BMRB Entry 30501

Title:
Solution structure of ZZZ3 ZZ domain in complex with histone H3 tail
Deposition date:
2018-07-27
Original release date:
2018-09-12
Authors:
Zhang, Y.; Kutateladze, T.
Citation:

Citation: Mi, Wenyi; Zhang, Yi; Lyu, Jie; Wang, Xiaolu; Tong, Qiong; Peng, Danni; Xue, Yongming; Tencer, Adam; Wen, Hong; Li, Wei; Kutateladze, Tatiana; Shi, Xiaobing. "The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation."  Nat. Commun. 9, 3759-3759 (2018).
PubMed: 30217978

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7279.126 Da.
entity_2, polymer, 12 residues, 1308.488 Da.
entity_ZN, non-polymer, 65.409 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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts177
15N chemical shifts63
1H chemical shifts415

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_3, 13
4entity_3, 23

Entities:

Entity 1, entity_1 64 residues - 7279.126 Da.

1   GLYPROLEUGLYSERVALGLNHISVALGLY
2   PHELYSCYSASPASNCYSGLYILEGLUPRO
3   ILEGLNGLYVALARGTRPHISCYSGLNASP
4   CYSPROPROGLUMETSERLEUASPPHECYS
5   ASPSERCYSSERASPCYSLEUHISGLUTHR
6   ASPILEHISLYSGLUASPHISGLNLEUGLU
7   PROILETYRARG

Entity 2, entity_2 12 residues - 1308.488 Da.

1   ALAARGTHRLYSGLNTHRALAARGLYSSER
2   THRGLY

Entity 3, entity_3, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: ZZ domain of ZZZ3, [U-13C; U-15N], 2 mM; Histone H3 10 mM; sodium chloride 100 mM; TRIS 20 mM; D2O, [U-99% 2H], 7%

sample_2: ZZ domain of ZZZ3, [U-13C; U-15N], 4 mM; sodium chloride 100 mM; TRIS 20 mM; D2O, [U-99% 2H], 7%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D filtered 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D filtered 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1

Software:

VNMR, Varian - collection

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

Analysis, CCPN - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

AMBER, D.A. Case, etc. - refinement

NMR spectrometers:

  • Varian INOVA 900 MHz
  • 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