BMRB Entry 27843

Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the ligand-binding domain of human ionotropic glutamate receptor 2 complexed with kainate
Deposition date:
2019-03-19
Original release date:
2019-09-26
Authors:
Sakakura, Masayoshi; Ohkubo, Yumi; Oshima, Hiraku; Re, Suyong; Ito, Masahiro; Sugita, Yuij; Takahashi, Hideo
Citation:

Citation: Sakakura, Masayoshi; Ohkubo, Yumi; Oshima, Hiraku; Re, Suyong; Ito, Masahiro; Sugita, Yuij; Takahashi, Hideo. "Structural Mechanisms Underlying Activity Changes in an AMPA-type Glutamate Receptor Induced by Substitutions in Its Ligand-Binding Domain"  Structure 27, 1698-1709 (2019).
PubMed: 31585769

Assembly members:

Assembly members:
hGluR2-LBD, polymer, 263 residues, 29236.77 Da.
3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE, non-polymer, 213.230 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: pET15b

Data sets:
Data typeCount
13C chemical shifts488
15N chemical shifts252
1H chemical shifts252

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hGluR2-LBD1
2kainate2

Entities:

Entity 1, hGluR2-LBD 263 residues - 29236.77 Da.

1   GLYALAASNLYSTHRVALVALVALTHRTHR
2   ILELEUGLUSERPROTYRVALMETMETLYS
3   LYSASNHISGLUMETLEUGLUGLYASNGLU
4   ARGTYRGLUGLYTYRCYSVALASPLEUALA
5   ALAGLUILEALALYSHISCYSGLYPHELYS
6   TYRLYSLEUTHRILEVALGLYASPGLYLYS
7   TYRGLYALAARGASPALAASPTHRLYSILE
8   TRPASNGLYMETVALGLYGLULEUVALTYR
9   GLYLYSALAASPILEALAILEALAPROLEU
10   THRILETHRLEUVALARGGLUGLUVALILE
11   ASPPHESERLYSPROPHEMETSERLEUGLY
12   ILESERILEMETILELYSLYSGLYTHRPRO
13   ILEGLUSERALAGLUASPLEUSERLYSGLN
14   THRGLUILEALATYRGLYTHRLEUASPSER
15   GLYSERTHRLYSGLUPHEPHEARGARGSER
16   LYSILEALAVALPHEASPLYSMETTRPTHR
17   TYRMETARGSERALAGLUPROSERVALPHE
18   VALARGTHRTHRALAGLUGLYVALALAARG
19   VALARGLYSSERLYSGLYLYSTYRALATYR
20   LEULEUGLUSERTHRMETASNGLUTYRILE
21   GLUGLNARGLYSPROCYSASPTHRMETLYS
22   VALGLYGLYASNLEUASPSERLYSGLYTYR
23   GLYILEALATHRPROLYSGLYSERSERLEU
24   ARGTHRPROVALASNLEUALAVALLEULYS
25   LEUSERGLUGLNGLYVALLEUASPLYSLEU
26   LYSASNLYSTRPTRPTYRASPLYSGLYGLU
27   CYSGLYALA

Entity 2, kainate - C10 H15 N O4 - 213.230 Da.

1   KAI

Samples:

sample_1: hGluR2-LBD, [U-13C; U-15N], 0.19 mM; kainate 2.9 mM; acetic acid 10.1 mM; sodium acetate 13.9 mM; sodium chloride 24 mM

sample_conditions_1: ionic strength: 0.038 M; pH: 4.9; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.038 M; pH: 4.9; pressure: 1 atm; temperature: 300.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_2
3D HN(CO)CAsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2
3D CBCA(CO)NHsample_1isotropicsample_conditions_2

Software:

TOPSPIN v3.2, Bruker Biospin - collection

NMRPipe v2012.090.12.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.134, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

Related Database Links:

NCBI NP_000817.2

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