BMRB Entry 51415

Name: Bromodomain Interactions with Acetylated Histone 4 Peptides in the Tandem Domain BRD4 -- Effects on Domain Dynamics and Internal Flexibility
Published: 2022-10-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51415

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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:

Bromodomain Interactions with Acetylated Histone 4 Peptides in the Tandem Domain BRD4 -- Effects on Domain Dynamics and Internal Flexibility

Deposition date:

2022-04-26

Original release date:

2022-10-11

Authors:

Wernersson, Sven; Romel, Bobby; Flavell, Liz; Milbradt, Alexander; Holdgate, Geoff; Embrey, Kevin; Akke, Mikael

Citation:

Citation: Wernersson, Sven; Bobby, Romel; Flavell, Liz; Milbradt, Alexander; Holdgate, Geoffrey; Embrey, Kevin; Akke, Mikael. "Bromodomain Interactions with Acetylated Histone 4 Peptides in the BRD4 Tandem Domain: Effects on Domain Dynamics and Internal Flexibility" Biochemistry 61, 2303-2318 (2022).
PubMed: 36215732

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, Formula weight is not available
entity_2, polymer, 16 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NPPPPETSNPNKPKRQTNQL QYLLRVVLKTLWKHQFAWPF QQPVDAVKLNLPDYYKIIKT PMDMGTIKKRLENNYYWNAQ ECIQDFNTMFTNCYIYNKPG DDIVLMAEALEKLFLQKINE LPTEE
entity_2: SGRGXGGXGLGXGGAX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
- heteronucl_NOEs_2
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
- heteronucl_T1_relaxation_2
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1
- heteronucl_T2_relaxation_2
order_parameters
- order_parameters_1

Data type	Count
15N chemical shifts	105
1H chemical shifts	105
T1 relaxation values	157
T2 relaxation values	158
heteronuclear NOE values	157
order parameters	79

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BD1	1
2	H4Kac	2

Entities:

Entity 1, BD1 125 residues - Formula weight is not available

1

ASN

PRO

GLU

THR

SER

ASN

PRO

2

ASN

LYS

PRO

LYS

ARG

GLN

THR

ASN

GLN

LEU

3

GLN

TYR

LEU

ARG

VAL

LEU

LYS

THR

4

LEU

TRP

LYS

HIS

GLN

PHE

ALA

TRP

PRO

PHE

5

GLN

PRO

VAL

ASP

ALA

VAL

LYS

LEU

ASN

6

LEU

PRO

ASP

TYR

LYS

ILE

LYS

THR

7

PRO

MET

ASP

MET

GLY

THR

ILE

LYS

ARG

8

LEU

GLU

ASN

TYR

TRP

ASN

ALA

GLN

9

GLU

CYS

ILE

GLN

ASP

PHE

ASN

THR

MET

PHE

10

THR

ASN

CYS

TYR

ILE

TYR

ASN

LYS

PRO

GLY

11

ASP

ILE

VAL

LEU

MET

ALA

GLU

ALA

LEU

12

GLU

LYS

LEU

PHE

LEU

GLN

LYS

ILE

ASN

GLU

13

LEU

PRO

THR

GLU

Entity 2, H4Kac 16 residues - Formula weight is not available

1

SER

GLY

ARG

GLY

ALY

GLY

ALY

GLY

LEU

2

GLY

ALY

GLY

ALA

ALY

Samples:

sample_1: apo Bromodomain 1 (BD1) of BRD4, [U-100% 13C; U-100% 15N], 0.135 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 1 mM; H4Kac 0.9 mM

sample_conditions_1: ionic strength: 0.180 M; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMRPipe - processing

Relax - data analysis

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker Avance 600 MHz

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