BMRB Entry 16720

Name: Horse prion protein
Published: 2010-05-18

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PDB ID: 2ku4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16720
MolProbity Validation Chart

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

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Title:

Horse prion protein

Deposition date:

2010-02-12

Original release date:

2010-05-18

Authors:

Perez, Daniel; Damberger, Fred; Wuthrich, Kurt

Citation:

Citation: Perez, Daniel; Damberger, Fred; Wuthrich, Kurt. "Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein." J. Mol. Biol. 400, 121-128 (2010).
PubMed: 20460128

Assembly members:

Assembly members:
mouse prion protein mutant D167S, polymer, 113 residues, 13203.797 Da.

Natural source:

Natural source: Common Name: Horse Taxonomy ID: 9796 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Equus caballus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mouse prion protein mutant D167S: GSVVGGLGGYMLGSAMSRPL IHFGNDYEDRYYRENMYRYP NQVYYRPVSEYSNQKNFVHD CVNITVKQHTVTTTTKGENF TETDVKIMERVVEQMCITQY QKEYEAFQQRGAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	366
15N chemical shifts	131
1H chemical shifts	424

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mouse prion protein mutant D167S	1

Entities:

Entity 1, mouse prion protein mutant D167S 113 residues - 13203.797 Da.

1

GLY

SER

VAL

GLY

LEU

GLY

TYR

2

MET

LEU

GLY

SER

ALA

MET

SER

ARG

PRO

LEU

3

ILE

HIS

PHE

GLY

ASN

ASP

TYR

GLU

ASP

ARG

4

TYR

ARG

GLU

ASN

MET

TYR

ARG

TYR

PRO

5

ASN

GLN

VAL

TYR

ARG

PRO

VAL

SER

GLU

6

TYR

SER

ASN

GLN

LYS

ASN

PHE

VAL

HIS

ASP

7

CYS

VAL

ASN

ILE

THR

VAL

LYS

GLN

HIS

THR

8

VAL

THR

LYS

GLY

GLU

ASN

PHE

9

THR

GLU

THR

ASP

VAL

LYS

ILE

MET

GLU

ARG

10

VAL

GLU

GLN

MET

CYS

ILE

THR

GLN

TYR

11

GLN

LYS

GLU

TYR

GLU

ALA

PHE

GLN

ARG

12

GLY

ALA

SER

Samples:

sample_1: sodium acetate, [U-2H], 10 ± 1 mM; H2O 90%; D2O 10%; entity 1.3 ± 1 mM

sample_conditions_1: ionic strength: 10 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

ATHNOS-CANDID, Herrmann and Wuthrich - automatic peak picking and NOE assignment

NMR spectrometers:

Bruker DRX 750 MHz
Bruker DRX 600 MHz
Bruker DRX 500 MHz

PDB	2KU4
DBJ	BAD72795
GB	AAD19983 AAD19988 AAD19989 AAD20000 AAN16505
REF	NP_001137270 XP_008518008 XP_008518010