2B1J
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4LZM
| COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS | Descriptor: | BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME | Authors: | Bell, J.A, Wilson, K, Zhang, X.-J, Faber, H.R, Nicholson, H, Matthews, B.W. | Deposit date: | 1991-01-25 | Release date: | 1992-07-15 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins, 10, 1991
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7LZM
| COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS | Descriptor: | CHLORIDE ION, T4 LYSOZYME | Authors: | Bell, J.A, Wilson, K, Zhang, X.-J, Faber, H.R, Nicholson, H, Matthews, B.W. | Deposit date: | 1991-01-25 | Release date: | 1992-07-15 | Last modified: | 2024-03-06 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins, 10, 1991
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5LZM
| COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS | Descriptor: | BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME | Authors: | Bell, J.A, Wilson, K, Zhang, X.-J, Faber, H.R, Nicholson, H, Matthews, B.W. | Deposit date: | 1991-01-25 | Release date: | 1992-07-15 | Last modified: | 2021-06-30 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins, 10, 1991
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6LZM
| COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS | Descriptor: | BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME | Authors: | Bell, J.A, Wilson, K, Zhang, X.-J, Faber, H.R, Nicholson, H, Matthews, B.W. | Deposit date: | 1991-01-25 | Release date: | 1992-07-15 | Last modified: | 2021-06-30 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins, 10, 1991
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3LZM
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2LP4
| Solution structure of P1-CheY/P2 complex in bacterial chemotaxis | Descriptor: | Chemotaxis protein CheA, Chemotaxis protein CheY | Authors: | Dahlquist, F, Mo, G, Zhou, H, Kamamura, T. | Deposit date: | 2012-01-31 | Release date: | 2012-10-24 | Last modified: | 2024-05-15 | Method: | SOLUTION NMR | Cite: | Solution structure of a complex of the histidine autokinase CheA with its substrate CheY. Biochemistry, 51, 2012
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1QSQ
| 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
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5TLN
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5TMN
| Slow-and fast-binding inhibitors of thermolysin display different modes of binding. crystallographic analysis of extended phosphonamidate transition-state analogues | Descriptor: | CALCIUM ION, N-[(S)-({[(benzyloxy)carbonyl]amino}methyl)(hydroxy)phosphoryl]-L-leucyl-L-leucine, THERMOLYSIN, ... | Authors: | Holden, H.M, Tronrud, D.E, Monzingo, A.F, Weaver, L.H, Matthews, B.W. | Deposit date: | 1987-06-29 | Release date: | 1989-01-09 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues. Biochemistry, 26, 1987
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7TLN
| STRUCTURAL ANALYSIS OF THE INHIBITION OF THERMOLYSIN BY AN ACTIVE-SITE-DIRECTED IRREVERSIBLE INHIBITOR | Descriptor: | 2-(ACETYL-HYDROXY-AMINO)-4-METHYL-PENTANOIC ACID METHYL ESTER, CALCIUM ION, THERMOLYSIN, ... | Authors: | Matthews, B.W, Holmes, M.A, Tronrud, D.E. | Deposit date: | 1983-01-27 | Release date: | 1983-03-09 | Last modified: | 2024-10-23 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor. Biochemistry, 22, 1983
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2TMN
| CRYSTALLOGRAPHIC STRUCTURAL ANALYSIS OF PHOSPHORAMIDATES AS INHIBITORS AND TRANSITION-STATE ANALOGS OF THERMOLYSIN | Descriptor: | CALCIUM ION, N~2~-phosphono-L-leucinamide, Thermolysin, ... | Authors: | Tronrud, D.E, Monzingo, A.F, Matthews, B.W. | Deposit date: | 1987-06-29 | Release date: | 1989-01-09 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin. Eur.J.Biochem., 157, 1986
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1CU0
| 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
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1CV4
| 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
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1CVK
| 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
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1TMN
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1CU2
| 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
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1CUQ
| 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
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1CV0
| 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
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1CTW
| 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
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1CU5
| 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
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1CV6
| 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
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8TLN
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1KS3
| 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
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1KW5
| 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
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