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BMRB: 51096

1H, 13C and 15N chemical shift assignments of the GYF cytoplasmic domain of the GltJ protein from Myxococcus xanthus

Authors

Attia, B., Serrano, B., Bornet, O., Guerlesquin, F., Elantak, L.

Assembly

GltJ-GYF

Entity

1. GltJ-GYF (polymer, Thiol state: all free), 88 monomers, 9600.632 Da Detail

GSHMDKEEAK ANAAAHEWYV AIDEKQVGPF NVEKVKDLWD RGEVGPDSLC WRSGFSDWIP LSETAELASV LAPRPSKPVI VAPEPVSG

Formula weight

9600.632 Da

Source organism

Myxococcus xanthus

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.6 %, Completeness: 87.2 %, Completeness (bb): 93.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	87.2 % (869 of 996)	85.6 % (441 of 515)	87.7 % (343 of 391)	94.4 % (85 of 90)
Backbone	93.6 % (479 of 512)	92.0 % (160 of 174)	94.6 % (244 of 258)	93.8 % (75 of 80)
Sidechain	83.0 % (470 of 566)	82.4 % (281 of 341)	83.3 % (179 of 215)	100.0 % (10 of 10)
Aromatic	69.0 % (58 of 84)	69.0 % (29 of 42)	65.8 % (25 of 38)	100.0 % (4 of 4)
Methyl	87.8 % (79 of 90)	93.3 % (42 of 45)	82.2 % (37 of 45)

1. entity 1

GSHMDKEEAK ANAAAHEWYV AIDEKQVGPF NVEKVKDLWD RGEVGPDSLC WRSGFSDWIP LSETAELASV LAPRPSKPVI VAPEPVSG

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

Release date

2021-09-22

Citation

¹H, ¹³C and ¹⁵N chemical shift assignments of the ZnR and GYF cytoplasmic domains of the GltJ protein from Myxococcus xanthus
Attia, B., Serrano, B., Bornet, O., Guerlesquin, F., My, L., Castaing, J.P., Mignot, T., Elantak, L.
Biomol. NMR Assign. (2022), 16, 219-223, PubMed 35445965 , DOI 10.1007/s12104-022-10083-6 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 51104 released on 2021-09-26
Title 1H, 13C and 15N chemical shift assignments of the ZnR and GYF cytoplasmic domains of the GltJ protein from Myxococcus xanthus

Related entities 1. GltJ-GYF, : 1 entities Detail

Experiments performed 10 experiments Detail

1 3D HNCO

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

2 3D HN(CA)CO

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

3 3D HN(CO)CA

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

4 3D HNCA

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

5 3D HN(CO)CACB

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

6 3D HNCACB

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

7 3D HCCH-TOCSY

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

8 3D 1H-15N NOESY

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

9 3D 1H-15N TOCSY

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

10 3D 1H-13C NOESY

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	GltJ-GYF	[U-100% 13C; U-100% 15N]		1 mM
2	sodium phosphate	natural abundance		10 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr51096_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: bmr51096_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	947		96.6 (chain: 1, length: 88)
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: 88, Sequence coverage: 96.6%
- Total number of assignments
  - ¹³C chemical shifts: 341
  - ¹H chemical shifts: 521
  - ¹⁵N chemical shifts: 85
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- 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