BMRB Entry 19480

Title:
The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase
Deposition date:
2013-09-06
Original release date:
2014-02-12
Authors:
zhang, shengnan; Huang, Tao; Hinck, Andrew; Fitzpatrick, Paul
Citation:

Citation: Zhang, Shengnan; Huang, Tao; Ilangovan, Udayar; Hinck, Andrew; Fitzpatrick, Paul. "The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase."  J. Mol. Biol. 426, 1483-1497 (2013).
PubMed: 24361276

Assembly members:

Assembly members:
regulatory_domain_of_tyrosine_hydroxylase, polymer, 159 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETNTERM

Data sets:
Data typeCount
13C chemical shifts217
15N chemical shifts123
1H chemical shifts123

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1RDTH, chain 11
2RDTH, chain 21

Entities:

Entity 1, RDTH, chain 1 159 residues - Formula weight is not available

1   METPROTHRPROSERALAPROSERPROGLN
2   PROLYSGLYPHEARGARGALAVALSERGLU
3   GLNASPALALYSGLNALAGLUALAVALTHR
4   SERPROARGPHEILEGLYARGARGGLNSER
5   LEUILEGLUASPALAARGLYSGLUARGGLU
6   ALAALAALAALAALAALAALAALAALAVAL
7   ALASERSERGLUPROGLYASNPROLEUGLU
8   ALAVALVALPHEGLUGLUARGASPGLYASN
9   ALAVALLEUASNLEULEUPHESERLEUARG
10   GLYTHRLYSPROSERSERLEUSERARGALA
11   VALLYSVALPHEGLUTHRPHEGLUALALYS
12   ILEHISHISLEUGLUTHRARGPROALAGLN
13   ARGPROLEUALAGLYSERPROHISLEUGLU
14   TYRPHEVALARGPHEGLUVALPROSERGLY
15   ASPLEUALAALALEULEUSERSERVALARG
16   ARGVALSERASPASPVALARGSERALA

Samples:

sample_1: 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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_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 19481 19482
PDB
GB AAA40434 AAA42257 AAA42258 AAB59722 AAI56669
REF NP_033403 NP_036872
SP P04177 P24529
AlphaFold P04177 P24529

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks