BMRB Entry 26615

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26615

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Title:
Backbone resonance assignments for rat SUR2A NBD1
Deposition date:
2015-07-16
Original release date:
2015-09-29
Authors:
de Araujo, Elvin; Kanelis, Voula
Citation:

Citation: de Araujo, Elvin; Alvarez, Claudia; Lopez-Alonso, Jorge; Sooklal, Clarissa; Stagljar, Marijana; Kanelis, Voula. "Phosphorylation-dependent Changes in Nucleotide Binding, Conformation, and Dynamics of the First Nucleotide Binding Domain (NBD1) of the Sulfonylurea Receptor 2B (SUR2B)"  J. Biol. Chem. 290, 22699-22714 (2015).
PubMed: 26198630

Assembly members:

Assembly members:
SUR2A_NBD1-deltaN, polymer, 274 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Norway   Taxonomy ID: 10116   Superkingdom: not available   Kingdom: Eukaryota   Genus/species: Metazoa Rattus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: na

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SUR2A_NBD1-deltaN: TGSMGDVAIKVTNGYFSWGS GLATLSNIDIRIPTGQLTMI VGQVGCGKSSLLLAILGEMQ TLEGKVYWNNVNESEPSFEA TRSRSRYSVAYAAQKPWLLN ATVEENITFGSSFNRQRYKA VTDACSLQPDIDLLPFGDQT EIGERGINLSGGQRQRICVA RALYQNTNIVFLDDPFSALD IHLSDHLMQEGILKFLQDDK RTVVLVTHKLQYLTHADWII AMKDGSVLREGTLKDIQTKD VELYEHWKTLMNRQDQELEK DMEADQTTLERKTL

Data sets:
Data typeCount
13C chemical shifts490
15N chemical shifts340
1H chemical shifts340

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NBD1-deltaN1

Entities:

Entity 1, NBD1-deltaN 274 residues - Formula weight is not available

The natural sequence of SUR2A NBD1-delta N begins at D665, which is the 6th residue in the sequence above. Residues T660-G664 are vector-derived amino acids.

1   THRGLYSERMETGLYASPVALALAILELYS
2   VALTHRASNGLYTYRPHESERTRPGLYSER
3   GLYLEUALATHRLEUSERASNILEASPILE
4   ARGILEPROTHRGLYGLNLEUTHRMETILE
5   VALGLYGLNVALGLYCYSGLYLYSSERSER
6   LEULEULEUALAILELEUGLYGLUMETGLN
7   THRLEUGLUGLYLYSVALTYRTRPASNASN
8   VALASNGLUSERGLUPROSERPHEGLUALA
9   THRARGSERARGSERARGTYRSERVALALA
10   TYRALAALAGLNLYSPROTRPLEULEUASN
11   ALATHRVALGLUGLUASNILETHRPHEGLY
12   SERSERPHEASNARGGLNARGTYRLYSALA
13   VALTHRASPALACYSSERLEUGLNPROASP
14   ILEASPLEULEUPROPHEGLYASPGLNTHR
15   GLUILEGLYGLUARGGLYILEASNLEUSER
16   GLYGLYGLNARGGLNARGILECYSVALALA
17   ARGALALEUTYRGLNASNTHRASNILEVAL
18   PHELEUASPASPPROPHESERALALEUASP
19   ILEHISLEUSERASPHISLEUMETGLNGLU
20   GLYILELEULYSPHELEUGLNASPASPLYS
21   ARGTHRVALVALLEUVALTHRHISLYSLEU
22   GLNTYRLEUTHRHISALAASPTRPILEILE
23   ALAMETLYSASPGLYSERVALLEUARGGLU
24   GLYTHRLEULYSASPILEGLNTHRLYSASP
25   VALGLULEUTYRGLUHISTRPLYSTHRLEU
26   METASNARGGLNASPGLNGLULEUGLULYS
27   ASPMETGLUALAASPGLNTHRTHRLEUGLU
28   ARGLYSTHRLEU

Samples:

sample_1: SUR2A NBD1-deltaN, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; glycerol 2%; DTT 5 mM; MgATP 5 mM; DSS 1 mM; H2O 90%; D2O 10%

sample_2: SUR2A NBD1-deltaN 0.25 mM; sodium phosphate 20 mM; sodium chloride 150 mM; glycerol 2%; DTT 2 mM; MgATP 2 mM; DSS 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 170 mM; pH: 7.3; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY-HSQCsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY-HN(COCA)CBsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N TROSY-HSQCsample_2isotropicsample_conditions_2

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

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

VNMRJ, Varian - collection

NMR spectrometers:

  • Agilent INOVA 800 MHz
  • Agilent INOVA 600 MHz

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