TABLE 3.
New polar interactions directly involving or induced by side chain atoms of mutated residues in mFMO_20
| Hydrogen donora | Hydrogen acceptora | Distance (Å)b | Structural locationc |
|
|---|---|---|---|---|
| Donor | Acceptor | |||
| K300 (Nζ) | D351 (Oδ2) | 3.0 | Loop β18-β19 | α6 |
| K300 (Nζ) | N378D (Oδ2) | 2.8 | Loop β18-β19 | α7 |
| R356 (Nε/Nη2) | M353Q (Oε1) | 2.8/2.7 | α6 | α6 |
| R356 (Nη1) | L360E (Oε2) | 3.4 | α6 | α6 |
| K358R (Nη1/Nη2) | D374 (Oδ2) | 3.0/2.8 | α6 | α7 |
| N394 (Nδ2) | T370D (Oδ1) | 3.4 | α8 | α7 |
| L398K (Nζ) | E366 (Oε2) | 3.1 | α8 | α7 |
| K401 (Nζ) | A365D (Oδ2) | 2.7 | α8 | α7 |
a
Hydrogen donor and acceptor atoms of the amino acid side chains are indicated in parentheses.
b
The distances between hydrogen donor and acceptor atoms of the amino acid side chains are shown.
c
The structural location is indicated by the secondary structure element.