BMRB Entry 18205
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18205
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Title: PDZ Domain of CAL (Cystic Fibrosis Transmembrane Regulator-Associated Ligand) PubMed: 16331976
Deposition date: 2012-01-20 Original release date: 2012-03-02
Authors: Piserchio, Andrea; Fellows, Abigail; Maden, Dean; Mierke, Dale
Citation: Piserchio, Andrea; Fellows, Abigail; Madden, Dean; Mierke, Dale. "Association of the cystic fibrosis transmembrane regulator with CAL: structural features and molecular dynamics." Biochemistry 44, 16158-16166 (2005).
Assembly members:
PDZ Domain of CAL, polymer, 112 residues, 9256.696 Da.
C-terminus of the CFTR, polymer, 8 residues, 990.055 Da.
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):
PDZ Domain of CAL: HHHHHHHHHHSSGHIEGRHM
ENLYFQGIRKVLLLKEDHEG
LGISITGGKEHGVPILISEI
HPGQPADRCGGLHVGDAILA
VNGVNLRDTKHKEAVTILSQ
QRGEIEFEVVYV
C-terminus of the CFTR: EEVQDTRL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 222 |
| 15N chemical shifts | 79 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PDZ Domain of CAL | 1 |
| 2 | C-terminus of the CFTR | 2 |
Entities:
Entity 1, PDZ Domain of CAL 112 residues - 9256.696 Da.
Residues 1-10 represent a polyhistidine purification tag. Residues 11-27 represent a cloning linker. Residues 28-112 represent the PDZ domain of the CAL protein (residues 278-362 in the full-length sequence).
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | HIS | ILE | GLU | GLY | ARG | HIS | MET | ||||
| 3 | GLU | ASN | LEU | TYR | PHE | GLN | GLY | ILE | ARG | LYS | ||||
| 4 | VAL | LEU | LEU | LEU | LYS | GLU | ASP | HIS | GLU | GLY | ||||
| 5 | LEU | GLY | ILE | SER | ILE | THR | GLY | GLY | LYS | GLU | ||||
| 6 | HIS | GLY | VAL | PRO | ILE | LEU | ILE | SER | GLU | ILE | ||||
| 7 | HIS | PRO | GLY | GLN | PRO | ALA | ASP | ARG | CYS | GLY | ||||
| 8 | GLY | LEU | HIS | VAL | GLY | ASP | ALA | ILE | LEU | ALA | ||||
| 9 | VAL | ASN | GLY | VAL | ASN | LEU | ARG | ASP | THR | LYS | ||||
| 10 | HIS | LYS | GLU | ALA | VAL | THR | ILE | LEU | SER | GLN | ||||
| 11 | GLN | ARG | GLY | GLU | ILE | GLU | PHE | GLU | VAL | VAL | ||||
| 12 | TYR | VAL |
Entity 2, C-terminus of the CFTR 8 residues - 990.055 Da.
residues 1-8 represent the C-terminus of the CFTR protein (residues 1473-1480 in the full-length sequence)
| 1 | GLU | GLU | VAL | GLN | ASP | THR | ARG | LEU |
Samples:
sample_1: PDZ Domain of CAL, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 1.0 M; pH: 6.8; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| UNP | Q9HD26-2 P13569-1 |
| PDB | |
| DBJ | BAB69946 BAC26958 BAC27058 BAC27951 |
| EMBL | CAH90325 |
| GB | AAG00571 AAG00572 AAH09553 AAH51171 AAI68160 |
| PRF | 1611455A |
| REF | NP_001017408 NP_001101101 NP_001125151 NP_001186201 NP_001193086 |
| SP | Q5RD32 Q8BH60 Q9HD26 |
| TPG | DAA26316 DAA26317 |