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2MGB	HIGH RESOLUTION CRYSTAL STRUCTURES OF FIVE DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN Descriptor: MYOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION Authors: Quillin, M.L, Arduini, R.M, Phillips Jr, G.N. Deposit date: 1993-05-10 Release date: 1994-01-31 Last modified: 2024-02-21 Method: X-RAY DIFFRACTION (2 Å) Cite: High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J.Mol.Biol., 234, 1993
2MGL	HIGH RESOLUTION CRYSTAL STRUCTURES OF FIVE DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN Descriptor: MYOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION Authors: Quillin, M.L, Arduini, R.M, Phillips Jr, G.N. Deposit date: 1993-05-10 Release date: 1994-01-31 Last modified: 2024-02-21 Method: X-RAY DIFFRACTION (2 Å) Cite: High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J.Mol.Biol., 234, 1993
1GOB	COOPERATIVE STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY INSERTION OF GLY-80B AND GLY-77-> ALA SUBSTITUTION Descriptor: RIBONUCLEASE H Authors: Ishikawa, K, Kimura, S, Nakamura, H, Morikawa, K, Kanaya, S. Deposit date: 1993-05-10 Release date: 1994-01-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2 Å) Cite: Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution. Biochemistry, 32, 1993
1GOC	COOPERATIVE STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY INSERTION OF GLY-80B AND GLY-77-> ALA SUBSTITUTION Descriptor: RIBONUCLEASE H Authors: Ishikawa, K, Kimura, S, Nakamura, H, Morikawa, K, Kanaya, S. Deposit date: 1993-05-10 Release date: 1994-01-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2 Å) Cite: Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution. Biochemistry, 32, 1993
1LAW	STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY CAVITY-FILLING MUTATIONS WITHIN A HYDROPHOBIC CORE Descriptor: RIBONUCLEASE H Authors: Ishikawa, K, Nakamura, H, Morikawa, K, Kanaya, S. Deposit date: 1993-05-10 Release date: 1993-10-31 Last modified: 2024-02-14 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. Biochemistry, 32, 1993
1GOA	COOPERATIVE STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY INSERTION OF GLY-80B AND GLY-77-> ALA SUBSTITUTION Descriptor: RIBONUCLEASE H Authors: Ishikawa, K, Kimura, S, Nakamura, H, Morikawa, K, Kanaya, S. Deposit date: 1993-05-10 Release date: 1994-01-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.9 Å) Cite: Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution. Biochemistry, 32, 1993
1LAV	STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY CAVITY-FILLING MUTATIONS WITHIN A HYDROPHOBIC CORE Descriptor: RIBONUCLEASE H Authors: Ishikawa, K, Nakamura, H, Morikawa, K, Kanaya, S. Deposit date: 1993-05-10 Release date: 1993-10-31 Last modified: 2024-02-14 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. Biochemistry, 32, 1993
1ETA	THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL 30-->MET VARIANT TO 1.7 ANGSTROMS RESOLUTION Descriptor: 3,5,3',5'-TETRAIODO-L-THYRONINE, TRANSTHYRETIN Authors: Braden, B.C, Steinrauf, L.K, Hamilton, J.A. Deposit date: 1993-05-12 Release date: 1995-01-26 Last modified: 2023-11-15 Method: X-RAY DIFFRACTION (1.7 Å) Cite: The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution. J.Biol.Chem., 268, 1993
1ETB	THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL 30-->MET VARIANT TO 1.7 ANGSTROMS RESOLUTION Descriptor: 3,5,3',5'-TETRAIODO-L-THYRONINE, TRANSTHYRETIN Authors: Braden, B.C, Steinrauf, L.K, Hamilton, J.A. Deposit date: 1993-05-12 Release date: 1995-01-26 Last modified: 2023-11-15 Method: X-RAY DIFFRACTION (1.7 Å) Cite: The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution. J.Biol.Chem., 268, 1993
1RGC	THE COMPLEX BETWEEN RIBONUCLEASE T1 AND 3'-GUANYLIC ACID SUGGESTS GEOMETRY OF ENZYMATIC REACTION PATH. AN X-RAY STUDY Descriptor: CALCIUM ION, GUANOSINE-3'-MONOPHOSPHATE, RIBONUCLEASE T1 Authors: Heydenreich, A, Koellner, G, Choe, H.W, Cordes, F, Kisker, C, Schindelin, H, Adamiak, R, Hahn, U, Saenger, W. Deposit date: 1993-05-12 Release date: 1994-01-31 Last modified: 2017-11-29 Method: X-RAY DIFFRACTION (2 Å) Cite: The complex between ribonuclease T1 and 3'GMP suggests geometry of enzymic reaction path. An X-ray study. Eur.J.Biochem., 218, 1993
1RBL	STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301 Descriptor: 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE, FORMIC ACID, MAGNESIUM ION, ... Authors: Newman, J, Gutteridge, S, Branden, C.-I, Jones, T.A. Deposit date: 1993-05-12 Release date: 1994-06-22 Last modified: 2024-06-05 Method: X-RAY DIFFRACTION (2.2 Å) Cite: Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301. Acta Crystallogr.,Sect.D, 49, 1993
1CSQ	CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN Descriptor: COLD SHOCK PROTEIN B(CSPB) Authors: Schindelin, H, Heinemann, U. Deposit date: 1993-05-12 Release date: 1995-05-12 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2.7 Å) Cite: Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature, 364, 1993
1CSP	CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN Descriptor: COLD SHOCK PROTEIN B(CSPB) Authors: Schindelin, H, Heinemann, U. Deposit date: 1993-05-12 Release date: 1995-05-12 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2.45 Å) Cite: Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature, 364, 1993
1EDB	CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE Descriptor: CHLORIDE ION, HALOALKANE DEHALOGENASE Authors: Verschueren, K.H.G, Dijkstra, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2.01 Å) Cite: Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site. Biochemistry, 32, 1993
1DYF	DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Zhou, H.-J, Matthews, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2017-11-29 Method: X-RAY DIFFRACTION (1.9 Å) Cite: Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J.Mol.Biol., 235, 1994
1DYC	DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Zhang, X, Matthews, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2.1 Å) Cite: Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J.Mol.Biol., 235, 1994
1DYD	DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Zhang, X, Matthews, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2017-11-29 Method: X-RAY DIFFRACTION (2.1 Å) Cite: Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J.Mol.Biol., 235, 1994
1DYB	DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Zhang, X, Matthews, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2017-11-29 Method: X-RAY DIFFRACTION (1.75 Å) Cite: Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J.Mol.Biol., 235, 1994
1EDD	CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE Descriptor: CHLORIDE ION, HALOALKANE DEHALOGENASE Authors: Verschueren, K.H.G, Dijkstra, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2.19 Å) Cite: Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site. Biochemistry, 32, 1993
1DYE	DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Zhang, X, Matthews, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J.Mol.Biol., 235, 1994
1DYA	DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Zhang, X, Matthews, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2017-11-29 Method: X-RAY DIFFRACTION (1.9 Å) Cite: Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J.Mol.Biol., 235, 1994
1DYG	DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME Authors: Zhou, H.-J, Matthews, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2017-11-29 Method: X-RAY DIFFRACTION (2.1 Å) Cite: Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J.Mol.Biol., 235, 1994
1GCA	THE 1.7 ANGSTROMS REFINED X-RAY STRUCTURE OF THE PERIPLASMIC GLUCOSE(SLASH)GALACTOSE RECEPTOR FROM SALMONELLA TYPHIMURIUM Descriptor: CALCIUM ION, GLUCOSE/GALACTOSE-BINDING PROTEIN, beta-D-galactopyranose Authors: Zou, J.-Y, Mowbray, S.L. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.7 Å) Cite: The 1.7 A refined X-ray structure of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J.Mol.Biol., 233, 1993
1EDE	REFINED X-RAY STRUCTURES OF HALOALKANE DEHALOGENASE AT PH 6.2 AND PH 8.2 AND IMPLICATIONS FOR THE REACTION MECHANISM Descriptor: HALOALKANE DEHALOGENASE Authors: Verschueren, K.H.G, Dijkstra, B.W. Deposit date: 1993-05-13 Release date: 1993-10-31 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (1.9 Å) Cite: Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism. J.Mol.Biol., 232, 1993
1RTP	REFINED X-RAY STRUCTURE OF RAT PARVALBUMIN, A MAMMALIAN ALPHA-LINEAGE PARVALBUMIN, AT 2.0 A RESOLUTION Descriptor: ALPHA-PARVALBUMIN, CALCIUM ION Authors: Mcphalen, C.A, Sielecki, A.R, Santarsiero, B.D, James, M.N.G. Deposit date: 1993-05-14 Release date: 1994-01-31 Last modified: 2024-02-14 Method: X-RAY DIFFRACTION (2 Å) Cite: Refined crystal structure of rat parvalbumin, a mammalian alpha-lineage parvalbumin, at 2.0 A resolution. J.Mol.Biol., 235, 1994

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