Beta Pleated Sheet: Structural Design
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Four β-pleated sheets are evident as highlighted by the different colors of the arrows.  
For N » C orientation, the N-terminal amide nitrogen atom of each β-strand is represented by a light blue sphere while the C-terminal carbonyl carbon atom is similarly represented by a gray sphere .  
17 Strands of polypeptide in β-sheet conformation are found as listed below.
Sheet 1 (dark green) is comprised of six backbone strands encompassing (from top to bottom) AA residues 73-79, 59-66, 48-56, 188-196, 108-116, 124-130.
Sheet 2 (turquoise) is comprised of four backbone strands, AA residues 103-106, 153-156, 147-149, and 197-200; note that the last segment here is continuous with segment 188-196 of Sheet 1.
Sheet 3 (lavender) consists of seven backbone strands, AA 35-40, 23-30, 4-11, 208-215, 87-97, 169-176, 139-144.
"Sheet" 4 (red) consists of only one backbone strand, AA 179-181.

Except for the color-coded polypeptide Cα carbonsin this image, the other protein atoms in the backbone and sidechains are depicted by a modified CPK color convention.

Exercise: Move the molecule with the mouse and click the buttons below the image (as well as the polar and hydrophobic buttons) in order to get a better idea of the organization of residues on "one side surface" or on the "opposite side surface" of tβ-sheets.
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© Duane W. Sears
Revise February 3, 2019