BMRB Entry 50149

Name: 1H, 15N, and 13C backbone chemical shift assignments for the second bromodomain of BRD2 (BRD2-BD2)
Published: 2021-08-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50149

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 15N, and 13C backbone chemical shift assignments for the second bromodomain of BRD2 (BRD2-BD2)

Deposition date:

2019-12-31

Original release date:

2021-08-12

Authors:

Patel, Karishma; Mackay, Joel; Solomon, Paul

Citation:

Citation: Patel, Karishma; Solomon, Paul; Walshe, James; Ford, Daniel; Wilkinson-White, Lorna; Payne, Richard; Low, Jason; Mackay, Joel. "BET-Family Bromodomains Can Recognize Diacetylated Sequences from Transcription Factors Using a Conserved Mechanism" Biochemistry 60, 648-662 (2021).
PubMed: 33620209

Assembly members:

Assembly members:
The second bromodomain of BRD2, polymer, 114 residues, Formula weight is not available

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: pGEX-6P

Entity Sequences (FASTA):

Entity Sequences (FASTA):
The second bromodomain of BRD2: GPLGSSEQLKHCNGILKELL SKKHAAYAWPFYKPVDASAL GLHDYHDIIKHPMDLSTVKR KMENRDYRDAQEFAADVRLM FSNCYKYNPPDHDVVAMARK LQDVFEFRYAKMPD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	139
15N chemical shifts	78
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	The second bromdomain of BRD2	1

Entities:

Entity 1, The second bromdomain of BRD2 114 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

GLU

GLN

LEU

LYS

2

HIS

CYS

ASN

GLY

ILE

LEU

LYS

GLU

LEU

3

SER

LYS

HIS

ALA

TYR

ALA

TRP

PRO

4

PHE

TYR

LYS

PRO

VAL

ASP

ALA

SER

ALA

LEU

5

GLY

LEU

HIS

ASP

TYR

HIS

ASP

ILE

LYS

6

HIS

PRO

MET

ASP

LEU

SER

THR

VAL

LYS

ARG

7

LYS

MET

GLU

ASN

ARG

ASP

TYR

ARG

ASP

ALA

8

GLN

GLU

PHE

ALA

ASP

VAL

ARG

LEU

MET

9

PHE

SER

ASN

CYS

TYR

LYS

TYR

ASN

PRO

10

ASP

HIS

ASP

VAL

ALA

MET

ALA

ARG

LYS

11

LEU

GLN

ASP

VAL

PHE

GLU

PHE

ARG

TYR

ALA

12

LYS

MET

PRO

ASP

Samples:

sample_1: DSS 0.01 mM; TRIS 10 mM; sodium chloride 100 mM; DTT 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

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