BMRB Entry 25851

Title:
TRIM24 PHD-Bromo dual-domain backbone assignment
Deposition date:
2015-10-16
Original release date:
2016-05-31
Authors:
Walser, Reto; Milbradt, Alexander
Citation:

Citation: Walser, Reto; Milbradt, Alexander; Renshaw, Jonathan. "Backbone resonance assignments for the PHD-Bromo dual-domain of the human chromatin reader TRIM24"  Biomol. NMR Assignments 10, 207-211 (2016).
PubMed: 26878853

Assembly members:

Assembly members:
TRIM24, polymer, 196 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts327
15N chemical shifts154
1H chemical shifts312

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TRIM241
2ZN, 12
3ZN, 22

Entities:

Entity 1, TRIM24 196 residues - Formula weight is not available

1   GLYSERTHRARGLYSGLUASPASPPROASN
2   GLUASPTRPCYSALAVALCYSGLNASNGLY
3   GLYGLULEULEUCYSCYSGLULYSCYSPRO
4   LYSVALPHEHISLEUSERCYSHISVALPRO
5   THRLEUTHRASNPHEPROSERGLYGLUTRP
6   ILECYSTHRPHECYSARGASPLEUSERLYS
7   PROGLUVALGLUTYRASPCYSASPALAPRO
8   SERHISASNSERGLULYSLYSLYSTHRGLU
9   GLYLEUVALLYSLEUTHRPROILEASPLYS
10   ARGLYSCYSGLUARGLEULEULEUPHELEU
11   TYRCYSHISGLUMETSERLEUALAPHEGLN
12   ASPPROVALPROLEUTHRVALPROASPTYR
13   TYRLYSILEILELYSASNPROMETASPLEU
14   SERTHRILELYSLYSARGLEUGLNGLUASP
15   TYRSERMETTYRSERLYSPROGLUASPPHE
16   VALALAASPPHEARGLEUILEPHEGLNASN
17   CYSALAGLUPHEASNGLUPROASPSERGLU
18   VALALAASNALAGLYILELYSLEUGLUASN
19   TYRPHEGLUGLULEULEULYSASNLEUTYR
20   PROGLULYSARGPHEPRO

Entity 2, ZN, 1 - 65.409 Da.

1   ZN

Samples:

sample_1: TRIM24, [U-100% 13C; U-100% 15N], 0.8 mM; HEPES 50 mM; sodium chloride 100 mM; TCEP 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.25 M; pH: 7.4; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2.5, Bruker Biospin - collection

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

Cara, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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