post-embryonic forelimb morphogenesis / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / positive regulation of nuclear cell cycle DNA replication / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / chromosome organization involved in meiotic cell cycle / chromosome, subtelomeric region / Sertoli cell development / meiotic spindle organization / cellular response to hydroxyurea ...post-embryonic forelimb morphogenesis / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / positive regulation of nuclear cell cycle DNA replication / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / chromosome organization involved in meiotic cell cycle / chromosome, subtelomeric region / Sertoli cell development / meiotic spindle organization / cellular response to hydroxyurea / DNA translocase activity / chromo shadow domain binding / positive regulation of telomere maintenance / condensed chromosome, centromeric region / ATP-dependent chromatin remodeler activity / protein localization to chromosome, telomeric region / nuclear chromosome / seminiferous tubule development / replication fork processing / DNA damage response, signal transduction by p53 class mediator / subtelomeric heterochromatin formation / heterochromatin / pericentric heterochromatin / forebrain development / Inhibition of DNA recombination at telomere / methylated histone binding / helicase activity / multicellular organism growth / chromatin DNA binding / PML body / nucleosome assembly / chromatin organization / histone binding / spermatogenesis / DNA helicase / transcription by RNA polymerase II / chromosome, telomeric region / nuclear body / chromatin remodeling / DNA repair / chromatin binding / regulation of DNA-templated transcription / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / nucleoplasm / ATP binding / nucleus / metal ion binding Similarity search - Function
Method to determine structure: SAD / Resolution: 1.901→32.115 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8336 / σ(F): 2.13 / Stereochemistry target values: TWIN_LSQ_F Details: THE FRIEDEL PAIRS WERE USED IN SAD PHASING. DURING REFINEMENT, FRIEDEL PAIRS WERE MERGED.
Rfactor
Num. reflection
% reflection
Rfree
0.1583
1997
7.63 %
Rwork
0.1271
-
-
obs
0.1298
26159
99.97 %
Solvent computation
Shrinkage radii: 0.72 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 51.109 Å2 / ksol: 0.348 e/Å3
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