BMRB Entry 30444

Name: Solution structure of the Extraterminal (ET) Domain of BRD2
Published: 2019-03-01

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PDB ID: 6cui
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30444
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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 structure of the Extraterminal (ET) Domain of BRD2

Deposition date:

2018-03-26

Original release date:

2019-03-01

Authors:

Houliston, S.; Lemak, A.; Picaud, S.; Filippakopoulos, P.; Arrowsmith, C.

Citation:

Citation: Houliston, S.; Lemak, A.; Picaud, S.; Filippakopoulos, P.; Arrowsmith, C.. "Solution structure of the Extraterminal (ET) Domain of BRD2" .

Assembly members:

Assembly members:
entity_1, polymer, 132 residues, 15275.450 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: SMKTAPPALPTGYDSEEEEE SRPMSYDEKRQLSLDINKLP GEKLGRVVHIIQAREPSLRD SNPEEIEIDFETLKPSTLRE LERYVLSCLRKKPRKPYTIK KPVGKTKEELALEKKRELEK RLQDVSGQLNST

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	528
15N chemical shifts	116
1H chemical shifts	864

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 132 residues - 15275.450 Da.

1

SER

MET

LYS

THR

ALA

PRO

ALA

LEU

PRO

2

THR

GLY

TYR

ASP

SER

GLU

3

SER

ARG

PRO

MET

SER

TYR

ASP

GLU

LYS

ARG

4

GLN

LEU

SER

LEU

ASP

ILE

ASN

LYS

LEU

PRO

5

GLY

GLU

LYS

LEU

GLY

ARG

VAL

HIS

ILE

6

ILE

GLN

ALA

ARG

GLU

PRO

SER

LEU

ARG

ASP

7

SER

ASN

PRO

GLU

ILE

GLU

ILE

ASP

PHE

8

GLU

THR

LEU

LYS

PRO

SER

THR

LEU

ARG

GLU

9

LEU

GLU

ARG

TYR

VAL

LEU

SER

CYS

LEU

ARG

10

LYS

PRO

ARG

LYS

PRO

TYR

THR

ILE

LYS

11

LYS

PRO

VAL

GLY

LYS

THR

LYS

GLU

LEU

12

ALA

LEU

GLU

LYS

ARG

GLU

LEU

GLU

LYS

13

ARG

LEU

GLN

ASP

VAL

SER

GLY

GLN

LEU

ASN

14

SER

THR

Samples:

sample_1: BRD2-ET, [U-13C; U-15N], 250 uM; NaCl 500 mM

sample_conditions_1: ionic strength: 500 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

SPARKY, Goddard - peak picking

NMR spectrometers:

Bruker AvanceII 800 MHz
Bruker AvanceIII 600 MHz

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