+
Open data
-
Basic information
Entry | Database: PDB / ID: 3fi5 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal Structure of T4 Lysozyme Mutant R96W | ||||||
![]() | Lysozyme | ||||||
![]() | HYDROLASE / Antimicrobial / Bacteriolytic enzyme / Glycosidase / T4 lysozyme / electrostatics / strain / protein stability | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Mooers, B.H.M. / Matthews, B.W. | ||||||
![]() | ![]() Title: Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. Authors: Mooers, B.H. / Baase, W.A. / Wray, J.W. / Matthews, B.W. #1: ![]() Title: Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His. Authors: Mooers, B.H. / Tronrud, D.E. / Matthews, B.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 305.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 246.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 470.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 484.5 KB | Display | |
Data in XML | ![]() | 38.6 KB | Display | |
Data in CIF | ![]() | 58.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3c7wC ![]() 3c7yC ![]() 3c7zC ![]() 3c80C ![]() 3c81C ![]() 3c82C ![]() 3c83C ![]() 3c8qC ![]() 3c8rC ![]() 3c8sC ![]() 3cdoC ![]() 3cdqC ![]() 3cdrC ![]() 3cdtC ![]() 3cdvC ![]() 1lw9S C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
4 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 18691.482 Da / Num. of mol.: 4 / Mutation: R96W Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-CL / #3: Chemical | #4: Chemical | ChemComp-IPA / | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.66 % |
---|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: May 29, 1999 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.53→18.804 Å / Num. all: 101134 / Num. obs: 92759 / % possible obs: 70.2 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Biso Wilson estimate: 12.42 Å2 / Rmerge(I) obs: 0.038 / Rsym value: 0.038 / Net I/σ(I): 19.96 |
Reflection shell | Resolution: 1.53→1.57 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.195 / Mean I/σ(I) obs: 5.15 / Num. unique all: 3111 / Rsym value: 0.195 / % possible all: 41.4 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 1LW9 Resolution: 1.53→18.804 Å / SU ML: 0.22 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Stereochemistry target values: ML
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 80.343 Å2 / ksol: 0.408 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.53→18.804 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 17
|