BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 28048

Title: Chemical Shift Assignments for BRG1 ATBD   PubMed: 32376391

Deposition date: 2019-11-25 Original release date: 2020-01-10

Authors: Sanchez, Julio

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).

Assembly members:
BRG1_ATBD, polymer, 141 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX

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

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts113
1H chemical shifts252

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ATBD1

Entities:

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

1   GLYPROLEUGLYSERASPASPGLUSERLYS
2   LYSGLNLYSLYSARGGLYARGPROPROALA
3   GLULYSLEUSERPROASNPROPROASNLEU
4   THRLYSLYSMETLYSLYSILEVALASPALA
5   VALILELYSTYRLYSASPSERSERSERGLY
6   ARGGLNLEUSERGLUVALPHEILEGLNLEU
7   PROSERARGLYSGLULEUPROGLUTYRTYR
8   GLULEUILEARGLYSPROVALASPPHELYS
9   LYSILELYSGLUARGILEARGASNHISLYS
10   TYRARGSERLEUASNASPLEUGLULYSASP
11   VALMETLEULEUCYSGLNASNALAGLNTHR
12   PHEASNLEUGLUGLYSERLEUILETYRGLU
13   ASPSERILEVALLEUGLNSERVALPHETHR
14   SERVALARGGLNLYSILEGLULYSGLUASP
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_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 shifts
SPARKY: Backbone or all simulated shifts