BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27672

Title: NMR backbone and methyl assignment of G-protein alpha i,1 subunit bound to GDP   PubMed: 30539422

Deposition date: 2018-10-31 Original release date: 2019-01-08

Authors: Goricanec, David; Hagn, Franz

Citation: Goricanec, David; Hagn, Franz. "NMR Backbone and Methyl Resonance Assignments of an inhibitory G-alpha subunit in complex with GDP"  Biomol. NMR Assignments 13, 131-137 (2019).

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

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 shifts794
15N chemical shifts230
1H chemical shifts231

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], 0.4 mM; GDP 5 mM; potassium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02%; D2O, [U-99% 2H], 5%; magnesium chloride 10 mM; DTT 5 mM

sample_2: GNAI1, [U- 2H; U-15N], ILVA, 0.2 mM; potassium phosphate 10 mM; sodium chloride 50 mM; D2O, [U-99% 2H], 5%; GDP 5 mM; DTT 5 mM; sodium azide 0.02%; magnesium chloride 10 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 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 HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

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

SPARKY vNMRFAM, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz

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