BMRB Entry 25855
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25855
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: Zipcode-binding-protein-1 KH3(DD)KH4 domains in complex with the RNA target UCGGACU PubMed: 22547390
Deposition date: 2015-10-21 Original release date: 2017-01-19
Authors: Nicastro, Giuseppe; Ramos, Andres; Candel, Adela; Hollingworth, David
Citation: Hollingworth, David; Candel, Adela; Nicastro, Giuseppe; Martin, Stephen; Briata, Paola; Gherzi, Roberto; Ramos, Andres. "KH domains with impaired nucleic acid binding as a tool for functional analysis." Nucleic Acids Res. 40, 6873-6886 (2012).
Assembly members:
entity_1, polymer, 191 residues, 20613.682 Da.
entity_2, polymer, 8 residues, Formula weight is not available
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
Entity Sequences (FASTA):
entity_1: GAMGPSSVSGAAPFSSFMPP
EQETVHVFIPAQAVGAIIGK
KGQHIKQLSRFASASIKIAP
PETPDSKVRMVVITGPPEAQ
FKAQGRIYGKLKEENFFGPK
EEVKLETHIRVPASAAGRVI
GKGGKTVNELQNLTAAEVVV
PRDQTPDENEQVIVKIIGHF
YASQMAQRKIRDILAQVKQQ
HQKGQSGQLQA
entity_2: UCGGACU
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 403 |
| 1H chemical shifts | 941 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 191 residues - 20613.682 Da.
| 1 | GLY | ALA | MET | GLY | PRO | SER | SER | VAL | SER | GLY | ||||
| 2 | ALA | ALA | PRO | PHE | SER | SER | PHE | MET | PRO | PRO | ||||
| 3 | GLU | GLN | GLU | THR | VAL | HIS | VAL | PHE | ILE | PRO | ||||
| 4 | ALA | GLN | ALA | VAL | GLY | ALA | ILE | ILE | GLY | LYS | ||||
| 5 | LYS | GLY | GLN | HIS | ILE | LYS | GLN | LEU | SER | ARG | ||||
| 6 | PHE | ALA | SER | ALA | SER | ILE | LYS | ILE | ALA | PRO | ||||
| 7 | PRO | GLU | THR | PRO | ASP | SER | LYS | VAL | ARG | MET | ||||
| 8 | VAL | VAL | ILE | THR | GLY | PRO | PRO | GLU | ALA | GLN | ||||
| 9 | PHE | LYS | ALA | GLN | GLY | ARG | ILE | TYR | GLY | LYS | ||||
| 10 | LEU | LYS | GLU | GLU | ASN | PHE | PHE | GLY | PRO | LYS | ||||
| 11 | GLU | GLU | VAL | LYS | LEU | GLU | THR | HIS | ILE | ARG | ||||
| 12 | VAL | PRO | ALA | SER | ALA | ALA | GLY | ARG | VAL | ILE | ||||
| 13 | GLY | LYS | GLY | GLY | LYS | THR | VAL | ASN | GLU | LEU | ||||
| 14 | GLN | ASN | LEU | THR | ALA | ALA | GLU | VAL | VAL | VAL | ||||
| 15 | PRO | ARG | ASP | GLN | THR | PRO | ASP | GLU | ASN | GLU | ||||
| 16 | GLN | VAL | ILE | VAL | LYS | ILE | ILE | GLY | HIS | PHE | ||||
| 17 | TYR | ALA | SER | GLN | MET | ALA | GLN | ARG | LYS | ILE | ||||
| 18 | ARG | ASP | ILE | LEU | ALA | GLN | VAL | LYS | GLN | GLN | ||||
| 19 | HIS | GLN | LYS | GLY | GLN | SER | GLY | GLN | LEU | GLN | ||||
| 20 | ALA |
Entity 2, entity_2 8 residues - Formula weight is not available
| 1 | U | C | G | G | A | C | U |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.3 mM; entity_2 0.3 mM; phosphate buffer 20 mM; potassium phosphate 20 mM
sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
XEASY, Bartels et al. - chemical shift assignment
ARIA, Linge, O'Donoghue and Nilges - structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 950 MHz