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PDB: 867 件
1CU6
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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
1CV3
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T4 LYSOZYME MUTANT L121M
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1999-08-24
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
1CU0
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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
1CU2
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BU of 1cu2 by Molmil
T4 LYSOZYME MUTANT L84M
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 (1.85 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
1CUQ
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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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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
1CTW
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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
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
1D2W
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BU of 1d2w by Molmil
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Matthews, B.W.
登録日1999-09-28
公開日1999-10-08
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (1.89 Å)
主引用文献Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
1D2Y
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BU of 1d2y by Molmil
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Matthews, B.W.
登録日1999-09-28
公開日1999-10-08
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.06 Å)
主引用文献Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
1CX6
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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
1JTN
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Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet Region has weak intrinsic Folding Propensity
分子名称: LYSOZYME, SULFATE ION
著者Sagermann, M, Matthews, B.W.
登録日2001-08-21
公開日2002-03-20
最終更新日2023-08-16
実験手法X-RAY DIFFRACTION (2.3 Å)
主引用文献Crystal Structures of a T4-lysozyme Duplication-extension Mutant Demonstrate that the Highly Conserved beta-Sheet Region has Low Intrinsic Folding Propensity
J.Mol.Biol., 316, 2002
1JTM
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Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet has Weak Intrinsic Folding Propensity
分子名称: BETA-MERCAPTOETHANOL, LYSOZYME
著者Sagermann, M, Matthews, B.W.
登録日2001-08-21
公開日2002-03-20
最終更新日2023-08-16
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Crystal Structures of a T4-lysozyme Duplication-extension Mutant Demonstrate that the Highly Conserved beta-Sheet Region has Low Intrinsic Folding Propensity
J.Mol.Biol., 316, 2002
1I6S
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T4 LYSOZYME MUTANT C54T/C97A/N101A
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Kovall, R.A, Baldwin, E.P, Matthews, B.W.
登録日2001-03-04
公開日2001-05-09
最終更新日2023-08-09
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme.
Protein Sci., 10, 2001
1KW7
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BU of 1kw7 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
登録日2002-01-28
公開日2003-06-03
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.89 Å)
主引用文献Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1KS3
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BU of 1ks3 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
登録日2002-01-10
公開日2003-06-03
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (2.16 Å)
主引用文献Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1KW5
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METHIONINE CORE MUTANT OF T4 LYSOZYME
分子名称: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
著者Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
登録日2002-01-28
公開日2003-06-03
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.75 Å)
主引用文献Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1JQU
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Are Carboxy Terminii of Helices Coded by the Local Sequence or by Tertiary Structure Contacts
分子名称: Lysozyme
著者Sagermann, M, Martensson, L.-G, Baase, W.A, Matthews, B.W.
登録日2001-08-08
公開日2002-03-06
最終更新日2023-08-16
実験手法X-RAY DIFFRACTION (2.6 Å)
主引用文献A test of proposed rules for helix capping: Implications for protein design
Protein Sci., 11, 2002
1L02
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CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
分子名称: T4 LYSOZYME
著者Dao-Pin, S, Alber, T, Matthews, B.W.
登録日1988-02-05
公開日1988-04-16
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.
Nature, 330, 1987
1L09
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CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
分子名称: T4 LYSOZYME
著者Dao-Pin, S, Bell, J, Alber, T, Matthews, B.W.
登録日1988-02-05
公開日1988-04-16
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.
Nature, 330, 1987
1L26
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REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
分子名称: BETA-MERCAPTOETHANOL, T4 LYSOZYME
著者Bell, J.A, Dao-Pin, S, Matthews, B.W.
登録日1989-05-01
公開日1990-01-15
最終更新日2022-11-23
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239, 1988
1L44
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CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
分子名称: T4 LYSOZYME
著者Daopin, S, Matthews, B.W.
登録日1991-01-28
公開日1991-10-15
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991

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