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BMRB: 36447

7VKV

NMR structure of the zeta-subunit of the F1F0-ATPase from Sinorhizobium meliloti

Authors

Yang, L.Y., Mendoza-Hoffmann, F., Buratto, D.

Assembly

zeta-subunit

Entity

1. zeta-subunit (polymer, Thiol state: not present), 104 monomers, 11600.01 Da Detail

MTTMQDREKA FEAKFALDEE LRFKATARRN KLLGLWAAGL LAKSDPEAYA SEIVAADFEE AGHEDVVRKI KTDFDAAGVA ISEDDIRVRM IELLSEAVAQ LQKN

Formula weight

11600.01 Da

Source organism

Sinorhizobium meliloti 1021

Exptl. method

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 94.2 %, Completeness: 76.6 %, Completeness (bb): 91.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	76.6 % (918 of 1199)	73.1 % (451 of 617)	79.6 % (371 of 466)	82.8 % (96 of 116)
Backbone	91.8 % (571 of 622)	91.9 % (194 of 211)	92.2 % (284 of 308)	90.3 % (93 of 103)
Sidechain	64.8 % (439 of 677)	63.3 % (257 of 406)	69.4 % (179 of 258)	23.1 % (3 of 13)
Aromatic	25.7 % (19 of 74)	32.4 % (12 of 37)	19.4 % (7 of 36)	0.0 % (0 of 1)
Methyl	85.2 % (109 of 128)	85.9 % (55 of 64)	84.4 % (54 of 64)

1. zeta-subunit

MTTMQDREKA FEAKFALDEE LRFKATARRN KLLGLWAAGL LAKSDPEAYA SEIVAADFEE AGHEDVVRKI KTDFDAAGVA ISEDDIRVRM IELLSEAVAQ LQKN

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.8, Details 1.0 mM [U-13C; U-15N] zeta-subunit, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	zeta-subunit	[U-13C; U-15N]	protein	1.0 mM
2	PBS	natural abundance	buffer	25 mM
3	NaCl	natural abundance	salt	50 mM
4	NaN3	natural abundance	salt	4.5 mM
5	H2O	natural abundance	solvent	95 %
6	D2O	[U-2H]	solvent	5 %

Release date

2022-03-01

Citation

NMR structure of the zeta-subunit of the F1F0-ATPase from Sinorhizobium meliloti
Yang, L.Y., Mendoza-Hoffmann, F., Buratto, D.

Related entities 1. zeta-subunit, : 1 : 7 entities Detail

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AVANCE III HD - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.8, Details 1.0 mM [U-13C; U-15N] zeta-subunit, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	zeta-subunit	[U-13C; U-15N]	protein	1.0 mM
2	PBS	natural abundance	buffer	25 mM
3	NaCl	natural abundance	salt	50 mM
4	NaN3	natural abundance	salt	4.5 mM
5	H2O	natural abundance	solvent	95 %
6	D2O	[U-2H]	solvent	5 %

2 5D APSY CBCACONH

Instrument

Bruker AVANCE III HD - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.8, Details 1.0 mM [U-13C; U-15N] zeta-subunit, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	zeta-subunit	[U-13C; U-15N]	protein	1.0 mM
2	PBS	natural abundance	buffer	25 mM
3	NaCl	natural abundance	salt	50 mM
4	NaN3	natural abundance	salt	4.5 mM
5	H2O	natural abundance	solvent	95 %
6	D2O	[U-2H]	solvent	5 %

3 4D APSY HACANH

Instrument

Bruker AVANCE III HD - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.8, Details 1.0 mM [U-13C; U-15N] zeta-subunit, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	zeta-subunit	[U-13C; U-15N]	protein	1.0 mM
2	PBS	natural abundance	buffer	25 mM
3	NaCl	natural abundance	salt	50 mM
4	NaN3	natural abundance	salt	4.5 mM
5	H2O	natural abundance	solvent	95 %
6	D2O	[U-2H]	solvent	5 %

4 5D APSY HACACONH

Instrument

Bruker AVANCE III HD - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.8, Details 1.0 mM [U-13C; U-15N] zeta-subunit, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	zeta-subunit	[U-13C; U-15N]	protein	1.0 mM
2	PBS	natural abundance	buffer	25 mM
3	NaCl	natural abundance	salt	50 mM
4	NaN3	natural abundance	salt	4.5 mM
5	H2O	natural abundance	solvent	95 %
6	D2O	[U-2H]	solvent	5 %

5 3D 1H-13C NOESY aromatic

Instrument

Bruker AVANCE III HD - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.8, Details 1.0 mM [U-13C; U-15N] zeta-subunit, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	zeta-subunit	[U-13C; U-15N]	protein	1.0 mM
2	PBS	natural abundance	buffer	25 mM
3	NaCl	natural abundance	salt	50 mM
4	NaN3	natural abundance	salt	4.5 mM
5	H2O	natural abundance	solvent	95 %
6	D2O	[U-2H]	solvent	5 %

6 3D 1H-15N NOESY

Instrument

Bruker AVANCE III HD - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.8, Details 1.0 mM [U-13C; U-15N] zeta-subunit, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	zeta-subunit	[U-13C; U-15N]	protein	1.0 mM
2	PBS	natural abundance	buffer	25 mM
3	NaCl	natural abundance	salt	50 mM
4	NaN3	natural abundance	salt	4.5 mM
5	H2O	natural abundance	solvent	95 %
6	D2O	[U-2H]	solvent	5 %

7 3D 1H-13C NOESY aliphatic

Instrument

Bruker AVANCE III HD - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.8, Details 1.0 mM [U-13C; U-15N] zeta-subunit, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	zeta-subunit	[U-13C; U-15N]	protein	1.0 mM
2	PBS	natural abundance	buffer	25 mM
3	NaCl	natural abundance	salt	50 mM
4	NaN3	natural abundance	salt	4.5 mM
5	H2O	natural abundance	solvent	95 %
6	D2O	[U-2H]	solvent	5 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr36447_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: bmr36447_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1019		94.2 (chain: 1, length: 104)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 104, Sequence coverage: 94.2%
- Total number of assignments
  - ¹H chemical shifts: 559
  - ¹³C chemical shifts: 364
  - ¹⁵N chemical shifts: 96
- 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

Keywords 4 alpha-helix, F1FO-ATPase binding subunit, PROTEIN BINDING, soluble protein