BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	85.5 % (916 of 1071)	84.1 % (467 of 555)	84.9 % (361 of 425)	96.7 % (88 of 91)
Backbone	96.9 % (529 of 546)	97.8 % (180 of 184)	96.4 % (265 of 275)	96.6 % (84 of 87)
Sidechain	77.2 % (474 of 614)	77.4 % (287 of 371)	76.6 % (183 of 239)	100.0 % (4 of 4)
Aromatic	17.5 % (14 of 80)	35.0 % (14 of 40)	0.0 % (0 of 40)
Methyl	96.6 % (112 of 116)	96.6 % (56 of 58)	96.6 % (56 of 58)

1. RDTyrH65-159

NPLEAVVFEE RDGNAVLNLL FSLRGTKPSS LSRAVKVFET FEAKIHHLET RPAQRPLAGS PHLEYFVRFE VPSGDLAALL SSVRRVSDDV RSA

Show sample condition

Sample #1

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	Concentration
1	RDTyrH65-159	[U-95% 15N]	0.8 mM
2	sodium phosphate	natural abundance	50 mM
3	D2O	[U-100% 2H]	5 %
4	H2O	[U-100% 2H]	95 %

Sample #2

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

Sample #3

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	Concentration
9	RDTyrH65-159	natural abundance	0.9 mM
10	RDTyrH65-159	[U-2H; U-15N]	0.9 mM
11	sodium phosphate	natural abundance	50 mM
12	D2O	[U-100% 2H]	5 %
13	H2O	[U-100% 2H]	95 %

Sample #4

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	Concentration
14	RDTyrH65-159	[U-95% 15N]	0.8 mM
15	sodium phosphate	natural abundance	50 mM
16	D2O	[U-100% 2H]	5 %
17	Pf1 phage	natural abundance	8 mg/mL
18	H2O	[U-100% 2H]	95 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.17 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.17 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.07 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.37 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2MDA, Strand ID: A, B Detail

Release date

2014-01-01

Citation

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

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 19480 released on 2014-02-11
    Title The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase
  BMRB: 19481 released on 2014-02-11
    Title The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase

Related entities 1. Regulatory Domain of Tyrosine Hydroxylase, : 1 : 2 : 2 : 19 entities Detail

Interaction partners 1. Regulatory Domain of Tyrosine Hydroxylase, : 3 interactors Detail

More details for 3 interactors identified by 3 citations

Experiments performed 20 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	Concentration
1	RDTyrH65-159	[U-95% 15N]	0.8 mM
2	sodium phosphate	natural abundance	50 mM
3	D2O	[U-100% 2H]	5 %
4	H2O	[U-100% 2H]	95 %

2 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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

3 2D 1H-13C 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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

4 3D CBCA(CO)NH

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

5 3D C(CO)NH

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

6 3D HNCO

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

7 3D HNCA

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

8 3D HNCACB

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

9 3D HBHA(CO)NH

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

10 3D HN(CO)CA

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

11 3D H(CCO)NH

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

12 3D HCCH-TOCSY

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

13 3D HNHA

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

14 3D 1H-15N NOESY

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	Concentration
1	RDTyrH65-159	[U-95% 15N]	0.8 mM
2	sodium phosphate	natural abundance	50 mM
3	D2O	[U-100% 2H]	5 %
4	H2O	[U-100% 2H]	95 %

15 3D 1H-15N NOESY

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	Concentration
9	RDTyrH65-159	natural abundance	0.9 mM
10	RDTyrH65-159	[U-2H; U-15N]	0.9 mM
11	sodium phosphate	natural abundance	50 mM
12	D2O	[U-100% 2H]	5 %
13	H2O	[U-100% 2H]	95 %

16 3D 1H-13C NOESY

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	Concentration
5	RDTyrH65-159	[U-95% 13C; U-95% 15N]	1.0-1.2 mM
6	sodium phosphate	natural abundance	50 mM
7	D2O	[U-100% 2H]	5 %
8	h2O	[U-100% 2H]	95 %

17 2D IPAP-HSQC

Instrument

Bruker Avance - 700 MHz

Sample

State anisotropic, 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	Concentration
14	RDTyrH65-159	[U-95% 15N]	0.8 mM
15	sodium phosphate	natural abundance	50 mM
16	D2O	[U-100% 2H]	5 %
17	Pf1 phage	natural abundance	8 mg/mL
18	H2O	[U-100% 2H]	95 %

18 T1

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	Concentration
1	RDTyrH65-159	[U-95% 15N]	0.8 mM
2	sodium phosphate	natural abundance	50 mM
3	D2O	[U-100% 2H]	5 %
4	H2O	[U-100% 2H]	95 %

19 T2

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	Concentration
1	RDTyrH65-159	[U-95% 15N]	0.8 mM
2	sodium phosphate	natural abundance	50 mM
3	D2O	[U-100% 2H]	5 %
4	H2O	[U-100% 2H]	95 %

20 Relax_NOE

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	Concentration
1	RDTyrH65-159	[U-95% 15N]	0.8 mM
2	sodium phosphate	natural abundance	50 mM
3	D2O	[U-100% 2H]	5 %
4	H2O	[U-100% 2H]	95 %

NMR combined restraints 10 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_19482_2mda.nef
Input source #2: Coordindates	2mda.cif
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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

----70--------80--------90-------100-------110-------120-------130-------140-------150---------
PGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA
--------10--------20--------30--------40--------50--------60--------70--------80--------90-----

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

----70--------80--------90-------100-------110-------120-------130-------140-------150---------
PGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA
--------10--------20--------30--------40--------50--------60--------70--------80--------90-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	95	0	0	100.0
B	B	95	0	0	100.0

Content subtype: combined_19482_2mda.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	906		95.8 (chain: A, length: 95)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	22 (1)	noe	13.7 (chain: A, length: 95), 13.7 (chain: B, length: 95)
2	Distance restraints	CNS/XPLOR_distance_constraints_5	Warning	16 (1)	noe	7.4 (chain: A, length: 95), 6.3 (chain: B, length: 95)
3	Distance restraints	CNS/XPLOR_distance_constraints_10	Warning	1802 (1)	noe	95.8 (chain: A, length: 95), 95.8 (chain: B, length: 95)
4	Distance restraints	CNS/XPLOR_distance_constraints_8	Warning	1272 (1)	noe	93.7 (chain: A, length: 95), 93.7 (chain: B, length: 95)
5	Distance restraints	CNS/XPLOR_distance_constraints_9	OK	2 (1)	noe	No information
1	Dihedral angle restraints	CNS/XPLOR_dihedral_6	OK	138 (138)	.	87.4 (chain: A, length: 95)
2	Dihedral angle restraints	CNS/XPLOR_dihedral_7	OK	138 (138)	.	87.4 (chain: A, length: 95)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_3	OK	112 (112)	.	58.9 (chain: A, length: 95), 58.9 (chain: B, length: 95)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 95, Sequence coverage: 95.8%
- Total number of assignments
  - ¹H chemical shifts: 460
  - ¹³C chemical shifts: 358
  - ¹⁵N chemical shifts: 88
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	565	460	81.4
¹³C chemical shifts	432	358	82.9
¹⁵N chemical shifts	101	88	87.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	188	180	95.7
¹³C chemical shifts	190	177	93.2
¹⁵N chemical shifts	88	84	95.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	377	280	74.3
¹³C chemical shifts	242	181	74.8
¹⁵N chemical shifts	13	4	30.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	58	55	94.8
¹³C chemical shifts	58	55	94.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	14	35.0
¹³C chemical shifts	40	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 95, Sequence coverage: 13.7%
  - Entity_assembly_ID: B, Chain length: 95, Sequence coverage: 13.7%
- Total number of restraints: 22
- Weight of restraints: 1.0 (22)
- Potential type of restraints: square-well-parabolic (22)
- Range of distance target values: 3.16, 4.74 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_5
  - Status: Warning
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 95, Sequence coverage: 7.4%
    - Entity_assembly_ID: B, Chain length: 95, Sequence coverage: 6.3%
  - Total number of restraints: 16
  - Weight of restraints: 1.0 (16)
  - Potential type of restraints: square-well-parabolic (16)
  - Range of distance target values: 3.4, 3.4 (Å)
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
  - Distance restraints on contact map
  - Saveframe: CNS/XPLOR_distance_constraints_10
    - Status: Warning
    - Experiment type: noe
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 95, Sequence coverage: 95.8%
      - Entity_assembly_ID: B, Chain length: 95, Sequence coverage: 95.8%
    - Total number of restraints: 1802
    - Weight of restraints: 1.0 (1802)
    - Potential type of restraints: square-well-parabolic (1802)
    - Range of distance target values: 1.97, 5.04 (Å)
    - Histogram of distance target values
    - Histogram of discrepancy in distance target values
    - Distance restraints per residue
      - Chain_ID: A
      - Chain_ID: B
    - Distance restraints on contact map
    - Saveframe: CNS/XPLOR_distance_constraints_8
      - Status: Warning
      - Experiment type: noe
      - Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 95, Sequence coverage: 93.7%
        ----70--------80--------90-------100-------110-------120-------130-------140-------150--------- PGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA |||||||||||||||||||||||||| |||||||||| ||||||||||||||||||| |||||||||||||||||||||||||||||||||| ..NPLEAVVFEERDGNAVLNLLFSLRGT..SSLSRAVKVF.TFEAKIHHLETRPAQRPLA.SPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA
        Entity_assembly_ID: B, Chain length: 95, Sequence coverage: 93.7%
        ----70--------80--------90-------100-------110-------120-------130-------140-------150--------- PGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA |||||||||||||||||||||||||| |||||||||| ||||||||||||||||||| |||||||||||||||||||||||||||||||||| ..NPLEAVVFEERDGNAVLNLLFSLRGT..SSLSRAVKVF.TFEAKIHHLETRPAQRPLA.SPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA
      - Total number of restraints: 1272
        Intra-residue restraints, i = j : 612
        Sequential restraints, | i - j | = 1 : 228
        Backbone-backbone: 26
        Backbone-side chain: 142
        Side chain-side chain: 60
        Medium range restraints, 1 < | i - j | < 5 : 144
        Backbone-backbone: 20
        Backbone-side chain: 74
        Side chain-side chain: 50
        Long range restraints, | i - j | >= 5 : 288
      - Weight of restraints: 1.0 (1272)
        Intra-residue restraints, i = j : 1.0 (612)
        Sequential restraints, | i - j | = 1 : 1.0 (228)
        Backbone-backbone: 1.0 (26)
        Backbone-side chain: 1.0 (142)
        Side chain-side chain: 1.0 (60)
        Medium range restraints, 1 < | i - j | < 5 : 1.0 (144)
        Backbone-backbone: 1.0 (20)
        Backbone-side chain: 1.0 (74)
        Side chain-side chain: 1.0 (50)
        Long range restraints, | i - j | >= 5 : 1.0 (288)
      - Potential type of restraints: square-well-parabolic (1272)
        Intra-residue restraints, i = j : square-well-parabolic (612)
        Sequential restraints, | i - j | = 1 : square-well-parabolic (228)
        Backbone-backbone: square-well-parabolic (26)
        Backbone-side chain: square-well-parabolic (142)
        Side chain-side chain: square-well-parabolic (60)
        Medium range restraints, 1 < | i - j | < 5 : square-well-parabolic (144)
        Backbone-backbone: square-well-parabolic (20)
        Backbone-side chain: square-well-parabolic (74)
        Side chain-side chain: square-well-parabolic (50)
        Long range restraints, | i - j | >= 5 : square-well-parabolic (288)
      - Range of distance target values: 1.79, 6.4 (Å)
      - Histogram of distance target values
      - Histogram of discrepancy in distance target values
      - Distance restraints per residue
        Chain_ID: A
        Chain_ID: B
      - Distance restraints on contact map
        Chain_ID_1: A - Chain_ID_2: A
        Chain_ID_1: B - Chain_ID_2: B
      - Saveframe: CNS/XPLOR_distance_constraints_9
        Status: OK
        Experiment type: noe
        Total number of restraints: 2
        Intra-residue restraints, i = j : 2
        Weight of restraints: 1.0 (2)
        Intra-residue restraints, i = j : 1.0 (2)
        Potential type of restraints: square-well-parabolic (2)
        Intra-residue restraints, i = j : square-well-parabolic (2)
        Range of distance target values: 2.63, 2.63 (Å)
        Distance restraints per residue
        Chain_ID: A
        Chain_ID: B
        Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_6
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 95, Sequence coverage: 87.4%
- Total number of restraints: 138
- Total number of restraints per polymer type: 138
- Weight of restraints: 1.0 (138)
- Potential type of restraints: square-well-parabolic (138)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
- Saveframe: CNS/XPLOR_dihedral_7
  - Status: OK
  - Experiment type: .
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 95, Sequence coverage: 87.4%
  - Total number of restraints: 138
  - Total number of restraints per polymer type: 138
  - Weight of restraints: 1.0 (138)
  - Potential type of restraints: square-well-parabolic (138)
  - Plot of Phi-Psi angle restraints
  - Dihedral angle restraints per residue
    - Chain_ID: A

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_3

Status: OK
Experiment type: .

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 95, Sequence coverage: 58.9%

----70--------80--------90-------100-------110-------120-------130-------140-------150---------
PGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA
    |||||| || | ||||| ||| |    |||    ||  ||||||| |   |||    |    |  |||| ||||   ||||||| ||| ||
....LEAVVF.ER.G.AVLNL.FSL.G....SLS....VF..FEAKIHH.E...AQR....S....Y..RFEV.SGDL...LSSVRRV.DDV.SA

Entity_assembly_ID: B, Chain length: 95, Sequence coverage: 58.9%

----70--------80--------90-------100-------110-------120-------130-------140-------150---------
PGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSA
    |||||| || | ||||| ||| |    |||    ||  ||||||| |   |||    |    |  |||| ||||   ||||||| ||| ||
....LEAVVF.ER.G.AVLNL.FSL.G....SLS....VF..FEAKIHH.E...AQR....S....Y..RFEV.SGDL...LSSVRRV.DDV.SA

Total number of restraints: 112
Potential type of restraints: undefined (112)
Range of observed RDC values: 100.0, -100.0 (Hz)
RDC restraints per residue
- Chain_ID: A
  None
- Chain_ID: B
  None

Keywords ACT domain, NMR Spectroscopy, regulation, Tyrosine hydroxylase

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BMRB: 19482

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Entries sharing articles BMRB: 2 entries Detail

Related entities 1. Regulatory Domain of Tyrosine Hydroxylase, : 1 : 2 : 2 : 19 entities Detail

Interaction partners 1. Regulatory Domain of Tyrosine Hydroxylase, : 3 interactors Detail

Experiments performed 20 experiments Detail

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NMR combined restraints 10 contents Detail