BMRB Entry 25901
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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/BMR25901
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Title: Structure of SUMO-2 bound to phosphorylated RAP80 SIM. PubMed: 26719330
Deposition date: 2016-01-19 Original release date: 2016-01-19
Authors: Anamika, Anamika; Spyracopoulos, Leo
Citation: Anamika, Anamika; Spyracopoulos, Leo. "Molecular Basis for Phosphorylation Dependent SUMO Recognition by the DNA Repair Protein RAP80" J. Biol. Chem. 291, 4417-4428 (2016).
Assembly members:
entity_1, polymer, 15 residues, 1745.656 Da.
entity_2, polymer, 95 residues, 11502.955 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: XEDAFIVIXDXDGEX
entity_2: MADEKPKEGVKTENNDHINL
KVAGQDGSVVQFKIKRHTPL
SKLMKAYCERQGLSMRQIRF
RFDGQPINETDTPAQLEMED
EDTIDVFQQQTGGVY
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 230 |
15N chemical shifts | 81 |
1H chemical shifts | 81 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 15 residues - 1745.656 Da.
The polypeptide belongs to residues 37-49 of human RAP80.
1 | ACE | GLU | ASP | ALA | PHE | ILE | VAL | ILE | SEP | ASP | ||||
2 | SEP | ASP | GLY | GLU | NH2 |
Entity 2, entity_2 95 residues - 11502.955 Da.
1 | MET | ALA | ASP | GLU | LYS | PRO | LYS | GLU | GLY | VAL | ||||
2 | LYS | THR | GLU | ASN | ASN | ASP | HIS | ILE | ASN | LEU | ||||
3 | LYS | VAL | ALA | GLY | GLN | ASP | GLY | SER | VAL | VAL | ||||
4 | GLN | PHE | LYS | ILE | LYS | ARG | HIS | THR | PRO | LEU | ||||
5 | SER | LYS | LEU | MET | LYS | ALA | TYR | CYS | GLU | ARG | ||||
6 | GLN | GLY | LEU | SER | MET | ARG | GLN | ILE | ARG | PHE | ||||
7 | ARG | PHE | ASP | GLY | GLN | PRO | ILE | ASN | GLU | THR | ||||
8 | ASP | THR | PRO | ALA | GLN | LEU | GLU | MET | GLU | ASP | ||||
9 | GLU | ASP | THR | ILE | ASP | VAL | PHE | GLN | GLN | GLN | ||||
10 | THR | GLY | GLY | VAL | TYR |
Samples:
sample_1: entity_1 1.2 mM; entity_2, [U-100% 13C; U-100% 15N], 0.4 mM
sample_conditions_1: ionic strength: 25 mM; pH: 7.3; pressure: 1 atm; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HCACO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.113, Goddard - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
AMBER v14, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure solution
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Related Database Links:
NCBI | Q96RL1 P61956 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts