BMRB Entry 25251

Name: Solution structure of Ovis Aries PrP with mutation delta193-196
Published: 2015-10-05

Click here to enlarge.

PDB ID: 2mv9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25251
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of Ovis Aries PrP with mutation delta193-196

Deposition date:

2014-09-25

Original release date:

2015-10-05

Authors:

Munoz, Carola; Egalon, Angelique; Beringue, Vincent; Rezaei, Human; Dron, Michel; Sizun, Christina

Citation:

Citation: Munoz, Carola; Sizun, Christina; Egalon, Angelique; Beringue, Vincent; Rezaei, Human; Dron, Michel. "Conversion ability of prion protein helix 2 deletion mutants" .

Assembly members:

Assembly members:
PrPdelta193-196, polymer, 150 residues, 17123.1885 Da.

Natural source:

Natural source: Common Name: Sheep Taxonomy ID: 9940 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Ovis aries

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PrPdelta193-196: MGSSHHHHHHSSGLVPRGSH MSNKPSKPKTNMKHVAGAAA AGAVVGGLGGYMLGSVMSRP LIHFGNDYEDRYYRENMYRY PNQVYYRPVDQYSNQNNFVH DCVNITVKQHTVKGENFTET DIKIMERVVEQMCITQYQRE SQAYYQRGAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	138
15N chemical shifts	146
1H chemical shifts	786

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 150 residues - 17123.1885 Da.

1	MET	GLY	SER	SER	HIS	HIS	HIS	HIS	HIS	HIS
2	SER	SER	GLY	LEU	VAL	PRO	ARG	GLY	SER	HIS
3	MET	SER	ASN	LYS	PRO	SER	LYS	PRO	LYS	THR
4	ASN	MET	LYS	HIS	VAL	ALA	GLY	ALA	ALA	ALA
5	ALA	GLY	ALA	VAL	VAL	GLY	GLY	LEU	GLY	GLY
6	TYR	MET	LEU	GLY	SER	VAL	MET	SER	ARG	PRO
7	LEU	ILE	HIS	PHE	GLY	ASN	ASP	TYR	GLU	ASP
8	ARG	TYR	TYR	ARG	GLU	ASN	MET	TYR	ARG	TYR
9	PRO	ASN	GLN	VAL	TYR	TYR	ARG	PRO	VAL	ASP
10	GLN	TYR	SER	ASN	GLN	ASN	ASN	PHE	VAL	HIS
11	ASP	CYS	VAL	ASN	ILE	THR	VAL	LYS	GLN	HIS
12	THR	VAL	LYS	GLY	GLU	ASN	PHE	THR	GLU	THR
13	ASP	ILE	LYS	ILE	MET	GLU	ARG	VAL	VAL	GLU
14	GLN	MET	CYS	ILE	THR	GLN	TYR	GLN	ARG	GLU
15	SER	GLN	ALA	TYR	TYR	GLN	ARG	GLY	ALA	SER

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.15 ± 2e-05 mM; Sodium acetate 10.00 ± 0.001 mM; H2O 90 ± 0.001 mM; D2O 10 ± 0.001 mM

sample_2: entity, [U-99% 15N], 0.46 ± 2e-05 mM; Sodium acetate 10.00 ± 0.001 mM; H2O 90 ± 0.001 mM; D2O 10 ± 0.001 mM

condition1: ionic strength: 0 M; pH: 5.300; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	condition1
3D HN(CO)CA	sample_1	isotropic	condition1
2D 1H-15N HSQC	sample_1	isotropic	condition1
3D 1H-15N NOESY	sample_2	isotropic	condition1
3D 1H-15N TOCSY	sample_2	isotropic	condition1
2D 1H-15N HSQC	sample_2	isotropic	condition1
2D 1H-1H NOESY	sample_2	isotropic	condition1
2D 1H-15N HSQC	sample_2	isotropic	condition1

Software:

CYANA v3.0, Peter Guntert - Structure calculation

CcpNmr_Analysis v2.2, CCPN - Data analysis

Talos+ v1.0, Yang Shen - Dihedral angles

Topspin v3.1, Bruker - collection, procession

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 950 MHz

GenBank	CAA04276
GB	AJ000738.1 AAW88332
BMRB	25250
EMBL	CAA04276 CAE00190

1	MET	GLY	SER	SER	HIS	HIS	HIS	HIS	HIS	HIS
2	SER	SER	GLY	LEU	VAL	PRO	ARG	GLY	SER	HIS
3	MET	SER	ASN	LYS	PRO	SER	LYS	PRO	LYS	THR
4	ASN	MET	LYS	HIS	VAL	ALA	GLY	ALA	ALA	ALA
5	ALA	GLY	ALA	VAL	VAL	GLY	GLY	LEU	GLY	GLY
6	TYR	MET	LEU	GLY	SER	VAL	MET	SER	ARG	PRO
7	LEU	ILE	HIS	PHE	GLY	ASN	ASP	TYR	GLU	ASP
8	ARG	TYR	TYR	ARG	GLU	ASN	MET	TYR	ARG	TYR
9	PRO	ASN	GLN	VAL	TYR	TYR	ARG	PRO	VAL	ASP
10	GLN	TYR	SER	ASN	GLN	ASN	ASN	PHE	VAL	HIS
11	ASP	CYS	VAL	ASN	ILE	THR	VAL	LYS	GLN	HIS
12	THR	VAL	LYS	GLY	GLU	ASN	PHE	THR	GLU	THR
13	ASP	ILE	LYS	ILE	MET	GLU	ARG	VAL	VAL	GLU
14	GLN	MET	CYS	ILE	THR	GLN	TYR	GLN	ARG	GLU
15	SER	GLN	ALA	TYR	TYR	GLN	ARG	GLY	ALA	SER

1	MET	GLY	SER	SER	HIS	HIS	HIS	HIS	HIS	HIS
2	SER	SER	GLY	LEU	VAL	PRO	ARG	GLY	SER	HIS
3	MET	SER	ASN	LYS	PRO	SER	LYS	PRO	LYS	THR
4	ASN	MET	LYS	HIS	VAL	ALA	GLY	ALA	ALA	ALA
5	ALA	GLY	ALA	VAL	VAL	GLY	GLY	LEU	GLY	GLY
6	TYR	MET	LEU	GLY	SER	VAL	MET	SER	ARG	PRO
7	LEU	ILE	HIS	PHE	GLY	ASN	ASP	TYR	GLU	ASP
8	ARG	TYR	TYR	ARG	GLU	ASN	MET	TYR	ARG	TYR
9	PRO	ASN	GLN	VAL	TYR	TYR	ARG	PRO	VAL	ASP
10	GLN	TYR	SER	ASN	GLN	ASN	ASN	PHE	VAL	HIS
11	ASP	CYS	VAL	ASN	ILE	THR	VAL	LYS	GLN	HIS
12	THR	VAL	LYS	GLY	GLU	ASN	PHE	THR	GLU	THR
13	ASP	ILE	LYS	ILE	MET	GLU	ARG	VAL	VAL	GLU
14	GLN	MET	CYS	ILE	THR	GLN	TYR	GLN	ARG	GLU
15	SER	GLN	ALA	TYR	TYR	GLN	ARG	GLY	ALA	SER