BMRB Entry 18297
Click here to enlarge.
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/BMR18297
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition PubMed: 22821745
Deposition date: 2012-02-27 Original release date: 2012-08-29
Authors: Elgin, Emine; Peterson, Francis; Volkman, Brian
Citation: Elgin, E. Sonay; Sokmen, Nazl; Peterson, Francis; Volkman, Brian; Da, Cada; Haas, Arthur. "E2-binding surface on Uba3 -grasp domain undergoes a conformational transition." Proteins 80, 2482-2487 (2012).
Assembly members:
Uba3, polymer, 97 residues, 10658.173 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Uba3: GSQLPQNIQFSPSAKLQEVL
DYLTNSASLQMKSPAITATL
EGKNRTLYLQSVTSIEERTR
PNLSKTLKELGLVDGQELAV
ADVTTPQTVLFKLHFTS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 367 |
| 15N chemical shifts | 82 |
| 1H chemical shifts | 591 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Uba3 | 1 |
Entities:
Entity 1, Uba3 97 residues - 10658.173 Da.
The N-terminal GS dipeptide is a cloning artifact.
| 1 | GLY | SER | GLN | LEU | PRO | GLN | ASN | ILE | GLN | PHE | ||||
| 2 | SER | PRO | SER | ALA | LYS | LEU | GLN | GLU | VAL | LEU | ||||
| 3 | ASP | TYR | LEU | THR | ASN | SER | ALA | SER | LEU | GLN | ||||
| 4 | MET | LYS | SER | PRO | ALA | ILE | THR | ALA | THR | LEU | ||||
| 5 | GLU | GLY | LYS | ASN | ARG | THR | LEU | TYR | LEU | GLN | ||||
| 6 | SER | VAL | THR | SER | ILE | GLU | GLU | ARG | THR | ARG | ||||
| 7 | PRO | ASN | LEU | SER | LYS | THR | LEU | LYS | GLU | LEU | ||||
| 8 | GLY | LEU | VAL | ASP | GLY | GLN | GLU | LEU | ALA | VAL | ||||
| 9 | ALA | ASP | VAL | THR | THR | PRO | GLN | THR | VAL | LEU | ||||
| 10 | PHE | LYS | LEU | HIS | PHE | THR | SER |
Samples:
sample_1: Uba3, [U-100% 13C; U-100% 15N], 0.4 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%; sodium azide 90%; sodium azide 10%
sample_conditions_1: ionic strength: 127 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | 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 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
XEASY, Bartels et al. - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA33144 BAC27905 BAC33258 BAE35036 BAE38920 |
| EMBL | CAB55996 CAG38568 CAH90059 CAH92113 CAH92482 |
| GB | AAC27323 AAC27648 AAH02002 AAH22853 AAH80776 |
| REF | NP_001069042 NP_001104576 NP_001126234 NP_001128861 NP_001252890 |
| SP | Q5R4A0 Q8C878 Q8TBC4 Q99MI7 |
| TPG | DAA17089 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts