BMRB Entry 19482
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19482
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Title: The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase PubMed: 24361276
Deposition date: 2013-09-08 Original release date: 2014-01-02
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:
RDTyrH65-159, polymer, 93 residues, 10485.973 Da.
Natural source: Common Name: Norway 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):
RDTyrH65-159: NPLEAVVFEERDGNAVLNLL
FSLRGTKPSSLSRAVKVFET
FEAKIHHLETRPAQRPLAGS
PHLEYFVRFEVPSGDLAALL
SSVRRVSDDVRSA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 358 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 570 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Regulatory Domain of Tyrosine Hydroxylase | 1 |
Entities:
Entity 1, Regulatory Domain of Tyrosine Hydroxylase 93 residues - 10485.973 Da.
| 1 | ASN | PRO | LEU | GLU | ALA | VAL | VAL | PHE | GLU | GLU | ||||
| 2 | ARG | ASP | GLY | ASN | ALA | VAL | LEU | ASN | LEU | LEU | ||||
| 3 | PHE | SER | LEU | ARG | GLY | THR | LYS | PRO | SER | SER | ||||
| 4 | LEU | SER | ARG | ALA | VAL | LYS | VAL | PHE | GLU | THR | ||||
| 5 | PHE | GLU | ALA | LYS | ILE | HIS | HIS | LEU | GLU | THR | ||||
| 6 | ARG | PRO | ALA | GLN | ARG | PRO | LEU | ALA | GLY | SER | ||||
| 7 | PRO | HIS | LEU | GLU | TYR | PHE | VAL | ARG | PHE | GLU | ||||
| 8 | VAL | PRO | SER | GLY | ASP | LEU | ALA | ALA | LEU | LEU | ||||
| 9 | SER | SER | VAL | ARG | ARG | VAL | SER | ASP | ASP | VAL | ||||
| 10 | ARG | SER | ALA |
Samples:
sample_1: RDTyrH65-159, [U-95% 15N], 0.8 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 5%; H2O, [U-100% 2H], 95%
sample_2: RDTyrH65-159, [U-95% 13C; U-95% 15N], 1.0-1.2 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 5%; h2O, [U-100% 2H], 95%
sample_3: RDTyrH65-159 0.9 mM; RDTyrH65-159, [U-2H; U-15N], 0.9 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 5%; H2O, [U-100% 2H], 95%
sample_4: RDTyrH65-159, [U-95% 15N], 0.8 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 5%; Pf1 phage 8 mg/mL; H2O, [U-100% 2H], 95%
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 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D IPAP-HSQC | sample_4 | anisotropic | sample_conditions_1 |
| T1 | sample_1 | isotropic | sample_conditions_1 |
| T2 | sample_1 | isotropic | sample_conditions_1 |
| Relax_NOE | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O, . - refinement, structure solution
ModelFree, Palmer - data analysis
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
PECAN, Eghbalnia, Wang, Bahrami, Assadi, and Markley - chemical shift calculation
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
ProcheckNMR, Laskowski and MacArthur - data analysis
TALOS, Cornilescu, Delaglio and Bax - data analysis
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Related Database Links:
| BMRB | 19480 19481 |
| PDB | |
| DBJ | BAE24067 |
| GB | AAA40434 AAA42257 AAA42258 AAI56669 AAX55332 |
| 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