BMRBj - BMREntryMaster

Found 1 Document (0.525 seconds)

BMRB: 27232

7WEM

13C chemical shifts of solid-state NMR signals of subunit c-ring of TFoF1 ATP synthase

Authors

Akutsu, H., Kang, S., Todokoro, Y., Bak, S., Suzuki, T., Yoshida, M., Fujiwara, T.

Assembly

subunit c ring of FoF1 ATP synthase

Entity

1. subunit c ring of FoF1 ATP synthase (polymer, Thiol state: not present), 72 monomers, 7383.806 Da Detail

MHLGVLAAAI AVGLGALGAG IGNGLIVSRT IEGIARQPEL RPVLQTTMFI GVALVEALPI IGVVFSFIYL GR

Formula weight

7383.806 Da

Source organism

Bacillus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.6 %, Completeness: 88.9 %, Completeness (bb): 96.6 % Detail

Polymer type: polypeptide(L)

	Total	¹³C
All	88.9 % (289 of 325)	88.9 % (289 of 325)
Backbone	96.6 % (198 of 205)	96.6 % (198 of 205)
Sidechain	83.4 % (151 of 181)	83.4 % (151 of 181)
Aromatic	23.8 % (5 of 21)	23.8 % (5 of 21)
Methyl	84.8 % (56 of 66)	84.8 % (56 of 66)

1. FoF1 ATP synthase subunit c

MHLGVLAAAI AVGLGALGAG IGNGLIVSRT IEGIARQPEL RPVLQTTMFI GVALVEALPI IGVVFSFIYL GR

Show sample condition

Sample #1

Solvent system DMPC-d54 or POPC-d31, Temperature 248 K, pH 7.5, Details reverse-labeled(delete HRIVL)

#	Name	Isotope labeling	Type	Concentration
1	FoF1 ATP synthase subunit c-ring	[U-13C]		3 mg

Sample #2

Solvent system DMPC-d54 or POPC-d31, Temperature 248 K, pH 7.5, Details reverse-labeled(delete RIFTPMN)

#	Name	Isotope labeling	Type	Concentration
2	FoF1 ATP synthase subunit c-ring	[U-13C]		3 mg

Sample #3

Solvent system DMPC-d54 or POPC-d31, Temperature 248 K, pH 7.5, Details reverse-labeled(delete VLFP)

#	Name	Isotope labeling	Type	Concentration
3	FoF1 ATP synthase subunit c-ring	[U-13C]		3 mg

Release date

2017-08-23

Citation

Direct assignment of ¹³C solid-state NMR signals of TF_oF₁ ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure
Kang, S.J., Todokoro, Y., Bak, S., Suzuki, T., Yoshida, M., Fujiwara, T., Akutsu, H.
J. Biomol. NMR (2017), 70, 53-65, PubMed 29197977 , DOI 10.1007/s10858-017-0158-x , Abstract

Related entities 1. subunit c ring of FoF1 ATP synthase, : 1 : 8 : 166 entities Detail

Experiments performed 6 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr27232_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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr27232_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	294		97.2 (chain: 1, length: 72)
1	Chemical shift references	chemical_shift_reference_1	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 72, Sequence coverage: 97.2%
- Total number of assignments
  - ¹³C chemical shifts: 294
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
23	ASN	CG	170.7
32	GLU	CD	183.1
37	GLN	CD	180.9
39	GLU	CD	182.6
49	PHE	CG	134.8
56	GLU	CD	174.5
69	TYR	CG	129.7
69	TYR	CZ	158.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	325	286	88.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	144	136	94.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	181	150	82.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	68	56	82.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	21	5	23.8

Keywords CP/MAS NMR, FoF1-ATP synthase, lipid-protein interaction, membrane protein, secondary structure, specific isotope labeling

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Found 1 Document (0.525 seconds)

BMRB: 27232

Sample #1

Sample #2

Sample #3

Related entities 1. subunit c ring of FoF1 ATP synthase, : 1 : 8 : 166 entities Detail

Experiments performed 6 experiments Detail

Instrument

Sample

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Sample

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Instrument

Sample

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Sample

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Chemical shift validation 3 contents Detail