BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	85.8 % (1115 of 1300)	99.3 % (672 of 677)	64.2 % (321 of 500)	99.2 % (122 of 123)
Backbone	82.9 % (552 of 666)	99.6 % (229 of 230)	65.7 % (215 of 327)	99.1 % (108 of 109)
Sidechain	90.4 % (666 of 737)	99.1 % (443 of 447)	75.7 % (209 of 276)	100.0 % (14 of 14)
Aromatic	47.0 % (63 of 134)	94.0 % (63 of 67)	0.0 % (0 of 67)
Methyl	100.0 % (86 of 86)	100.0 % (43 of 43)	100.0 % (43 of 43)

1. human prion protein 121-230

GSVVGGLGGY MLGSAMSRPI IHFGSDYEDR YYRENMHRYP NQVYYRPCDE YSNQNNFVHD CVNITIKQHT VTTTTKGENF TETDVKMMER VVEQMCITQY ERCSQAYYQR GS

Show sample condition

Sample #1

Temperature 293 (±1) K, pH 4.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	human prion protein 121-230	[U-15N; U-13C]		0.7 mM

Sample #2

Temperature 293 (±1) K, pH 4.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	human prion protein 121-230			0.7 mM

LACS Plot; CA

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

Referencing offset: -0.08 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.08 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.08 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 1H0L, Strand ID: A Detail

Release date

2003-02-19

Citation

NMR structure of a variant human prion protein with two disulfide bridges
Zahn, R., Guntert, P., von Schroetter, C., Wuthrich, K.
J. Mol. Biol. (2003), 326, 225-234, PubMed 12547204 , DOI: , Abstract

Related entities 1. Human prion protein fragment 121-230 with mutations Met166Cys and Glu221Cys, : 1 : 7 : 151 entities Detail

Interaction partners 1. Human prion protein fragment 121-230 with mutations Met166Cys and Glu221Cys, : 70 interactors Detail

More details for 70 interactors identified by 14 citations

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5378_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)
1:48:CYS:SG	1:103:CYS:SG	oxidized, CA 60.9, CB 41.4 ppm	oxidized, CA 57.1, CB 39.6 ppm	n/a
1:61:CYS:SG	1:96:CYS:SG	oxidized, CA 58.8, CB 40.9 ppm	oxidized, CA 59.9, CB 41.6 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr5378_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	CSS	Warning	1221		100.0 (chain: 1, length: 112)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: CSS
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 112, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 321
  - ¹H chemical shifts: 770
  - ¹⁵N chemical shifts: 130
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	500	321	64.2
¹H chemical shifts	677	672	99.3
¹⁵N chemical shifts	131	130	99.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	224	112	50.0
¹H chemical shifts	230	229	99.6
¹⁵N chemical shifts	109	108	99.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	276	209	75.7
¹H chemical shifts	447	443	99.1
¹⁵N chemical shifts	22	22	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	49	49	100.0
¹H chemical shifts	49	49	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	67	0	0.0
¹H chemical shifts	67	63	94.0

Keywords Prion Protein, Doppel Protein, NMR structure, Disulfide Bonds, Factor X Epitope

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.975 seconds)

BMRB: 5378

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Human prion protein fragment 121-230 with mutations Met166Cys and Glu221Cys, : 1 : 7 : 151 entities Detail

Interaction partners 1. Human prion protein fragment 121-230 with mutations Met166Cys and Glu221Cys, : 70 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample #1

Sample #2

Instrument

Sample #1

Sample #2

Instrument

Sample #1

Sample #2

Instrument

Sample #1

Sample #2

Chemical shift validation 3 contents Detail