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Found 1 Document (0.892 seconds)

BMRB: 16077

7TD6

Mouse prion protein fragment mPrP[P105L](91-231) at pH 7.0

Authors

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

Assembly

mPrP90 P105L

Entity

1. mPrP90 P105L (polymer, Thiol state: all disulfide bound), 141 monomers, 16157.85 Da Detail

QGGGTHNQWN KPSKLKTNLK HVAGAAAAGA VVGGLGGYML GSAMSRPMIH FGNDWEDRYY RENMYRYPNQ VYYRPVDQYS NQNNFVHDCV NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCVTQYQK ESQAYYDGRR S

Formula weight

16157.85 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS89:SG	1:CYS124:SG

Source organism

Mus musculus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.5 %, Completeness: 37.7 %, Completeness (bb): 66.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	37.7 % (618 of 1638)	21.9 % (187 of 854)	48.4 % (302 of 624)	80.6 % (129 of 160)
Backbone	66.1 % (554 of 838)	48.5 % (141 of 291)	69.5 % (285 of 410)	93.4 % (128 of 137)
Sidechain	8.6 % (80 of 928)	8.2 % (46 of 563)	9.6 % (33 of 342)	4.3 % (1 of 23)
Aromatic	4.9 % (8 of 162)	4.9 % (4 of 81)	5.1 % (4 of 79)	0.0 % (0 of 2)
Methyl	9.6 % (11 of 114)	8.8 % (5 of 57)	10.5 % (6 of 57)

1. mPrP90 P105L

QGGGTHNQWN KPSKLKTNLK HVAGAAAAGA VVGGLGGYML GSAMSRPMIH FGNDWEDRYY RENMYRYPNQ VYYRPVDQYS NQNNFVHDCV NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCVTQYQK ESQAYYDGRR S

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_P105L	[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: 16078 released on 2008-12-21
    Title Mouse prion protein fragment mPrP[A117V](90-231) 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 P105L, : 1 : 6 : 105 entities Detail

Interaction partners 1. mPrP90 P105L, : 36 interactors Detail

More details for 36 interactors identified by 12 citations

Experiments performed 6 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr16077_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)
1:89:CYS:SG	1:124:CYS:SG	unknown, CA 58.24 ppm	unknown, CA 59.707 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr16077_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	522		95.7 (chain: 1, length: 141)
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: 141, Sequence coverage: 95.7%
- Total number of assignments
  - ¹H chemical shifts: 127
  - ¹³C chemical shifts: 268
  - 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	854	127	14.9
¹³C chemical shifts	624	268	42.9
¹⁵N chemical shifts	168	127	75.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	291	127	43.6
¹³C chemical shifts	282	268	95.0
¹⁵N chemical shifts	137	127	92.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	563	0	0.0
¹³C chemical shifts	342	0	0.0
¹⁵N chemical shifts	31	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	64	0	0.0
¹³C chemical shifts	64	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 (0.892 seconds)

BMRB: 16077

Sample

Entries sharing articles BMRB: 6 entries Detail

Related entities 1. mPrP90 P105L, : 1 : 6 : 105 entities Detail

Interaction partners 1. mPrP90 P105L, : 36 interactors Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 3 contents Detail