BMRB Entry 25837
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25837
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Title: Chemical shift assignment, NMR constraints and PDB for chromodomain 3 (CD3) of cpSRP43 PubMed: 26568381
Deposition date: 2015-10-06 Original release date: 2015-12-07
Authors: Hennig, Janosch; Sattler, Michael
Citation: Horn, Annemarie; Hennig, Janosch; Ahmed, Yasar; Stier, Gunter; Wild, Klemes; Sattler, Michael; Sinning, Irmgard. "Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction" Nat. Commun. 6, 8875-8875 (2015).
Assembly members:
CD3, polymer, 58 residues, 6580.293 Da.
Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CD3: GLEYAVAESVIGKRVGDDGK
TIEYLVKWTDMSDATWEPQD
NVDSTLVLLYQQQQPMNE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 242 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 408 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CD3 | 1 |
Entities:
Entity 1, CD3 58 residues - 6580.293 Da.
| 1 | GLY | LEU | GLU | TYR | ALA | VAL | ALA | GLU | SER | VAL | ||||
| 2 | ILE | GLY | LYS | ARG | VAL | GLY | ASP | ASP | GLY | LYS | ||||
| 3 | THR | ILE | GLU | TYR | LEU | VAL | LYS | TRP | THR | ASP | ||||
| 4 | MET | SER | ASP | ALA | THR | TRP | GLU | PRO | GLN | ASP | ||||
| 5 | ASN | VAL | ASP | SER | THR | LEU | VAL | LEU | LEU | TYR | ||||
| 6 | GLN | GLN | GLN | GLN | PRO | MET | ASN | GLU |
Samples:
sample_1: CD3, [U-100% 13C; U-100% 15N], 0.26 mM
sample_2: CD3, [U-100% 13C; U-100% 15N], 0.8 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
ARIA v1.2, Linge, O'Donoghue and Nilges - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
TOPSPIN, Bruker Biospin - collection
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance III 800 MHz
- Bruker Avance III 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts