1QUH
 
 | | L99G/E108V MUTANT OF T4 LYSOZYME | | 分子名称: | CHLORIDE ION, HEXANE-1,6-DIOL, PROTEIN (LYSOZYME) | | 著者 | Wray, J, Baase, W.A, Lindstrom, J.D, Poteete, A.R, Matthews, B.W. | | 登録日 | 1999-07-01 | | 公開日 | 1999-07-08 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | | 主引用文献 | 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
 | | L99A/E108V MUTANT OF T4 LYSOZYME | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, PROTEIN (LYSOZYME) | | 著者 | Wray, J, Baase, W.A, Lindstrom, J.D, Poteete, A.R, Matthews, B.W. | | 登録日 | 1999-07-01 | | 公開日 | 1999-07-08 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | 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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1YM3
 | | Crystal Structure of carbonic anhydrase RV3588c from Mycobacterium tuberculosis | | 分子名称: | CARBONIC ANHYDRASE (CARBONATE DEHYDRATASE) (CARBONIC DEHYDRATASE), MAGNESIUM ION, ZINC ION | | 著者 | Covarrubias, A.S, Larsson, A.M, Hogbom, M, Lindberg, J, Bergfors, T, Bjorkelid, C, Mowbray, S.L, Unge, T, Jones, T.A, Structural Proteomics in Europe (SPINE) | | 登録日 | 2005-01-20 | | 公開日 | 2005-03-08 | | 最終更新日 | 2023-08-23 | | 実験手法 | X-RAY DIFFRACTION (1.75 Å) | | 主引用文献 | Structure and function of carbonic anhydrases from Mycobacterium tuberculosis.
J.Biol.Chem., 280, 2005
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1QSQ
 | | CAVITY CREATING MUTATION | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Matthews, B.W. | | 登録日 | 1999-06-22 | | 公開日 | 1999-06-29 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | 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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1CU6
 | | T4 LYSOZYME MUTANT L91A | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-17 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | 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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1CV3
 | | T4 LYSOZYME MUTANT L121M | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-22 | | 公開日 | 1999-08-24 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | | 主引用文献 | 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
 | | T4 LYSOZYME MUTANT V87M | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.12 Å) | | 主引用文献 | 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
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.89 Å) | | 主引用文献 | 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
 | | T4 LYSOZYME MUTANT V111M | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | 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
 | | T4 LYSOZYME MUTANT L133M | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-22 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.87 Å) | | 主引用文献 | 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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1LWG
 | | Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, Lysozyme, ... | | 著者 | 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. | | 登録日 | 2002-05-31 | | 公開日 | 2003-05-20 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.
Biophys.Chem., 100, 2003
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1CU2
 | | T4 LYSOZYME MUTANT L84M | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.05 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.12 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.05 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-22 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | 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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1CU0
 | | T4 LYSOZYME MUTANT I78M | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-22 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | 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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1LPY
 | | Multiple Methionine Substitutions in T4 Lysozyme | | 分子名称: | BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME, ... | | 著者 | 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. | | 登録日 | 2002-05-08 | | 公開日 | 2002-05-22 | | 最終更新日 | 2024-04-03 | | 実験手法 | X-RAY DIFFRACTION (1.65 Å) | | 主引用文献 | 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
 | | T4 LYSOZYME METHIONINE CORE MUTANT | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-28 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.94 Å) | | 主引用文献 | Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
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1LWK
 | | Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, Lysozyme | | 著者 | 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. | | 登録日 | 2002-05-31 | | 公開日 | 2003-05-20 | | 最終更新日 | 2021-10-27 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | 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
 | | Design and synthesis of potent hydroxyethylamine (hea) bace-1 inhibitors | | 分子名称: | 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 | | 著者 | Borkakoti, N, Lindberg, J, Derbyshire, D. | | 登録日 | 2012-04-27 | | 公開日 | 2012-10-31 | | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | | 主引用文献 | 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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1LW9
 | | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME, ... | | 著者 | 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. | | 登録日 | 2002-05-30 | | 公開日 | 2003-05-20 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.45 Å) | | 主引用文献 | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.
Biophys.Chem., 100, 2003
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4EXG
 | | Design and synthesis of potent hydroxyethylamine (hea) bace-1 inhibitors | | 分子名称: | 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 | | 著者 | Borkakoti, N, Lindberg, J, Derbyshire, D. | | 登録日 | 2012-04-30 | | 公開日 | 2012-10-31 | | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | | 主引用文献 | 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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