BMRB Entry 15466
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PDB ID: 2jv4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15466
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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).
PubMed: 18503784
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 Vector: PLYSS
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 |
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