BMRB Entry 50146

Name: 1H, 15N, and 13C backbone chemical shift assignments for the second bromodomain of BRD4 (BRD4-BD2)
Published: 2021-08-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50146

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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 BRD4 (BRD4-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 bromdomain of BRD4, polymer, 122 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 bromdomain of BRD4: GPLGSSKVSEQLKCCSGILK EMFAKKHAAYAWPFYKPVDV EALGLHDYCDIIKHPMDMST IKSKLEAREYRDAQEFGADV RLMFSNCYKYNPPDHEVVAM ARKLQDVFEMRFAKMPDEPE EP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	143
15N chemical shifts	84
1H chemical shifts	84

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	The second bromodomain of BRD4	1

Entities:

Entity 1, The second bromodomain of BRD4 122 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

LYS

VAL

SER

GLU

2

GLN

LEU

LYS

CYS

SER

GLY

ILE

LEU

LYS

3

GLU

MET

PHE

ALA

LYS

HIS

ALA

TYR

4

ALA

TRP

PRO

PHE

TYR

LYS

PRO

VAL

ASP

VAL

5

GLU

ALA

LEU

GLY

LEU

HIS

ASP

TYR

CYS

ASP

6

ILE

LYS

HIS

PRO

MET

ASP

MET

SER

THR

7

ILE

LYS

SER

LYS

LEU

GLU

ALA

ARG

GLU

TYR

8

ARG

ASP

ALA

GLN

GLU

PHE

GLY

ALA

ASP

VAL

9

ARG

LEU

MET

PHE

SER

ASN

CYS

TYR

LYS

TYR

10

ASN

PRO

ASP

HIS

GLU

VAL

ALA

MET

11

ALA

ARG

LYS

LEU

GLN

ASP

VAL

PHE

GLU

MET

12

ARG

PHE

ALA

LYS

MET

PRO

ASP

GLU

PRO

GLU

13

GLU

PRO

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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	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