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BMRB: 19480

The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase

Authors

zhang, S., Huang, T., Hinck, A., Fitzpatrick, P.

Assembly

RDTH dimer

Entity

1. RDTH dimer (polymer, Thiol state: not present), 159 monomers, 17174.12 × 2 Da Detail

MPTPSAPSPQ PKGFRRAVSE QDAKQAEAVT SPRFIGRRQS LIEDARKERE AAAAAAAAAV ASSEPGNPLE AVVFEERDGN AVLNLLFSLR GTKPSSLSRA VKVFETFEAK IHHLETRPAQ RPLAGSPHLE YFVRFEVPSG DLAALLSSVR RVSDDVRSA

Total weight

34348.24 Da

Max. entity weight

17174.12 Da

Source organism

Rattus norvegicus

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 90.6 %, Completeness: 29.3 %, Completeness (bb): 52.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	29.3 % (521 of 1777)	16.9 % (157 of 927)	34.2 % (238 of 696)	81.8 % (126 of 154)
Backbone	52.7 % (489 of 928)	42.9 % (134 of 312)	48.9 % (230 of 470)	85.6 % (125 of 146)
Sidechain	10.7 % (107 of 1001)	3.9 % (24 of 615)	21.7 % (82 of 378)	12.5 % (1 of 8)
Aromatic	0.0 % (0 of 100)	0.0 % (0 of 50)	0.0 % (0 of 50)
Methyl	17.6 % (31 of 176)	9.1 % (8 of 88)	26.1 % (23 of 88)

1. regulatory domain of tyrosine hydroxylase

MPTPSAPSPQ PKGFRRAVSE QDAKQAEAVT SPRFIGRRQS LIEDARKERE AAAAAAAAAV ASSEPGNPLE AVVFEERDGN AVLNLLFSLR GTKPSSLSRA VKVFETFEAK IHHLETRPAQ RPLAGSPHLE YFVRFEVPSG DLAALLSSVR RVSDDVRSA

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 300 K, pH 7, Details 1 M leupeptin and 1 M pepstatin A were added as protease inhibitor

#	Name	Isotope labeling	Type	Concentration
1	regulatory domain of tyrosine hydroxylase	[U-95% 13C; U-95% 15N]		0.8 ~ 1.2 mM
2	D2O	natural abundance		5 %
3	H2O	natural abundance		95 %
4	sodium phosphate	natural abundance		50 mM

LACS Plot; CA

Referencing offset: 0.03 ppm, Outliers: 2 Detail

LACS Plot; CB

Referencing offset: 0.03 ppm, Outliers: 2 Detail

Release date

2014-02-11

Citation

The solution structure of the regulatory domain of tyrosine hydroxylase
Zhang, S., Huang, T., Ilangovan, U., Hinck, A.P., Fitzpatrick, P.F.
J. Mol. Biol. (2014), 426, 1483-1497, PubMed 24361276 , DOI 10.1016/j.jmb.2013.12.015 , Abstract

Related entities 1. RDTH dimer, : 2 : 9 entities Detail

Interaction partners 1. RDTH dimer, : 4 interactors Detail

More details for 4 interactors identified by 4 citations

Experiments performed 5 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 300 K, pH 7, Details 1 M leupeptin and 1 M pepstatin A were added as protease inhibitor

#	Name	Isotope labeling	Type	Concentration
1	regulatory domain of tyrosine hydroxylase	[U-95% 13C; U-95% 15N]		0.8 ~ 1.2 mM
2	D2O	natural abundance		5 %
3	H2O	natural abundance		95 %
4	sodium phosphate	natural abundance		50 mM

2 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 300 K, pH 7, Details 1 M leupeptin and 1 M pepstatin A were added as protease inhibitor

#	Name	Isotope labeling	Type	Concentration
1	regulatory domain of tyrosine hydroxylase	[U-95% 13C; U-95% 15N]		0.8 ~ 1.2 mM
2	D2O	natural abundance		5 %
3	H2O	natural abundance		95 %
4	sodium phosphate	natural abundance		50 mM

3 3D HNCA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 300 K, pH 7, Details 1 M leupeptin and 1 M pepstatin A were added as protease inhibitor

#	Name	Isotope labeling	Type	Concentration
1	regulatory domain of tyrosine hydroxylase	[U-95% 13C; U-95% 15N]		0.8 ~ 1.2 mM
2	D2O	natural abundance		5 %
3	H2O	natural abundance		95 %
4	sodium phosphate	natural abundance		50 mM

4 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 300 K, pH 7, Details 1 M leupeptin and 1 M pepstatin A were added as protease inhibitor

#	Name	Isotope labeling	Type	Concentration
1	regulatory domain of tyrosine hydroxylase	[U-95% 13C; U-95% 15N]		0.8 ~ 1.2 mM
2	D2O	natural abundance		5 %
3	H2O	natural abundance		95 %
4	sodium phosphate	natural abundance		50 mM

5 3D HCACO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 300 K, pH 7, Details 1 M leupeptin and 1 M pepstatin A were added as protease inhibitor

#	Name	Isotope labeling	Type	Concentration
1	regulatory domain of tyrosine hydroxylase	[U-95% 13C; U-95% 15N]		0.8 ~ 1.2 mM
2	D2O	natural abundance		5 %
3	H2O	natural abundance		95 %
4	sodium phosphate	natural abundance		50 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr19480_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr19480_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	463		89.9 (chain: 1, length: 159)
1	Chemical shift references	chemical_shift_reference_1	OK	4		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 159, Sequence coverage: 89.9%
- Total number of assignments
  - ¹³C chemical shifts: 217
  - ¹⁵N chemical shifts: 123
  - ¹H chemical shifts: 123
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Keywords ACT domain, NMR spectroscopy, regulation, Tyrosine hydroxylase