+Open data
-Basic information
Entry | Database: PDB / ID: 2za6 | ||||||
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Title | recombinant horse L-chain apoferritin | ||||||
Components | Ferritin light chain | ||||||
Keywords | METAL BINDING PROTEIN / ferric iron binding / Acetylation / Iron storage / Metal-binding | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | ||||||
Authors | Yamashita, I. / Mishima, Y. / Park, S.-Y. / Heddle, J.G. / Tame, J.R.H. | ||||||
Citation | Journal: J.BIOCHEM.(TOKYO) / Year: 2007 Title: Effect of N-terminal Residues on the Structural Stability of Recombinant Horse L-chain Apoferritin in an Acidic Environment Authors: Yoshizawa, K. / Mishima, Y. / Park, S.-Y. / Heddle, J.G. / Tame, J.R.H. / Iwahori, K. / Kobayashi, M. / Yamashita, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2za6.cif.gz | 52.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2za6.ent.gz | 38.1 KB | Display | PDB format |
PDBx/mmJSON format | 2za6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2za6_validation.pdf.gz | 358.4 KB | Display | wwPDB validaton report |
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Full document | 2za6_full_validation.pdf.gz | 358.5 KB | Display | |
Data in XML | 2za6_validation.xml.gz | 4.6 KB | Display | |
Data in CIF | 2za6_validation.cif.gz | 7.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/za/2za6 ftp://data.pdbj.org/pub/pdb/validation_reports/za/2za6 | HTTPS FTP |
-Related structure data
Related structure data | 2za7C 2za8C 1aewS 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
#1: Protein | Mass: 19987.580 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Equus caballus (horse) / Plasmid: PMK2 / Production host: Escherichia coli (E. coli) / References: UniProt: P02791 | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | SEE REF. 2 IN THE DATABASE, P02791 IN UNP. | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.06 Å3/Da / Density % sol: 59.83 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.1M Tris-HCl, 0.13% cadmium chloride, 15% PEG4000, 19 mM calcium chloride, 5% glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44B2 / Wavelength: 0.9 Å |
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Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Oct 20, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→99 Å / Num. obs: 25894 / % possible obs: 99.7 % / Biso Wilson estimate: 9.8 Å2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1AEW Resolution: 1.75→19.8 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.909 / SU B: 1.711 / SU ML: 0.057 / Cross valid method: THROUGHOUT / ESU R: 0.101 / ESU R Free: 0.101 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.703 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→19.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.75→1.795 Å / Total num. of bins used: 20 /
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