E3ubiquitin-proteinligaseUHRF1 / Ubiquitin-like PHD and RING finger domain-containing protein 1 / Ubiquitin-like-containing PHD and ...Ubiquitin-like PHD and RING finger domain-containing protein 1 / Ubiquitin-like-containing PHD and RING finger domains protein 1 / Nuclear zinc finger protein Np95 / Nuclear protein 95
Mass: 23915.711 Da / Num. of mol.: 1 / Fragment: SRA domain, residues 419-628 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Np95 / Plasmid: pXC666 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-Gold Cells References: UniProt: Q8VDF2, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)
#2: DNA chain
DNA (5'-D(*DTP*DCP*DCP*DAP*DTP*DGP*DCP*DGP*DCP*DTP*DGP*DAP*DC)-3')
Mass: 3927.561 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: 12 base pair DNA duplex
#3: DNA chain
DNA (5'-D(*DGP*DTP*DCP*DAP*DGP*(5CM)P*DGP*DCP*DAP*DAP*DTP*DGP*DG)-3')
Mass: 4030.650 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: 12 base pair DNA duplex
Resolution: 2.19→29.4 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 708338.01 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER Details: The density for the nucleotide at position 9 in chain E indicated an extrahelical conformation (E429) as well as an intrahelical conformation (E430). The depositors made a model as if an ...Details: The density for the nucleotide at position 9 in chain E indicated an extrahelical conformation (E429) as well as an intrahelical conformation (E430). The depositors made a model as if an additional nucleotide A10 was inserted.
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