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Open data
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Basic information
Entry | Database: PDB / ID: 1h96 | ||||||
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Title | recombinant mouse L-chain ferritin | ||||||
![]() | FERRITIN LIGHT CHAIN 1 | ||||||
![]() | IRON STORAGE | ||||||
Function / homology | ![]() : / autolysosome / intracellular sequestering of iron ion / endocytic vesicle lumen / ferric iron binding / ferrous iron binding / iron ion transport / iron ion binding / extracellular region / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Granier, T. / Gallois, B. / D'Estaintot, B.L. / Dautant, A. / Chevalier, J.M. / Mellado, J.M. / Beaumont, C. / Santambrogio, P. / Arosio, P. / Precigoux, G. | ||||||
![]() | ![]() Title: Structure of Mouse L-Chain Ferritin at 1.6 A Resolution Authors: Granier, T. / Gallois, B. / D'Estaintot, B.L. / Dautant, A. / Chevalier, J.M. / Mellado, J.M. / Beaumont, C. / Santambrogio, P. / Arosio, P. / Precigoux, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 59 KB | Display | ![]() |
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PDB format | ![]() | 42.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.8 KB | Display | ![]() |
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Full document | ![]() | 429.9 KB | Display | |
Data in XML | ![]() | 11.9 KB | Display | |
Data in CIF | ![]() | 17.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1datS S: Starting model for refinement |
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Similar structure data |
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Links
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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
#1: Protein | Mass: 20670.164 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: FOR DETAILS SEE BEAUMONT, C., DUGAST, I., RENAUDIE, F., SOUROUJON, M., GRANDCHAMP, B. J. BIOL. CHEM., 1989, VOL. 264, 13, PP 7498-7504 Organ: LIVER / Production host: ![]() ![]() | ||||||
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#2: Chemical | ChemComp-CD / #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | Compound details | CHAIN A ENGINEERED | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.3 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.4 Details: HANGING DROP VAPOR DIFFUSION: DROPS MADE UP OF 3MICROL OF PROTEIN (3.5 MG/ML) IN 20 MM TRIS PH 7.4 AND 3 MICROL OF PRECIPITANT SOLUTION COMPOSED OF 0.92 M AMMONIUM SULFATE, 0.4% CDSO4 AND 3 MM NAN3 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 15, 1999 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→20 Å / Num. obs: 32400 / % possible obs: 95.7 % / Redundancy: 4.9 % / Biso Wilson estimate: 11.83 Å2 / Rsym value: 0.071 / Net I/σ(I): 9.3 |
Reflection shell | Resolution: 1.6→1.64 Å / Redundancy: 4.4 % / Mean I/σ(I) obs: 1.9 / Rsym value: 0.38 / % possible all: 83.8 |
Reflection | *PLUS Num. obs: 32292 / Num. measured all: 158991 / Rmerge(I) obs: 0.071 |
Reflection shell | *PLUS % possible obs: 83.8 % / Num. unique obs: 2042 / Num. measured obs: 8894 / Rmerge(I) obs: 0.38 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1DAT Resolution: 1.6→14 Å / SU B: 1.2 / SU ML: 0.041 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.071 / ESU R Free: 0.075 Details: THE C-TERMINAL RESIDUE WAS NOT SEEN IN THE DENSITY MAP
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Displacement parameters | Biso mean: 13 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→14 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 19 Å / Rfactor obs: 0.16 / Rfactor Rfree: 0.19 / Rfactor Rwork: 0.16 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 1.64 Å / Rfactor Rfree: 0.27 / Rfactor obs: 0.22 |