BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 50628

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50628

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Title: Backbone chemical shift assignments for the D1 translational isoform of the human glucocorticoid receptor   PubMed: 33901472

Deposition date: 2020-12-09 Original release date: 2021-05-07

Authors: Grasso, Emily; Majumdar, Ananya; Wrabl, James; Frueh, Dominique; Hilser, Vincent

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).

Assembly members:
entity_1, polymer, 213 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

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: pj411

Entity Sequences (FASTA):
entity_1: GSHMSAISVHGVSTSGGQMY HYDMNTASLSQQQDQKPIFN VIPPIPVGSENWNRCQGSGD DNLTSLGTLNFPGRTVFSNG YSSPSMRPDVSSPPSSSSTA TTGPPPKLCLVCSDEASGCH YGVLTCGSCKVFFKRAVEGQ HNYLCAGRNDCIIDKIRRKN CPACRYRKCLQAGMNLEARK TKKKIKGIQQATTGVSQETS ENPGNKTIVPATL

Data sets:
Data typeCount
13C chemical shifts406
15N chemical shifts182
1H chemical shifts182

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 213 residues - Formula weight is not available

The initial 3 amino acids remain after cleavage of N-terminal his tag; residue 316 is the initial M in the sequence.

1   GLYSERHISMETSERALAILESERVALHIS
2   GLYVALSERTHRSERGLYGLYGLNMETTYR
3   HISTYRASPMETASNTHRALASERLEUSER
4   GLNGLNGLNASPGLNLYSPROILEPHEASN
5   VALILEPROPROILEPROVALGLYSERGLU
6   ASNTRPASNARGCYSGLNGLYSERGLYASP
7   ASPASNLEUTHRSERLEUGLYTHRLEUASN
8   PHEPROGLYARGTHRVALPHESERASNGLY
9   TYRSERSERPROSERMETARGPROASPVAL
10   SERSERPROPROSERSERSERSERTHRALA
11   THRTHRGLYPROPROPROLYSLEUCYSLEU
12   VALCYSSERASPGLUALASERGLYCYSHIS
13   TYRGLYVALLEUTHRCYSGLYSERCYSLYS
14   VALPHEPHELYSARGALAVALGLUGLYGLN
15   HISASNTYRLEUCYSALAGLYARGASNASP
16   CYSILEILEASPLYSILEARGARGLYSASN
17   CYSPROALACYSARGTYRARGLYSCYSLEU
18   GLNALAGLYMETASNLEUGLUALAARGLYS
19   THRLYSLYSLYSILELYSGLYILEGLNGLN
20   ALATHRTHRGLYVALSERGLNGLUTHRSER
21   GLUASNPROGLYASNLYSTHRILEVALPRO
22   ALATHRLEU

Entity 2, zinc 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: D1DBD monomer, [U-13C; U-15N], 152 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
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CA)Nsample_1isotropicsample_conditions_1

Software:

SPARKY - data analysis

TOPSPIN - collection

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE II 600 MHz

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