BMRB Entry 50477

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments of co-activator nuclear receptor interacting domain TIF2 NRID
Published: 2021-04-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50477

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments of co-activator nuclear receptor interacting domain TIF2 NRID PubMed: 33647291

Deposition date: 2020-09-22 Original release date: 2021-04-13

Authors: Senicourt, Lucile; Sibille, Nathalie

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).

Assembly members:
entity_1, polymer, 154 residues, 16611.58 Da.

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: pDB vector

Entity Sequences (FASTA):
entity_1: GPHMERADGQSRLHDSKGQT KLLQLLTTKSDQMEPSPLAS SLSDTNKDSTGSLPGSGSTH GTSLKEKHKILHRLLQDSSS PVDLAKLTAEATGKDLSQES SSTAPGSEVTIKQEPVSPKK KENALLRYLLDKDDTKDIGL PEITPKLERLDSKT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	444
15N chemical shifts	141
1H chemical shifts	141

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TIF2 NRID	1

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

GLY

PRO

HIS

MET

GLU

ARG

ALA

ASP

GLY

GLN

2

SER

ARG

LEU

HIS

ASP

SER

LYS

GLY

GLN

THR

3

LYS

LEU

GLN

LEU

THR

LYS

SER

4

ASP

GLN

MET

GLU

PRO

SER

PRO

LEU

ALA

SER

5

SER

LEU

SER

ASP

THR

ASN

LYS

ASP

SER

THR

6

GLY

SER

LEU

PRO

GLY

SER

GLY

SER

THR

HIS

7

GLY

THR

SER

LEU

LYS

GLU

LYS

HIS

LYS

ILE

8

LEU

HIS

ARG

LEU

GLN

ASP

SER

9

PRO

VAL

ASP

LEU

ALA

LYS

LEU

THR

ALA

GLU

10

ALA

THR

GLY

LYS

ASP

LEU

SER

GLN

GLU

SER

11

SER

THR

ALA

PRO

GLY

SER

GLU

VAL

THR

12

ILE

LYS

GLN

GLU

PRO

VAL

SER

PRO

LYS

13

LYS

GLU

ASN

ALA

LEU

ARG

TYR

LEU

14

ASP

LYS

ASP

THR

LYS

ASP

ILE

GLY

LEU

15

PRO

GLU

ILE

THR

PRO

LYS

LEU

GLU

ARG

LEU

16

ASP

SER

LYS

THR

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:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	anisotropic	sample_conditions_1
1D 13C	sample_1	isotropic	sample_conditions_1
1D 15N	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

SPARKY - data analysis

MARS - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 700 MHz

Biological Magnetic Resonance Data Bank