BMRBj - BMREntryMaster

Found 1 Document (0.763 seconds)

BMRB: 15052

3HJX

HPRP-173-195-D178N SOLUTION STRUCTURE

Authors

Saviano, G., Tancredi, T.

Assembly

prion protein fragment

Entity

1. prion protein fragment (polymer, Thiol state: all free), 23 monomers, 2570.874 Da Detail

NNFVHNCVNI TIKQHTVTTT TKG

Formula weight

2570.874 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 89.5 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	89.5 % (119 of 133)	89.5 % (119 of 133)
Backbone	100.0 % (47 of 47)	100.0 % (47 of 47)
Sidechain	83.7 % (72 of 86)	83.7 % (72 of 86)
Aromatic	55.6 % (5 of 9)	55.6 % (5 of 9)
Methyl	87.5 % (14 of 16)	87.5 % (14 of 16)

1. HPRP-173-195-D178N

NNFVHNCVNI TIKQHTVTTT TKG

Show sample condition

Sample

Pressure 1.0 atm, Temperature 300.0 K, pH 5.0, Details TRIFLUOROETHANOL-D2

#	Name	Isotope labeling	Type	Concentration
1	HPRP-173-195-D178N	natural abundance		1.0 ~ 2.0 mM
2	TRIFLUOROETHANOL-D2	[U-2H]		100 %

Release date

2007-01-31

Citation

Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein alpha 2-helical 180-195 segment, and comparison with full-length alpha 2-helix-derived peptides
Ronga, L., Palladino, P., Saviano, G., Tancredi, T., Benedetti, E., Ragone, R., Rossi, F.
J. Pept. Sci. (2008), 14, 1096-1102, PubMed 18563793 , DOI 10.1002/psc.1046 , Abstract

Related entities 1. prion protein fragment, : 1 : 3 : 124 : 19 entities Detail

Interaction partners 1. prion protein fragment, : 36 interactors Detail

More details for 36 interactors identified by 12 citations

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	149		100.0 (chain: 1, length: 23)
1	Chemical shift references	chemical_shift_reference_1	OK	1		No information

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
13	LYS	HZ1	7.04
13	LYS	HZ2	7.04
13	LYS	HZ3	7.04
22	LYS	HZ1	6.94
22	LYS	HZ2	6.94
22	LYS	HZ3	6.94

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	133	115	86.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	47	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	86	68	79.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	14	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	5	55.6

Keywords HUMAN PRION PROTEIN, NMR, PEPTIDE, SOLUTION STRUCTURE

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr15052_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

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Found 1 Document (0.763 seconds)

BMRB: 15052

Sample

Related entities 1. prion protein fragment, : 1 : 3 : 124 : 19 entities Detail

Interaction partners 1. prion protein fragment, : 36 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail