BMRB Entry 25219
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25219
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Title: Solution Structure of the UBM1 domain of human HUWE1/ARF-BP1
Deposition date: 2014-09-12 Original release date: 2015-09-14
Authors: Farhadi, Sahar; Khatun, Rahima; Lemak, Alexander; Kaustov, Lilia; Ramabadran, Raghav; Hunter, Howard; Sheng, Yi
Citation: Khatun, Rahima; Sheng, Yi. "Solution structure of Ubiquitin Binding Motif of human Arf-bp1" Not known ., .-..
Assembly members:
entity, polymer, 53 residues, 5663.236 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):
entity: TSSEEEDPLAGISLPEGVDP
SFLAALPDDIRREVLQNQLG
IRPPTRTAPSTNS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 195 |
| 15N chemical shifts | 45 |
| 1H chemical shifts | 325 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 53 residues - 5663.236 Da.
| 1 | THR | SER | SER | GLU | GLU | GLU | ASP | PRO | LEU | ALA | ||||
| 2 | GLY | ILE | SER | LEU | PRO | GLU | GLY | VAL | ASP | PRO | ||||
| 3 | SER | PHE | LEU | ALA | ALA | LEU | PRO | ASP | ASP | ILE | ||||
| 4 | ARG | ARG | GLU | VAL | LEU | GLN | ASN | GLN | LEU | GLY | ||||
| 5 | ILE | ARG | PRO | PRO | THR | ARG | THR | ALA | PRO | SER | ||||
| 6 | THR | ASN | SER |
Samples:
sample_1: entity, [U-13C; U-15N], 0.4 mM; sodium chloride 300 mM; potassium chloride 2.7 mM; sodium phosphate 10 mM; potassium phosphate 2 mM; CHAPS 0.05 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 300 mM; pH: 6.5; pressure: 1 atm; temperature: 273 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | 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:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
FMCGUI, Lemak A., Gutmanas A., Chitayat S., Karra M., Far s C., Sunnerhagen M., and Arrowsmith CH - chemical shift assignment, refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| PDB | |
| DBJ | BAA20771 BAC06833 |
| EMBL | CAI39580 CAI39581 CAI42354 CAI42654 CAI42656 |
| GB | AAF28950 AAV90838 AAX24125 AAY98258 EAW93160 |
| REF | NP_001103474 NP_001253681 NP_113584 XP_001914766 XP_002831735 |
| SP | Q7Z6Z7 |
| TPG | DAA12802 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts