BMRB Entry 16211
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16211
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Title: Solution structure of putative prolyl isomerase PpiD from E.Coli PubMed: 19866485
Deposition date: 2009-03-12 Original release date: 2009-11-05
Authors: Weininger, Ulrich; Jakob, Roman
Citation: Weininger, Ulrich; Jakob, Roman; Kovermann, Michael; Balbach, Jochen; Schmid, Franz. "The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity." Protein Sci. 19, 6-18 (2010).
Assembly members:
prolyl isomerase domain, polymer, 102 residues, 11173.603 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
prolyl isomerase domain: TQPQRTRYSIIQTKTEDEAK
AVLDELNKGGDFAALAKEKS
ADIISARNGGDMGWLEDATI
PDELKNAGLKEKGQLSGVIK
SSVGFLIVRLDDIQAAHHHH
HH
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 690 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | prolyl isomerase domain | 1 |
Entities:
Entity 1, prolyl isomerase domain 102 residues - 11173.603 Da.
| 1 | THR | GLN | PRO | GLN | ARG | THR | ARG | TYR | SER | ILE | ||||
| 2 | ILE | GLN | THR | LYS | THR | GLU | ASP | GLU | ALA | LYS | ||||
| 3 | ALA | VAL | LEU | ASP | GLU | LEU | ASN | LYS | GLY | GLY | ||||
| 4 | ASP | PHE | ALA | ALA | LEU | ALA | LYS | GLU | LYS | SER | ||||
| 5 | ALA | ASP | ILE | ILE | SER | ALA | ARG | ASN | GLY | GLY | ||||
| 6 | ASP | MET | GLY | TRP | LEU | GLU | ASP | ALA | THR | ILE | ||||
| 7 | PRO | ASP | GLU | LEU | LYS | ASN | ALA | GLY | LEU | LYS | ||||
| 8 | GLU | LYS | GLY | GLN | LEU | SER | GLY | VAL | ILE | LYS | ||||
| 9 | SER | SER | VAL | GLY | PHE | LEU | ILE | VAL | ARG | LEU | ||||
| 10 | ASP | ASP | ILE | GLN | ALA | ALA | HIS | HIS | HIS | HIS | ||||
| 11 | HIS | HIS |
Samples:
sample_1: potassium phosphate 100 mM; entity, [U-15N], 5 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.0, Linge, O, . - chemical shift assignment, structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA11645 BAB33918 BAE76221 BAG75991 BAI23815 |
| EMBL | CAP74975 CAQ30914 CAQ97317 CAR01785 CAR06675 |
| GB | AAB40197 AAC73544 AAG54791 AAN42042 AAN79035 |
| REF | NP_308522 NP_414975 NP_706335 WP_000969091 WP_000969347 |
| SP | P0ADY1 P0ADY2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
or all simulated shifts