221L
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200L
| THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME | Descriptor: | BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME | Authors: | Baldwin, E, Xu, J, Hajiseyedjavadi, O, Matthews, B.W. | Deposit date: | 1995-11-06 | Release date: | 1996-03-08 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.95 Å) | Cite: | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. J.Mol.Biol., 259, 1996
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224L
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258L
| AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME | Descriptor: | CHLORIDE ION, LYSOZYME, ZINC ION | Authors: | Wray, J.W, Baase, W.A, Ostheimer, G.J, Matthews, B.W. | Deposit date: | 1999-01-05 | Release date: | 2000-09-11 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site. Protein Eng., 13, 2000
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260L
| AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME | Descriptor: | CHLORIDE ION, NICKEL (II) ION, PROTEIN (LYSOZYME) | Authors: | Wray, J.W, Baase, W.A, Ostheimer, G.J, Matthews, B.W. | Deposit date: | 1999-03-01 | Release date: | 2000-09-11 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site. Protein Eng., 13, 2000
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259L
| AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME | Descriptor: | CHLORIDE ION, COBALT (II) ION, PROTEIN (LYSOZYME) | Authors: | Wray, J.W, Baase, W.A, Ostheimer, G.J, Matthews, B.W. | Deposit date: | 1999-02-10 | Release date: | 1999-04-12 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.92 Å) | Cite: | Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site. Protein Eng., 13, 2000
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257L
| AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, PROTEIN (LYSOZYME) | Authors: | Wray, J.W, Baase, W.A, Ostheimer, G.J, Matthews, B.W. | Deposit date: | 1999-01-05 | Release date: | 2000-09-11 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site. Protein Eng., 13, 2000
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1P5C
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1P56
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2L78
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2NQ7
| Crystal structure of type 1 human methionine aminopeptidase in complex with 3-(2,2-Dimethylpropionylamino)pyridine-2-carboxylic acid thiazole-2-ylamide | Descriptor: | 3-[(2,2-DIMETHYLPROPANOYL)AMINO]-N-1,3-THIAZOL-2-YLPYRIDINE-2-CARBOXAMIDE, COBALT (II) ION, GLYCEROL, ... | Authors: | Addlagatta, A, Matthews, B.W. | Deposit date: | 2006-10-30 | Release date: | 2006-11-21 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc.Natl.Acad.Sci.Usa, 103, 2006
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2NQ6
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2OE4
| High Pressure Psuedo Wild Type T4 Lysozyme | Descriptor: | BETA-MERCAPTOETHANOL, CHLORIDE ION, Lysozyme | Authors: | Collins, M.D, Quillin, M.L, Matthews, B.W, Gruner, S.M. | Deposit date: | 2006-12-28 | Release date: | 2007-01-30 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Cooperative water filling of a non-polar protein cavity observed by high-pressure crystallography and simulation Proc.Natl.Acad.Sci.USA, 102, 2005
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2NVH
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1LNE
| A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN | Descriptor: | CADMIUM ION, CALCIUM ION, DIMETHYL SULFOXIDE, ... | Authors: | Holland, D.R, Hausrath, A.C, Juers, D, Matthews, B.W. | Deposit date: | 1994-05-13 | Release date: | 1995-05-08 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci., 4, 1995
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1LNF
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1LNB
| A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN | Descriptor: | CALCIUM ION, DIMETHYL SULFOXIDE, FE (III) ION, ... | Authors: | Holland, D.R, Hausrath, A.C, Juers, D, Matthews, B.W. | Deposit date: | 1994-05-13 | Release date: | 1995-05-08 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci., 4, 1995
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1LND
| A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN | Descriptor: | CALCIUM ION, DIMETHYL SULFOXIDE, LYSINE, ... | Authors: | Holland, D.R, Hausrath, A.C, Juers, D, Matthews, B.W. | Deposit date: | 1994-05-13 | Release date: | 1995-05-08 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci., 4, 1995
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1LNA
| A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN | Descriptor: | CALCIUM ION, COBALT (II) ION, DIMETHYL SULFOXIDE, ... | Authors: | Holland, D.R, Hausrath, A.C, Juers, D, Matthews, B.W. | Deposit date: | 1994-05-13 | Release date: | 1995-05-08 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci., 4, 1995
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1LNC
| A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN | Descriptor: | CALCIUM ION, DIMETHYL SULFOXIDE, LYSINE, ... | Authors: | Holland, D.R, Hausrath, A.C, Juers, D, Matthews, B.W. | Deposit date: | 1994-05-13 | Release date: | 1995-05-08 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci., 4, 1995
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2EWN
| Ecoli Biotin Repressor with co-repressor analog | Descriptor: | ((2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDROFURAN-2-YL)METHYL 5-((3AS,4S,6AR)-2-OXO-HEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL)PENTYL HYDROGEN PHOSPHATE, BirA bifunctional protein | Authors: | Wood, Z.A, Weaver, L.H, Matthews, B.W. | Deposit date: | 2005-11-04 | Release date: | 2006-02-21 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Co-repressor Induced Order and Biotin Repressor Dimerization: A Case for Divergent Followed by Convergent Evolution. J.Mol.Biol., 357, 2006
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2G6P
| Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in complex with Pyridyl pyrimidine derivative | Descriptor: | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, 5-CHLORO-6-METHYL-N-(2-PHENYLETHYL)-2-PYRIDIN-2-YLPYRIMIDIN-4-AMINE, COBALT (II) ION, ... | Authors: | Addlagatta, A, Hu, X, Liu, J.O, Matthews, B.W. | Deposit date: | 2006-02-24 | Release date: | 2006-06-20 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Identification of Pyridinylpyrimidines as Inhibitors of Human Methionine Aminopeptidases. Angew.Chem.Int.Ed.Engl., 45, 2006
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2GZ5
| Human Type 1 methionine aminopeptidase in complex with ovalicin at 1.1 Ang | Descriptor: | 3,4-DIHYDROXY-2-METHOXY-4-METHYL-3-[2-METHYL-3-(3-METHYL-BUT-2-ENYL) -OXIRANYL]-CYCLOHEXANONE, COBALT (II) ION, GLYCEROL, ... | Authors: | Addlagatta, A, Matthews, B.W. | Deposit date: | 2006-05-10 | Release date: | 2006-05-23 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (1.1 Å) | Cite: | Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase. Protein Sci., 15, 2006
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2HPT
| Crystal Structure of E. coli PepN (Aminopeptidase N)in complex with Bestatin | Descriptor: | 2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC ACID, Aminopeptidase N, GLYCEROL, ... | Authors: | Addlagatta, A, Matthews, B.W, Gay, L. | Deposit date: | 2006-07-17 | Release date: | 2006-08-15 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site. Proc.Natl.Acad.Sci.Usa, 103, 2006
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2HPO
| Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site | Descriptor: | Aminopeptidase N, GLYCEROL, ZINC ION | Authors: | Addlagatta, A, Matthews, B.W, Gay, L. | Deposit date: | 2006-07-17 | Release date: | 2006-08-15 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.65 Å) | Cite: | Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site. Proc.Natl.Acad.Sci.Usa, 103, 2006
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