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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:	2024-05-22
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

1L42

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:	2024-05-22
Method:	X-RAY DIFFRACTION (1.8 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

1L59

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

7K45

SARS-CoV-2 spike in complex with the S2E12 neutralizing antibody Fab fragment (local refinement of the RBD and Fab variable domains)
Descriptor:	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, S2E12 neutralizing antibody Fab fragment (heavy chain), S2E12 neutralizing antibody Fab fragment (light chain), ...
Authors:	Tortorici, M.A, Veesler, D, Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Deposit date:	2020-09-14
Release date:	2020-10-07
Last modified:	2024-10-30
Method:	ELECTRON MICROSCOPY (3.7 Å)
Cite:	Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms. Science, 370, 2020

7K3Q

An ultra-potent human neutralizing antibody locks the SARS-CoV-2 spike in the closed conformation
Descriptor:	1,2-ETHANEDIOL, Fab fragment of S2E12 monoclonal antibody, heavy chain, ...
Authors:	Snell, G, Czudnochowski, N, Ng, C.
Deposit date:	2020-09-12
Release date:	2020-10-07
Last modified:	2024-10-23
Method:	X-RAY DIFFRACTION (1.38 Å)
Cite:	Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms. Science, 370, 2020

7K4N

SARS-CoV-2 spike in complex with the S2E12 neutralizing antibody Fab fragment
Descriptor:	2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, S2E12 neutralizing antibody Fab fragment (heavy chain), ...
Authors:	Tortorici, M, Veesler, D, Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Deposit date:	2020-09-15
Release date:	2020-10-07
Last modified:	2020-12-02
Method:	ELECTRON MICROSCOPY (3.3 Å)
Cite:	Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms. Science, 370, 2020

5LZM

COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:	Bell, J.A, Wilson, K, Zhang, X.-J, Faber, H.R, Nicholson, H, Matthews, B.W.
Deposit date:	1991-01-25
Release date:	1992-07-15
Last modified:	2021-06-30
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins, 10, 1991

7K43

SARS-CoV-2 spike in complex with the S2M11 neutralizing antibody Fab fragment
Descriptor:	2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, S2M11 Fab fragment (heavy chain), ...
Authors:	Tortorici, M.A, Veesler, D, Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Deposit date:	2020-09-14
Release date:	2020-10-07
Last modified:	2024-10-30
Method:	ELECTRON MICROSCOPY (2.6 Å)
Cite:	Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms. Science, 370, 2020

2LZM

STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME REFINED AT 1.7 ANGSTROMS RESOLUTION
Descriptor:	T4 LYSOZYME
Authors:	Weaver, L.H, Matthews, B.W.
Deposit date:	1986-08-18
Release date:	1986-10-24
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. J.Mol.Biol., 193, 1987

7UFV

Crystal structure of the WDR domain of human DCAF1 in complex with OICR-6766
Descriptor:	(3P)-N-[(1S)-3-amino-1-(3-chlorophenyl)-3-oxopropyl]-3-(2-fluorophenyl)-1H-pyrazole-4-carboxamide, DDB1- and CUL4-associated factor 1, UNKNOWN ATOM OR ION
Authors:	Kimani, S, Li, A, Li, Y, Dong, A, Hutchinson, A, Seitova, A, Wilson, B, Al-Awar, R, Vedadi, M, Brown, P, Arrowsmith, C.H, Edwards, A.M, Halabelian, L, Structural Genomics Consortium (SGC)
Deposit date:	2022-03-23
Release date:	2022-05-04
Last modified:	2024-04-03
Method:	X-RAY DIFFRACTION (1.9 Å)
Cite:	Discovery of Nanomolar DCAF1 Small Molecule Ligands. J.Med.Chem., 66, 2023

6LZM

COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS
Descriptor:	BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:	Bell, J.A, Wilson, K, Zhang, X.-J, Faber, H.R, Nicholson, H, Matthews, B.W.
Deposit date:	1991-01-25
Release date:	1992-07-15
Last modified:	2021-06-30
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins, 10, 1991

1L06

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Wilson, K, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

1L15

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

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

1L05

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 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

1L66

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 (1.7 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

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

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

1L13

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

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

1L03

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	BETA-MERCAPTOETHANOL, T4 LYSOZYME
Authors:	Dao-Pin, S, Wilson, K, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2022-11-23
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

1L12

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor:	T4 LYSOZYME
Authors:	Dao-Pin, S, Alber, T, Matthews, B.W.
Deposit date:	1988-02-05
Release date:	1988-04-16
Last modified:	2024-05-22
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330, 1987

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