BMRB Entry 11443
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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/BMR11443
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Title: Crystal structure of the UBA domain of p62 and its interaction with ubiquitin
Deposition date: 2011-06-09 Original release date: 2011-07-05
Authors: Isogai, Shin; Morimoto, Daichi; Arita, Kyouhei; Unzai, Satoru; Tenno, Takeshi; Hasegawa, Jun; Sou, Yu-shin; Komatsu, Masaaki; Tanaka, Keiji; Shirakawa, Masahiro; Tochio, Hidehito
Citation: Isogai, Shin; Morimoto, Daichi; Arita, Kyouhei; Unzai, Satoru; Tenno, Takeshi; Sou, Yu-shin; Komatsu, Masaaki; Tanaka, Keiji; Shirakawa, Masahiro; Tochio, Hidehito. "Crystal structure of the UBA domain of p62 and its interaction with ubiquitin" To be Published ., .-..
Assembly members:
P62/SEQUESTOSOME-1, polymer, 53 residues, 5817.546 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 Vector: PGEX-6P1
Entity Sequences (FASTA):
P62/SEQUESTOSOME-1: GPLGSEADPRLIESLSQMLS
MGFSDEGGWLTRLLQTKNYD
IGAALDTIQYSKH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 219 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 356 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | P62/SEQUESTOSOME-1 | 1 |
Entities:
Entity 1, P62/SEQUESTOSOME-1 53 residues - 5817.546 Da.
Expression Tag sequence GPLGS
| 1 | GLY | PRO | LEU | GLY | SER | GLU | ALA | ASP | PRO | ARG | ||||
| 2 | LEU | ILE | GLU | SER | LEU | SER | GLN | MET | LEU | SER | ||||
| 3 | MET | GLY | PHE | SER | ASP | GLU | GLY | GLY | TRP | LEU | ||||
| 4 | THR | ARG | LEU | LEU | GLN | THR | LYS | ASN | TYR | ASP | ||||
| 5 | ILE | GLY | ALA | ALA | LEU | ASP | THR | ILE | GLN | TYR | ||||
| 6 | SER | LYS | HIS |
Samples:
sample_1: P62/SEQUESTOSOME-1, [U-95% 13C; U-95% 15N], 0.4 mM; Ubiquitin 2.4 mM; potassium phosphate 20 mM; potassium chloride 5 mM; EDTA 1 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0.025 M; pH: 6.8; pressure: 1 atm; temperature: 298 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)N 3D C(CO)NH | 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 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, GUNTERT, MUMENTHALER - refinement, structure solution
SPARKY v3.113, Goddard - data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment
ATNOS, Herrmann and Wuthrich - peak picking
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- BRUKER AVANCE 700 MHz
Related Database Links:
| BMRB | 11149 15591 15592 |
| PDB | |
| DBJ | BAC26183 |
| GB | AAH06019 AKI70216 EDL33719 EHH27114 EHH54825 |
| REF | NP_001277698 XP_006246276 XP_006246277 XP_008273207 XP_008987787 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts