BMRB Entry 16117
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16117
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Title: NMR structures of GA95 and GB95, two designed proteins with 95% sequence identity but different folds and functions PubMed: 19998407
Deposition date: 2009-01-12 Original release date: 2010-01-12
Authors: He, Yanan; Alexander, Patrick; Chen, Yihong; Bryan, Philip; Orban, John
Citation: Shen, Yang; Bryan, Philip; He, Yanan; Orban, John; Baker, David; Bax, Ad. "De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds." Protein Sci. 19, 349-356 (2009).
Assembly members:
entity, polymer, 56 residues, 6317.434 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: over expression in E. Coli
Entity Sequences (FASTA):
entity: TTYKLILNLKQAKEEAIKEA
VDAGTAEKYFKLIANAKTVE
GVWTYKDEIKTFTVTE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 242 |
| 15N chemical shifts | 59 |
| 1H chemical shifts | 354 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 56 residues - 6317.434 Da.
| 1 | THR | THR | TYR | LYS | LEU | ILE | LEU | ASN | LEU | LYS | ||||
| 2 | GLN | ALA | LYS | GLU | GLU | ALA | ILE | LYS | GLU | ALA | ||||
| 3 | VAL | ASP | ALA | GLY | THR | ALA | GLU | LYS | TYR | PHE | ||||
| 4 | LYS | LEU | ILE | ALA | ASN | ALA | LYS | THR | VAL | GLU | ||||
| 5 | GLY | VAL | TRP | THR | TYR | LYS | ASP | GLU | ILE | LYS | ||||
| 6 | THR | PHE | THR | VAL | THR | GLU |
Samples:
Gb95: Gb95, [U-100% 13C; U-100% 15N], 0.15-0.3 mM; potassium phosphate pH 7.2 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Gb95 | isotropic | sample_conditions_1 |
| 3D HNCACB | Gb95 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | Gb95 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | Gb95 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | Gb95 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | Gb95 | isotropic | sample_conditions_1 |
| 3D HNCO | Gb95 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | Gb95 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY(aliphatic) | Gb95 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY(aromatic) | Gb95 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
xwinnmr v2.5, Bruker Biospin - collection
NMRPipe vn/a, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3, Goddard - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts