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- PDB-2y0n: CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE COMPENSATION FACT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2y0n | ||||||
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Title | CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE COMPENSATION FACTORS MSL1 AND MSL3 | ||||||
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![]() | TRANSCRIPTION / CHROMATIN / X CHROMOSOME / MSL COMPLEX | ||||||
Function / homology | ![]() MSL complex / HATs acetylate histones / Rpd3S complex / histone H4K16 acetyltransferase activity / NuA4 histone acetyltransferase complex / methylated histone binding / HATs acetylate histones / nuclear speck / chromatin remodeling / chromatin binding ...MSL complex / HATs acetylate histones / Rpd3S complex / histone H4K16 acetyltransferase activity / NuA4 histone acetyltransferase complex / methylated histone binding / HATs acetylate histones / nuclear speck / chromatin remodeling / chromatin binding / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / DNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kadlec, J. / Hallacli, E. / Lipp, M. / Holz, H. / Sanchez Weatherby, J. / Cusack, S. / Akhtar, A. | ||||||
![]() | ![]() Title: Structural Basis for Mof and Msl3 Recruitment Into the Dosage Compensation Complex by Msl1. Authors: Kadlec, J. / Hallacli, E. / Lipp, M. / Holz, H. / Sanchez-Weatherby, J. / Cusack, S. / 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 | ![]() | 343.6 KB | Display | ![]() |
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PDB format | ![]() | 285.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 484.9 KB | Display | ![]() |
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Full document | ![]() | 496.9 KB | Display | |
Data in XML | ![]() | 28.4 KB | Display | |
Data in CIF | ![]() | 38.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2y0mC ![]() 2f5jS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
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Components
#1: Protein | Mass: 24776.662 Da / Num. of mol.: 4 / Fragment: MRG DOMAIN, RESIDUES 167-289 AND 442-518 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 6271.082 Da / Num. of mol.: 4 / Fragment: PEHE DOMAIN, RESIDUES 545-597 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Sequence details | RESIDUES 290-441 IN UNP Q8N5Y2 WERE SUBSTITUTED WITH AN INSERTION SEQUENCE YDIPPTTEF. YDIPPTT WERE ...RESIDUES 290-441 IN UNP Q8N5Y2 WERE SUBSTITUTE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.8 % / Description: NONE |
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Crystal grow | pH: 6.5 / Details: 0.1M ADA (PH 6.5), 0.1M LI2SO4, 0.9M MGSO4. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 26, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 3→46 Å / Num. obs: 25057 / % possible obs: 93.5 % / Observed criterion σ(I): 2 / Redundancy: 2.2 % / Biso Wilson estimate: 100 Å2 / Rmerge(I) obs: 0.03 / Net I/σ(I): 16.37 |
Reflection shell | Resolution: 3→3.12 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 2.04 / % possible all: 94.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2F5J Resolution: 3→46.13 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.916 / SU B: 51.587 / SU ML: 0.398 / Cross valid method: THROUGHOUT / ESU R: 0.889 / ESU R Free: 0.413 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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: 100.475 Å2
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Refinement step | Cycle: LAST / Resolution: 3→46.13 Å
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Refine LS restraints |
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