BMRBj - BMREntryMaster

Found 1 Document (2.451 seconds)

BMRB: 2410

8BGU

Sequence-specific 1H, 15N, and 13C assignment of the N-terminal domain of the human oncoprotein MDM2 that binds to p53

Authors

Stoll, R., Renner, C., Muhlhahn, P., Hansen, S., Schumacher, R., Hesse, F., Kaluza, B., Engh, R.A., Voelter, W., Holak, T.A.

Assembly

N-terminal domain of the human oncoprotein MDM2

Entity

1. N-terminal domain of the human oncoprotein MDM2 (polymer, Thiol state: all free), 119 monomers, 13556.47 Da Detail

MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEVLFYLGQY IMTKRLYDEK QQHIVYCSND LLGDLFGVPS FSVKEHRKIY TMIYRNLVVV NQQESSDSS

Formula weight

13556.47 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 81.5 %, Completeness: 29.7 %, Completeness (bb): 56.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	29.7 % (421 of 1418)	22.1 % (163 of 738)	30.7 % (170 of 553)	69.3 % (88 of 127)
Backbone	56.1 % (395 of 704)	59.2 % (141 of 238)	47.2 % (166 of 352)	77.2 % (88 of 114)
Sidechain	11.6 % (96 of 828)	4.4 % (22 of 500)	23.5 % (74 of 315)	0.0 % (0 of 13)
Aromatic	0.0 % (0 of 94)	0.0 % (0 of 47)	0.0 % (0 of 47)
Methyl	10.0 % (14 of 140)	10.0 % (7 of 70)	10.0 % (7 of 70)

1. N-terminal domain of the human murine double minute clone 2 protein

MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEVLFYLGQY IMTKRLYDEK QQHIVYCSND LLGDLFGVPS FSVKEHRKIY TMIYRNLVVV NQQESSDSS

Show sample condition

Sample

Temperature 300 (±1) K, pH 7.4 (±0.2)

#	Name	Isotope labeling	Type	Concentration
2	N-terminal domain of the human murine double minute clone 2 protein	[U-15N; U-13C]		0.1 ~ 0.5 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.73 ppm	internal	direct	0.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 1.88 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.73 ppm	internal	direct	0.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 1.88 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.73 ppm	internal	direct	0.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: -0.08 ppm, Outliers: 1 Detail

Release date

1995-07-30

Citation

Letter to the Editor: Sequence-specific 1H, 15N, and 13C assignment of the N-terminal domain of the human oncoprotein MDM2 that binds to p53
Stoll, R., Renner, C., Muhlhahn, P., Hansen, S., Schumacher, R., Hesse, F., Kaluza, B., Engh, R.A., Voelter, W., Holak, T.A.
J. Biomol. NMR (2000), 17, 91-92

Related entities 1. N-terminal domain of the human oncoprotein MDM2, : 1 : 1 : 37 : 61 entities Detail

Interaction partners 1. N-terminal domain of the human oncoprotein MDM2, : 170 interactors Detail

More details for 170 interactors identified by 57 citations

Experiments performed 1 experiments Detail

#	Name	Isotope labeling	Type	Concentration
1	N-terminal domain of the human murine double minute clone 2 protein	[U-15N]		0.1 ~ 0.5 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr2410_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: bmr2410_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	364		79.0 (chain: 1, length: 119)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 119, Sequence coverage: 79.0%
- Total number of assignments
  - ¹³C chemical shifts: 150
  - ¹H chemical shifts: 131
  - ¹⁵N chemical shifts: 83
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	553	150	27.1
¹H chemical shifts	738	131	17.8
¹⁵N chemical shifts	131	83	63.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	238	86	36.1
¹H chemical shifts	238	131	55.0
¹⁵N chemical shifts	114	83	72.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	315	64	20.3
¹H chemical shifts	500	0	0.0
¹⁵N chemical shifts	17	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	75	3	4.0
¹H chemical shifts	75	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	47	0	0.0
¹H chemical shifts	47	0	0.0

Keywords Human MDM2, NMR assignments, p53

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Found 1 Document (2.451 seconds)

BMRB: 2410

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. N-terminal domain of the human oncoprotein MDM2, : 1 : 1 : 37 : 61 entities Detail

Interaction partners 1. N-terminal domain of the human oncoprotein MDM2, : 170 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Chemical shift validation 3 contents Detail