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. 2016 Apr 5;11(4):e0152517. doi: 10.1371/journal.pone.0152517

Table 3. Protein structure prediction results from limited experimental data.

T0 TP TC TS TX
Target μ10 e μ10 e μ10 e μ10 e μ10 e
T0761 30 0.8 32 0.8 37 0.8 30 1.3 - -
T0763 26 1.3 29 1.1 42 1.0 36 0.9 - -
T0767 24 1.1 27 0.9 29 1.0 25 1.3 26 1.2
T0785 44 1.0 43 1.4 46 0.6 36 1.2 - -
T0794 22 1.1 24 1.5 21 1.5 22 1.1 - -
T0814 10 1.2 19 1.1 23 1.3 17 1.0 - -
T0818 41 2.0 42 1.9 52 2.0 43 1.9 - -
T0831 29 2.0 37 1.8 35 3.5 - - - -
T0832 31 1.1 29 0.4 46 3.0 29 2.7 - -
T0834 24 1.3 24 1.5 25 2.1 - - - -
T0848 24 1.6 35 1.2 36 1.3 - - - -
T0853 50 0.8 49 0.7 60 1.9 - - - -
30 1.3 33 1.2 38 1.7 30 1.4 26 1.2

The average GDT_TS values of the ten most accurate models (μ10) and the enrichment (e) are shown for prediction from the primary structure alone (T0), from predicted residue-residue contacts (TP), only correct residue-residue contacts (TC), NMR-NOE restraints (TS), and MS-XL restraints (TX).