1IP1
| G37A HUMAN LYSOZYME | Descriptor: | LYSOZYME C, SODIUM ION | Authors: | Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2001-04-20 | Release date: | 2001-11-14 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. Proteins, 45, 2001
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1INU
| CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS | Descriptor: | LYSOZYME, SODIUM ION | Authors: | Funahashi, J, Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2000-12-04 | Release date: | 2000-12-20 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. J.Biol.Chem., 277, 2002
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1IP5
| G105A HUMAN LYSOZYME | Descriptor: | LYSOZYME C, SODIUM ION | Authors: | Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2001-04-20 | Release date: | 2001-11-14 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. Proteins, 45, 2001
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1IP7
| G129A HUMAN LYSOZYME | Descriptor: | LYSOZYME C, SODIUM ION | Authors: | Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2001-04-20 | Release date: | 2001-11-14 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. Proteins, 45, 2001
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1IP4
| G72A HUMAN LYSOZYME | Descriptor: | LYSOZYME C, SODIUM ION | Authors: | Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2001-04-20 | Release date: | 2001-11-14 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. Proteins, 45, 2001
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1IP3
| G68A HUMAN LYSOZYME | Descriptor: | LYSOZYME C, SODIUM ION, SULFATE ION | Authors: | Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2001-04-20 | Release date: | 2001-11-14 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. Proteins, 45, 2001
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1IP2
| G48A HUMAN LYSOZYME | Descriptor: | LYSOZYME C, SODIUM ION | Authors: | Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2001-04-20 | Release date: | 2001-11-14 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. Proteins, 45, 2001
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1IX0
| I59A-3SS human lysozyme | Descriptor: | SODIUM ION, lysozyme | Authors: | Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2002-06-06 | Release date: | 2003-07-22 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Buried water molecules contribute to the conformational stability of a protein PROTEIN ENG., 16, 2003
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1IP6
| G127A HUMAN LYSOZYME | Descriptor: | LYSOZYME C, SODIUM ION | Authors: | Takano, K, Yamagata, Y, Yutani, K. | Deposit date: | 2001-04-20 | Release date: | 2001-11-14 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. Proteins, 45, 2001
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8I1H
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8I18
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8I1G
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8I1C
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8I1D
| Crystal structure of human MTH1(G2K mutant) in complex with 2-oxo-dATP at pH 7.7 | Descriptor: | 7,8-dihydro-8-oxoguanine triphosphatase, SODIUM ION, [[(2R,3S,5R)-5-(6-azanyl-2-oxidanylidene-1H-purin-9-yl)-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate | Authors: | Nakamura, T, Yamagata, Y. | Deposit date: | 2023-01-13 | Release date: | 2023-03-22 | Last modified: | 2023-07-26 | Method: | X-RAY DIFFRACTION (1.2 Å) | Cite: | Protonation states of Asp residues in the human Nudix hydrolase MTH1 contribute to its broad substrate recognition. Febs Lett., 597, 2023
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8I1A
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8I1J
| Crystal structure of human MTH1(G2K/D120N mutant) in complex with 2-oxo-dATP at pH 9.7 | Descriptor: | 7,8-dihydro-8-oxoguanine triphosphatase, SODIUM ION, [[(2R,3S,5R)-5-(6-azanyl-2-oxidanylidene-1H-purin-9-yl)-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate | Authors: | Nakamura, T, Yamagata, Y. | Deposit date: | 2023-01-13 | Release date: | 2023-03-22 | Last modified: | 2023-07-26 | Method: | X-RAY DIFFRACTION (1.08 Å) | Cite: | Protonation states of Asp residues in the human Nudix hydrolase MTH1 contribute to its broad substrate recognition. Febs Lett., 597, 2023
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8I19
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8I1I
| Crystal structure of human MTH1(G2K/D120N mutant) in complex with 2-oxo-dATP at pH 7.7 | Descriptor: | 7,8-dihydro-8-oxoguanine triphosphatase, SODIUM ION, [[(2R,3S,5R)-5-(6-azanyl-2-oxidanylidene-1H-purin-9-yl)-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate | Authors: | Nakamura, T, Yamagata, Y. | Deposit date: | 2023-01-13 | Release date: | 2023-03-22 | Last modified: | 2023-07-26 | Method: | X-RAY DIFFRACTION (1.2 Å) | Cite: | Protonation states of Asp residues in the human Nudix hydrolase MTH1 contribute to its broad substrate recognition. Febs Lett., 597, 2023
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8I1F
| Crystal structure of human MTH1(G2K mutant) in complex with 2-oxo-dATP at pH 8.6 | Descriptor: | 7,8-dihydro-8-oxoguanine triphosphatase, SODIUM ION, [[(2R,3S,5R)-5-(6-azanyl-2-oxidanylidene-1H-purin-9-yl)-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate | Authors: | Nakamura, T, Yamagata, Y. | Deposit date: | 2023-01-13 | Release date: | 2023-03-22 | Last modified: | 2023-07-26 | Method: | X-RAY DIFFRACTION (1.05 Å) | Cite: | Protonation states of Asp residues in the human Nudix hydrolase MTH1 contribute to its broad substrate recognition. Febs Lett., 597, 2023
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8I1E
| Crystal structure of human MTH1(G2K mutant) in complex with 2-oxo-dATP at pH 8.0 | Descriptor: | 7,8-dihydro-8-oxoguanine triphosphatase, SODIUM ION, [[(2R,3S,5R)-5-(6-azanyl-2-oxidanylidene-1H-purin-9-yl)-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate | Authors: | Nakamura, T, Yamagata, Y. | Deposit date: | 2023-01-13 | Release date: | 2023-03-22 | Last modified: | 2023-07-26 | Method: | X-RAY DIFFRACTION (1.1 Å) | Cite: | Protonation states of Asp residues in the human Nudix hydrolase MTH1 contribute to its broad substrate recognition. Febs Lett., 597, 2023
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8I8S
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8I8T
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1WDW
| Structural basis of mutual activation of the tryptophan synthase a2b2 complex from a hyperthermophile, Pyrococcus furiosus | Descriptor: | PYRIDOXAL-5'-PHOSPHATE, Tryptophan synthase alpha chain, Tryptophan synthase beta chain 1 | Authors: | Lee, S.J, Ogasahara, K, Ma, J, Nishio, K, Ishida, M, Yamagata, Y, Tsukihara, T, Yutani, K, RIKEN Structural Genomics/Proteomics Initiative (RSGI) | Deposit date: | 2004-05-19 | Release date: | 2005-07-12 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (3 Å) | Cite: | Conformational Changes in the Tryptophan Synthase from a Hyperthermophile upon alpha(2)beta(2) Complex Formation: Crystal Structure of the Complex Biochemistry, 44, 2005
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1X12
| Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192D) 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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1X10
| Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192A) 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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