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A method for simultaneous prediction of secondary structure and dihedral angles of the polypeptide backbone in proteins is presented here. Based on a ten-fold cross-validation on a non-redundant set of 2670 protein chains with <= 25% sequence identity, the threestate accuracy (Q3) is 81-82%. Every doubling of the number of non-redundant protein chains used in the training set results in 1% better prediction of secondary structure. With the dihedral angles discretized as 8 or 3 states on thedoi:10.1107/s0108767308092751 fatcat:7delip4p5bcgpfxrnlpsnu2cyy