BMRB Entry 30185
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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/BMR30185
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Title: NMR structure of apo-PS1 PubMed: 29168496
Deposition date: 2016-09-28 Original release date: 2017-08-03
Authors: Polizzi, N.; Wu, Y.
Citation: Polizzi, Nicholas; Wu, Yibing; Lemmin, Thomas; Maxwell, Alison; Zhang, Shao-Qing; Rawson, Jeff; Beratan, David; Therien, Michael; DeGrado, William. "De novo design of a hyperstable non-natural protein-ligand complex with sub-angstrom accuracy." Nat. Chem. 9, 1157-1164 (2017).
Assembly members:
PS1, polymer, 109 residues, 12965.262 Da.
Natural source: Common Name: enterobacteria 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):
PS1: SEFEKLRQTGDELVQAFQRL
REIFDKGDDDSLEQVLEEIE
ELIQKHRQLFDNRQEAADTE
AAKQGDQWVQLFQRFREAID
KGDKDSLEQLLEELEQALQK
IRELAEKKN
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 363 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 784 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 109 residues - 12965.262 Da.
| 1 | SER | GLU | PHE | GLU | LYS | LEU | ARG | GLN | THR | GLY | ||||
| 2 | ASP | GLU | LEU | VAL | GLN | ALA | PHE | GLN | ARG | LEU | ||||
| 3 | ARG | GLU | ILE | PHE | ASP | LYS | GLY | ASP | ASP | ASP | ||||
| 4 | SER | LEU | GLU | GLN | VAL | LEU | GLU | GLU | ILE | GLU | ||||
| 5 | GLU | LEU | ILE | GLN | LYS | HIS | ARG | GLN | LEU | PHE | ||||
| 6 | ASP | ASN | ARG | GLN | GLU | ALA | ALA | ASP | THR | GLU | ||||
| 7 | ALA | ALA | LYS | GLN | GLY | ASP | GLN | TRP | VAL | GLN | ||||
| 8 | LEU | PHE | GLN | ARG | PHE | ARG | GLU | ALA | ILE | ASP | ||||
| 9 | LYS | GLY | ASP | LYS | ASP | SER | LEU | GLU | GLN | LEU | ||||
| 10 | LEU | GLU | GLU | LEU | GLU | GLN | ALA | LEU | GLN | LYS | ||||
| 11 | ILE | ARG | GLU | LEU | ALA | GLU | LYS | LYS | ASN |
Samples:
sample_1: apo-PS1, [U-100% 13C; U-100% 15N], 780 uM; NaPi 100 mM; NaCl 50 mM; H2O 95%; D2O 5%
sample_2: apo-PS1, U-100% 15N; 10% 13C], 780 uM; NaPi 100 mM; NaCl 50 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 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 CO(CA)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-13Caliphatic-13Caromatic-resolved [1H-1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D simultaneous NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
XEASY, Bartels et al. - peak picking
NMR spectrometers:
- Bruker AvanceII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts