Considering that the CD14 sequence of the PDB database had a truncation problem, we used the Robetta server to model the structure of the human CD14 molecule and then adopted the extracellular ORF7a and the modeled human CD14 for protein docking (Figure .B). Figure .B shows that the extracellular ORF7a can bind to the human CD14. The extracellular ORF7a binding sites are in the middle and C-terminal beta folding region. The one binding area of CD14 is near the alpha-helix between the second beta-sheet and the third beta-sheet. Another binding area is closed to alpha-helix between the third beta-sheet and the fourth beta-sheet. The N-terminal alpha-helix of CD14 is behind the binding region, which shows that the N-terminal structure of CD14 plays a vital role in assisting the binding of extracellular ORF7a to CD14. The N-terminal BPI1/LBP domain of extracellular ORF7a is outside. The first ATP binding site("HYQEC") is in the BPI1/LBP domain. The second ATP binding site ("TYEGNS") is close to the N-terminal active pocket of CD14.