BMRB Entry 50145

Name: 1H, 15N, and 13C backbone chemical shift assignments for the first bromodomain of BRD4 (BRD4-BD1)
Published: 2021-08-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50145

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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 BRD4 (BRD4-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 BRD4, polymer, 145 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 BRD4: GPLGSSTNPPPPETSNPNKP KRQTNQLQYLLRVVLKTLWK HQFAWPFQQPVDAVKLNLPD YYKIIKTPMDMGTIKKRLEN NYYWNAQECIQDFNTMFTNC YIYNKPGDDIVLMAEALEKL FLQKINELPTEEPEFPGRLE RPHRD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	221
15N chemical shifts	105
1H chemical shifts	105

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 BRD4	1

Entities:

Entity 1, The first bromodomain of BRD4 145 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

THR

ASN

PRO

2

PRO

GLU

THR

SER

ASN

PRO

ASN

LYS

PRO

3

LYS

ARG

GLN

THR

ASN

GLN

LEU

GLN

TYR

LEU

4

LEU

ARG

VAL

LEU

LYS

THR

LEU

TRP

LYS

5

HIS

GLN

PHE

ALA

TRP

PRO

PHE

GLN

PRO

6

VAL

ASP

ALA

VAL

LYS

LEU

ASN

LEU

PRO

ASP

7

TYR

LYS

ILE

LYS

THR

PRO

MET

ASP

8

MET

GLY

THR

ILE

LYS

ARG

LEU

GLU

ASN

9

ASN

TYR

TRP

ASN

ALA

GLN

GLU

CYS

ILE

10

GLN

ASP

PHE

ASN

THR

MET

PHE

THR

ASN

CYS

11

TYR

ILE

TYR

ASN

LYS

PRO

GLY

ASP

ILE

12

VAL

LEU

MET

ALA

GLU

ALA

LEU

GLU

LYS

LEU

13

PHE

LEU

GLN

LYS

ILE

ASN

GLU

LEU

PRO

THR

14

GLU

PRO

GLU

PHE

PRO

GLY

ARG

LEU

GLU

15

ARG

PRO

HIS

ARG

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