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 26756

Title: 1H, 13C, 15N backbone and 1H, 13C methionine methyl chemical shifts of human wildtype Glucocorticoid receptor Ligand Binding Domain   PubMed: 29667121

Deposition date: 2016-03-11 Original release date: 2018-06-27

Authors: Kohler, Christian; Weininger, Ulrich; Backstrom, Stefan; Carlstrom, Goran; Lepisto, Matti; Papavoine, Tineke; Edman, Karl; Akke, Mikael

Citation: Kohler, Christian; Carlstrom, Goran; Tangefjord, Stefan; Papavoine, Tineke; Lepisto, Matti; Edman, Karl; Akke, Mikael. "Backbone 1H, 13C, and 15N resonance assignments of the ligand binding domain of the human wildtype glucocorticoid receptor and the F602S mutant variant"  Biomol. NMR Assign. 12, 263-268 (2018).

Assembly members:
Glucocorticoid_Receptor_Ligand_Binding_Domain, polymer, 250 residues, 29078.9 Da.
TIF-2_Nuclear_coactivator_2, polymer, 14 residues, 1705.9 Da.
entity_DEX, non-polymer, 392.461 Da.
entity_CPS, non-polymer, 614.877 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

Entity Sequences (FASTA):
Glucocorticoid_Receptor_Ligand_Binding_Domain: GTPTLVSLLEVIEPEVLYAG YDSSVPDSYWRIMTTLNMLG GRQVIAAVKWAKAIPGFRNL HLDDQMTLLQYSWMFLMAFA LGWRSYRQSSANLLCFAPDL IINEQRMTLPCMYDQCKHML YVSSELHRLQVSYEEYLCMK TLLLLSSVPKDGLKSQELFD EIRMTYIKELGKAIVKREGN SSQNWQRFYQLTKLLDSMHE VVENLLNYCFQTFLDKTMSI EFPEMLAEIITNQIPKYSNG NIKKLLFHQK
TIF-2_Nuclear_coactivator_2: KENALLRYLLDKDD

Data sets:
Data typeCount
13C chemical shifts462
15N chemical shifts221
1H chemical shifts260

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Glucocorticoid Receptor Ligand Binding Domain, 11
2Dexamethasone, 13
3TIF-2 Nuclear coactivator 2, 12
4CHAPS, 14
5Glucocorticoid Receptor Ligand Binding Domain, 21
6Dexamethasone, 23
7TIF-2 Nuclear coactivator 2, 22
8CHAPS, 24

Entities:

Entity 1, Glucocorticoid Receptor Ligand Binding Domain, 1 250 residues - 29078.9 Da.

First Gly remains from purification tag

1   GLYTHRPROTHRLEUVALSERLEULEUGLU
2   VALILEGLUPROGLUVALLEUTYRALAGLY
3   TYRASPSERSERVALPROASPSERTYRTRP
4   ARGILEMETTHRTHRLEUASNMETLEUGLY
5   GLYARGGLNVALILEALAALAVALLYSTRP
6   ALALYSALAILEPROGLYPHEARGASNLEU
7   HISLEUASPASPGLNMETTHRLEULEUGLN
8   TYRSERTRPMETPHELEUMETALAPHEALA
9   LEUGLYTRPARGSERTYRARGGLNSERSER
10   ALAASNLEULEUCYSPHEALAPROASPLEU
11   ILEILEASNGLUGLNARGMETTHRLEUPRO
12   CYSMETTYRASPGLNCYSLYSHISMETLEU
13   TYRVALSERSERGLULEUHISARGLEUGLN
14   VALSERTYRGLUGLUTYRLEUCYSMETLYS
15   THRLEULEULEULEUSERSERVALPROLYS
16   ASPGLYLEULYSSERGLNGLULEUPHEASP
17   GLUILEARGMETTHRTYRILELYSGLULEU
18   GLYLYSALAILEVALLYSARGGLUGLYASN
19   SERSERGLNASNTRPGLNARGPHETYRGLN
20   LEUTHRLYSLEULEUASPSERMETHISGLU
21   VALVALGLUASNLEULEUASNTYRCYSPHE
22   GLNTHRPHELEUASPLYSTHRMETSERILE
23   GLUPHEPROGLUMETLEUALAGLUILEILE
24   THRASNGLNILEPROLYSTYRSERASNGLY
25   ASNILELYSLYSLEULEUPHEHISGLNLYS

Entity 3, Dexamethasone, 1 - C22 H29 F O5 - 392.461 Da.

1   DEX

Entity 2, TIF-2 Nuclear coactivator 2, 1 14 residues - 1705.9 Da.

Nuclear coactivator 2

1   LYSGLUASNALALEULEUARGTYRLEULEU
2   ASPLYSASPASP

Entity 4, CHAPS, 1 - C32 H58 N2 O7 S - 614.877 Da.

1   CPS

Samples:

sample_1: Glucocorticoid Receptor Ligand Binding Domain, [U-13C; U-15N; U-2H], 0.3 mM; Dexamethasone 50 uM; CHAPS 1%; TIF-2 Nuclear coactivator 2 0.3 mM; potassium phosphate 20 mM; DTT 2 mM; sodium azide 0.02%

sample_2: Glucocorticoid Receptor Ligand Binding Domain, L-methionine (methyl-13C), 0.3 mM; Dexamethasone 50 uM; CHAPS 1%; TIF-2 Nuclear coactivator 2 0.3 mM; potassium phosphate 20 mM; DTT 2 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.12 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP P04150
NCBI NP_000167.1

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