+Open data
-Basic information
Entry | Database: PDB / ID: 5gu2 | ||||||
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Title | Crystal structure of Au(M).CL-apo-E45C/R52C-rHLFr | ||||||
Components | Ferritin light chain | ||||||
Keywords | METAL BINDING PROTEIN / IRON STORAGE | ||||||
Function / homology | Function and homology information intracellular ferritin complex / intracellular sequestering of iron ion / ferric iron binding / ferrous iron binding / iron ion transport / iron ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Equus caballus (horse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.12 Å | ||||||
Authors | Maity, B. / Abe, S. / Ueno, T. | ||||||
Citation | Journal: Nat Commun / Year: 2017 Title: Observation of gold sub-nanocluster nucleation within a crystalline protein cage Authors: Maity, B. / Abe, S. / Ueno, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5gu2.cif.gz | 52.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5gu2.ent.gz | 37.4 KB | Display | PDB format |
PDBx/mmJSON format | 5gu2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gu/5gu2 ftp://data.pdbj.org/pub/pdb/validation_reports/gu/5gu2 | HTTPS FTP |
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-Related structure data
Related structure data | 5gu0C 5gu1C 5gu3C 1datS 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 X
#1: Protein | Mass: 19792.406 Da / Num. of mol.: 1 / Mutation: E45C,R52C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Equus caballus (horse) / Gene: FTL / Production host: Escherichia coli (E. coli) / References: UniProt: P02791 |
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-Non-polymers , 5 types, 66 molecules
#2: Chemical | ChemComp-AU / #3: Chemical | ChemComp-CD / #4: Chemical | #5: Chemical | ChemComp-EDO / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 60.64 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: Ammonium Sulphate, Cadmium Sulphate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B1 / Wavelength: 1.03895 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: May 12, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.03895 Å / Relative weight: 1 |
Reflection | Resolution: 2.12→30 Å / Num. obs: 14946 / % possible obs: 99.9 % / Redundancy: 11.5 % / Net I/σ(I): 60.7 |
Reflection shell | Redundancy: 11.5 % / Mean I/σ(I) obs: 11.1 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1DAT Resolution: 2.12→25.36 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.929 / SU B: 3.715 / SU ML: 0.1 / Cross valid method: THROUGHOUT / ESU R: 0.165 / ESU R Free: 0.157 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.172 Å2
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Refinement step | Cycle: LAST / Resolution: 2.12→25.36 Å
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Refine LS restraints |
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