BMRB Entry 19125

Name: Molecular Basis of Histone Acetyllysine Recognition by the BRPF1 Bromodomain.
Published: 2014-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19125

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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:

Molecular Basis of Histone Acetyllysine Recognition by the BRPF1 Bromodomain.

Deposition date:

2013-03-28

Original release date:

2014-02-12

Authors:

Poplawski, Amanda; Hu, Kaifeng; Lee, Woonghee; Peng, Danni; Carlson, Samuel; Neuhardt, Elizabeth; Shi, Xiaobing; Markley, John; Glass, Karen

Citation:

Citation: Poplawski, Amanda; Hu, Kaifeng; Lee, Woonghee; Natesan, Senthil; Peng, Danni; Carlson, Samuel; Shi, Xiaobing; Balaz, Stefan; Markley, John; Glass, Karen. "Molecular Insights into the Recognition of N-Terminal Histone Modifications by the BRPF1 Bromodomain." J. Mol. Biol. 426, 1661-1676 (2014).
PubMed: 24333487

Assembly members:

Assembly members:
BRPF1_bromodomain, polymer, 117 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: pDEST15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BRPF1_bromodomain: GPLQLTPFLILLRKTLEQLQ EKDTGNIFSEPVPLSEVPDY LDHIKKPMDFFTMKQNLEAY RYLNFDDFEEDFNLIVSNCL KYNAKDTIFYRAAVRLREQG GAVLRQARRQAEKMGID

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	317
15N chemical shifts	99
1H chemical shifts	99

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BRPF1	1

Entities:

Entity 1, BRPF1 117 residues - Formula weight is not available

1

GLY

PRO

LEU

GLN

LEU

THR

PRO

PHE

LEU

ILE

2

LEU

ARG

LYS

THR

LEU

GLU

GLN

LEU

GLN

3

GLU

LYS

ASP

THR

GLY

ASN

ILE

PHE

SER

GLU

4

PRO

VAL

PRO

LEU

SER

GLU

VAL

PRO

ASP

TYR

5

LEU

ASP

HIS

ILE

LYS

PRO

MET

ASP

PHE

6

PHE

THR

MET

LYS

GLN

ASN

LEU

GLU

ALA

TYR

7

ARG

TYR

LEU

ASN

PHE

ASP

PHE

GLU

8

ASP

PHE

ASN

LEU

ILE

VAL

SER

ASN

CYS

LEU

9

LYS

TYR

ASN

ALA

LYS

ASP

THR

ILE

PHE

TYR

10

ARG

ALA

VAL

ARG

LEU

ARG

GLU

GLN

GLY

11

GLY

ALA

VAL

LEU

ARG

GLN

ALA

ARG

GLN

12

ALA

GLU

LYS

MET

GLY

ILE

ASP

Samples:

sample_1: Tris HCl 20 mM; NaCl 150 mM; DTT 10 mM; BRPF1_bromodomain, [U-13C; U-15N], 0 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

ADAPT-NMR, (ADAPT-NMR)-NMRFAM - chemical shift assignment, collection, peak picking

NMR spectrometers:

Bruker Avance III 500 MHz

PDB	4LC2 4QYD 4QYL 4UYE 5C7N
DBJ	BAC31528 BAE33691 BAG10583 BAG57257
EMBL	CAD28495
GB	AAB02119 AAF19605 AAH05647 AAH46521 AAI38362
REF	NP_001178501 NP_001269055 NP_001269056 NP_004625 NP_084454
SP	P55201
TPG	DAA17219
AlphaFold	P55201