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1CUQ
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BU of 1cuq by Molmil
T4 LYSOZYME MUTANT V103M
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
登録日1999-08-20
公開日1999-11-10
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.05 Å)
主引用文献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
1CV0
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BU of 1cv0 by Molmil
T4 LYSOZYME MUTANT F104M
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
登録日1999-08-20
公開日1999-11-10
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.12 Å)
主引用文献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
1CU5
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BU of 1cu5 by Molmil
T4 LYSOZYME MUTANT L91M
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
登録日1999-08-20
公開日1999-11-10
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (2.05 Å)
主引用文献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
1CV6
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BU of 1cv6 by Molmil
T4 LYSOZYME MUTANT V149M
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W.
登録日1999-08-22
公開日1999-11-10
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献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
1CX6
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BU of 1cx6 by Molmil
T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Matthews, B.W.
登録日1999-08-28
公開日1999-12-15
最終更新日2021-11-03
実験手法X-RAY DIFFRACTION (2.01 Å)
主引用文献Substitution with selenomethionine can enhance the stability of methionine-rich proteins.
J.Mol.Biol., 294, 1999
1CU0
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BU of 1cu0 by Molmil
T4 LYSOZYME MUTANT I78M
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
登録日1999-08-20
公開日1999-11-10
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.2 Å)
主引用文献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
1CV4
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BU of 1cv4 by Molmil
T4 LYSOZYME MUTANT L118M
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W.
登録日1999-08-22
公開日1999-11-10
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献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
1CVK
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BU of 1cvk by Molmil
T4 LYSOZYME MUTANT L118A
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W.
登録日1999-08-23
公開日1999-11-10
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (1.8 Å)
主引用文献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
1CU6
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BU of 1cu6 by Molmil
T4 LYSOZYME MUTANT L91A
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
登録日1999-08-20
公開日1999-11-17
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.1 Å)
主引用文献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
1CTW
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BU of 1ctw by Molmil
T4 LYSOZYME MUTANT I78A
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
登録日1999-08-20
公開日1999-11-10
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.1 Å)
主引用文献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
230L
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BU of 230l by Molmil
T4 LYSOZYME MUTANT M6L
分子名称: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
著者Lipscomb, L.A, Gassner, N.C, Snow, S, Eldridge, A.M, Drew, D.L, Baase, W.A, Matthews, B.W.
登録日1997-10-02
公開日1998-01-14
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme.
Protein Sci., 7, 1998
234L
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BU of 234l by Molmil
T4 LYSOZYME MUTANT M106L
分子名称: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
著者Lipscomb, L.A, Drew, D.L, Gassner, N, Baase, W.A, Matthews, B.W.
登録日1997-10-07
公開日1998-01-14
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme.
Protein Sci., 7, 1998
232L
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BU of 232l by Molmil
T4 LYSOZYME MUTANT M120K
分子名称: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
著者Lipscomb, L.A, Drew, D.L, Gassner, N, Baase, W.A, Matthews, B.W.
登録日1997-10-05
公開日1998-01-14
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.73 Å)
主引用文献Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme.
Protein Sci., 7, 1998
233L
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BU of 233l by Molmil
T4 LYSOZYME MUTANT M120L
分子名称: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
著者Lipscomb, L.A, Drew, D.L, Gassner, N, Baase, W.A, Matthews, B.W.
登録日1997-10-07
公開日1998-01-14
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme.
Protein Sci., 7, 1998
231L
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BU of 231l by Molmil
T4 LYSOZYME MUTANT M106K
分子名称: CHLORIDE ION, T4 LYSOZYME
著者Lipscomb, L.A, Drew, D.L, Gassner, N, Baase, W.A, Matthews, B.W.
登録日1997-10-03
公開日1998-01-14
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (2.5 Å)
主引用文献Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme.
Protein Sci., 7, 1998
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