BMRB Entry 34144
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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/BMR34144
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Title: NMR structure of TIA-1 RRM1 domain
Deposition date: 2017-05-22 Original release date: 2017-06-23
Authors: Jagtap, P.
Citation: Sonntag, M.; Jagtap, P.. "NMR structure of TIA-1 RRM1 domain" . ., .-..
Assembly members:
entity_1, polymer, 92 residues, 10275.843 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_1: MEDEMPKTLYVGNLSRDVTE
ALILQLFSQIGPCKNCKMIM
DTAGNDPYCFVEFHEHRHAA
AALAAMNGRKIMGKEVKVNW
ATTPSSQKKDTS
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 383 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 599 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 92 residues - 10275.843 Da.
| 1 | MET | GLU | ASP | GLU | MET | PRO | LYS | THR | LEU | TYR | ||||
| 2 | VAL | GLY | ASN | LEU | SER | ARG | ASP | VAL | THR | GLU | ||||
| 3 | ALA | LEU | ILE | LEU | GLN | LEU | PHE | SER | GLN | ILE | ||||
| 4 | GLY | PRO | CYS | LYS | ASN | CYS | LYS | MET | ILE | MET | ||||
| 5 | ASP | THR | ALA | GLY | ASN | ASP | PRO | TYR | CYS | PHE | ||||
| 6 | VAL | GLU | PHE | HIS | GLU | HIS | ARG | HIS | ALA | ALA | ||||
| 7 | ALA | ALA | LEU | ALA | ALA | MET | ASN | GLY | ARG | LYS | ||||
| 8 | ILE | MET | GLY | LYS | GLU | VAL | LYS | VAL | ASN | TRP | ||||
| 9 | ALA | THR | THR | PRO | SER | SER | GLN | LYS | LYS | ASP | ||||
| 10 | THR | SER |
Samples:
sample_1: entity_1, [U-15N; U-13C], 0.5 mM
sample_2: entity_1, [U-15N], 0.5 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 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 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O'Donoghue and Nilges - refinement
Analysis, CCPN - chemical shift assignment, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker AvanceIII 800 MHz
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts