BMRB Entry 50269
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50269
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: Liu, Xinyue; Garber, Abigail; Ryan, Julia; Deshpande, Aditi; Ringe, Dagmar; Pochapsky, Thomas. "Solution structure of human Fe(II)-bound acireductone dioxygenase and interactions with the regulatory domain of matrix metalloproteinase I (MMP-1)" Biochemistry 59, 4238-4249 (2020).
PubMed: 33135413
Assembly members:
entity_1, polymer, 179 residues, Formula weight is not available
entity_FE2, non-polymer, 55.845 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 Vector: pET19
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 425 |
| 15N chemical shifts | 153 |
| 1H chemical shifts | 989 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | acireductone dioxygenase | 1 |
| 2 | FE (II) ION | 2 |
Entities:
Entity 1, acireductone dioxygenase 179 residues - Formula weight is not available
| 1 | MET | VAL | GLN | ALA | TRP | TYR | MET | ASP | ASP | ALA | ||||
| 2 | PRO | GLY | ASP | PRO | ARG | GLN | PRO | HIS | ARG | PRO | ||||
| 3 | ASP | PRO | GLY | ARG | PRO | VAL | GLY | LEU | GLU | GLN | ||||
| 4 | LEU | ARG | ARG | LEU | GLY | VAL | LEU | TYR | TRP | LYS | ||||
| 5 | LEU | ASP | ALA | ASP | LYS | TYR | GLU | ASN | ASP | PRO | ||||
| 6 | GLU | LEU | GLU | LYS | ILE | ARG | ARG | GLU | ARG | ASN | ||||
| 7 | TYR | SER | TRP | MET | ASP | ILE | ILE | THR | ILE | CYS | ||||
| 8 | LYS | ASP | LYS | LEU | PRO | ASN | TYR | GLU | GLU | LYS | ||||
| 9 | ILE | LYS | MET | PHE | TYR | GLU | GLU | HIS | LEU | HIS | ||||
| 10 | LEU | ASP | ASP | GLU | ILE | ARG | TYR | ILE | LEU | ASP | ||||
| 11 | GLY | SER | GLY | TYR | PHE | ASP | VAL | ARG | ASP | LYS | ||||
| 12 | GLU | ASP | GLN | TRP | ILE | ARG | ILE | PHE | MET | GLU | ||||
| 13 | LYS | GLY | ASP | MET | VAL | THR | LEU | PRO | ALA | GLY | ||||
| 14 | ILE | TYR | HIS | ARG | PHE | THR | VAL | ASP | GLU | LYS | ||||
| 15 | ASN | TYR | THR | LYS | ALA | MET | ARG | LEU | PHE | VAL | ||||
| 16 | GLY | GLU | PRO | VAL | TRP | THR | ALA | TYR | ASN | ARG | ||||
| 17 | PRO | ALA | ASP | HIS | PHE | GLU | ALA | ARG | GLY | GLN | ||||
| 18 | TYR | VAL | LYS | PHE | LEU | ALA | GLN | THR | ALA |
Entity 2, FE (II) ION - Fe - 55.845 Da.
| 1 | FE2 |
Samples:
sample_1: acireductone dioxygenase, [U-100% 13C; U-100% 15N], 500 uM; HEPES 50 mM; NaCl 100 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY vNMRFAM - data analysis
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