BMRB Entry 15689
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15689
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Lee, Woonghee; Jung, Jin-Won; Lee, Weontae. "The Automated Suite for Protein Structure by NMR Spectroscopy" .
Assembly members:
UBB, polymer, 103 residues, 11539.073 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 Vector: PET
Entity Sequences (FASTA):
UBB: GSLVPRGSMQIFVKTLTGKT
ITLEVEPSDTIENVKAKIQD
KEGIPPDQQRLIFAGKQLED
GRTLSEYNIQKESTLHLVLR
LRGYADLREDPDRQDHHPGS
GAQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 294 |
| 15N chemical shifts | 92 |
| 1H chemical shifts | 615 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UBB | 1 |
Entities:
Entity 1, UBB 103 residues - 11539.073 Da.
| 1 | GLY | SER | LEU | VAL | PRO | ARG | GLY | SER | MET | GLN | ||||
| 2 | ILE | PHE | VAL | LYS | THR | LEU | THR | GLY | LYS | THR | ||||
| 3 | ILE | THR | LEU | GLU | VAL | GLU | PRO | SER | ASP | THR | ||||
| 4 | ILE | GLU | ASN | VAL | LYS | ALA | LYS | ILE | GLN | ASP | ||||
| 5 | LYS | GLU | GLY | ILE | PRO | PRO | ASP | GLN | GLN | ARG | ||||
| 6 | LEU | ILE | PHE | ALA | GLY | LYS | GLN | LEU | GLU | ASP | ||||
| 7 | GLY | ARG | THR | LEU | SER | GLU | TYR | ASN | ILE | GLN | ||||
| 8 | LYS | GLU | SER | THR | LEU | HIS | LEU | VAL | LEU | ARG | ||||
| 9 | LEU | ARG | GLY | TYR | ALA | ASP | LEU | ARG | GLU | ASP | ||||
| 10 | PRO | ASP | ARG | GLN | ASP | HIS | HIS | PRO | GLY | SER | ||||
| 11 | GLY | ALA | GLN |
Samples:
sample_1: UBB, [U-98% 13C; U-98% 15N], 1 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert P. - refinement
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| BMRB | 11505 11547 15047 15410 15907 16582 16626 16895 17181 17439 17769 17919 18582 18583 18584 18610 18611 18737 19406 19412 25070 25123 26604 4245 4375 |
| PDB | |
| DBJ | BAA03983 BAA09860 BAA11842 BAA11843 BAA23486 |
| EMBL | CAA28495 CAA30815 CAA35999 CAA37227 CAA37599 |
| GB | AAA28154 AAA28997 AAA28998 AAA28999 AAA29000 |
| PIR | I50437 I51568 I65237 S13928 S21083 |
| PRF | 0412265A 1212243A 1212243B 1212243C 1212243D |
| REF | NP_001005123 NP_001006688 NP_001009117 NP_001009202 NP_001009286 |
| SP | P0C273 P0C275 P0C276 P0CG47 P0CG48 |
| TPE | CEL68433 CEL70397 CEL75964 CEL78064 |
| TPG | DAA18802 DAA20663 DAA20672 DAA24675 DAA28295 |
| AlphaFold | P0C273 P0C275 P0C276 P0CG47 P0CG48 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks