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BMRB: 25790

2N72

Solution structure of regulatory protein

Authors

Veverka, V., Hexnerova, R.

Assembly

polyQ regulatory protein

Entity

1. polyQ regulatory protein (polymer, Thiol state: not present), 69 monomers, 8289.174 Da Detail

MQQKQQIMAA LNSQTAVQFQ QYAAQQYPGN YEQQQILIRQ LQEQHYQQYM QQLYQVQLAQ QQAALQKQQ

Formula weight

8289.174 Da

Source organism

Exptl. method

Refine. method

simulated annealing, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.6 %, Completeness: 91.6 %, Completeness (bb): 98.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.6 % (814 of 889)	92.6 % (441 of 476)	92.1 % (290 of 315)	84.7 % (83 of 98)
Backbone	98.1 % (404 of 412)	97.8 % (135 of 138)	98.5 % (203 of 206)	97.1 % (66 of 68)
Sidechain	87.5 % (477 of 545)	90.5 % (306 of 338)	87.0 % (154 of 177)	56.7 % (17 of 30)
Aromatic	77.4 % (48 of 62)	100.0 % (31 of 31)	54.8 % (17 of 31)
Methyl	98.4 % (61 of 62)	100.0 % (31 of 31)	96.8 % (30 of 31)

1. entity

MQQKQQIMAA LNSQTAVQFQ QYAAQQYPGN YEQQQILIRQ LQEQHYQQYM QQLYQVQLAQ QQAALQKQQ

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

Protein Blocks Logo

Calculated from 30 models in PDB: 2N72, Strand ID: A Detail

Release date

2016-07-12

Citation

Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein
Klima, M., Toth, D.J., Hexnerova, R., Baumlova, A., Chalupska, D., Tykvart, J., Rezabkova, L., Sengupta, N., Man, P., Dubankova, A., Humpolickova, J., Nencka, R., Veverka, V., Balla, T., Boura, E.
Sci. Rep. (2016), 6, 23641-23641, PubMed 27009356 , DOI 10.1038/srep23641 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 25791 released on 2016-07-12
    Title Solution structure of kinase in complex with its regulatory protein
  BMRB: 25803 released on 2016-07-12
    Title UBL domain of the yeast DNA damage-inducible protein homolog 1

Related entities 1. polyQ regulatory protein, : 6 : 1 entities Detail

Interaction partners 1. polyQ regulatory protein, : 20 interactors Detail

More details for 20 interactors identified by 9 citations

Experiments performed 8 experiments Detail

1 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

2 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

3 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

4 3D HN(CO)CA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

5 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

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

6 3D 1H-15N NOESY

Instrument

Bruker Avance - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

7 3D 1H-13C NOESY

Instrument

Bruker Avance - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

8 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-13C; U-15N]		0.28 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25790_2n72.nef
Input source #2: Coordindates	2n72.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---------
MQQKQQIMAALNSQTAVQFQQYAAQQYPGNYEQQQILIRQLQEQHYQQYMQQLYQVQLAQQQAALQKQQ
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MQQKQQIMAALNSQTAVQFQQYAAQQYPGNYEQQQILIRQLQEQHYQQYMQQLYQVQLAQQQAALQKQQ

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	69	0	0	100.0

Content subtype: combined_25790_2n72.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	814		98.6 (chain: A, length: 69)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	1493 (1)	noe	95.7 (chain: A, length: 69)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	118 (118)	.	91.3 (chain: A, length: 69)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 69, Sequence coverage: 98.6%
- Total number of assignments
  - ¹H chemical shifts: 442
  - ¹³C chemical shifts: 289
  - ¹⁵N chemical shifts: 83
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Tautomeric state of HIS
- 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

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 69, Sequence coverage: 95.7%
- Total number of restraints: 1493
- Weight of restraints: 1.0 (1493)
- Potential type of restraints: square-well-parabolic (1493)
- Range of distance target values: 1.27, 2.75 (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

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 69, Sequence coverage: 91.3%
- Total number of restraints: 118
- Total number of restraints per polymer type: 118
- Weight of restraints: 1.0 (118)
- Potential type of restraints: square-well-parabolic (118)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords protein