BMRB Entry 17818
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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/BMR17818
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Title: Solution NMR structure of a FKBP-type peptidyl-prolyl cis-trans isomerase from Giardia lamblia. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target GilaA.00840.a PubMed: 24293257
Deposition date: 2011-07-29 Original release date: 2011-08-17
Authors: Buchko, Garry
Citation: Buchko, Garry; Hewitt, Stephen; Van Voorhis, Wesley; Myler, Peter. "Solution structure of a putative FKBP-type peptidyl-propyl cis-trans isomerase from Giardia lamblia." J. Biomol. NMR 57, 369-374 (2013).
Assembly members:
FKBP, polymer, 130 residues, 14160.289 Da.
Natural source: Common Name: Giardia lamblia Taxonomy ID: 184922 Superkingdom: Eukaryota Kingdom: not available Genus/species: Giardia lamblia
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FKBP: MAHHHHHHMGTLEAQTQGPG
SMSAQLEKKVLTPGDGVTKP
QAGKKVTVHYDGRFPDGKQF
DSSRSRGKPFQFTLGAGEVI
KGWDQGVATMTLGEKALFTI
PYQLAYGERGYPPVIPPKAT
LVFEVELLAV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 378 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 726 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FKBP | 1 |
Entities:
Entity 1, FKBP 130 residues - 14160.289 Da.
The first 21 residues are a tag for protein isolation (MAHHHHHHMGTLEAQTQGPGS). The first native residue is M22.
| 1 | MET | ALA | HIS | HIS | HIS | HIS | HIS | HIS | MET | GLY | |
| 2 | THR | LEU | GLU | ALA | GLN | THR | GLN | GLY | PRO | GLY | |
| 3 | SER | MET | SER | ALA | GLN | LEU | GLU | LYS | LYS | VAL | |
| 4 | LEU | THR | PRO | GLY | ASP | GLY | VAL | THR | LYS | PRO | |
| 5 | GLN | ALA | GLY | LYS | LYS | VAL | THR | VAL | HIS | TYR | |
| 6 | ASP | GLY | ARG | PHE | PRO | ASP | GLY | LYS | GLN | PHE | |
| 7 | ASP | SER | SER | ARG | SER | ARG | GLY | LYS | PRO | PHE | |
| 8 | GLN | PHE | THR | LEU | GLY | ALA | GLY | GLU | VAL | ILE | |
| 9 | LYS | GLY | TRP | ASP | GLN | GLY | VAL | ALA | THR | MET | |
| 10 | THR | LEU | GLY | GLU | LYS | ALA | LEU | PHE | THR | ILE | |
| 11 | PRO | TYR | GLN | LEU | ALA | TYR | GLY | GLU | ARG | GLY | |
| 12 | TYR | PRO | PRO | VAL | ILE | PRO | PRO | LYS | ALA | THR | |
| 13 | LEU | VAL | PHE | GLU | VAL | GLU | LEU | LEU | ALA | VAL |
Samples:
sample_1: FKBP, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium chloride 100 mM; TRIS 20 mM; DTT 1 mM; D2O 7%; H2O 93%
sample_2: FKBP, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium chloride 100 mM; TRIS 20 mM; DTT 1 mM; D2O 100%
sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 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 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| deuterium exchange | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCDHD | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
FELIX v2007, Accelrys Software Inc. - processing
SPARKY v3.115, Goddard - data analysis
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS, Bhattacharya and Montelione - data analysis
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts