Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help
PDB: 36 results

1CV4
DownloadVisualize
BU of 1cv4 by Molmil
T4 LYSOZYME MUTANT L118M
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W.
Deposit date:1999-08-22
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1CU2
DownloadVisualize
BU of 1cu2 by Molmil
T4 LYSOZYME MUTANT L84M
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
Deposit date:1999-08-20
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1CUQ
DownloadVisualize
BU of 1cuq by Molmil
T4 LYSOZYME MUTANT V103M
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
Deposit date:1999-08-20
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.05 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1CV0
DownloadVisualize
BU of 1cv0 by Molmil
T4 LYSOZYME MUTANT F104M
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
Deposit date:1999-08-20
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.12 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1CU5
DownloadVisualize
BU of 1cu5 by Molmil
T4 LYSOZYME MUTANT L91M
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
Deposit date:1999-08-20
Release date:1999-11-10
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.05 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1CV6
DownloadVisualize
BU of 1cv6 by Molmil
T4 LYSOZYME MUTANT V149M
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W.
Deposit date:1999-08-22
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1CU3
DownloadVisualize
BU of 1cu3 by Molmil
T4 LYSOZYME MUTANT V87M
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
Deposit date:1999-08-20
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.12 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1CUP
DownloadVisualize
BU of 1cup by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
Deposit date:1999-08-20
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.89 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
1CX6
DownloadVisualize
BU of 1cx6 by Molmil
T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Matthews, B.W.
Deposit date:1999-08-28
Release date:1999-12-15
Last modified:2024-10-30
Method:X-RAY DIFFRACTION (2.01 Å)
Cite:Substitution with selenomethionine can enhance the stability of methionine-rich proteins.
J.Mol.Biol., 294, 1999
1CTW
DownloadVisualize
BU of 1ctw by Molmil
T4 LYSOZYME MUTANT I78A
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W.
Deposit date:1999-08-20
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38, 1999
230L
DownloadVisualize
BU of 230l by Molmil
T4 LYSOZYME MUTANT M6L
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Lipscomb, L.A, Gassner, N.C, Snow, S, Eldridge, A.M, Drew, D.L, Baase, W.A, Matthews, B.W.
Deposit date:1997-10-02
Release date:1998-01-14
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme.
Protein Sci., 7, 1998
<12

 

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon