+
Open data
-
Basic information
Entry | Database: PDB / ID: 1qsq | ||||||
---|---|---|---|---|---|---|---|
Title | CAVITY CREATING MUTATION | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / HYDROLASE (O-GLYCOSYL) / T4 LYSOZYME / CAVITY MUTANT / PROTEIN ENGINEERING / PROTEIN FOLDING | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / host cell cytoplasm / defense response to bacterium Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Gassner, N.C. / Baase, W.A. / Lindstrom, J. / Matthews, B.W. | ||||||
![]() | ![]() Title: 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. Authors: Gassner, N.C. / Baase, W.A. / Lindstrom, J.D. / Lu, J. / Dahlquist, F.W. / Matthews, B.W. #1: ![]() Title: The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect Authors: Xu, J. / Baase, W.A. / Baldwin, E.P. / Matthews, B.W. #2: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 A Resolution Authors: Weaver, L.H. / Matthews, B.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 47.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 33.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.2 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 424.4 KB | Display | |
Data in XML | ![]() | 10 KB | Display | |
Data in CIF | ![]() | 13.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ctwC ![]() 1cu0C ![]() 1cu2C ![]() 1cu3C ![]() 1cu5C ![]() 1cu6C ![]() 1cupC ![]() 1cuqC ![]() 1cv0C ![]() 1cv1C ![]() 1cv3C ![]() 1cv4C ![]() 1cv5C ![]() 1cv6C ![]() 1cvkC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | The biological assembly is a monomer. |
-
Components
#1: Protein | Mass: 18568.244 Da / Num. of mol.: 1 / Mutation: C54T, C97A, M106A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
---|---|---|---|---|---|
#2: Chemical | #3: Chemical | ChemComp-HED / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.78 % | ||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.6 Details: NA2PO4, NACL, pH 6.6, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.7 / Method: vapor diffusion / Details: Eriksson, A.E., (1993) J.Mol.Biol., 229, 747. / PH range low: 7.1 / PH range high: 6.3 | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source |
| ||||||||||||
Detector |
| ||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 | ||||||||||||
Reflection | Resolution: 1.85→10 Å / Num. all: 11951 / Num. obs: 11951 / % possible obs: 64 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Biso Wilson estimate: 18.9 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 10 | ||||||||||||
Reflection shell | Resolution: 1.85→1.9 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.258 / Num. unique all: 59 / % possible all: 67 | ||||||||||||
Reflection shell | *PLUS % possible obs: 67 % |
-
Processing
Software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.9→10 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT PROTGEO
| |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
| |||||||||||||||
Refine LS restraints |
|