BMRB Entry 30602
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30602
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Title: NMR Structure of Branched K11/K48-Linked Tri-Ubiquitin
Deposition date: 2019-04-25 Original release date: 2019-10-15
Authors: Boughton, A.; Fushman, D.
Citation: Boughton, A.; Krueger, S.; Fushman, D.. "Branched K11/K48-Linked Tri-Ubiquitin Exhibits a Unique Interdomain Interface and Enhanced Affinity for Proteasomal Subunit Rpn1" . ., .-..
Assembly members:
entity_1, polymer, 76 residues, 8660.873 Da.
entity_2, polymer, 76 residues, 8604.845 Da.
entity_3, polymer, 77 residues, 8691.918 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MQIFVKTLTGRTITLEVEPS
DTIENVKAKIQDKEGIPPDQ
QRLIFAGRQLEDGRTLSDYN
IQRESTLHLVLRLRGG
entity_2: MQIFVKTLTGKTITLEVEPS
DTIENVKAKIQDKEGIPPDQ
QRLIFAGRQLEDGRTLSDYN
IQKESTLHLVLRLRGG
entity_3: MQIFVKTLTGKTITLEVEPS
DTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGGD
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 140 |
| 1H chemical shifts | 140 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
| 3 | entity_3 | 3 |
Entities:
Entity 1, entity_1 76 residues - 8660.873 Da.
| 1 | MET | GLN | ILE | PHE | VAL | LYS | THR | LEU | THR | GLY | ||||
| 2 | ARG | THR | ILE | THR | LEU | GLU | VAL | GLU | PRO | SER | ||||
| 3 | ASP | THR | ILE | GLU | ASN | VAL | LYS | ALA | LYS | ILE | ||||
| 4 | GLN | ASP | LYS | GLU | GLY | ILE | PRO | PRO | ASP | GLN | ||||
| 5 | GLN | ARG | LEU | ILE | PHE | ALA | GLY | ARG | GLN | LEU | ||||
| 6 | GLU | ASP | GLY | ARG | THR | LEU | SER | ASP | TYR | ASN | ||||
| 7 | ILE | GLN | ARG | GLU | SER | THR | LEU | HIS | LEU | VAL | ||||
| 8 | LEU | ARG | LEU | ARG | GLY | GLY |
Entity 2, entity_2 76 residues - 8604.845 Da.
| 1 | MET | GLN | ILE | PHE | VAL | LYS | THR | LEU | THR | GLY | ||||
| 2 | LYS | THR | ILE | THR | LEU | GLU | VAL | GLU | PRO | SER | ||||
| 3 | ASP | THR | ILE | GLU | ASN | VAL | LYS | ALA | LYS | ILE | ||||
| 4 | GLN | ASP | LYS | GLU | GLY | ILE | PRO | PRO | ASP | GLN | ||||
| 5 | GLN | ARG | LEU | ILE | PHE | ALA | GLY | ARG | GLN | LEU | ||||
| 6 | GLU | ASP | GLY | ARG | THR | LEU | SER | ASP | TYR | ASN | ||||
| 7 | ILE | GLN | LYS | GLU | SER | THR | LEU | HIS | LEU | VAL | ||||
| 8 | LEU | ARG | LEU | ARG | GLY | GLY |
Entity 3, entity_3 77 residues - 8691.918 Da.
| 1 | MET | GLN | ILE | PHE | VAL | LYS | THR | LEU | THR | GLY | ||||
| 2 | LYS | THR | ILE | THR | LEU | GLU | VAL | GLU | PRO | SER | ||||
| 3 | ASP | THR | ILE | GLU | ASN | VAL | LYS | ALA | LYS | ILE | ||||
| 4 | GLN | ASP | LYS | GLU | GLY | ILE | PRO | PRO | ASP | GLN | ||||
| 5 | GLN | ARG | LEU | ILE | PHE | ALA | GLY | LYS | GLN | LEU | ||||
| 6 | GLU | ASP | GLY | ARG | THR | LEU | SER | ASP | TYR | ASN | ||||
| 7 | ILE | GLN | LYS | GLU | SER | THR | LEU | HIS | LEU | VAL | ||||
| 8 | LEU | ARG | LEU | ARG | GLY | GLY | ASP |
Samples:
sample_1: entity_1, [U-15N-distal11], 120 uM; entity_2, [U-15N-distal11], 120 uM; entity_3, [U-15N-distal11], 120 uM
sample_2: entity_1, [U-15N-distal48], 100 uM; entity_2, [U-15N-distal48], 100 uM; entity_3, [U-15N-distal48], 100 uM
sample_3: entity_1, [U-15N-distal11], 60 uM; entity_2, [U-15N-distal11], 60 uM; entity_3, [U-15N-distal11], 60 uM
sample_4: entity_1, [U-15N-distal48], 110 uM; entity_2, [U-15N-distal48], 110 uM; entity_3, [U-15N-distal48], 110 uM
sample_conditions_1: ionic strength: 0 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - processing
Sparky, Goddard - peak picking
HADDOCK, Bonvin - refinement, structure calculation
NMR spectrometers:
- Bruker AvanceIII 800 MHz
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts