BMRB Entry 25439
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PDB ID: 2my1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25439
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: van Roon, Anne-Marie; Yang, Ji-Chun; Mathieu, Daniel; Bermel, Wolfgang; Nagai, Kiyoshi; Neuhaus, David. "113 Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p" Angew. Chem. Int. Ed. Engl. 54, 4861-4864 (2015).
PubMed: 25703931
Assembly members:
Bud31p_polypeptide, polymer, 159 residues, 18554.609 Da.
ZINC ION, non-polymer, 65.409 Da.
Natural source: Common Name: Baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRK172
Entity Sequences (FASTA):
Bud31p_polypeptide: GGSPRIKTRRSKPAPDGFEK
IKPTLTDFEIQLRDAQKDKS
SKLAAKSNEQLWEIMQLHHQ
RSRYIYTLYYKRKAISKDLY
DWLIKEKYADKLLIAKWRKT
GYEKLCCLRCIQKNETNNGS
TCICRVPRAQLEEEARKKGT
QVSFHQCVHCGCRGCASTD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 509 |
| 15N chemical shifts | 167 |
| 1H chemical shifts | 1022 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Bud31p polypeptide | 1 |
| 2 | ZN1 | 2 |
| 3 | ZN2 | 2 |
| 4 | ZN3 | 2 |
Entities:
Entity 1, Bud31p polypeptide 159 residues - 18554.609 Da.
| 1 | GLY | GLY | SER | PRO | ARG | ILE | LYS | THR | ARG | ARG | ||||
| 2 | SER | LYS | PRO | ALA | PRO | ASP | GLY | PHE | GLU | LYS | ||||
| 3 | ILE | LYS | PRO | THR | LEU | THR | ASP | PHE | GLU | ILE | ||||
| 4 | GLN | LEU | ARG | ASP | ALA | GLN | LYS | ASP | LYS | SER | ||||
| 5 | SER | LYS | LEU | ALA | ALA | LYS | SER | ASN | GLU | GLN | ||||
| 6 | LEU | TRP | GLU | ILE | MET | GLN | LEU | HIS | HIS | GLN | ||||
| 7 | ARG | SER | ARG | TYR | ILE | TYR | THR | LEU | TYR | TYR | ||||
| 8 | LYS | ARG | LYS | ALA | ILE | SER | LYS | ASP | LEU | TYR | ||||
| 9 | ASP | TRP | LEU | ILE | LYS | GLU | LYS | TYR | ALA | ASP | ||||
| 10 | LYS | LEU | LEU | ILE | ALA | LYS | TRP | ARG | LYS | THR | ||||
| 11 | GLY | TYR | GLU | LYS | LEU | CYS | CYS | LEU | ARG | CYS | ||||
| 12 | ILE | GLN | LYS | ASN | GLU | THR | ASN | ASN | GLY | SER | ||||
| 13 | THR | CYS | ILE | CYS | ARG | VAL | PRO | ARG | ALA | GLN | ||||
| 14 | LEU | GLU | GLU | GLU | ALA | ARG | LYS | LYS | GLY | THR | ||||
| 15 | GLN | VAL | SER | PHE | HIS | GLN | CYS | VAL | HIS | CYS | ||||
| 16 | GLY | CYS | ARG | GLY | CYS | ALA | SER | THR | ASP |
Entity 2, ZN1 - Zn - 65.409 Da.
| 1 | ZN |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks