1C6G
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1C6Q
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1C6H
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186L
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191L
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175L
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181L
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188L
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169L
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187L
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159L
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![BU of 159l by Molmil](/molmil-images/mine/159l) | CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND | Descriptor: | BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME | Authors: | Blaber, M, Matthews, B.W. | Deposit date: | 1994-06-20 | Release date: | 1994-08-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. J.Mol.Biol., 246, 1995
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1CU0
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![BU of 1cu0 by Molmil](/molmil-images/mine/1cu0) | T4 LYSOZYME MUTANT I78M | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-20 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1CV4
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![BU of 1cv4 by Molmil](/molmil-images/mine/1cv4) | T4 LYSOZYME MUTANT L118M | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-22 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1CVK
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![BU of 1cvk by Molmil](/molmil-images/mine/1cvk) | T4 LYSOZYME MUTANT L118A | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-23 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1C69
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1C6B
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1C63
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1C68
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1C6C
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1C6D
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1CU2
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![BU of 1cu2 by Molmil](/molmil-images/mine/1cu2) | T4 LYSOZYME MUTANT L84M | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-20 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1CUQ
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![BU of 1cuq by Molmil](/molmil-images/mine/1cuq) | T4 LYSOZYME MUTANT V103M | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-20 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.05 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1CV0
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![BU of 1cv0 by Molmil](/molmil-images/mine/1cv0) | T4 LYSOZYME MUTANT F104M | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-20 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.12 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1CTW
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![BU of 1ctw by Molmil](/molmil-images/mine/1ctw) | T4 LYSOZYME MUTANT I78A | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-20 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1CU5
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![BU of 1cu5 by Molmil](/molmil-images/mine/1cu5) | T4 LYSOZYME MUTANT L91M | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-20 | Release date: | 1999-11-10 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.05 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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