1435900.</p><p>Copyright © 2006 Peters et al; licensee BioMed Central Ltd.</p>windows illustrating both the query and the selected hit. For each hit, the Z-score, the PSI-BLAST e-value, the SCOP ID, the GO annotations and the EC number are displayed, if available. B) The function prediction page of 1DSU:A, showing how close each residue environment is to the annotation of the SCOP family b.47.1.2, trypsin fold serine proteases and how conserved the residues are in the PSI-BLAST PSSM