BMRB Entry 25576
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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/BMR25576
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Title: Solution structure of human SUMO1
Deposition date: 2015-04-24 Original release date: 2016-04-18
Authors: Naik, Mandar; Naik, Nandita; Shih, Hsiu-Ming; Huang, Tai-huang
Citation: Naik, Mandar; Naik, Nandita; Shih, Hsiu-Ming; Huang, Tai-huang. "Structures of human SUMO" Not known ., .-..
Assembly members:
SUMO1, polymer, 111 residues, 11149.640 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):
SUMO1: MGSSHHHHHHSQDPMSDQEA
KPSTEDLGDKKEGEYIKLKV
IGQDSSEIHFKVKMTTHLKK
LKESYCQRQGVPMNSLRFLF
EGQRIADNHTPKELGMEEED
VIEVYQEQTGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 433 |
| 15N chemical shifts | 104 |
| 1H chemical shifts | 697 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | human SUMO1 | 1 |
Entities:
Entity 1, human SUMO1 111 residues - 11149.640 Da.
Residues 1-14 (MGSSHHHHHHSQDP) represent a non-native purification tag. These residues were neither assigned nor included in structure calculation.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | GLN | ASP | PRO | MET | SER | ASP | GLN | GLU | ALA | ||||
| 3 | LYS | PRO | SER | THR | GLU | ASP | LEU | GLY | ASP | LYS | ||||
| 4 | LYS | GLU | GLY | GLU | TYR | ILE | LYS | LEU | LYS | VAL | ||||
| 5 | ILE | GLY | GLN | ASP | SER | SER | GLU | ILE | HIS | PHE | ||||
| 6 | LYS | VAL | LYS | MET | THR | THR | HIS | LEU | LYS | LYS | ||||
| 7 | LEU | LYS | GLU | SER | TYR | CYS | GLN | ARG | GLN | GLY | ||||
| 8 | VAL | PRO | MET | ASN | SER | LEU | ARG | PHE | LEU | PHE | ||||
| 9 | GLU | GLY | GLN | ARG | ILE | ALA | ASP | ASN | HIS | THR | ||||
| 10 | PRO | LYS | GLU | LEU | GLY | MET | GLU | GLU | GLU | ASP | ||||
| 11 | VAL | ILE | GLU | VAL | TYR | GLN | GLU | GLN | THR | GLY | ||||
| 12 | GLY |
Samples:
CN: SUMO1, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%
N: SUMO1, [U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%
Phage: SUMO1, [U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; Pf1 phage 10 ± 0.1 w/v; H2O 90%; D2O 10%
Unlabeled: SUMO10.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%
Default: pH: 6.5; pressure: 1 atm; temperature: 290 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | N | isotropic | Default |
| 2D 1H-13C HSQC | CN | isotropic | Default |
| 3D HNCO | CN | isotropic | Default |
| 3D HNCA | CN | isotropic | Default |
| 3D HN(CO)CA | CN | isotropic | Default |
| 3D HNCACB | CN | isotropic | Default |
| 3D CBCA(CO)NH | CN | isotropic | Default |
| 3D HCCH-TOCSY | CN | isotropic | Default |
| 3D HCCH-COSY | CN | isotropic | Default |
| 3D HBHAcoNH | CN | isotropic | Default |
| 2D-hbCBcgcdHD | CN | isotropic | Default |
| 2D-hbCBcgcdceHE | CN | isotropic | Default |
| 3D 1H-15N TOCSY | CN | isotropic | Default |
| 2D 1H-1H NOESY | Unlabeled | isotropic | Default |
| 3D 1H-15N NOESY | CN | isotropic | Default |
| 3D 1H-13C NOESY | CN | isotropic | Default |
| 2D 1H-15N HSQC IPAP | Phage | anisotropic | Default |
Software:
TOPSPIN v3.2, Bruker Biospin - collection, processing
SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking
CYANA v3.9, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution
X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts