Research Article

In Silico Modeling and Functional Interpretations of Cry1Ab15 Toxin from Bacillus thuringiensis BtB-Hm-16

Table 1

The comparison among three-domain structural components of Cry1Aa and Cry1Ab15 toxin molecules.

Domain IDomain IIDomain III
Cry1AaCry1Ab15Cry1AaCry1Ab15Cry1AaCry1Ab15

β0Thr31-Tyr33α8aPro271-Glu274Pro271-Asn275α11aLeu475-Lys477
α1Pro35-Ser48Pro35-Ser48α8bAla284-Gln289Ser283-Ser290β13aSer486-Val488Ser487-Val489
α2aAln54-Ile63Aln54-Trp65β2Asp298-His310Ile299-His310β13bIle498-Arg501Ile499-Arg502
α2bPro70-Ile84Pro70-Ile84β3Phe313-Trp316Glu313-Ser324β14Gly505-Asn513Gly506-Asn514
α3Glu90-Ala119Glu90-Ala119β4Gly318-Pro325Tyr359-Arg368β15Tyr522-Ser530Tyr523-Ala530
α4Pro124-Leu148Pro124-Leu148α9Val326-Phe328 * Ser409-Glu412 β16Leu534-Ile540Leu534-Ile541
α5Gln154-Trp182Val155-Trp182β5Val348-Ser351Leu380-Tyr390β17Arg543-Phe550Arg544-Phe551
α6Ala186-Val218Ala186-Val218β6Ile357-Arg367Ala399-Tyr401α12aSer562-Ser564Ser563-Ser565
α7aSer223-Thr239Ser223-Tyr250β7Leu380-Leu383Thr406-Asp408β18Arg566-Gly569Arg567-Phe571
α7bLeu241-Tyr250β8Gly385-Phe390His428-Arg437β19Ser580-His588Ser581-His589
β1aGlu266-Thr269β9Thr400-Tyr402Ile447-His457β20Val596-Pro605Val597-Pro606
α10aSer410-Asp412α13Phe611-Ala623
α10bPro423-Gly426
β10His429-Val434Gln473-Pro475
β11Phe452-His456Thr480-Leu482
β12Thr471-Pro474

—: similar component not present. *Components in italics are spatially present at downstream sites.