BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34178

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: Martinez, D.; Daskalov, A.; Andreas, L.; Bardiaux, B.; Coustou, V.; Stanek, J.; Berbon, M.; Noubhani, A.; Kauffmann, B.; Wall, J.; Pintacuda, G.; Saupe, S.; Habenstein, B.; Loquet, A.. "Amyloid fold conservation in the twilight zone of sequence similarity"  To Be published ., .-..

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts179
15N chemical shifts45
1H chemical shifts258

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21
3entity_1, 31
4entity_1, 41
5entity_1, 51

Entities:

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

1   METLYSTHRLEUSERALATHRARGALACYS
2   ARGTHRGLYGLNLYSPHEGLYGLUMETLYS
3   THRASPASPHISSERILEALAMETGLNGLY
4   ILEVALGLYVALALAGLNPROGLYVALASP
5   GLNSERPHEGLYSERLEUTHRTHRTHRLYS
6   SERSERARGALAPHEGLNGLYGLNMETASP
7   ALAGLYSERPHESERASNLEUPHESERLYS
8   LEUGLUHISHISHISHISHISHIS

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:

NameSampleSample stateSample conditions
HhCHsample_1anisotropicsample_conditions_1
HhNHsample_1anisotropicsample_conditions_1
HhNHsample_2anisotropicsample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts