BMRB Entry 25033
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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/BMR25033
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Title: Solution structure of the Chlamydomonas reinhardtii NAB1 cold shock domain, CSD1 PubMed: 25919092
Deposition date: 2014-06-20 Original release date: 2015-05-04
Authors: Sawyer, Anne; Mobli, Mehdi
Citation: Sawyer, Anne; Mobli, Mehdi; Landsberg, Michael; Ross, Ian; Hankamer, Ben. "Solution structure of the RNA-binding cold shock domain of the Chlamydomonas reinhardtii NAB1 protein and insights into RNA recognition" Biochem. J. ., .-. (2015).
Assembly members:
NAB1_cold_shock_domain, polymer, 82 residues, 7736.490 Da.
Natural source: Common Name: green algae Taxonomy ID: 3055 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Chlamydomonas reinhardtii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NAB1_cold_shock_domain: MRGSHHHHHHGSGEQLRQQG
TVKWFNATKGFGFITPGGGG
EDLFVHQTNINSEGFRSLRE
GEVVEFEVEAGPDGRSKAVN
VT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 265 |
| 15N chemical shifts | 71 |
| 1H chemical shifts | 428 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 82 residues - 7736.490 Da.
Residues 1-12 are part of a non-native His tag, this is the cold shock domain of NAB1
| 1 | MET | ARG | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | GLY | SER | GLY | GLU | GLN | LEU | ARG | GLN | GLN | GLY | ||||
| 3 | THR | VAL | LYS | TRP | PHE | ASN | ALA | THR | LYS | GLY | ||||
| 4 | PHE | GLY | PHE | ILE | THR | PRO | GLY | GLY | GLY | GLY | ||||
| 5 | GLU | ASP | LEU | PHE | VAL | HIS | GLN | THR | ASN | ILE | ||||
| 6 | ASN | SER | GLU | GLY | PHE | ARG | SER | LEU | ARG | GLU | ||||
| 7 | GLY | GLU | VAL | VAL | GLU | PHE | GLU | VAL | GLU | ALA | ||||
| 8 | GLY | PRO | ASP | GLY | ARG | SER | LYS | ALA | VAL | ASN | ||||
| 9 | VAL | THR |
Samples:
sample_1: NAB1 cold shock domain, [U-100% 13C; U-100% 15N], 267 uM; sodium phosphate 20 mM; sodium chloride 300 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.3 M; pH: 7; pressure: 1 atm; temperature: 298 K
Sample_conditions_2: ionic strength: 0.3 M; pH: 7; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | Sample_conditions_2 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNmr v2.4.0, CCPN - chemical shift assignment, data analysis, peak picking
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
TOPSPIN v3.1, Bruker Biospin - collection
Rowland_NMR_Toolkit v3, A. Stern, J. C. Hoch - processing
NMR spectrometers:
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts