BMRB Entry 16722

Name: mPrP_D167S
Published: 2010-05-18

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PDB ID: 2ku5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16722
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:

mPrP_D167S

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 double mutant D167S, N173K, polymer, 113 residues, 13203.797 Da.

Natural source:

Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mouse prion protein double mutant D167S, N173K: SVVGGLGGYMLGSAMSRPMI HFGNDWEDRYYRENMYRYPN QVYYRPVSQYSNQNNFVHDC VNITIKQHTVTTTTKGENFT ETDVKMMERVVEQMCVTQYQ KESQAYYDGRRSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	367
15N chemical shifts	134
1H chemical shifts	790

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mouse prion protein double mutant D167S, N173K	1

Entities:

Entity 1, mouse prion protein double mutant D167S, N173K 113 residues - 13203.797 Da.

1

SER

VAL

GLY

LEU

GLY

TYR

MET

2

LEU

GLY

SER

ALA

MET

SER

ARG

PRO

MET

ILE

3

HIS

PHE

GLY

ASN

ASP

TRP

GLU

ASP

ARG

TYR

4

TYR

ARG

GLU

ASN

MET

TYR

ARG

TYR

PRO

ASN

5

GLN

VAL

TYR

ARG

PRO

VAL

SER

GLN

TYR

6

SER

ASN

GLN

ASN

PHE

VAL

HIS

ASP

CYS

7

VAL

ASN

ILE

THR

ILE

LYS

GLN

HIS

THR

VAL

8

THR

LYS

GLY

GLU

ASN

PHE

THR

9

GLU

THR

ASP

VAL

LYS

MET

GLU

ARG

VAL

10

VAL

GLU

GLN

MET

CYS

VAL

THR

GLN

TYR

GLN

11

LYS

GLU

SER

GLN

ALA

TYR

ASP

GLY

ARG

12

ARG

SER

Samples:

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

BMRB	15845 16071 16075 16076 16077 16078 16079 16080 16184 16185 16723 17081 17082 17084 17174 17213 17758 17759
PDB	1AG2 1XYX 1Y15 1Y16 2K5O 2KFM 2KFO 2KU5 2KU6 2L1D 2L1E 2L1H 2L39 2L40 4H88 4MA7 4MA8
DBJ	BAA08790 BAE28320 BAE28693 BAE29994 BAE34221
EMBL	CAJ18553
GB	AAA39996 AAA39997 AAA39998 AAA41947 AAB30728
REF	NP_001265185 NP_035300 NP_036763 XP_006235124
SP	P04925 P13852 Q9Z0T3
AlphaFold	P04925 P13852 Q9Z0T3