Table 1 of
Sergeev, Mol Vis 4:9, 1998.
Table 1. Secondary structure occurrence frequencies of overlapping sequence tripeptides for the mouse ßA3-crystallin N-terminal extension
Residue Observed frequencies Preferred Number Entropy Helix Coil state of hits ------- -------------------- --------- ------- ------- E-29 0.50 0.25 - 1.50 T-28 0.31 0.62 L 4 1.85 Q-27 0.22 0.65 L 9 1.90 T-26 0.25 0.54 L 10 1.95 V-25 0.48 0.24 9 1.93 Q-24 0.60 0.23 H 10 1.72 R-23 0.64 0.30 H 9 1.47 E-22 0.64 0.21 H 32 1.51 L-21 0.65 0.21 H 15 1.58 E-20 0.59 0.34 H 10 1.80 T-19 0.47 0.40 26 2.07 L-18 0.31 0.57 L 9 2.00 P-17 0.15 0.74 L 17 1.77 T-16 0.17 0.66 L 8 2.09 T-15 0.22 0.55 L 16 2.19 K-14 0.38 0.42 7 2.18 M-13 0.62 0.34 H 9 1.70 A-12 0.54 0.39 H 7 1.84 Q-11 0.42 0.42 12 2.05 T-10 0.20 0.67(0.50) L(T) 6 1.78 N-9 0.14 0.86 L 12 1.48 P-8 0.40 0.60 L 4 1.96 M-7 0.33 0.67 L 4 1.73 P-6 0.08 0.82 L 4 1.72 G-5 0.15 0.74 L 19 1.90 S-4 0.28 0.44 38 2.19 L-3 0.33 0.48 28 2.21 G-2 0.23 0.69 L 9 1.92 P-1 0.42 0.43 5 2.27 |
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]. Observed frequencies: frequencies of overlapped sequence tripeptides, calculated for the helical and coil secondary structure. Preferred states: the preferred conformation state Sj for the j-th residue with the observed frequency greater than or equal to 0.5. X-ray data: the secondary structure content, estimated from the X-ray model by the method [6], "-" correspond to residues which were not located from the electron density map [4]. Number of hits: number of tripeptide matches in the SCAN3D database [22]. Information entropy: calculated by formula [3]. "H", "L", and "T" are helical, coil, and turn residue conformations, respectively.