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1DN9	STRUCTURE OF AN ALTERNATING-B DNA HELIX AND ITS RELATIONSHIP TO A-TRACT DNA Descriptor: DNA (5'-D(*CP*GP*CP*AP*TP*AP*TP*AP*TP*GP*CP*G)-3') Authors: Yoon, C, Dickerson, R.E. Deposit date: 1989-04-25 Release date: 1990-04-15 Last modified: 2024-02-07 Method: X-RAY DIFFRACTION (2.2 Å) Cite: Structure of an alternating-B DNA helix and its relationship to A-tract DNA. Proc.Natl.Acad.Sci.USA, 85, 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
3LZM	STRUCTURAL STUDIES OF MUTANTS OF T4 LYSOZYME THAT ALTER HYDROPHOBIC STABILIZATION Descriptor: T4 LYSOZYME Authors: Wilson, K, Faber, R, 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: Structural studies of mutants of T4 lysozyme that alter hydrophobic stabilization. J.Biol.Chem., 264, 1989
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
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
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
1L17	HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3 Descriptor: T4 LYSOZYME Authors: Matsumura, M, 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: Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature, 334, 1988
1L18	HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3 Descriptor: T4 LYSOZYME Authors: Matsumura, M, 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: Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature, 334, 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
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
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
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
1L26	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
3MCG	THREE-DIMENSIONAL STRUCTURE OF A LIGHT CHAIN DIMER CRYSTALLIZED IN WATER. CONFORMATIONAL FLEXIBILITY OF A MOLECULE IN TWO CRYSTAL FORMS Descriptor: IMMUNOGLOBULIN LAMBDA DIMER MCG (LIGHT CHAIN) Authors: Ely, K.R, Herron, J.N, Edmundson, A.B. Deposit date: 1989-05-09 Release date: 1990-10-15 Last modified: 2019-12-25 Method: X-RAY DIFFRACTION (2 Å) Cite: Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms. J.Mol.Biol., 210, 1989
1MCW	THREE-DIMENSIONAL STRUCTURE OF A HYBRID LIGHT CHAIN DIMER. PROTEIN ENGINEERING OF A BINDING CAVITY Descriptor: IMMUNOGLOBULIN MCG (LIGHT CHAIN), IMMUNOGLOBULIN WEIR (LIGHT CHAIN) Authors: Ely, K.R, Herron, J.N, Edmundson, A.B. Deposit date: 1989-05-09 Release date: 1990-10-15 Last modified: 2024-10-16 Method: X-RAY DIFFRACTION (3.5 Å) Cite: Three-dimensional structure of a hybrid light chain dimer: protein engineering of a binding cavity. Mol.Immunol., 27, 1990
2MCG	THREE-DIMENSIONAL STRUCTURE OF A LIGHT CHAIN DIMER CRYSTALLIZED IN WATER. CONFORMATIONAL FLEXIBILITY OF A MOLECULE IN TWO CRYSTAL FORMS Descriptor: IMMUNOGLOBULIN LAMBDA DIMER MCG (LIGHT CHAIN) Authors: Ely, K.R, Herron, J.N, Edmundson, A.B. Deposit date: 1989-05-09 Release date: 1990-10-15 Last modified: 2019-12-25 Method: X-RAY DIFFRACTION (2 Å) Cite: Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms. J.Mol.Biol., 210, 1989
5EST	Crystallographic analysis of the inhibition of porcine pancreatic elastase by a peptidyl boronic acid: structure of a reaction intermediate Descriptor: CALCIUM ION, ELASTASE, N~2~-[(benzyloxy)carbonyl]-N-[(1R,2S)-1-(dihydroxyboranyl)-2-methylbutyl]-L-alaninamide, ... Authors: Takahashi, L.H, Radhakrishnan, R, Rosenfieldjunior, R.E, Meyerjunior, E.F. Deposit date: 1989-05-15 Release date: 1992-04-15 Last modified: 2024-10-16 Method: X-RAY DIFFRACTION (2.09 Å) Cite: Crystallographic analysis of the inhibition of porcine pancreatic elastase by a peptidyl boronic acid: structure of a reaction intermediate. Biochemistry, 28, 1989
4EST	CRYSTAL STRUCTURE OF THE COVALENT COMPLEX FORMED BY A PEPTIDYL ALPHA,ALPHA-DIFLUORO-BETA-KETO AMIDE WITH PORCINE PANCREATIC ELASTASE AT 1.78-ANGSTROMS RESOLUTION Descriptor: CALCIUM ION, ELASTASE, INHIBITOR ACE-ALA-PRO-VAI-DIFLUORO-N-PHENYLETHYLACETAMIDE, ... Authors: Takahashi, L.H, Radhakrishnan, R, Rosenfieldjunior, R.E, Meyerjunior, E.F, Trainor, D.A. Deposit date: 1989-05-15 Release date: 1992-04-15 Last modified: 2024-10-09 Method: X-RAY DIFFRACTION (1.78 Å) Cite: Crystal Structure of the Covalent Complex Formed by a Peptidyl Alpha,Alpha-Difluoro-Beta-Keto Amide with Porcine Pancreatic Elastase at 1.78-Angstroms Resolution J.Am.Chem.Soc., 111, 1989

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