BMRB Entry 51010

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

Data sets:
Data typeCount
13C chemical shifts452
15N chemical shifts120
1H chemical shifts629

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1BAF250b_ARID1

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   METGLYSERSERTHRTHRTHRGLYGLULYS
2   ILETHRLYSVALTYRGLULEUGLYASNGLU
3   PROGLUARGLYSLEUTRPVALASPARGTYR
4   LEUTHRPHEMETGLUGLUARGGLYSERPRO
5   VALSERSERLEUPROALAVALGLYLYSLYS
6   PROLEUASPLEUPHEARGLEUTYRVALCYS
7   VALLYSGLUILEGLYGLYLEUALAGLNVAL
8   ASNLYSASNLYSLYSTRPARGGLULEUALA
9   THRASNLEUASNVALGLYTHRSERSERSER
10   ALAALASERSERLEULYSLYSGLNTYRILE
11   GLNTYRLEUPHEALAPHEGLUCYSLYSILE
12   GLUARGGLYGLUGLUPROPROPROGLUVAL
13   PHESERTHRGLYASPTHRLEUGLUHISHIS
14   HISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_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