| # | Atom names | Bond length (Å) | N-O-C angle (°) |
|---|---|---|---|
| α-helix | |||
| 1 | N(139:B [GLN])-O(135:B [LYS]) | 3.01 | 120.3 |
| 2 | N(125:B [GLU])-O(122:B [LEU]) | 3.12 | 126.2 |
| 3 | N(129:A [ALA])-O(125:A [GLU]) | 2.95 | 162.4 |
| 4 | N(136:A [LEU])-O(132:A [GLU]) | 3.59 | 137.1 |
| β-sheet | |||
| 1 | N(61:B [LEU])-O(69:B [ILE]) | 2.96 | 158.7 |
| 2 | N(67:A [HIS])-O(64:A [ASP]) | 2.89 | 126.2 |
| 3 | N(69:A [ILE])-O(62:A [LEU]) | 2.97 | 162.9 |
| 4 | N(62:A [LEU])-O(69:A [ILE]) | 3 | 158.4 |
Table 1. Parameters of hydrogen bonding between backbone atoms in secondary structure
Parameters of hydrogen bonding between backbone atoms in secondary structure of the 5HWL protein are represented in the Table 1.
Accordind to the provided parameters, the average length and angle values of hydrogen bonds in alpha-helices are 3.17Å and 136.5° respectively. For beta-sheets: 2.96Å and 151.05°. The length of hydrogen bonds, observed in the protein, corresponds to theoretical data (2.8-3.5Å). The angels in both alpha-helices and beta-sheets cannot be called ideal because of the effect the numerous side-chains have on the protein structure.