SpringerImages - Deviations from random coil 13Cα and 13Cβ chemical shifts in the protein nsp3(1066–1181) plotted versus the amino acid sequence. The ΔδCα and ΔδCβ values were determined with the program package ATNOS/CANDID (Herrmann et al. 2002a, b) by subtracting the random coil 13Cα and 13Cβ shifts from the experimentally determined chemical shifts. The Δδi value for residue i represents a three-point average value over the three consecutive residues i − 1, i and i + 1, calculated as follows: $$ \Updelta \delta _{i} \, = \,1/3\,(\Updelta \delta C^{\alpha }_{{i - 1}} \, + \,\Updelta \delta C^{\alpha }_{i} \, + \,\Updelta \delta C^{\alpha }_{{i + 1}} \, - \,\Updelta \delta C^{\beta }_{{i - 1}} \, - \,\Updelta \delta C^{\beta }_{i} \, - \,\Updelta \delta C^{\beta }_{{i + 1}}) $$ (Metzler et al. 1993). A positive value for Δδi indicates that the residue i is located in a regular helical structure, while a negative value indicates its location in a regular β-strand. The positions of regular secondary structures indicated at the bottom of the figure were obtained with the criterion that |Δδi| ≥ 1 for three or more sequentially adjacent residues

$Deviations from random coil 13Cα and 13Cβ chemical shifts in the protein nsp3(1066–1181) plotted versus the amino acid sequence. The ΔδCα and ΔδCβ values were determined with the program package ATNOS/CANDID (Herrmann et al. 2002a, b) by subtracting the random coil 13Cα and 13Cβ shifts from the experimentally determined chemical shifts. The Δδi value for residue i represents a three-point average value over the three consecutive residues i − 1, i and i + 1, calculated as follows: $$ \\Updelta \\delta _{i} \\, = \\,1/3\\,(\\Updelta \\delta C^{\\alpha }_{{i - 1}} \\, + \\,\\Updelta \\delta C^{\\alpha }_{i} \\, + \\,\\Updelta \\delta C^{\\alpha }_{{i + 1}} \\, - \\,\\Updelta \\delta C^{\\beta }_{{i - 1}} \\, - \\,\\Updelta \\delta C^{\\beta }_{i} \\, - \\,\\Updelta \\delta C^{\\beta }_{{i + 1}}) $$ (Metzler et al. 1993). A positive value for Δδi indicates that the residue i is located in a regular helical structure, while a negative value indicates its location in a regular β-strand. The positions of regular secondary structures indicated at the bottom of the figure were obtained with the criterion that |Δδi| ≥ 1 for three or more sequentially adjacent residues$

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Fig 2

Deviations from random coil ¹³C^α and ¹³C^β chemical shifts in the protein nsp3(1066–1181) plotted versus the amino acid sequence. The ΔδC^α and ΔδC^β values were determined with the program package ATNOS/CANDID (Herrmann et al. 2002a, b) by subtracting the random coil ¹³C^α and ¹³C^β shifts from the experimentally determined chemical shifts. The Δδ_i value for residue i represents a three-point average value over the three consecutive residues i − 1, i and i + 1, calculated as follows: $$ \Updelta \delta _{i} \, = \,1/3\,(\Updelta \delta C^{\alpha }_{{i - 1}} \, + \,\Updelta \delta C^{\alpha }_{i} \, + \,\Updelta \delta C^{\alpha }_{{i + 1}} \, - \,\Updelta \delta C^{\beta }_{{i - 1}} \, - \,\Updelta \delta C^{\beta }_{i} \, - \,\Updelta \delta C^{\beta }_{{i + 1}}) $$ (Metzler et al. 1993). A positive value for Δδ_i indicates that the residue i is located in a regular helical structure, while a negative value indicates its location in a regular β-strand. The positions of regular secondary structures indicated at the bottom of the figure were obtained with the criterion that |Δδ_i| ≥ 1 for three or more sequentially adjacent residues

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The numbers above the sequence represent the numbering in the full-length nsp3 protein, and below the sequence the numbering for the construct used in this study is given, which is also used in the Figs. 1 and 2 .

The Fig. 2 shows a plot of the deviations of the experimentally observed ¹³ C chemical shifts from the random coil values, Δδi, versus the amino acid sequence, where Δδi is defined as $$ 1/3\,(\Updelta \delta C^{\alpha }_{{i - 1}} \, + \,\Updelta \delta C^{\alpha }_{i} \, + \,\Updelta \delta C^{\alpha }_{{i + 1}} \, - \,\Updelta \delta C^{\beta }_{{i - 1}} \, - \,\Updelta \delta C^{\beta }_{i} \, - \,\Updelta \delta C^{\beta }_{{i + 1}}) $$ (Metzler et al.

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