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BMRB: 17475

2Y9T

Structural basis of p63a SAM domain mutants involved in AEC syndrome

Authors

Sathyamurthy, A., Freund, S.M.V., Johnson, C.M., Allen, M.D.

Assembly

Structural basis of p63a SAM domain mutants involved in AEC syndrome

Entity

1. Structural basis of p63a SAM domain mutants involved in AEC syndrome (polymer, Thiol state: all free), 82 monomers, 9319.422 Da Detail

GSYPTDCSIV SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG ILDHRQLHEF SSPSHLLRTP SS

Formula weight

9319.422 Da

Source organism

Exptl. method

Refine. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 64.0 %, Completeness (bb): 83.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	64.0 % (611 of 954)	71.5 % (351 of 491)	48.2 % (183 of 380)	92.8 % (77 of 83)
Backbone	83.1 % (402 of 484)	93.3 % (153 of 164)	71.1 % (172 of 242)	98.7 % (77 of 78)
Sidechain	52.4 % (287 of 548)	60.6 % (198 of 327)	41.2 % (89 of 216)	0.0 % (0 of 5)
Aromatic	17.3 % (18 of 104)	30.8 % (16 of 52)	3.9 % (2 of 51)	0.0 % (0 of 1)
Methyl	22.1 % (19 of 86)	20.9 % (9 of 43)	23.3 % (10 of 43)

1. TUMOR PROTEIN 63

GSYPTDCSIV SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG ILDHRQLHEF SSPSHLLRTP SS

Show sample condition

Sample

Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

LACS Plot; CA

Referencing offset: -0.14 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: -0.14 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: 0.02 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2Y9T, Strand ID: A Detail

Release date

2011-05-31

Citation

Structural basis of p63α SAM domain mutants involved in AEC syndrome
Sathyamurthy, A., Freund, S.M.V., Johnson, C.M., Allen, M.D., Bycroft, M.
FEBS J. (2011), 278, 2680-2688, PubMed 21615690 , DOI 10.1111/j.1742-4658.2011.08194.x , Abstract

Related entities 1. Structural basis of p63a SAM domain mutants involved in AEC syndrome, : 1 : 3 : 15 entities Detail

Interaction partners 1. Structural basis of p63a SAM domain mutants involved in AEC syndrome, : 19 interactors Detail

More details for 19 interactors identified by 13 citations

Experiments performed 10 experiments Detail

1 2D 1H NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

2 2D TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

3 DQF COSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

4 HSQC (13C and 15N)

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

5 3D HNCACB

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

6 CBCACONH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

7 CCCONH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

8 HNCACO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

9 HNCO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

10 HNHB

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% water/10% D2O, Pressure 1 atm, Temperature 298.000 K, pH 6.500, Details 1.5 mM

#	Name	Isotope labeling	Type	Concentration
1	TUMOR PROTEIN 63	[U-13C; U-15N]		1.5 mM
2	NaCl	natural abundance		100 mM
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17475_2y9t.nef
Input source #2: Coordindates	2y9t.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	Error

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

-------550-------560-------570-------580-------590-------600-------610-------620--
GSYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSS
--------10--------20--------30--------40--------50--------60--------70--------80--

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	82	0	0	100.0

Content subtype: combined_17475_2y9t.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list	Warning	572		98.8 (chain: A, length: 82)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1762 (1)	noe	95.1 (chain: A, length: 82)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	123 (123)	.	80.5 (chain: A, length: 82)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 82, Sequence coverage: 98.8%
- Total number of assignments
  - ¹H chemical shifts: 340
  - ¹³C chemical shifts: 157
  - ¹⁵N chemical shifts: 75
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 82, Sequence coverage: 95.1%
- Total number of restraints: 1754
- Weight of restraints: 1.0 (1754)
- Potential type of restraints: square-well-parabolic (1754)
- Range of distance target values: 2.3, 3.9 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 82, Sequence coverage: 80.5%
- Total number of restraints: 123
- Total number of restraints per polymer type: 123
- Weight of restraints: 1.0 (123)
- Potential type of restraints: square-well-parabolic (123)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords 5-helix bundle, AEC syndrome, APOPTOSIS, MUTATIO, mutations, p53, p63, p73, sterile alpha motif