BMRB Entry 25382
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25382
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Title: UBX-L domain of VCIP135
Deposition date: 2014-12-07 Original release date: 2016-07-11
Authors: Iwazu, Takahiro; Murayama, Shuhei; Igarashi, Ryuji; Hrioaki, Hidekazu; Shirakawa, Masahiro; Tochio, Hidehito
Citation: Iwazu, Takahiro; Murayama, Shuhei; Igarashi, Ryuji; Hrioaki, Hidekazu; Shirakawa, Masahiro; Tochio, Hidehito. "Structure and interaction mode of the UBX-L domain of VCIP135 determined by solution NMR spectroscopy" Sci. Rep. ., .-..
Assembly members:
VCIP135 UBX, polymer, 86 residues, 9331.919 Da.
Natural source: Common Name: Norway Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
VCIP135 UBX: GSDHSKEKKIRITTNDGRQS
MVTLKSSTTFFELQESIARE
FNIPPYLQCIRYGFPPKELM
PPQAGMEKEPVPLQHGDRIT
IEILKG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 316 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 638 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | VCIP135 UBX | 1 |
Entities:
Entity 1, VCIP135 UBX 86 residues - 9331.919 Da.
| 1 | GLY | SER | ASP | HIS | SER | LYS | GLU | LYS | LYS | ILE | ||||
| 2 | ARG | ILE | THR | THR | ASN | ASP | GLY | ARG | GLN | SER | ||||
| 3 | MET | VAL | THR | LEU | LYS | SER | SER | THR | THR | PHE | ||||
| 4 | PHE | GLU | LEU | GLN | GLU | SER | ILE | ALA | ARG | GLU | ||||
| 5 | PHE | ASN | ILE | PRO | PRO | TYR | LEU | GLN | CYS | ILE | ||||
| 6 | ARG | TYR | GLY | PHE | PRO | PRO | LYS | GLU | LEU | MET | ||||
| 7 | PRO | PRO | GLN | ALA | GLY | MET | GLU | LYS | GLU | PRO | ||||
| 8 | VAL | PRO | LEU | GLN | HIS | GLY | ASP | ARG | ILE | THR | ||||
| 9 | ILE | GLU | ILE | LEU | LYS | GLY |
Samples:
sample_1: VCIP135 UBX, [U-13C; U-15N], 1.86 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-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 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker DRX 700 MHz
- Bruker DPX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts