BMRB Entry 30493
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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/BMR30493
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Title: Solution NMR Structure of the Colied-coil PALB2 Homodimer PubMed: 30289697
Deposition date: 2018-07-17 Original release date: 2018-10-08
Authors: Song, F.; Li, M.; Liu, G.; Swapna, G.; Xia, B.; Bunting, S.; Montelione, G.
Citation: Song, F.; Li, M.; Liu, G.; Swapna, G.; Daigham, N.; Xia, B.; Montelione, G.; Bunting, S.. "Antiparallel Coiled-Coil Interactions Mediate Homodimerization of the DNA Damage Repair Protein, PALB2" Biochemistry 57, 6581-6591 (2018).
Assembly members:
entity_1, polymer, 68 residues, 7948.166 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MEELSGKPLSYAEKEKLKEK
LAFLKKEYSRTLARLQRAKR
AEKAKNSKKAIEDGVPQPEA
LEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 211 |
| 15N chemical shifts | 59 |
| 1H chemical shifts | 426 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1, 1 | 1 |
| 2 | entity_1, 2 | 1 |
Entities:
Entity 1, entity_1, 1 68 residues - 7948.166 Da.
| 1 | MET | GLU | GLU | LEU | SER | GLY | LYS | PRO | LEU | SER | ||||
| 2 | TYR | ALA | GLU | LYS | GLU | LYS | LEU | LYS | GLU | LYS | ||||
| 3 | LEU | ALA | PHE | LEU | LYS | LYS | GLU | TYR | SER | ARG | ||||
| 4 | THR | LEU | ALA | ARG | LEU | GLN | ARG | ALA | LYS | ARG | ||||
| 5 | ALA | GLU | LYS | ALA | LYS | ASN | SER | LYS | LYS | ALA | ||||
| 6 | ILE | GLU | ASP | GLY | VAL | PRO | GLN | PRO | GLU | ALA | ||||
| 7 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: PALB2cc, [U-100% 13C; U-100% 15N], 1.2 mM; MES 20 mM; sodium chloride 200 mM; Calcium Chloride 5 mM; DTT 10 mM; DSS 10%; sodium azide 0.02%
sample_2: PALB2cc, [U-100% 13C; U-100% 15N], 1 v/v; MES 20 mM; sodium chloride 200 mM; Calcium Chloride 5 mM; DTT 10 mM; DSS 10%; sodium azide 0.02%; unlabeled PALB2cc 2 v/v
sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D TROSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCOCA | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCOCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HBHACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| AROMATIC CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D simultaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| X-filtered noesy (pulse sequence: noesyhsqcgpwgx13d) | sample_2 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - peak picking
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AVS, Moseley and Montelione - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
PSVS, Bhattacharya and Montelione - data analysis
XEASY, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts