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BMRB: 27354

5ZCZ

1H, 13C, and 15N Chemical Shift Assignments for the Thermus thermophilus HB8 TTHA1718 protein in sf9 cells by in-cell NMR spectroscopy

Authors

Ito, Y., Ikeya, T., Tanaka, T., Kamoshida, H., Mishima, M., Shirakawa, M., Guentert, P.

Assembly

the Thermus thermophilus HB8 TTHA1718 protein

Entity

1. the Thermus thermophilus HB8 TTHA1718 protein (polymer, Thiol state: all free), 66 monomers, 7041.243 Da Detail

MLKLKVEGMT CNHCVMAVTK ALKKVPGVEK VEVSLEKGEA LVEGTADPKA LVQAVEEEGY KAEVLA

Formula weight

7041.243 Da

Source organism

Thermus thermophilus

Exptl. method

Refine. method

energy minimization

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.5 %, Completeness: 49.1 %, Completeness (bb): 59.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	49.1 % (365 of 743)	54.4 % (209 of 384)	34.1 % (100 of 293)	84.8 % (56 of 66)
Backbone	59.9 % (235 of 392)	81.5 % (110 of 135)	35.8 % (69 of 193)	87.5 % (56 of 64)
Sidechain	34.5 % (142 of 412)	39.8 % (99 of 249)	26.7 % (43 of 161)	0.0 % (0 of 2)
Aromatic	0.0 % (0 of 12)	0.0 % (0 of 6)	0.0 % (0 of 6)
Methyl	80.9 % (76 of 94)	83.0 % (39 of 47)	78.7 % (37 of 47)

1. TTHA1718

MLKLKVEGMT CNHCVMAVTK ALKKVPGVEK VEVSLEKGEA LVEGTADPKA LVQAVEEEGY KAEVLA

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

Protein Blocks Logo

Calculated from 20 models in PDB: 5ZCZ, Strand ID: A Detail

Release date

2018-01-10

Citation

High-Resolution Protein 3D Structure Determination in Living Eukaryotic Cells
Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Guntert, P., Ito, Y.
Angew. Chem Int Ed Engl. (2019), 58, 7284-7288, PubMed 30938016 , DOI 10.1002/anie.201900840 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 27356 released on 2018-01-10
Title 1H, 13C, and 15N Chemical Shift Assignments for ubiquitin in sf9 cells by in-cell NMR spectroscopy

Related entities 1. the Thermus thermophilus HB8 TTHA1718 protein, : 1 : 2 : 403 entities Detail

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

2 2D 1H-13C HSQC

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

3 3D HNCO

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

4 3D HNCA

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

5 3D HN(CO)CA

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

6 3D CBCA(CO)NH

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

7 3D HCCH-TOCSY

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

8 3D HBHA(CO)NH

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

9 3D 1H-15N NOESY

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

10 3D 1H-13C NOESY

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K

#	Name	Isotope labeling	Type	Concentration
1	TTHA1718	[U-100% 15N]		50 (±12.0) uM
2	TTHA1718	[U-100% 13C; U-100% 15N]		50 (±12.0) uM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr27354_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: bmr27354_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	432		95.5 (chain: 1, length: 66)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 66, Sequence coverage: 95.5%
- Total number of assignments
  - ¹H chemical shifts: 287
  - ¹³C chemical shifts: 89
  - ¹⁵N chemical shifts: 56
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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 in-cell NMR, protein structure determination, sf9 cell