+
Open data
-
Basic information
Entry | Database: PDB / ID: 1qtv | ||||||
---|---|---|---|---|---|---|---|
Title | T26E APO STRUCTURE OF T4 LYSOZYME | ||||||
![]() | PROTEIN (T4 LYSOZYME) | ||||||
![]() | ![]() | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kuroki, R. / Weaver, L.H. / Matthews, B.W. | ||||||
![]() | ![]() Title: Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site. Authors: Kuroki, R. / Weaver, L.H. / Matthews, B.W. #1: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 A Resolution Authors: Weaver, L.H. / Matthews, B.W. #2: ![]() Title: Structure-based Design of a Lysozyme with Altered Catalytic Activity Authors: Kuroki, R. / Weaver, L.H. / Matthews, B.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 44.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 31.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 1qt3C ![]() 1qt4C ![]() 1qt5C ![]() 1qt6C ![]() 1qt7C ![]() 1qt8C ![]() 1qtzC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 18656.373 Da / Num. of mol.: 1 / Mutation: T26E, C54T, C97A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() | ||||
---|---|---|---|---|---|
#2: Chemical | ![]() #3: Chemical | ChemComp-BME / | ![]() #4: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.95 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow![]() | *PLUS 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 | Mean temperature: 75 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Mar 29, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.3→20 Å / Num. all: 9715 / Num. obs: 9358 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 7.2 |
Reflection shell | Resolution: 2.3→2.48 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.223 / Num. unique all: 1740 / % possible all: 92 |
Reflection | *PLUS Num. measured all: 30082 / Rmerge(I) obs: 0.07 |
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.3→19 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT
| ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→19 Å
| ||||||||||||
Refine LS restraints |
| ||||||||||||
Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / σ(F): 0 / Rfactor all![]() | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
|