+Open data
-Basic information
Entry | Database: PDB / ID: 1zyt | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of spin labeled T4 Lysozyme (A82R1) | ||||||
Components | Lysozyme | ||||||
Keywords | HYDROLASE / NITROXIDE SPIN LABEL / MODIFIED CYSTEINE | ||||||
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 / EPR / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Fleissner, M.R. / Cascio, D. / Sawaya, M.R. / Hideg, K. / Hubbell, W.L. | ||||||
Citation | Journal: Protein Sci. / Year: 2009 Title: Structural origin of weakly ordered nitroxide motion in spin-labeled proteins Authors: Fleissner, M.R. / Cascio, D. / Hubbell, W.L. #1: Journal: BIOCHEMISTRY / Year: 2000 Title: Crystal Structures of Spin Labeled T4 Lysozyme Mutants: Implications for the Interpretation of EPR Spectra in Terms of Structure Authors: Langen, R. / Oh, K.J. / Cascio, D. / Hubbell, W.L. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1zyt.cif.gz | 53 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1zyt.ent.gz | 36.9 KB | Display | PDB format |
PDBx/mmJSON format | 1zyt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1zyt_validation.pdf.gz | 673.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1zyt_full_validation.pdf.gz | 674.6 KB | Display | |
Data in XML | 1zyt_validation.xml.gz | 11.1 KB | Display | |
Data in CIF | 1zyt_validation.cif.gz | 16.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zy/1zyt ftp://data.pdbj.org/pub/pdb/validation_reports/zy/1zyt | HTTPS FTP |
-Related structure data
Related structure data | 2cuuC 3g3vC 3g3wC 3g3xC 1c6tS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 18660.428 Da / Num. of mol.: 1 / Mutation: C54T/C97A/A82C 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 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P00720, lysozyme |
---|
-Non-polymers , 5 types, 226 molecules
#2: Chemical | ChemComp-MTN / | ||||
---|---|---|---|---|---|
#3: Chemical | ChemComp-AZI / | ||||
#4: Chemical | #5: Chemical | ChemComp-HED / | #6: Water | ChemComp-HOH / | |
-Details
Has protein modification | Y |
---|
-Experimental details
-Experiment
Experiment |
|
---|
-Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 53.42 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.8 Details: potassium phosphate, sodium phospahte, sodium choloride, sodium azide, oxidized beta-mercaptoehtanol , pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-D / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Feb 23, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→80 Å / Num. all: 22885 / Num. obs: 22843 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.3 % / Biso Wilson estimate: 30.8 Å2 / Rsym value: 0.057 / Net I/σ(I): 41.2 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 8.7 % / Mean I/σ(I) obs: 5.98 / Num. unique all: 2244 / Rsym value: 0.314 / % possible all: 99.9 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1C6T Resolution: 1.7→52.2 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.939 / SU B: 1.725 / SU ML: 0.059 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.103 / ESU R Free: 0.096 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. WITH THE EXCEPTION OF C3, THE POSITIONS OF THE ATOMS OF THE NITROXIDE RING OF MTN ARE NOT UNIQUE, AS THOSE PARTICULAR ATOMS WERE NOT ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. WITH THE EXCEPTION OF C3, THE POSITIONS OF THE ATOMS OF THE NITROXIDE RING OF MTN ARE NOT UNIQUE, AS THOSE PARTICULAR ATOMS WERE NOT RESOLVED. THE COORDINATES FOR THOSE ATOMS OF THE NITROXIDE RING WERE DEPOSITED IN A MINIMUM ENERGY CONFIGURATION.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 18.839 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→52.2 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.7→1.744 Å / Total num. of bins used: 20
|