Table 2 of
Sergeev, Mol Vis 4:9, 1998.Table 2 of
Sergeev, Mol Vis 4:9, 1998.
Table 2. Secondary structure occurrence frequencies of overlapping sequence tripeptides for the mouse ßB2-crystallin N-terminal extension
Residue Observed frequencies Preferred X-ray Number Entropy
Helix Loop state data of hits
------- -------------------- --------- ----- ------- -------
N-arm M-16 0.50 0.20 H - - 1.49
A-15 0.48 0.31 - 10 2.02
S-14 0.39 0.40 - 19 2.07
D-13 0.33 0.67(0.50) L(T) - 9 1.62
H-12 0.31 0.46 - 2 1.99
Q-11 0.50 0.17 H - 2 1.92
T-10 0.53 0.27 H - 2 1.67
Q-9 0.55 0.20 H - 11 1.94
A-8 0.36 0.54 L L 17 1.78
G-7 0.15 0.81(0.68) L(T) L 34 1.45
K-6 0.14 0.78 L L 11 1.72
P-5 0.04 0.79 L L 6 1.31
Q-4 0.14 0.82 L L 6 1.62
P-3 0.16 0.80 L L 10 1.70
L-2 0.33 0.54 L L 10 2.20
N-1 0.17 0.83 L L 9 1.28
C-arm Q174 0.20 0.60 L L 1 1.37
W175 0.00 0.50(0.50) L(T) L 0 1.00
H176 0.50 0.33 H - 1 1.46
Q177 0.44 0.44 - 5 2.11
R178 0.48 0.33 - 4 2.17
G179 0.36 0.50 L - 12 1.94
A180 0.33 0.53 L - 15 2.09
F181 0.27 0.41 - 2 1.97
H182 0.00 0.83(0.58) L(T) - 5 1.38
P183 0.21 0.67 L - 5 2.05
S184 0.27 0.68 L - 14 2.02
S185 0.35 0.64 L - - 1.61
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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]. 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.