PDB: 222624 resultsInfo pagesStatus searchChemie searchBIRD

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1GB5	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: 2000-06-26 Release date: 2000-07-27 Last modified: 2023-12-27 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry, 39, 2000
1GB6	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: 2000-06-26 Release date: 2000-07-27 Last modified: 2023-12-27 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry, 39, 2000
1GB7	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: 2000-06-26 Release date: 2000-07-27 Last modified: 2023-12-27 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry, 39, 2000
1GB8	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: 2000-06-26 Release date: 2000-07-27 Last modified: 2023-12-27 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry, 39, 2000
1GB9	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: 2000-06-26 Release date: 2000-07-27 Last modified: 2023-12-27 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry, 39, 2000
1GBA	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2.15 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBB	Alpha-lytic protease with met 190 replaced by ALA AND GLY 216 replaced by ALA complex with METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2024-06-05 Method: X-RAY DIFFRACTION (2.15 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBC	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2.2 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBD	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2.2 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBE	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2.3 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBF	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2024-06-05 Method: X-RAY DIFFRACTION (2.15 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBG	BACILLUS LICHENIFORMIS BETA-GLUCANASE Descriptor: (1,3-1,4)-BETA-D-GLUCAN 4 GLUCANOHYDROLASE, CALCIUM ION Authors: Hahn, M, Heinemann, U. Deposit date: 1995-08-25 Release date: 1995-12-07 Last modified: 2024-06-05 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution. FEBS Lett., 374, 1995
1GBH	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2.2 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBI	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2.3 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBJ	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBK	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2024-06-05 Method: X-RAY DIFFRACTION (2.13 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBL	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2.15 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBM	ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION Authors: Mace, J.E, Agard, D.A. Deposit date: 1995-09-06 Release date: 1996-01-29 Last modified: 2021-11-03 Method: X-RAY DIFFRACTION (2.28 Å) Cite: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254, 1995
1GBN	HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH THE NEUROTOXIN GABACULINE Descriptor: 3-AMINOBENZOIC ACID, GABACULINE, ORNITHINE AMINOTRANSFERASE, ... Authors: Shah, S.A, Shen, B.W, Brunger, A.T. Deposit date: 1997-05-29 Release date: 1998-06-03 Last modified: 2024-05-22 Method: X-RAY DIFFRACTION (2.3 Å) Cite: Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition. Structure, 5, 1997
1GBO	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: 2000-06-26 Release date: 2000-07-27 Last modified: 2023-12-27 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry, 39, 2000
1GBQ	SOLUTION NMR STRUCTURE OF THE GRB2 N-TERMINAL SH3 DOMAIN COMPLEXED WITH A TEN-RESIDUE PEPTIDE DERIVED FROM SOS DIRECT REFINEMENT AGAINST NOES, J-COUPLINGS, AND 1H AND 13C CHEMICAL SHIFTS, MINIMIZED AVERAGE STRUCTURE Descriptor: GRB2, SOS-1 Authors: Wittekind, M, Mapelli, C, Lee, V, Goldfarb, V, Friedrichs, M.S, Meyers, C.A, Mueller, L. Deposit date: 1996-12-23 Release date: 1997-09-04 Last modified: 2022-02-23 Method: SOLUTION NMR Cite: Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts. J.Mol.Biol., 267, 1997
1GBR	ORIENTATION OF PEPTIDE FRAGMENTS FROM SOS PROTEINS BOUND TO THE N-TERMINAL SH3 DOMAIN OF GRB2 DETERMINED BY NMR SPECTROSCOPY Descriptor: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2, SOS-A PEPTIDE Authors: Wittekind, M, Mapelli, C, Farmer, B.T, Suen, K.-L, Goldfarb, V, Tsao, J, Lavoie, T, Barbacid, M, Meyers, C.A, Mueller, L. Deposit date: 1994-08-12 Release date: 1995-01-26 Last modified: 2024-05-22 Method: SOLUTION NMR Cite: Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy. Biochemistry, 33, 1994
1GBS	CRYSTAL STRUCTURE OF BLACK SWAN GOOSE-TYPE LYSOZYME AT 1.8 ANGSTROMS RESOLUTION Descriptor: AUSTRALIAN BLACK SWAN EGG WHITE LYSOZYME Authors: Rao, Z, Machin, K, Isaacs, N. Deposit date: 1995-03-15 Release date: 1995-07-10 Last modified: 2024-06-05 Method: X-RAY DIFFRACTION (1.5 Å) Cite: A strategy for rapid and effective refinement applied to black swan lysozyme. Acta Crystallogr.,Sect.D, 51, 1995
1GBT	STRUCTURE OF AN ACYL-ENZYME INTERMEDIATE DURING CATALYSIS: (GUANIDINOBENZOYL) TRYPSIN Descriptor: 4-carbamimidamidobenzoic acid, BETA-TRYPSIN, CALCIUM ION, ... Authors: Singer, P.T, Sweet, R.M. Deposit date: 1991-09-17 Release date: 1994-01-31 Last modified: 2024-06-19 Method: X-RAY DIFFRACTION (2 Å) Cite: Structure of an acyl-enzyme intermediate during catalysis: (guanidinobenzoyl)trypsin. Biochemistry, 29, 1990
1GBU	DEOXY (BETA-(C93A,C112G)) HUMAN HEMOGLOBIN Descriptor: HEMOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION Authors: Vasquez, G.B, Ji, X, Fronticelli, C, Gilliland, G.L. Deposit date: 1996-01-04 Release date: 1997-01-11 Last modified: 2023-08-30 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces. Biophys.J., 76, 1999

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