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
 | | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | | Descriptor: | LYSOZYME, SODIUM ION | | Authors: | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | | Deposit date: | 1995-09-29 | | Release date: | 1996-04-03 | | Last modified: | 2021-11-03 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | 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
 | | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | | Descriptor: | LYSOZYME, SODIUM ION | | Authors: | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | | Deposit date: | 1995-09-29 | | Release date: | 1996-04-03 | | Last modified: | 2021-11-03 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | 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
 | | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | | Descriptor: | LYSOZYME, SODIUM ION | | Authors: | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | | Deposit date: | 1995-09-29 | | Release date: | 1996-04-03 | | Last modified: | 2021-11-03 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | 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
 | | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | | Descriptor: | LYSOZYME, SODIUM ION | | Authors: | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | | Deposit date: | 1995-09-29 | | Release date: | 1996-04-03 | | Last modified: | 2021-11-03 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | 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
 | | CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS | | Descriptor: | LYSOZYME, SODIUM ION | | Authors: | Yamagata, Y, Kaneda, H, Fujii, S, Takano, K, Ogasahara, K, Kanaya, E, Kikuchi, M, Oobatake, M, Yutani, K. | | Deposit date: | 1995-09-29 | | Release date: | 1996-04-03 | | Last modified: | 2021-11-03 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | 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
 | | ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS | | Descriptor: | HUMAN LYSOZYME | | Authors: | Inaka, K, Matsushima, M, Herning, T, Kuroki, R, Yutani, K, Kikuchi, M. | | Deposit date: | 1992-03-27 | | Release date: | 1994-01-31 | | Last modified: | 2017-11-29 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | 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
 | | Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature | | Descriptor: | SULFATE ION, Tryptophan synthase alpha chain | | Authors: | Nishio, K, Morimoto, Y, Ishizuka, M, Ogasahara, K, Yutani, K, Tsukihara, T, RIKEN Structural Genomics/Proteomics Initiative (RSGI) | | Deposit date: | 2003-12-25 | | Release date: | 2005-02-15 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | 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
 | | Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192I) from a Hyperthermophile, Pyrococcus furiosus | | Descriptor: | Pyrrolidone-carboxylate peptidase | | Authors: | Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K. | | Deposit date: | 2005-03-31 | | Release date: | 2006-06-13 | | Last modified: | 2023-10-25 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | 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
 | | Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192V) from a Hyperthermophile, Pyrococcus furiosus | | Descriptor: | Pyrrolidone-carboxylate peptidase | | Authors: | Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K. | | Deposit date: | 2005-03-31 | | Release date: | 2006-06-13 | | Last modified: | 2023-10-25 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | 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
 | | Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192Q) from a Hyperthermophile, Pyrococcus furiosus | | Descriptor: | Pyrrolidone-carboxylate peptidase | | Authors: | Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K. | | Deposit date: | 2005-03-31 | | Release date: | 2006-06-13 | | Last modified: | 2023-10-25 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | 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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