BMRB Entry 53369

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53369

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Title:
GHR-ICD(270-620)
Deposition date:
2025-09-23
Original release date:
2025-10-22
Authors:
Nikolajsen, Louise; Seiffert, Pernille; Sieme, Daniel; Kragelund, Birthe Brandt
Citation:

Citation: Haxholm, Gitte; Nikolajsen, Louise; Olsen, Johan; Fredsted, Jacob; Larsen, Flemming; Goffin, Vincent; Pedersen, Stine; Brooks, Andrew; Waters, Michael; Kragelund, Birthe. "Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes."  Biochem. J. 468, 495-506 (2015).
PubMed: 25846210

Assembly members:

Assembly members:
entity_1, polymer, 351 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SKQQRIKMLILPPVPVPKIK GIDPDLLKEGKLEEVNTILA IHDSYKPEFHSDDSWVEFIE LDIDEPDEKTEESDTDRLLS SDHEKSHSNLGVKDGDSGRT SCCEPDILETDFNANDIHEG TSEVAQPQRLKGEADLLCLD QKNQNNSPYHDACPATQQPS VIQAEKNKPQPLPTEGAEST HQAAHIQLSNPSSLSNIDFY AQVSDITPAGSVVLSPGQKN KAGMSQCDMHPEMVSLCQEN FLMDNAYFCEADAKKCIPVA PHIKVESHIQPSLNQEDIYI TTESLTTAAGRPGTGEHVPG SEMPVPDYTSIHIVQSPQGL ILNATALPLPDKEFLSSCGY VSTDQLNKIMP

Data sets:
Data typeCount
13C chemical shifts978
15N chemical shifts339
1H chemical shifts316

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GHR1

Entities:

Entity 1, GHR 351 residues - Formula weight is not available

1   SERLYSGLNGLNARGILELYSMETLEUILE
2   LEUPROPROVALPROVALPROLYSILELYS
3   GLYILEASPPROASPLEULEULYSGLUGLY
4   LYSLEUGLUGLUVALASNTHRILELEUALA
5   ILEHISASPSERTYRLYSPROGLUPHEHIS
6   SERASPASPSERTRPVALGLUPHEILEGLU
7   LEUASPILEASPGLUPROASPGLULYSTHR
8   GLUGLUSERASPTHRASPARGLEULEUSER
9   SERASPHISGLULYSSERHISSERASNLEU
10   GLYVALLYSASPGLYASPSERGLYARGTHR
11   SERCYSCYSGLUPROASPILELEUGLUTHR
12   ASPPHEASNALAASNASPILEHISGLUGLY
13   THRSERGLUVALALAGLNPROGLNARGLEU
14   LYSGLYGLUALAASPLEULEUCYSLEUASP
15   GLNLYSASNGLNASNASNSERPROTYRHIS
16   ASPALACYSPROALATHRGLNGLNPROSER
17   VALILEGLNALAGLULYSASNLYSPROGLN
18   PROLEUPROTHRGLUGLYALAGLUSERTHR
19   HISGLNALAALAHISILEGLNLEUSERASN
20   PROSERSERLEUSERASNILEASPPHETYR
21   ALAGLNVALSERASPILETHRPROALAGLY
22   SERVALVALLEUSERPROGLYGLNLYSASN
23   LYSALAGLYMETSERGLNCYSASPMETHIS
24   PROGLUMETVALSERLEUCYSGLNGLUASN
25   PHELEUMETASPASNALATYRPHECYSGLU
26   ALAASPALALYSLYSCYSILEPROVALALA
27   PROHISILELYSVALGLUSERHISILEGLN
28   PROSERLEUASNGLNGLUASPILETYRILE
29   THRTHRGLUSERLEUTHRTHRALAALAGLY
30   ARGPROGLYTHRGLYGLUHISVALPROGLY
31   SERGLUMETPROVALPROASPTYRTHRSER
32   ILEHISILEVALGLNSERPROGLNGLYLEU
33   ILELEUASNALATHRALALEUPROLEUPRO
34   ASPLYSGLUPHELEUSERSERCYSGLYTYR
35   VALSERTHRASPGLNLEUASNLYSILEMET
36   PRO

Samples:

sample_1: GHR(270-620) 0.65 mM; D2O 5%; DSS 500 uM; sodium phosphate 20 mM; TCEP 6.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.3; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

POKY v20240829 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

Related Database Links:

UNP P10912

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