+Open data
-Basic information
Entry | Database: PDB / ID: 4nzd | |||||||||
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Title | Interleukin 21 receptor | |||||||||
Components | Interleukin-21 receptor | |||||||||
Keywords | SIGNALING PROTEIN / Fibronectine III domain / Interleukin 21 / Glycosylated | |||||||||
Function / homology | Function and homology information interleukin-21 receptor activity / Interleukin-21 signaling / natural killer cell activation / cytokine receptor activity / immunoglobulin mediated immune response / cytokine-mediated signaling pathway / transmembrane signaling receptor activity / external side of plasma membrane / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.75 Å | |||||||||
Authors | Hamming, O.T. / Kang, L. / Siupka, P. / Gad, H.H. / Hartmann, R. | |||||||||
Citation | Journal: To be Published Title: Interleukin 21 receptor structure and function Authors: Hamming, O.T. / Kang, L. / Siupka, P. / Gad, H.H. / Hartmann, R. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4nzd.cif.gz | 143.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4nzd.ent.gz | 118.1 KB | Display | PDB format |
PDBx/mmJSON format | 4nzd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nz/4nzd ftp://data.pdbj.org/pub/pdb/validation_reports/nz/4nzd | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
-Protein , 1 types, 3 molecules ABC
#1: Protein | Mass: 25451.297 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IL21R, NILR, UNQ3121/PRO10273 / Cell line (production host): HEK293 cells / Production host: homo sapiens (human) / References: UniProt: Q9HBE5 |
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-Sugars , 2 types, 6 molecules
#2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Sugar | |
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-Non-polymers , 5 types, 178 molecules
#4: Chemical | ChemComp-NA / #5: Chemical | ChemComp-CL / #6: Chemical | #7: Chemical | ChemComp-EDO / | #8: 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: 4.18 Å3/Da / Density % sol: 70.57 % |
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Crystal grow | Temperature: 278 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 5 mg/ml Protein in 10 mM Hepes, 150 mM NaCl, pH7.5 Crystalized in 1M Potassium sodium tartrate tetrahydrate, 3% W/V Peg5000 and 0.1 M tris Ph 8.5. Drops were 1:1, VAPOR DIFFUSION, SITTING DROP, temperature 278K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: MAX II / Beamline: I911-2 / Wavelength: 1.04 Å |
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Detector | Type: ADSC QUANTUM 315r / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.04 Å / Relative weight: 1 |
Reflection | Resolution: 2.75→29.78 Å / Num. all: 33646 / Num. obs: 33261 / % possible obs: 99 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 2.75→2.848 Å / % possible all: 99 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.75→29.778 Å / SU ML: 0.38 / σ(F): 1.36 / Phase error: 27.98 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.75→29.778 Å
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Refine LS restraints |
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LS refinement shell |
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