BMRB Entry 50477

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments of co-activator nuclear receptor interacting domain TIF2 NRID
Deposition date:
2020-09-22
Original release date:
2021-04-13
Authors:
Senicourt, Lucile; Sibille, Nathalie
Citation:

Citation: Senicourt, Lucile; le Maire, Albane; Allemand, Frederic; Carvalho, JoAo; Guee, Laura; Germain, Pierre; Schubert, Michael; Bernado, Pau; Bourguet, William; Sibille, Nathalie. "Structural Insights into the Interaction of the Intrinsically Disordered Co-activator TIF2 with Retinoic Acid Receptor Heterodimer (RXR/RAR)"  J. Mol. Biol. 433, 166899-166899 (2021).
PubMed: 33647291

Assembly members:

Assembly members:
entity_1, polymer, 154 residues, 16611.58 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   Vector: pDB vector

Data sets:
Data typeCount
13C chemical shifts444
15N chemical shifts141
1H chemical shifts141

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TIF2 NRID1

Entities:

Entity 1, TIF2 NRID 154 residues - 16611.58 Da.

The TIF2 NRID polypeptide studied here corresponds to the NRID 150-residue long NRID fragment of the human TIF2 co-activator (Uniprot entry Q15596-1) ranging from residue 624 to residue 773. Four extra residues (GPHM) at the N-terminal are remaining from the His-tag cleavage site. TIF2 NRID recombinant protein is composed of 154 residues with a theoretical molecular weight of 16.6 kDa.

1   GLYPROHISMETGLUARGALAASPGLYGLN
2   SERARGLEUHISASPSERLYSGLYGLNTHR
3   LYSLEULEUGLNLEULEUTHRTHRLYSSER
4   ASPGLNMETGLUPROSERPROLEUALASER
5   SERLEUSERASPTHRASNLYSASPSERTHR
6   GLYSERLEUPROGLYSERGLYSERTHRHIS
7   GLYTHRSERLEULYSGLULYSHISLYSILE
8   LEUHISARGLEULEUGLNASPSERSERSER
9   PROVALASPLEUALALYSLEUTHRALAGLU
10   ALATHRGLYLYSASPLEUSERGLNGLUSER
11   SERSERTHRALAPROGLYSERGLUVALTHR
12   ILELYSGLNGLUPROVALSERPROLYSLYS
13   LYSGLUASNALALEULEUARGTYRLEULEU
14   ASPLYSASPASPTHRLYSASPILEGLYLEU
15   PROGLUILETHRPROLYSLEUGLUARGLEU
16   ASPSERLYSTHR

Samples:

sample_1: TIF2 NRID, [U-15N], 100 uM; TIF2 NRID, [U-13C; U-15N], 350 uM; TIF2 NRID, [U-15N], 5 uM; TIF2 NRID, [U-15N], 200 uM; TIF2 NRID, [U-15N], 250 uM; TIF2 NRID + MTSL, [U-15N], 50 uM; TIF2 NRID, [U-13C; U-15N], 120 uM; NaCl 150 mM; BisTris 50 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1anisotropicsample_conditions_1
1D 13Csample_1isotropicsample_conditions_1
1D 15Nsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

SPARKY - data analysis

MARS - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 700 MHz

Related Database Links:

NCOA2_HUMAN Q15596

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