BMRB Entry 31007
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31007
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
Title: Evolution avoids a pathological stabilizing interaction in the immune protein S100A9 PubMed: 36194634
Deposition date: 2022-03-28 Original release date: 2022-09-22
Authors: Reardon, P.; Harman, J.; Costello, S.; Warren, G.; Phillips, S.; Connor, P.; Marqusee, S.; Harms, M.
Citation: Harman, J.; Reardon, P.; Costello, S.; Warren, G.; Phillips, S.; Connor, P.; Marqusee, S.; Harms, M.. "Evolution avoids a pathological stabilizing interaction in the immune protein S100A9" Proc. Natl. Acad. Sci. U. S. A. 119, e2208029119-e2208029119 (2022).
Assembly members:
entity_1, polymer, 114 residues, 13263.934 Da.
entity_CA, non-polymer, 40.078 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: pETDuet-1
Entity Sequences (FASTA):
entity_1: MTSKMSQLERNIETIINTFH
QYSVKLGHPDTLNQGEFKEL
VRKDLQNFLKKENKNEKVIE
HIFEDLDTNADKQLSFEEFI
MLMARLTWASHEKMHEGDEG
PGHHHKPGLGEGTP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 343 |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 609 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 1 |
| 3 | unit_3 | 2 |
| 4 | unit_4 | 2 |
| 5 | unit_5 | 2 |
| 6 | unit_6 | 2 |
Entities:
Entity 1, unit_1 114 residues - 13263.934 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 | PHE | 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 |
Entity 2, unit_3 - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: TRIS 25 mM; sodium chloride 100 mM; calcium chloride 10 mM; S100A9-M63F, [U-100% 13C; U-100% 15N], 1 mM
sample_conditions_1: ionic strength: 110 mM; pH: 7.4; pressure: 1.01 bar; 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 2D HDCB | sample_1 | isotropic | sample_conditions_1 |
| 2D HECB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AVANCE III HD 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts