BMRB Entry 18522
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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/BMR18522
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Title: Chemical Shift Assignments for the PICK1 PDZ domain fused to the C10 DAT ligand PubMed: 25023278
Deposition date: 2012-06-14 Original release date: 2013-06-17
Authors: Erlendsson, Simon; Teilum, Kaare
Citation: Erlendsson, Simon; Rathje, Mette; Heidarsson, Petur; Poulsen, Flemming; Madsen, Kenneth; Teilum, Kaare; Gether, Ulrik. "Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligand" J. Biol. Chem. 289, 25327-25340 (2014).
Assembly members:
entity, polymer, 232 residues, 24838.865 Da.
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GSPGIPVPGKVTLQKDAQNL
IGISIGGGAQYCPCLYIVQV
FDNTPAALDGTVAAGDEITG
VNGRSIKGKTKVEVAKMIQE
VKGEVTIHYNKLQADPKQLE
VLFQGPQFTLRHWLKVGSPG
IPVPGKVTLQKDAQNLIGIS
IGGGAQYCPCLYIVQVFDNT
PAALDGTVAAGDEITGVNGR
SIKGKTKVEVAKMIQEVKGE
VTIHYNKLQADPKQLEVLFQ
GPQFTLRHWLKV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 382 |
| 15N chemical shifts | 106 |
| 1H chemical shifts | 638 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PICK1 PDZ domain fused to the C10 DAT ligand | 1 |
Entities:
Entity 1, PICK1 PDZ domain fused to the C10 DAT ligand 232 residues - 24838.865 Da.
| 1 | GLY | SER | PRO | GLY | ILE | PRO | VAL | PRO | GLY | LYS | ||||
| 2 | VAL | THR | LEU | GLN | LYS | ASP | ALA | GLN | ASN | LEU | ||||
| 3 | ILE | GLY | ILE | SER | ILE | GLY | GLY | GLY | ALA | GLN | ||||
| 4 | TYR | CYS | PRO | CYS | LEU | TYR | ILE | VAL | GLN | VAL | ||||
| 5 | PHE | ASP | ASN | THR | PRO | ALA | ALA | LEU | ASP | GLY | ||||
| 6 | THR | VAL | ALA | ALA | GLY | ASP | GLU | ILE | THR | GLY | ||||
| 7 | VAL | ASN | GLY | ARG | SER | ILE | LYS | GLY | LYS | THR | ||||
| 8 | LYS | VAL | GLU | VAL | ALA | LYS | MET | ILE | GLN | GLU | ||||
| 9 | VAL | LYS | GLY | GLU | VAL | THR | ILE | HIS | TYR | ASN | ||||
| 10 | LYS | LEU | GLN | ALA | ASP | PRO | LYS | GLN | LEU | GLU | ||||
| 11 | VAL | LEU | PHE | GLN | GLY | PRO | GLN | PHE | THR | LEU | ||||
| 12 | ARG | HIS | TRP | LEU | LYS | VAL | GLY | SER | PRO | GLY | ||||
| 13 | ILE | PRO | VAL | PRO | GLY | LYS | VAL | THR | LEU | GLN | ||||
| 14 | LYS | ASP | ALA | GLN | ASN | LEU | ILE | GLY | ILE | SER | ||||
| 15 | ILE | GLY | GLY | GLY | ALA | GLN | TYR | CYS | PRO | CYS | ||||
| 16 | LEU | TYR | ILE | VAL | GLN | VAL | PHE | ASP | ASN | THR | ||||
| 17 | PRO | ALA | ALA | LEU | ASP | GLY | THR | VAL | ALA | ALA | ||||
| 18 | GLY | ASP | GLU | ILE | THR | GLY | VAL | ASN | GLY | ARG | ||||
| 19 | SER | ILE | LYS | GLY | LYS | THR | LYS | VAL | GLU | VAL | ||||
| 20 | ALA | LYS | MET | ILE | GLN | GLU | VAL | LYS | GLY | GLU | ||||
| 21 | VAL | THR | ILE | HIS | TYR | ASN | LYS | LEU | GLN | ALA | ||||
| 22 | ASP | PRO | LYS | GLN | LEU | GLU | VAL | LEU | PHE | GLN | ||||
| 23 | GLY | PRO | GLN | PHE | THR | LEU | ARG | HIS | TRP | LEU | ||||
| 24 | LYS | VAL |
Samples:
backbone: TRIS 50 mM; sodium chloride 125 mM; DTT 2 mM; protein, [U-100% 13C; U-100% 15N], 600 uM; DSS 0.25 mM; sodium azide 0.01%; H2O 90%; D2O 10%
13C-HSQC-NOESY: TRIS, [U-99% 2H], 50 mM; sodium chloride 125 mM; DTT 2 mM; protein, [U-100% 13C; U-100% 15N], 600 uM; DSS 0.25 mM; sodium azide 0.01%; D2O 100%
sample_conditions_1: ionic strength: 0.175 M; pH: 7.4; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | backbone | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 13C-HSQC-NOESY | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | backbone | isotropic | sample_conditions_1 |
| 3D HNCO | backbone | isotropic | sample_conditions_1 |
| 3D HNCA | backbone | isotropic | sample_conditions_1 |
| 3D HNCACB | backbone | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | backbone | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | backbone | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | backbone | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | 13C-HSQC-NOESY | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.2D, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ARIA, Linge, O'Donoghue and Nilges - refinement, structure solution
CING, Geerten W. Vuister , Alan Wilter Sousa da Silva , and Jurgen F. Doreleijers - validation
Molmol, Koradi, Billeter and Wuthrich - representation
Analysis, CCPN - chemical shift assignment, data analysis, peak picking, refinement
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
X-PLOR, Brunger - restraint deposition
NMR spectrometers:
- Varian INOVA 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts