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. 2012 Feb 2;7(2):e30361. doi: 10.1371/journal.pone.0030361

Table 3. Prediction performance comparison of TANGLE with ANGLOR and the random amino acid-specific predictor.

Phi angle (°) Psi angle (°)
MAETANGLE MAEANGLOR MAErandom MAETANGLE MAEANGLOR MAErandom
AAa ALA 21.9 22.5 27.4 38.2 42.7 79.7
CYS 25.5 27.7 32.5 45.0 48.7 85.3
ASP 29.7 30.8 32.2 48.7 48.9 73.5
GLU 22.3 23.3 27.4 39.1 43.1 75.2
PHE 23.6 24.2 32.0 39.4 40.8 85.8
GLY 84.1 75.1 95.1 76.7 66.9 79.2
HIS 29.6 31.8 35.7 46.4 48.2 76.4
ILE 17.5 18.1 26.4 32.1 35.3 84.4
LYS 24.8 25.6 30.6 41.8 45.6 79.0
LEU 17.8 18.3 24.4 35.2 38.1 81.4
MET 22.0 22.4 29.5 36.5 40.9 81.6
ASN 37.1 37.6 42.3 45.2 45.9 68.2
PRO 13.6 15.2 19.5 59.3 61.3 86.3
GLN 23.9 25.1 30.0 39.4 43.0 76.9
ARG 23.5 25.0 30.4 40.9 44.1 80.5
SER 30.6 32.3 35.3 53.5 55.4 87.0
THR 23.9 26.0 29.9 50.4 51.1 88.6
VAL 19.1 20.1 28.5 34.8 37.6 83.1
TRP 22.8 23.1 29.8 41.6 43.5 86.4
TYR 23.7 25.3 32.4 40.1 42.3 85.5
All 27.8 28.2 33.8 44.6 46.4 80.9
SSb H 9.9 11.0 19.0 18.7 28.2 29.3
E 26.1 27.9 28.1 38.9 39.9 36.1
C 40.8 41.8 51.5 66.0 63.9 81.3
SAc E 30.7 31.2 55.7 47.0 49.9 84.6
B 24.1 24.1 52.0 40.2 41.5 84.0

Prediction performance is categorized according to twenty amino acid types, three secondary structure types (H, helix; E, beta-strand; and C, coil) and two-state solvent accessibility (E, exposed and B, buried), evaluated by the mean absolute error (MAE). The results were obtained using an independent test set of 1,026 proteins from the set of PDB data compiled by Wu and Zhang [11], where the rest 500 proteins were used for training.

a

Twenty amino acid types.

b

Three secondary structure types. H: alpha-helix; E: beta-strand; C: coil.

c

Two-class solvent accessibility: E: exposed; B: buried.