BMRB Entry 17713
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17713
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Title: Fpr4p PPIase domain PubMed: 21898050
Deposition date: 2011-06-16 Original release date: 2011-09-13
Authors: Monneau, Yoan; Mackereth, Cameron
Citation: Monneau, Yoan; Nelson, Christopher; Mackereth, Cameron. "Chemical shift assignments of the catalytic domain from the yeast proline isomerase Fpr4p." Biomol. NMR Assignments 6, 123-126 (2012).
Assembly members:
Fpr4p, polymer, 117 residues, Formula weight is not available
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Fpr4p: GAMAKPKTKLLEGGIIIEDR
VTGKGPHAKKGTRVGMRYVG
KLKNGKVFDKNTKGKPFVFK
LGQGEVIKGWDIGVAGMAVG
GERRIVIPAPYAYGKQALPG
IPANSELTFDVKLVSMK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 532 |
| 15N chemical shifts | 120 |
| 1H chemical shifts | 859 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Fpr4p(280-392) | 1 |
Entities:
Entity 1, Fpr4p(280-392) 117 residues - Formula weight is not available
Contains N-terminal Gly-Ala-Met-Ala- residues following cleavage of the His6-tag by TEV protease
| 1 | GLY | ALA | MET | ALA | LYS | PRO | LYS | THR | LYS | LEU | ||||
| 2 | LEU | GLU | GLY | GLY | ILE | ILE | ILE | GLU | ASP | ARG | ||||
| 3 | VAL | THR | GLY | LYS | GLY | PRO | HIS | ALA | LYS | LYS | ||||
| 4 | GLY | THR | ARG | VAL | GLY | MET | ARG | TYR | VAL | GLY | ||||
| 5 | LYS | LEU | LYS | ASN | GLY | LYS | VAL | PHE | ASP | LYS | ||||
| 6 | ASN | THR | LYS | GLY | LYS | PRO | PHE | VAL | PHE | LYS | ||||
| 7 | LEU | GLY | GLN | GLY | GLU | VAL | ILE | LYS | GLY | TRP | ||||
| 8 | ASP | ILE | GLY | VAL | ALA | GLY | MET | ALA | VAL | GLY | ||||
| 9 | GLY | GLU | ARG | ARG | ILE | VAL | ILE | PRO | ALA | PRO | ||||
| 10 | TYR | ALA | TYR | GLY | LYS | GLN | ALA | LEU | PRO | GLY | ||||
| 11 | ILE | PRO | ALA | ASN | SER | GLU | LEU | THR | PHE | ASP | ||||
| 12 | VAL | LYS | LEU | VAL | SER | MET | LYS |
Samples:
sample_1: Fpr4p, [U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
sample_2: Fpr4p, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
sample_3: Fpr4p, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
sample_4: Fpr4p, [U-10% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 292 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 HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D HBHD | sample_3 | isotropic | sample_conditions_1 |
| 2D HBHE | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQCCT | sample_4 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_4 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
Related Database Links:
| PDB | |
| DBJ | GAA25303 |
| EMBL | CAY81672 |
| GB | AAB67528 AHY78796 AJP40573 AJV46477 AJV46929 |
| REF | NP_013554 |
| SP | Q06205 |
| TPG | DAA09749 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts