BMRB Entry 16184

Name: Mouse Prion Protein (121-231) with Mutations Y225A and Y226A
Published: 2009-05-20

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PDB ID: 2kfm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16184
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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 Mutations Y225A and Y226A

Deposition date:

2009-02-24

Original release date:

2009-05-20

Authors:

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

Citation:

Citation: Christen, Barbara; Hornemann, Simone; Damberger, Fred; Wuthrich, Kurt. "Prion Protein NMR Structure from Tammar Wallaby (Macropus eugenii) Shows that the beta2-alpha2 Loop Is Modulated by Long-Range Sequence Effects" J. Mol. Biol. ., .-. (2009).
PubMed: 19393664

Assembly members:

Assembly members:
mpp_121-231, polymer, 114 residues, 13167.715 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: pRSETA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mpp_121-231: GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPVDQYSNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAAADGRRSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	364
15N chemical shifts	135
1H chemical shifts	412

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mpp_121-231	1

Entities:

Entity 1, mpp_121-231 114 residues - 13167.715 Da.

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

TYR

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

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
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

BMRB	15845 16071 16076 16077 16078 16079 16080 16185 16722 17081 17082 17084 17087 17174 17213 17758
PDB	1AG2 1XYX 1Y15 2K5O 2KFM 2KFO 2KU5 2L1D 2L1E 2L1H 2L1K 2L39 2L40 4H88 4MA7 4MA8
DBJ	BAE34221 BAE34724 BAE34788 BAE34911 BAE35622
EMBL	CAJ18553
GB	AAA39997 AAC02804 AAD19985 AAH06703 AAL57230
REF	NP_001265185 NP_035300
SP	P04925
AlphaFold	P04925

BMRB Entry 16184

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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