BMRB Entry 11067

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11067

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Title:
Backbone resonance assignments for the cytoplasmic regions of G protein-activated inwardly rectifying potassium channel1 (GIRK1)
Deposition date:
2009-02-07
Original release date:
2009-04-16
Authors:
Yokogawa, Mariko; Muramatsu, Takahiro; Takeuchi, Koh; Osawa, Masanori; Shimada, Ichio
Citation:

Citation: Yokogawa, Mariko; Muramatsu, Takahiro; Takeuchi, Koh; Osawa, Masanori; Shimada, Ichio. "Backbone resonance assignments for the cytoplasmic regions of G protein-activated inwardly rectifying potassium channel 1 (GIRK1)"  Biomol. NMR Assignments 3, 125-128 (2009).
PubMed: 19636962

Assembly members:

Assembly members:
GIRK1 subunit, polymer, 211 residues, 24100 Da.

Natural source:

Natural source:   Common Name: mouse   Taxonomy ID: not available   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24d(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GIRK1 subunit: GPDDHMKKRQRFVDKNGRCN VQHGNLGSERAETLMFSEHA VISMRDGKLTLMFRVGNLRN SHMVSAQIRCKLLKSRQTPE GEFLPLDQLELDVGFSTGAD QLFLVSPLTICHVIDAKSPF YDLSQRSMQTEQFEVVVILE GIVETTGMTCQARTSYTEDE VLWGHRFFPVISLEEGFFKV DYSQFHATFEVPTPPYSVKE QEEMLLMSSPL

Data sets:
Data typeCount
13C chemical shifts578
15N chemical shifts187
1H chemical shifts187

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GIRK1 subunit 11
2GIRK1 subunit 21
3GIRK1 subunit 31
4GIRK1 subunit 41

Entities:

Entity 1, GIRK1 subunit 1 211 residues - 24100 Da.

Residues 1-6 represent a non-native affinity tag related segments. This is the cytoplasmic globular regions of a membrane protein.

1   GLYPROASPASPHISMETLYSLYSARGGLN
2   ARGPHEVALASPLYSASNGLYARGCYSASN
3   VALGLNHISGLYASNLEUGLYSERGLUARG
4   ALAGLUTHRLEUMETPHESERGLUHISALA
5   VALILESERMETARGASPGLYLYSLEUTHR
6   LEUMETPHEARGVALGLYASNLEUARGASN
7   SERHISMETVALSERALAGLNILEARGCYS
8   LYSLEULEULYSSERARGGLNTHRPROGLU
9   GLYGLUPHELEUPROLEUASPGLNLEUGLU
10   LEUASPVALGLYPHESERTHRGLYALAASP
11   GLNLEUPHELEUVALSERPROLEUTHRILE
12   CYSHISVALILEASPALALYSSERPROPHE
13   TYRASPLEUSERGLNARGSERMETGLNTHR
14   GLUGLNPHEGLUVALVALVALILELEUGLU
15   GLYILEVALGLUTHRTHRGLYMETTHRCYS
16   GLNALAARGTHRSERTYRTHRGLUASPGLU
17   VALLEUTRPGLYHISARGPHEPHEPROVAL
18   ILESERLEUGLUGLUGLYPHEPHELYSVAL
19   ASPTYRSERGLNPHEHISALATHRPHEGLU
20   VALPROTHRPROPROTYRSERVALLYSGLU
21   GLNGLUGLUMETLEULEUMETSERSERPRO
22   LEU

Samples:

sample_1: mGIRK1cp subunit, [U-13C; U-15N; U-2H], 2 mM; HEPES 10 mM; DTT 10 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 15N-edited NOESY-TROSYsample_1isotropicsample_conditions_1

Software:

SPARKY vv3.114, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN vv2.1, Bruker Biospin - collection, processing

xwinnmr vv3.5, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAG57305
GB AAB63355 EHB07269 EMC85247 KFO85024 KFP72020
REF XP_005007746 XP_005139441 XP_005432727 XP_005495069 XP_005601545

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