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- PDB-4o46: 14-3-3-gamma in complex with influenza NS1 C-terminal tail phosph... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4o46 | ||||||
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Title | 14-3-3-gamma in complex with influenza NS1 C-terminal tail phosphorylated at S228 | ||||||
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Function / homology | ![]() symbiont-mediated suppression of host mRNA processing / symbiont-mediated suppression of host PKR/eIFalpha signaling / protein serine/threonine kinase inhibitor activity / regulation of neuron differentiation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Qin, S. / Liu, Y. / Tempel, W. / Arrowsmith, C.H. / Bountra, C. / Edwards, A.M. / Min, J. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() Title: Structural basis for histone mimicry and hijacking of host proteins by influenza virus protein NS1. Authors: Qin, S. / Liu, Y. / Tempel, W. / Eram, M.S. / Bian, C. / Liu, K. / Senisterra, G. / Crombet, L. / Vedadi, M. / Min, 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 | ![]() | 548.1 KB | Display | ![]() |
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PDB format | ![]() | 454.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4nw2C ![]() 4o42C ![]() 4o45C ![]() 3uzdS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Details | THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS UNKNOWN. |
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Components
#1: Protein | Mass: 29494.809 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 1872.202 Da / Num. of mol.: 6 / Source method: obtained synthetically / Details: synthetic peptide / Source: (synth.) ![]() ![]() #3: Protein/peptide | Mass: 2060.531 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #4: Chemical | ChemComp-UNX / Sequence details | THE AUTHORS STATE THAT THE UNIDENTIFIED POLYMER IN CHAINS M, N, O, AND V IS LIKELY PART OF ...THE AUTHORS STATE THAT THE UNIDENTIFI | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.6 Å3/Da / Density % sol: 65.2 % |
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Crystal grow![]() | Temperature: 291 K Details: 20% PEG3350, 0.2 M magnesium nitrate, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 2, 2012 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.8→113.59 Å / Num. all: 53464 / Num. obs: 53464 / % possible obs: 100 % / Redundancy: 14.8 % / Biso Wilson estimate: 71.39 Å2 / Rsym value: 0.14 / Net I/σ(I): 21.7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing![]() | Method: ![]() |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: pdb entry 3uzd Resolution: 2.9→38.53 Å / Cor.coef. Fo:Fc: 0.8997 / Cor.coef. Fo:Fc free: 0.889 / Occupancy max: 1 / Occupancy min: 0.01 / SU R Cruickshank DPI: 0.682 / Cross valid method: THROUGHOUT / σ(F): 0 Details: coot was used for interactive model building. refmac was used during intermediate refinement steps. Model geometry was assessed on the molprobity server. disjoint helices have been modeled ...Details: coot was used for interactive model building. refmac was used during intermediate refinement steps. Model geometry was assessed on the molprobity server. disjoint helices have been modeled into weak density. They have not been assigned specific amino acid sequences, and their direction is uncertain. additional uninterpreted density remains in that area of the electron density map. Attempts to locate additional 14-3-3-g molecules or larger fragments thereof by molecular replacement failed.
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Displacement parameters | Biso max: 215.11 Å2 / Biso mean: 69.7905 Å2 / Biso min: 18.32 Å2
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Refine analyze | Luzzati coordinate error obs: 0.494 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→38.53 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.9→2.98 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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