1QUH
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![BU of 1quh by Molmil](/molmil-images/mine/1quh) | 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
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1QUO
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![BU of 1quo by Molmil](/molmil-images/mine/1quo) | 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
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1L0K
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![BU of 1l0k by Molmil](/molmil-images/mine/1l0k) | 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
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1CV3
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![BU of 1cv3 by Molmil](/molmil-images/mine/1cv3) | 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
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1QUD
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![BU of 1qud by Molmil](/molmil-images/mine/1qud) | 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
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1CU0
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![BU of 1cu0 by Molmil](/molmil-images/mine/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
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![BU of 1cv4 by Molmil](/molmil-images/mine/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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1CU2
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![BU of 1cu2 by Molmil](/molmil-images/mine/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
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![BU of 1cuq by Molmil](/molmil-images/mine/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
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![BU of 1cv0 by Molmil](/molmil-images/mine/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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1CU5
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![BU of 1cu5 by Molmil](/molmil-images/mine/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
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![BU of 1cv6 by Molmil](/molmil-images/mine/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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1CV1
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![BU of 1cv1 by Molmil](/molmil-images/mine/1cv1) | 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
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1CV5
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![BU of 1cv5 by Molmil](/molmil-images/mine/1cv5) | 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
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1QSQ
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![BU of 1qsq by Molmil](/molmil-images/mine/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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1CU3
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![BU of 1cu3 by Molmil](/molmil-images/mine/1cu3) | 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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1CUP
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![BU of 1cup by Molmil](/molmil-images/mine/1cup) | 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
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1QUG
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![BU of 1qug by Molmil](/molmil-images/mine/1qug) | 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
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1LWG
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![BU of 1lwg by Molmil](/molmil-images/mine/1lwg) | 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
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1CX7
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![BU of 1cx7 by Molmil](/molmil-images/mine/1cx7) | T4 LYSOZYME METHIONINE CORE MUTANT | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-28 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.94 Å) | Cite: | Use of differentially substituted selenomethionine proteins in X-ray structure determination. Acta Crystallogr.,Sect.D, 55, 1999
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1LPY
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![BU of 1lpy by Molmil](/molmil-images/mine/1lpy) | 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
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4EWO
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![BU of 4ewo by Molmil](/molmil-images/mine/4ewo) | Design and synthesis of potent hydroxyethylamine (hea) bace-1 inhibitors | Descriptor: | Beta-secretase 1, N-[(2S,3R)-4-{[(4S)-2-(2,2-dimethylpropyl)-6,6-dimethyl-4,5,6,7-tetrahydro-2H-indazol-4-yl]amino}-3-hydroxy-1-phenylbutan-2-yl]acetamide | Authors: | Borkakoti, N, Lindberg, J, Derbyshire, D. | Deposit date: | 2012-04-27 | Release date: | 2012-10-31 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Design and synthesis of potent hydroxyethylamine (HEA) BACE-1 inhibitors carrying prime side 4,5,6,7-tetrahydrobenzazole and 4,5,6,7-tetrahydropyridinoazole templates. Bioorg.Med.Chem.Lett., 22, 2012
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4EXG
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![BU of 4exg by Molmil](/molmil-images/mine/4exg) | Design and synthesis of potent hydroxyethylamine (hea) bace-1 inhibitors | Descriptor: | Beta-secretase 1, N-[(2S,3R)-4-{[(4S)-6-(2,2-dimethylpropyl)-2,2-dimethyl-3,4-dihydro-2H-thieno[2,3-b]pyran-4-yl]amino}-3-hydroxy-1-phenylbutan-2-yl]acetamide | Authors: | Borkakoti, N, Lindberg, J, Derbyshire, D. | Deposit date: | 2012-04-30 | Release date: | 2012-10-31 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Design and synthesis of potent hydroxyethylamine (HEA) BACE-1 inhibitors carrying prime side 4,5,6,7-tetrahydrobenzazole and 4,5,6,7-tetrahydropyridinoazole templates. Bioorg.Med.Chem.Lett., 22, 2012
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1LWK
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![BU of 1lwk by Molmil](/molmil-images/mine/1lwk) | 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
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1LW9
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![BU of 1lw9 by Molmil](/molmil-images/mine/1lw9) | 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
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