BMRBj - BMREntryMaster

	Total	¹H
All	28.7 % (47 of 164)	28.7 % (47 of 164)
Backbone	55.2 % (32 of 58)	55.2 % (32 of 58)
Sidechain	14.2 % (15 of 106)	14.2 % (15 of 106)
Aromatic	0.0 % (0 of 6)	0.0 % (0 of 6)
Methyl	11.8 % (2 of 17)	11.8 % (2 of 17)

1. entity 1

GSKDNIKHVP GGGSVQIVYK PVDLSKVT

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 278 K, pH 6.8, Details 800 uM Tau(292-319), 27 uM F-actin, 50 mM sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	Tau(292-319)	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	sodium phosphate	natural abundance		50 mM
5	Tau(254-290)	natural abundance		800 uM

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Calculated from 20 models in PDB: 5N5B, 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

Related entities 1. Microtubule-associated protein tau, : 1 : 88 : 4 : 221 entities Detail

Interaction partners 1. Microtubule-associated protein tau, : 18 interactors Detail

More details for 18 interactors identified by 8 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_34099_5n5b.nef
Input source #2: Coordindates	5n5b.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

------300-------310---------
GSKDNIKHVPGGGSVQIVYKPVDLSKVT
||||||||||||||||||||||||||||
GSKDNIKHVPGGGSVQIVYKPVDLSKVT
--------10--------20--------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	28	0	0	100.0

Content subtype: combined_34099_5n5b.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	32		100.0 (chain: A, length: 28)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	94 (1)	noe	85.7 (chain: A, length: 28)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 28, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 32
- 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	164	31	18.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	58	27	46.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	106	4	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	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: 28, Sequence coverage: 85.7%
- Total number of restraints: 94
- Weight of restraints: 1.0 (94)
- Potential type of restraints: square-well-parabolic (94)
- 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, STRUCTURAL PROTEIN, protein binding, tau

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Found 1 Document (4.713 seconds)

BMRB: 34099

Sample #1

Sample #2

Related entities 1. Microtubule-associated protein tau, : 1 : 88 : 4 : 221 entities Detail

Interaction partners 1. Microtubule-associated protein tau, : 18 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail