BMRB Entry 5552
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5552
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments of the Catalytic Domain of Pac1 PubMed: 12575935
Deposition date: 2002-10-10 Original release date: 2003-03-14
Authors: Farooq, A.; Zhou, M.-M.
Citation: Farooq, A.; Plotnikova, O.; Chaturvedi, G.; Yan, S.; Zeng, L.; Zhang, Q.; Zhou, M.-M.. "Solution Structure of the MAPK Phosphotase PAC-1: Catalytic Domain. Insights into Substrate-induced Enzymatic Activation of MKP" Structure 11, 155-164 (2003).
Assembly members:
dual specificity protein phosphatase 2, polymer, 145 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):
dual specificity protein phosphatase 2: QGGPVEILPYLFLGSCSHSS
DLQGLQACGITAVLNVSASC
PNHFEGLFRYKSIPVEDNQM
VEISAWFQEAIGFIDWVKNS
GGRVLVHSQAGISRSATICL
AYLMQSRRVRLDEAFDFVKQ
RRGVISPNFSFMGQLLQFET
QVLCH
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 666 |
| 13C chemical shifts | 334 |
| 15N chemical shifts | 124 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | dual specificity protein phosphatase 2 | 1 |
Entities:
Entity 1, dual specificity protein phosphatase 2 145 residues - Formula weight is not available
| 1 | GLN | GLY | GLY | PRO | VAL | GLU | ILE | LEU | PRO | TYR | ||||
| 2 | LEU | PHE | LEU | GLY | SER | CYS | SER | HIS | SER | SER | ||||
| 3 | ASP | LEU | GLN | GLY | LEU | GLN | ALA | CYS | GLY | ILE | ||||
| 4 | THR | ALA | VAL | LEU | ASN | VAL | SER | ALA | SER | CYS | ||||
| 5 | PRO | ASN | HIS | PHE | GLU | GLY | LEU | PHE | ARG | TYR | ||||
| 6 | LYS | SER | ILE | PRO | VAL | GLU | ASP | ASN | GLN | MET | ||||
| 7 | VAL | GLU | ILE | SER | ALA | TRP | PHE | GLN | GLU | ALA | ||||
| 8 | ILE | GLY | PHE | ILE | ASP | TRP | VAL | LYS | ASN | SER | ||||
| 9 | GLY | GLY | ARG | VAL | LEU | VAL | HIS | SER | GLN | ALA | ||||
| 10 | GLY | ILE | SER | ARG | SER | ALA | THR | ILE | CYS | LEU | ||||
| 11 | ALA | TYR | LEU | MET | GLN | SER | ARG | ARG | VAL | ARG | ||||
| 12 | LEU | ASP | GLU | ALA | PHE | ASP | PHE | VAL | LYS | GLN | ||||
| 13 | ARG | ARG | GLY | VAL | ILE | SER | PRO | ASN | PHE | SER | ||||
| 14 | PHE | MET | GLY | GLN | LEU | LEU | GLN | PHE | GLU | THR | ||||
| 15 | GLN | VAL | LEU | CYS | HIS |
Samples:
sample_1: dual specificity protein phosphatase 2, [U-13C; U-15N], 0.5 mM; phosphate buffer 5 mM
sample_cond_1: pH: 6.5; temperature: 298 K; ionic strength: 10 mM; pressure: 1 atm
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 |
| HNHA | not available | not available | not available |
Software:
XPLOR - structure solution, refinement
ARIA - structure solution, refinement
XWINNMR - collection
NMRPIPE - processing
NMRVIEW - data analysis
NMR spectrometers:
- BRUKER DRX 600 MHz
Related Database Links:
| BMRB | 5000 |
| PDB | |
| GB | AAA50779 AAA86112 AAH07771 AAL57044 AAY24222 |
| REF | NP_004409 XP_001111118 XP_002757414 XP_002811694 XP_003281084 |
| SP | Q05923 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts