BMRB Entry 18671
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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/BMR18671
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Title: Solution structure of the complex between the Sgt2 homodimerization domain and the Get5 UBL domain PubMed: 23142665
Deposition date: 2012-08-19 Original release date: 2012-11-20
Authors: Chartron, Justin; VanderVelde, David; Clemons, William
Citation: Chartron, Justin; VanderVelde, David; Clemons, William. "Structures of the Sgt2/SGTA dimerization domain with the Get5/UBL4A UBL domain reveal an interaction that forms a conserved dynamic interface." Cell Rep. 2, 1620-1632 (2012).
Assembly members:
Get5, polymer, 81 residues, 9170.889 Da.
Sgt2, polymer, 74 residues, 7889.790 Da.
Natural source: Common Name: Baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Get5: MVHLTLKKIQAPKFSIEHDF
SPSDTILQIKQHLISEEKAS
HISEIKLLLKGKVLHDNLFL
SDLKVTPANSTITVMIKPNL
E
Sgt2: SVDSASKEEIAALIVNYFSS
IVEKKEISEDGADSLNVAMD
CISEAFGFEREAVSGILGKS
EFKGQHLADILNSA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 522 |
15N chemical shifts | 136 |
1H chemical shifts | 948 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Get5 | 1 |
2 | Sgt2_1 | 2 |
3 | Sgt2_2 | 2 |
Entities:
Entity 1, Get5 81 residues - 9170.889 Da.
1 | MET | VAL | HIS | LEU | THR | LEU | LYS | LYS | ILE | GLN | ||||
2 | ALA | PRO | LYS | PHE | SER | ILE | GLU | HIS | ASP | PHE | ||||
3 | SER | PRO | SER | ASP | THR | ILE | LEU | GLN | ILE | LYS | ||||
4 | GLN | HIS | LEU | ILE | SER | GLU | GLU | LYS | ALA | SER | ||||
5 | HIS | ILE | SER | GLU | ILE | LYS | LEU | LEU | LEU | LYS | ||||
6 | GLY | LYS | VAL | LEU | HIS | ASP | ASN | LEU | PHE | LEU | ||||
7 | SER | ASP | LEU | LYS | VAL | THR | PRO | ALA | ASN | SER | ||||
8 | THR | ILE | THR | VAL | MET | ILE | LYS | PRO | ASN | LEU | ||||
9 | GLU |
Entity 2, Sgt2_1 74 residues - 7889.790 Da.
1 | SER | VAL | ASP | SER | ALA | SER | LYS | GLU | GLU | ILE | ||||
2 | ALA | ALA | LEU | ILE | VAL | ASN | TYR | PHE | SER | SER | ||||
3 | ILE | VAL | GLU | LYS | LYS | GLU | ILE | SER | GLU | ASP | ||||
4 | GLY | ALA | ASP | SER | LEU | ASN | VAL | ALA | MET | ASP | ||||
5 | CYS | ILE | SER | GLU | ALA | PHE | GLY | PHE | GLU | ARG | ||||
6 | GLU | ALA | VAL | SER | GLY | ILE | LEU | GLY | LYS | SER | ||||
7 | GLU | PHE | LYS | GLY | GLN | HIS | LEU | ALA | ASP | ILE | ||||
8 | LEU | ASN | SER | ALA |
Samples:
sample_1: Get5 1 mM; Sgt2, [U-100% 13C; U-100% 15N], 2 mM; Bis-Tris 10 mM; L-arginine 50 mM; L-glutamic acid 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_2: Get5 1 mM; Sgt2, [U-100% 13C; U-100% 15N], 2 mM; Bis-Tris 10 mM; L-arginine 50 mM; L-glutamic acid 50 mM; sodium azide 0.02%; polyacrylamide 3.5%; H2O 90%; D2O 10%
sample_3: Get5, [U-100% 13C; U-100% 15N], 1 mM; Sgt2 2 mM; Bis-Tris 10 mM; L-arginine 50 mM; L-glutamic acid 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_4: Get5, [U-100% 13C; U-100% 15N], 1 mM; Sgt2 2 mM; Bis-Tris 10 mM; L-arginine 50 mM; L-glutamic acid 50 mM; sodium azide 0.02%; polyacrylamide 3.5%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 mM; pH: 6.1; pressure: 1 atm; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | 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 |
2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
3D HNCO | sample_3 | isotropic | sample_conditions_1 |
3D (H)CCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_4 | anisotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
Analysis, CCPN - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS+, Cornilescu, Delaglio and Bax - data analysis
ARIA v2.3, Linge, O, . - refinement, structure solution
HADDOCK v2.1, Alexandre Bonvin - refinement, structure solution
TOPSPIN, Bruker Biospin - collection
PALES, Zweckstetter and Bax - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
BMRB | 18342 18669 18341 18670 |
PDB | |
DBJ | GAA26218 GAA26330 |
EMBL | CAA88151 CAA99130 CAY86179 CAA99195 CAY86295 |
GB | AHY77206 AJP41438 AJT70857 AJT71348 AJT71834 AAC49487 AHY77314 EDN63877 EDV10615 EDZ69384 |
REF | NP_014530 NP_014649 |
SP | Q12285 Q12118 |
TPG | DAA10672 DAA10789 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts