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 26746

Title: Backbone resonance assignment of an inhibitory G-alpha domain   PubMed: 27298341

Deposition date: 2016-02-14 Original release date: 2016-10-04

Authors: Hagn, Franz; Wagner, Gerhard; Goricanec, David; Stehle, Ralf; Egloff, Pascal; Grigori, Simina; Pl ckthun, Andreas

Citation: Goricanec, David; Stehle, Ralf; Egloff, Pascal; Grigoriu, Simina; Plueckthun, Andreas; Wagner, Gerhard; Hagn, Franz. "Conformational dynamics of a G-protein alpha subunit is tightly regulated by nucleotide binding"  Proc. Natl. Acad. Sci. U.S.A. 113, E3629-E3638 (2016).

Assembly members:
GNAI1, polymer, 326 residues, Formula weight is not available

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: pQE30

Entity Sequences (FASTA):
GNAI1: GASREVKLLLLGAGESGKST IVKQMKIIHEAGYSEEECKQ YKAVVYSNTIQSIIAIIRAM GRLKIDFGDSARADDARQLF VLAGAAEEGFMTAELAGVIK RLWKDSGVQACFNRSREYQL NDSAAYYLNDLDRIAQPNYI PTQQDVLRTRVKTTGIVETH FTFKDLHFKMFDVGGQRSER KKWIHCFEGVAAIIFCVALS DYDLVLAEDEEMNRMHESMK LFDSICNNKWFTDTSIILFL NKKDLFEEKIKKSPLTICYQ EYAGSNTYEEAAAYIQCQFE DLNKRKDTKEIYTHFTCATD TKNVQFVFDAVTDVIIKNNL KDCGLF

Data sets:
Data typeCount
13C chemical shifts962
15N chemical shifts282
1H chemical shifts283

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GNAI11

Entities:

Entity 1, GNAI1 326 residues - Formula weight is not available

1   GLYALASERARGGLUVALLYSLEULEULEU
2   LEUGLYALAGLYGLUSERGLYLYSSERTHR
3   ILEVALLYSGLNMETLYSILEILEHISGLU
4   ALAGLYTYRSERGLUGLUGLUCYSLYSGLN
5   TYRLYSALAVALVALTYRSERASNTHRILE
6   GLNSERILEILEALAILEILEARGALAMET
7   GLYARGLEULYSILEASPPHEGLYASPSER
8   ALAARGALAASPASPALAARGGLNLEUPHE
9   VALLEUALAGLYALAALAGLUGLUGLYPHE
10   METTHRALAGLULEUALAGLYVALILELYS
11   ARGLEUTRPLYSASPSERGLYVALGLNALA
12   CYSPHEASNARGSERARGGLUTYRGLNLEU
13   ASNASPSERALAALATYRTYRLEUASNASP
14   LEUASPARGILEALAGLNPROASNTYRILE
15   PROTHRGLNGLNASPVALLEUARGTHRARG
16   VALLYSTHRTHRGLYILEVALGLUTHRHIS
17   PHETHRPHELYSASPLEUHISPHELYSMET
18   PHEASPVALGLYGLYGLNARGSERGLUARG
19   LYSLYSTRPILEHISCYSPHEGLUGLYVAL
20   ALAALAILEILEPHECYSVALALALEUSER
21   ASPTYRASPLEUVALLEUALAGLUASPGLU
22   GLUMETASNARGMETHISGLUSERMETLYS
23   LEUPHEASPSERILECYSASNASNLYSTRP
24   PHETHRASPTHRSERILEILELEUPHELEU
25   ASNLYSLYSASPLEUPHEGLUGLULYSILE
26   LYSLYSSERPROLEUTHRILECYSTYRGLN
27   GLUTYRALAGLYSERASNTHRTYRGLUGLU
28   ALAALAALATYRILEGLNCYSGLNPHEGLU
29   ASPLEUASNLYSARGLYSASPTHRLYSGLU
30   ILETYRTHRHISPHETHRCYSALATHRASP
31   THRLYSASNVALGLNPHEVALPHEASPALA
32   VALTHRASPVALILEILELYSASNASNLEU
33   LYSASPCYSGLYLEUPHE

Samples:

sample_1: GNAI1, [U-13C; U-15N; U-2H], 200 – 400 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 5 mM; MgCl2 5 mM; GMPPNP 5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

GB BC026326

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