BMRB Entry 30275
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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/BMR30275
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: Solution NMR structure of histone H2A-H2B mono-ubiquitylated at H2A Lys15 in complex with RNF169 (653-708) PubMed: 28506460
Deposition date: 2017-04-06 Original release date: 2017-05-15
Authors: Hu, Q.; Botuyan, M.; Cui, G.; Mer, G.
Citation: Hu, Qi; Botuyan, Maria Victoria; Cui, Gaofeng; Zhao, Debiao; Mer, Georges. "Mechanisms of Ubiquitin-Nucleosome Recognition and Regulation of 53BP1 Chromatin Recruitment by RNF168/169 and RAD18" Mol. Cell 66, 473-487.e9 (2017).
Assembly members:
entity_1, polymer, 194 residues, 21658.943 Da.
entity_2, polymer, 76 residues, 8576.831 Da.
entity_3, polymer, 59 residues, 7016.938 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: MHHHHHHMRKESYSIYVYKV
LKQVHPDTGISSKAMGIMNS
FVNDIFERIAGEASRLAHYN
KRSTITSREIQTAVRLLLPG
ELAKHAVSEGTKAVTKYTSS
ASAKTRSSRAGLQFPVGRVH
RLLRKGNYSERVGAGAPVYL
AAVLEYLTAEILELAGNAAR
DNKKTRIIPRHLQLAIRNDE
ELNKLLGRVTIAQG
entity_2: MQIFVKTLTGKTITLEVEPS
DTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG
entity_3: GHMDPVLREMEQKLQQEEED
RQLALQLQRMFDNERRTVSR
RKGSVDQYLLRSSNMAGAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 1268 |
| 15N chemical shifts | 319 |
| 1H chemical shifts | 2144 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
| 3 | entity_3 | 3 |
Entities:
Entity 1, entity_1 194 residues - 21658.943 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | MET | ARG | LYS | ||||
| 2 | GLU | SER | TYR | SER | ILE | TYR | VAL | TYR | LYS | VAL | ||||
| 3 | LEU | LYS | GLN | VAL | HIS | PRO | ASP | THR | GLY | ILE | ||||
| 4 | SER | SER | LYS | ALA | MET | GLY | ILE | MET | ASN | SER | ||||
| 5 | PHE | VAL | ASN | ASP | ILE | PHE | GLU | ARG | ILE | ALA | ||||
| 6 | GLY | GLU | ALA | SER | ARG | LEU | ALA | HIS | TYR | ASN | ||||
| 7 | LYS | ARG | SER | THR | ILE | THR | SER | ARG | GLU | ILE | ||||
| 8 | GLN | THR | ALA | VAL | ARG | LEU | LEU | LEU | PRO | GLY | ||||
| 9 | GLU | LEU | ALA | LYS | HIS | ALA | VAL | SER | GLU | GLY | ||||
| 10 | THR | LYS | ALA | VAL | THR | LYS | TYR | THR | SER | SER | ||||
| 11 | ALA | SER | ALA | LYS | THR | ARG | SER | SER | ARG | ALA | ||||
| 12 | GLY | LEU | GLN | PHE | PRO | VAL | GLY | ARG | VAL | HIS | ||||
| 13 | ARG | LEU | LEU | ARG | LYS | GLY | ASN | TYR | SER | GLU | ||||
| 14 | ARG | VAL | GLY | ALA | GLY | ALA | PRO | VAL | TYR | LEU | ||||
| 15 | ALA | ALA | VAL | LEU | GLU | TYR | LEU | THR | ALA | GLU | ||||
| 16 | ILE | LEU | GLU | LEU | ALA | GLY | ASN | ALA | ALA | ARG | ||||
| 17 | ASP | ASN | LYS | LYS | THR | ARG | ILE | ILE | PRO | ARG | ||||
| 18 | HIS | LEU | GLN | LEU | ALA | ILE | ARG | ASN | ASP | GLU | ||||
| 19 | GLU | LEU | ASN | LYS | LEU | LEU | GLY | ARG | VAL | THR | ||||
| 20 | ILE | ALA | GLN | GLY |
Entity 2, entity_2 76 residues - 8576.831 Da.
| 1 | MET | GLN | ILE | PHE | VAL | LYS | THR | LEU | THR | GLY | ||||
| 2 | LYS | THR | ILE | THR | LEU | GLU | VAL | GLU | PRO | SER | ||||
| 3 | ASP | THR | ILE | GLU | ASN | VAL | LYS | ALA | LYS | ILE | ||||
| 4 | GLN | ASP | LYS | GLU | GLY | ILE | PRO | PRO | ASP | GLN | ||||
| 5 | GLN | ARG | LEU | ILE | PHE | ALA | GLY | LYS | GLN | LEU | ||||
| 6 | GLU | ASP | GLY | ARG | THR | LEU | SER | ASP | TYR | ASN | ||||
| 7 | ILE | GLN | LYS | GLU | SER | THR | LEU | HIS | LEU | VAL | ||||
| 8 | LEU | ARG | LEU | ARG | GLY | GLY |
Entity 3, entity_3 59 residues - 7016.938 Da.
| 1 | GLY | HIS | MET | ASP | PRO | VAL | LEU | ARG | GLU | MET | ||||
| 2 | GLU | GLN | LYS | LEU | GLN | GLN | GLU | GLU | GLU | ASP | ||||
| 3 | ARG | GLN | LEU | ALA | LEU | GLN | LEU | GLN | ARG | MET | ||||
| 4 | PHE | ASP | ASN | GLU | ARG | ARG | THR | VAL | SER | ARG | ||||
| 5 | ARG | LYS | GLY | SER | VAL | ASP | GLN | TYR | LEU | LEU | ||||
| 6 | ARG | SER | SER | ASN | MET | ALA | GLY | ALA | LYS |
Samples:
sample_1: EDTA 4 mM; KCl 50 mM; MES-Bis-TRIS 25 mM; RNF169 3 mM; Ubiquitylated H2A-H2B 1 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 303 K
sample_conditions_2: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| ALL_Experiments | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRDRAW - structure solution
NMRPIPE - structure solution
NMRVIEW - structure solution
SPARKY - structure solution
TALOS - structure solution
TOPSPIN - structure solution
X-PLOR NIH, SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE III 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts