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Structure paper

TitleIncreasing protein stability by engineering the n -> pi * interaction at the beta-turn.
Journal, issue, pagesChem Sci, Vol. 11, Page 9480-9487, Year 2020
Publish dateNov 7, 2019 (structure data deposition date)
AuthorsKhatri, B. / Majumder, P. / Nagesh, J. / Penmatsa, A. / Chatterjee, J.
External linksChem Sci / PubMed:34094214
MethodsX-ray diffraction
Resolution1.73 - 1.95 Å
Structure data

PDB-6l91:
X-ray structure of synthetic GB1 domain with the mutation K10(DVA).
Method: X-RAY DIFFRACTION / Resolution: 1.842 Å

PDB-6l9b:
X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11A
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-6l9d:
X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11S
Method: X-RAY DIFFRACTION / Resolution: 1.73 Å

PDB-6lji:
X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11V
Method: X-RAY DIFFRACTION / Resolution: 1.843 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • streptococcus sp. group g (bacteria)
KeywordsIMMUNE SYSTEM / Synthetic GB1 domain variant / D-aminoacid substitution

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