BMRB Entry 17824
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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/BMR17824
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Title: Rbx1 PubMed: 22433864
Deposition date: 2011-08-02 Original release date: 2012-03-26
Authors: Spratt, Donald; Shaw, Gary
Citation: Spratt, Donald; Wu, Kenneth; Kovacev, Jordan; Pan, Zhen-Qiang; Shaw, Gary. "Selective recruitment of an E2~ubiquitin complex by an E3 ubiquitin ligase." J. Biol. Chem. 287, 17374-17385 (2012).
Assembly members:
Rbx1, polymer, 100 residues,   11159.5 Da.
ZN, 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):
Rbx1: GGGGTNSGAGKKRFEVKKSN
ASAQSAWDIVVDNCAICRNH
IMDLCIECQANQASATSEEC
TVAWGVCNHAFHFHCISRWL
KTRQVCPLDNREWEFQKYGH
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 321 | 
| 15N chemical shifts | 76 | 
| 1H chemical shifts | 451 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | Rbx1 | 1 | 
| 2 | ZINC ION_1 | 2 | 
| 3 | ZINC ION_2 | 2 | 
| 4 | ZINC ION_3 | 2 | 
Entities:
Entity 1, Rbx1 100 residues - 11159.5 Da.
Residues G9-G11 represent the non-native N-terminus of the protein after TEV cleavage to remove a 6His affinity tag. Residues G1-G8 are spacer residues that were added to maintain proper sequence numbering.
| 1 | GLY | GLY | GLY | GLY | THR | ASN | SER | GLY | ALA | GLY | |
| 2 | LYS | LYS | ARG | PHE | GLU | VAL | LYS | LYS | SER | ASN | |
| 3 | ALA | SER | ALA | GLN | SER | ALA | TRP | ASP | ILE | VAL | |
| 4 | VAL | ASP | ASN | CYS | ALA | ILE | CYS | ARG | ASN | HIS | |
| 5 | ILE | MET | ASP | LEU | CYS | ILE | GLU | CYS | GLN | ALA | |
| 6 | ASN | GLN | ALA | SER | ALA | THR | SER | GLU | GLU | CYS | |
| 7 | THR | VAL | ALA | TRP | GLY | VAL | CYS | ASN | HIS | ALA | |
| 8 | PHE | HIS | PHE | HIS | CYS | ILE | SER | ARG | TRP | LEU | |
| 9 | LYS | THR | ARG | GLN | VAL | CYS | PRO | LEU | ASP | ASN | |
| 10 | ARG | GLU | TRP | GLU | PHE | GLN | LYS | TYR | GLY | HIS | 
Entity 2, ZINC ION_1 - Zn - 65.409 Da.
| 1 | ZN | 
Samples:
sample_1: sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; entity_1, [U-98% 15N], 700 uM; H2O 90%; D2O 10%
sample_2: sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; Rbx1, [U-98% 13C; U-98% 15N], 700 uM; H2O 90%; D2O 10%
sample_3: sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; Rbx1, [U-98% 13C; U-98% 15N], 700 uM; D2O 100%
sample_conditions_1: ionic strength: 0.120 M; pH: 7.5; 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_3 | isotropic | sample_conditions_1 | 
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 | 
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 | 
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 | 
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 | 
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 | 
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 | 
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 | 
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 | 
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 | 
Software:
VNMRJ vVarian VnmrJ 2.2D, Varian - collection
NMRPipe v2009.015.15.35, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw vVer 5.0 Rev 2009.244.15.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v8.0.rc47 with Java 1.6.0_26, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
TALOS vTALOSPlus, Cornilescu, Delaglio and Bax - geometry optimization
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
 
Related Database Links:
| PDB | |
| GB | EAW60402 EKC33263 KFM64926 KFP48973 KFQ68825 | 
| REF | XP_004063570 XP_008474369 XP_010219658 XP_011232809 XP_011232810 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts