Table 1.
Summary of mutations and interaction partners exhibiting native or novel interactions
| Mutation (SNPs) | Interacting amino acid | Measured distance (Å) | Interaction/H-bond | Type of interaction |
|---|---|---|---|---|
| N34S |
N34‒S294 N34‒T295 N34‒T310 |
2.0 > 4.0 3.4 |
Strong H-bond Weak H-bond Weak H-bond |
Native/non-covalent Native/non-covalent Native/non-covalent |
| S66F |
S66‒Q422 S66F‒M420 |
2.6 – |
Moderate H-bond Packing defect |
Native/non-covalent – |
| G76D | G76D‒W412 | 1.7 | Anion–quadrupole | Redundant/non-covalent |
| G91D | G91D‒F213 | 2.9 | Anion–quadrupole | Redundant/non-covalent |
| R126H |
R126‒N29 R126‒S68 |
2.0 2.2 |
Strong/covalent Strong/covalent |
Native Native |
| R126L | R126L‒I33 | 3.8 | Hydrophobic | Redundant/non-covalent |
| E146K |
E146‒R92 E146K‒F213 |
2.1 3.3 |
Strong electrostatic Cation‒pi |
Native/non-covalent Redundant/non-covalent |
| L156R | L156R | – | Packing defect | – |
| L156N | L156N‒S148 | – | H-bond* | Redundant/non-covalent |
| R218H |
R218‒E220 R218H‒F213 |
2.4 2.1 |
Strong electrostatic NH‒pi |
Native/non-covalent Redundant/non-covalent |
| K256V | K256V-P401 | 3.6 | Hydrophobic | Redundant/non-covalent |
| E299K | E299‒K38 | 1.9 | Strong electrostatic | Native/non-covalent |
| T310I |
T310‒N34 T310‒Q172 |
3.4 3.3 |
Weak H-bond Weak H-bond |
Native/non-covalent Native/non-covalent |
| R333W |
R333‒E329 R333W‒F389 |
> 4.0* 3.1 |
Flexible region* pi‒pi |
Native/non-covalent Redundant/non-covalent |
*Refers to the positioning of amino acids in dynamic loop which can change its position upon formation of interaction pairs