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PDB: 579 results

1T8F
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Crystal structure of phage T4 lysozyme mutant R14A/K16A/I17A/K19A/T21A/E22A/C54T/C97A
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, Lysozyme
Authors:He, M.M, Wood, Z.A, Baase, W.A, Xiao, H, Matthews, B.W.
Deposit date:2004-05-12
Release date:2004-10-19
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation.
Protein Sci., 13, 2004
1L35
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STRUCTURE OF A THERMOSTABLE DISULFIDE-BRIDGE MUTANT OF PHAGE T4 LYSOZYME SHOWS THAT AN ENGINEERED CROSSLINK IN A FLEXIBLE REGION DOES NOT INCREASE THE RIGIDITY OF THE FOLDED PROTEIN
Descriptor: T4 LYSOZYME
Authors:Pjura, P.E, Matsumura, M, Wozniak, J.A, Matthews, B.W.
Deposit date:1989-10-26
Release date:1990-01-15
Last modified:2024-10-30
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.
Biochemistry, 29, 1990
1SX7
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Use of an ion-binding site to bypass the 1000-atom limit to ab initio structure determination by direct methods
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, Lysozyme, ...
Authors:Mooers, B.H.M, Matthews, B.W.
Deposit date:2004-03-30
Release date:2004-11-30
Last modified:2023-08-23
Method:X-RAY DIFFRACTION (1.06 Å)
Cite:Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods.
Acta Crystallogr.,Sect.D, 60, 2004
1SSY
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BU of 1ssy by Molmil
Crystal structure of phage T4 lysozyme mutant G28A/I29A/G30A/C54T/C97A
Descriptor: Lysozyme
Authors:He, M.M, Baase, W.A, Xiao, H, Heinz, D.W, Matthews, B.W.
Deposit date:2004-03-24
Release date:2004-10-19
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation
Protein Sci., 13, 2004
1SWZ
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BU of 1swz by Molmil
Use of an ion-binding site to bypass the 1000-atom limit to ab initio structure determination by direct methods
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, Lysozyme, ...
Authors:Mooers, B.H.M, Matthews, B.W.
Deposit date:2004-03-30
Release date:2005-01-18
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.06 Å)
Cite:Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods.
Acta Crystallogr.,Sect.D, 60, 2004
1YJ3
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BU of 1yj3 by Molmil
Crystal structure analysis of product bound methionine aminopeptidase Type 1c from Mycobacterium Tuberculosis
Descriptor: BETA-MERCAPTOETHANOL, COBALT (II) ION, METHIONINE, ...
Authors:Addlagatta, A, Quillin, M.L, Omotoso, O, Liu, J.O, Matthews, B.W.
Deposit date:2005-01-13
Release date:2005-07-05
Last modified:2023-08-23
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome.
Biochemistry, 44, 2005
1Y3G
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Crystal Structure of a Silanediol Protease Inhibitor Bound to Thermolysin
Descriptor: (2S)-2-{[(AMINOMETHYL)(DIHYDROXY)SILYL]METHYL}-4-METHYLPENTANAL, 3-PHENYLPROPANAL, CALCIUM ION, ...
Authors:Juers, D.H, Kim, J, Matthews, B.W, Sieburth, S.M.
Deposit date:2004-11-24
Release date:2006-01-17
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Structural Analysis of Silanediols as Transition-State-Analogue Inhibitors of the Benchmark Metalloprotease Thermolysin(,).
Biochemistry, 44, 2005
1L26
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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
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BU of 1l30 by Molmil
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
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BU of 1l21 by Molmil
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
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BU of 1l28 by Molmil
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
1L17
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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
1L33
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BU of 1l33 by Molmil
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
1L18
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BU of 1l18 by Molmil
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
1L32
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BU of 1l32 by Molmil
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
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BU of 1l24 by Molmil
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
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BU of 1l34 by Molmil
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
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BU of 1l25 by Molmil
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
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BU of 1l31 by Molmil
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
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BU of 1l19 by Molmil
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
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BU of 1l22 by Molmil
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
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BU of 1l23 by Molmil
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
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BU of 1l20 by Molmil
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
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BU of 1l29 by Molmil
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
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BU of 1l27 by Molmil
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

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