BMRB Entry 50627

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50627

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Title:
Backbone chemical shift assignments for the D2 translational isoform of the human glucocorticoid receptor
Deposition date:
2020-12-09
Original release date:
2021-05-07
Authors:
Grasso, Emily; Majumdar, Ananya; Wrabl, James; Frueh, Dominique; Hilser, Vincent
Citation:

Citation: Grasso, Emily; Majumdar, Ananya; Wrabl, James; Frueh, Dominique; Hilser, Vincent. "Conserved allosteric ensembles in a disordered protein using TROSY/Anti-TROSY R 2-filtered spectroscopy"  Biophys. J. 120, 2498-2510 (2021).
PubMed: 33901472

Assembly members:

Assembly members:
entity_1, polymer, 198 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 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   Vector: pj411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMYHYDMNTASLSQQQDQ KPIFNVIPPIPVGSENWNRC QGSGDDNLTSLGTLNFPGRT VFSNGYSSPSMRPDVSSPPS SSSTATTGPPPKLCLVCSDE ASGCHYGVLTCGSCKVFFKR AVEGQHNYLCAGRNDCIIDK IRRKNCPACRYRKCLQAGMN LEARKTKKKIKGIQQATTGV SQETSENPGNKTIVPATL

Data sets:
Data typeCount
13C chemical shifts433
15N chemical shifts171
1H chemical shifts171

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1
2zinc 12
3zinc 22

Entities:

Entity 1, protein 198 residues - Formula weight is not available

The initial 3 amino acids remain after cleavage of N-terminal his tag; residue 331 is the initial M in the sequence.

1   GLYSERHISMETTYRHISTYRASPMETASN
2   THRALASERLEUSERGLNGLNGLNASPGLN
3   LYSPROILEPHEASNVALILEPROPROILE
4   PROVALGLYSERGLUASNTRPASNARGCYS
5   GLNGLYSERGLYASPASPASNLEUTHRSER
6   LEUGLYTHRLEUASNPHEPROGLYARGTHR
7   VALPHESERASNGLYTYRSERSERPROSER
8   METARGPROASPVALSERSERPROPROSER
9   SERSERSERTHRALATHRTHRGLYPROPRO
10   PROLYSLEUCYSLEUVALCYSSERASPGLU
11   ALASERGLYCYSHISTYRGLYVALLEUTHR
12   CYSGLYSERCYSLYSVALPHEPHELYSARG
13   ALAVALGLUGLYGLNHISASNTYRLEUCYS
14   ALAGLYARGASNASPCYSILEILEASPLYS
15   ILEARGARGLYSASNCYSPROALACYSARG
16   TYRARGLYSCYSLEUGLNALAGLYMETASN
17   LEUGLUALAARGLYSTHRLYSLYSLYSILE
18   LYSGLYILEGLNGLNALATHRTHRGLYVAL
19   SERGLNGLUTHRSERGLUASNPROGLYASN
20   LYSTHRILEVALPROALATHRLEU

Entity 2, zinc 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: D2DBD monomer, [U-13C; U-15N], 150 uM; sodium chloride 100 mM; sodium phosphate 20 mM; TCEP 5 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.16 M; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY - data analysis

TOPSPIN - collection

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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