<p>H97R (A); I35K (B); S68Y (C). The left panel shows WT interaction and the right panel shows interaction after mutation. N-TIMP2 is shown in blue and MMP14 is shown in green. Mutated residues and surrounding residues are shown as sticks and hydrogen bonds and salt bridges are shown as yellow dots.</p
<div><p>(A) Ribbon representation of the WT STAT1 homodimer complexed with DNA. Secondary structure ...
<p>(a) Superposition of the YW/ELA/HLA-A2 and the DMF5/ELA/HLA-A2 complexes. DMF5 α chain is yellow,...
<p>Residues at mutated sites on homologous proteins are shown in red (wild type) and blue (mutant) s...
<p>The rigidity analysis provided information based on the structural rigidity and flexibility of re...
<p>N-TIMP2 binding interface positions with their WT identity are displayed on the left, the mutated...
<p>A. Molecular interactions of E-DENV1 protein (shown in rainbow color cartoon) are shown with the ...
<p>The structure of GCK in the closed form (PDB code:1v4s) is shown as cyan ribbons. A) p.His137Asp....
<p><b>(A) Wild-type enzyme; (B) A269K/S187D mutant; (C) S187D/N188T mutant; D) A269K/S187D/N188T mut...
<p>Carbon atom, cyan; Nitrogen atom, blue; Oxygen atom, red. Mutation of CMG2 117 Glu to Gln is show...
<p>(a) OBody sequences from the first round of affinity maturation, showing only the mutations at th...
<p>Based on an analysis of the current atomic model, we analyzed interactions between residues (midd...
<p><b>A.</b> The predicted structure of the wild-type MKK4-JNK3 complex with predicted binding energ...
<p>(A) WT; (B) Pmut. Pair mutation sites were shown with sticks: magenta represented L175 in WT and ...
<p>(A)Left panel: Ribon structure of the equilibrated VP1 from the EV71 particle (PDB ID 3VBU). BC l...
<p>(a) Crystal structure (PDB id: 3W4U) depicting a D100Y mutation (on Hbb) at an interface residue ...
<div><p>(A) Ribbon representation of the WT STAT1 homodimer complexed with DNA. Secondary structure ...
<p>(a) Superposition of the YW/ELA/HLA-A2 and the DMF5/ELA/HLA-A2 complexes. DMF5 α chain is yellow,...
<p>Residues at mutated sites on homologous proteins are shown in red (wild type) and blue (mutant) s...
<p>The rigidity analysis provided information based on the structural rigidity and flexibility of re...
<p>N-TIMP2 binding interface positions with their WT identity are displayed on the left, the mutated...
<p>A. Molecular interactions of E-DENV1 protein (shown in rainbow color cartoon) are shown with the ...
<p>The structure of GCK in the closed form (PDB code:1v4s) is shown as cyan ribbons. A) p.His137Asp....
<p><b>(A) Wild-type enzyme; (B) A269K/S187D mutant; (C) S187D/N188T mutant; D) A269K/S187D/N188T mut...
<p>Carbon atom, cyan; Nitrogen atom, blue; Oxygen atom, red. Mutation of CMG2 117 Glu to Gln is show...
<p>(a) OBody sequences from the first round of affinity maturation, showing only the mutations at th...
<p>Based on an analysis of the current atomic model, we analyzed interactions between residues (midd...
<p><b>A.</b> The predicted structure of the wild-type MKK4-JNK3 complex with predicted binding energ...
<p>(A) WT; (B) Pmut. Pair mutation sites were shown with sticks: magenta represented L175 in WT and ...
<p>(A)Left panel: Ribon structure of the equilibrated VP1 from the EV71 particle (PDB ID 3VBU). BC l...
<p>(a) Crystal structure (PDB id: 3W4U) depicting a D100Y mutation (on Hbb) at an interface residue ...
<div><p>(A) Ribbon representation of the WT STAT1 homodimer complexed with DNA. Secondary structure ...
<p>(a) Superposition of the YW/ELA/HLA-A2 and the DMF5/ELA/HLA-A2 complexes. DMF5 α chain is yellow,...
<p>Residues at mutated sites on homologous proteins are shown in red (wild type) and blue (mutant) s...