BMRBj - BMREntryMaster

Found 1 Document (1.674 seconds)

BMRB: 5197

2L1K

1H and 13CA chemical shift assignments of the polypeptide mPrP(143-158)

Authors

Liu, A., Riek, R., Zahn, R., Glockshuber, R., Wuthrich, K.

Assembly

mouse prion protein

Entity

1. mouse prion protein (polymer, Thiol state: not present), 16 monomers, 2270.396 × 2 Da Detail

NDWEDRYYRE NMYRYP

Total weight

4540.792 Da

Max. entity weight

2270.396 Da

Source organism

Mus musculus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 65.8 %, Completeness (bb): 58.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	65.8 % (129 of 196)	98.3 % (113 of 115)	19.8 % (16 of 81)
Backbone	58.2 % (46 of 79)	96.8 % (30 of 31)	33.3 % (16 of 48)
Sidechain	62.4 % (83 of 133)	98.8 % (83 of 84)	0.0 % (0 of 49)
Aromatic	51.2 % (22 of 43)	100.0 % (22 of 22)	0.0 % (0 of 21)

1. mPrP(143-158)

NDWEDRYYRE NMYRYP

Show sample condition

Sample

Temperature 293 K, pH 4.5

#	Name	Concentration
1	mPrP(143-158)	1.0 mM
2	H2O	90 %
3	D2O	10 %

Chem. Shift Complete2

Sequence coverage: 50.0 %, Completeness: 46.2 %, Completeness (bb): 39.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	46.2 % (181 of 392)	70.4 % (162 of 230)	11.7 % (19 of 162)
Backbone	39.9 % (63 of 158)	71.0 % (44 of 62)	19.8 % (19 of 96)
Sidechain	44.7 % (119 of 266)	70.2 % (118 of 168)	1.0 % (1 of 98)
Aromatic	34.9 % (30 of 86)	68.2 % (30 of 44)	0.0 % (0 of 42)

1. mPrP(143-158)

NDWEDRYYRE NMYRYP

Show sample condition

Sample

Temperature 293 K, pH 4.5

#	Name	Concentration
1	mPrP(143-158)	1.0 mM
2	H2O	90 %
3	D2O	10 %

Chem. Shift Complete3

Sequence coverage: 100.0 %, Completeness: 53.4 %, Completeness (bb): 46.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	53.4 % (314 of 588)	79.7 % (275 of 345)	16.0 % (39 of 243)
Backbone	46.8 % (111 of 237)	79.6 % (74 of 93)	25.7 % (37 of 144)
Sidechain	51.4 % (205 of 399)	79.8 % (201 of 252)	2.7 % (4 of 147)
Aromatic	40.3 % (52 of 129)	78.8 % (52 of 66)	0.0 % (0 of 63)

1. mPrP(143-158)

NDWEDRYYRE NMYRYP

Show sample condition

Sample

Temperature 293 K, pH 4.5

#	Name	Isotope labeling	Concentration
4	mPrP(143-158)		1.0 mM
5	H2O		90 %
6	TFE	[U-2H]	10 %

Chem. Shift Complete4

Sequence coverage: 43.8 %, Completeness: 46.9 %, Completeness (bb): 40.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	46.9 % (368 of 784)	70.0 % (322 of 460)	14.2 % (46 of 324)
Backbone	40.5 % (128 of 316)	69.4 % (86 of 124)	21.9 % (42 of 192)
Sidechain	45.9 % (244 of 532)	70.2 % (236 of 336)	4.1 % (8 of 196)
Aromatic	37.2 % (64 of 172)	72.7 % (64 of 88)	0.0 % (0 of 84)

1. mPrP(143-158)

NDWEDRYYRE NMYRYP

Show sample condition

Sample

Temperature 293 K, pH 4.5

#	Name	Isotope labeling	Concentration
4	mPrP(143-158)		1.0 mM
5	H2O		90 %
6	TFE	[U-2H]	10 %

Chem. Shift Complete5

Sequence coverage: 100.0 %, Completeness: 51.1 %, Completeness (bb): 44.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	51.1 % (501 of 980)	75.7 % (435 of 575)	16.3 % (66 of 405)
Backbone	44.8 % (177 of 395)	74.8 % (116 of 155)	25.4 % (61 of 240)
Sidechain	49.6 % (330 of 665)	76.0 % (319 of 420)	4.5 % (11 of 245)
Aromatic	40.0 % (86 of 215)	78.2 % (86 of 110)	0.0 % (0 of 105)

1. mPrP(143-158)

NDWEDRYYRE NMYRYP

Show sample condition

Sample

Temperature 293 K, pH 4.5

#	Name	Isotope labeling	Concentration
7	mPrP(143-158)		1.0 mM
8	H2O		75 %
9	TFE	[U-2H]	25 %

Chem. Shift Complete6

Sequence coverage: 37.5 %, Completeness: 46.5 %, Completeness (bb): 40.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	46.5 % (547 of 1176)	69.4 % (479 of 690)	14.0 % (68 of 486)
Backbone	40.1 % (190 of 474)	68.3 % (127 of 186)	21.9 % (63 of 288)
Sidechain	45.6 % (364 of 798)	69.8 % (352 of 504)	4.1 % (12 of 294)
Aromatic	36.4 % (94 of 258)	71.2 % (94 of 132)	0.0 % (0 of 126)

1. mPrP(143-158)

NDWEDRYYRE NMYRYP

Show sample condition

Sample

Temperature 293 K, pH 4.5

#	Name	Isotope labeling	Concentration
7	mPrP(143-158)		1.0 mM
8	H2O		75 %
9	TFE	[U-2H]	25 %

Chem. Shift Complete7

Sequence coverage: 100.0 %, Completeness: 49.3 %, Completeness (bb): 42.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	49.3 % (676 of 1372)	73.5 % (592 of 805)	14.8 % (84 of 567)
Backbone	42.7 % (236 of 553)	72.4 % (157 of 217)	23.5 % (79 of 336)
Sidechain	48.0 % (447 of 931)	74.0 % (435 of 588)	3.5 % (12 of 343)
Aromatic	38.5 % (116 of 301)	75.3 % (116 of 154)	0.0 % (0 of 147)

1. mPrP(143-158)

NDWEDRYYRE NMYRYP

Show sample condition

Sample

Temperature 293 K, pH 4.5

#	Name	Isotope labeling	Concentration
10	mPrP(143-158)		1.0 mM
11	H2O		50 %
12	TFE	[U-2H]	50 %

Chem. Shift Complete8

Sequence coverage: 43.8 %, Completeness: 46.4 %, Completeness (bb): 40.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	46.4 % (728 of 1568)	69.2 % (637 of 920)	14.0 % (91 of 648)
Backbone	40.0 % (253 of 632)	67.7 % (168 of 248)	22.1 % (85 of 384)
Sidechain	45.5 % (484 of 1064)	69.8 % (469 of 672)	3.8 % (15 of 392)
Aromatic	36.3 % (125 of 344)	70.5 % (124 of 176)	0.6 % (1 of 168)

1. mPrP(143-158)

NDWEDRYYRE NMYRYP

Show sample condition

Sample

Temperature 293 K, pH 4.5

#	Name	Isotope labeling	Concentration
10	mPrP(143-158)		1.0 mM
11	H2O		50 %
12	TFE	[U-2H]	50 %

Release date

2001-11-11

Citation

Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy
Liu, A., Riek, R., Zahn, R., Glockshuber, R., Wuthrich, K.
Biopolymers (1999), 51, 145-152, PubMed 10397798 , DOI 10.1002/(SICI)1097-0282(1999)51:2<145::AID-BIP4>3.0.CO;2-4 , Abstract

Related entities 1. mouse prion protein, : 1 : 22 : 103 : 7 : 6 entities Detail

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

More details for 36 interactors identified by 12 citations

Experiments performed 1 experiments Detail

Chemical shift validation 10 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5197_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: bmr5197_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	OK	129	100.0 (chain: 1, length: 16)
2	Assigned chemical shifts	shift_set_2	OK	38	31.2 (chain: 1, length: 16)
3	Assigned chemical shifts	shift_set_3	OK	129	100.0 (chain: 1, length: 16)
4	Assigned chemical shifts	shift_set_4	OK	38	31.2 (chain: 1, length: 16)
5	Assigned chemical shifts	shift_set_5	OK	129	100.0 (chain: 1, length: 16)
6	Assigned chemical shifts	shift_set_6	OK	38	31.2 (chain: 1, length: 16)
7	Assigned chemical shifts	shift_set_7	OK	129	100.0 (chain: 1, length: 16)
8	Assigned chemical shifts	shift_set_8	OK	38	31.2 (chain: 1, length: 16)
1	Chemical shift references	chemical_shift_reference	OK	2	No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 16
  - ¹H chemical shifts: 113
- 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: shift_set_2
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 31.2%
- Total number of assignments
  - ¹H chemical shifts: 38
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: shift_set_3
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 16
  - ¹H chemical shifts: 113
- 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: shift_set_4
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 31.2%
- Total number of assignments
  - ¹H chemical shifts: 38
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: shift_set_5
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 16
  - ¹H chemical shifts: 113
- 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: shift_set_6
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 31.2%
- Total number of assignments
  - ¹H chemical shifts: 38
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: shift_set_7
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 16
  - ¹H chemical shifts: 113
- 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: shift_set_8
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 31.2%
- Total number of assignments
  - ¹H chemical shifts: 38
- Completeness of assignments
- 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	81	16	19.8
¹H chemical shifts	115	113	98.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	32	16	50.0
¹H chemical shifts	31	30	96.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	49	0	0.0
¹H chemical shifts	84	83	98.8

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	21	0	0.0
¹H chemical shifts	22	22	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	81	16	19.8
¹H chemical shifts	115	113	98.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	32	16	50.0
¹H chemical shifts	31	30	96.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	49	0	0.0
¹H chemical shifts	84	83	98.8

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	21	0	0.0
¹H chemical shifts	22	22	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	81	16	19.8
¹H chemical shifts	115	113	98.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	32	16	50.0
¹H chemical shifts	31	30	96.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	49	0	0.0
¹H chemical shifts	84	83	98.8

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	21	0	0.0
¹H chemical shifts	22	22	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	81	16	19.8
¹H chemical shifts	115	113	98.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	32	16	50.0
¹H chemical shifts	31	30	96.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	49	0	0.0
¹H chemical shifts	84	83	98.8

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	21	0	0.0
¹H chemical shifts	22	22	100.0

Keywords transmissible spongiform encephalopathies, protein-only hypothesis, polypeptides in neurodegenerative disease, NMR structure determination, helix propensity of a prion protein fragment

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Found 1 Document (1.674 seconds)

BMRB: 5197

Sample

Sample

Sample

Sample

Sample

Sample

Sample

Sample

Related entities 1. mouse prion protein, : 1 : 22 : 103 : 7 : 6 entities Detail

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

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Sample #3

Sample #4

Chemical shift validation 10 contents Detail