Table 3 of
Sergeev, Mol Vis 4:9, 1998.Table 3 of
Sergeev, Mol Vis 4:9, 1998.
Table 3. PHD and NNSSP secondary structure predictions for the N-terminal extension of ßA3-crystallin from mouse lens
PHD NNSSP
--------------------------------- -------------------------
Residue Predicted probability Preferred Preferred
Helix Sheet Coil state Helix Sheet State
------- ----- ----- ---- --------- ----- ----- ---------
E-29 0 0 9 L 2 2
T-28 0 0 9 L 3 2
Q-27 1 0 7 L 3 1
T-26 3 0 5 - 3 1
V-25 7 0 2 H 6 2 H
Q-24 8 0 1 H 6 2 H
R-23 8 0 1 H 6 2 H
E-22 8 0 1 H 5 2 H
L-21 8 0 1 H 4 2 H
E-20 6 0 2 H 3 2
T-19 2 0 6 - 3 1
L-18 0 0 8 L 1 1
P-17 0 0 8 L 0 1
T-16 0 2 6 - 0 1
T-15 1 3 5 - 1 2
K-14 1 4 4 - 1 2
M-13 1 3 4 - 1 2
A-12 0 4 4 - 1 1
Q-11 0 3 5 - 0 1
T-10 0 1 8 L 1 1
N-9 0 0 9 L 0 0
P-8 0 0 9 L 0 0
M-7 0 0 9 L 0 0
P-6 0 0 9 L 0 0
G-5 0 0 9 L 0 1
S-4 0 0 9 L 0 1
L-3 0 0 9 L 0 1
G-2 - - - - 0 1
P-1 - - - - 0 0
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From left to right: Residue: residue and its relative position in the terminal extension (negative numbers) with residue 1 corresponding to the first residue of the proposed structural domain, located after multiple sequence alignment [6]. Predicted probability: a probability of a particular state (helix, sheet, or loop) as predicted by the PHD program. Preferred state: selected by the PHD program. NNSSP: helices, sheets, and preferred state as estimated by the NNSSP program. "H" and "L" are helical and coil residue conformations, respectively.