BMRB Entry 25697

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25697

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Title:
human CFTR NBD1 deltaRI I539T mutant chemical shift assignments
Deposition date:
2015-07-09
Original release date:
2015-08-12
Authors:
Chong, Andrew; Forman-Kay, Julie
Citation:

Citation: Chong, Andrew; Farber, Patrick; Vernon, Robert; Hudson, Rhea; Mittermaier, Anthony; Forman-Kay, Julie. "Deletion of Phenylalanine-508 in the First Nucleotide Binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization"  J. Biol. Chem. 290, 22862-22878 (2015).
PubMed: 26149808

Assembly members:

Assembly members:
hCFTR_NBD1_delta_RI_I539T, polymer, 229 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-SUMO hNBD1 deltaRI I539T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hCFTR_NBD1_delta_RI_I539T: SLTTTEVVMENVTAFWEEGG TPVLKDINFKIERGQLLAVA GSTGAGKTSLLMMIMGELEP SEGKIKHSGRISFCSQFSWI MPGTIKENIIFGVSYDEYRY RSVIKACQLEEDISKFAEKD NTVLGEGGITLSGGQRARIS LARAVYKDADLYLLDSPFGY LDVLTEKEIFESCVCKLMAN KTRILVTSKMEHLKKADKIL ILHEGSSYFYGTFSELQNLQ PDFSSKLMG

Data sets:
Data typeCount
13C chemical shifts581
15N chemical shifts206
1H chemical shifts220

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hCFTR NBD1 delta RI I539T1

Entities:

Entity 1, hCFTR NBD1 delta RI I539T 229 residues - Formula weight is not available

1   SERLEUTHRTHRTHRGLUVALVALMETGLU
2   ASNVALTHRALAPHETRPGLUGLUGLYGLY
3   THRPROVALLEULYSASPILEASNPHELYS
4   ILEGLUARGGLYGLNLEULEUALAVALALA
5   GLYSERTHRGLYALAGLYLYSTHRSERLEU
6   LEUMETMETILEMETGLYGLULEUGLUPRO
7   SERGLUGLYLYSILELYSHISSERGLYARG
8   ILESERPHECYSSERGLNPHESERTRPILE
9   METPROGLYTHRILELYSGLUASNILEILE
10   PHEGLYVALSERTYRASPGLUTYRARGTYR
11   ARGSERVALILELYSALACYSGLNLEUGLU
12   GLUASPILESERLYSPHEALAGLULYSASP
13   ASNTHRVALLEUGLYGLUGLYGLYILETHR
14   LEUSERGLYGLYGLNARGALAARGILESER
15   LEUALAARGALAVALTYRLYSASPALAASP
16   LEUTYRLEULEUASPSERPROPHEGLYTYR
17   LEUASPVALLEUTHRGLULYSGLUILEPHE
18   GLUSERCYSVALCYSLYSLEUMETALAASN
19   LYSTHRARGILELEUVALTHRSERLYSMET
20   GLUHISLEULYSLYSALAASPLYSILELEU
21   ILELEUHISGLUGLYSERSERTYRPHETYR
22   GLYTHRPHESERGLULEUGLNASNLEUGLN
23   PROASPPHESERSERLYSLEUMETGLY

Samples:

sample_1: hCFTR NBD1 delta RI I539T, [U-99% 13C; U-99% 15N; 50% 2H]], 1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; glycerol 274 mM; magnesium chloride 5 mM; sodium azide .08 mM; DTT 5 mM; adenosine triphosphate 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.89 M; pH: 7.6; pressure: 1 atm; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian 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