BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34481

Title: Solution NMR structure of the S0_2.126 designed protein   PubMed: 32409444

Deposition date: 2020-01-23 Original release date: 2020-04-13

Authors: Abriata, L.

Citation: Sesterhenn, Fabian; Yang, Che; Bonet, Jaume; Cramer, Johannes; Wen, Xiaolin; Wang, Yimeng; Chiang, Chi-I; Abriata, Luciano; Kucharska, Iga; Castoro, Giacomo; Vollers, Sabrina; Galloux, Marie; Dheilly, Elie; Rosset, Stephane; Corthesy, Patricia; Georgeon, Sandrine; Villard, Melanie; Richard, Charles-Adrien; Descamps, Delphyne; Delgado, Teresa; Oricchio, Elisa; Rameix-Welti, Marie-Anne; Mas, Vicente; Ervin, Sean; Eleouet, Jean-Francois; Riffault, Sabine; Bates, John; Julien, Jean-Philippe; Li, Yuxing; Jardetzky, Theodore; Krey, Thomas; Correia, Bruno. "De novo protein design enables precise induction of RSV neutralizing antibodies"  Science 368, .-. (2020).

Assembly members:
entity_1, polymer, 71 residues, 8209.471 Da.

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
entity_1: ASPCDKQKNYIDKQLLPIVN KAGCSRPEEVEERIRRALKK MGDTSCFDEILKGLKEIKCG GSWLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts207
15N chemical shifts61
1H chemical shifts313

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 71 residues - 8209.471 Da.

1   ALASERPROCYSASPLYSGLNLYSASNTYR
2   ILEASPLYSGLNLEULEUPROILEVALASN
3   LYSALAGLYCYSSERARGPROGLUGLUVAL
4   GLUGLUARGILEARGARGALALEULYSLYS
5   METGLYASPTHRSERCYSPHEASPGLUILE
6   LEULYSGLYLEULYSGLUILELYSCYSGLY
7   GLYSERTRPLEUGLUHISHISHISHISHIS
8   HIS

Samples:

sample_1: protein 3hb_126543, natural anundance, 500 uM; sodium phosphate, natural anundance, 20 mM

sample_2: protein 3hb_126543, [U-99% 15N], 500 uM; sodium phosphate, natural anundance, 20 mM

sample_3: protein 3hb_126543, [U-99% 13C; U-99% 15N], 400 uM; sodium phosphate, natural anundance, 20 mM

sample_4: protein 3hb_126543, natural anundance, 500 uM; sodium phosphate, natural anundance, 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

UNIO, T. Herrmann - structure calculation

TopSpin, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE II 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts