Results are available for 36634 alternative models in 5837 sets. Each set includes the different domain structures determined by x-ray crystallography and grouped in a SCOP species level. The results can be queried by PDB identifier, by SCOP sid identifier, which uniquely identifies a domain structure, or by the SCOP species sunid, which uniquely identify a set of alternative structures. The complete list of sets is also available.

The results for each set are summarised on individual pages, each divided into several sections. The first section provides a description of the set according to the SCOP classification. This is followed by the number of entries and their identifiers. An alignment file is also provided describing the correspondences between alignment position, position in the reference UniProt sequence, and the PDB residue identifiers of the different entries. The sequence alignment is also given in the traditional FASTA format. The hierarchical clustering results are displayed in a dendrogram, and the dissimilarity matrix used for clustering is provided as a text file. The three different types of standard deviation plots are provided: distance standard-deviation matrix S, the total standard-deviation matrix T, and relative standard-deviation matrix R. The hinge and invariant regions are given according to the total standard deviation matrix. PDB format files are provided that include the structures optimally superimposed for each invariant region.

For a detailed description of the method see:
Domingues FS, Rahnenführer J, Lengauer T.
Conformational analysis of alternative protein structures.
Bioinformatics 2007 23:3131-3138.