BMRB Entry 52044
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52044
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Citation: Miles, Jennifer; Batchelor, Matthew; Bayliss, Richard. "Working title - Interaction between CEP192 and Aurora-A" EMBO J. ., .-..
Assembly members:
entity_1, polymer, 95 residues, Formula weight is not available
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: pET30TEV-SUMO
Entity Sequences (FASTA):
entity_1: GSMIWSPTCERRTCECHESI
EKNKDKTDLPQSVVYQNEEG
RWVTDLAYYTSFNSKQNLNV
SLSDEMNEDFRSGSEAFDLI
AQDEEEFNKEHQFIQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 276 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 315 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CEP192 | 1 |
Entities:
Entity 1, CEP192 95 residues - Formula weight is not available
CEP192 sequence starts I442 (4th residue in sequence)
| 1 | GLY | SER | MET | ILE | TRP | SER | PRO | THR | CYS | GLU | ||||
| 2 | ARG | ARG | THR | CYS | GLU | CYS | HIS | GLU | SER | ILE | ||||
| 3 | GLU | LYS | ASN | LYS | ASP | LYS | THR | ASP | LEU | PRO | ||||
| 4 | GLN | SER | VAL | VAL | TYR | GLN | ASN | GLU | GLU | GLY | ||||
| 5 | ARG | TRP | VAL | THR | ASP | LEU | ALA | TYR | TYR | THR | ||||
| 6 | SER | PHE | ASN | SER | LYS | GLN | ASN | LEU | ASN | VAL | ||||
| 7 | SER | LEU | SER | ASP | GLU | MET | ASN | GLU | ASP | PHE | ||||
| 8 | ARG | SER | GLY | SER | GLU | ALA | PHE | ASP | LEU | ILE | ||||
| 9 | ALA | GLN | ASP | GLU | GLU | GLU | PHE | ASN | LYS | GLU | ||||
| 10 | HIS | GLN | PHE | ILE | GLN |
Samples:
sample_1: CEP192 442-533, [U-99% 13C; U-99% 15N], 75 uM; (K/H)3PO4 10 mM; NaCl 150 mM; TCEP 0.5 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR vAnalysis v 2.5 - chemical shift assignment
NMRPipe - processing
TOPSPIN - collection
NMR spectrometers:
- Oxford/Bruker Avance 750 MHz
- Oxford/Bruker Avance 750 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks