BMRB Entry 25692

Name: SOLUTION STRUCTURE OF OVIS ARIES PRP
Published: 2016-05-23

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PDB ID: 2n53
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25692
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: SOLUTION STRUCTURE OF OVIS ARIES PRP PubMed: 27226369

Deposition date: 2015-07-06 Original release date: 2016-05-23

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

Citation: Munoz-Montesino, Carola; Sizun, Christina; Moudjou, Mohammed; Herzog, Laetitia; Reine, Fabienne; Chapuis, Jerome; Ciric, Danica; Igel-Egalon, Angelique; Laude, Hubert; Beringue, Vincent; Rezaei, Human; Dron, Michel. "Generating Bona Fide Mammalian Prions with Internal Deletions" J. Virol. 90, 6963-6975 (2016).

Assembly members:
entity, polymer, 206 residues, 16263.355 Da.

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

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

Entity Sequences (FASTA):
entity: MGSSHHHHHHSSGLVPRGSH MSNKPSKPKTNMKHVAGAAA AGAVVGGLGGYMLGSVMSRP LIHFGNDYEDRYYRENMYRY PNQVYYRPVDQYSNQNNFVH DCVNITVKQHTVTTTTKGEN FTETDIKIMERVVEQMCITQ YQRESQAYYQRGASVNITVK QHTVTTTTKGENFTETDIKI MERVVEQMCITQYQRESQAY YQRGAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
15N chemical shifts	148
1H chemical shifts	836

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 206 residues - 16263.355 Da.

Residues 92-102 correspond to anN-terminal His-tag for purification purposes.

1

MET

GLY

SER

HIS

2

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

5

ALA

GLY

ALA

VAL

GLY

LEU

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

ARG

GLU

ASN

MET

TYR

ARG

TYR

9

PRO

ASN

GLN

VAL

TYR

ARG

PRO

VAL

ASP

10

GLN

TYR

SER

ASN

GLN

ASN

PHE

VAL

HIS

11

ASP

CYS

VAL

ASN

ILE

THR

VAL

LYS

GLN

HIS

12

THR

VAL

THR

LYS

GLY

GLU

ASN

13

PHE

THR

GLU

THR

ASP

ILE

LYS

ILE

MET

GLU

14

ARG

VAL

GLU

GLN

MET

CYS

ILE

THR

GLN

15

TYR

GLN

ARG

GLU

SER

GLN

ALA

TYR

GLN

16

ARG

GLY

ALA

SER

VAL

ASN

ILE

THR

VAL

LYS

17

GLN

HIS

THR

VAL

THR

LYS

GLY

18

GLU

ASN

PHE

THR

GLU

THR

ASP

ILE

LYS

ILE

19

MET

GLU

ARG

VAL

GLU

GLN

MET

CYS

ILE

20

THR

GLN

TYR

GLN

ARG

GLU

SER

GLN

ALA

TYR

21

TYR

GLN

ARG

GLY

ALA

SER

Samples:

N15_H2O: PrPWT, [U-99% 15N], 0.3 ± 3e-05 mM; Sodium acetate 10.0 ± 0.001 mM; H2O 90 ± 0.001 %; D2O 10 ± 0.001 %

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	N15_H2O	isotropic	condition1
3D 1H-15N NOESY	N15_H2O	isotropic	condition1
3D 1H-15N TOCSY 20ms	N15_H2O	isotropic	condition1
3D 1H-15N TOCSY 50ms	N15_H2O	isotropic	condition1
2D 1H-1H NOESY	N15_H2O	isotropic	condition1

Software:

CcpNmr_Analysis v2.2, CCPN - Assignment and NMR data analysis

Cyana v3.0, Peter Guntert - Structure calculation

Talos+ v1.0, Yang Shen - Secondary structure prediction

Topspin v3.1, Bruker - NMR data processing

NMR spectrometers:

Bruker Avance 950 MHz

Biological Magnetic Resonance Data Bank