+Open data
-Basic information
Entry | Database: PDB / ID: 6qb7 | ||||||
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Title | Structure of the H1 domain of human KCTD16 | ||||||
Components | BTB/POZ domain-containing protein KCTD16 | ||||||
Keywords | SIGNALING PROTEIN / KCTD16 / H1 / CTD / C-terminal domain / GABAB / GABABR2 / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | Function and homology information regulation of G protein-coupled receptor signaling pathway / cell projection / protein homooligomerization / presynaptic membrane / postsynaptic membrane / receptor complex Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.23 Å | ||||||
Authors | Pinkas, D.M. / Bufton, J.C. / Williams, E.P. / Strain-Damerell, C. / Kupinska, K. / Burgess-Brown, N.A. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Bountra, C. ...Pinkas, D.M. / Bufton, J.C. / Williams, E.P. / Strain-Damerell, C. / Kupinska, K. / Burgess-Brown, N.A. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Bountra, C. / Bullock, A.N. / Structural Genomics Consortium (SGC) | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: To be published Title: Structure of the H1 domain of human KCTD16 Authors: Pinkas, D.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6qb7.cif.gz | 134.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6qb7.ent.gz | 103.5 KB | Display | PDB format |
PDBx/mmJSON format | 6qb7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6qb7_validation.pdf.gz | 480 KB | Display | wwPDB validaton report |
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Full document | 6qb7_full_validation.pdf.gz | 485.2 KB | Display | |
Data in XML | 6qb7_validation.xml.gz | 23 KB | Display | |
Data in CIF | 6qb7_validation.cif.gz | 31.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qb/6qb7 ftp://data.pdbj.org/pub/pdb/validation_reports/qb/6qb7 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18779.020 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCTD16, KIAA1317 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta / References: UniProt: Q68DU8 #2: Chemical | ChemComp-PO4 / #3: 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: 2.25 Å3/Da / Density % sol: 45.36 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: Mother liquor: 0.8M ammonium phosphate monobasic -- 0.8M ammonium phosphate dibasic 1:1 drops with protein in: 300 mM NaCl, 50 mM HEPES pH 7.5, 1 mM TCEP, 5 mM DTT |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.9282 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jun 25, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9282 Å / Relative weight: 1 |
Reflection | Resolution: 2.23→60 Å / Num. obs: 42017 / % possible obs: 97.36 % / Redundancy: 9.5 % / Net I/σ(I): 9.22 |
Reflection shell | Resolution: 2.23→2.31 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Unpublished Resolution: 2.23→60 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 34.87
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.23→60 Å
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Refine LS restraints |
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LS refinement shell |
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