BMRB Entry 30249
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30249
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Title: Solution NMR structure of the de novo mini protein HEEH_rd4_0097 PubMed: 28706065
Deposition date: 2017-02-24 Original release date: 2017-07-20
Authors: Lemak, A.; Rocklin, G.; Houliston, S.; 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, 64 residues, 7469.417 Da.
Natural source: Common Name: Escherichia Taxonomy ID: 561 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia not available
Experimental source: Production method: recombinant technology Host organism: Escherichia
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH
MDVEEQIRRLEEVLKKNQPV
TWNGTTYTDPNEIKKVIEEL
RKSM
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 173 |
| 15N chemical shifts | 46 |
| 1H chemical shifts | 287 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 64 residues - 7469.417 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | ASP | VAL | GLU | GLU | GLN | ILE | ARG | ARG | LEU | ||||
| 4 | GLU | GLU | VAL | LEU | LYS | LYS | ASN | GLN | PRO | VAL | ||||
| 5 | THR | TRP | ASN | GLY | THR | THR | TYR | THR | ASP | PRO | ||||
| 6 | ASN | GLU | ILE | LYS | LYS | VAL | ILE | GLU | GLU | LEU | ||||
| 7 | ARG | LYS | SER | MET |
Samples:
sample_1: protein, [U-13C; U-15N], 400 uM; sodium chloride 150 mM; sodium phosphate 50 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
Software:
ABACUS, Lemak and Arrowsmith - chemical shift assignment
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY, Goddard - peak picking
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts