BMRB Entry 25923
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25923
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Title: ULD complex PubMed: 27827373
Deposition date: 2015-12-17 Original release date: 2016-11-14
Authors: Cierpicki, Tomasz; Gray, Felicia; Cho, Hyo Je
Citation: Gray, Felicia; Cho, Hyo Je; Shulka, Shirish; He, Shihan; Harris, Ashley; Boytsov, Bohdan; Jaremko, Lukasz; Jaremko, Mariusz; Demeler, Borries; Lawlor, Elizabeth; Grembecka, Jolanta; Cierpicki, Tomasz. "BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization" Nat. Commun. 9, 13343-13343 (2016).
Assembly members:
entity, polymer, 155 residues, 17139.982 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
Entity Sequences (FASTA):
entity: GPAMGKPQILTHVIEGFVIQ
EGAEPFPVGRSSLLVGNLKG
DKRIITDDEIISLSIEFFDQ
NRLDRKVNKDKEKSKEEVND
KRYLRCPAAMTVMHLRKFLR
SKMDIPNTFQIDVMYEEEPL
KDYYTLMDIAYIYTWRRNGP
LPLKYRVRPTCKRMK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 469 |
| 15N chemical shifts | 129 |
| 1H chemical shifts | 553 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 155 residues - 17139.982 Da.
Residues 1-5 are cloning artifact. Sequence contains fusion of PHC2_B residues 30-64 directly to N-terminus of BMI1 residues 121-235.
| 1 | GLY | PRO | ALA | MET | GLY | LYS | PRO | GLN | ILE | LEU | ||||
| 2 | THR | HIS | VAL | ILE | GLU | GLY | PHE | VAL | ILE | GLN | ||||
| 3 | GLU | GLY | ALA | GLU | PRO | PHE | PRO | VAL | GLY | ARG | ||||
| 4 | SER | SER | LEU | LEU | VAL | GLY | ASN | LEU | LYS | GLY | ||||
| 5 | ASP | LYS | ARG | ILE | ILE | THR | ASP | ASP | GLU | ILE | ||||
| 6 | ILE | SER | LEU | SER | ILE | GLU | PHE | PHE | ASP | GLN | ||||
| 7 | ASN | ARG | LEU | ASP | ARG | LYS | VAL | ASN | LYS | ASP | ||||
| 8 | LYS | GLU | LYS | SER | LYS | GLU | GLU | VAL | ASN | ASP | ||||
| 9 | LYS | ARG | TYR | LEU | ARG | CYS | PRO | ALA | ALA | MET | ||||
| 10 | THR | VAL | MET | HIS | LEU | ARG | LYS | PHE | LEU | ARG | ||||
| 11 | SER | LYS | MET | ASP | ILE | PRO | ASN | THR | PHE | GLN | ||||
| 12 | ILE | ASP | VAL | MET | TYR | GLU | GLU | GLU | PRO | LEU | ||||
| 13 | LYS | ASP | TYR | TYR | THR | LEU | MET | ASP | ILE | ALA | ||||
| 14 | TYR | ILE | TYR | THR | TRP | ARG | ARG | ASN | GLY | PRO | ||||
| 15 | LEU | PRO | LEU | LYS | TYR | ARG | VAL | ARG | PRO | THR | ||||
| 16 | CYS | LYS | ARG | MET | LYS |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 0.2 mM; D2O, [U-2H], 10%; sodium chloride 50 mM; TCEP 1 mM; TRIS 100 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303.2 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
SPARKY, Goddard - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PSVS, Bhattacharya and Montelione - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
Rosetta, (Rosetta-Relax)- Tyka, Keedy, Andre, Dimaio, Song, Richardson, Richardson and Baker - refinement
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts