Successful ab initio prediction of the tertiary structure of NK‐lysin using multiple sequences and recognized supersecondary structural motifs

A simple approach to protein tertiary structure prediction is described, based on the assembly of recognized supersecondary structural fragments taken from highly resolved protein structures by using a simulated annealing algorithm. The results of blind‐testing this method on CASP2 target T0042 (pig NK‐lysin) are presented. The predicted structure had a Cα root‐mean‐square deviation of only 6.2 Å from the experimental structure (and less than 5.0 Å over the first 66 residues), and clearly had the correct fold when judged by using a number of objective measures. Despite the significant degree of success in this case, there is clearly much more development required before predictions with the accuracy of a good homology model can be made with this kind of approach. Proteins, Suppl. 1:185–191, 1997. © 1998 Wiley‐Liss, Inc.

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