BMRB Entry 30019
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PDB ID: 5iay
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30019
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Title: NMR structure of UHRF1 Tandem Tudor Domains in a complex with Spacer peptide PubMed: 27045799
Deposition date: 2016-02-22 Original release date: 2016-04-12
Authors: Fang, J.; Cheng, J.; Wang, J.; Zhang, Q.; Liu, M.; Gong, R.; Wang, P.; Zhang, X.; Feng, Y.; Lan, W.; Gong, Z.; Tang, C.; Wong, J.; Yang, H.; Cao, C.; Xu, Y.
Citation: Fang, J.; Cheng, J.; Wang, J.; Zhang, Q.; Liu, M.; Gong, R.; Wang, P.; Zhang, X.; Feng, Y.; Lan, W.; Gong, Z.; Tang, C.; Wong, J.; Yang, H.; Cao, C.; Xu, Y.. "Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition" Nat. Commun. 7, .-. (2016).
Assembly members:
E3 ubiquitin-protein ligase UHRF1, polymer, 152 residues, 17804.875 Da.
Spacer, polymer, 16 residues, 1606.849 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
E3 ubiquitin-protein ligase UHRF1: LYKVNEYVDARDTNMGAWFE
AQVVRVTRKAPSRDEPCSST
SRPALEEDVIYHVKYDDYPE
NGVVQMNSRDVRARARTIIK
WQDLEVGQVVMLNYNPDNPK
ERGFWYDAEISRKRETRTAR
ELYANVVLGDDSLNDCRIIF
VDEVFKIERPGE
Spacer: TGKGKWKRKSAGGGPS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 421 |
| 15N chemical shifts | 152 |
| 1H chemical shifts | 951 |
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