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PDB: 148 results

3JR6
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BU of 3jr6 by Molmil
Sequential reorganization of beta-sheet topology by insertion of a single strand
Descriptor: Lysozyme, SULFATE ION
Authors:Sagermann, M, Baas, W.A, Matthews, B.W.
Deposit date:2009-09-08
Release date:2009-10-20
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (3 Å)
Cite:Sequential reorganization of beta-sheet topology by insertion of a single strand.
Protein Sci., 15, 2006
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
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
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
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
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
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
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
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
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
261L
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BU of 261l by Molmil
STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING
Descriptor: LYSOZYME
Authors:Sagermann, M, Baase, W.A, Matthews, B.W.
Deposit date:1999-05-11
Release date:1999-05-24
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.
Proc.Natl.Acad.Sci.USA, 96, 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
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
262L
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BU of 262l by Molmil
STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING
Descriptor: LYSOZYME
Authors:Sagermann, M, Baase, W.A, Matthews, B.W.
Deposit date:1999-05-11
Release date:1999-05-24
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.
Proc.Natl.Acad.Sci.USA, 96, 1999
1CX6
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BU of 1cx6 by Molmil
T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Matthews, B.W.
Deposit date:1999-08-28
Release date:1999-12-15
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.01 Å)
Cite:Substitution with selenomethionine can enhance the stability of methionine-rich proteins.
J.Mol.Biol., 294, 1999
1B6I
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BU of 1b6i by Molmil
T4 LYSOZYME MUTANT WITH CYS 54 REPLACED BY THR, CYS 97 REPLACED BY ALA, THR 21 REPLACED BY CYS AND LYS 124 REPLACED BY CYS (C54T,C97A,T21C,K124C)
Descriptor: 2-HYDROXYETHYL DISULFIDE, PROTEIN (LYSOZYME)
Authors:Vetter, I.R, Baase, W.A, Snow, S, Matthews, B.W.
Deposit date:1999-01-14
Release date:2000-01-12
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme.
Proc.Natl.Acad.Sci.USA, 97, 2000
226L
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BU of 226l by Molmil
GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Baldwin, E.P, Baase, W.A, Zhang, X.-J, Feher, V, Matthews, B.W.
Deposit date:1997-06-25
Release date:1998-03-18
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions.
J.Mol.Biol., 277, 1998
223L
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BU of 223l by Molmil
GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS
Descriptor: BENZENE, BETA-MERCAPTOETHANOL, CHLORIDE ION, ...
Authors:Baldwin, E.P, Baase, W.A, Zhang, X.-J, Feher, V, Matthews, B.W.
Deposit date:1997-06-25
Release date:1998-03-18
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions.
J.Mol.Biol., 277, 1998
210L
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BU of 210l by Molmil
PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, T4 LYSOZYME
Authors:Vetter, I.R, Baase, W.A, Heinz, D.W, Xiong, J.-P, Snow, S, Matthews, B.W.
Deposit date:1996-09-23
Release date:1996-12-23
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.89 Å)
Cite:Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme.
Protein Sci., 5, 1996
220L
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BU of 220l by Molmil
GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS
Descriptor: BENZENE, BETA-MERCAPTOETHANOL, CHLORIDE ION, ...
Authors:Baldwin, E.P, Baase, W.A, Zhang, X.-J, Feher, V, Matthews, B.W.
Deposit date:1997-06-25
Release date:1998-03-18
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions.
J.Mol.Biol., 277, 1998
225L
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BU of 225l by Molmil
GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS
Descriptor: BETA-MERCAPTOETHANOL, PARA-XYLENE, T4 LYSOZYME
Authors:Baldwin, E.P, Baase, W.A, Zhang, X.-J, Feher, V, Matthews, B.W.
Deposit date:1997-06-25
Release date:1998-03-18
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions.
J.Mol.Biol., 277, 1998

222036

数据于2024-07-03公开中

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