BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27706

Title: EZH2 SANT1   PubMed: 30700785

Deposition date: 2018-11-28 Original release date: 2018-12-19

Authors: Weaver, Tyler; Musselman, Catherine

Citation: Weaver, Tyler; Liu, Jiachen; Connelly, Katelyn; Coble, Chris; Varzavand, Katayoun; Dykhuizen, Emily; Musselman, Catherine. "The EZH2 SANT1 domains is a histone reader domain providing sensitivity to the modification state of the H4 tail"  Sci. Rep. 9, 987-987 (2019).

Assembly members:
EZH2_SANT1, polymer, 113 residues, Formula weight is not available

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   Vector: pDEST15

Entity Sequences (FASTA):
EZH2_SANT1: GPQDGTFIEELIKNYDGKVH GDRECGFINDEIFVELVNAL GQYNDDDDDDDGDDPEEREE KQKDLEDHRDDKESRPPRKF PSDKIFEAISSMFPDKGTAE ELKEKYKELTEQQ

Data sets:
Data typeCount
13C chemical shifts252
15N chemical shifts84
1H chemical shifts84

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EZH2 SANT11

Entities:

Entity 1, EZH2 SANT1 113 residues - Formula weight is not available

1   GLYPROGLNASPGLYTHRPHEILEGLUGLU
2   LEUILELYSASNTYRASPGLYLYSVALHIS
3   GLYASPARGGLUCYSGLYPHEILEASNASP
4   GLUILEPHEVALGLULEUVALASNALALEU
5   GLYGLNTYRASNASPASPASPASPASPASP
6   ASPGLYASPASPPROGLUGLUARGGLUGLU
7   LYSGLNLYSASPLEUGLUASPHISARGASP
8   ASPLYSGLUSERARGPROPROARGLYSPHE
9   PROSERASPLYSILEPHEGLUALAILESER
10   SERMETPHEPROASPLYSGLYTHRALAGLU
11   GLULEULYSGLULYSTYRLYSGLULEUTHR
12   GLUGLNGLN

Samples:

sample_1: EZH2 SANT1, [U-100% 13C; U-100% 15N], 700 mM; NaCL 150 mM

sample_2: EZH2 SANT1, [U-100% 13C; U-100% 15N], 715 uM; NaCL 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

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

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 500 MHz

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