BMRB Entry 5131
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5131
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Walma, Tine; Spronk, Chris; Tessari, Marco; Aelen, Jan; Schepens, Jan; Hendriks, Wiljan; Vuister, Geerten. "Structure, Dynamics and Binding Characteristics of the Second PDZ Domain of
PTP-BL" J. Mol. Biol. 316, 1101-1110 (2002).
PubMed: 11884147
Assembly members:
Protein Tyrosine Phosphatase-BAS Like, polymer, 102 residues, 10837.30 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: pET28a
Entity Sequences (FASTA):
Protein Tyrosine Phosphatase-BAS Like: MHHHHHHMKPGDTFEVELAK
TDGSLGISVTGGVNTSVRHG
GIYVKAIIPKGAAESDGRIH
KGDRVLAVNGVSLEGATHKQ
AVETLRNTGQVVHLLLEKGQ
VP
- assigned_chemical_shifts
- coupling_constants
- RDCs
- heteronucl_T1_relaxation
- heteronucl_NOEs
| Data type | Count |
| 1H chemical shifts | 616 |
| 13C chemical shifts | 355 |
| 15N chemical shifts | 102 |
| coupling constants | 101 |
| T1 relaxation values | 78 |
| residual dipolar couplings | 72 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PDZ2 | 1 |
Entities:
Entity 1, PDZ2 102 residues - 10837.30 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | MET | LYS | PRO | ||||
| 2 | GLY | ASP | THR | PHE | GLU | VAL | GLU | LEU | ALA | LYS | ||||
| 3 | THR | ASP | GLY | SER | LEU | GLY | ILE | SER | VAL | THR | ||||
| 4 | GLY | GLY | VAL | ASN | THR | SER | VAL | ARG | HIS | GLY | ||||
| 5 | GLY | ILE | TYR | VAL | LYS | ALA | ILE | ILE | PRO | LYS | ||||
| 6 | GLY | ALA | ALA | GLU | SER | ASP | GLY | ARG | ILE | HIS | ||||
| 7 | LYS | GLY | ASP | ARG | VAL | LEU | ALA | VAL | ASN | GLY | ||||
| 8 | VAL | SER | LEU | GLU | GLY | ALA | THR | HIS | LYS | GLN | ||||
| 9 | ALA | VAL | GLU | THR | LEU | ARG | ASN | THR | GLY | GLN | ||||
| 10 | VAL | VAL | HIS | LEU | LEU | LEU | GLU | LYS | GLY | GLN | ||||
| 11 | VAL | PRO |
Samples:
sample_1: Protein Tyrosine Phosphatase-BAS Like, [U-2H; U-15N; U-13C], 1.3 mM; K2HPO4/KH2PO4 50 mM; KCl 50 mM
conditions_1: pH: 6.3; temperature: 298 K; ionic strength: 0.1 M; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | not available | conditions_1 |
| 3D C(CO)NH | sample_1 | not available | conditions_1 |
| 3D HNCO | sample_1 | not available | conditions_1 |
| 3D HNCACB | sample_1 | not available | conditions_1 |
| 3D CBCA(CO)NH | sample_1 | not available | conditions_1 |
| 3D HBCBCA(CO)NH | sample_1 | not available | conditions_1 |
| 3D HNHA | sample_1 | not available | conditions_1 |
| 3D HNHB | sample_1 | not available | conditions_1 |
| 3D HCCH | sample_1 | not available | conditions_1 |
| 3D CCH | sample_1 | not available | conditions_1 |
| 3D 13C NOESY HSQC (aliphatic) | sample_1 | not available | conditions_1 |
| 3D 13C NOESY HMQC (aromatic) | sample_1 | not available | conditions_1 |
| 3D 15N Noesy HSQC | sample_1 | not available | conditions_1 |
Software:
nmrPipe v1.8 - spectral processing
XEASY v1.2 - peak integration and assignment
X-PLOR v3.851 - simulated annealing, restrained molecular dynamics
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks