BMRB Entry 25553
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25553
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Title: Docked structure between SUMO1 and ZZ-domain from CBP PubMed: 27129204
Deposition date: 2015-03-26 Original release date: 2016-06-01
Authors: Diehl, C.
Citation: Diehl, C.; Akke, M.; Bekker-Jensen, S.; Mailand, N.; Streicher, W.; Wikstrom, M.. "Structural Analysis of a Complex between Small Ubiquitin-like Modifier 1 (SUMO1) and the ZZ Domain of CREB-binding Protein (CBP/p300) Reveals a New Interaction Surface on SUMO" J. Biol. Chem. 291, 12658-12672 (2016).
Assembly members:
entity_1, polymer, 100 residues, 11518.051 Da.
entity_2, polymer, 53 residues, 6315.152 Da.
ZINC ION, non-polymer, 65.409 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_1: MSDQEAKPSTEDLGDKKEGE
YIKLKVIGQDSSEIHFKVKM
TTHLKKLKESYCQRQGVPMN
SLRFLFEGQRIADNHTPKEL
GMEEEDVIEVYQEQTGHSTV
entity_2: GQDRFVYTCNECKHHVETRW
HCTVCEDYDLCINCYNTKSH
AHKMVKWGLGLDD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 14 |
| 15N chemical shifts | 92 |
| 1H chemical shifts | 92 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
| 3 | ZN_1 | 3 |
| 4 | ZN_2 | 3 |
Entities:
Entity 1, entity_1 100 residues - 11518.051 Da.
| 1 | MET | SER | ASP | GLN | GLU | ALA | LYS | PRO | SER | THR | |
| 2 | GLU | ASP | LEU | GLY | ASP | LYS | LYS | GLU | GLY | GLU | |
| 3 | TYR | ILE | LYS | LEU | LYS | VAL | ILE | GLY | GLN | ASP | |
| 4 | SER | SER | GLU | ILE | HIS | PHE | LYS | VAL | LYS | MET | |
| 5 | THR | THR | HIS | LEU | LYS | LYS | LEU | LYS | GLU | SER | |
| 6 | TYR | CYS | GLN | ARG | GLN | GLY | VAL | PRO | MET | ASN | |
| 7 | SER | LEU | ARG | PHE | LEU | PHE | GLU | GLY | GLN | ARG | |
| 8 | ILE | ALA | ASP | ASN | HIS | THR | PRO | LYS | GLU | LEU | |
| 9 | GLY | MET | GLU | GLU | GLU | ASP | VAL | ILE | GLU | VAL | |
| 10 | TYR | GLN | GLU | GLN | THR | GLY | HIS | SER | THR | VAL |
Entity 2, entity_2 53 residues - 6315.152 Da.
| 1 | GLY | GLN | ASP | ARG | PHE | VAL | TYR | THR | CYS | ASN | ||||
| 2 | GLU | CYS | LYS | HIS | HIS | VAL | GLU | THR | ARG | TRP | ||||
| 3 | HIS | CYS | THR | VAL | CYS | GLU | ASP | TYR | ASP | LEU | ||||
| 4 | CYS | ILE | ASN | CYS | TYR | ASN | THR | LYS | SER | HIS | ||||
| 5 | ALA | HIS | LYS | MET | VAL | LYS | TRP | GLY | LEU | GLY | ||||
| 6 | LEU | ASP | ASP |
Entity 3, ZN_1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: entity_1 mM; entity_2 mM; MES 20 mM; H2O 93%; D2O, [U-2H], 7%
sample_2: entity_1 mM; entity_2 mM; MES 20 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 15N IPAP-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 15N IPAP-HSQC | sample_2 | anisotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts