BMRB Entry 27106

Name: Human BRM AT-hook and Bromodomain
Published: 2017-06-01

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27106

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:

Human BRM AT-hook and Bromodomain

Deposition date:

2017-05-15

Original release date:

2017-06-01

Authors:

Morrison, Emma

Citation:

Citation: Morrison, Emma; Sanchez, Julio; Ronan, Jehnna; Farrell, Daniel; Varzavand, Katayoun; Johnson, Jenna; Gu, Brian; Crabtree, Gerald; Musselman, Catherine. "DNA binding drives the association of BRG1/hBRM bromodomains with nucleosomes" Nat Commun. 8, 16080-16080 (2017).
PubMed: 28706277

Assembly members:

Assembly members:
BRM_AT-BRD, polymer, 153 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):
BRM_AT-BRD: GPKEDVEKAKKRRGRPPAEK LSPNPPKLTKQMNAIIDTVI NYKDRCNVEKVPSNSQLEIE GNSSGRQLSEVFIQLPSRKE LPEYYELIRKPVDFKKIKER IRNHKYRSLGDLEKDVMLLC HNAQTFNLEGSQIYEDSIVL QSVFKSARQKIAK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	190
15N chemical shifts	131
1H chemical shifts	131

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AT-BRD	1

Entities:

Entity 1, AT-BRD 153 residues - Formula weight is not available

1

GLY

PRO

LYS

GLU

ASP

VAL

GLU

LYS

ALA

LYS

2

LYS

ARG

GLY

ARG

PRO

ALA

GLU

LYS

3

LEU

SER

PRO

ASN

PRO

LYS

LEU

THR

LYS

4

GLN

MET

ASN

ALA

ILE

ASP

THR

VAL

ILE

5

ASN

TYR

LYS

ASP

ARG

CYS

ASN

VAL

GLU

LYS

6

VAL

PRO

SER

ASN

SER

GLN

LEU

GLU

ILE

GLU

7

GLY

ASN

SER

GLY

ARG

GLN

LEU

SER

GLU

8

VAL

PHE

ILE

GLN

LEU

PRO

SER

ARG

LYS

GLU

9

LEU

PRO

GLU

TYR

GLU

LEU

ILE

ARG

LYS

10

PRO

VAL

ASP

PHE

LYS

ILE

LYS

GLU

ARG

11

ILE

ARG

ASN

HIS

LYS

TYR

ARG

SER

LEU

GLY

12

ASP

LEU

GLU

LYS

ASP

VAL

MET

LEU

CYS

13

HIS

ASN

ALA

GLN

THR

PHE

ASN

LEU

GLU

GLY

14

SER

GLN

ILE

TYR

GLU

ASP

SER

ILE

VAL

LEU

15

GLN

SER

VAL

PHE

LYS

SER

ALA

ARG

GLN

LYS

16

ILE

ALA

LYS

Samples:

sample_1: BRM, [U-100% 13C; U-100% 15N], 0.5 mM; KPi 50 mM; KCl 50 mM

sample_conditions_1: ionic strength: 129 mM; pH: 7.0; pressure: 1 atm; temperature: 293 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
HNCA	sample_1	isotropic	sample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 600 MHz

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