BMRB Entry 15537
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15537
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Title: Solution NMR structures of two designed proteins with 88% sequence identity but different fold and function PubMed: 18796611
Deposition date: 2007-10-25 Original release date: 2008-11-03
Authors: He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John
Citation: He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John. "NMR structures of two designed proteins with high sequence identity but different fold and function" Proc. Natl. Acad. Sci. U.S.A. 105, 14412-14417 (2008).
Assembly members:
Gb88, 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 Host organism: not applicable
Entity Sequences (FASTA):
Gb88: TTYKLILNLKQAKEEAIKEL
VDAATAEKYFKLYANAKTVE
GVWTYKDETKTFTVTE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 247 |
| 15N chemical shifts | 57 |
| 1H chemical shifts | 367 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Gb88 | 1 |
Entities:
Entity 1, Gb88 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 | LEU | ||||
| 3 | VAL | ASP | ALA | ALA | THR | ALA | GLU | LYS | TYR | PHE | ||||
| 4 | LYS | LEU | TYR | ALA | ASN | ALA | LYS | THR | VAL | GLU | ||||
| 5 | GLY | VAL | TRP | THR | TYR | LYS | ASP | GLU | THR | LYS | ||||
| 6 | THR | PHE | THR | VAL | THR | GLU |
Samples:
Gb88_sample: Gb88, [U-100% 13C; U-100% 15N], 0.2 – 0.4 mM; sodium phosphate 50 mM; sodium chloride 50 mM; H20 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Gb88_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | Gb88_sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | Gb88_sample | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | Gb88_sample | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | Gb88_sample | isotropic | sample_conditions_1 |
| 3D C(CO)NH | Gb88_sample | isotropic | sample_conditions_1 |
| 3D HNCO | Gb88_sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | Gb88_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY(aliphatic) | Gb88_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY(aromatic) | Gb88_sample | isotropic | sample_conditions_1 |
Software:
CNS v1.1, 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
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
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