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Open data
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Basic information
| Entry | Database: PDB / ID: 2yoq | ||||||
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| Title | Structure of FAM3B PANDER E30 construct | ||||||
Components | PROTEIN FAM3B | ||||||
Keywords | APOPTOSIS / DIABETES / ILEI / EMT | ||||||
| Function / homology | Function and homology informationinsulin secretion / nuclear envelope lumen / cytokine activity / carbohydrate binding / apoptotic process / extracellular space / extracellular region Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å | ||||||
Authors | Johansson, P. / Bernstrom, J. / Gorman, T. / Oster, L. / Backstrom, S. / Schweikart, F. / Xu, B. / Xue, Y. / Holmberg Schiavone, L. | ||||||
Citation | Journal: Structure / Year: 2013Title: Fam3B Pander and Fam3C Ilei Represent a Distinct Class of Signaling Molecules with a Non-Cytokine-Like Fold. Authors: Johansson, P. / Bernstrom, J. / Gorman, T. / Oster, L. / Backstrom, S. / Schweikart, F. / Xu, B. / Xue, Y. / Schiavone, L.H. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2yoq.cif.gz | 127.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2yoq.ent.gz | 99 KB | Display | PDB format |
| PDBx/mmJSON format | 2yoq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2yoq_validation.pdf.gz | 445.9 KB | Display | wwPDB validaton report |
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| Full document | 2yoq_full_validation.pdf.gz | 447.1 KB | Display | |
| Data in XML | 2yoq_validation.xml.gz | 27.6 KB | Display | |
| Data in CIF | 2yoq_validation.cif.gz | 38.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yo/2yoq ftp://data.pdbj.org/pub/pdb/validation_reports/yo/2yoq | HTTPS FTP |
-Related 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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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS oper:
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Components
| #1: Protein | Mass: 23974.236 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() HOMO SAPIENS (human) / References: UniProt: Q9D309#2: Chemical | #3: Water | ChemComp-HOH / | Has protein modification | Y | |
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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: 3.2 Å3/Da / Density % sol: 61.13 % / Description: NONE |
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| Crystal grow | pH: 7 / Details: pH 7 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1.072 |
| Detector | Type: ADSC CCD / Detector: CCD / Date: Nov 11, 2011 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.072 Å / Relative weight: 1 |
| Reflection | Resolution: 2.35→34.47 Å / Num. obs: 33513 / % possible obs: 99.9 % / Observed criterion σ(I): 1 / Redundancy: 4.3 % / Biso Wilson estimate: 42.49 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 11.2 |
| Reflection shell | Resolution: 2.35→2.43 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.79 / Mean I/σ(I) obs: 2.6 / % possible all: 99.7 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.35→21.64 Å / Cor.coef. Fo:Fc: 0.9457 / Cor.coef. Fo:Fc free: 0.9344 / SU R Cruickshank DPI: 0.211 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.215 / SU Rfree Blow DPI: 0.167 / SU Rfree Cruickshank DPI: 0.167 Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
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| Displacement parameters | Biso mean: 34.55 Å2
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| Refine analyze | Luzzati coordinate error obs: 0.226 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.35→21.64 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.35→2.42 Å / Total num. of bins used: 17
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X-RAY DIFFRACTION
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HOMO SAPIENS (human)


