Introduction
mulPBA is a tool for comparison of protein structures based on similarity in the local backbone conformation. The local backbone conformation is defined as pentapeptide dihedrals, using Protein Blocks (PBs)[de Brevern et al. 2000, Joseph et al. 2010]. The protein structures represented as PB sequences, are aligned by dynamic programming scored by a PB substitution matrix [Joseph et al. 2011]. A progressive alignment strategy similar to CLUSTALW was adopted for multiple PB sequence alignment. Highly similar stretches identified by the pairwise alignments are given higher weights during the progressive alignment. Encoding the information on backbone conformation as PB sequences, enables 'sequence-like' structural alignment, which is minimally influenced by structural flexibility (see examples). The residue equivalences from PB based alignments are identified to obtain a three dimensional fit of the structures, followed by an iterative refinement of the structural superposition.
Compare and align multiple protein structure - PDB data
Use this form to analyse chain from Protein Data Bank files. In order to make multiple protein analysis a minimum of 3 protein are required. The files can also be uploaded see bellow.
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Data have to be formatted as below: PDBCODECHAIN. |
Compare and align multiple protein structure - files analysis
Upload PDB files and enter the respective chain IDs.
The files can be uploaded as an archive see bellow.
Personal PDB files:Note that data upload is limited to 50 Mb. |
Compare and align multiple protein structure - archive file
You can upload archive containing all your pdb files (zip, tar, tar.gz, tgz and gz).
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Note that data upload is limited to 50 Mb and the number of files have to be between 3 and 20. |
Compare and align multiple protein structure - archive
You can use your analysis number to reprint analysis.
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Note that analysis older than 7 days are deleted. To found your analysis ID : |