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Structure paper

TitleContribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,).
Journal, issue, pagesBiochemistry, Vol. 38, Page 12698-12708, Year 1999
Publish dateApr 22, 1999 (structure data deposition date)
AuthorsTakano, K. / Yamagata, Y. / Funahashi, J. / Hioki, Y. / Kuramitsu, S. / Yutani, K.
External linksBiochemistry / PubMed:10504240
MethodsX-ray diffraction
Resolution1.8 - 2.2 Å
Structure data

PDB-1cj6:
T11A MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1cj7:
T11V MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1cj8:
T40A MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1cj9:
T40V MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1ckc:
T43A MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1ckd:
T43V MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1ckf:
T52A MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1ckg:
T52V MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1ckh:
T70V MUTANT HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / STABILITY / HYDROGEN BOND

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