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Found 1 Document (1.75 seconds)

BMRB: 4402

1QLZ

1H, 13C and 15N chemical shift assignment of human prion protein hPrP(23-230)

Authors

Liu, A., Riek, R., Wider, G., von Schroetter, C., Zahn, R., Wuthrich, K.

Assembly

human prion protein hPrP(23-230)

Entity

1. human prion protein hPrP(23-230) (polymer, Thiol state: all disulfide bound), 210 monomers, 22890.93 Da Detail

GSKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGGWGQP HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHSQWN KPSKPKTNMK HMAGAAAAGA VVGGLGGYML GSAMSRPIIH FGSDYEDRYY RENMHRYPNQ VYYRPMDEYS NQNNFVHDCV NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCITQYER ESQAYYQRGS

Formula weight

22890.93 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS159:SG	1:CYS194:SG

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 88.3 %, Completeness (bb): 85.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.3 % (2073 of 2347)	97.2 % (1200 of 1235)	73.2 % (647 of 884)	99.1 % (226 of 228)
Backbone	85.4 % (1051 of 1230)	99.3 % (445 of 448)	70.5 % (414 of 587)	98.5 % (192 of 195)
Sidechain	92.4 % (1186 of 1284)	95.9 % (755 of 787)	85.8 % (398 of 464)	100.0 % (33 of 33)
Aromatic	68.6 % (177 of 258)	82.9 % (107 of 129)	51.6 % (63 of 122)	100.0 % (7 of 7)
Methyl	100.0 % (104 of 104)	100.0 % (52 of 52)	100.0 % (52 of 52)

1. human prion protein

Show sample condition

Sample

Temperature 293 (±1) K, pH 4.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	human prion protein	[U-13C; U-15N]		1 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.22 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.22 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.08 ppm, Outliers: 2 Detail

Release date

2000-01-31

Citation 1

NMR Solution Structure of the Human Prion Protein
Zahn, R., Liu, A., Luhrs, T., Riek, R., von Schroetter, C., Lopez Garcia, F., Billeter, M., Calzolai, L., Wider, G., Wuthrich, K.
Proc. Natl. Acad. Sci. U. S. A. (2000), 97, 145-150

Show more 2 citaions

Citation 2

Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization
Hornemann, S., Korth, C., Oesch, B., Riek, R., Wider, G., Wuthrich, K., Glockshuber, R.
FEBS Lett. (1997), 413, 277-281, PubMed 9280297 , DOI: , Abstract

Citation 3

NMR structure of the mouse prion protein domain PrP(121-231)
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., Wuthrich, K.
Nature (1996), 382, 180-182, PubMed 8700211 , DOI 10.1038/382180a0 , Abstract

Hide non-primary 2 citaions

Entries sharing articles Swiss-Prot: 1 entries Detail

Swiss-Prot: P04925 released on 1987-08-13
Title PRIO_MOUSE Entity Major prion protein

Related entities 1. human prion protein hPrP(23-230), : 1 : 1 : 5 : 62 entities Detail

Interaction partners 1. human prion protein hPrP(23-230), : 74 interactors Detail

More details for 74 interactors identified by 16 citations

Experiments performed 8 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4402_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	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:159:CYS:SG	1:194:CYS:SG	oxidized, CA 58.5, CB 40.2 ppm	oxidized, CA 59.7, CB 41.7 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr4402_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	2157		100.0 (chain: 1, length: 210)
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: 210, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 600
  - ¹H chemical shifts: 1311
  - ¹⁵N chemical shifts: 246
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
6	PRO	N	116.9
8	PRO	N	117.7
19	PRO	N	117.3
24	PRO	N	118.4
30	PRO	N	115.2
31	PRO	N	115.2
40	PRO	N	116.8
48	PRO	N	116.8
56	PRO	N	116.8
64	PRO	N	116.8
82	PRO	N	117.3
85	PRO	N	117.3
163	THR	HG1	6.31

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	884	600	67.9
¹H chemical shifts	1235	1192	96.5
¹⁵N chemical shifts	239	234	97.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	420	207	49.3
¹H chemical shifts	448	441	98.4
¹⁵N chemical shifts	195	190	97.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	464	393	84.7
¹H chemical shifts	787	751	95.4
¹⁵N chemical shifts	44	44	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	61	59	96.7
¹H chemical shifts	61	59	96.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	122	59	48.4
¹H chemical shifts	129	105	81.4
¹⁵N chemical shifts	7	7	100.0

Keywords carbonyl carbon homonuclear isotropic mixing, flexible polypeptide chains, human prion protein, sequential NMR assignment, triple resonance experiments

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Found 1 Document (1.75 seconds)

BMRB: 4402

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles Swiss-Prot: 1 entries Detail

Related entities 1. human prion protein hPrP(23-230), : 1 : 1 : 5 : 62 entities Detail

Interaction partners 1. human prion protein hPrP(23-230), : 74 interactors Detail

Experiments performed 8 experiments Detail

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Chemical shift validation 3 contents Detail