BMRB Entry 30368

Name: Solution NMR structure of Brd3 ET domain bound to Brg1 peptide
Published: 2018-03-14

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PDB ID: 6bgh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30368
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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 structure of Brd3 ET domain bound to Brg1 peptide

Deposition date:

2017-10-28

Original release date:

2018-03-14

Authors:

Szyszka, T.; Wai, D.; 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, 87 residues, 10179.387 Da.
entity_2, polymer, 12 residues, 1417.829 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: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ASASYDSEEEEEGLPMSYDE KRQLSLDINRLPGEKLGRVV HIIQSREPSLRDSNPDEIEI DFETLKPTTLRELERYVKSC LQKKQRK
entity_2: RSVKVKIKLGRK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	352
15N chemical shifts	79
1H chemical shifts	669

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 87 residues - 10179.387 Da.

1

ALA

SER

ALA

SER

TYR

ASP

SER

GLU

2

GLU

GLY

LEU

PRO

MET

SER

TYR

ASP

GLU

3

LYS

ARG

GLN

LEU

SER

LEU

ASP

ILE

ASN

ARG

4

LEU

PRO

GLY

GLU

LYS

LEU

GLY

ARG

VAL

5

HIS

ILE

GLN

SER

ARG

GLU

PRO

SER

LEU

6

ARG

ASP

SER

ASN

PRO

ASP

GLU

ILE

GLU

ILE

7

ASP

PHE

GLU

THR

LEU

LYS

PRO

THR

LEU

8

ARG

GLU

LEU

GLU

ARG

TYR

VAL

LYS

SER

CYS

9

LEU

GLN

LYS

GLN

ARG

LYS

Entity 2, entity_2 12 residues - 1417.829 Da.

1

ARG

SER

VAL

LYS

VAL

LYS

ILE

LYS

LEU

GLY

2

ARG

LYS

Samples:

sample_1: Brd3_ET 300 uM; Brg1 600 uM; Roche Complete Protease Inhibitor 0.02%; DSS 166 uM; NaCl 50 mM

sample_2: Brd3_ET, [U-15N], 300 uM; Brg1 600 uM; Roche Complete Protease Inhibitor 0.02%; DSS 166 uM; NaCl 50 mM

sample_3: Brd3_ET, [U-13C; U-15N], 300 uM; Brg1 600 uM; Roche Complete Protease Inhibitor 0.02%; DSS 166 uM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_3
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_3
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
3D 13C/15N (F2/F1) Filtered, 1H-1H NOESY	sample_3	isotropic	sample_conditions_3
2D 13C/15N (F2/F1) Filtered, 1H-1H NOESY	sample_3	isotropic	sample_conditions_3
2D 13C/15N (F2/F1) Filtered, 1H-1H TOCSY	sample_3	isotropic	sample_conditions_3
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_3
3D HCCH-COSY	sample_3	isotropic	sample_conditions_3
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_3	isotropic	sample_conditions_3
3D H(CC)(CO)HN	sample_3	isotropic	sample_conditions_3
3D HNCA	sample_3	isotropic	sample_conditions_3
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_3
3D HNCACB	sample_3	isotropic	sample_conditions_3

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

Bruker AvanceIII 600 MHz
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