BMRB Entry 34336
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34336
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Title: Structural and functional insights into the condensin ATPase cycle PubMed: 31226277
Deposition date: 2018-12-10 Original release date: 2019-06-27
Authors: Simon, B.; Hassler, M.; Haering, C.; Hennig, J.
Citation: Hassler, Markus; Shaltiel, Indra; Kschonsak, Marc; Simon, Bernd; Merkel, Fabian; Tharichen, Lena; Bailey, Henry; Macosek, Jakub; Bravo, Sol; Metz, Jutta; Hennig, Janosch; Haering, Christian. "Structural Basis of an Asymmetric Condensin ATPase Cycle." Mol. Cell 74, 1175-1188 (2019).
Assembly members:
entity_1, polymer, 221 residues, 25200.189 Da.
Natural source: Common Name: Chaetomium thermophilum Taxonomy ID: 209285 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Chaetomium thermophilum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: GHMRAVTPMKRVPILANFEE
WMKMATDNKINAANSWNFAL
IDYFHDMSLLKEGDSVNFQK
ASCTLDGCVKIYTSRVDSVA
TETGKLLSGLADSRDSKKKD
REDGGGSGGSLRKKINPKVM
NMIDSVEKKEMSLKHMMKTV
LKDKHKIEETIATLDEYKRK
ASGGSAGTRMFEDRKEKALK
TMAKKDLKLQEITELLRDEI
EPKLEKLRQEKRAFLDFQQT
Q
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 695 |
| 15N chemical shifts | 224 |
| 1H chemical shifts | 1266 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 221 residues - 25200.189 Da.
| 1 | GLY | HIS | MET | ARG | ALA | VAL | THR | PRO | MET | LYS | ||||
| 2 | ARG | VAL | PRO | ILE | LEU | ALA | ASN | PHE | GLU | GLU | ||||
| 3 | TRP | MET | LYS | MET | ALA | THR | ASP | ASN | LYS | ILE | ||||
| 4 | ASN | ALA | ALA | ASN | SER | TRP | ASN | PHE | ALA | LEU | ||||
| 5 | ILE | ASP | TYR | PHE | HIS | ASP | MET | SER | LEU | LEU | ||||
| 6 | LYS | GLU | GLY | ASP | SER | VAL | ASN | PHE | GLN | LYS | ||||
| 7 | ALA | SER | CYS | THR | LEU | ASP | GLY | CYS | VAL | LYS | ||||
| 8 | ILE | TYR | THR | SER | ARG | VAL | ASP | SER | VAL | ALA | ||||
| 9 | THR | GLU | THR | GLY | LYS | LEU | LEU | SER | GLY | LEU | ||||
| 10 | ALA | ASP | SER | ARG | ASP | SER | LYS | LYS | LYS | ASP | ||||
| 11 | ARG | GLU | ASP | GLY | GLY | GLY | SER | GLY | GLY | SER | ||||
| 12 | LEU | ARG | LYS | LYS | ILE | ASN | PRO | LYS | VAL | MET | ||||
| 13 | ASN | MET | ILE | ASP | SER | VAL | GLU | LYS | LYS | GLU | ||||
| 14 | MET | SER | LEU | LYS | HIS | MET | MET | LYS | THR | VAL | ||||
| 15 | LEU | LYS | ASP | LYS | HIS | LYS | ILE | GLU | GLU | THR | ||||
| 16 | ILE | ALA | THR | LEU | ASP | GLU | TYR | LYS | ARG | LYS | ||||
| 17 | ALA | SER | GLY | GLY | SER | ALA | GLY | THR | ARG | MET | ||||
| 18 | PHE | GLU | ASP | ARG | LYS | GLU | LYS | ALA | LEU | LYS | ||||
| 19 | THR | MET | ALA | LYS | LYS | ASP | LEU | LYS | LEU | GLN | ||||
| 20 | GLU | ILE | THR | GLU | LEU | LEU | ARG | ASP | GLU | ILE | ||||
| 21 | GLU | PRO | LYS | LEU | GLU | LYS | LEU | ARG | GLN | GLU | ||||
| 22 | LYS | ARG | ALA | PHE | LEU | ASP | PHE | GLN | GLN | THR | ||||
| 23 | GLN |
Samples:
sample_1: Ct Smc2 Brn1 fusion protein, [U-100% 13C; U-100% 15N], 0.8 mM
sample_2: Ct Smc2 Brn1 fusion protein, [U-100% 13C; U-100% 15N], 0.6 mM
sample_3: Ct Smc2 Brn1 fusion protein, [U-100% 13C; U-100% 15N; U-100% 2H], 0.4 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_3 | 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-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger A. T. et.al. - structure calculation
ARIA, Linge, O'Donoghue and Nilges - structure calculation
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
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