BMRB Entry 30367

Name: Solution NMR structures of the BRD3 ET domain in complex with a CHD4 peptide
Published: 2018-03-14

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PDB ID: 6bgg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30367
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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:

Solution NMR structures of the BRD3 ET domain in complex with a CHD4 peptide

Deposition date:

2017-10-28

Original release date:

2018-03-14

Authors:

Wai, D.; Szyszka, T.; Campbell, A.; Kwong, C.; Wilkinson-White, L.; Silva, A.; Low, J.; Kwan, A.; Gamsjaeger, R.; Lu, B.; Vakoc, C.; Blobel, G.; Mackay, J.

Citation:

Citation: Wai, Dorothy; Szyszka, Taylor; Campbell, Amy; Kwong, Cherry; Wilkinson-White, Lorna; Silva, Ana; Low, Jason; Kwan, Ann; Gamsjaeger, Roland; Chalmers, James; Patrick, Wayne; Lu, Bin; Vakoc, Christopher; Blobel, Gerd; Mackay, Joel. "The BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators" J. Biol. Chem. 293, 7160-7175 (2018).
PubMed: 29567837

Assembly members:

Assembly members:
entity_1, polymer, 12 residues, 1273.629 Da.
entity_2, polymer, 93 residues, 10687.956 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KVAPLKIKLGGF
entity_2: GPLGSASASYDSEEEEEGLP MSYDEKRQLSLDINRLPGEK LGRVVHIIQSREPSLRDSNP DEIEIDFETLKPTTLRELER YVKSCLQKKQRKP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	354
15N chemical shifts	82
1H chemical shifts	603

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 12 residues - 1273.629 Da.

1

LYS

VAL

ALA

PRO

LEU

LYS

ILE

LYS

LEU

GLY

2

GLY

PHE

Entity 2, entity_2 93 residues - 10687.956 Da.

1

GLY

PRO

LEU

GLY

SER

ALA

SER

ALA

SER

TYR

2

ASP

SER

GLU

GLY

LEU

PRO

3

MET

SER

TYR

ASP

GLU

LYS

ARG

GLN

LEU

SER

4

LEU

ASP

ILE

ASN

ARG

LEU

PRO

GLY

GLU

LYS

5

LEU

GLY

ARG

VAL

HIS

ILE

GLN

SER

6

ARG

GLU

PRO

SER

LEU

ARG

ASP

SER

ASN

PRO

7

ASP

GLU

ILE

GLU

ILE

ASP

PHE

GLU

THR

LEU

8

LYS

PRO

THR

LEU

ARG

GLU

LEU

GLU

ARG

9

TYR

VAL

LYS

SER

CYS

LEU

GLN

LYS

GLN

10

ARG

LYS

PRO

Samples:

sample_1: BRD3, [U-13C; U-15N], 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_2: BRD3, [U-13C; U-15N], 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_3: BRD3 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C (F1)-filtered NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
HNCACO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D 15N13C (F2,F1)-filtered) 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY v3.1.3, Goddard - chemical shift assignment, peak picking

TOPSPIN v3.5.6, Bruker Biospin - processing

NMR spectrometers:

Bruker AvanceIII 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks