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![[Figure 2]](lp5062fig2mag.jpg)
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Figure 2
Per-residue Rosetta energy terms and comparison of the per-residue r.m.s.d. of the models to the crystal structure. (a, b) Energies in Rosetta energy units (REU) for each residue position of the template RBP structure (black, circles, dashed line), the model of RBP-CPN or RBP-CPC (gray, squares, solid line) and the respective crystal structures (blue for RBP-CPN and yellow for RBP-CPC, triangles, dashed lines). Sites where loop residues were introduced are highlighted by colored brackets for each protein. Secondary-structural elements as observed in the crystal are shown and are labeled as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif){kind=small} (a). (c, d) Superposition of the computational models (gray) and the corresponding crystal structures of RBP-CPN (blue) and RBP-CPC (yellow). The borders of the area of missing density in RBP-CPC are labeled D96 and M116. (e, f) Per-residue r.m.s.d. (based on Cα atoms) of the obtained crystal structures of RBP-CPN (blue) and RBP-CPC (yellow) compared with their models. The representation and alignment were obtained using PyMOL 2.5.0 (Schrödinger) and the align command with cycles=0, considering only Cα atoms of chains A and transferring per-residue values with the rmsd_b script (https://pldserver1.biochem.queensu.ca/~rlc/work/pymol/rmsd_b.py). |
![[Figure 2]](lp5062fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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