BMRBj - BMREntryMaster

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BMRB: 4048

Solution Structure of the tetrameric minimum transforming domain of p53

Authors

Lee, W., Harvey, T.S., Yin, Y., Yau, P., Litchfield, D., Arrowsmith, C.H.

Assembly

p53 nuclear phosphoprotein

Entity

1. p53 nuclear phosphoprotein (polymer), 66 monomers, 7470.293 × 4 Da Detail

HMSTKRALPN NTSSSPQPKK KPLDGEYFTL QIRGRERFEM FRELNEALEL KDAQAGKEPG GSRAHS

Total weight

29881.172 Da

Max. entity weight

7470.293 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 56.1 %, Completeness: 54.1 %, Completeness (bb): 57.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	54.1 % (421 of 778)	55.9 % (233 of 417)	50.3 % (148 of 294)	59.7 % (40 of 67)
Backbone	57.5 % (222 of 386)	58.3 % (77 of 132)	56.0 % (108 of 193)	60.7 % (37 of 61)
Sidechain	51.4 % (233 of 453)	54.7 % (156 of 285)	45.7 % (74 of 162)	50.0 % (3 of 6)
Aromatic	41.3 % (19 of 46)	82.6 % (19 of 23)	0.0 % (0 of 23)
Methyl	72.7 % (32 of 44)	72.7 % (16 of 22)	72.7 % (16 of 22)

1. p53 nuclear phosphoprotein

HMSTKRALPN NTSSSPQPKK KPLDGEYFTL QIRGRERFEM FRELNEALEL KDAQAGKEPG GSRAHS

Show sample condition

Sample #1

Temperature 318 K, pH 7.0

#	Name	Concentration
1	p53 nuclear phosphoprotein	2.0 mM
2	NaCL	250 mM
3	Na2HPO4	25 mM
4	NaN3	0.02 %

Sample #2

Temperature 318 K, pH 7.0

#	Name	Isotope labeling	Concentration
5	p53 nuclear phosphoprotein	[U-15N]	2.0 mM
6	NaCL		250 mM
7	Na2HPO4		25 mM
8	NaN3		0.02 %

Sample #3

Temperature 318 K, pH 7.0

#	Name	Isotope labeling	Concentration
9	p53 nuclear phosphoprotein	[U-13C; U-15N]	2.0 mM
10	NaCL		250 mM
11	Na2HPO4		25 mM
12	NaN3		0.02 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	CH3CO2NA	methyl carbon	25.85 ppm	external	indirect
¹H	H2O	protons	4.58 ppm	internal	direct
¹⁵N	CH4(15N2O)	na	78.98 ppm	external	indirect

Referencing offset: -0.15 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	CH3CO2NA	methyl carbon	25.85 ppm	external	indirect
¹H	H2O	protons	4.58 ppm	internal	direct
¹⁵N	CH4(15N2O)	na	78.98 ppm	external	indirect

Referencing offset: -0.15 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	CH3CO2NA	methyl carbon	25.85 ppm	external	indirect
¹H	H2O	protons	4.58 ppm	internal	direct
¹⁵N	CH4(15N2O)	na	78.98 ppm	external	indirect

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type
¹³C	CH3CO2NA	methyl carbon	25.85 ppm	external	indirect
¹H	H2O	protons	4.58 ppm	internal	direct
¹⁵N	CH4(15N2O)	na	78.98 ppm	external	indirect

Referencing offset: 4.26 ppm, Outliers: 1 Detail

Release date

1999-08-16

Citation

Solution structure of the tetrameric minimum transforming domain of p53
Lee, W., Harvey, T.S., Yin, Y., Yau, P., Litchfield, D., Arrowsmith, C.H.
Nat. Struct. Biol. (1994), 1, 877-890, PubMed 7773777 , DOI: , Abstract

Related entities 1. p53 nuclear phosphoprotein, : 6 : 27 entities Detail

Interaction partners 1. p53 nuclear phosphoprotein, : 374 interactors Detail

More details for 374 interactors identified by 181 citations

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4048_3.str
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

Content subtype: bmr4048_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_one	Warning	446		54.5 (chain: 1, length: 66)
1	Chemical shift references	chemical_shift_reference_one	OK	2		No information

Assigned chemical shifts

Saveframe: chemical_shift_assignment_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 66, Sequence coverage: 54.5%
- Total number of assignments
  - ¹H chemical shifts: 262
  - ¹³C chemical shifts: 145
  - ¹⁵N chemical shifts: 39
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	417	228	54.7
¹³C chemical shifts	294	145	49.3
¹⁵N chemical shifts	73	39	53.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	132	75	56.8
¹³C chemical shifts	132	72	54.5
¹⁵N chemical shifts	61	36	59.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	285	153	53.7
¹³C chemical shifts	162	73	45.1
¹⁵N chemical shifts	12	3	25.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	17	70.8
¹³C chemical shifts	24	17	70.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	23	19	82.6
¹³C chemical shifts	23	0	0.0

Keywords Cellular tumor antigen p53 - human, minimum transforming domain (residues 303-366) of human p53 (p53tet), NMR, Nuclear Magnetic Resonance, p53, nuclear phosphoprotein, tumor suppressor

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Found 1 Document (6.02 seconds)

BMRB: 4048

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. p53 nuclear phosphoprotein, : 6 : 27 entities Detail

Interaction partners 1. p53 nuclear phosphoprotein, : 374 interactors Detail

Chemical shift validation 3 contents Detail