BMRB Entry 50802

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignment for Brd3-BD1 bound to inhibitor PCC
Published: 2022-12-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50802

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NMR-STAR v3 text file.
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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignment for Brd3-BD1 bound to inhibitor PCC

Deposition date:

2021-03-05

Original release date:

2022-12-16

Authors:

Zerio, Christopher; Clarkson, Michael; Gunatilaka, A.; Chapman, Eli

Citation:

Citation: Zerio, Christopher; Sivinski, Jared; Wijeratne, E; Xu, Ya-Ming; Ngo, Duc; Ambrose, Andrew; Villa-Celis, Luis; Ghadirian, Niloofar; Clarkson, Michael; Zhang, Donna; Horton, Nancy; Gunatilaka, A; Fromme, Raimund; Chapman, Eli. "Physachenolide C is a Potent, Selective BET Inhibitor" J. Med. Chem. 66, 913-933 (2023).
PubMed: 36577036

Assembly members:

Assembly members:
entity_1, polymer, 122 residues, 14409.65 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: PIPET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPEVSNPSKPGRKTNQLQYM QNVVVKTLWKHQFAWPFYQP VDAIKLNLPDYHKIIKNPMD MGTIKKRLENNYYWSASECM QDFNTMFTNCYIYNKPTDDI VLMAQALEKIFLQKVAQMPQ EE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	240
15N chemical shifts	111
1H chemical shifts	111

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Brd3-BD1	1

Entities:

Entity 1, Brd3-BD1 122 residues - 14409.65 Da.

The first G is a scar from cloning. In the real protein, the numbering would start with P24. In the NMRSTAR file I submitted, it starts as P1.

1

GLY

PRO

GLU

VAL

SER

ASN

PRO

SER

LYS

PRO

2

GLY

ARG

LYS

THR

ASN

GLN

LEU

GLN

TYR

MET

3

GLN

ASN

VAL

LYS

THR

LEU

TRP

LYS

4

HIS

GLN

PHE

ALA

TRP

PRO

PHE

TYR

GLN

PRO

5

VAL

ASP

ALA

ILE

LYS

LEU

ASN

LEU

PRO

ASP

6

TYR

HIS

LYS

ILE

LYS

ASN

PRO

MET

ASP

7

MET

GLY

THR

ILE

LYS

ARG

LEU

GLU

ASN

8

ASN

TYR

TRP

SER

ALA

SER

GLU

CYS

MET

9

GLN

ASP

PHE

ASN

THR

MET

PHE

THR

ASN

CYS

10

TYR

ILE

TYR

ASN

LYS

PRO

THR

ASP

ILE

11

VAL

LEU

MET

ALA

GLN

ALA

LEU

GLU

LYS

ILE

12

PHE

LEU

GLN

LYS

VAL

ALA

GLN

MET

PRO

GLN

13

GLU

Samples:

sample_1: Bromodomain-containing Protein 3, Bromodomain 1, [U-99% 13C; U-99% 15N], 350 uM; PCC 350 uM; Tris 20 mM; NaCl 100 mM; DTT 1 mM

sample_conditions_1: pH: 7.0; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v1.414 - chemical shift assignment, peak picking

NMR spectrometers:

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