BMRBj - BMREntryMaster

	Total	¹H
All	15.0 % (36 of 240)	15.0 % (36 of 240)
Backbone	46.8 % (36 of 77)	46.8 % (36 of 77)
Sidechain	0.0 % (0 of 163)	0.0 % (0 of 163)
Aromatic	0.0 % (0 of 2)	0.0 % (0 of 2)
Methyl	0.0 % (0 of 19)	0.0 % (0 of 19)

1. entity 1

KNVKSKIGST ENLKHQPGGG KVQIINKKLD LSNVQSK

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 278 K, pH 6.8, Details 800 uM Tau(254-290), 27 uM F-actin, 50 mM sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	Tau(254-290)	natural abundance	800 uM
2	F-actin	natural abundance	27 uM
3	sodium phosphate	natural abundance	50 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 278 K, pH 6.8, Details 800 uM Tau(254-290), 50 mM sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
4	Tau(254-290)	natural abundance		800 uM
5	sodium phosphate	natural abundance		50 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 5N5A, Strand ID: A Detail

Release date

2017-12-17

Citation

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau
Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., Zweckstetter, M.
Nat. Commun. (2017), 8, 1981-1981, PubMed 29215007 , DOI 10.1038/s41467-017-02230-8 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 34099 released on 2017-12-17
Title Structure of Tau(292-319) bound to F-actin

Related entities 1. Microtubule-associated protein tau, : 1 : 78 : 6 : 243 entities Detail

Interaction partners 1. Microtubule-associated protein tau, : 49 interactors Detail

More details for 49 interactors identified by 26 citations

Experiments performed 4 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_34098_5n5a.nef
Input source #2: Coordindates	5n5a.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

----260-------270-------280-------290
KNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSK
|||||||||||||||||||||||||||||||||||||
KNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSK
--------10--------20--------30-------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	37	0	0	100.0

Content subtype: combined_34098_5n5a.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	36		97.3 (chain: A, length: 37)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	336 (1)	noe	94.6 (chain: A, length: 37)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 97.3%
- Total number of assignments
  - ¹H chemical shifts: 36
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	240	35	14.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	35	45.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	163	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	2	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 94.6%
- Total number of restraints: 334
- Weight of restraints: 1.0 (334)
- Potential type of restraints: square-well-parabolic (334)
- Range of distance target values: 3.9, 3.9 (Å)
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords Alzheimer's disease, F-actin, protein binding, structural protein, tau

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Found 1 Document (1.248 seconds)

BMRB: 34098

Sample #1

Sample #2

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Microtubule-associated protein tau, : 1 : 78 : 6 : 243 entities Detail

Interaction partners 1. Microtubule-associated protein tau, : 49 interactors Detail

Experiments performed 4 experiments Detail

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Instrument

Sample

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NMR combined restraints 3 contents Detail