BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	84.9 % (527 of 621)	77.0 % (248 of 322)	91.9 % (227 of 247)	100.0 % (52 of 52)
Backbone	99.4 % (310 of 312)	98.2 % (107 of 109)	100.0 % (153 of 153)	100.0 % (50 of 50)
Sidechain	74.2 % (264 of 356)	66.2 % (141 of 213)	85.8 % (121 of 141)	100.0 % (2 of 2)
Aromatic	30.0 % (12 of 40)	50.0 % (10 of 20)	10.0 % (2 of 20)
Methyl	93.2 % (69 of 74)	91.9 % (34 of 37)	94.6 % (35 of 37)

1. entity 1

ALFGLGVPEL AVIAGVAALL FGPKKLPEIG KSIGKTVKSF QQAAKEFESE LKT

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 310 K, pH 6.5, Details 200 uM [U-13C; U-15N] core AthTatA, 120 mM NA DHPC-d22, 20 mM NA sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 310 K, pH 6.5, Details 200 uM [U-15N] core AthTatA, 120 mM NA DHPC-d22, 20 mM NA sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
4	core AthTatA	[U-15N]	200 uM
5	DHPC-d22	natural abundance	120 mM
6	sodium phosphate	natural abundance	20 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 7B7O, Strand ID: A Detail

Release date

2021-01-05

Citation

Structure and dynamics of plant TatA in micelles and lipid bilayers studied by solution NMR
Pettersson, P., Ye, W., Jakob, M., Tannert, F., Klosgen, R.B., Maler, L.
FEBS J. (2018), 285, 1886-1906, PubMed 29654717 , DOI 10.1111/febs.14452 , Abstract

Related entities 1. Sec-independent protein translocase protein TATA, chloroplastic, : 1 : 2 : 118 entities Detail

Experiments performed 14 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AVANCE - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 310 K, pH 6.5, Details 200 uM [U-13C; U-15N] core AthTatA, 120 mM NA DHPC-d22, 20 mM NA sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

2 2D 1H-13C HSQC

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

3 3D CBCANH

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

4 3D CBCA(CO)NH

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

5 3D HNCO

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

6 3D HNCACO

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

7 3D 1H-15N NOESY

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

8 3D 1H-15N TOCSY

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

9 3D H(CCO)NH

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

10 3D C(CO)NH

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

11 3D HCCH-TOCSY

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

12 3D HNHA

Instrument

Bruker AVANCE - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 310 K, pH 6.5, Details 200 uM [U-15N] core AthTatA, 120 mM NA DHPC-d22, 20 mM NA sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
4	core AthTatA	[U-15N]	200 uM
5	DHPC-d22	natural abundance	120 mM
6	sodium phosphate	natural abundance	20 mM

13 3D 1H-15N TOCSY

Instrument

Bruker AVANCE - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

14 3D 1H-13C NOESY

Instrument

Bruker AVANCE - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	core AthTatA	[U-13C; U-15N]	200 uM
2	DHPC-d22	natural abundance	120 mM
3	sodium phosphate	natural abundance	20 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34582_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: bmr34582_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	589		100.0 (chain: 1, length: 53)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 53, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 312
  - ¹³C chemical shifts: 226
  - ¹⁵N chemical shifts: 51
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	322	246	76.4
¹³C chemical shifts	247	226	91.5
¹⁵N chemical shifts	52	51	98.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	109	106	97.2
¹³C chemical shifts	106	105	99.1
¹⁵N chemical shifts	50	49	98.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	213	140	65.7
¹³C chemical shifts	141	121	85.8
¹⁵N chemical shifts	2	2	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	37	33	89.2
¹³C chemical shifts	37	35	94.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	20	10	50.0
¹³C chemical shifts	20	2	10.0

Keywords MEMBRANE PROTEIN, amphiphilic helix, bitopic membrane protein, micelles, twin-arginine translocase

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Found 1 Document (0.528 seconds)

BMRB: 34582

Sample #1

Sample #2

Related entities 1. Sec-independent protein translocase protein TATA, chloroplastic, : 1 : 2 : 118 entities Detail

Experiments performed 14 experiments Detail

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Chemical shift validation 3 contents Detail