BMRB Entry 15567
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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/BMR15567
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Title: Structure of the second PDZ domain of NHERF-1 PubMed: 19446522
Deposition date: 2007-11-27 Original release date: 2009-05-28
Authors: Cheng, Hong; Li, Jianquan; Dai, Zhongping; Bu, Zimei; Roder, Heinrich
Citation: Cheng, Hong; Li, Jianquan; Ruzaliya, Fazlieva; Dai, Zhongping; Bu, Zimei; Roder, Heinrich. "Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF-1" Structure 17, 660-669 (2009).
Assembly members:
PDZ2, polymer, 98 residues, 10731 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):
PDZ2: GIDPFTMLRPRLCTMKKGPS
GYGFNLHSDKSKPGQFIRSV
DPDSPAEASGLRAQDRIVEV
NGVCMEGKQHGDVVSAIRAG
GDETKLLVVDRETDEFFK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 340 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 569 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 98 residues - 10731 Da.
| 1 | GLY | ILE | ASP | PRO | PHE | THR | MET | LEU | ARG | PRO | ||||
| 2 | ARG | LEU | CYS | THR | MET | LYS | LYS | GLY | PRO | SER | ||||
| 3 | GLY | TYR | GLY | PHE | ASN | LEU | HIS | SER | ASP | LYS | ||||
| 4 | SER | LYS | PRO | GLY | GLN | PHE | ILE | ARG | SER | VAL | ||||
| 5 | ASP | PRO | ASP | SER | PRO | ALA | GLU | ALA | SER | GLY | ||||
| 6 | LEU | ARG | ALA | GLN | ASP | ARG | ILE | VAL | GLU | VAL | ||||
| 7 | ASN | GLY | VAL | CYS | MET | GLU | GLY | LYS | GLN | HIS | ||||
| 8 | GLY | ASP | VAL | VAL | SER | ALA | ILE | ARG | ALA | GLY | ||||
| 9 | GLY | ASP | GLU | THR | LYS | LEU | LEU | VAL | VAL | ASP | ||||
| 10 | ARG | GLU | THR | ASP | GLU | PHE | PHE | LYS |
Samples:
sample_1: PDZ2 1 mM; NaCl 150 mM; HEPES 20 mM; DTT 0.5 mM; D2O, [U-100% 2H], 5%; H2O 95%
sample_2: PDZ2, [U-100% 15N], 1 mM; NaCl 150 mM; HEPES 20 mM; DTT 0.5 mM; D2O, [U-100% 2H], 5%; H2O 95%
sample_3: PDZ2, [U-100% 13C; U-100% 15N], 1 mM; NaCl 150 mM; HEPES 20 mM; DTT 0.5 mM; D2O, [U-100% 2H], 5%; H2O 95%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 288.1 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
FELIX v2000, Accelrys Software Inc. - chemical shift calculation, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
xwinnmr, Bruker Biospin - chemical shift calculation, collection
NMR spectrometers:
- Bruker DMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts