BMRB Entry 30527
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30527
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Title: De novo Designed Protein Foldit3 PubMed: 31168091
Deposition date: 2018-10-17 Original release date: 2019-06-07
Authors: Liu, G.; Ishida, Y.; Swapna, G.; Kleinfelter, S.; Koepnick, B.; Baker, D.; Montelione, G.
Citation: Koepnick, Brian; Flatten, Jeff; Husain, Tamir; Ford, Alex; Silva, Daniel-Adriano; Bick, Matthew; Bauer, Aaron; Liu, Gaohua; Ishida, Yojiro; Boykov, Alexander; Estep, Roger; Kleinfelter, Susan; Norgard-Solano, Toke; Wei, Linda; Players, Foldit; Montelione, Gaetano; DiMaio, Frank; Popovic, Zoran; Khatib, Firas; Cooper, Seth; Baker, David. "De novo protein design by citizen scientists." Nature 570, 390-394 (2019).
Assembly members:
entity_1, polymer, 97 residues, 11725.060 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 K-12
Entity Sequences (FASTA):
entity_1: MGHHHHHHENLYFQSHMTDE
LLERLRQLFEELHERGTEIV
VEVHINGERDEIRVRNISKE
ELKKLLERIREKIEREGSSE
VEVNVHSGGQTWTFNEK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 285 |
| 15N chemical shifts | 92 |
| 1H chemical shifts | 605 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 97 residues - 11725.060 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | GLU | ASN | ||||
| 2 | LEU | TYR | PHE | GLN | SER | HIS | MET | THR | ASP | GLU | ||||
| 3 | LEU | LEU | GLU | ARG | LEU | ARG | GLN | LEU | PHE | GLU | ||||
| 4 | GLU | LEU | HIS | GLU | ARG | GLY | THR | GLU | ILE | VAL | ||||
| 5 | VAL | GLU | VAL | HIS | ILE | ASN | GLY | GLU | ARG | ASP | ||||
| 6 | GLU | ILE | ARG | VAL | ARG | ASN | ILE | SER | LYS | GLU | ||||
| 7 | GLU | LEU | LYS | LYS | LEU | LEU | GLU | ARG | ILE | ARG | ||||
| 8 | GLU | LYS | ILE | GLU | ARG | GLU | GLY | SER | SER | GLU | ||||
| 9 | VAL | GLU | VAL | ASN | VAL | HIS | SER | GLY | GLY | GLN | ||||
| 10 | THR | TRP | THR | PHE | ASN | GLU | LYS |
Samples:
sample_1: foldit3, [U-13C; U-15N], 0.3 ± 0.05 mM
sample_conditions_1: ionic strength: 0.2 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStructure, Huang, Tejero, Powers and Montelione - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
SPARKY, Goddard - peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts