This structure is from an actual protein, and therefore it shows the typical twist of an actual beta sheet.
This is a side view of the same sheet. The side chains of residues 90, 92, and 94 are colored magenta, while the side chains of residues 91 and 93 are colored green. This illustrates that the side chains of neighboring residues in a beta strand are found on opposite faces of the beta sheet. The backbone atoms, and the atoms of the other residues, are colored in the CPK scheme.
The Hydrogen bonding pattern of a parallel beta sheet is shown here by dotted lines. The Hbonds between the strands are somewhat diagonal. Notice that the amino acid with the green alpha carbon, on the right strand, does not Hbond to its closest neighbor in the other strand, also colored green. Instead, it makes one Hbond to each of the adjacent residues, colored yellow
Note: there are two H bonds drawn within the left strand. These are not actually H bonds, but instead reflect a limitation of the software.