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Open data
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Basic information
Entry | Database: PDB / ID: 4zgu | ||||||
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Title | Crystal structure of monomer Y60W hCRBPII | ||||||
![]() | Retinol-binding protein 2 | ||||||
![]() | TRANSPORT PROTEIN / 3D domain Swapping human CRBPII protein dimerization | ||||||
Function / homology | ![]() vitamin A metabolic process / retinoid binding / retinal binding / retinol binding / epidermis development / fatty acid transport / Retinoid metabolism and transport / fatty acid binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Nossoni, Z. / Geiger, J. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates. Authors: Assar, Z. / Nossoni, Z. / Wang, W. / Santos, E.M. / Kramer, K. / McCornack, C. / Vasileiou, C. / Borhan, B. / Geiger, J.H. #1: ![]() Title: Structures of holo wild-type human cellular retinol-binding protein II (hCRBPII) bound to retinol and retinal Authors: Nossoni, Z. / Assar, Z. / Nosrati, M. / Yapici, I. / Vasileiou, C. / Borhan, B. / Geiger, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 128.8 KB | Display | ![]() |
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PDB format | ![]() | 99.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 474.4 KB | Display | ![]() |
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Full document | ![]() | 491.1 KB | Display | |
Data in XML | ![]() | 28.4 KB | Display | |
Data in CIF | ![]() | 39.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4zcbC ![]() 4zh6C ![]() 4zh9C ![]() 4zj0C ![]() 4zr2C ![]() 5dg4C ![]() 5dpqC C: citing same article ( |
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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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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 15620.487 Da / Num. of mol.: 4 / Mutation: Y60W Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-ACT / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37.4 % |
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Crystal grow | Temperature: 294.15 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 30% PEG 4000, 0.1M CH3COONa.3H2O pH4.6, 0.1M CH3COONH4 PH range: 4.2-4.6 |
-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 10, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0781 Å / Relative weight: 1 |
Reflection | Resolution: 1.49→50 Å / Num. obs: 77520 / % possible obs: 98.9 % / Redundancy: 3 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 47.91 |
Reflection shell | Resolution: 1.49→1.51 Å / Rmerge(I) obs: 0.408 / % possible all: 89.9 |
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Processing
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Refinement | Resolution: 1.49→30.01 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.946 / SU B: 1.859 / SU ML: 0.069 / Cross valid method: THROUGHOUT / ESU R: 0.093 / ESU R Free: 0.098 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.618 Å2
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Refinement step | Cycle: 1 / Resolution: 1.49→30.01 Å
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Refine LS restraints |
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