BMRB Entry 34330
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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/BMR34330
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Title: Solution structure of TRIM28 RING domain
Deposition date: 2018-11-23 Original release date: 2019-04-24
Authors: Stevens, R.; Esposito, D.; Rittinger, K.
Citation: Stevens, R.; Esposito, D.; Rittinger, K.. "Solution structure of TRIM28 RING domain" . ., .-..
Assembly members:
entity_1, polymer, 94 residues, 9674.865 Da.
entity_ZN, non-polymer, 65.409 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: GPGGAEALELLEHCGVCRER
LRPEREPRLLPCLHSACSAC
LGPAAPAAANSSGDGGAAGD
GTVVDCPVCKQQCFSKDIVE
NYFMRDSGSKAATD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 369 |
15N chemical shifts | 90 |
1H chemical shifts | 579 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2, 1 | 2 |
3 | entity_2, 2 | 2 |
Entities:
Entity 1, entity_1 94 residues - 9674.865 Da.
1 | GLY | PRO | GLY | GLY | ALA | GLU | ALA | LEU | GLU | LEU | ||||
2 | LEU | GLU | HIS | CYS | GLY | VAL | CYS | ARG | GLU | ARG | ||||
3 | LEU | ARG | PRO | GLU | ARG | GLU | PRO | ARG | LEU | LEU | ||||
4 | PRO | CYS | LEU | HIS | SER | ALA | CYS | SER | ALA | CYS | ||||
5 | LEU | GLY | PRO | ALA | ALA | PRO | ALA | ALA | ALA | ASN | ||||
6 | SER | SER | GLY | ASP | GLY | GLY | ALA | ALA | GLY | ASP | ||||
7 | GLY | THR | VAL | VAL | ASP | CYS | PRO | VAL | CYS | LYS | ||||
8 | GLN | GLN | CYS | PHE | SER | LYS | ASP | ILE | VAL | GLU | ||||
9 | ASN | TYR | PHE | MET | ARG | ASP | SER | GLY | SER | LYS | ||||
10 | ALA | ALA | THR | ASP |
Entity 2, entity_2, 1 - Zn - 65.409 Da.
1 | ZN |
Samples:
sample_1: TRIM28 RING, [U-15N], 1 mM; MES 20 mM; NaCl 100 mM; TCEP 0.5 mM
sample_2: TRIM28 RING, [U-13C; U-15N], 1 mM; MES 20 mM; NaCl 100 mM; TCEP 0.5 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCA | sample_2 | isotropic | sample_conditions_2 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_2 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
3D HNCO | sample_2 | isotropic | sample_conditions_2 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_2 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_2 |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_2 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_2 |
Software:
CcpNMR, CCPN - chemical shift assignment
ARIA, Linge, O'Donoghue and Nilges - structure calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker AvanceIII 700 MHz
- Bruker AvanceIII 800 MHz
- Bruker A 950 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts