<p>Note that the residue numbers in D chain, which includes 381 amino acids as C chain, were counted from No. 382 to No. 762. The mutation site G56S in both C chain and D chain is pointed to by the blue arrow.</p
<p>(A) Protein structures predicted by SWISS-MODEL were visualized by PyMOL. The wild type is repres...
<p>(A) Overall representative structure of the XfOhr-SH (cyan), E51A-XfOhr (orange) and R19A-XfOhr (...
<p>(A) CYP2B6.4, (B) CYP2B6.8, (C) CYP2B6.11, (D) CYP2B6.12, (E) CYP2B6. 15, (F) CYP2B6. 18, (G) CYP...
<p>Crystal structure of the wild-type enzyme and the mutants ribbons indicating the variation of the...
<p>Colors for α chain, β chain, peptide, MHC, and mutant side chains from the crystal structure are ...
<p>(A) Overlay of crystal structures of L46F (blue) L46A (green) and L46G (red). (B, C, D) Secondary...
(A) RMSD plot of C-α atoms for WT and V1067G show the convergence for both the structures over 50 ns...
(a). Details of the Trp loop and lid regions in the open wild-type structure (orange and red, respec...
<p>(A) The RMSF value of each residue C<sub>α</sub> atom of the wild type PG8fn (black) and mutants ...
<p>The amino acid number was designated according to the previous nomenclature described in the Huma...
<p>Mutation sites of the amino acid residues in the six sub-clones compared to the B6 consensus sequ...
<p>End view (A) and side view (B) of the voluminous model of the GFP-can. Four structure elements ar...
<p>The 5 amino acids identified by MUMBO as having constrained ΔΔG mutational profiles relative to o...
<p>B-factors were calculated from the three first modes of NMA (blue), and EDA (orange) and plotted ...
<div><p>(A) Ribbon representation of the WT STAT1 homodimer complexed with DNA. Secondary structure ...
<p>(A) Protein structures predicted by SWISS-MODEL were visualized by PyMOL. The wild type is repres...
<p>(A) Overall representative structure of the XfOhr-SH (cyan), E51A-XfOhr (orange) and R19A-XfOhr (...
<p>(A) CYP2B6.4, (B) CYP2B6.8, (C) CYP2B6.11, (D) CYP2B6.12, (E) CYP2B6. 15, (F) CYP2B6. 18, (G) CYP...
<p>Crystal structure of the wild-type enzyme and the mutants ribbons indicating the variation of the...
<p>Colors for α chain, β chain, peptide, MHC, and mutant side chains from the crystal structure are ...
<p>(A) Overlay of crystal structures of L46F (blue) L46A (green) and L46G (red). (B, C, D) Secondary...
(A) RMSD plot of C-α atoms for WT and V1067G show the convergence for both the structures over 50 ns...
(a). Details of the Trp loop and lid regions in the open wild-type structure (orange and red, respec...
<p>(A) The RMSF value of each residue C<sub>α</sub> atom of the wild type PG8fn (black) and mutants ...
<p>The amino acid number was designated according to the previous nomenclature described in the Huma...
<p>Mutation sites of the amino acid residues in the six sub-clones compared to the B6 consensus sequ...
<p>End view (A) and side view (B) of the voluminous model of the GFP-can. Four structure elements ar...
<p>The 5 amino acids identified by MUMBO as having constrained ΔΔG mutational profiles relative to o...
<p>B-factors were calculated from the three first modes of NMA (blue), and EDA (orange) and plotted ...
<div><p>(A) Ribbon representation of the WT STAT1 homodimer complexed with DNA. Secondary structure ...
<p>(A) Protein structures predicted by SWISS-MODEL were visualized by PyMOL. The wild type is repres...
<p>(A) Overall representative structure of the XfOhr-SH (cyan), E51A-XfOhr (orange) and R19A-XfOhr (...
<p>(A) CYP2B6.4, (B) CYP2B6.8, (C) CYP2B6.11, (D) CYP2B6.12, (E) CYP2B6. 15, (F) CYP2B6. 18, (G) CYP...