BMRB Entry 19551
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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/BMR19551
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Title: 1H, 13C, and 15N Chemical Shift Assignments for human FK506 binding Protein 25 PubMed: 24414276
Deposition date: 2013-10-12 Original release date: 2014-02-12
Authors: Shin, Joon; Prakash, Ajit; Yoon, Ho Sup
Citation: Prakash, Ajit; Shin, Joon; Yoon, Ho Sup. "(1)H, (13)C and (15)N resonance assignments of human FK506 binding protein 25." Biomol. NMR Assignments ., .-. (2014).
Assembly members:
hFKBP25, polymer, 224 residues, Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
hFKBP25: MAAAVPQRAWTVEQLRSEQL
PKKDIIKFLQEHGSDSFLAE
HKLLGNIKNVAKTANKDHLV
TAYNHLFETKRFKGTESISK
VSEQVKNVKLNEDKPKETKS
EETLDEGPPKYTKSVLKKGD
KTNFPKKGDVVHCWYTGTLQ
DGTVFDTNIQTSAKKKKNAK
PLSFKVGVGKVIRGWDEALL
TMSKGEKARLEIEPEWAYGK
KGQPDAKIPPNAKLTFEVEL
VDID
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 945 |
| 15N chemical shifts | 229 |
| 1H chemical shifts | 1630 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hFKBP25 | 1 |
Entities:
Entity 1, hFKBP25 224 residues - Formula weight is not available
| 1 | MET | ALA | ALA | ALA | VAL | PRO | GLN | ARG | ALA | TRP | ||||
| 2 | THR | VAL | GLU | GLN | LEU | ARG | SER | GLU | GLN | LEU | ||||
| 3 | PRO | LYS | LYS | ASP | ILE | ILE | LYS | PHE | LEU | GLN | ||||
| 4 | GLU | HIS | GLY | SER | ASP | SER | PHE | LEU | ALA | GLU | ||||
| 5 | HIS | LYS | LEU | LEU | GLY | ASN | ILE | LYS | ASN | VAL | ||||
| 6 | ALA | LYS | THR | ALA | ASN | LYS | ASP | HIS | LEU | VAL | ||||
| 7 | THR | ALA | TYR | ASN | HIS | LEU | PHE | GLU | THR | LYS | ||||
| 8 | ARG | PHE | LYS | GLY | THR | GLU | SER | ILE | SER | LYS | ||||
| 9 | VAL | SER | GLU | GLN | VAL | LYS | ASN | VAL | LYS | LEU | ||||
| 10 | ASN | GLU | ASP | LYS | PRO | LYS | GLU | THR | LYS | SER | ||||
| 11 | GLU | GLU | THR | LEU | ASP | GLU | GLY | PRO | PRO | LYS | ||||
| 12 | TYR | THR | LYS | SER | VAL | LEU | LYS | LYS | GLY | ASP | ||||
| 13 | LYS | THR | ASN | PHE | PRO | LYS | LYS | GLY | ASP | VAL | ||||
| 14 | VAL | HIS | CYS | TRP | TYR | THR | GLY | THR | LEU | GLN | ||||
| 15 | ASP | GLY | THR | VAL | PHE | ASP | THR | ASN | ILE | GLN | ||||
| 16 | THR | SER | ALA | LYS | LYS | LYS | LYS | ASN | ALA | LYS | ||||
| 17 | PRO | LEU | SER | PHE | LYS | VAL | GLY | VAL | GLY | LYS | ||||
| 18 | VAL | ILE | ARG | GLY | TRP | ASP | GLU | ALA | LEU | LEU | ||||
| 19 | THR | MET | SER | LYS | GLY | GLU | LYS | ALA | ARG | LEU | ||||
| 20 | GLU | ILE | GLU | PRO | GLU | TRP | ALA | TYR | GLY | LYS | ||||
| 21 | LYS | GLY | GLN | PRO | ASP | ALA | LYS | ILE | PRO | PRO | ||||
| 22 | ASN | ALA | LYS | LEU | THR | PHE | GLU | VAL | GLU | LEU | ||||
| 23 | VAL | ASP | ILE | ASP |
Samples:
sample_1: human FK506 binding protein 25 (hFKBP25), [U-13C; U-15N], 0.5 mM; D2O, [U-100% 2H], 10%; H2O 90%; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 0.001%
sample_2: human FK506 binding protein 25 (hFKBP25), [U-15N], 0.5 mM; D2O, [U-100% 2H], 10%; H2O 90%; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 0.001%
sample_3: human FK506 binding protein 25 (hFKBP25), [U-13C], 0.5 mM; D2O, [U-100% 2H], 100%; sodium chloride 50 mM; sodium phosphate 20 mM; sodium phosphate 0.001%
sample_conditions_1: ionic strength: 70 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Related Database Links:
| PDB | |
| DBJ | BAD96713 BAE01700 BAE87176 BAG34856 BAI46571 |
| GB | AAA30348 AAA58471 AAA58475 AAH16288 AAH20809 |
| REF | NP_001033201 NP_001270679 NP_002004 XP_001096116 XP_002753901 |
| SP | P26884 Q00688 |
| TPG | DAA17319 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts