BMRB Entry 17005
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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/BMR17005
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Title: Three-dimensional structure of a truncated phosphoribosylanthranilate isomerase (residues 255-384) from Escherichia coli PubMed: 21354426
Deposition date: 2010-06-17 Original release date: 2011-05-31
Authors: Setiyaputra, Surya; Mackay, Joel; Patrick, Wayne
Citation: Setiyaputra, Surya; Mackay, Joel; Patrick, Wayne. "The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the ()8 barrel fold." J. Mol. Biol. 408, 291-303 (2011).
Assembly members:
trPRAI, polymer, 134 residues, 14308.270 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):
trPRAI: MGENKVCGLTRGQDAKAAYD
AGAIYGGLIFVATSPRCVNV
EQAQEVMAAAPLQYVGVFRN
HDIADVVDKAKVLSLAAVQL
HGNEEQLYIDTLREALPAHV
AIWKALSVGETLPAREFQHV
DKYVLDNGQGGAGS
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 503 |
| 15N chemical shifts | 137 |
| 1H chemical shifts | 842 |
| coupling constants | 74 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | trPRAI | 1 |
Entities:
Entity 1, trPRAI 134 residues - 14308.270 Da.
Residue 132-134 are cloning artifacts from the plasmid display selection and not part of the original sequence of PRAI from E.coli
| 1 | MET | GLY | GLU | ASN | LYS | VAL | CYS | GLY | LEU | THR | ||||
| 2 | ARG | GLY | GLN | ASP | ALA | LYS | ALA | ALA | TYR | ASP | ||||
| 3 | ALA | GLY | ALA | ILE | TYR | GLY | GLY | LEU | ILE | PHE | ||||
| 4 | VAL | ALA | THR | SER | PRO | ARG | CYS | VAL | ASN | VAL | ||||
| 5 | GLU | GLN | ALA | GLN | GLU | VAL | MET | ALA | ALA | ALA | ||||
| 6 | PRO | LEU | GLN | TYR | VAL | GLY | VAL | PHE | ARG | ASN | ||||
| 7 | HIS | ASP | ILE | ALA | ASP | VAL | VAL | ASP | LYS | ALA | ||||
| 8 | LYS | VAL | LEU | SER | LEU | ALA | ALA | VAL | GLN | LEU | ||||
| 9 | HIS | GLY | ASN | GLU | GLU | GLN | LEU | TYR | ILE | ASP | ||||
| 10 | THR | LEU | ARG | GLU | ALA | LEU | PRO | ALA | HIS | VAL | ||||
| 11 | ALA | ILE | TRP | LYS | ALA | LEU | SER | VAL | GLY | GLU | ||||
| 12 | THR | LEU | PRO | ALA | ARG | GLU | PHE | GLN | HIS | VAL | ||||
| 13 | ASP | LYS | TYR | VAL | LEU | ASP | ASN | GLY | GLN | GLY | ||||
| 14 | GLY | ALA | GLY | SER |
Samples:
sample_1: trPRAI 0.8 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%
sample_2: trPRAI, [U-99% 15N], .6 – 1 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%
sample_3: trPRAI, [U-98% 13C; U-98% 15N], .6 – .8 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%
sample_4: trPRAI, [U-98% 13C; U-98% 15N], 0.7 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; D2O 100%
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_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_4 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY AROMATIC | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - automated NOE peak assignments, NOE peaks calibration
TOPSPIN v2.1, Bruker Biospin - collection, processing
SPARKY v3.113, Goddard - chemical shift assignment, peak picking
TALOS vTALOS+, Cornilescu, Delaglio and Bax - prediction of protein backbone torsion angles from NMR chemical shifts
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution, water refinement
ProcheckNMR v3.5.3, Laskowski and MacArthur - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA14794 BAG66423 BAG76835 BAI25111 BAI30254 |
| EMBL | CAA23664 CAQ31763 CAQ98141 CAU97277 CBJ00867 |
| GB | AAA57299 AAA65138 AAA65144 AAA65150 AAA65156 |
| REF | NP_415778 NP_707171 WP_000983871 WP_000983893 WP_001195309 |
| SP | P00909 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts