BMRB Entry 27251

Title:
Backbone and sidechain 1H, 13C, and 15N Chemical Shift Assignments for CW domain of Histone-lysine N-methyltransferase ASHH2 bound to H3K4me1
Deposition date:
2017-09-09
Original release date:
2018-03-08
Authors:
Dobrovolska, Olena; Halskau, Oyvind; Stromland, Oyvind; Aasland, Rein; Brilkov, Maxim; Odegar, Oyvind
Citation:

Citation: Dobrovolska, Olena; Brilkov, Maxim; Odegard, Oyvind; Aasland, Rein; Halskau, Oyvind. "1H, 13C, and 15N resonance assignments of CW domain of the N-methyltransferase ASHH2 free and bound to the mono-, di- and tri-methylated histone H3 tail peptides"  Biomol. NMR Assign. 12, 215-220 (2018).
PubMed: 29453713

Assembly members:

Assembly members:
CW42, polymer, 79 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.
H3K4me1, polymer, 9 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts232
15N chemical shifts88
1H chemical shifts488

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CW42 monomer1
2ZINC ION2
3H3K4me13

Entities:

Entity 1, CW42 monomer 79 residues - Formula weight is not available

1   GLYSERARGARGALASERVALGLYSERGLU
2   PHETHRGLUSERALATRPVALARGCYSASP
3   ASPCYSPHELYSTRPARGARGILEPROALA
4   SERVALVALGLYSERILEASPGLUSERSER
5   ARGTRPILECYSMETASNASNSERASPLYS
6   ARGPHEALAASPCYSSERLYSSERGLNGLU
7   METSERASNGLUGLUILEASNGLUGLULEU
8   GLYILEGLYGLNASPGLUALAASPALA

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Entity 3, H3K4me1 9 residues - Formula weight is not available

1   ALAARGTHRMLZGLNTHRALAARGTYR

Samples:

sample_1: CW42 bound to H3K4me1, [U-99% 13C; U-99% 15N], 1.6 mM; sodium phosphate 20 mM; DTT 1 mM; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5 pI5, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Ascend 850 MHz

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