BMRBj - BMREntryMaster

Found 1 Document (5.553 seconds)

BMRB: 6521

8F2I

Characterization of an amyloid fibril intermediate

Authors

Galea, C.A., Bowman, P., Kriwacki, R.W.

Assembly

p53 tetramer

Entity

1. p53 tetramer (polymer, Thiol state: not present), 55 monomers, 6264.923 × 4 Da Detail

GSHMNNTSSS PQPKKKPLDG EYFTLQIRGR ERFEMFRELN EALELKDAQA GKEPG

Total weight

25059.691 Da

Max. entity weight

6264.923 Da

Source organism

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 96.4 %, Completeness: 27.7 %, Completeness (bb): 49.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	27.7 % (181 of 654)	19.1 % (67 of 351)	26.4 % (65 of 246)	86.0 % (49 of 57)
Backbone	49.7 % (160 of 322)	46.8 % (52 of 111)	36.9 % (59 of 160)	96.1 % (49 of 51)
Sidechain	6.3 % (24 of 382)	6.3 % (15 of 240)	6.6 % (9 of 136)	0.0 % (0 of 6)
Aromatic	0.0 % (0 of 42)	0.0 % (0 of 21)	0.0 % (0 of 21)
Methyl	11.8 % (4 of 34)	11.8 % (2 of 17)	11.8 % (2 of 17)

1. p53tet

GSHMNNTSSS PQPKKKPLDG EYFTLQIRGR ERFEMFRELN EALELKDAQA GKEPG

Show sample condition

Sample #1

Temperature 293.0 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	p53tet	[U-15N]		4.0 mM
6	Na2HPO4			10 mM
7	NaCl			50 mM
8	NaN3			0.02 %

Sample #2

Temperature 293.0 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
9	p53tet	[U-13C; U-15N]		4.0 mM
10	Na2HPO4			10 mM
11	NaCl			50 mM
12	NaN3			0.02 %

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 29.1 %, Completeness (bb): 51.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	29.1 % (381 of 1308)	21.4 % (150 of 702)	26.8 % (132 of 492)	86.8 % (99 of 114)
Backbone	51.1 % (329 of 644)	49.1 % (109 of 222)	38.1 % (122 of 320)	96.1 % (98 of 102)
Sidechain	7.7 % (59 of 764)	8.5 % (41 of 480)	6.3 % (17 of 272)	8.3 % (1 of 12)
Aromatic	0.0 % (0 of 84)	0.0 % (0 of 42)	0.0 % (0 of 42)
Methyl	8.8 % (6 of 68)	8.8 % (3 of 34)	8.8 % (3 of 34)

1. p53tet

GSHMNNTSSS PQPKKKPLDG EYFTLQIRGR ERFEMFRELN EALELKDAQA GKEPG

Show sample condition

Sample #1

Temperature 293.0 (±0.1) K, pH 4.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	p53tet	[U-15N]		4.0 mM
6	Na2HPO4			10 mM
7	NaCl			50 mM
8	NaN3			0.02 %

Sample #2

Temperature 293.0 (±0.1) K, pH 4.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
9	p53tet	[U-13C; U-15N]		4.0 mM
10	Na2HPO4			10 mM
11	NaCl			50 mM
12	NaN3			0.02 %

Release date

2007-01-28

Citation

Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils
Galea, C.A., Bowman, P., Kriwacki, R.W.
Protein Sci. (2005), 14, 2993-3003, PubMed 16260757 , DOI 10.1110/ps.051622005 , Abstract

Related entities 1. p53 tetramer, : 1 : 12 : 25 entities Detail

Interaction partners 1. p53 tetramer, : 373 interactors Detail

More details for 373 interactors identified by 182 citations

Experiments performed 6 experiments Detail

1 1H15N_HSQC

Instrument

Model Varian INOVA (600 MHz)

Sample #1

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	p53tet	[U-15N]		4.0 mM
2	Na2HPO4			10 mM
3	NaCl			50 mM
4	NaN3			0.02 %

Sample #2

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
5	p53tet	[U-15N]		4.0 mM
6	Na2HPO4			10 mM
7	NaCl			50 mM
8	NaN3			0.02 %

Sample #3

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
9	p53tet	[U-13C; U-15N]		4.0 mM
10	Na2HPO4			10 mM
11	NaCl			50 mM
12	NaN3			0.02 %

Sample #4

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
13	p53tet	[U-13C; U-15N]		4.0 mM
14	Na2HPO4			10 mM
15	NaCl			50 mM
16	NaN3			0.02 %

2 HNCA

Instrument

Model Varian INOVA (600 MHz)

Sample #1

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	p53tet	[U-15N]		4.0 mM
2	Na2HPO4			10 mM
3	NaCl			50 mM
4	NaN3			0.02 %

Sample #2

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
5	p53tet	[U-15N]		4.0 mM
6	Na2HPO4			10 mM
7	NaCl			50 mM
8	NaN3			0.02 %

Sample #3

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
9	p53tet	[U-13C; U-15N]		4.0 mM
10	Na2HPO4			10 mM
11	NaCl			50 mM
12	NaN3			0.02 %

Sample #4

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
13	p53tet	[U-13C; U-15N]		4.0 mM
14	Na2HPO4			10 mM
15	NaCl			50 mM
16	NaN3			0.02 %

3 HN(CO)CA

Instrument

Model Varian INOVA (600 MHz)

Sample #1

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	p53tet	[U-15N]		4.0 mM
2	Na2HPO4			10 mM
3	NaCl			50 mM
4	NaN3			0.02 %

Sample #2

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
5	p53tet	[U-15N]		4.0 mM
6	Na2HPO4			10 mM
7	NaCl			50 mM
8	NaN3			0.02 %

Sample #3

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
9	p53tet	[U-13C; U-15N]		4.0 mM
10	Na2HPO4			10 mM
11	NaCl			50 mM
12	NaN3			0.02 %

Sample #4

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
13	p53tet	[U-13C; U-15N]		4.0 mM
14	Na2HPO4			10 mM
15	NaCl			50 mM
16	NaN3			0.02 %

4 HNCACB

Instrument

Model Varian INOVA (600 MHz)

Sample #1

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	p53tet	[U-15N]		4.0 mM
2	Na2HPO4			10 mM
3	NaCl			50 mM
4	NaN3			0.02 %

Sample #2

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
5	p53tet	[U-15N]		4.0 mM
6	Na2HPO4			10 mM
7	NaCl			50 mM
8	NaN3			0.02 %

Sample #3

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
9	p53tet	[U-13C; U-15N]		4.0 mM
10	Na2HPO4			10 mM
11	NaCl			50 mM
12	NaN3			0.02 %

Sample #4

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
13	p53tet	[U-13C; U-15N]		4.0 mM
14	Na2HPO4			10 mM
15	NaCl			50 mM
16	NaN3			0.02 %

5 CBCA(CO)NH

Instrument

Model Varian INOVA (600 MHz)

Sample #1

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	p53tet	[U-15N]		4.0 mM
2	Na2HPO4			10 mM
3	NaCl			50 mM
4	NaN3			0.02 %

Sample #2

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
5	p53tet	[U-15N]		4.0 mM
6	Na2HPO4			10 mM
7	NaCl			50 mM
8	NaN3			0.02 %

Sample #3

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
9	p53tet	[U-13C; U-15N]		4.0 mM
10	Na2HPO4			10 mM
11	NaCl			50 mM
12	NaN3			0.02 %

Sample #4

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
13	p53tet	[U-13C; U-15N]		4.0 mM
14	Na2HPO4			10 mM
15	NaCl			50 mM
16	NaN3			0.02 %

6 1H15N_NOESY

Instrument

Model Varian INOVA (600 MHz)

Sample #1

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	p53tet	[U-15N]		4.0 mM
2	Na2HPO4			10 mM
3	NaCl			50 mM
4	NaN3			0.02 %

Sample #2

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
5	p53tet	[U-15N]		4.0 mM
6	Na2HPO4			10 mM
7	NaCl			50 mM
8	NaN3			0.02 %

Sample #3

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
9	p53tet	[U-13C; U-15N]		4.0 mM
10	Na2HPO4			10 mM
11	NaCl			50 mM
12	NaN3			0.02 %

Sample #4

Temperature 293.0 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
13	p53tet	[U-13C; U-15N]		4.0 mM
14	Na2HPO4			10 mM
15	NaCl			50 mM
16	NaN3			0.02 %

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6521_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	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr6521_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	OK	147		94.5 (chain: 1, length: 55)
2	Assigned chemical shifts	chem_shift_list_2	OK	153		100.0 (chain: 1, length: 55)
1	Chemical shift references	chemical_shift_referencing	OK	1		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 55, Sequence coverage: 94.5%
- Total number of assignments
  - ¹H chemical shifts: 49
  - ¹⁵N chemical shifts: 49
  - ¹³C chemical shifts: 49
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: chem_shift_list_2
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 55, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 55
  - ¹H chemical shifts: 49
  - ¹⁵N chemical shifts: 49
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Keywords p53 tetramerization domain, tumor suppressor protein, H/D exchange, Amyloid fibril intermediate, pKa, Nuclear Magnetic Resonance, p53tet, Tumor suppressor protein p53 - human, Tetramerization domain of p53 (residues 310 - 360), Hydrogen exchange studies, Amyloid fibrils, Intermediate, p53tet-wt