Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help
PDB: 30 results

1QSQ
DownloadVisualize
BU of 1qsq by Molmil
CAVITY CREATING MUTATION
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J, Matthews, B.W.
Deposit date:1999-06-22
Release date:1999-06-29
Last modified:2024-02-14
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
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
1CU6
DownloadVisualize
BU of 1cu6 by Molmil
T4 LYSOZYME MUTANT L91A
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:1999-11-17
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
1CU0
DownloadVisualize
BU of 1cu0 by Molmil
T4 LYSOZYME MUTANT I78M
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 (2.2 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
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
1CVK
DownloadVisualize
BU of 1cvk by Molmil
T4 LYSOZYME MUTANT L118A
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W.
Deposit date:1999-08-23
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 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
1CV1
DownloadVisualize
BU of 1cv1 by Molmil
T4 LYSOZYME MUTANT V111M
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
1CV5
DownloadVisualize
BU of 1cv5 by Molmil
T4 LYSOZYME MUTANT L133M
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 (1.87 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
1CV3
DownloadVisualize
BU of 1cv3 by Molmil
T4 LYSOZYME MUTANT L121M
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:1999-08-24
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 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
1CX7
DownloadVisualize
BU of 1cx7 by Molmil
T4 LYSOZYME METHIONINE CORE MUTANT
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W.
Deposit date:1999-08-28
Release date:1999-11-10
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.94 Å)
Cite:Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
1KW7
DownloadVisualize
BU of 1kw7 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-01-28
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.89 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1KS3
DownloadVisualize
BU of 1ks3 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-01-10
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.16 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1KW5
DownloadVisualize
BU of 1kw5 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-01-28
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
1D2Y
DownloadVisualize
BU of 1d2y by Molmil
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Matthews, B.W.
Deposit date:1999-09-28
Release date:1999-10-08
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.06 Å)
Cite:Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
1D2W
DownloadVisualize
BU of 1d2w by Molmil
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Matthews, B.W.
Deposit date:1999-09-28
Release date:1999-10-08
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.89 Å)
Cite:Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
1D3J
DownloadVisualize
BU of 1d3j by Molmil
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Matthews, B.W.
Deposit date:1999-09-29
Release date:1999-10-08
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.97 Å)
Cite:Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
1D3N
DownloadVisualize
BU of 1d3n by Molmil
METHIONINE CORE MUTATION
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Matthews, B.W.
Deposit date:1999-09-29
Release date:1999-09-30
Last modified:2024-10-30
Method:X-RAY DIFFRACTION (2 Å)
Cite:Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
1KY0
DownloadVisualize
BU of 1ky0 by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W.
Deposit date:2002-02-01
Release date:2003-06-03
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.97 Å)
Cite:Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003

 

12>

227111

数据于2024-11-06公开中

PDB statisticsPDBj update infoContact PDBjnumon