BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	85.6 % (734 of 857)	85.7 % (378 of 441)	83.4 % (281 of 337)	94.9 % (75 of 79)
Backbone	94.2 % (426 of 452)	94.2 % (147 of 156)	93.8 % (210 of 224)	95.8 % (69 of 72)
Sidechain	78.9 % (375 of 475)	81.1 % (231 of 285)	75.4 % (138 of 183)	85.7 % (6 of 7)
Aromatic	43.1 % (25 of 58)	58.6 % (17 of 29)	25.0 % (7 of 28)	100.0 % (1 of 1)
Methyl	83.7 % (77 of 92)	97.8 % (45 of 46)	69.6 % (32 of 46)

1. entity 1

MSEYIRVTED ENDEPIEIPS EDDGTVLLST VTAQFPGASG LRYRNPVSQS MRGVRLVEGI LHAPDAGWGN LVYVVNY

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 1 mM U-99% 13C; U-99% 15N TDP(1-77)-GB1-C39/C50S, 20 mM sodium phosphate, 50 mM sodium chloride, 0.05 v/v sodium azide, 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.01 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.01 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.05 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.38 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 5X4F, Strand ID: A Detail

Release date

2017-05-22

Citation

The N-terminal dimerization is required for TDP-43 splicing activity
Jiang, L.L., Xue, W., Hong, J.Y., Zhang, J.T., Li, M.J., Yu, S.N., He, J.H., Hu, H.Y.
Sci. Rep. (2017), 7, 6196-6196, PubMed 28733604 , DOI 10.1038/s41598-017-06263-3 , Abstract

Related entities 1. TAR DNA-binding protein 43, : 1 : 12 : 12 entities Detail

Interaction partners 1. TAR DNA-binding protein 43, : 25 interactors Detail

More details for 25 interactors identified by 8 citations

Experiments performed 9 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 1 mM U-99% 13C; U-99% 15N TDP(1-77)-GB1-C39/C50S, 20 mM sodium phosphate, 50 mM sodium chloride, 0.05 v/v sodium azide, 90 % H2O, 10 % D2O, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

2 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

3 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

4 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

5 3D HNHA

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

6 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

7 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

8 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

9 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TDP(1-77)-GB1-C39/C50S	U-99% 13C; U-99% 15N	protein	1 mM
2	sodium azide	natural abundance		0.05 v/v
3	sodium chloride	natural abundance	salt	50 mM
4	sodium phosphate	natural abundance	buffer	20 mM
5	H2O	natural abundance	solvent	90 %
6	D2O	[U-2H]	solvent	10 %

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_36060_5x4f.nef
Input source #2: Coordindates	5x4f.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-------
MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGASGLRYRNPVSQSMRGVRLVEGILHAPDAGWGNLVYVVNY
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGASGLRYRNPVSQSMRGVRLVEGILHAPDAGWGNLVYVVNY

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	77	0	0	100.0

Content subtype: combined_36060_5x4f.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	730		98.7 (chain: A, length: 77)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	829 (1)	noe	96.1 (chain: A, length: 77)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 98.7%
- Total number of assignments
  - ¹³C chemical shifts: 275
  - ¹H chemical shifts: 377
  - ¹⁵N chemical shifts: 78
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
6	ARG	CZ	159.501
42	ARG	CZ	159.337
55	ARG	CZ	159.645

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	337	272	80.7
¹H chemical shifts	441	377	85.5
¹⁵N chemical shifts	84	78	92.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	154	142	92.2
¹H chemical shifts	156	149	95.5
¹⁵N chemical shifts	72	69	95.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	183	130	71.0
¹H chemical shifts	285	228	80.0
¹⁵N chemical shifts	12	9	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	48	30	62.5
¹H chemical shifts	48	45	93.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	28	2	7.1
¹H chemical shifts	29	13	44.8
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 96.1%
- Total number of restraints: 829
- Weight of restraints: 1.0 (829)
- Potential type of restraints: square-well-parabolic (829)
- Range of distance target values: 1.45, 23.32 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords Dimerization

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Sequence chart about interacting regions

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Link destinations for BMRB, PDB and EMDB

Found 1 Document (5.873 seconds)

BMRB: 36060

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. TAR DNA-binding protein 43, : 1 : 12 : 12 entities Detail

Interaction partners 1. TAR DNA-binding protein 43, : 25 interactors Detail

Experiments performed 9 experiments Detail

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NMR combined restraints 3 contents Detail