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BMRB: 27466

6GF2

Chemical shift assignments of the C-terminal domain of human FAT10

Authors

Aichem, A., Anders, S., Catone, N., Roessler, P., Stotz, S., Berg, A., Schwab, R., Scheuermann, S., Bialas, J., Schmidtke, G., Peter, C., Groettrup, M., Wiesner, S.

Assembly

FAT10 C-terminal domain

Entity

1. FAT10 C-terminal domain (polymer, Thiol state: all free), 85 monomers, 9251.601 Da Detail

GAMGDEELPL FLVESGDEAK RHLLQVRRSS SVAQVKAMIE TKTGIIPETQ IVTLNGKRLE DGKMMADYGI RKGNLLFLAS YSIGG

Formula weight

9251.601 Da

Source organism

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 9.4 %, Completeness: 3.9 %, Completeness (bb): 5.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	3.9 % (38 of 971)	3.6 % (18 of 506)	4.5 % (17 of 377)	3.4 % (3 of 88)
Backbone	5.1 % (26 of 506)	4.5 % (8 of 178)	6.1 % (15 of 245)	3.6 % (3 of 83)
Sidechain	3.1 % (17 of 540)	3.0 % (10 of 328)	3.4 % (7 of 207)	0.0 % (0 of 5)
Aromatic	0.0 % (0 of 40)	0.0 % (0 of 20)	0.0 % (0 of 20)
Methyl	0.0 % (0 of 104)	0.0 % (0 of 52)	0.0 % (0 of 52)

1. fat10 c

GAMGDEELPL FLVESGDEAK RHLLQVRRSS SVAQVKAMIE TKTGIIPETQ IVTLNGKRLE DGKMMADYGI RKGNLLFLAS YSIGG

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

Release date

2018-04-24

Citation

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation
Aichem, A., Anders, S., Catone, N., Rossler, P., Stotz, S., Berg, A., Schwab, R., Scheuermann, S., Bialas, J., Schutz-Stoffregen, M.C., Schmidtke, G., Peter, C., Groettrup, M., Wiesner, S.
Nat. Commun. (2018), 9, 3321-3321, PubMed 30127417 , DOI 10.1038/s41467-018-05776-3 , Abstract

Related entities 1. FAT10 C-terminal domain, : 1 : 2 : 6 entities Detail

Interaction partners 1. FAT10 C-terminal domain, : 4 interactors Detail

More details for 4 interactors identified by 3 citations

Experiments performed 11 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

3 3D HNCACB

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

4 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

5 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

6 3D HBHA(CO)NH

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

7 3D HNHA

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

8 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

9 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

10 3D 1H-13C NOESY

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

11 2D 1H-1H NOESY

Instrument

Bruker Avance - 600 MHz Chemical shift assignment

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Type	Concentration
1	fat10_c	[U-100% 13C; U-100% 15N]		2 mM
2	sodium chloride	natural abundance		150 mM
3	sodium phosphate	natural abundance		20 mM

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_27466_6gf2.nef
Input source #2: Coordindates	6gf2.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80-----
GAMGDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTLNGKRLEDGKMMADYGIRKGNLLFLASYSIGG
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GAMGDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTLNGKRLEDGKMMADYGIRKGNLLFLASYSIGG

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	85	0	0	100.0

Content subtype: combined_27466_6gf2.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	12		5.9 (chain: A, length: 85)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	2337 (1)	noe	98.8 (chain: A, length: 85)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	76 (1)	hbond	57.6 (chain: A, length: 85)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	136 (136)	.	89.4 (chain: A, length: 85)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 85, Sequence coverage: 5.9%
- Total number of assignments
  - ¹³C chemical shifts: 6
  - ¹H chemical shifts: 5
  - ¹⁵N chemical shifts: 1
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 85, Sequence coverage: 98.8%
- Total number of restraints: 2337
- Weight of restraints: 1.0 (2337)
- Potential type of restraints: square-well-parabolic (2337)
- Range of distance target values: 1.65, 4.0 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 85, Sequence coverage: 57.6%
  - Total number of restraints: 76
  - Weight of restraints: 1.0 (76)
  - Potential type of restraints: square-well-parabolic (76)
  - Range of distance target values: 1.85, 3.05 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 85, Sequence coverage: 89.4%
- Total number of restraints: 136
- Total number of restraints per polymer type: 136
- Weight of restraints: 1.0 (136)
- Potential type of restraints: square-well-parabolic (136)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords FAT10, degradation, proteasome, ubiquitin-like modifier, vcp