BMRB Entry 16394

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16394

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Title:
NMR Evidence for differential phosphorylation-dependent interactions in WT and deltaF508 CFTR
Deposition date:
2009-07-03
Original release date:
2009-12-14
Authors:
Kanelis, Voula; Hudson, Rhea; Thibodeau, Patrick; Thomas, Philip; Forman-Kay, Julie
Citation:

Citation: Kanelis, Voula; Hudson, Rhea; Thibodeau, Patrick; Thomas, Philip; Forman-Kay, Julie. "NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR."  EMBO J. 29, 263-277 (2010).
PubMed: 19927121

Assembly members:

Assembly members:
deltaF508 CFTR NBD1-RE, polymer, 284 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-His-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
deltaF508 CFTR NBD1-RE: TTGIIMENVTAFWEEGFGEL LEKVQQSNGDRKHSSDENNV SFSHLCLVGNPVLKNINLNI EKGEMLAITGSTGSGKTSLL MLILGELEASEGIIKHSGRV SFCSQFSWIMPGTIKENIIG VSYDEYRYKSVVKACQLQQD ITKFAEQDNTVLGEGGVTLS GGQRARISLARAVYKDADLY LLDSPFGYLDVFTEEQVFES CVCKLMANKTRILVTSKMEH LRKADKILILHQGSSYFYGT FSELQSLRPDFSSKLMGYDT FDQFTEERRSSILTETLRRF SVDD

Data sets:
Data typeCount
15N chemical shifts114
1H chemical shifts114

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1deltaF508 CFTR NBD1-RE1

Entities:

Entity 1, deltaF508 CFTR NBD1-RE 284 residues - Formula weight is not available

1   THRTHRGLYILEILEMETGLUASNVALTHR
2   ALAPHETRPGLUGLUGLYPHEGLYGLULEU
3   LEUGLULYSVALGLNGLNSERASNGLYASP
4   ARGLYSHISSERSERASPGLUASNASNVAL
5   SERPHESERHISLEUCYSLEUVALGLYASN
6   PROVALLEULYSASNILEASNLEUASNILE
7   GLULYSGLYGLUMETLEUALAILETHRGLY
8   SERTHRGLYSERGLYLYSTHRSERLEULEU
9   METLEUILELEUGLYGLULEUGLUALASER
10   GLUGLYILEILELYSHISSERGLYARGVAL
11   SERPHECYSSERGLNPHESERTRPILEMET
12   PROGLYTHRILELYSGLUASNILEILEGLY
13   VALSERTYRASPGLUTYRARGTYRLYSSER
14   VALVALLYSALACYSGLNLEUGLNGLNASP
15   ILETHRLYSPHEALAGLUGLNASPASNTHR
16   VALLEUGLYGLUGLYGLYVALTHRLEUSER
17   GLYGLYGLNARGALAARGILESERLEUALA
18   ARGALAVALTYRLYSASPALAASPLEUTYR
19   LEULEUASPSERPROPHEGLYTYRLEUASP
20   VALPHETHRGLUGLUGLNVALPHEGLUSER
21   CYSVALCYSLYSLEUMETALAASNLYSTHR
22   ARGILELEUVALTHRSERLYSMETGLUHIS
23   LEUARGLYSALAASPLYSILELEUILELEU
24   HISGLNGLYSERSERTYRPHETYRGLYTHR
25   PHESERGLULEUGLNSERLEUARGPROASP
26   PHESERSERLYSLEUMETGLYTYRASPTHR
27   PHEASPGLNPHETHRGLUGLUARGARGSER
28   SERILELEUTHRGLUTHRLEUARGARGPHE
29   SERVALASPASP

Samples:

sample_1: deltaF508 CFTR NBD1-RE, [U-100% 15N], 175 mM; sodium phosphate 20 mM; sodium chloride 150 mM; magnesium chloride 5 mM; ATP 5 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 170 mM; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16367 16393
PDB

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