BMRB Entry 16491
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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/BMR16491
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Zheng, Suxin; Leeper, Thomas; Varani, Gabriele. "Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with Cycloheximide-N-ethylethanoate" To be Published ., .-..
Assembly members:
entity_1, polymer, 117 residues, 12239.810 Da.
JZF, non-polymer, 367.437 Da.
Natural source: Common Name: Burkholderia pseudomallei Taxonomy ID: 28450 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia pseudomallei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: RIL
Entity Sequences (FASTA):
entity_1: GPGSMTVVTTESGLKYEDLT
EGSGAEARAGQTVSVHYTGW
LTDGQKFDSSKDRNDPFAFV
LGGGMVIKGWDEGVQGMKVG
GVRRLTIPPQLGYGARGAGG
VIPPNATLVFEVELLDV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 325 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 788 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | peptidyl-prolyl cis-trans isomerase | 1 |
| 2 | Cycloheximide-N-ethylethanoate | 2 |
Entities:
Entity 1, peptidyl-prolyl cis-trans isomerase 117 residues - 12239.810 Da.
| 1 | GLY | PRO | GLY | SER | MET | THR | VAL | VAL | THR | THR | ||||
| 2 | GLU | SER | GLY | LEU | LYS | TYR | GLU | ASP | LEU | THR | ||||
| 3 | GLU | GLY | SER | GLY | ALA | GLU | ALA | ARG | ALA | GLY | ||||
| 4 | GLN | THR | VAL | SER | VAL | HIS | TYR | THR | GLY | TRP | ||||
| 5 | LEU | THR | ASP | GLY | GLN | LYS | PHE | ASP | SER | SER | ||||
| 6 | LYS | ASP | ARG | ASN | ASP | PRO | PHE | ALA | PHE | VAL | ||||
| 7 | LEU | GLY | GLY | GLY | MET | VAL | ILE | LYS | GLY | TRP | ||||
| 8 | ASP | GLU | GLY | VAL | GLN | GLY | MET | LYS | VAL | GLY | ||||
| 9 | GLY | VAL | ARG | ARG | LEU | THR | ILE | PRO | PRO | GLN | ||||
| 10 | LEU | GLY | TYR | GLY | ALA | ARG | GLY | ALA | GLY | GLY | ||||
| 11 | VAL | ILE | PRO | PRO | ASN | ALA | THR | LEU | VAL | PHE | ||||
| 12 | GLU | VAL | GLU | LEU | LEU | ASP | VAL |
Entity 2, Cycloheximide-N-ethylethanoate - C19 H29 N O6 - 367.437 Da.
| 1 | JZF |
Samples:
sample_2: entity_1, [U-100% 15N], 0.6~1.2 mM
sample_3: entity_1, [U-100% 13C; U-100% 15N], 0.6~1.2 mM
sample_4: entity_1, [U-100% 15N], 0.6~1.2 mM
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.6~1.2 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ANALYSIS, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 16406 17151 |
| PDB | |
| EMBL | CAH39299 CDU31864 CFB51428 CFD89802 CFD92609 |
| GB | ABA51599 ABC34056 ABN85861 ABN94560 AFI70186 |
| REF | WP_004525093 WP_004537279 WP_009895623 WP_010110204 WP_010120234 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks