+Open data
-Basic information
Entry | Database: PDB / ID: 5gu0 | ||||||
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Title | Crystal structure of Au.CL-apo-E45C/R52C-rHLFr | ||||||
Components | Ferritin light chain | ||||||
Keywords | METAL BINDING PROTEIN / IRON STORAGE | ||||||
Function / homology | Function and homology information : / 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 / MAD / Resolution: 1.95 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 | 5gu0.cif.gz | 52.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5gu0.ent.gz | 38.1 KB | Display | PDB format |
PDBx/mmJSON format | 5gu0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5gu0_validation.pdf.gz | 451.8 KB | Display | wwPDB validaton report |
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Full document | 5gu0_full_validation.pdf.gz | 452.3 KB | Display | |
Data in XML | 5gu0_validation.xml.gz | 9.6 KB | Display | |
Data in CIF | 5gu0_validation.cif.gz | 12.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gu/5gu0 ftp://data.pdbj.org/pub/pdb/validation_reports/gu/5gu0 | HTTPS FTP |
-Related 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, 92 molecules
#2: Chemical | ChemComp-AU / #3: Chemical | #4: Chemical | #5: Chemical | #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: 60.52 % |
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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: BL38B1 / Wavelength: 1.03586, 1.05777 | |||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 24, 2014 | |||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.95→40 Å / Num. obs: 19055 / % possible obs: 99.9 % / Redundancy: 11 % / Net I/σ(I): 65.7 | |||||||||
Reflection shell | Redundancy: 11.3 % / Mean I/σ(I) obs: 12.8 / % possible all: 100 |
-Processing
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Refinement | Method to determine structure: MAD / Resolution: 1.95→31.98 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.948 / SU B: 2.49 / SU ML: 0.072 / Cross valid method: THROUGHOUT / ESU R: 0.122 / ESU R Free: 0.116 / 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: 29.491 Å2
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Refinement step | Cycle: 1 / Resolution: 1.95→31.98 Å
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Refine LS restraints |
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