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BMRB: 4151

1A91

1H, 13C, and 15N Assignment and Secondary Structure of the High pH Form of Subunit c of the F1FO ATP Synthase

Authors

Rastogi, V.K., Girvin, M.E.

Assembly

F1FO ATP Synthase Subunit c

Entity

1. F1FO ATP Synthase Subunit c (polymer, Thiol state: not present), 79 monomers, 8284.044 Da Detail

XENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR TQFFIVMGLV DAIPMIAVGL GLYVMFAVA

Formula weight

8284.044 Da

Source organism

Escherichia coli

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.7 %, Completeness: 90.2 %, Completeness (bb): 97.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	90.2 % (794 of 880)	89.0 % (396 of 445)	89.6 % (319 of 356)	100.0 % (79 of 79)
Backbone	97.6 % (451 of 462)	95.1 % (155 of 163)	98.7 % (221 of 224)	100.0 % (75 of 75)
Sidechain	84.6 % (411 of 486)	85.5 % (241 of 282)	83.0 % (166 of 200)	100.0 % (4 of 4)
Aromatic	100.0 % (56 of 56)	100.0 % (28 of 28)	100.0 % (28 of 28)
Methyl	78.0 % (103 of 132)	86.4 % (57 of 66)	69.7 % (46 of 66)

1. F1FO ATP Synthase Subunit c

XENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR TQFFIVMGLV DAIPMIAVGL GLYVMFAVA

Show sample condition

Sample

Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

Release date

2015-05-06

Citation 1

1H, 13C, and 15N Assignment and Secondary Structure of the High pH Form of Subunit c of the F1FO ATP Synthase
Rastogi, V.K., Girvin, M.E.
J. Biomol. NMR (1999), 13, 91-92, DOI 10.2210/pdb1c99/pdb

Show more 1 citaion

Citation 2

1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI: , Abstract

Hide non-primary 1 citaion

Related entities 1. F1FO ATP Synthase Subunit c, : 1 : 22 : 112 entities Detail

Interaction partners 1. F1FO ATP Synthase Subunit c, : 3 interactors Detail

More details for 3 interactors identified by 3 citations

Experiments performed 12 experiments Detail

1 1H-15N HSQC

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

2 CT 1H-13C HSQC

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

3 HNCO

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

4 1H-15N TOCSY-HSQC

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

5 H(CCO)NH

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

6 C(CO)NH

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

7 HNCACB

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

8 HCCH-COSY

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

9 HCCH-TOCSY

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

10 1H-15N HMQC-NOESY-HSQC

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

11 1H-15N NOESY-HSQC

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

12 HNHA

Instrument

Bruker DRX - 600 MHz

Sample

State isotropic, Temperature 300 K, pH 8.0 (±0.0)

#	Name	Isotope labeling	Type	Concentration
1	F1FO ATP Synthase Subunit c	[U98%-13C; U98%-15N]		1.5 ~ 2.0 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4151_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

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
1	1	FME	N-FORMYLMETHIONINE	Assigned chemical shifts

Content subtype: bmr4151_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	Warning	898		100.0 (chain: 1, length: 79)
1	Chemical shift references	chemical_shift_reference_one	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 79, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 503
  - ¹³C chemical shifts: 315
  - ¹⁵N chemical shifts: 80
- 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