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3L64
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BU of 3l64 by Molmil
T4 Lysozyme S44E/WT*
Descriptor: BETA-MERCAPTOETHANOL, Lysozyme
Authors:Blaber, M, Zhang, X.-J, Lindstrom, J.D, Pepiot, S.D, Baase, W.A, Matthews, B.W.
Deposit date:2009-12-23
Release date:2010-01-19
Last modified:2024-02-21
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
J.Mol.Biol., 235, 1994
1QUH
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BU of 1quh by Molmil
L99G/E108V MUTANT OF T4 LYSOZYME
Descriptor: CHLORIDE ION, HEXANE-1,6-DIOL, PROTEIN (LYSOZYME)
Authors:Wray, J, Baase, W.A, Lindstrom, J.D, Poteete, A.R, Matthews, B.W.
Deposit date:1999-07-01
Release date:1999-07-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.
J.Mol.Biol., 292, 1999
1QUO
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BU of 1quo by Molmil
L99A/E108V MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, PROTEIN (LYSOZYME)
Authors:Wray, J, Baase, W.A, Lindstrom, J.D, Poteete, A.R, Matthews, B.W.
Deposit date:1999-07-01
Release date:1999-07-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.
J.Mol.Biol., 292, 1999
1QUD
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BU of 1qud by Molmil
L99G MUTANT OF T4 LYSOZYME
Descriptor: CHLORIDE ION, HEXANE-1,6-DIOL, PROTEIN (LYSOZYME)
Authors:Wray, J, Baase, W.A, Lindstrom, J.D, Poteete, A.R, Matthews, B.W.
Deposit date:1999-07-01
Release date:1999-07-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.
J.Mol.Biol., 292, 1999
1QUG
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BU of 1qug by Molmil
E108V MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, PROTEIN (LYSOZYME)
Authors:Wray, J, Baase, W.A, Lindstrom, J.D, Poteete, A.R, Matthews, B.W.
Deposit date:1999-07-01
Release date:1999-07-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.
J.Mol.Biol., 292, 1999
1KW7
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BU of 1kw7 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-01-28
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.89 Å)
Cite: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
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-01-10
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.16 Å)
Cite: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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BU of 1kw5 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-01-28
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1KY1
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BU of 1ky1 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-02-01
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.05 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1L0K
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BU of 1l0k by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-02-11
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.02 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1KY0
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BU of 1ky0 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-02-01
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.97 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1L0J
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BU of 1l0j by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-02-11
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.98 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1LPY
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BU of 1lpy by Molmil
Multiple Methionine Substitutions in T4 Lysozyme
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME, ...
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H.M, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-05-08
Release date:2002-05-22
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.
Biophys.Chem., 100, 2003
1LWK
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BU of 1lwk by Molmil
Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, Lysozyme
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H.M, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.M.
Deposit date:2002-05-31
Release date:2003-05-20
Last modified:2021-10-27
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.
Biophys.Chem., 100, 2003
1LWG
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BU of 1lwg by Molmil
Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, Lysozyme, ...
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H.M, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.M.
Deposit date:2002-05-31
Release date:2003-05-20
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.
Biophys.Chem., 100, 2003
1LW9
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BU of 1lw9 by Molmil
Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME, ...
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H.M, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-05-30
Release date:2003-05-20
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.45 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.
Biophys.Chem., 100, 2003
1CV1
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BU of 1cv1 by Molmil
T4 LYSOZYME MUTANT V111M
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
1CU6
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BU of 1cu6 by Molmil
T4 LYSOZYME MUTANT L91A
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:1999-11-17
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
1CU0
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BU of 1cu0 by Molmil
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
1CU2
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BU of 1cu2 by Molmil
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
1CUQ
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BU of 1cuq by Molmil
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
1CV0
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BU of 1cv0 by Molmil
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
1CTW
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BU of 1ctw by Molmil
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
1CU5
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BU of 1cu5 by Molmil
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
1CU3
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BU of 1cu3 by Molmil
T4 LYSOZYME MUTANT V87M
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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