BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	91.0 % (1218 of 1338)	99.3 % (694 of 699)	77.6 % (398 of 513)	100.0 % (126 of 126)
Backbone	86.3 % (580 of 672)	98.3 % (227 of 231)	73.4 % (243 of 331)	100.0 % (110 of 110)
Sidechain	96.4 % (743 of 771)	99.8 % (467 of 468)	90.6 % (260 of 287)	100.0 % (16 of 16)
Aromatic	81.7 % (116 of 142)	100.0 % (71 of 71)	62.9 % (44 of 70)	100.0 % (1 of 1)
Methyl	100.0 % (86 of 86)	100.0 % (43 of 43)	100.0 % (43 of 43)

1. mouse prion protein double mutant D167S, N173K

SVVGGLGGYM LGSAMSRPMI HFGNDWEDRY YRENMYRYPN QVYYRPVSQY SNQKNFVHDC VNITIKQHTV TTTTKGENFT ETDVKMMERV VEQMCVTQYQ KESQAYYDGR RSS

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Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	sodium acetate	[U-2H]	10 (±1.0) mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %
4	entity	natural abundance	1.3 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.25145
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.10133

Referencing offset: 0.42 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.25145
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.10133

Referencing offset: 0.42 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.25145
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.10133

Referencing offset: 0.14 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2KU6, Strand ID: A Detail

Release date

2010-05-17

Citation

Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein
Perez, D.R., Damberger, F.F., Wuthrich, K.
J. Mol. Biol. (2010), 400, 121-128, PubMed 20460128 , DOI 10.1016/j.jmb.2010.04.066 , Abstract

Related entities 1. mouse prion protein double mutant D167S, N173K, : 1 : 13 : 142 entities Detail

Interaction partners 1. mouse prion protein double mutant D167S, N173K, : 36 interactors Detail

More details for 36 interactors identified by 12 citations

Experiments performed 5 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_16723_2ku6.nef
Input source #2: Coordindates	2ku6.cif
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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

120-----130-------140-------150-------160-------170-------180-------190-------200-------210-------22
SVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVSQYSNQKNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQ
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVSQYSNQKNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQ
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

0-------230--
KESQAYYDGRRSS
|||||||||||||
KESQAYYDGRRSS
-------110---

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	113	0	0	100.0

Content subtype: combined_16723_2ku6.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1197		100.0 (chain: A, length: 113)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	3322 (1)	noe	100.0 (chain: A, length: 113)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 113, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 694
  - ¹³C chemical shifts: 370
  - ¹⁵N chemical shifts: 133
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
156	ARG	HH21	6.318

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	699	692	99.0
¹³C chemical shifts	513	370	72.1
¹⁵N chemical shifts	134	133	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	231	225	97.4
¹³C chemical shifts	226	113	50.0
¹⁵N chemical shifts	110	110	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	468	467	99.8
¹³C chemical shifts	287	257	89.5
¹⁵N chemical shifts	24	23	95.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	50	100.0
¹³C chemical shifts	50	50	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	71	71	100.0
¹³C chemical shifts	70	42	60.0
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 113, Sequence coverage: 100.0%
- Total number of restraints: 3308
- Weight of restraints: 1.0 (3308)
- Potential type of restraints: upper-bound-parabolic (3308)
- Range of distance target values: 2.4, 5.5 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords mouse, mPrP_D167S_N173K, mutant, prion protein

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Found 1 Document (1.06 seconds)

BMRB: 16723

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. mouse prion protein double mutant D167S, N173K, : 1 : 13 : 142 entities Detail

Interaction partners 1. mouse prion protein double mutant D167S, N173K, : 36 interactors Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 3 contents Detail