BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19482

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

Data sets:
Data typeCount
13C chemical shifts358
15N chemical shifts88
1H chemical shifts570

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Regulatory Domain of Tyrosine Hydroxylase1

Entities:

Entity 1, Regulatory Domain of Tyrosine Hydroxylase 93 residues - 10485.973 Da.

1   ASNPROLEUGLUALAVALVALPHEGLUGLU
2   ARGASPGLYASNALAVALLEUASNLEULEU
3   PHESERLEUARGGLYTHRLYSPROSERSER
4   LEUSERARGALAVALLYSVALPHEGLUTHR
5   PHEGLUALALYSILEHISHISLEUGLUTHR
6   ARGPROALAGLNARGPROLEUALAGLYSER
7   PROHISLEUGLUTYRPHEVALARGPHEGLU
8   VALPROSERGLYASPLEUALAALALEULEU
9   SERSERVALARGARGVALSERASPASPVAL
10   ARGSERALA

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D IPAP-HSQCsample_4anisotropicsample_conditions_1
T1sample_1isotropicsample_conditions_1
T2sample_1isotropicsample_conditions_1
Relax_NOEsample_1isotropicsample_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