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REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	BETA-MERCAPTOETHANOL, T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2022-11-23
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

1L30

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

1L21

CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.85 Å)
Cite:	Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. J.Mol.Biol., 210, 1989

1L28

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.9 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

1L33

CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. J.Mol.Biol., 210, 1989

1L32

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

1L24

ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
Descriptor:	T4 LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc.Natl.Acad.Sci.USA, 84, 1987

1L34

HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS
Descriptor:	T4 LYSOZYME
Authors:	Weaver, L.H, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.9 Å)
Cite:	High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His. Biochemistry, 28, 1989

1L25

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

149L

CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Wilson, K, Matthews, B.W.
Deposit date:	1994-01-25
Release date:	1994-04-30
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (2.6 Å)
Cite:	Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme. Protein Sci., 3, 1994

1L31

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

1L19

ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
Descriptor:	T4 LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature, 336, 1988

1L22

CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. J.Mol.Biol., 210, 1989

1L23

ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
Descriptor:	T4 LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc.Natl.Acad.Sci.USA, 84, 1987

1L20

ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
Descriptor:	T4 LYSOZYME
Authors:	Nicholson, H, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.85 Å)
Cite:	Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature, 336, 1988

1L29

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

1L27

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Descriptor:	T4 LYSOZYME
Authors:	Bell, J.A, Dao-Pin, S, Matthews, B.W.
Deposit date:	1989-05-01
Release date:	1990-01-15
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science, 239, 1988

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

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

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

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

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

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