BMRB Entry 25709
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25709
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Kumar, Atul; Aguirre, Jacob; Condos, Tara; Martinez-Torres, R. Julio; Chaugule, Viduth; Toth, Rachel; Sundaramoorthy, Ramasubramanian; Mercier, Pascal; Knebel, Axel; Spratt, Donald; Barber, Kathryn; Shaw, Gary; Walden, Helen. "Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis" EMBO J. 34, 2506-2521 (2015).
PubMed: 26254304
Assembly members:
Ub_S65E, polymer, 79 residues, Formula weight is not available
Parkin_R0RBR_(141-465), polymer, 325 residues, Formula weight is not available
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: pet28a
Entity Sequences (FASTA):
Ub_S65E: SNAMQIFVKTLTGKTITLEV
ESSDTIDNVKSKIQDKEGIP
PDQQRLIFAGKQLEDGRTLS
DYNIQKEETLHLVLRLRGG
Parkin_R0RBR_(141-465): SIYNSFYVYCKGPCQRVQPG
KLRVQCSTCRQATLTLTQGP
SCWDDVLIPNRMSGECQSPH
CPGTSAEFFFKCGAHPTSDK
ETSVALHLIATNSRNITCIT
CTDVRSPVLVFQCNSRHVIC
LDCFHLYCVTRLNDRQFVHD
PQLGYSLPCVAGCPNSLIKE
LHHFRILGEEQYNRYQQYGA
EECVLQMGGVLCPRPGCGAG
LLPEPDQRKVTCEGGNGLGC
GFAFCRECKEAYHEGECSAV
FEASGTTTQAYRVDERAAEQ
ARWEAASKETIKKTTKPCPR
CHVPVEKNGGCMHMKCPQPQ
CRLEWCWNCGCEWNRVCMGD
HWFDV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 38 |
| 1H chemical shifts | 114 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ub S65E | 1 |
| 2 | parkin R0RBR | 2 |
| 3 | ZINC ION 1 | 3 |
| 4 | ZINC ION 2 | 3 |
| 5 | ZINC ION 3 | 3 |
| 6 | ZINC ION 4 | 3 |
| 7 | ZINC ION 5 | 3 |
| 8 | ZINC ION 6 | 3 |
| 9 | ZINC ION 7 | 3 |
| 10 | ZINC ION 8 | 3 |
Entities:
Entity 1, Ub S65E 79 residues - Formula weight is not available
| 1 | SER | ASN | ALA | MET | GLN | ILE | PHE | VAL | LYS | THR | ||||
| 2 | LEU | THR | GLY | LYS | THR | ILE | THR | LEU | GLU | VAL | ||||
| 3 | GLU | SER | SER | ASP | THR | ILE | ASP | ASN | VAL | LYS | ||||
| 4 | SER | LYS | ILE | GLN | ASP | LYS | GLU | GLY | ILE | PRO | ||||
| 5 | PRO | ASP | GLN | GLN | ARG | LEU | ILE | PHE | ALA | GLY | ||||
| 6 | LYS | GLN | LEU | GLU | ASP | GLY | ARG | THR | LEU | SER | ||||
| 7 | ASP | TYR | ASN | ILE | GLN | LYS | GLU | GLU | THR | LEU | ||||
| 8 | HIS | LEU | VAL | LEU | ARG | LEU | ARG | GLY | GLY |
Entity 2, parkin R0RBR 325 residues - Formula weight is not available
| 1 | SER | ILE | TYR | ASN | SER | PHE | TYR | VAL | TYR | CYS | ||||
| 2 | LYS | GLY | PRO | CYS | GLN | ARG | VAL | GLN | PRO | GLY | ||||
| 3 | LYS | LEU | ARG | VAL | GLN | CYS | SER | THR | CYS | ARG | ||||
| 4 | GLN | ALA | THR | LEU | THR | LEU | THR | GLN | GLY | PRO | ||||
| 5 | SER | CYS | TRP | ASP | ASP | VAL | LEU | ILE | PRO | ASN | ||||
| 6 | ARG | MET | SER | GLY | GLU | CYS | GLN | SER | PRO | HIS | ||||
| 7 | CYS | PRO | GLY | THR | SER | ALA | GLU | PHE | PHE | PHE | ||||
| 8 | LYS | CYS | GLY | ALA | HIS | PRO | THR | SER | ASP | LYS | ||||
| 9 | GLU | THR | SER | VAL | ALA | LEU | HIS | LEU | ILE | ALA | ||||
| 10 | THR | ASN | SER | ARG | ASN | ILE | THR | CYS | ILE | THR | ||||
| 11 | CYS | THR | ASP | VAL | ARG | SER | PRO | VAL | LEU | VAL | ||||
| 12 | PHE | GLN | CYS | ASN | SER | ARG | HIS | VAL | ILE | CYS | ||||
| 13 | LEU | ASP | CYS | PHE | HIS | LEU | TYR | CYS | VAL | THR | ||||
| 14 | ARG | LEU | ASN | ASP | ARG | GLN | PHE | VAL | HIS | ASP | ||||
| 15 | PRO | GLN | LEU | GLY | TYR | SER | LEU | PRO | CYS | VAL | ||||
| 16 | ALA | GLY | CYS | PRO | ASN | SER | LEU | ILE | LYS | GLU | ||||
| 17 | LEU | HIS | HIS | PHE | ARG | ILE | LEU | GLY | GLU | GLU | ||||
| 18 | GLN | TYR | ASN | ARG | TYR | GLN | GLN | TYR | GLY | ALA | ||||
| 19 | GLU | GLU | CYS | VAL | LEU | GLN | MET | GLY | GLY | VAL | ||||
| 20 | LEU | CYS | PRO | ARG | PRO | GLY | CYS | GLY | ALA | GLY | ||||
| 21 | LEU | LEU | PRO | GLU | PRO | ASP | GLN | ARG | LYS | VAL | ||||
| 22 | THR | CYS | GLU | GLY | GLY | ASN | GLY | LEU | GLY | CYS | ||||
| 23 | GLY | PHE | ALA | PHE | CYS | ARG | GLU | CYS | LYS | GLU | ||||
| 24 | ALA | TYR | HIS | GLU | GLY | GLU | CYS | SER | ALA | VAL | ||||
| 25 | PHE | GLU | ALA | SER | GLY | THR | THR | THR | GLN | ALA | ||||
| 26 | TYR | ARG | VAL | ASP | GLU | ARG | ALA | ALA | GLU | GLN | ||||
| 27 | ALA | ARG | TRP | GLU | ALA | ALA | SER | LYS | GLU | THR | ||||
| 28 | ILE | LYS | LYS | THR | THR | LYS | PRO | CYS | PRO | ARG | ||||
| 29 | CYS | HIS | VAL | PRO | VAL | GLU | LYS | ASN | GLY | GLY | ||||
| 30 | CYS | MET | HIS | MET | LYS | CYS | PRO | GLN | PRO | GLN | ||||
| 31 | CYS | ARG | LEU | GLU | TRP | CYS | TRP | ASN | CYS | GLY | ||||
| 32 | CYS | GLU | TRP | ASN | ARG | VAL | CYS | MET | GLY | ASP | ||||
| 33 | HIS | TRP | PHE | ASP | VAL |
Entity 3, ZINC ION 1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: Ub S65E, [U-99% 13C; U-99% 15N], 290 uM; Parkin R0RBR (141-465), [U-99% 2H], 290 uM; HEPES 25 mM; Sodium chloride 100 mM; TCEP 500 uM; Imidazole 500 uM; DSS 100 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HMQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView v8.2.36, Johnson, One Moon Scientific - chemical shift assignment, peak picking
VNMRJ v3.2, Varian - collection
NMRPipe v2010.260.15.01, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz