BMRB Entry 28048

Name: Chemical Shift Assignments for BRG1 ATBD
Published: 2020-01-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR28048

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:

Chemical Shift Assignments for BRG1 ATBD

Deposition date:

2019-11-25

Original release date:

2020-01-10

Authors:

Sanchez, Julio

Citation:

Citation: Sanchez, Julio; Zhang, Liyang; Evoli, Stefania; Schnicker, Nicholas; Nunez-Hernandez, Maria; Yu, Liping; Wereszczynski, Jeff; Pufall, Miles; Musselman, Catherine. "The molecular basis of specific DNA binding by the BRG1 AT-hook and bromodomain" Biochim. Biophys. Acta Gene Regul. Mech. ., 194566-194566 (2020).
PubMed: 32376391

Assembly members:

Assembly members:
BRG1_ATBD, polymer, 141 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: pGEX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BRG1_ATBD: GPLGSDDESKKQKKRGRPPA EKLSPNPPNLTKKMKKIVDA VIKYKDSSSGRQLSEVFIQL PSRKELPEYYELIRKPVDFK KIKERIRNHKYRSLNDLEKD VMLLCQNAQTFNLEGSLIYE DSIVLQSVFTSVRQKIEKED D

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	272
15N chemical shifts	113
1H chemical shifts	252

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ATBD	1

Entities:

Entity 1, ATBD 141 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

ASP

GLU

SER

LYS

2

LYS

GLN

LYS

ARG

GLY

ARG

PRO

ALA

3

GLU

LYS

LEU

SER

PRO

ASN

PRO

ASN

LEU

4

THR

LYS

MET

LYS

ILE

VAL

ASP

ALA

5

VAL

ILE

LYS

TYR

LYS

ASP

SER

GLY

6

ARG

GLN

LEU

SER

GLU

VAL

PHE

ILE

GLN

LEU

7

PRO

SER

ARG

LYS

GLU

LEU

PRO

GLU

TYR

8

GLU

LEU

ILE

ARG

LYS

PRO

VAL

ASP

PHE

LYS

9

LYS

ILE

LYS

GLU

ARG

ILE

ARG

ASN

HIS

LYS

10

TYR

ARG

SER

LEU

ASN

ASP

LEU

GLU

LYS

ASP

11

VAL

MET

LEU

CYS

GLN

ASN

ALA

GLN

THR

12

PHE

ASN

LEU

GLU

GLY

SER

LEU

ILE

TYR

GLU

13

ASP

SER

ILE

VAL

LEU

GLN

SER

VAL

PHE

THR

14

SER

VAL

ARG

GLN

LYS

ILE

GLU

LYS

GLU

ASP

15

ASP

Samples:

sample_1: BRG1 ATBD, [U-99% 13C; U-99% 15N], 600 uM; potassium phosphate 50 mM; KCl 50 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMR spectrometers:

Bruker Avance 800 MHz

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