BMRB Entry 16872
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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/BMR16872
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Title: Mcm10 C-terminal DNA binding domain PubMed: 20489205
Deposition date: 2010-04-15 Original release date: 2010-05-26
Authors: Robertson, Patrick; Chagot, Benjamin; Chazin, Walter; Eichman, Brandt
Citation: Robertson, Patrick; Chagot, Benjamin; Chazin, Walter; Eichman, Brandt. "Solution NMR structure of the C-terminal DNA binding domain of Mcm10 reveals a conserved MCM motif." J. Biol. Chem. 285, 22942-22949 (2010).
Assembly members:
Mcm10, polymer, 92 residues, 10596.545 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus laevis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Mcm10: GPMGMQSIREQSCRVVTCKT
CKYTHFKPKETCVSENHDFH
WHNGVKRFFKCPCGNRTISL
DRLPKKHCSTCGLFKWERVG
MLKEKTGPKLGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 282 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 645 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Mcm10 | 1 |
| 2 | ZINC ION 1 | 2 |
| 3 | ZINC ION 2 | 2 |
Entities:
Entity 1, Mcm10 92 residues - 10596.545 Da.
First four residues are a non-native affinity tag residual
| 1 | GLY | PRO | MET | GLY | MET | GLN | SER | ILE | ARG | GLU | ||||
| 2 | GLN | SER | CYS | ARG | VAL | VAL | THR | CYS | LYS | THR | ||||
| 3 | CYS | LYS | TYR | THR | HIS | PHE | LYS | PRO | LYS | GLU | ||||
| 4 | THR | CYS | VAL | SER | GLU | ASN | HIS | ASP | PHE | HIS | ||||
| 5 | TRP | HIS | ASN | GLY | VAL | LYS | ARG | PHE | PHE | LYS | ||||
| 6 | CYS | PRO | CYS | GLY | ASN | ARG | THR | ILE | SER | LEU | ||||
| 7 | ASP | ARG | LEU | PRO | LYS | LYS | HIS | CYS | SER | THR | ||||
| 8 | CYS | GLY | LEU | PHE | LYS | TRP | GLU | ARG | VAL | GLY | ||||
| 9 | MET | LEU | LYS | GLU | LYS | THR | GLY | PRO | LYS | LEU | ||||
| 10 | GLY | GLY |
Entity 2, ZINC ION 1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
N-enriched_(920): entity_1, [U-100% 15N], 920 uM; sodium phosphate 25 mM; sodium chloride 100 mM; D2O 5%; H2O 95%
N-enriched_(300): entity_1, [U-100% 15N], 300 uM; sodium phosphate 25 mM; sodium chloride 100 mM; D2O 5%; H2O 95%
C-enriched_(920): entity_1, [U-100% 13C], 920 uM; sodium phosphate 25 mM; sodium chloride 100 mM; D2O 5%; H2O 95%
NC-enriched_(920): entity_1, [U-100% 13C; U-100% 15N], 920 uM; sodium phosphate 25 mM; sodium chloride 100 mM; D2O 5%; H2O 95%
natural: entity_1 920 uM; sodium phosphate 25 mM; sodium chloride 100 mM; D2O 5%; H2O 95%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | N-enriched_(300) | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | C-enriched_(920) | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | natural | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | natural | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | natural | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC-enriched_(920) | isotropic | sample_conditions_1 |
| 3D HNCO | NC-enriched_(920) | isotropic | sample_conditions_1 |
| 3D HNCACB | NC-enriched_(920) | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC-enriched_(920) | isotropic | sample_conditions_1 |
| 3D HNHA | N-enriched_(920) | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | NC-enriched_(920) | isotropic | sample_conditions_1 |
| 3D C(CO)NH | NC-enriched_(920) | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | N-enriched_(920) | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | C-enriched_(920) | isotropic | sample_conditions_1 |
| 3D (HB)CB(CGCD)HD | N-enriched_(920) | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
SPARKY, Goddard - peak picking
TOPSPIN, Bruker Biospin - collection
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts