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Structure paper

TitleContribution of polar groups in the interior of a protein to the conformational stability.
Journal, issue, pagesBiochemistry, Vol. 40, Page 4853-4858, Year 2001
Publish dateNov 30, 2000 (structure data deposition date)
AuthorsTakano, K. / Yamagata, Y. / Yutani, K.
External linksBiochemistry / PubMed:11294653
MethodsX-ray diffraction
Resolution1.8 - 2.1 Å
Structure data

PDB-1gev:
BURIED POLAR MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1gez:
BURIED POLAR MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1gf0:
BURIED POLAR MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1gf3:
BURIED POLAR MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1gf4:
BURIED POLAR MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1gf5:
BURIED POLAR MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1gf6:
BURIED POLAR MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1gf7:
BURIED POLAR MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / buried polar / stability

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