BMRB Entry 34437

Click here to enlarge.

PDB ID: 6sy2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34437
MolProbity Validation Chart

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:

Structure of the BRK domain of the SWI/SNF chromatin remodelling complex subunit BRG1 reveals a potential role in protein-protein interactions

Deposition date:

2019-09-27

Original release date:

2020-01-17

Authors:

Allen, M.; Bycoft, M.; Zinzalla, G.

Citation:

Citation: Allen, M.; Bycoft, M.; Zinzalla, G.. "Structure of the BRK domain of the SWI/SNF chromatin remodeling complex subunit BRG1 reveals a potential role in protein-protein interactions" Protein Sci. 29, 1047-1053 (2020).
PubMed: 31909846

Assembly members:

Assembly members:
entity_1, polymer, 49 residues, 5287.906 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 BL21(DE3) Vector: HLTV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SQMSDLPVKVIHVESGKILT GTDAPKAGQLEAWLEMNPGY EVAPRSDSE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	172
15N chemical shifts	48
1H chemical shifts	338

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 49 residues - 5287.906 Da.

1

SER

GLN

MET

SER

ASP

LEU

PRO

VAL

LYS

VAL

2

ILE

HIS

VAL

GLU

SER

GLY

LYS

ILE

LEU

THR

3

GLY

THR

ASP

ALA

PRO

LYS

ALA

GLY

GLN

LEU

4

GLU

ALA

TRP

LEU

GLU

MET

ASN

PRO

GLY

TYR

5

GLU

VAL

ALA

PRO

ARG

SER

ASP

SER

GLU

Samples:

sample_1: BRG1 BRK domain, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 20 mM; NaCl 100 mM; beta-mercaptoethanol 5 mM

sample_2: BRG1 BRK domain 2 mM; potassium phosphate 20 mM; NaCl 100 mM; beta-mercaptoethanol 5 mM

sample_3: BRG1 BRK domain, [U-10% 13C], 1 mM; potassium phosphate 20 mM; NaCl 100 mM; beta-mercaptoethanol 5 mM

sample_conditions_1: ionic strength: 140 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_2	isotropic	sample_conditions_1
2D TOCSY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

ANSIG, Kraulis - chemical shift assignment

Azara, Boucher - processing

NMR spectrometers:

Bruker AVANCE 800 MHz
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