BMRB Entry 16367
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16367
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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:
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 593 |
| 15N chemical shifts | 197 |
| 1H chemical shifts | 197 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NBD1-RE | 1 |
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 | THR | THR | GLY | ILE | ILE | MET | GLU | ASN | VAL | THR | ||||
| 2 | ALA | PHE | TRP | GLU | GLU | GLY | PHE | GLY | GLU | LEU | ||||
| 3 | LEU | GLU | LYS | VAL | GLN | GLN | SER | ASN | GLY | ASP | ||||
| 4 | ARG | LYS | HIS | SER | SER | ASP | GLU | ASN | ASN | VAL | ||||
| 5 | SER | PHE | SER | HIS | LEU | CYS | LEU | VAL | GLY | ASN | ||||
| 6 | PRO | VAL | LEU | LYS | ASN | ILE | ASN | LEU | ASN | ILE | ||||
| 7 | GLU | LYS | GLY | GLU | MET | LEU | ALA | ILE | THR | GLY | ||||
| 8 | SER | THR | GLY | SER | GLY | LYS | THR | SER | LEU | LEU | ||||
| 9 | MET | LEU | ILE | LEU | GLY | GLU | LEU | GLU | ALA | SER | ||||
| 10 | GLU | GLY | ILE | ILE | LYS | HIS | SER | GLY | ARG | VAL | ||||
| 11 | SER | PHE | CYS | SER | GLN | PHE | SER | TRP | ILE | MET | ||||
| 12 | PRO | GLY | THR | ILE | LYS | GLU | ASN | ILE | ILE | PHE | ||||
| 13 | GLY | VAL | SER | TYR | ASP | GLU | TYR | ARG | TYR | LYS | ||||
| 14 | SER | VAL | VAL | LYS | ALA | CYS | GLN | LEU | GLN | GLN | ||||
| 15 | ASP | ILE | THR | LYS | PHE | ALA | GLU | GLN | ASP | ASN | ||||
| 16 | THR | VAL | LEU | GLY | GLU | GLY | GLY | VAL | THR | LEU | ||||
| 17 | SER | GLU | GLY | GLN | MET | ALA | LYS | ILE | SER | LEU | ||||
| 18 | ALA | ARG | ALA | VAL | TYR | LYS | ASP | ALA | ASP | LEU | ||||
| 19 | TYR | LEU | LEU | ASP | SER | PRO | PHE | GLY | TYR | LEU | ||||
| 20 | ASP | VAL | PHE | THR | GLU | GLU | GLN | VAL | PHE | GLU | ||||
| 21 | SER | CYS | VAL | CYS | LYS | LEU | MET | ALA | ASN | LYS | ||||
| 22 | THR | ARG | ILE | LEU | VAL | THR | SER | LYS | MET | GLU | ||||
| 23 | HIS | LEU | ARG | LYS | ALA | ASP | LYS | ILE | LEU | ILE | ||||
| 24 | LEU | HIS | GLN | GLY | SER | SER | TYR | PHE | TYR | GLY | ||||
| 25 | THR | PHE | SER | GLU | LEU | GLN | SER | LEU | ARG | PRO | ||||
| 26 | ASP | PHE | SER | SER | LYS | LEU | MET | GLY | TYR | ASP | ||||
| 27 | THR | PHE | ASP | GLN | PHE | THR | GLU | GLU | ARG | ARG | ||||
| 28 | SER | SER | ILE | LEU | THR | GLU | THR | LEU | ARG | ARG | ||||
| 29 | PHE | SER | VAL | ASP | ASP |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO TROSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC TROSY | sample_1 | isotropic | sample_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
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks