BMRB Entry 16478
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16478
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: Solution structure of UBA domain of XIAP PubMed: 19916060
Deposition date: 2009-09-04 Original release date: 2010-05-05
Authors: Hui, Sin-Kam; Tse, Man-Kit; Sze, Kong-Hung
Citation: Hui, Sin-Kam; Tse, Man-Kit; Yang, Yinhua; Wong, Benjamin Chun-Yu; Sze, Kong-Hung. "Backbone and side-chain 1H, 13C and 15N assignments of the ubiquitin-associated domain of human X-linked inhibitor of apoptosis protein." Biomol. NMR Assignments 4, 13-15 (2010).
Assembly members:
UBA, polymer, 104 residues, 11873.473 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):
UBA: GSAMADIGSEFEKTPSLTRR
IDDTIFQNPMVQEAIRMGFS
FKDIKKIMEEKIQISGSNYK
SLEVLVADLVNAQKDSMQDE
SSQTSLQKEISTEEQLRRLQ
EEKL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 445 |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 752 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UBA | 1 |
Entities:
Entity 1, UBA 104 residues - 11873.473 Da.
| 1 | GLY | SER | ALA | MET | ALA | ASP | ILE | GLY | SER | GLU | ||||
| 2 | PHE | GLU | LYS | THR | PRO | SER | LEU | THR | ARG | ARG | ||||
| 3 | ILE | ASP | ASP | THR | ILE | PHE | GLN | ASN | PRO | MET | ||||
| 4 | VAL | GLN | GLU | ALA | ILE | ARG | MET | GLY | PHE | SER | ||||
| 5 | PHE | LYS | ASP | ILE | LYS | LYS | ILE | MET | GLU | GLU | ||||
| 6 | LYS | ILE | GLN | ILE | SER | GLY | SER | ASN | TYR | LYS | ||||
| 7 | SER | LEU | GLU | VAL | LEU | VAL | ALA | ASP | LEU | VAL | ||||
| 8 | ASN | ALA | GLN | LYS | ASP | SER | MET | GLN | ASP | GLU | ||||
| 9 | SER | SER | GLN | THR | SER | LEU | GLN | LYS | GLU | ILE | ||||
| 10 | SER | THR | GLU | GLU | GLN | LEU | ARG | ARG | LEU | GLN | ||||
| 11 | GLU | GLU | LYS | LEU |
Samples:
sample_1: Bis-TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; PMSF 1 mM; UBA, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 100 mM; pH: 6.7; 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 | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAG36609 BAI46620 |
| GB | AAC50373 AAC50518 AAH32729 AAW62257 AAX29953 |
| REF | NP_001158 NP_001191330 XP_001086574 XP_003262340 XP_003779771 |
| SP | P98170 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts