2BQE
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2BQI
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2BQF
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2BQK
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2BQJ
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2BQA
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2BQC
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2BQH
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2BQL
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2BQM
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2BQB
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2BQO
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2BQG
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2BQD
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2BQN
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1YAO
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![BU of 1yao by Molmil](/molmil-images/mine/1yao) | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | 分子名称: | LYSOZYME, SODIUM ION | 著者 | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | 登録日 | 1995-09-29 | 公開日 | 1996-04-03 | 最終更新日 | 2021-11-03 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J.Mol.Biol., 254, 1995
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1YAM
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![BU of 1yam by Molmil](/molmil-images/mine/1yam) | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | 分子名称: | LYSOZYME, SODIUM ION | 著者 | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | 登録日 | 1995-09-29 | 公開日 | 1996-04-03 | 最終更新日 | 2021-11-03 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J.Mol.Biol., 254, 1995
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1YAN
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![BU of 1yan by Molmil](/molmil-images/mine/1yan) | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | 分子名称: | LYSOZYME, SODIUM ION | 著者 | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | 登録日 | 1995-09-29 | 公開日 | 1996-04-03 | 最終更新日 | 2021-11-03 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J.Mol.Biol., 254, 1995
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1YAQ
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![BU of 1yaq by Molmil](/molmil-images/mine/1yaq) | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | 分子名称: | LYSOZYME, SODIUM ION | 著者 | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | 登録日 | 1995-09-29 | 公開日 | 1996-04-03 | 最終更新日 | 2021-11-03 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J.Mol.Biol., 254, 1995
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1YAP
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![BU of 1yap by Molmil](/molmil-images/mine/1yap) | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | 分子名称: | LYSOZYME, SODIUM ION | 著者 | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | 登録日 | 1995-09-29 | 公開日 | 1996-04-03 | 最終更新日 | 2021-11-03 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J.Mol.Biol., 254, 1995
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1LHJ
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![BU of 1lhj by Molmil](/molmil-images/mine/1lhj) | ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS | 分子名称: | HUMAN LYSOZYME | 著者 | Inaka, K, Matsushima, M, Herning, T, Kuroki, R, Yutani, K, Kikuchi, M. | 登録日 | 1992-03-27 | 公開日 | 1994-01-31 | 最終更新日 | 2017-11-29 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. Biochemistry, 31, 1992
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1V7Y
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![BU of 1v7y by Molmil](/molmil-images/mine/1v7y) | Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature | 分子名称: | SULFATE ION, Tryptophan synthase alpha chain | 著者 | Nishio, K, Morimoto, Y, Ishizuka, M, Ogasahara, K, Yutani, K, Tsukihara, T, RIKEN Structural Genomics/Proteomics Initiative (RSGI) | 登録日 | 2003-12-25 | 公開日 | 2005-02-15 | 最終更新日 | 2023-12-27 | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | 主引用文献 | Conformational Changes in the alpha-Subunit Coupled to Binding of the beta(2)-Subunit of Tryptophan Synthase from Escherichia coli: Crystal Structure of the Tryptophan Synthase alpha-Subunit Alon Biochemistry, 44, 2005
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1Z8W
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![BU of 1z8w by Molmil](/molmil-images/mine/1z8w) | Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192I) from a Hyperthermophile, Pyrococcus furiosus | 分子名称: | Pyrrolidone-carboxylate peptidase | 著者 | Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K. | 登録日 | 2005-03-31 | 公開日 | 2006-06-13 | 最終更新日 | 2023-10-25 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles. Biochemistry, 45, 2006
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1Z8X
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![BU of 1z8x by Molmil](/molmil-images/mine/1z8x) | Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192V) from a Hyperthermophile, Pyrococcus furiosus | 分子名称: | Pyrrolidone-carboxylate peptidase | 著者 | Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K. | 登録日 | 2005-03-31 | 公開日 | 2006-06-13 | 最終更新日 | 2023-10-25 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles. Biochemistry, 45, 2006
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1Z8T
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![BU of 1z8t by Molmil](/molmil-images/mine/1z8t) | Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192Q) from a Hyperthermophile, Pyrococcus furiosus | 分子名称: | Pyrrolidone-carboxylate peptidase | 著者 | Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K. | 登録日 | 2005-03-31 | 公開日 | 2006-06-13 | 最終更新日 | 2023-10-25 | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | 主引用文献 | Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles. Biochemistry, 45, 2006
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