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STRUCTURAL BASIS OF AMINO ACID ALPHA HELIX PROPENSITY
Descriptor:	T4 LYSOZYME
Authors:	Blaber, M, Matthews, B.W.
Deposit date:	1993-08-17
Release date:	1994-07-31
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (1.85 Å)
Cite:	Structural basis of amino acid alpha helix propensity. Science, 260, 1993

1FO0

MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX
Descriptor:	NATURALLY PROCESSED OCTAPEPTIDE PBM1, PROTEIN (ALLOGENEIC H-2KB MHC CLASS I MOLECULE), PROTEIN (BETA-2 MICROGLOBULIN), ...
Authors:	Reiser, J.B, Darnault, C, Guimezanes, A, Gregoire, C, Mosser, T, Schmitt-Verhulst, A.-M, Fontecilla-Camps, J.C, Malissen, B, Housset, D, Mazza, G.
Deposit date:	2000-08-24
Release date:	2000-10-02
Last modified:	2023-08-09
Method:	X-RAY DIFFRACTION (2.5 Å)
Cite:	Crystal structure of a T cell receptor bound to an allogeneic MHC molecule. Nat.Immunol., 1, 2000

1NAM

MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX
Descriptor:	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, BM3.3 T Cell Receptor alpha-Chain, BM3.3 T Cell Receptor beta-Chain, ...
Authors:	Reiser, J.-B, Darnault, C, Gregoire, C, Mosser, T, Mazza, G, Kearnay, A, van der Merwe, P.A, Fontecilla-Camps, J.C, Housset, D, Malissen, B.
Deposit date:	2002-11-28
Release date:	2003-03-11
Last modified:	2023-08-16
Method:	X-RAY DIFFRACTION (2.7 Å)
Cite:	CDR3 loop flexibility contributes to the degeneracy of TCR recognition Nat.Immunol., 4, 2003

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

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

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

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

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

1L44

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

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

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

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

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

1L63

ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1991-05-06
Release date:	1991-10-15
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (1.75 Å)
Cite:	Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry, 30, 1991

1L36

TOWARD A SIMPLIFICATION OF THE PROTEIN FOLDING PROBLEM: A STABILIZING POLYALANINE ALPHA-HELIX ENGINEERED IN T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:	Zhang, X.-J, Baase, W.A, Matthews, B.W.
Deposit date:	1990-12-26
Release date:	1991-10-15
Last modified:	2022-11-23
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. Biochemistry, 30, 1991

1L52

STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
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:	Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. J.Mol.Biol., 221, 1991

1L40

CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
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 (1.85 Å)
Cite:	Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry, 30, 1991

1L47

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

1L50

STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
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 (1.85 Å)
Cite:	Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. J.Mol.Biol., 221, 1991

1L38

CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
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 (1.8 Å)
Cite:	Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry, 30, 1991

1L45

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

1L55

ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1991-05-06
Release date:	1991-10-15
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (1.9 Å)
Cite:	Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry, 30, 1991

1L69

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 (1.9 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

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