BMRB Entry 27840

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27840

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

Citation: Sakakura, Masayoshi; Ohkubo, Yumi; Oshima, Hiraku; Re, Suyong; Ito, Masahiro; Sugita, Yuji; 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.
entity_GLU, non-polymer, 147.129 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hGluR2-LBD: GANKTVVVTTILESPYVMMK KNHEMLEGNERYEGYCVDLA AEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVY GKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKGTP IESAEDLSKQTEIAYGTLDS GSTKEFFRRSKIAVFDKMWT YMRSAEPSVFVRTTAEGVAR VRKSKGKYAYLLESTMNEYI EQRKPCDTMKVGGNLDSKGY GIATPKGSSLRTPVNLAVLK LSEQGVLDKLKNKWWYDKGE CGA

Data sets:
Data typeCount
13C chemical shifts732
15N chemical shifts250
1H chemical shifts250

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hGluR2-LBD1
2glutamate2

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, glutamate - C5 H9 N O4 - 147.129 Da.

1   GLU

Samples:

sample_1: hGluR2-LBD, [U-13C; U-15N], 0.3 mM; glutamate 2.9 mM; acetic acid 7.5 mM; sodium acetate 16.5 mM; sodium chloride 24 mM

sample_conditions_1: ionic strength: 0.041 M; pH: 5.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

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

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