BMRB Entry 10054
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10054
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: Goroncy, A.; Kigawa, T.; Koshiba, S.; Tomizawa, T.; Kobayashi, N.; Tochio, N.; Inoue, M.; Yokoyama, S.. "Solution structure of the first cold-shock domain of the human KIAA0885 protein
(UNR protein)" .
Assembly members:
First cold-shock domain, polymer, 89 residues, Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: cell free synthesis Vector: P040114-45
Entity Sequences (FASTA):
First cold-shock domain: GSSGSSGGYPNGTSAALRET
GVIEKLLTSYGFIQCSERQA
RLFFHCSQYNGNLQDLKVGD
DVEFEVSSDRRTGKPIAVKL
VKISGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 377 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 589 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UNR protein | 1 |
Entities:
Entity 1, UNR protein 89 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | GLY | TYR | PRO | ||||
| 2 | ASN | GLY | THR | SER | ALA | ALA | LEU | ARG | GLU | THR | ||||
| 3 | GLY | VAL | ILE | GLU | LYS | LEU | LEU | THR | SER | TYR | ||||
| 4 | GLY | PHE | ILE | GLN | CYS | SER | GLU | ARG | GLN | ALA | ||||
| 5 | ARG | LEU | PHE | PHE | HIS | CYS | SER | GLN | TYR | ASN | ||||
| 6 | GLY | ASN | LEU | GLN | ASP | LEU | LYS | VAL | GLY | ASP | ||||
| 7 | ASP | VAL | GLU | PHE | GLU | VAL | SER | SER | ASP | ARG | ||||
| 8 | ARG | THR | GLY | LYS | PRO | ILE | ALA | VAL | LYS | LEU | ||||
| 9 | VAL | LYS | ILE | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: cold-shock domain, [U-13C; U-15N], 1.09 mM; phosphate 20 mM; NaCl 100 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | sample_1 | not available | condition_1 |
| 3D 13C-separated NOESY | sample_1 | not available | condition_1 |
Software:
xwinnmr v2.6, BRUKER - collection
NMRPipe v20031121, DELAGLIO, FRANK - processing
NMRView v5.0.14, JOHNSON, BRUCE, A. - data analysis
Kujira v0.899, KOBAYASHI, NAOHIRO - data analysis
CYANA v2.0.17, GUENTERT, P. - refinement
NMR spectrometers:
- Bruker AVANCE 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks