The X-ray structure of a putative translation initiation inhibitor from Vibrio vulnificus CMCP6 was determined by molecular replacement and refined to 1.8 Å resolution. Asymmetric unit is comprised of three identical chains that form a trimer with buried surface area of 7,410 Å2. Every polypeptide chain possesses six-stranded antiparallel β-sheet that faces the interior of the trimer creating a β-barrel. Five α-helices and adjacent loops flank the β-sheet. The protein has a β3,α2, β,α2,β,α,β topology. The interior of the barrel has two hydrophobic sections that are on the terminal opposite sides of the structure and one hydrophilic section that has trapped water molecules.