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- PDB-4nw2: Tandem chromodomains of human CHD1 in complex with Influenza viru... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4nw2 | ||||||
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Title | Tandem chromodomains of human CHD1 in complex with Influenza virus NS1 C-terminal tail trimethylated at K229 | ||||||
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![]() | PEPTIDE BINDING PROTEIN/VIRAL PROTEIN / Structural Genomics Consortium / SGC / PEPTIDE BINDING PROTEIN-VIRAL PROTEIN complex | ||||||
Function / homology | ![]() symbiont-mediated suppression of host cytokine production / symbiont-mediated suppression of host innate immune response / symbiont-mediated suppression of host mRNA processing / symbiont-mediated suppression of host PKR/eIFalpha signaling / nucleosome organization / protein serine/threonine kinase inhibitor activity / positive regulation by host of viral transcription / ATP-dependent chromatin remodeler activity / nuclear chromosome / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity ...symbiont-mediated suppression of host cytokine production / symbiont-mediated suppression of host innate immune response / symbiont-mediated suppression of host mRNA processing / symbiont-mediated suppression of host PKR/eIFalpha signaling / nucleosome organization / protein serine/threonine kinase inhibitor activity / positive regulation by host of viral transcription / ATP-dependent chromatin remodeler activity / nuclear chromosome / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / methylated histone binding / helicase activity / double-stranded RNA binding / histone binding / Estrogen-dependent gene expression / DNA helicase / host cell cytoplasm / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / chromatin remodeling / virus-mediated perturbation of host defense response / chromatin binding / host cell nucleus / chromatin / regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / RNA binding / nucleoplasm / ATP binding / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Qin, S. / Tempel, W. / Xu, C. / El Bakkouri, M. / Bountra, C. / Arrowsmith, C.H. / 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 | ![]() | 169.3 KB | Display | ![]() |
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PDB format | ![]() | 132.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 466.9 KB | Display | ![]() |
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Full document | ![]() | 467.6 KB | Display | |
Data in XML | ![]() | 17.6 KB | Display | |
Data in CIF | ![]() | 24.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4o42C ![]() 4o45C ![]() 4o46C ![]() 2b2wS S: Starting model for refinement 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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Unit cell |
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Components
#1: Protein | Mass: 22942.408 Da / Num. of mol.: 2 / Fragment: UNP residues 268-443 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 1834.303 Da / Num. of mol.: 2 / Fragment: UNP residues 216-230 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() #3: Chemical | ChemComp-UNX / #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.54 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 10% PEG8000, 0.2M magnesium chloride, 0.1M Tris, pH 8.5, vapor diffusion, sitting drop, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 18, 2012 | ||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||
Radiation wavelength | Wavelength: 0.97926 Å / Relative weight: 1 | ||||||||||||||||||
Reflection | Resolution: 1.9→70.694 Å / Num. obs: 39818 / % possible obs: 100 % / Redundancy: 3.8 % / Biso Wilson estimate: 28.8 Å2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 14.5 | ||||||||||||||||||
Reflection shell | Rmerge(I) obs: 0.012 / 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 2b2w Resolution: 1.9→42.968 Å / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.7981 / SU ML: 0.26 / σ(F): 0.12 / Phase error: 26.09 / Stereochemistry target values: ML Details: REFMAC WAS USED DURING INTERMEDIATE REFINEMENT STAGES. COOT WAS USED FOR INTERACTIVE MODEL BUILDING. MODEL GEOMETRY WAS ASSESSED ON THE MOLPROBITY SERVER. ELECTRON DENSITY FOR THE BACKBONE ...Details: REFMAC WAS USED DURING INTERMEDIATE REFINEMENT STAGES. COOT WAS USED FOR INTERACTIVE MODEL BUILDING. MODEL GEOMETRY WAS ASSESSED ON THE MOLPROBITY SERVER. ELECTRON DENSITY FOR THE BACKBONE OF THE PEPTIDE LIGAND IS NOT CONTINUOUS. IT IS THEREFORE POSSIBLE THAT THE PEPTIDE'S AMINO-TERMINUS IS MODELED IN A DIFFERENT ASYMMETRIC UNIT RELATIVE TO THE CARBOXY-TERMINUS. WEAK ELECTRON DENSITY NEAR P417 OF EITHER CHD1 CHAIN FAINTLY RESEMBLES A PEPTIDE.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 106.87 Å2 / Biso mean: 39.8335 Å2 / Biso min: 16.24 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→42.968 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30
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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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