BMRB Entry 51326

Name: PBRM1 Bromodomain 2
Published: 2023-07-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51326

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

PBRM1 Bromodomain 2

Deposition date:

2022-02-13

Original release date:

2023-07-04

Authors:

De Silva, Saumya; Sood, Surbhi; Dhiman, Alisha; Mercedes, Kilsia; Henen, Morkos; Vogeli, Beat; Dykhuizen, Emily; Musselman, Catherine

Citation:

Citation: De Silva, Saumya; Sood, Surbhi; Dhiman, Alisha; Mercedes, Kilsia; Henen, Morkos; Vogeli, Beat; Dykhuizen, Emily; Musselman, Catherine. "PBRM1 BD2 and BD4 associate with RNA to facilitate chromatin association" Nucleic Acids Res. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 116 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: pNIC28-Bsa4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMSPAYLKEILEQLLEAIVV ATNPSGRLISELFQKLPSKV QYPDYYAIIKEPIDLKTIAQ RIQNGSYKSIHAMAKDIDLL AKNAKTYNEPGSQVFKDANS IKKIFYMKKAEIEHHE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	332
15N chemical shifts	100
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PBRM1 Bromodomain 2	1

Entities:

Entity 1, PBRM1 Bromodomain 2 116 residues - Formula weight is not available

1

SER

MET

SER

PRO

ALA

TYR

LEU

LYS

GLU

ILE

2

LEU

GLU

GLN

LEU

GLU

ALA

ILE

VAL

3

ALA

THR

ASN

PRO

SER

GLY

ARG

LEU

ILE

SER

4

GLU

LEU

PHE

GLN

LYS

LEU

PRO

SER

LYS

VAL

5

GLN

TYR

PRO

ASP

TYR

ALA

ILE

LYS

6

GLU

PRO

ILE

ASP

LEU

LYS

THR

ILE

ALA

GLN

7

ARG

ILE

GLN

ASN

GLY

SER

TYR

LYS

SER

ILE

8

HIS

ALA

MET

ALA

LYS

ASP

ILE

ASP

LEU

9

ALA

LYS

ASN

ALA

LYS

THR

TYR

ASN

GLU

PRO

10

GLY

SER

GLN

VAL

PHE

LYS

ASP

ALA

ASN

SER

11

ILE

LYS

ILE

PHE

TYR

MET

LYS

ALA

12

GLU

ILE

GLU

HIS

GLU

Samples:

sample_1: PBRM1 Bromodomain 2, [U-100% 13C; U-100% 15N], 1 mM; potassium chloride 50 mM; potassium phosphate 50 mM; DTT 2 mM; EDTA 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CcpNMR v2.5.2 - chemical shift assignment, peak picking

TOPSPIN v4.0.9 - collection, data analysis

NMRPipe - peak picking, processing

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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