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Structure paper

TitleComparison of design strategies for alpha-helix backbone modification in a protein tertiary fold.
Journal, issue, pagesChem. Commun. (Camb. ), Vol. 52, Page 3789-3792, Year 2016
Publish dateJan 7, 2016 (structure data deposition date)
AuthorsTavenor, N.A. / Reinert, Z.E. / Lengyel, G.A. / Griffith, B.D. / Horne, W.S.
External linksChem. Commun. (Camb. ) / PubMed:26853882
MethodsX-ray diffraction
Resolution1.8 - 2.15 Å
Structure data

PDB-5hfy:
Backbone Modifications in the Protein GB1 Helix: beta-2-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-5hg2:
Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-2-Asn35
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5hi1:
Backbone Modifications in the Protein GB1 Helix: Aib24, beta-3-Lys28, beta-3-Lys31, Aib35
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-MG:
Unknown entry

ChemComp-ACT:
ACETATE ION

Source
  • streptococcus sp. group g (bacteria)
KeywordsDE NOVO PROTEIN / synthetic protein

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