BMRB Entry 4516
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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/BMR4516
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: Kozlov, G.; Gehring, K.; Ekiel, I.. "Solution Structure of the PDZ2 Domain from Human Phosphatase hPTP1E and its
Interactions with C-terminal Peptides from the Fas Receptor" Biochemistry 39, 2572-2580 (2000).
Assembly members:
HUMAN PHOSPHATASE HPTP1E, polymer, 96 residues, Formula weight is not available
peptide, polymer, 15 residues, Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
HUMAN PHOSPHATASE HPTP1E: PKPGDIFEVELAKNDNSLGI
SVTGGVNTSVRHGGIYVKAV
IPQGAAESDGRIHKGDRVLA
VNGVSLEGATHKQAVETLRN
TGQVVHLLLEKGQSPT
peptide: FADSEADENEQVSAV
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 208 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 570 |
| coupling constants | 71 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PDZ domain | 1 |
| 2 | peptide | 2 |
Entities:
Entity 1, PDZ domain 96 residues - Formula weight is not available
| 1 | PRO | LYS | PRO | GLY | ASP | ILE | PHE | GLU | VAL | GLU | ||||
| 2 | LEU | ALA | LYS | ASN | ASP | ASN | SER | LEU | GLY | ILE | ||||
| 3 | SER | VAL | THR | GLY | GLY | VAL | ASN | THR | SER | VAL | ||||
| 4 | ARG | HIS | GLY | GLY | ILE | TYR | VAL | LYS | ALA | VAL | ||||
| 5 | ILE | PRO | GLN | GLY | ALA | ALA | GLU | SER | ASP | GLY | ||||
| 6 | ARG | ILE | HIS | LYS | GLY | ASP | ARG | VAL | LEU | ALA | ||||
| 7 | VAL | ASN | GLY | VAL | SER | LEU | GLU | GLY | ALA | THR | ||||
| 8 | HIS | LYS | GLN | ALA | VAL | GLU | THR | LEU | ARG | ASN | ||||
| 9 | THR | GLY | GLN | VAL | VAL | HIS | LEU | LEU | LEU | GLU | ||||
| 10 | LYS | GLY | GLN | SER | PRO | THR |
Entity 2, peptide 15 residues - Formula weight is not available
| 1 | PHE | ALA | ASP | SER | GLU | ALA | ASP | GLU | ASN | GLU | ||||
| 2 | GLN | VAL | SER | ALA | VAL |
Samples:
sample_1: HUMAN PHOSPHATASE HPTP1E, [U-15N], 1.0 – 5.0 mM; peptide1.2 – 6.0 mM
sample_2: HUMAN PHOSPHATASE HPTP1E1.0 – 5.0 mM; peptide1.2 – 6.0 mM
sample_3: HUMAN PHOSPHATASE HPTP1E, [U-13C; U-15N], 1.0 – 5.0 mM; peptide1.2 – 6.0 mM
sample_cond_1: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-SEPARATED_NOESY | not available | not available | not available |
| 3D 15N-SEPARATED NOESY | not available | not available | not available |
| 2D NOESY | not available | not available | not available |
Software:
xwinnmr v2.1 - COLLECTION
GIFA v4.0 - PROCESSING
XEASY v1.3.13 - DATA ANALYSIS
CNS v0.5 - STRUCTURE SOLUTION
ARIA v0.1 - STRUCTURE SOLUTION
NMR spectrometers:
- BRUKER DRX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks