BMRB Entry 18118
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18118
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Title: NMR structure of the protein BC040485 from Homo sapiens
Deposition date: 2011-12-01 Original release date: 2012-01-25
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the human RNA binding protein BC040485" Not known ., .-..
Assembly members:
entity, polymer, 107 residues, 12443.094 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: GSKLEEEVDDVFLIRAQGLP
WSCTMEDVLNFFSDCRIRNG
ENGIHFLLNRDGKRRGDALI
EMESEQDVQKALEKHRMYMG
QRYVEVYEINNEDVDALMKS
LQVKSSP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 340 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 698 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BC040485 | 1 |
Entities:
Entity 1, BC040485 107 residues - 12443.094 Da.
| 1 | GLY | SER | LYS | LEU | GLU | GLU | GLU | VAL | ASP | ASP | ||||
| 2 | VAL | PHE | LEU | ILE | ARG | ALA | GLN | GLY | LEU | PRO | ||||
| 3 | TRP | SER | CYS | THR | MET | GLU | ASP | VAL | LEU | ASN | ||||
| 4 | PHE | PHE | SER | ASP | CYS | ARG | ILE | ARG | ASN | GLY | ||||
| 5 | GLU | ASN | GLY | ILE | HIS | PHE | LEU | LEU | ASN | ARG | ||||
| 6 | ASP | GLY | LYS | ARG | ARG | GLY | ASP | ALA | LEU | ILE | ||||
| 7 | GLU | MET | GLU | SER | GLU | GLN | ASP | VAL | GLN | LYS | ||||
| 8 | ALA | LEU | GLU | LYS | HIS | ARG | MET | TYR | MET | GLY | ||||
| 9 | GLN | ARG | TYR | VAL | GLU | VAL | TYR | GLU | ILE | ASN | ||||
| 10 | ASN | GLU | ASP | VAL | ASP | ALA | LEU | MET | LYS | SER | ||||
| 11 | LEU | GLN | VAL | LYS | SER | SER | PRO |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium azide 5 mM; sodium chloride 50 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.080 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 4D HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, G ntert P. - structure solution
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts