<p>(A) Sequence conservation of the α4β5α5 dimeric interface of RegX3, PhoB, TorR and YycF in OmpR/PhoB family. Residues are numbered according to RegX3 and colored based on chemistry: acidic in red, basic in blue, hydrophobic in black, polar in green and neutral in purple. Coevolved pairs are under-dotted with the same colors. (B-E) Active state structures of RegX3 (2OQR), TorR (1ZGZ), PhoB (1ZES) and YycF (1NXP) in OmpR/PhoB family with coevolved residues in dimeric interface highlighted in sticks. It is noteworthy that RegX3 forms a complete dimeric structure with swapped domains that are colored in light and dark greys.</p
<p>Residue index of 8 to 11 are colored in green and residue 19 to the end of the chain is colored i...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
<p>Italicized pairs indicate coevolved inter-monomeric contacts of RegX3 but intra-monomeric contact...
<p>Contact map of coevolved residues in OmpR/PhoB family. Axes are residue numbers. Grey spots repre...
<p>The subunits of the homo-dimer are shown in blue and orange respectively. The secondary structure...
The full-length, two-domain response regulator RegX3 from Mycobacterium tuberculosis is a dimer stab...
<p>(A) Surface representation of the dimer interface of <i>Mtu</i>DAH7PS (PDB 3NV8). Residues contri...
<p>Superposed A-chains of monomeric (shown in orange) and inhibited dimeric (shown in green) PrV pro...
<p>(A) Structure of the intertwined dimer of the c-Src-SH3 domain. Open chain of the WT c-Src-SH3 do...
<p>(A) β1/β1′ and (B) α1/α1′ residues that stabilize the dimer interface are highlighted. The interf...
<p>(A) Subunits of the dimer are arranged in head to tail manner where subunit A and B are shown in ...
<p>Numbers above the sequences correspond to <i>C. trachomatis</i> ChxR. The secondary structure of ...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
<p>Residue index of 8 to 11 are colored in green and residue 19 to the end of the chain is colored i...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
<p>Italicized pairs indicate coevolved inter-monomeric contacts of RegX3 but intra-monomeric contact...
<p>Contact map of coevolved residues in OmpR/PhoB family. Axes are residue numbers. Grey spots repre...
<p>The subunits of the homo-dimer are shown in blue and orange respectively. The secondary structure...
The full-length, two-domain response regulator RegX3 from Mycobacterium tuberculosis is a dimer stab...
<p>(A) Surface representation of the dimer interface of <i>Mtu</i>DAH7PS (PDB 3NV8). Residues contri...
<p>Superposed A-chains of monomeric (shown in orange) and inhibited dimeric (shown in green) PrV pro...
<p>(A) Structure of the intertwined dimer of the c-Src-SH3 domain. Open chain of the WT c-Src-SH3 do...
<p>(A) β1/β1′ and (B) α1/α1′ residues that stabilize the dimer interface are highlighted. The interf...
<p>(A) Subunits of the dimer are arranged in head to tail manner where subunit A and B are shown in ...
<p>Numbers above the sequences correspond to <i>C. trachomatis</i> ChxR. The secondary structure of ...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
<p>Residue index of 8 to 11 are colored in green and residue 19 to the end of the chain is colored i...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...
Supplementary files for the paper: Coevolution of residues provides evidence of a functional heterod...