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Open data
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Basic information
Entry | Database: PDB / ID: 4cy3 | ||||||
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Title | Crystal structure of the NSL1-WDS complex. | ||||||
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![]() | TRANSCRIPTION / EPIGENETIC REGULATOR / HISTONE ACETYLATION / CHROMATIN | ||||||
Function / homology | ![]() polytene chromosome interband / Formation of WDR5-containing histone-modifying complexes / haltere development / germarium-derived female germ-line cyst formation / Neddylation / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / larval somatic muscle development / germ-line stem cell population maintenance / eye development / MLL3/4 complex ...polytene chromosome interband / Formation of WDR5-containing histone-modifying complexes / haltere development / germarium-derived female germ-line cyst formation / Neddylation / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / larval somatic muscle development / germ-line stem cell population maintenance / eye development / MLL3/4 complex / Set1C/COMPASS complex / MLL1/2 complex / ATAC complex / NSL complex / neuromuscular junction development / histone acetyltransferase binding / oogenesis / regulation of endocytosis / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / heart development / histone binding / chromatin remodeling / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dias, J. / Brettschneider, J. / Cusack, S. / Kadlec, J. | ||||||
![]() | ![]() Title: Structural Analysis of the Kansl1/Wdr5/Kansl2 Complex Reveals that Wdr5 is Required for Efficient Assembly and Chromatin Targeting of the Nsl Complex. Authors: Dias, J. / Van Nguyen, N. / Georgiev, P. / Gaub, A. / Brettschneider, J. / Cusack, S. / Kadlec, J. / Akhtar, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 131.8 KB | Display | ![]() |
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PDB format | ![]() | 101.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.3 KB | Display | ![]() |
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Full document | ![]() | 435.6 KB | Display | |
Data in XML | ![]() | 14.7 KB | Display | |
Data in CIF | ![]() | 21 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4cy1C ![]() 4cy2C ![]() 4cy5C ![]() 2g99S C: citing same article ( S: Starting model for refinement |
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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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 34673.297 Da / Num. of mol.: 1 / Fragment: RESIDUES 50-361 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1768.003 Da / Num. of mol.: 1 / Fragment: RESIDUES 714-729 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() References: UniProt: A4V2Z1, Ligases; Forming carbon-oxygen bonds; Ligases forming aminoacyl-tRNA and related compounds |
#3: Chemical | ChemComp-GOL / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 0.43 % / Description: NONE |
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Crystal grow | pH: 7.2 Details: 20% (W/V) PEG 3350, 0.2 M POTASSIUM SODIUM TARTRATE, PH 7.2. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 30, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93928 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→100 Å / Num. obs: 60987 / % possible obs: 98.9 % / Observed criterion σ(I): 2.4 / Redundancy: 7.3 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 13.9 |
Reflection shell | Resolution: 1.4→1.46 Å / Redundancy: 7.1 % / Rmerge(I) obs: 0.87 / Mean I/σ(I) obs: 2.4 / % possible all: 91.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2G99 Resolution: 1.4→48.81 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.955 / SU B: 1.238 / SU ML: 0.026 / Cross valid method: THROUGHOUT / ESU R: 0.015 / ESU R Free: 0.012 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 10.337 Å2
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Refinement step | Cycle: LAST / Resolution: 1.4→48.81 Å
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Refine LS restraints |
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