BMRB Entry 30495
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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/BMR30495
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Title: Solution NMR structure of a de novo designed double-stranded beta-helix PubMed: 30374087
Deposition date: 2018-07-19 Original release date: 2018-10-31
Authors: Marcos, E.; Chidyausiku, T.; McShan, A.; Evangelidis, T.; Nerli, S.; Sgourakis, N.; Tripsianes, K.; Baker, D.
Citation: Marcos, Enrique; Chidyausiku, Tamuka; McShan, Andrew; Evangelidis, Thomas; Nerli, Santrupti; Carter, Lauren; Nivon, Lucas; Davis, Audrey; Oberdorfer, Gustav; Tripsianes, Konstantinos; Sgourakis, Nikolaos; Baker, David. "De novo design of a non-local beta-sheet protein with high stability and accuracy." Nat. Struct. Mol. Biol. 25, 1028-1034 (2018).
Assembly members:
entity_1, polymer, 78 residues, 8916.916 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: TRETKVTVNPGEEYEVKVNP
GTRVEIQAKGPAEFEGGGTR
TRLNPGESYKFENLTSQPLR
IRLRNLSDTPIEFRIREE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 237 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 504 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 78 residues - 8916.916 Da.
| 1 | THR | ARG | GLU | THR | LYS | VAL | THR | VAL | ASN | PRO | ||||
| 2 | GLY | GLU | GLU | TYR | GLU | VAL | LYS | VAL | ASN | PRO | ||||
| 3 | GLY | THR | ARG | VAL | GLU | ILE | GLN | ALA | LYS | GLY | ||||
| 4 | PRO | ALA | GLU | PHE | GLU | GLY | GLY | GLY | THR | ARG | ||||
| 5 | THR | ARG | LEU | ASN | PRO | GLY | GLU | SER | TYR | LYS | ||||
| 6 | PHE | GLU | ASN | LEU | THR | SER | GLN | PRO | LEU | ARG | ||||
| 7 | ILE | ARG | LEU | ARG | ASN | LEU | SER | ASP | THR | PRO | ||||
| 8 | ILE | GLU | PHE | ARG | ILE | ARG | GLU | GLU |
Samples:
sample_1: 3NIK, [U-99% 13C; U-99% 15N], 0.81 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.7; pressure: 1 bar; temperature: 310.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_1 |
| 4D HC(CC-TOCSY(CO))NH | sample_1 | anisotropic | sample_conditions_1 |
| 4D 13C,15N edited HMQC-NOESY-HSQC | sample_1 | anisotropic | sample_conditions_1 |
Software:
CS-Rosetta, Shen, Vernon, Baker and Bax - refinement, structure calculation
4D-CHAINS, Evangelidis, et. al. - chemical shift assignment
SPARKY, Goddard - peak picking
NMR spectrometers:
- Bruker AvanceIII 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts