BMRB Entry 19481

Name: The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase
Published: 2014-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19481

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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; 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:
Ser40_phosphorylated_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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ser40_phosphorylated_regulatory_domain_of_tyrosine_hydroxylase: MPTPSAPSPQPKGFRRAVSE QDAKQAEAVTSPRFIGRRQS LIEDARKEREAAAAAAAAAV ASSEPGNPLEAVVFEERDGN AVLNLLFSLRGTKPSSLSRA VKVFETFEAKIHHLETRPAQ RPLAGSPHLEYFVRFEVPSG DLAALLSSVRRVSDDVRSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	223
15N chemical shifts	127
1H chemical shifts	127

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

ALA

VAL

SER

GLU

3

GLN

ASP

ALA

LYS

GLN

ALA

GLU

ALA

VAL

THR

4

SER

PRO

ARG

PHE

ILE

GLY

ARG

GLN

SER

5

LEU

ILE

GLU

ASP

ALA

ARG

LYS

GLU

ARG

GLU

6

ALA

VAL

7

ALA

SER

GLU

PRO

GLY

ASN

PRO

LEU

GLU

8

ALA

VAL

PHE

GLU

ARG

ASP

GLY

ASN

9

ALA

VAL

LEU

ASN

LEU

PHE

SER

LEU

ARG

10

GLY

THR

LYS

PRO

SER

LEU

SER

ARG

ALA

11

VAL

LYS

VAL

PHE

GLU

THR

PHE

GLU

ALA

LYS

12

ILE

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

LEU

SER

VAL

ARG

16

ARG

VAL

SER

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

BMRB	19480 19482
PDB	2MDA
GB	AAA40434 AAA42257 AAA42258 AAB59722 AAI56669
REF	NP_033403 NP_036872
SP	P04177 P24529
AlphaFold	P04177 P24529