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Found 1 Document (1.106 seconds)

BMRB: 16078

7TD6

Mouse prion protein fragment mPrP[A117V](90-231) at pH 7.0

Authors

Damberger, F.F., Wuthrich, K., Hornemann, S., von Schroetter, C.

Assembly

mPrP90 A117V

Entity

1. mPrP90 A117V (polymer, Thiol state: all disulfide bound), 142 monomers, 16226.91 Da Detail

GQGGGTHNQW NKPSKPKTNL KHVAGAAVAG AVVGGLGGYM LGSAMSRPMI HFGNDWEDRY YRENMYRYPN QVYYRPVDQY SNQNNFVHDC VNITIKQHTV TTTTKGENFT ETDVKMMERV VEQMCVTQYQ KESQAYYDGR RS

Formula weight

16226.91 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS90:SG	1:CYS125:SG

Source organism

Mus musculus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.5 %, Completeness: 35.5 %, Completeness (bb): 64.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	35.5 % (584 of 1646)	19.0 % (163 of 859)	46.9 % (294 of 627)	79.4 % (127 of 160)
Backbone	64.3 % (541 of 842)	45.4 % (133 of 293)	68.2 % (281 of 412)	92.7 % (127 of 137)
Sidechain	5.7 % (53 of 932)	5.3 % (30 of 566)	6.7 % (23 of 343)	0.0 % (0 of 23)
Aromatic	7.4 % (12 of 162)	7.4 % (6 of 81)	7.6 % (6 of 79)	0.0 % (0 of 2)
Methyl	1.8 % (2 of 112)	1.8 % (1 of 56)	1.8 % (1 of 56)

1. mPrP90 A117V

GQGGGTHNQW NKPSKPKTNL KHVAGAAVAG AVVGGLGGYM LGSAMSRPMI HFGNDWEDRY YRENMYRYPN QVYYRPVDQY SNQNNFVHDC VNITIKQHTV TTTTKGENFT ETDVKMMERV VEQMCVTQYQ KESQAYYDGR RS

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.2 (±0.2) K, pH 7.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
1	mPrP90_A117V	[U-99% 13C; U-99% 15N]		1.2 (±0.05) mM
2	sodium phosphate buffer	natural abundance		5 mM

Release date

2008-12-21

Citation

Prion protein-detergent micelle interactions studied by NMR in solution
Hornemann, S., von Schroetter, C., Damberger, F.F., Wuthrich, K.
J. Biol. Chem. (2009), 284, 22713-22721, PubMed 19546219 , DOI 10.1074/jbc.M109.000430 , Abstract

Entries sharing articles BMRB: 6 entries Detail

  BMRB: 16075 released on 2008-12-21
    Title Mouse prion protein fragment mPrP[M129V](91-231) at pH 7.0
  BMRB: 16076 released on 2008-12-21
    Title Mouse prion protein fragment mPrP[P102L](91-231) at pH 7.0
  BMRB: 16077 released on 2008-12-21
    Title Mouse prion protein fragment mPrP[P105L](91-231) at pH 7.0
  BMRB: 16079 released on 2008-12-21
    Title Mouse prion protein fragment mPrP[A113V,A115V,A118V](90-231) at pH 7.0
  BMRB: 16080 released on 2008-12-21
    Title Mouse prion protein fragment mPrP[K119I,H111I](90-231) at pH 7.0
  BMRB: 16071 released on 2008-12-18
    Title Mouse prion protein fragment 90-231 at pH 7.0

Related entities 1. mPrP90 A117V, : 1 : 4 : 108 entities Detail

Interaction partners 1. mPrP90 A117V, : 36 interactors Detail

More details for 36 interactors identified by 12 citations

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr16078_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	OK

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:90:CYS:SG	1:125:CYS:SG	unknown, CA 58.25 ppm	unknown, CA 59.659 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr16078_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	524		95.8 (chain: 1, length: 142)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 142, Sequence coverage: 95.8%
- Total number of assignments
  - ¹H chemical shifts: 127
  - ¹³C chemical shifts: 270
  - ¹⁵N chemical shifts: 127
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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	859	127	14.8
¹³C chemical shifts	627	270	43.1
¹⁵N chemical shifts	168	127	75.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	293	127	43.3
¹³C chemical shifts	284	270	95.1
¹⁵N chemical shifts	137	127	92.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	566	0	0.0
¹³C chemical shifts	343	0	0.0
¹⁵N chemical shifts	31	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	0	0.0
¹³C chemical shifts	63	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	81	0	0.0
¹³C chemical shifts	79	0	0.0
¹⁵N chemical shifts	2	0	0.0

Keywords detergent micelles, mouse prion protein variants, pH-dependent conformational transition

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Found 1 Document (1.106 seconds)

BMRB: 16078

Sample

Entries sharing articles BMRB: 6 entries Detail

Related entities 1. mPrP90 A117V, : 1 : 4 : 108 entities Detail

Interaction partners 1. mPrP90 A117V, : 36 interactors Detail

Experiments performed 5 experiments Detail

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Chemical shift validation 3 contents Detail