BMRB Entry 25698

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25698

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Title:
human CFTR NBD1 deltaRI F508del mutant chemical shift assignments
Deposition date:
2015-07-09
Original release date:
2015-08-12
Authors:
Hudson, Rhea; 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_F508del, polymer, 228 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 F508del

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hCFTR_NBD1_delta_RI_F508del: SLTTTEVVMENVTAFWEEGG TPVLKDINFKIERGQLLAVA GSTGAGKTSLLMMIMGELEP SEGKIKHSGRISFCSQFSWI MPGTIKENIIGVSYDEYRYR SVIKACQLEEDISKFAEKDN IVLGEGGITLSGGQRARISL ARAVYKDADLYLLDSPFGYL DVLTEKEIFESCVCKLMANK TRILVTSKMEHLKKADKILI LHEGSSYFYGTFSELQNLQP DFSSKLMG

Data sets:
Data typeCount
13C chemical shifts375
15N chemical shifts186
1H chemical shifts185

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1hCFTR NBD1 delta RI F508del1

Entities:

Entity 1, hCFTR NBD1 delta RI F508del 228 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   GLYVALSERTYRASPGLUTYRARGTYRARG
11   SERVALILELYSALACYSGLNLEUGLUGLU
12   ASPILESERLYSPHEALAGLULYSASPASN
13   ILEVALLEUGLYGLUGLYGLYILETHRLEU
14   SERGLYGLYGLNARGALAARGILESERLEU
15   ALAARGALAVALTYRLYSASPALAASPLEU
16   TYRLEULEUASPSERPROPHEGLYTYRLEU
17   ASPVALLEUTHRGLULYSGLUILEPHEGLU
18   SERCYSVALCYSLYSLEUMETALAASNLYS
19   THRARGILELEUVALTHRSERLYSMETGLU
20   HISLEULYSLYSALAASPLYSILELEUILE
21   LEUHISGLUGLYSERSERTYRPHETYRGLY
22   THRPHESERGLULEUGLNASNLEUGLNPRO
23   ASPPHESERSERLYSLEUMETGLY

Samples:

sample_1: hCFTR NBD1 delta RI F508del, [U-99% 13C; U-99% 15N; 50%D20], 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
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_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