BMRB Entry 50143

Name: 1H, 15N, and 13C backbone chemical shift assignments for the first bromodomain of BRD2 (BRD2-BD1)
Published: 2021-08-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50143

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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 first bromodomain of BRD2 (BRD2-BD1)

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 first bromodomain of BRD2, polymer, 135 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 first bromodomain of BRD2: GPLGSEVSNPKKPGRVTNQL QYLHKVVMKALWKHQFAWPF RQPVDAVKLGLPDYHKIIKQ PMDMGTIKRRLENNYYWAAS ECMQDFNTMFTNCYIYNKPT DDIVLMAQTLEKIFLQKVAS MPQEEQELVVTIPKN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	263
15N chemical shifts	122
1H chemical shifts	122

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	The first bromodomain of BRD2 (BRD2-BD1)	1

Entities:

Entity 1, The first bromodomain of BRD2 (BRD2-BD1) 135 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

GLU

VAL

SER

ASN

PRO

2

LYS

PRO

GLY

ARG

VAL

THR

ASN

GLN

LEU

3

GLN

TYR

LEU

HIS

LYS

VAL

MET

LYS

ALA

4

LEU

TRP

LYS

HIS

GLN

PHE

ALA

TRP

PRO

PHE

5

ARG

GLN

PRO

VAL

ASP

ALA

VAL

LYS

LEU

GLY

6

LEU

PRO

ASP

TYR

HIS

LYS

ILE

LYS

GLN

7

PRO

MET

ASP

MET

GLY

THR

ILE

LYS

ARG

8

LEU

GLU

ASN

TYR

TRP

ALA

SER

9

GLU

CYS

MET

GLN

ASP

PHE

ASN

THR

MET

PHE

10

THR

ASN

CYS

TYR

ILE

TYR

ASN

LYS

PRO

THR

11

ASP

ILE

VAL

LEU

MET

ALA

GLN

THR

LEU

12

GLU

LYS

ILE

PHE

LEU

GLN

LYS

VAL

ALA

SER

13

MET

PRO

GLN

GLU

GLN

GLU

LEU

VAL

14

THR

ILE

PRO

LYS

ASN

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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz
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