+Open data
-Basic information
Entry | Database: PDB / ID: 1l0k | ||||||
---|---|---|---|---|---|---|---|
Title | METHIONINE CORE MUTANT OF T4 LYSOZYME | ||||||
Components | LYSOZYME | ||||||
Keywords | HYDROLASE / hydrolase (o-glycosyl) / T4 lysozyme / methionine core mutant / protein engineering / protein folding | ||||||
Function / homology | Function and homology information 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 | Enterobacteria phage T4 (virus) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.02 Å | ||||||
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. | ||||||
Citation | Journal: BIOPHYS.CHEM. / Year: 2003 Title: Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability 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. #1: Journal: Biochemistry / Year: 1999 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. / Lu, J. / Dahlquist, F.W. / Matthews, B.W. #2: Journal: Biochemistry / Year: 1987 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: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1l0k.cif.gz | 47.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1l0k.ent.gz | 33.6 KB | Display | PDB format |
PDBx/mmJSON format | 1l0k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1l0k_validation.pdf.gz | 428.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1l0k_full_validation.pdf.gz | 433.5 KB | Display | |
Data in XML | 1l0k_validation.xml.gz | 10.5 KB | Display | |
Data in CIF | 1l0k_validation.cif.gz | 14.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l0/1l0k ftp://data.pdbj.org/pub/pdb/validation_reports/l0/1l0k | HTTPS FTP |
-Related structure data
Related structure data | 1ks3C 1kw5C 1kw7C 1ky0C 1ky1C 1l0jC 1lpyC 1lw9C 1lwgC 1lwkC C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 18541.395 Da / Num. of mol.: 1 / Mutation: C54T,L84M,L91M,C97A,L99M,V111M,L118M,L121M,L133M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage T4 (virus) / Genus: T4-like viruses / Species: Enterobacteria phage T4 sensu lato / Gene: gene E / Plasmid: phs1403 / Production host: Escherichia coli (E. coli) / Strain (production host): RR1 / References: UniProt: P00720, lysozyme | ||||
---|---|---|---|---|---|
#2: Chemical | #3: Chemical | ChemComp-HED / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 56.42 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.9 Details: Na2PO4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 298 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Detector: AREA DETECTOR |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.02→30 Å / Num. all: 14356 / Num. obs: 14356 / % possible obs: 90.4 % / Redundancy: 2.8 % / Biso Wilson estimate: 28.9 Å2 / Rmerge(I) obs: 0.055 / Net I/σ(I): 9.6 |
Reflection shell | Resolution: 1.78→1.86 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.267 / Num. unique all: 2587 / % possible all: 63.5 |
-Processing
Software |
| ||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.02→30 Å / Stereochemistry target values: TNT PROTGEO /
| ||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.02→30 Å
|