BMRB Entry 30019

Title:
NMR structure of UHRF1 Tandem Tudor Domains in a complex with Spacer peptide
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:

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).
PubMed: 27045799

Assembly members:

Assembly members:
E3 ubiquitin-protein ligase UHRF1, polymer, 152 residues, 17804.875 Da.
Spacer, polymer, 16 residues, 1606.849 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Data sets:
Data typeCount
13C chemical shifts421
15N chemical shifts152
1H chemical shifts951

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 152 residues - 17804.875 Da.

1   LEUTYRLYSVALASNGLUTYRVALASPALA
2   ARGASPTHRASNMETGLYALATRPPHEGLU
3   ALAGLNVALVALARGVALTHRARGLYSALA
4   PROSERARGASPGLUPROCYSSERSERTHR
5   SERARGPROALALEUGLUGLUASPVALILE
6   TYRHISVALLYSTYRASPASPTYRPROGLU
7   ASNGLYVALVALGLNMETASNSERARGASP
8   VALARGALAARGALAARGTHRILEILELYS
9   TRPGLNASPLEUGLUVALGLYGLNVALVAL
10   METLEUASNTYRASNPROASPASNPROLYS
11   GLUARGGLYPHETRPTYRASPALAGLUILE
12   SERARGLYSARGGLUTHRARGTHRALAARG
13   GLULEUTYRALAASNVALVALLEUGLYASP
14   ASPSERLEUASNASPCYSARGILEILEPHE
15   VALASPGLUVALPHELYSILEGLUARGPRO
16   GLYGLU

Entity 2, entity_2 16 residues - 1606.849 Da.

1   THRGLYLYSGLYLYSTRPLYSARGLYSSER
2   ALAGLYGLYGLYPROSER

Samples:

sample_1: Spacer 1.2 mM; TTD, [U-13C; U-15N], 1.0 mM; H2O 90 mM; D2O 10 mM

sample_2: Spacer, [U-15N], 1.0 mM; TTD 1.0 mM; H2O 90 mM; D2O 10 mM

sample_conditions_1: pH: 7.4; temperature: 297.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
w2 x-filter TOCSYsample_1isotropicsample_conditions_1
HBCBCGCDCEHEsample_1isotropicsample_conditions_1
HBCBCGCDHDsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
MQ-CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
13C-filer HSQC-NOESYsample_1isotropicsample_conditions_1
w1,w2 x-filter NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMR, Varian - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks