BMRB Entry 19481
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19481
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Title: The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase PubMed: 24361276
Deposition date: 2013-09-06 Original release date: 2014-02-12
Authors: zhang, shengnan; Huang, Tao; Hinck, Andrew; Fitzpatrick, Paul
Citation: Zhang, Shengnan; Huang, Tao; Hinck, Andrew; Fitzpatrick, Paul. "The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase." J. Mol. Biol. 426, 1483-1497 (2013).
Assembly members:
Ser40_phosphorylated_regulatory_domain_of_tyrosine_hydroxylase, polymer, 159 residues, Formula weight is not available
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):
Ser40_phosphorylated_regulatory_domain_of_tyrosine_hydroxylase: MPTPSAPSPQPKGFRRAVSE
QDAKQAEAVTSPRFIGRRQS
LIEDARKEREAAAAAAAAAV
ASSEPGNPLEAVVFEERDGN
AVLNLLFSLRGTKPSSLSRA
VKVFETFEAKIHHLETRPAQ
RPLAGSPHLEYFVRFEVPSG
DLAALLSSVRRVSDDVRSA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 223 |
| 15N chemical shifts | 127 |
| 1H chemical shifts | 127 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RDTH, chain 1 | 1 |
| 2 | RDTH, chain 2 | 1 |
Entities:
Entity 1, RDTH, chain 1 159 residues - Formula weight is not available
| 1 | MET | PRO | THR | PRO | SER | ALA | PRO | SER | PRO | GLN | ||||
| 2 | PRO | LYS | GLY | PHE | ARG | ARG | ALA | VAL | SER | GLU | ||||
| 3 | GLN | ASP | ALA | LYS | GLN | ALA | GLU | ALA | VAL | THR | ||||
| 4 | SER | PRO | ARG | PHE | ILE | GLY | ARG | ARG | GLN | SER | ||||
| 5 | LEU | ILE | GLU | ASP | ALA | ARG | LYS | GLU | ARG | GLU | ||||
| 6 | ALA | ALA | ALA | ALA | ALA | ALA | ALA | ALA | ALA | VAL | ||||
| 7 | ALA | SER | SER | GLU | PRO | GLY | ASN | PRO | LEU | GLU | ||||
| 8 | ALA | VAL | VAL | PHE | GLU | GLU | ARG | ASP | GLY | ASN | ||||
| 9 | ALA | VAL | LEU | ASN | LEU | LEU | PHE | SER | LEU | ARG | ||||
| 10 | GLY | THR | LYS | PRO | SER | SER | LEU | SER | ARG | ALA | ||||
| 11 | VAL | LYS | VAL | PHE | GLU | THR | PHE | GLU | ALA | LYS | ||||
| 12 | ILE | HIS | HIS | LEU | GLU | THR | ARG | PRO | ALA | GLN | ||||
| 13 | ARG | PRO | LEU | ALA | GLY | SER | PRO | HIS | LEU | GLU | ||||
| 14 | TYR | PHE | VAL | ARG | PHE | GLU | VAL | PRO | SER | GLY | ||||
| 15 | ASP | LEU | ALA | ALA | LEU | LEU | SER | SER | VAL | ARG | ||||
| 16 | ARG | VAL | SER | ASP | ASP | VAL | ARG | SER | ALA |
Samples:
sample_1: Ser40 phosphorylated regulatory domain of tyrosine hydroxylase, [U-95% 13C; U-95% 15N], 0.8 – 1.2 mM; D2O 5%; H2O 95%; sodium phosphate 50 mM
sample_conditions_1: ionic strength: 0.11 M; pH: 7; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignments
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Related Database Links:
| BMRB | 19480 19482 |
| PDB | |
| GB | AAA40434 AAA42257 AAA42258 AAB59722 AAI56669 |
| REF | NP_033403 NP_036872 |
| SP | P04177 P24529 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts