BMRB Entry 17918
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17918
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Sun, Lifang; Wu, Xueji; Peng, Yu; Goh, Jian-Yuan; Liou, Yih-Cherng; Lin, Donghai; Zhao, Yufen. "Solution Structural Analysis of the Single-Domain Parvulin TbPin1" PLoS One 7, e43017-e43017 (2012).
PubMed: 22900083
Assembly members:
Prolyl_Cis/trans_Isomerase_TbPIN1, polymer, 115 residues, 12515.130 Da.
Natural source: Common Name: Trypanosoma brucei Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
Entity Sequences (FASTA):
Prolyl_Cis/trans_Isomerase_TbPIN1: MSEKLRAAHLLVKFSGSRNP
VSRRTGDSTADVTYEDAIKE
LQKWSQRIASGEVSFEEAAS
QRSDCGSYASGGDLGFFSSG
EMMKPFEDAVRALKIGDISP
IVQTDSGLHIIKRLA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 456 |
| 15N chemical shifts | 122 |
| 1H chemical shifts | 801 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TbPIN1 | 1 |
Entities:
Entity 1, TbPIN1 115 residues - 12515.130 Da.
| 1 | MET | SER | GLU | LYS | LEU | ARG | ALA | ALA | HIS | LEU | ||||
| 2 | LEU | VAL | LYS | PHE | SER | GLY | SER | ARG | ASN | PRO | ||||
| 3 | VAL | SER | ARG | ARG | THR | GLY | ASP | SER | THR | ALA | ||||
| 4 | ASP | VAL | THR | TYR | GLU | ASP | ALA | ILE | LYS | GLU | ||||
| 5 | LEU | GLN | LYS | TRP | SER | GLN | ARG | ILE | ALA | SER | ||||
| 6 | GLY | GLU | VAL | SER | PHE | GLU | GLU | ALA | ALA | SER | ||||
| 7 | GLN | ARG | SER | ASP | CYS | GLY | SER | TYR | ALA | SER | ||||
| 8 | GLY | GLY | ASP | LEU | GLY | PHE | PHE | SER | SER | GLY | ||||
| 9 | GLU | MET | MET | LYS | PRO | PHE | GLU | ASP | ALA | VAL | ||||
| 10 | ARG | ALA | LEU | LYS | ILE | GLY | ASP | ILE | SER | PRO | ||||
| 11 | ILE | VAL | GLN | THR | ASP | SER | GLY | LEU | HIS | ILE | ||||
| 12 | ILE | LYS | ARG | LEU | ALA |
Samples:
sample_1: Prolyl Cis/trans Isomerase TbPIN1, [U-99% 13C; U-99% 15N], 0.8 – 1.0 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 101325 Pa; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks