BMRB Entry 34178

Name: Solid-state MAS NMR structure of the HELLF prion amyloid fibrils
Published: 2018-10-02

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PDB ID: 6eka
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34178
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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:

Solid-state MAS NMR structure of the HELLF prion amyloid fibrils

Deposition date:

2017-09-25

Original release date:

2018-10-02

Authors:

Martinez, D.; Daskalov, A.; Andreas, L.; Bardiaux, B.; Coustou, V.; Stanek, J.; Berbon, M.; Noubhani, M.; Kauffmann, B.; Wall, J.; Pintacuda, G.; Saupe, S.; Habenstein, B.; Loquet, A.

Citation:

Citation: Daskalov, Asen; Martinez, Denis; Coustou, Virginie; El Mammeri, Nadia; Berbon, Melanie; Andreas, Loren; Bardiaux, Benjamin; Stanek, Jan; Noubhani, Abdelmajid; Kauffmann, Brice; Wall, Joseph; Pintacuda, Guido; Saupe, Sven; Habenstein, Birgit; Loquet, Antoine. "Structural and molecular basis of cross-seeding barriers in amyloids" Proc. Natl. Acad. Sci. U. S. A. 118, e2014085118-e2014085118 (2021).
PubMed: 33443172

Assembly members:

Assembly members:
entity_1, polymer, 78 residues, 8515.534 Da.

Natural source:

Natural source: Common Name: Pleurage anserina Taxonomy ID: 515849 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Podospora anserina

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKTLSATRACRTGQKFGEMK TDDHSIAMQGIVGVAQPGVD QSFGSLTTTKSSRAFQGQMD AGSFSNLFSKLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	179
15N chemical shifts	45
1H chemical shifts	258

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1
3	entity_1, 3	1
4	entity_1, 4	1
5	entity_1, 5	1

Entities:

Entity 1, entity_1, 1 78 residues - 8515.534 Da.

1

MET

LYS

THR

LEU

SER

ALA

THR

ARG

ALA

CYS

2

ARG

THR

GLY

GLN

LYS

PHE

GLY

GLU

MET

LYS

3

THR

ASP

HIS

SER

ILE

ALA

MET

GLN

GLY

4

ILE

VAL

GLY

VAL

ALA

GLN

PRO

GLY

VAL

ASP

5

GLN

SER

PHE

GLY

SER

LEU

THR

LYS

6

SER

ARG

ALA

PHE

GLN

GLY

GLN

MET

ASP

7

ALA

GLY

SER

PHE

SER

ASN

LEU

PHE

SER

LYS

8

LEU

GLU

HIS

Samples:

sample_1: HELLF protein, U-15N/13C labeled, 1 mM

sample_2: HELLF, (U-14N/13C)/(U-15N/12C)]), 1 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
HhCH	sample_1	anisotropic	sample_conditions_1
HhNH	sample_1	anisotropic	sample_conditions_1
HhNH	sample_2	anisotropic	sample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment, peak picking

ARIA v2.3.2, Rieping, Habeck, Bardiaux, Bernard, Malliavin, Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker AvanceIII 1000 MHz

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