Fig. 12
The tryptophan residues closely interacting with A0 and A1 and their structural characteristics. Panel a, the hierarchical cluster analysis shows 3D structural relationships of the tryptophan residues of PsaA and PsaB from diverse organisms. The PDB IDs, the number of tryptophan and nine adjacent tryptophan residues as well as seventeen adjacent tryptophan residues are labeled. One tryptophan residue that is close to A0 and separated from the remaining seventeen tryptophan is labeled too; panel b, the residues closely interacting with A0A; panel c, the residues closely interacting with A0B; panel d, the MaxDist values for the tryptophan residues that are close to A0 and A1 and for the rest of tryptophan residues were calculated; panel e, the Theta values for the tryptophan residues that are close to A0 and A1 and for the rest of tryptophan residues were calculated; panels d–e, * means a p value is less than 0.05 using a t-test, ** means a p value is less than 0.01 and *** means a p value is less than 0.001 using a t-test; panel f, the residues close to A1A, A1B and the water cluster; panels b, c, f, the PDB is 5OY0; panel g, numbers of common TSR keys for the tryptophan residues that are close to A1, A0, and the rest of tryptophan residues and all tryptophan residues were calculated. Average numbers are labeled