BMRB Entry 15466
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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/BMR15466
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Title: STRUCTURE CHARACTERISATION OF PINA WW DOMAIN AND COMPARISON WITH OTHER GROUP IV WW DOMAINS, PIN1 AND ESS1 PubMed: 18503784
Deposition date: 2007-09-11 Original release date: 2008-06-25
Authors: Ng, C.; Kato, Y.; Tanokura, M.; Brownlee, R.
Citation: Ng, Chai; Kato, Yusuke; Tanokura, Masaru; Brownlee, Robert. "Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1" Biochim. Biophys. Acta 1784, 1208-1214 (2008).
Assembly members:
PEPTIDYL-PROLYL_CIS/TRANS_ISOMERASE, polymer, 54 residues, 6262.056 Da.
Natural source: Common Name: ASPERGILLUS NIDULANS Taxonomy ID: 162425 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: ASPERGILLUS NIDULANS
Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI
Entity Sequences (FASTA):
PEPTIDYL-PROLYL_CIS/TRANS_ISOMERASE: GSMVNTGLPAGWEVRHSNSK
NLPYYFNPATRESRWEPPAD
TDMETLKMYMATYH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 145 |
| 15N chemical shifts | 49 |
| 1H chemical shifts | 330 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PEPTIDYL-PROLYL CIS/TRANS ISOMERASE | 1 |
Entities:
Entity 1, PEPTIDYL-PROLYL CIS/TRANS ISOMERASE 54 residues - 6262.056 Da.
| 1 | GLY | SER | MET | VAL | ASN | THR | GLY | LEU | PRO | ALA | ||||
| 2 | GLY | TRP | GLU | VAL | ARG | HIS | SER | ASN | SER | LYS | ||||
| 3 | ASN | LEU | PRO | TYR | TYR | PHE | ASN | PRO | ALA | THR | ||||
| 4 | ARG | GLU | SER | ARG | TRP | GLU | PRO | PRO | ALA | ASP | ||||
| 5 | THR | ASP | MET | GLU | THR | LEU | LYS | MET | TYR | MET | ||||
| 6 | ALA | THR | TYR | HIS |
Samples:
sample_1: PEPTIDYL-PROLYL CIS/TRANS ISOMERASE, [U-100% 13C; U-100% 15N], 1.8 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 5.0; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C- SEPARATED_ NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_15N- SEPARATED_ NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH -COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3, Goddard - chemical shift assignment, data analysis, peak picking
VNMR, Varian - collection
TALOS, Cornilescu, Delaglio and Bax - Dihedral angle
AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - Energy minimisation, refinement
NMR spectrometers:
- VARIAN INOVA 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts