Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences.
Journal, issue, pages	J. Mol. Biol., Vol. 229, Page 747-769, Year 1993
Publish date	Jan 21, 1992 (structure data deposition date)
Authors	Eriksson, A.E. / Baase, W.A. / Matthews, B.W.
External links	J. Mol. Biol. / PubMed:8433369
Methods	X-ray diffraction
Resolution	1.7 - 2 Å
Structure data	PDB-1l85: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 2 Å PDB-1l86: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-1l87: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-1l88: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.85 Å PDB-1l89: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.9 Å PDB-1l90: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.75 Å PDB-1l91: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-1l92: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.7 Å PDB-1l93: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-1l94: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-1l95: SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES Method: X-RAY DIFFRACTION / Resolution: 2 Å
Chemicals	ChemComp-CL: Unknown entry ChemComp-BME: BETA-MERCAPTOETHANOL ChemComp-HOH: WATER
Source	enterobacteria phage t4 (virus)
Keywords	HYDROLASE(O-GLYCOSYL)