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 205 and 207 are colored magenta, while the side chains of residues 206 and 208 are colored green. This illustrates that the side chains of neighboring residues in 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 an anti-parallel beta sheet is shown here by dotted lines. The Hbonds between the strands are parallel to each other and somewhat perpendicular to the strands. Notice that the pair of amino acids with the yellow alpha carbons make two H bonds with each other. But the pair of amino acids with the green alpha carbons are pointed away from each other and do not make any H bonds with each other. Finally, the next pair of amino acids, colored gold repeat the H bonding pattern of the yellow ones.