BMRB Entry 25808
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25808
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: Santonico, Elena; Nepravishta, Ridvan; Mattioni, Anna; Valentini, Eleonora; Mandaliti, Walter; Procopio, Radha; Iannuccelli, Marta; Castagnoli, Luisa; Polo, Simona; Paci, Maurizio; Cesareni, Gianni. "Unveiling the structural determinants of KIAA0323 binding preference for NEDD8" .
Assembly members:
entity_1, polymer, 76 residues, 8574.057 Da.
entity_2, polymer, 52 residues, 6299.246 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGex6p1
Entity Sequences (FASTA):
entity_1: MLIKVKTLTGKEIEIDIEPT
DKVERIKERVEEKEGIPPQQ
QRLIYSGKQMNDEKTAADYK
ILGGSVLHLVLALRGG
entity_2: GGIRKTRETERLRRQLLEVF
WGQDHKVDFILQREPYCRDI
NQLSEALLSLNF
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 120 |
| 1H chemical shifts | 118 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 76 residues - 8574.057 Da.
| 1 | MET | LEU | ILE | LYS | VAL | LYS | THR | LEU | THR | GLY | ||||
| 2 | LYS | GLU | ILE | GLU | ILE | ASP | ILE | GLU | PRO | THR | ||||
| 3 | ASP | LYS | VAL | GLU | ARG | ILE | LYS | GLU | ARG | VAL | ||||
| 4 | GLU | GLU | LYS | GLU | GLY | ILE | PRO | PRO | GLN | GLN | ||||
| 5 | GLN | ARG | LEU | ILE | TYR | SER | GLY | LYS | GLN | MET | ||||
| 6 | ASN | ASP | GLU | LYS | THR | ALA | ALA | ASP | TYR | LYS | ||||
| 7 | ILE | LEU | GLY | GLY | SER | VAL | LEU | HIS | LEU | VAL | ||||
| 8 | LEU | ALA | LEU | ARG | GLY | GLY |
Entity 2, entity_2 52 residues - 6299.246 Da.
| 1 | GLY | GLY | ILE | ARG | LYS | THR | ARG | GLU | THR | GLU | ||||
| 2 | ARG | LEU | ARG | ARG | GLN | LEU | LEU | GLU | VAL | PHE | ||||
| 3 | TRP | GLY | GLN | ASP | HIS | LYS | VAL | ASP | PHE | ILE | ||||
| 4 | LEU | GLN | ARG | GLU | PRO | TYR | CYS | ARG | ASP | ILE | ||||
| 5 | ASN | GLN | LEU | SER | GLU | ALA | LEU | LEU | SER | LEU | ||||
| 6 | ASN | PHE |
Samples:
sample_1: entity_1, [U-100% 15N], 0.15 – 1.5 mM; entity_2, [U-100% 15N], 0.15 – 1.5 mM
sample_conditions_1: ionic strength: 0.02 M; pH: 5.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks