BMRB Entry 26043

Name: Solution NMR structures of BRD4 ET domain in complex with NSD3_3 peptide
Published: 2016-06-30

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PDB ID: 2nd1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26043
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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 BRD4 ET domain in complex with NSD3_3 peptide

Deposition date:

2016-04-19

Original release date:

2016-06-30

Authors:

Zeng, Lei; ZHOU, MING-MING

Citation:

Citation: Zhang, Qiang; Zeng, Lei; Shen, Chen; Ju, Ying; Konuma, Tsuyoshi; Zhao, Chengcheng; Vakoc, Christopher; ZHOU, MING-MING. "Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4" Structure 24, 1201-1208 (2016).
PubMed: 27291650

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, 9745.218 Da.
entity_2, polymer, 13 residues, 1557.956 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: recombinant technology Host organism: Escherichia coli Vector: pET32A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SEEEDKCKPMSYEEKRQLSL DINKLPGEKLGRVVHIIQSR EPSLKNSNPDEIEIDFETLK PSTLRELERYVTSCLRKKRK PQA
entity_2: VVPKKKIKKEQVE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	321
15N chemical shifts	81
1H chemical shifts	655

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 83 residues - 9745.218 Da.

1

SER

GLU

ASP

LYS

CYS

LYS

PRO

MET

2

SER

TYR

GLU

LYS

ARG

GLN

LEU

SER

LEU

3

ASP

ILE

ASN

LYS

LEU

PRO

GLY

GLU

LYS

LEU

4

GLY

ARG

VAL

HIS

ILE

GLN

SER

ARG

5

GLU

PRO

SER

LEU

LYS

ASN

SER

ASN

PRO

ASP

6

GLU

ILE

GLU

ILE

ASP

PHE

GLU

THR

LEU

LYS

7

PRO

SER

THR

LEU

ARG

GLU

LEU

GLU

ARG

TYR

8

VAL

THR

SER

CYS

LEU

ARG

LYS

ARG

LYS

9

PRO

GLN

ALA

Entity 2, entity_2 13 residues - 1557.956 Da.

1

VAL

PRO

LYS

ILE

LYS

GLU

2

GLN

VAL

GLU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D filtered 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D filtered 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

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SPARKY: Backbone or all simulated peaks

BMRB Entry 26043

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: