BMRB Entry 30240
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30240
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Title: Solution structure of the de novo mini protein HHH_rd1_0142 PubMed: 28706065
Deposition date: 2017-01-31 Original release date: 2017-07-20
Authors: Houliston, S.; Rocklin, G.; Lemak, A.; Carter, L.; Chidyausiku, T.; Baker, D.; Arrowsmith, C.
Citation: Rocklin, Gabriel; Chidyausiku, Tamuka; Goreshnik, Inna; Ford, Alex; Houliston, Scott; Lemak, Alexander; Carter, Lauren; Ravichandran, Rashmi; Mulligan, Vikram; Chevalier, Aaron; Arrowsmith, Cheryl; Baker, David. "Global analysis of protein folding using massively parallel design, synthesis, and testing" Science 357, 168-175 (2017).
Assembly members:
entity_1, polymer, 43 residues, 5190.805 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: RKWEEIAERLREEFNINPEE
AREAVEKAGGNEEEARRIVK
KRL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 168 |
| 15N chemical shifts | 40 |
| 1H chemical shifts | 280 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 43 residues - 5190.805 Da.
| 1 | ARG | LYS | TRP | GLU | GLU | ILE | ALA | GLU | ARG | LEU | ||||
| 2 | ARG | GLU | GLU | PHE | ASN | ILE | ASN | PRO | GLU | GLU | ||||
| 3 | ALA | ARG | GLU | ALA | VAL | GLU | LYS | ALA | GLY | GLY | ||||
| 4 | ASN | GLU | GLU | GLU | ALA | ARG | ARG | ILE | VAL | LYS | ||||
| 5 | LYS | ARG | LEU |
Samples:
sample_1: protein, [U-13C; U-15N], 400 ± 200 uM; sodium chloride, unlabeled, 150 mM; sodium phosphate, unlabeled, 50 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 Pa; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C NOESY (aromatic and aliphatic) | sample_1 | isotropic | sample_conditions_1 |
Software:
ABACUS, Lemak and Arrowsmith - chemical shift assignment, peak picking
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMR spectrometers:
- Bruker Avance III 600 MHz
- Bruker Avance II 800 MHz
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