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1CUP
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BU of 1cup by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
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 (1.89 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
1QSQ
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BU of 1qsq by Molmil
CAVITY CREATING MUTATION
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J, Matthews, B.W.
Deposit date:1999-06-22
Release date:1999-06-29
Last modified:2024-02-14
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
221L
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BU of 221l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1994-01-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
224L
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BU of 224l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-09-27
Release date:1994-01-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
206L
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BU of 206l by Molmil
PHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1996-03-19
Release date:1996-08-17
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
1CV5
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BU of 1cv5 by Molmil
T4 LYSOZYME MUTANT L133M
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 (1.87 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
1CV3
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BU of 1cv3 by Molmil
T4 LYSOZYME MUTANT L121M
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:1999-08-24
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
1CV4
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BU of 1cv4 by Molmil
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
1CVK
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BU of 1cvk by Molmil
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
1CV6
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BU of 1cv6 by Molmil
T4 LYSOZYME MUTANT V149M
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
119L
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BU of 119l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
118L
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BU of 118l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
120L
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BU of 120l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
122L
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BU of 122l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
123L
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BU of 123l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
125L
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BU of 125l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
126L
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BU of 126l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
128L
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BU of 128l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
127L
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BU of 127l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
1DYB
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BU of 1dyb by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.75 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
1DYE
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BU of 1dye by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 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
1DYA
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BU of 1dya by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
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
1DYG
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BU of 1dyg by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhou, H.-J, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.1 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
1DYF
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BU of 1dyf by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhou, H.-J, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
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
1DYD
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BU of 1dyd by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.1 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

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數據於2024-05-22公開中

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