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TitleDioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant.
Journal, issue, pagesProtein Sci., Vol. 14, Page 1115-1119, Year 2005
Publish dateDec 3, 2004 (structure data deposition date)
AuthorsHom, G.K. / Lassila, J.K. / Thomas, L.M. / Mayo, S.L.
External linksProtein Sci. / PubMed:15741348
MethodsX-ray diffraction
Resolution1.65 Å
Structure data

PDB-1y66:
Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-CD:
Unknown entry

ChemComp-DIO:
1,4-DIETHYLENE DIOXIDE

ChemComp-ACY:
ACETIC ACID

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsDE NOVO PROTEIN / protein design / dioxane / engrailed homeodomain

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