BMRB Entry 18825
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18825
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Title: Complex structure of C-terminal CFTR peptide and extended PDZ1 domain from NHERF1. PubMed: 23583913
Deposition date: 2012-11-06 Original release date: 2013-04-22
Authors: Bhattacharya, Shibani; Ju, Jeong; Cowburn, David; Bu, Zimei
Citation: Bhattacharya, Shibani; Ju, Jeong Ho; Orlova, Natalia; Khajeh, Jahan Ali; Cowburn, David; Bu, Zimei. "Ligand-Induced Dynamic Changes in Extended PDZ Domains from NHERF1." J. Mol. Biol. 425, 2509-2528 (2013).
Assembly members:
PDZ1, polymer, 117 residues, 12822.731 Da.
CFTR, polymer, 5 residues, 632.693 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):
PDZ1: GIDPFTMLPRLCCLEKGPNG
YGFHLHGEKGKLGQYIRLVE
PGSPAEKAGLLAGDRLVEVN
GENVEKETHQQVVSRIRAAL
NAVRLLVVDPETDEQLQKLG
VQVREELLRAQEAPGQA
CFTR: QDTRL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 481 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 832 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | extended PDZ1 domain from NHERF1 | 1 |
| 2 | C-terminal CFTR peptide | 2 |
Entities:
Entity 1, extended PDZ1 domain from NHERF1 117 residues - 12822.731 Da.
| 1 | GLY | ILE | ASP | PRO | PHE | THR | MET | LEU | PRO | ARG | ||||
| 2 | LEU | CYS | CYS | LEU | GLU | LYS | GLY | PRO | ASN | GLY | ||||
| 3 | TYR | GLY | PHE | HIS | LEU | HIS | GLY | GLU | LYS | GLY | ||||
| 4 | LYS | LEU | GLY | GLN | TYR | ILE | ARG | LEU | VAL | GLU | ||||
| 5 | PRO | GLY | SER | PRO | ALA | GLU | LYS | ALA | GLY | LEU | ||||
| 6 | LEU | ALA | GLY | ASP | ARG | LEU | VAL | GLU | VAL | ASN | ||||
| 7 | GLY | GLU | ASN | VAL | GLU | LYS | GLU | THR | HIS | GLN | ||||
| 8 | GLN | VAL | VAL | SER | ARG | ILE | ARG | ALA | ALA | LEU | ||||
| 9 | ASN | ALA | VAL | ARG | LEU | LEU | VAL | VAL | ASP | PRO | ||||
| 10 | GLU | THR | ASP | GLU | GLN | LEU | GLN | LYS | LEU | GLY | ||||
| 11 | VAL | GLN | VAL | ARG | GLU | GLU | LEU | LEU | ARG | ALA | ||||
| 12 | GLN | GLU | ALA | PRO | GLY | GLN | ALA |
Entity 2, C-terminal CFTR peptide 5 residues - 632.693 Da.
| 1 | GLN | ASP | THR | ARG | LEU |
Samples:
sample_1: PDZ1, [U-99% 13C; U-99% 15N], 286 uM; TRIS 20 mM; sodium chloride 150 mM; DTT 0.5 mM; EDTA 0.5 mM; CFTR 275 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C,15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C,13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C,15N f1,f2-filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C,15N f2-filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA v1.5, Keller and Wuthrich - data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
ARIA v2.2, Linge, O, . - refinement
TALOS v1.01, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts