Fig. 4
From: Dynamic disequilibrium-based pathogenicity model in mutated pyrin’s B30.2 domain—Casp1/p20 complex
Interface pocket amino acids between B30.2/SPRY and both p20 (A) and p10 (B) subunits of Casp-1 protein. The contributed amino acids inside the interface pocket divided to interacted residues (non-covalent bonding residues) and nearby ones (bonding scale <5 A° between its Cα atom and that of a surface residue as default setting). Out of the 13 retrieved variants, the interface nearby residues were arrowed by non-filled arrows, and the interacted ones were arrowed by the red filled arrows (B30.2/SPRY:Ser703 with casp1-p20:Ser175 ) & (casp1-p20:Val338 - B30.2/SPRY:Val726. CHARMM52 force field was applied and implemented in the prism server