BMRB Entry 17087

Name: Mouse prion protein (121-231) with the mutations Y169A, Y225A, and Y226A.
Published: 2012-08-02

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PDB ID: 2l1k
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17087
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:

Mouse prion protein (121-231) with the mutations Y169A, Y225A, and Y226A.

Deposition date:

2010-07-28

Original release date:

2012-08-02

Authors:

Christen, Barbara; Damberger, Fred; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt

Citation:

Citation: Christen, Barbara; Damberger, Fred; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt. "Temperature-dependent conformational exchange in the cellular form of prion proteins" J. Mol. Biol. ., .-..

Assembly members:

Assembly members:
Prion with Y169A, Y225A, Y226A mutation, polymer, 114 residues, Formula weight is not available

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: pRSETA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Prion with Y169A, Y225A, Y226A mutation: GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPVDQASNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAAADGRRSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	363
15N chemical shifts	135
1H chemical shifts	784

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	prion	1

Entities:

Entity 1, prion 114 residues - Formula weight is not available

1

GLY

SER

VAL

GLY

LEU

GLY

TYR

2

MET

LEU

GLY

SER

ALA

MET

SER

ARG

PRO

MET

3

ILE

HIS

PHE

GLY

ASN

ASP

TRP

GLU

ASP

ARG

4

TYR

ARG

GLU

ASN

MET

TYR

ARG

TYR

PRO

5

ASN

GLN

VAL

TYR

ARG

PRO

VAL

ASP

GLN

6

ALA

SER

ASN

GLN

ASN

PHE

VAL

HIS

ASP

7

CYS

VAL

ASN

ILE

THR

ILE

LYS

GLN

HIS

THR

8

VAL

THR

LYS

GLY

GLU

ASN

PHE

9

THR

GLU

THR

ASP

VAL

LYS

MET

GLU

ARG

10

VAL

GLU

GLN

MET

CYS

VAL

THR

GLN

TYR

11

GLN

LYS

GLU

SER

GLN

ALA

ASP

GLY

12

ARG

SER

Samples:

sample_1: prion, [U-99% 13C; U-99% 15N], 1.4 mM; sodium acetate, [U-2H], 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 293.2 K

Experiments:

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

Software:

xwinnmr, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

ATHNOS-CANDID v1.2, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking

DYANA v1.0.3, Guntert, Mumenthaler and Wuthrich - structure solution

OPALP, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

Bruker DRX 500 MHz
Bruker Avance 900 MHz
Bruker DRX 750 MHz
Bruker DRX 600 MHz

BMRB	16075 16184 17081 17084 17174 17213 17758
PDB	1AG2 1XYX 2KFM 2L1D 2L1H 2L1K 2L39 2L40