BMRB Entry 30017
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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/BMR30017
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Title: Solution Structure of human calcium-binding S100A9 (C3S) protein PubMed: 27524699
Deposition date: 2016-02-19 Original release date: 2016-08-19
Authors: Chang, Chin-Chi; Chin, Yu
Citation: Chang, Chin-Chi; Khan, Imran; Tsai, Kun-Lin; Li, Hongchun; Yang, Lee-Wei; Chou, Ruey-Hwang; Yu, Chin. "Blocking the interaction between S100A9 and RAGE V domain using CHAPS molecule: A novel route to drug development against cell proliferation" Biochim. Biophys. Acta 1864, 1558-1569 (2016).
Assembly members:
entity_1, polymer, 114 residues, 13247.955 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 'BL21-Gold(DE3)pLysS AG'
Entity Sequences (FASTA):
entity_1: MTSKMSQLERNIETIINTFH
QYSVKLGHPDTLNQGEFKEL
VRKDLQNFLKKENKNEKVIE
HIMEDLDTNADKQLSFEEFI
MLMARLTWASHEKMHEGDEG
PGHHHKPGLGEGTP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 435 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 668 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 1 |
Entities:
Entity 1, entity_1 114 residues - 13247.955 Da.
| 1 | MET | THR | SER | LYS | MET | SER | GLN | LEU | GLU | ARG | ||||
| 2 | ASN | ILE | GLU | THR | ILE | ILE | ASN | THR | PHE | HIS | ||||
| 3 | GLN | TYR | SER | VAL | LYS | LEU | GLY | HIS | PRO | ASP | ||||
| 4 | THR | LEU | ASN | GLN | GLY | GLU | PHE | LYS | GLU | LEU | ||||
| 5 | VAL | ARG | LYS | ASP | LEU | GLN | ASN | PHE | LEU | LYS | ||||
| 6 | LYS | GLU | ASN | LYS | ASN | GLU | LYS | VAL | ILE | GLU | ||||
| 7 | HIS | ILE | MET | GLU | ASP | LEU | ASP | THR | ASN | ALA | ||||
| 8 | ASP | LYS | GLN | LEU | SER | PHE | GLU | GLU | PHE | ILE | ||||
| 9 | MET | LEU | MET | ALA | ARG | LEU | THR | TRP | ALA | SER | ||||
| 10 | HIS | GLU | LYS | MET | HIS | GLU | GLY | ASP | GLU | GLY | ||||
| 11 | PRO | GLY | HIS | HIS | HIS | LYS | PRO | GLY | LEU | GLY | ||||
| 12 | GLU | GLY | THR | PRO |
Samples:
sample_1: S100A9 protein (C3S), [U-13C; U-15N], 2 ± 0.2 mM; TRIS 50 ± 0.2 mM; calcium chloride 2 ± 0.2 mM; sodium chloride 100 ± 0.2 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 310 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - peak picking, refinement, structure calculation
SPARKY v3.1, Goddard - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
Vnmrj v2.3, Varian - processing
NMR spectrometers:
- Varian VNMRS 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts