BMRB Entry 16882
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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/BMR16882
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Title: Solution Structure of the Ubiquitin-Binding Motif of Human Polymerase Iota PubMed: 20159559
Deposition date: 2010-04-19 Original release date: 2010-06-15
Authors: Bomar, Martha; D'Souza, Sanjay; Bienko, Marzena; Dikic, Ivan; Walker, Graham
Citation: Bomar, Martha; Bienko, Sanjay; Dikic, Marzena; Walker, Ivan; Zhou, Graham. "Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1." Mol. Cell 37, 408-417 (2010).
Assembly members:
Ubiquitin-Binding Motif, polymer, 108 residues, 3753.299 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):
Ubiquitin-Binding Motif: MQYKLILNGKTLKGETTTEA
VDAATAEKVFKQYANDNGVD
GEWTYDDATKTFTVTEGSDE
KITFPSDIDPQVFYELPEAV
QKELLAEWKRTGSDFHIGHK
LEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 435 |
15N chemical shifts | 103 |
1H chemical shifts | 694 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | UBM2 | 1 |
Entities:
Entity 1, UBM2 108 residues - 3753.299 Da.
Residues 1-56 represent the GB1-tag. Residues 57-58, 101-108 are cloning artifacts (including the His6-tag)
1 | MET | GLN | TYR | LYS | LEU | ILE | LEU | ASN | GLY | LYS | ||||
2 | THR | LEU | LYS | GLY | GLU | THR | THR | THR | GLU | ALA | ||||
3 | VAL | ASP | ALA | ALA | THR | ALA | GLU | LYS | VAL | PHE | ||||
4 | LYS | GLN | TYR | ALA | ASN | ASP | ASN | GLY | VAL | ASP | ||||
5 | GLY | GLU | TRP | THR | TYR | ASP | ASP | ALA | THR | LYS | ||||
6 | THR | PHE | THR | VAL | THR | GLU | GLY | SER | ASP | GLU | ||||
7 | LYS | ILE | THR | PHE | PRO | SER | ASP | ILE | ASP | PRO | ||||
8 | GLN | VAL | PHE | TYR | GLU | LEU | PRO | GLU | ALA | VAL | ||||
9 | GLN | LYS | GLU | LEU | LEU | ALA | GLU | TRP | LYS | ARG | ||||
10 | THR | GLY | SER | ASP | PHE | HIS | ILE | GLY | HIS | LYS | ||||
11 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: UBM2, [U-100% 13C; U-100% 15N], 1 4 mM; D2O 100%
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | 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 HN(COCA)CB | 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:
X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
or all simulated shifts