The Val side chain in A441V fits well in this position and makes contacts with W456.
In the crystal structure of SoBADH the side chain of A441 interacts only with the active site residue W456, but in the known structures of the other three plant ALDH10s the residue at this position also makes contacts with W443 (SoBADH numbering) (Additional file 2: Figure S1A and Table S2).
However, because P110 lies in the 'latching loop' region of eukaryotic Mre11 that is likely to mediate contacts with Xrs2 (Schiller et al, 2012), sae2Δ suppression by this mutation might arise through altering such contacts.
In this regard, we note that the site of one of the sae2∆ suppressors, P110, lies in the 'latching loop' region of eukaryotic Mre11 that is likely to mediate contacts with Xrs2 (Schiller et al, 2012), suggesting that, in this case, sae2Δ suppression might arise through weakening this interaction and dampening Tel1 activity.
Current-voltage curves of carbon chains, spanning between carbon contacts with sp2-or sp3-hybridized contact atoms, are measured and calculated.
The other regions that pembrolizumab interacts with are located on the C and C' strands of hPD-1, which contribute critical contacts with hPD-L1 (Fig. 2A right).
The regenerated catalyst firstly contacts with C4 (in the first riser) and light naphtha (in the second riser), then reacts with atmospheric residue (AR) and recycling oil, respectively.
The ATP molecule makes additional contacts with G197, K200, R202 (P-loop), R459, R462 (motif VI) and other ordered water molecules (Fig. 2C).
Other than these four residues, the four other sidechains of visible residues extend into the solvent and make only marginal contacts with B56γ1.
We found that residues G342 and P/R344 in the 340-loop determine the size of the 340-cavity, and the calcium ion plays an important role in maintaining the conformation of the 340-loop through contacts with G345 and Q347.
Lys382 binds to a well-defined cleft on the surface formed by blade 2 and 3 of RBBP4, with its ε-group specifically contacts with Glu126, Asn128, and Glu179.
