BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16367

Title: NMR Evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR   PubMed: 19927121

Deposition date: 2009-06-26 Original release date: 2009-12-11

Authors: Kanelis, Voula; Hudson, Rhea; Thibodeau, Patrick; Thomas, Phillip; 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_G550E/R553M/R555K, polymer, 285 residues, 32011.5 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   Vector: pET-His-SUMO

Entity Sequences (FASTA):
CFTR_NBD1-RE_G550E/R553M/R555K: TTGIIMENVTAFWEEGFGEL LEKVQQSNGDRKHSSDENNV SFSHLCLVGNPVLKNINLNI EKGEMLAITGSTGSGKTSLL MLILGELEASEGIIKHSGRV SFCSQFSWIMPGTIKENIIF GVSYDEYRYKSVVKACQLQQ DITKFAEQDNTVLGEGGVTL SEGQMAKISLARAVYKDADL YLLDSPFGYLDVFTEEQVFE SCVCKLMANKTRILVTSKME HLRKADKILILHQGSSYFYG TFSELQSLRPDFSSKLMGYD TFDQFTEERRSSILTETLRR FSVDD

Data sets:
Data typeCount
13C chemical shifts593
15N chemical shifts197
1H chemical shifts197

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NBD1-RE1

Entities:

Entity 1, NBD1-RE 285 residues - 32011.5 Da.

The protein used in these studies comprises residues T389-D673 of murine CFTR containing the mutations G550E, R553M, and R555K

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   SERGLUGLYGLNMETALALYSILESERLEU
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: CFTR NBD1-RE G550E/R553M/R555K, [U-100% 13C; U-100% 15N; 50% 2H], 0.6 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.170 M; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCO TROSYsample_1isotropicsample_conditions_1
3D HNCA TROSYsample_1isotropicsample_conditions_1
3D HNCACB TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CA TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CACB TROSYsample_1isotropicsample_conditions_1
3D HN(CA)CO TROSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC TROSYsample_1isotropicsample_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, data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 500 MHz

Related Database Links:

BMRB 16393 16394
PDB

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