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Figure 2.
Figure 2. (a) Ensemble of the 20 lowest energy conformers
calculated for the HckSH3:PD1 complex. The backbone of the
HckSH3 domain is shown in blue, that of the PD1 peptide in
green. For better visualisation of the three-dimensional
character of the conformers, the HckSH3 backbone is coloured by
different gradations. For reasons of clarity, the flexible
residues (60 to 76) of the HckSH3 construct used in the present
study are not represented in the Figure. (b) Ribbon structure of
a representative conformer. For the HckSH3 domain (residues 77
to 140) the elements of secondary structure are labelled. (c)
Surface representation of the chemical shift perturbation
mapping of the HcKSH3 complex with PD1. Red coloured regions
indicate the residues with chemical shift changes Δ[total]δ
≥ 0.2 ppm according to Figure 1(d), orange colour indicates
residues whose resonances could not be identified during the
mapping experiment. Figure 2. (a) Ensemble of the 20 lowest
energy conformers calculated for the HckSH3:PD1 complex. The
backbone of the HckSH3 domain is shown in blue, that of the PD1
peptide in green. For better visualisation of the
three-dimensional character of the conformers, the HckSH3
backbone is coloured by different gradations. For reasons of
clarity, the flexible residues (60 to 76) of the HckSH3
construct used in the present study are not represented in the
Figure. (b) Ribbon structure of a representative conformer. For
the HckSH3 domain (residues 77 to 140) the elements of secondary
structure are labelled. (c) Surface representation of the
chemical shift perturbation mapping of the HcKSH3 complex with
PD1. Red coloured regions indicate the residues with chemical
shift changes Δ[total]δ ≥ 0.2 ppm according to [3]Figure
1(d), orange colour indicates residues whose resonances could
not be identified during the mapping experiment.
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