BMRB Entry 19606
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                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19606
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Title: Solution Structure of the UBA Domain of Human NBR1 PubMed: 24692539
Deposition date: 2013-11-09 Original release date: 2014-04-07
Authors: Walinda, Erik; Morimoto, Daichi; Sugase, Kenji; Komatsu, Masaaki; Tochio, Hidehito; Shirakawa, Masahiro
Citation: Walinda, Erik; Morimoto, Daichi; Sugase, Kenji; Konuma, Tsuyoshi; Tochio, Hidehito; Shirakawa, Masahiro. "Solution Structure of the Ubiquitin-associated (UBA) Domain of Human Autophagy Receptor NBR1 and its Interaction with Ubiquitin and Polyubiquitin." J. Biol. Chem. ., .-. (2014).
Assembly members:
entity, polymer, 52 residues,   5918.827 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: GPLGSSEDQTAALMAHLFEM
GFCDRQLNLRLLKKHNYNIL
QVVTELLQLNNN
- assigned_chemical_shifts
 
| Data type | Count | 
| 1H chemical shifts | 356 | 
| 13C chemical shifts | 176 | 
| 15N chemical shifts | 50 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | UBA Domain of Human NBR1 | 1 | 
Entities:
Entity 1, UBA Domain of Human NBR1 52 residues - 5918.827 Da.
| 1 | GLY | PRO | LEU | GLY | SER | SER | GLU | ASP | GLN | THR | ||||
| 2 | ALA | ALA | LEU | MET | ALA | HIS | LEU | PHE | GLU | MET | ||||
| 3 | GLY | PHE | CYS | ASP | ARG | GLN | LEU | ASN | LEU | ARG | ||||
| 4 | LEU | LEU | LYS | LYS | HIS | ASN | TYR | ASN | ILE | LEU | ||||
| 5 | GLN | VAL | VAL | THR | GLU | LEU | LEU | GLN | LEU | ASN | ||||
| 6 | ASN | ASN | 
Samples:
sample_1: potassium phosphate 20 mM; potassium chloride 5 mM; EDTA 1 mM; benzamidine 1 mM; DTT 1 mM; sodium azide 0.02%; NBR1 residues 913-959, [U-100% 13C; U-100% 15N], 1.2 mM; H2O 95%; D2O 5%
aniso: potassium phosphate 20 mM; potassium chloride 5 mM; EDTA 1 mM; benzamidine 1 mM; DTT 1 mM; sodium azide 0.02%; NBR1 residues 913-959, [U-100% 13C; U-100% 15N], 0.5 mM; Pf1 phage 12.5 mg/mL; sodium chloride 150 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 6.6; 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 aliphatic | sample_1 | isotropic | sample_conditions_1 | 
| 2D 1H-13C HSQC aromatic | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 | 
| 2D 1H-15N HSQC IPAP | aniso | anisotropic | sample_conditions_1 | 
| 2D 1H-15N HSQC IPAP | sample_1 | isotropic | sample_conditions_1 | 
Software:
TOPSPIN v2.0, Bruker Biospin - collection
TALOS, Cornilescu, Delaglio and Bax - structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MAGRO, Dr. Naohiro Kobayashi - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
 
Related Database Links:
| PDB | |
| DBJ | BAA06417 BAF82694 BAG09582 BAH12580 | 
| EMBL | CAA54274 CAH90613 | 
| GB | AAI49980 AAS15047 EAW60946 EAW60947 EAW60949 | 
| REF | NP_001093837 NP_001127309 NP_005890 NP_114068 XP_001097043 | 
| SP | Q14596 Q5RC94 | 
| TPG | DAA18460 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts