BMRB Entry 50147

Name: 1H, 15N, and 13C backbone chemical shift assignments for the second bromodomain of BRD3 (BRD3-BD2)
Published: 2021-08-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50147

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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 BRD3 (BRD3-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 BRD3, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

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 BRD3: GPLGSKLSEHLRYCDSILRE MLSKKHAAYAWPFYKPVDAE ALELHDYHDIIKHPMDLSTV KRKMDGREYPDAQGFAADVR LMFSNCYKYNPPDHEVVAMA RKLQDVFEMRFAKMPDEP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	129
15N chemical shifts	62
1H chemical shifts	62

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 BRD3	1

Entities:

Entity 1, The second bromodomain of BRD3 118 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

LYS

LEU

SER

GLU

HIS

2

LEU

ARG

TYR

CYS

ASP

SER

ILE

LEU

ARG

GLU

3

MET

LEU

SER

LYS

HIS

ALA

TYR

ALA

4

TRP

PRO

PHE

TYR

LYS

PRO

VAL

ASP

ALA

GLU

5

ALA

LEU

GLU

LEU

HIS

ASP

TYR

HIS

ASP

ILE

6

ILE

LYS

HIS

PRO

MET

ASP

LEU

SER

THR

VAL

7

LYS

ARG

LYS

MET

ASP

GLY

ARG

GLU

TYR

PRO

8

ASP

ALA

GLN

GLY

PHE

ALA

ASP

VAL

ARG

9

LEU

MET

PHE

SER

ASN

CYS

TYR

LYS

TYR

ASN

10

PRO

ASP

HIS

GLU

VAL

ALA

MET

ALA

11

ARG

LYS

LEU

GLN

ASP

VAL

PHE

GLU

MET

ARG

12

PHE

ALA

LYS

MET

PRO

ASP

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 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