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 16393

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16393

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Title: NMR Evidence for differential phosphorylation-dependent interactions in WT and deltaF508 CFTR   PubMed: 19927121

Deposition date: 2009-07-03 Original release date: 2009-12-11

Authors: Kanelis, Voula; Hudson, Rhea; Thibodeau, Patrick; Thomas, Philip; Forman-Kay, Julie

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).

Assembly members:
CFTR NBD1-RE, polymer, 285 residues, 31994.5 Da.

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

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

Entity Sequences (FASTA):
CFTR NBD1-RE: TTGIIMENVTAFWEEGFGEL LEKVQQSNGDRKHSSDENNV SFSHLCLVGNPVLKNINLNI EKGEMLAITGSTGSGKTSLL MLILGELEASEGIIKHSGRV SFCSQFSWIMPGTIKENIIF GVSYDEYRYKSVVKACQLQQ DITKFAEQDNTVLGEGGVTL SGGQRARISLARAVYKDADL YLLDSPFGYLDVFTEEQVFE SCVCKLMANKTRILVTSKME HLRKADKILILHQGSSYFYG TFSELQSLRPDFSSKLMGYD TFDQFTEERRSSILTETLRR FSVDD

Data sets:
Data typeCount
13C chemical shifts166
15N chemical shifts170
1H chemical shifts170

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CFTR NBD1-RE1

Entities:

Entity 1, CFTR NBD1-RE 285 residues - 31994.5 Da.

This protein comprises residues T389-D673 of WT murine CFTR

1   THRTHRGLYILEILEMETGLUASNVALTHR
2   ALAPHETRPGLUGLUGLYPHEGLYGLULEU
3   LEUGLULYSVALGLNGLNSERASNGLYASP
4   ARGLYSHISSERSERASPGLUASNASNVAL
5   SERPHESERHISLEUCYSLEUVALGLYASN
6   PROVALLEULYSASNILEASNLEUASNILE
7   GLULYSGLYGLUMETLEUALAILETHRGLY
8   SERTHRGLYSERGLYLYSTHRSERLEULEU
9   METLEUILELEUGLYGLULEUGLUALASER
10   GLUGLYILEILELYSHISSERGLYARGVAL
11   SERPHECYSSERGLNPHESERTRPILEMET
12   PROGLYTHRILELYSGLUASNILEILEPHE
13   GLYVALSERTYRASPGLUTYRARGTYRLYS
14   SERVALVALLYSALACYSGLNLEUGLNGLN
15   ASPILETHRLYSPHEALAGLUGLNASPASN
16   THRVALLEUGLYGLUGLYGLYVALTHRLEU
17   SERGLYGLYGLNARGALAARGILESERLEU
18   ALAARGALAVALTYRLYSASPALAASPLEU
19   TYRLEULEUASPSERPROPHEGLYTYRLEU
20   ASPVALPHETHRGLUGLUGLNVALPHEGLU
21   SERCYSVALCYSLYSLEUMETALAASNLYS
22   THRARGILELEUVALTHRSERLYSMETGLU
23   HISLEUARGLYSALAASPLYSILELEUILE
24   LEUHISGLNGLYSERSERTYRPHETYRGLY
25   THRPHESERGLULEUGLNSERLEUARGPRO
26   ASPPHESERSERLYSLEUMETGLYTYRASP
27   THRPHEASPGLNPHETHRGLUGLUARGARG
28   SERSERILELEUTHRGLUTHRLEUARGARG
29   PHESERVALASPASP

Samples:

sample_1: WT CFTR NBD1-RE, [U-100% 13C; U-100% 15N], 400 uM; sodium phosphate 20 mM; sodium chloride 150 mM; magnesium chloride 5 mM; ATP 5 mM; DTT 5 mM; D2O 10%; H2O 90%

sample_2: WT CFTR NBD1-RE, [U-100% 13C; U-100% 15N; 50% 2H], 500 mM; sodium phosphate 20 mM; sodium chloride 150 mM; magnesium chloride 5 mM; ATP 5 mM; DTT 5 mM; D2O 10%; H2O 90%

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
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1

Software:

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

NMRDraw, 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 16394
PDB

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