BMRB Entry 15340
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15340
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Title: 1H, 13C, and 15N Backbone Assignments and 13C Aliphatic Sidechain Assignments for PKA Phosphorylated CFTR Regulatory Region PubMed: 17660831
Deposition date: 2007-06-28 Original release date: 2007-11-21
Authors: Baker, Jennifer; Hudson, Rhea; Kanelis, Voula; Choy, Wing-Yiu; Thibodeau, Patrick; Thomas, Philip; Forman-Kay, Julie
Citation: Baker, Jennifer; Hudson, Rhea; Kanelis, Voula; Choy, Wing-Yiu; Thibodeau, Patrick; Thomas, Philip; Forman-Kay, Julie. "CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices." Nat. Struct. Mol. Biol. 14, 738-745 (2007).
Assembly members:
Phosphorylated_CFTR_Regulatory_Region, polymer, 189 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Phosphorylated_CFTR_Regulatory_Region: GAMESAERRNSILTETLHRF
SLEGDAPVSWTETKKQSFKQ
TGEFGEKRKNSILNPINSIR
KFSIVQKTPLQMNGIEEDSD
EPLERRLSLVPDSEQGEAIL
PRISVISTGPTLQARRRQSV
LNLMTHSVNQGQNIHRKTTA
STRKVSLAPQANLTELDIYS
RRLSQETGLEISEEINEEDL
KECLFDDME
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 755 |
| 15N chemical shifts | 180 |
| 1H chemical shifts | 180 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | regulatory region | 1 |
Entities:
Entity 1, regulatory region 189 residues - Formula weight is not available
The first four residues are derived from the vector. The remaining residues are from human CFTR with the polymorphism L833. Shifts are reported for the major component of the sample phosphorylated at S660, S670, S700, S712, S737, S753, S768, S795, and S813.
| 1 | GLY | ALA | MET | GLU | SER | ALA | GLU | ARG | ARG | ASN | ||||
| 2 | SER | ILE | LEU | THR | GLU | THR | LEU | HIS | ARG | PHE | ||||
| 3 | SER | LEU | GLU | GLY | ASP | ALA | PRO | VAL | SER | TRP | ||||
| 4 | THR | GLU | THR | LYS | LYS | GLN | SER | PHE | LYS | GLN | ||||
| 5 | THR | GLY | GLU | PHE | GLY | GLU | LYS | ARG | LYS | ASN | ||||
| 6 | SER | ILE | LEU | ASN | PRO | ILE | ASN | SER | ILE | ARG | ||||
| 7 | LYS | PHE | SER | ILE | VAL | GLN | LYS | THR | PRO | LEU | ||||
| 8 | GLN | MET | ASN | GLY | ILE | GLU | GLU | ASP | SER | ASP | ||||
| 9 | GLU | PRO | LEU | GLU | ARG | ARG | LEU | SER | LEU | VAL | ||||
| 10 | PRO | ASP | SER | GLU | GLN | GLY | GLU | ALA | ILE | LEU | ||||
| 11 | PRO | ARG | ILE | SER | VAL | ILE | SER | THR | GLY | PRO | ||||
| 12 | THR | LEU | GLN | ALA | ARG | ARG | ARG | GLN | SER | VAL | ||||
| 13 | LEU | ASN | LEU | MET | THR | HIS | SER | VAL | ASN | GLN | ||||
| 14 | GLY | GLN | ASN | ILE | HIS | ARG | LYS | THR | THR | ALA | ||||
| 15 | SER | THR | ARG | LYS | VAL | SER | LEU | ALA | PRO | GLN | ||||
| 16 | ALA | ASN | LEU | THR | GLU | LEU | ASP | ILE | TYR | SER | ||||
| 17 | ARG | ARG | LEU | SER | GLN | GLU | THR | GLY | LEU | GLU | ||||
| 18 | ILE | SER | GLU | GLU | ILE | ASN | GLU | GLU | ASP | LEU | ||||
| 19 | LYS | GLU | CYS | LEU | PHE | ASP | ASP | MET | GLU |
Samples:
sample_1: Phosphorylated CFTR Regulatory Region, [U-98% 13C; U-98% 15N], 0.25 mM; potassium chloride 125 mM; potassium phosphate 125 mM; DSS 2 mM; DTT 5 mM; EDTA 5 mM; benzamidine 5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.25 M; pH: 6.8; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CCC-TOCSY-NNH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - chemical shift assignment, processing
NMR spectrometers:
- Varian INOVA 800 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts