BMRB Entry 17714

Name: human prion protein mutant HuPrP(90-231, M129, V210I)
Published: 2011-08-19

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PDB ID: 2lej
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17714
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:

human prion protein mutant HuPrP(90-231, M129, V210I)

Deposition date:

2011-06-16

Original release date:

2011-08-19

Authors:

Biljan, Ivana; Ilc, Gregor; Giachin, Gabriele; Raspadori, Andrea; Zhukov, Igor; Plavec, Janez; Legname, Giuseppe

Citation:

Citation: Biljan, Ivana; Ilc, Gregor; Giachin, Gabriele; Raspadori, Andrea; Zhukov, Igor; Plavec, Janez; Legname, Giuseppe. "Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation." J. Mol. Biol. 412, 660-673 (2011).
PubMed: 21839748

Assembly members:

Assembly members:
HuPrP, polymer, 147 residues, 16654.660 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HuPrP: GAMDPGQGGGTHSQWNKPSK PKTNMKHMAGAAAAGAVVGG LGGYMLGSAMSRPIIHFGSD YEDRYYRENMHRYPNQVYYR PMDEYSNQNNFVHDCVNITI KQHTVTTTTKGENFTETDVK MMERVIEQMCITQYERESQA YYQRGSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	459
15N chemical shifts	149
1H chemical shifts	928

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HuPrP	1

Entities:

Entity 1, HuPrP 147 residues - 16654.660 Da.

Gly85-Pro89 nonnative

1

GLY

ALA

MET

ASP

PRO

GLY

GLN

GLY

2

THR

HIS

SER

GLN

TRP

ASN

LYS

PRO

SER

LYS

3

PRO

LYS

THR

ASN

MET

LYS

HIS

MET

ALA

GLY

4

ALA

GLY

ALA

VAL

GLY

5

LEU

GLY

TYR

MET

LEU

GLY

SER

ALA

MET

6

SER

ARG

PRO

ILE

HIS

PHE

GLY

SER

ASP

7

TYR

GLU

ASP

ARG

TYR

ARG

GLU

ASN

MET

8

HIS

ARG

TYR

PRO

ASN

GLN

VAL

TYR

ARG

9

PRO

MET

ASP

GLU

TYR

SER

ASN

GLN

ASN

10

PHE

VAL

HIS

ASP

CYS

VAL

ASN

ILE

THR

ILE

11

LYS

GLN

HIS

THR

VAL

THR

LYS

12

GLY

GLU

ASN

PHE

THR

GLU

THR

ASP

VAL

LYS

13

MET

GLU

ARG

VAL

ILE

GLU

GLN

MET

CYS

14

ILE

THR

GLN

TYR

GLU

ARG

GLU

SER

GLN

ALA

15

TYR

GLN

ARG

GLY

SER

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2

Related Database Links:

BMRB	15676 16743 16757 17756 17757 17780 18426 18550 19268 4379 4402 4434 4620 4641 4736
PDB	1E1G 1E1J 1E1P 1E1S 1E1U 1E1W 1FKC 1FO7 1HJM 1HJN 1I4M 1QLX 1QLZ 1QM0 1QM1 1QM2 1QM3 2K1D 2KUN 2LEJ 2LFT 2LSB 2LV1 2M8T 2W9E 3HAF 3HAK 3HEQ 3HER 3HES 3HJ5 3HJX 4DGI 4KML 4N9O
DBJ	BAA00011 BAF62360 BAG32276 BAG32277 BAG32278
EMBL	CAA58442 CAG46836 CAG46869
GB	AAA19664 AAA60182 AAA68632 AAA68633 AAB59442
REF	NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP	P04156 P40252 P61766 P61767 P61768
AlphaFold	P04156 P40252 P61766 P61767 P61768

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 17714

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: