BMRB Entry 51010

Name: Sequential backbone resonance assignment of AT-rich interaction domain of BAF250b
Published: 2022-05-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51010

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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:

Sequential backbone resonance assignment of AT-rich interaction domain of BAF250b

Deposition date:

2021-07-07

Original release date:

2022-05-06

Authors:

Giri, Malyasree; Gupta, Parul; Singh, Mahavir

Citation:

Citation: Giri, Malyasree; Gupta, Parul; Maulik, Aditi; Gracias, Magaly; Singh, Mahavir. "Structure and DNA binding analysis of AT-rich interaction domain present in human BAF-B specific subunit BAF250b" Protein Sci. 31, e4294-e4294 (2022).
PubMed: 35481652

Assembly members:

Assembly members:
entity_1, polymer, 134 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSTTTGEKITKVYELGNE PERKLWVDRYLTFMEERGSP VSSLPAVGKKPLDLFRLYVC VKEIGGLAQVNKNKKWRELA TNLNVGTSSSAASSLKKQYI QYLFAFECKIERGEEPPPEV FSTGDTLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	452
15N chemical shifts	120
1H chemical shifts	629

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BAF250b_ARID	1

Entities:

Entity 1, BAF250b_ARID 134 residues - Formula weight is not available

134 residues, residues 126-134 represent a non-native residues L, E and six H of affinity tag. This is the ARID domain of BAF250b.

1

MET

GLY

SER

THR

GLY

GLU

LYS

2

ILE

THR

LYS

VAL

TYR

GLU

LEU

GLY

ASN

GLU

3

PRO

GLU

ARG

LYS

LEU

TRP

VAL

ASP

ARG

TYR

4

LEU

THR

PHE

MET

GLU

ARG

GLY

SER

PRO

5

VAL

SER

LEU

PRO

ALA

VAL

GLY

LYS

6

PRO

LEU

ASP

LEU

PHE

ARG

LEU

TYR

VAL

CYS

7

VAL

LYS

GLU

ILE

GLY

LEU

ALA

GLN

VAL

8

ASN

LYS

ASN

LYS

TRP

ARG

GLU

LEU

ALA

9

THR

ASN

LEU

ASN

VAL

GLY

THR

SER

10

ALA

SER

LEU

LYS

GLN

TYR

ILE

11

GLN

TYR

LEU

PHE

ALA

PHE

GLU

CYS

LYS

ILE

12

GLU

ARG

GLY

GLU

PRO

GLU

VAL

13

PHE

SER

THR

GLY

ASP

THR

LEU

GLU

HIS

14

HIS

Samples:

sample_1: BAF250b_ARID, [U-99% 15N], 0.6 ± 0.1 mM; NaH2PO4 50 ± 0.1 mM; EDTA 25 uM

sample_2: BAF250b_ARID, [U-99% 13C; U-99% 15N], 0.6 ± 0.1 mM; NaH2PO4 50 ± 0.1 mM; EDTA 25 uM

sample_conditions_1: pH: 6; 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_2	isotropic	sample_conditions_1
3D CBCANH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1

Software:

VNMRj - collection, data analysis

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, chemical shift calculation, data analysis, peak picking

TALOS+ - data analysis, dihedral angles

NMR spectrometers:

Agilent DRX 600 MHz

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