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The previous sections have shown that the three-dimensional coordinates of a protein structure can be represented in two dimensions with minimal loss of intramolecular relationships. In particular the relationships between residues making multiple and important interactions, such as those in -sheets, are most preserved (see the distance matrices in Figures 5.4 and 5.6(e)). We have not defined core residues per se, nor have we devised a means to compare the cores of analogous structures (as in Swindellsswindells:cores). In the following section we utilise the Kohonen self-organising map to extract essential information from both three-dimensional structural information and one-dimensional sequence information simultaneously. This is followed by a quantitative analysis of the suitability of mapped sequence information in fold recognition.