BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	34.6 % (102 of 295)	13.6 % (22 of 162)	54.5 % (61 of 112)	90.5 % (19 of 21)
Backbone	82.0 % (100 of 122)	48.8 % (20 of 41)	98.4 % (61 of 62)	100.0 % (19 of 19)
Sidechain	11.4 % (22 of 193)	1.7 % (2 of 121)	28.6 % (20 of 70)	0.0 % (0 of 2)
Aromatic	0.0 % (0 of 22)	0.0 % (0 of 11)	0.0 % (0 of 10)	0.0 % (0 of 1)
Methyl	6.3 % (1 of 16)	0.0 % (0 of 8)	12.5 % (1 of 8)

1. entity 1

KKPLGKMADW FRQTLLKKPK K

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.01) atm, Temperature 298 (±0.2) K, pH 6.0 (±0.05), Details 0.4 mM [U-99% 13C; U-99% 15N] TIRAP PBM, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	TIRAP PBM	[U-99% 13C; U-99% 15N]		0.4 (±0.04) mM

Protein Blocks Logo

Calculated from 20 models in PDB: 5T7Q, Strand ID: A Detail

Release date

2016-09-19

Citation

Membrane targeting of TIRAP is negatively regulated by phosphorylation in its phosphoinositide-binding motif
Zhao, X., Xiong, W., Xiao, S., Ellena, J.F., Armstrong, G.S., Finkielstein, C.V., Capelluto, D.G.S.
Sci. Rep. (2017), 7, 43043-43043, PubMed 28225045 , DOI 10.1038/srep43043 , Abstract

Related entities 1. Toll/interleukin-1 receptor domain-containing adapter protein, : 2 : 10 entities Detail

Interaction partners 1. Toll/interleukin-1 receptor domain-containing adapter protein, : 32 interactors Detail

More details for 32 interactors identified by 13 citations

Experiments performed 7 experiments Detail

1 3D HNCO

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 (±0.01) atm, Temperature 298 (±0.2) K, pH 6.0 (±0.05), Details 0.4 mM [U-99% 13C; U-99% 15N] TIRAP PBM, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	TIRAP PBM	[U-99% 13C; U-99% 15N]		0.4 (±0.04) mM

2 3D HN(CA)CO

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TIRAP PBM	[U-99% 13C; U-99% 15N]		0.4 (±0.04) mM

3 3D CBCA(CO)NH

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TIRAP PBM	[U-99% 13C; U-99% 15N]		0.4 (±0.04) mM

4 3D HNCACB

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TIRAP PBM	[U-99% 13C; U-99% 15N]		0.4 (±0.04) mM

5 3D TOCSYHSQC

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TIRAP PBM	[U-99% 13C; U-99% 15N]		0.4 (±0.04) mM

6 3D NOESYHSQC

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TIRAP PBM	[U-99% 13C; U-99% 15N]		0.4 (±0.04) mM

7 2D 1H-15N HSQC

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	TIRAP PBM	[U-99% 13C; U-99% 15N]		0.4 (±0.04) mM

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Dihedral angle restraints	combined_30170_5t7q.nef
Input source #2: Coordindates	5t7q.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

----20--------30-----
KKPLGKMADWFRQTLLKKPKK
|||||||||||||||||||||
KKPLGKMADWFRQTLLKKPKK
--------10--------20-

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	21	0	0	100.0

Content subtype: combined_30170_5t7q.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	99		100.0 (chain: A, length: 21)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	33 (33)	.	90.5 (chain: A, length: 21)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 19
  - ¹³C chemical shifts: 61
  - ¹⁵N chemical shifts: 19
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	162	18	11.1
¹³C chemical shifts	112	61	54.5
¹⁵N chemical shifts	22	19	86.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	41	18	43.9
¹³C chemical shifts	42	41	97.6
¹⁵N chemical shifts	19	19	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	121	0	0.0
¹³C chemical shifts	70	20	28.6
¹⁵N chemical shifts	3	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	0	0.0
¹³C chemical shifts	9	1	11.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	0	0.0
¹³C chemical shifts	10	0	0.0
¹⁵N chemical shifts	1	0	0.0

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 90.5%
- Total number of restraints: 33
- Total number of restraints per polymer type: 33
- Weight of restraints: 1.0 (33)
- Potential type of restraints: square-well-parabolic (33)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords TIRAP, phosphoinositide, phosphoinositide-binding motif; structure, phosphorylation

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Found 1 Document (0.674 seconds)

BMRB: 30170

Sample

Related entities 1. Toll/interleukin-1 receptor domain-containing adapter protein, : 2 : 10 entities Detail

Interaction partners 1. Toll/interleukin-1 receptor domain-containing adapter protein, : 32 interactors Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 3 contents Detail