BMRB Entry 18044
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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/BMR18044
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Title: Computational design of an eight-stranded (beta/alpha)-barrel from fragments of different folds PubMed: 22329686
Deposition date: 2011-11-07 Original release date: 2012-03-19
Authors: Coles, Murray; Truffault, Vincent; Eisenbeis, Simone; Proffitt, William; Meiler, Jens; Hocker, Birte
Citation: Eisenbeis, Simone; Proffitt, William; Coles, Murray; Truffault, Vincent; Shanmugarantam, Sooruban; Meiler, Jens; Hocker, Birte. "Potential of fragment recombination for rational design of proteins" J. Am. Chem. Soc. 134, 4019-4022 (2012).
Assembly members:
CheYHisF-sfr_RM, polymer, 234 residues, 25607.779 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: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CheYHisF-sfr_RM: MGKIVLIVDDATNGREAVEK
YKELKPDIVTMDITMPEMNG
IDAIKEIMKIDPNAKIIVCS
AMGQQAMVIEAIKAGAKGFI
VNTAAVENPSLITQLAQTFG
SQAVVVAIDAKRVDGEFMVF
TYSGKKNTGILLRDWVVEVE
KRGAGEILLTSIDRDGTKSG
YDTEMIRFVRPLTTLPIIAS
GGAGKMEHFLEAFLAGADAA
AAASVFHFREIDGRELKEYL
KKHGVNLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 904 |
| 15N chemical shifts | 217 |
| 1H chemical shifts | 1578 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CheYHisF-sfr_RM | 1 |
Entities:
Entity 1, CheYHisF-sfr_RM 234 residues - 25607.779 Da.
The protein is an engineered chimera between CheY (1-11 and 34-103 from 1TMY) and HisF (103-247 from 1THF) from Thermotoga maritima with five point mutations (R4I, D78G, I95L, L201A, V213G). The last 7 residues represent a purification tag.
| 1 | MET | GLY | LYS | ILE | VAL | LEU | ILE | VAL | ASP | ASP | ||||
| 2 | ALA | THR | ASN | GLY | ARG | GLU | ALA | VAL | GLU | LYS | ||||
| 3 | TYR | LYS | GLU | LEU | LYS | PRO | ASP | ILE | VAL | THR | ||||
| 4 | MET | ASP | ILE | THR | MET | PRO | GLU | MET | ASN | GLY | ||||
| 5 | ILE | ASP | ALA | ILE | LYS | GLU | ILE | MET | LYS | ILE | ||||
| 6 | ASP | PRO | ASN | ALA | LYS | ILE | ILE | VAL | CYS | SER | ||||
| 7 | ALA | MET | GLY | GLN | GLN | ALA | MET | VAL | ILE | GLU | ||||
| 8 | ALA | ILE | LYS | ALA | GLY | ALA | LYS | GLY | PHE | ILE | ||||
| 9 | VAL | ASN | THR | ALA | ALA | VAL | GLU | ASN | PRO | SER | ||||
| 10 | LEU | ILE | THR | GLN | LEU | ALA | GLN | THR | PHE | GLY | ||||
| 11 | SER | GLN | ALA | VAL | VAL | VAL | ALA | ILE | ASP | ALA | ||||
| 12 | LYS | ARG | VAL | ASP | GLY | GLU | PHE | MET | VAL | PHE | ||||
| 13 | THR | TYR | SER | GLY | LYS | LYS | ASN | THR | GLY | ILE | ||||
| 14 | LEU | LEU | ARG | ASP | TRP | VAL | VAL | GLU | VAL | GLU | ||||
| 15 | LYS | ARG | GLY | ALA | GLY | GLU | ILE | LEU | LEU | THR | ||||
| 16 | SER | ILE | ASP | ARG | ASP | GLY | THR | LYS | SER | GLY | ||||
| 17 | TYR | ASP | THR | GLU | MET | ILE | ARG | PHE | VAL | ARG | ||||
| 18 | PRO | LEU | THR | THR | LEU | PRO | ILE | ILE | ALA | SER | ||||
| 19 | GLY | GLY | ALA | GLY | LYS | MET | GLU | HIS | PHE | LEU | ||||
| 20 | GLU | ALA | PHE | LEU | ALA | GLY | ALA | ASP | ALA | ALA | ||||
| 21 | ALA | ALA | ALA | SER | VAL | PHE | HIS | PHE | ARG | GLU | ||||
| 22 | ILE | ASP | GLY | ARG | GLU | LEU | LYS | GLU | TYR | LEU | ||||
| 23 | LYS | LYS | HIS | GLY | VAL | ASN | LEU | GLU | HIS | HIS | ||||
| 24 | HIS | HIS | HIS | HIS |
Samples:
15N-labelled: CheYHisF-sfr_RM, [U-100% 15N], 0.5 mM; potassium phosphate 50 mM; potassium chloride 300 mM; H2O 90%; D2O 10%
double-labelled: CheYHisF-sfr_RM, [U-100% 13C; U-100% 15N], 0.5 mM; potassium phosphate 50 mM; potassium chloride 300 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 350 mM; pH: 7.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | double-labelled | isotropic | sample_conditions_1 |
| 3D HNCA | double-labelled | isotropic | sample_conditions_1 |
| 3D HNCACB | double-labelled | isotropic | sample_conditions_1 |
| 3D C(CO)NH | double-labelled | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | double-labelled | isotropic | sample_conditions_1 |
| 3D CCH-COSY | double-labelled | isotropic | sample_conditions_1 |
| 2D PLUSH-TACSY | double-labelled | isotropic | sample_conditions_1 |
| 3D HNHA | 15N-labelled | isotropic | sample_conditions_1 |
| 3D HNHB | 15N-labelled | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 15N-labelled | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | double-labelled | isotropic | sample_conditions_1 |
| 3D CNH-NOESY | double-labelled | isotropic | sample_conditions_1 |
| 3D CCH-NOESY | double-labelled | isotropic | sample_conditions_1 |
| 3D NNH-NOESY | 15N-labelled | isotropic | sample_conditions_1 |
| 2D 15N-filtered 1H-1H NOESY | 15N-labelled | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis
X-PLOR NIH v2.21, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 800 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts