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1FGA
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BU of 1fga by Molmil
REFINEMENT OF THE STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION AND ANALYSIS OF PRESUMED HEPARIN BINDING SITES BY SELENATE SUBSTITUTION
Descriptor: BASIC FIBROBLAST GROWTH FACTOR, BETA-MERCAPTOETHANOL, SELENATE ION
Authors:Eriksson, A.E, Matthews, B.W.
Deposit date:1993-02-26
Release date:1993-07-15
Last modified:2020-07-22
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.
Protein Sci., 2, 1993
3CDQ
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BU of 3cdq by Molmil
Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, Lysozyme, ...
Authors:Mooers, B.H.M, Matthews, B.W.
Deposit date:2008-02-27
Release date:2009-02-17
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (1.68 Å)
Cite:Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme.
Protein Sci., 18, 2009
1HEL
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BU of 1hel by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME
Descriptor: HEN EGG WHITE LYSOZYME
Authors:Wilson, K.P, Malcolm, B.A, Matthews, B.W.
Deposit date:1992-01-10
Release date:1993-10-31
Last modified:2021-06-30
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
J.Biol.Chem., 267, 1992
1HEM
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BU of 1hem by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME
Descriptor: HEN EGG WHITE LYSOZYME
Authors:Wilson, K.P, Malcolm, B.A, Matthews, B.W.
Deposit date:1992-01-10
Release date:1993-10-31
Last modified:2021-06-30
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
J.Biol.Chem., 267, 1992
1HER
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BU of 1her by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME
Descriptor: HEN EGG WHITE LYSOZYME
Authors:Wilson, K.P, Malcolm, B.A, Matthews, B.W.
Deposit date:1992-01-10
Release date:1993-10-31
Last modified:2021-06-30
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
J.Biol.Chem., 267, 1992
1HEO
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BU of 1heo by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME
Descriptor: HEN EGG WHITE LYSOZYME
Authors:Wilson, K.P, Malcolm, B.A, Matthews, B.W.
Deposit date:1992-01-10
Release date:1993-10-31
Last modified:2021-06-30
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
J.Biol.Chem., 267, 1992
1HEP
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BU of 1hep by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME
Descriptor: HEN EGG WHITE LYSOZYME
Authors:Wilson, K.P, Malcolm, B.A, Matthews, B.W.
Deposit date:1992-01-10
Release date:1993-10-31
Last modified:2021-06-30
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
J.Biol.Chem., 267, 1992
1HEN
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BU of 1hen by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME
Descriptor: HEN EGG WHITE LYSOZYME
Authors:Wilson, K.P, Malcolm, B.A, Matthews, B.W.
Deposit date:1992-01-10
Release date:1993-10-31
Last modified:2021-06-30
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
J.Biol.Chem., 267, 1992
1HEQ
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BU of 1heq by Molmil
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME
Descriptor: HEN EGG WHITE LYSOZYME
Authors:Wilson, K.P, Malcolm, B.A, Matthews, B.W.
Deposit date:1992-01-10
Release date:1993-10-31
Last modified:2021-06-30
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
J.Biol.Chem., 267, 1992
1THL
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BU of 1thl by Molmil
Thermolysin complexed with a novel glutaramide derivative, n-(1-(2(r,s)-carboxy-4-phenylbutyl) cyclopentylcarbonyl)-(s)-tryptophan
Descriptor: CALCIUM ION, N-({1-[(2S)-2-carboxy-4-phenylbutyl]cyclopentyl}carbonyl)-L-tryptophan, THERMOLYSIN, ...
Authors:Holland, D.R, Matthews, B.W.
Deposit date:1993-11-17
Release date:1994-01-31
Last modified:2023-08-09
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Inhibition of Thermolysin and Neutral Endopeptidase 24.11 By a Novel Glutaramide Derivative; X-Ray Structure Determination of the Thermolysin-Inhibitor Complex
Biochemistry, 33, 1994
2OE9
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BU of 2oe9 by Molmil
High-pressure structure of pseudo-WT 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 (2.01 Å)
Cite:Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography.
J.Mol.Biol., 367, 2007
2OE7
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BU of 2oe7 by Molmil
High-Pressure 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:Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography.
J.Mol.Biol., 367, 2007
2OEA
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BU of 2oea by Molmil
High-pressure structure of pseudo-WT 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 (2.01 Å)
Cite:Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography.
J.Mol.Biol., 367, 2007
2GCT
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BU of 2gct by Molmil
STRUCTURE OF GAMMA-CHYMOTRYPSIN IN THE RANGE PH 2.0 TO PH 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW PH
Descriptor: GAMMA-CHYMOTRYPSIN A, SULFATE ION, TETRAPEPTIDE ADDUCT
Authors:Dixon, M.M, Matthews, B.W.
Deposit date:1990-09-04
Release date:1991-10-15
Last modified:2013-03-13
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH.
Int.J.Biol.Macromol., 13, 1991
3F8V
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BU of 3f8v by Molmil
Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, Lysozyme, ...
Authors:Mooers, B.H.M, Matthews, B.W.
Deposit date:2008-11-13
Release date:2009-02-17
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (1.08 Å)
Cite:Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His.
Protein Sci., 18, 2009
3FA0
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BU of 3fa0 by Molmil
Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His
Descriptor: 2-HYDROXYETHYL DISULFIDE, BETA-MERCAPTOETHANOL, CHLORIDE ION, ...
Authors:Mooers, B.H.M, Matthews, B.W.
Deposit date:2008-11-14
Release date:2009-02-17
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.09 Å)
Cite:Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His.
Protein Sci., 18, 2009
3FAD
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BU of 3fad by Molmil
Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His
Descriptor: BETA-MERCAPTOETHANOL, Lysozyme, PHOSPHATE ION
Authors:Mooers, B.H.M, Matthews, B.W.
Deposit date:2008-11-17
Release date:2009-02-17
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.2 Å)
Cite:Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His.
Protein Sci., 18, 2009
3FI5
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BU of 3fi5 by Molmil
Crystal Structure of T4 Lysozyme Mutant R96W
Descriptor: CHLORIDE ION, ISOPROPYL ALCOHOL, Lysozyme, ...
Authors:Mooers, B.H.M, Matthews, B.W.
Deposit date:2008-12-11
Release date:2009-02-17
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (1.53 Å)
Cite:Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme.
Protein Sci., 18, 2009
3F9L
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BU of 3f9l by Molmil
Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His
Descriptor: CHLORIDE ION, Lysozyme, PHOSPHATE ION, ...
Authors:Mooers, B.H.M, Matthews, B.W.
Deposit date:2008-11-14
Release date:2009-02-17
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (1.19 Å)
Cite:Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His.
Protein Sci., 18, 2009
3GCT
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BU of 3gct by Molmil
STRUCTURE OF GAMMA-*CHYMOTRYPSIN IN THE RANGE $P*H 2.0 TO $P*H 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW $P*H
Descriptor: GAMMA-CHYMOTRYPSIN A, SULFATE ION, UNK PRO GLY ALA TYR PEPTIDE
Authors:Dixon, M.M, Matthews, B.W.
Deposit date:1990-09-04
Release date:1991-10-15
Last modified:2013-03-13
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH.
Int.J.Biol.Macromol., 13, 1991
1L44
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BU of 1l44 by Molmil
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor: T4 LYSOZYME
Authors:Daopin, S, Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2022-11-23
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L58
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BU of 1l58 by Molmil
ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, T4 LYSOZYME
Authors:Nicholson, H, Matthews, B.W.
Deposit date:1991-05-06
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:
To be Published
1L64
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BU of 1l64 by Molmil
TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Heinz, D, Matthews, B.W.
Deposit date:1991-09-23
Release date:1991-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence.
Proc.Natl.Acad.Sci.USA, 89, 1992
1L71
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BU of 1l71 by Molmil
MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA-HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1991-09-23
Release date:1991-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability.
Protein Sci., 1, 1992
1L76
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BU of 1l76 by Molmil
TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Sauer, U, Matthews, B.W.
Deposit date:1991-09-23
Release date:1991-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions.
J.Biol.Chem., 267, 1992

219869

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