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. Author manuscript; available in PMC: 2010 Mar 1.
Published in final edited form as: Proteins. 2009 Mar;74(4):847–856. doi: 10.1002/prot.22193

Table 2.

MAE for ϕ, ψ, and RSA for residue types and secondary-structure elements based on ten-fold cross validation with Experiment IV

ϕ(°) ψ(°) RSA SA
AA type Noa Yesb Noa Yesb Noa Yesb Maxc
R 20.9 20.7 35.1 34.3 0.141 0.139 271
K 20.9 20.4 36.2 35.4 0.125 0.122 257
D 25.2 24.7 40.5 39.8 0.148 0.145 183
E 18.6 18.3 33.8 33.0 0.108 0.105 286
N 33.1 32.1 40.4 39.8 0.150 0.147 188
Q 20.0 19.7 34.1 33.4 0.145 0.141 215
H 26.7 26.4 39.9 39.3 0.126 0.124 238
Y 21.8 21.4 34.9 34.3 0.119 0.118 250
W 20.7 20.6 35.6 35.3 0.113 0.112 260
S 24.7 24.3 44.8 43.9 0.114 0.111 181
T 20.0 19.7 42.2 41.1 0.114 0.111 192
G 61.6 61.0 58.2 56.4 0.110 0.108 136
P 11.0 9.7 49.6 46.8 0.148 0.145 170
A 18.5 18.2 33.2 32.4 0.090 0.087 169
M 19.6 19.5 32.2 31.7 0.102 0.101 236
C 23.5 23.1 37.5 36.9 0.083 0.085 139
F 21.3 20.9 34.5 34.1 0.105 0.104 221
L 15.7 15.4 30.2 29.6 0.088 0.088 221
V 16.5 16.3 29.5 28.9 0.095 0.096 171
I 15.3 15.1 27.7 27.1 0.085 0.083 210
Helix 10.5 10.2 20.4 20.2 0.108 0.105
Strand 25.7 25.3 32.5 31.6 0.089 0.087
Coil 34.0 33.5 57.6 56.1 0.139 0.137
a

No guided weights.

b

Guided weights are used.

c

Maximum solvent accessible surface area from database (Å2).