BMRB Entry 5762
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5762
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: The alternatively spliced PDZ2 domain of PTP-BL, PDZ2as PubMed: 14725761
Deposition date: 2003-04-07 Original release date: 2011-08-11
Authors: Walma, Tine; Aelen, Jan; Oostendorp, M.; Vuister, Geerten
Citation: Walma, Tine; Aelen, Jan; Nabuurs, S.; Oostendorp, Marlies; van den Berk, L.; Hendriks, W.; Vuister, Geerten. "A Closed Binding Pocket and Global Destabilization Modify the Binding Properties of an Alternatively Spliced Form of the Second PDZ Domain of PTP-BL" Structure (Cambridge, MA, U. S.) 12, 11-20 (2004).
Assembly members:
Second PDZ Domain from PTP-BL, polymer, 99 residues, 10355 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-2T
Entity Sequences (FASTA):
Second PDZ Domain from PTP-BL: KPGDTFEVELAKTDGSLGIS
VTVLFDKGGVNTSVRHGGIY
VKAIIPKGAAESDGRIHKGD
RVLAVNGVSLEGATHKQAVE
TLRNTGQVVHLLLEKGQVP
- assigned_chemical_shifts
- coupling_constants
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- H_exch_protection_factors
- H_exch_rates
- RDCs
| Data type | Count |
| 13C chemical shifts | 297 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 671 |
| coupling constants | 58 |
| heteronuclear NOE values | 90 |
| H exchange protection factors | 55 |
| residual dipolar couplings | 66 |
| T1 relaxation values | 88 |
| T2 relaxation values | 86 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PDZ2-AS | 1 |
Entities:
Entity 1, PDZ2-AS 99 residues - 10355 Da.
| 1 | LYS | PRO | GLY | ASP | THR | PHE | GLU | VAL | GLU | LEU | ||||
| 2 | ALA | LYS | THR | ASP | GLY | SER | LEU | GLY | ILE | SER | ||||
| 3 | VAL | THR | VAL | LEU | PHE | ASP | LYS | GLY | GLY | VAL | ||||
| 4 | ASN | THR | SER | VAL | ARG | HIS | GLY | GLY | ILE | TYR | ||||
| 5 | VAL | LYS | ALA | ILE | ILE | PRO | LYS | GLY | ALA | ALA | ||||
| 6 | GLU | SER | ASP | GLY | ARG | ILE | HIS | LYS | GLY | ASP | ||||
| 7 | ARG | VAL | LEU | ALA | VAL | ASN | GLY | VAL | SER | LEU | ||||
| 8 | GLU | GLY | ALA | THR | HIS | LYS | GLN | ALA | VAL | GLU | ||||
| 9 | THR | LEU | ARG | ASN | THR | GLY | GLN | VAL | VAL | HIS | ||||
| 10 | LEU | LEU | LEU | GLU | LYS | GLY | GLN | VAL | PRO |
Samples:
sample_1: Second PDZ Domain from PTP-BL, [U-2H; U-15N; U-13C], 1.4 mM; K2HPO4/KH2PO4 50 mM; KCl 50 mM
sample_2: Second PDZ Domain from PTP-BL, [U-2H; U-15N], 1.1 mM; CH3COO- 50 mM; KCl 50 mM
condition_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
condition_2: ionic strength: 0.1 M; pH: 3.5; pressure: 1 atm; temperature: 281.5 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|
Software:
No software information available
NMR spectrometers:
- Varian Inova 800 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts