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6XF8
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BU of 6xf8 by Molmil
DLP 5 fold
Descriptor: Inner capsid protein lambda-1, Inner capsid protein sigma-2, Outer capsid protein mu-1, ...
Authors:Sutton, G, Sun, D.P, Fu, X.F, Kotecha, A, Hecksel, G.W, Clare, D.K, Zhang, P, Stuart, D, Boyce, M.
Deposit date:2020-06-15
Release date:2020-09-23
Method:ELECTRON MICROSCOPY (6.5 Å)
Cite:Assembly intermediates of orthoreovirus captured in the cell.
Nat Commun, 11, 2020
1L44
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BU of 1l44 by Molmil
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
1L40
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BU of 1l40 by Molmil
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:2024-05-22
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
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BU of 1l47 by Molmil
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
1L38
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BU of 1l38 by Molmil
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:2024-05-22
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
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BU of 1l45 by Molmil
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
1L41
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BU of 1l41 by Molmil
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:2024-05-22
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L37
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BU of 1l37 by Molmil
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:2024-05-22
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
1L43
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BU of 1l43 by Molmil
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
1L39
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BU of 1l39 by Molmil
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:2024-05-22
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
1L46
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BU of 1l46 by Molmil
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
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BU of 1l42 by Molmil
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
3LZM
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BU of 3lzm by Molmil
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
1QUG
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BU of 1qug by Molmil
E108V MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, PROTEIN (LYSOZYME)
Authors:Wray, J, Baase, W.A, Lindstrom, J.D, Poteete, A.R, Matthews, B.W.
Deposit date:1999-07-01
Release date:1999-07-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.
J.Mol.Biol., 292, 1999
1L02
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BU of 1l02 by Molmil
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
1L09
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BU of 1l09 by Molmil
CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Descriptor: T4 LYSOZYME
Authors:Dao-Pin, S, Bell, J, 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
1L26
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BU of 1l26 by Molmil
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
1L06
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BU of 1l06 by Molmil
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
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BU of 1l15 by Molmil
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
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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
1L13
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BU of 1l13 by Molmil
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
1L12
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BU of 1l12 by Molmil
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
1L03
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BU of 1l03 by Molmil
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
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

 

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