BMRB Entry 18278
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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/BMR18278
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Title: Solution Structure of FKBP12 from Aedes aegypti PubMed: 22806993
Deposition date: 2012-02-20 Original release date: 2013-02-05
Authors: Chakraborty, Goutam; Shin, Joon
Citation: Chakraborty, Goutam; Shin, Joon; Nguyen, Q.; Harikishore, A.; Baek, K.; Yoon, H.. "Solution structure of FK506-binding protein 12 from Aedes aegypti" Proteins 80, 2476-2481 (2012).
Assembly members:
FKBP12, polymer, 108 residues, 11553.165 Da.
Natural source: Common Name: flies Taxonomy ID: 7159 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Aedes aegypti
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FKBP12: MGVQVVTLAAGDEATYPKAG
QVAVVHYTGTLADGKVFDSS
RTRGKPFRFTVGRGEVIRGW
DEGVAQMSVGQRAKLVCSPD
YAYGSRGHPGVIPPNATLTF
DVELLRVE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 423 |
| 15N chemical shifts | 104 |
| 1H chemical shifts | 715 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FKBP12 from Aedes aegypti | 1 |
Entities:
Entity 1, FKBP12 from Aedes aegypti 108 residues - 11553.165 Da.
| 1 | MET | GLY | VAL | GLN | VAL | VAL | THR | LEU | ALA | ALA | ||||
| 2 | GLY | ASP | GLU | ALA | THR | TYR | PRO | LYS | ALA | GLY | ||||
| 3 | GLN | VAL | ALA | VAL | VAL | HIS | TYR | THR | GLY | THR | ||||
| 4 | LEU | ALA | ASP | GLY | LYS | VAL | PHE | ASP | SER | SER | ||||
| 5 | ARG | THR | ARG | GLY | LYS | PRO | PHE | ARG | PHE | THR | ||||
| 6 | VAL | GLY | ARG | GLY | GLU | VAL | ILE | ARG | GLY | TRP | ||||
| 7 | ASP | GLU | GLY | VAL | ALA | GLN | MET | SER | VAL | GLY | ||||
| 8 | GLN | ARG | ALA | LYS | LEU | VAL | CYS | SER | PRO | ASP | ||||
| 9 | TYR | ALA | TYR | GLY | SER | ARG | GLY | HIS | PRO | GLY | ||||
| 10 | VAL | ILE | PRO | PRO | ASN | ALA | THR | LEU | THR | PHE | ||||
| 11 | ASP | VAL | GLU | LEU | LEU | ARG | VAL | GLU |
Samples:
sample_1: FKBP12, [U-15N], 0.5 mM; H2O 90%; D2O 10%
sample_2: FKBP12, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%
sample_3: FKBP12, [U-100% 13C; U-100% 15N], 0.5 mM; D2O 100%
sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
Molmol, Koradi, Billeter and Wuthrich - Structure Visualization
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| GB | ABF18244 EAT40395 EJY57709 EJY57710 |
| REF | XP_001652969 XP_011493401 XP_011493402 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts