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Yorodumi- PDB-3gui: T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3gui | ||||||
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Title | T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--Apo structure | ||||||
Components | Lysozyme | ||||||
Keywords | HYDROLASE / T4 lysozyme / apolar cavity / buried charge / ligand binding / Antimicrobial / Bacteriolytic enzyme / Glycosidase | ||||||
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 / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å | ||||||
Authors | Liu, L. / Matthews, B.W. | ||||||
Citation | Journal: Biochemistry / Year: 2009 Title: Use of stabilizing mutations to engineer a charged group within a ligand-binding hydrophobic cavity in T4 lysozyme. Authors: Liu, L. / Baase, W.A. / Michael, M.M. / Matthews, B.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3gui.cif.gz | 55.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3gui.ent.gz | 38.7 KB | Display | PDB format |
PDBx/mmJSON format | 3gui.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gu/3gui ftp://data.pdbj.org/pub/pdb/validation_reports/gu/3gui | HTTPS FTP |
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-Related structure data
Related structure data | 3gujC 3gukC 3gulC 3gumC 3gunC 3guoC 3gupC 3dmvS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 18785.688 Da / Num. of mol.: 1 / Mutation: T21C/S38D/L99A/M102E/E108V/S117V/T142C/N144D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage T4 (virus) / Gene: E / Plasmid: p1403 / Production host: Escherichia coli (E. coli) / Strain (production host): RR1 / References: UniProt: P00720, lysozyme |
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-Non-polymers , 5 types, 210 molecules
#2: Chemical | ChemComp-BME / |
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#3: Chemical | ChemComp-CO3 / |
#4: Chemical | ChemComp-TAM / |
#5: Chemical | ChemComp-SO4 / |
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.52 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8 Details: 30% PEG 8000, 0.20M ammonium sulfate, 0.10M Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 7, 2007 / Details: Double crystal Si(111) |
Radiation | Monochromator: KOHZU / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.45→45.6 Å / Num. obs: 28430 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 6.7 % / Rmerge(I) obs: 0.036 / Net I/σ(I): 42 |
Reflection shell | Resolution: 1.45→1.5 Å / Redundancy: 6.6 % / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 6.3 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3DMV Resolution: 1.45→38.84 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.959 / SU B: 2.495 / SU ML: 0.045 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.076 / ESU R Free: 0.074 / Stereochemistry target values: Engh & Huber
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.335 Å2
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Refinement step | Cycle: LAST / Resolution: 1.45→38.84 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.45→1.488 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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