Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18898
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Citation: Joseph, Soumya; Kwan, Ann; Mackay, Joel; Cubeddu, Liza; Matthews, Jacqueline. "Backbone and side-chain assignments of a tethered complex between LMO4 and DEAF-1." Biomol. NMR Assignments ., .-. (2013).
PubMed: 23417771
Assembly members:
LMO4-DEAF-1, polymer, 96 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-2T
Entity Sequences (FASTA):
LMO4-DEAF-1: GSYIRLFGNSGACSACGQSI
PASELVMRAQGNVYHLKCFT
CSTCRNRLVPGDRFHYINGS
LFCEHDRPTALINGGSGGSG
SIAPFPEAALPTSHPK
| Data type | Count |
| 13C chemical shifts | 354 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 608 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LMO4-DEAF-1 tethered complex | 1 |
| 2 | Zn2+, 1 | 2 |
| 3 | Zn2+, 2 | 2 |
Entity 1, LMO4-DEAF-1 tethered complex 96 residues - Formula weight is not available
G1 and S2 are non-native residues that remain from thrombin cleavage of the affinity tag. Residues Y3-N73 correspond to murine LMO4 residues 77-147. Residues G74-S81 correspond to a synthetic G/S linker peptide. Residues I82-K96 corresond to murine DEAF1 residues 404-418.
| 1 | GLY | SER | TYR | ILE | ARG | LEU | PHE | GLY | ASN | SER | ||||
| 2 | GLY | ALA | CYS | SER | ALA | CYS | GLY | GLN | SER | ILE | ||||
| 3 | PRO | ALA | SER | GLU | LEU | VAL | MET | ARG | ALA | GLN | ||||
| 4 | GLY | ASN | VAL | TYR | HIS | LEU | LYS | CYS | PHE | THR | ||||
| 5 | CYS | SER | THR | CYS | ARG | ASN | ARG | LEU | VAL | PRO | ||||
| 6 | GLY | ASP | ARG | PHE | HIS | TYR | ILE | ASN | GLY | SER | ||||
| 7 | LEU | PHE | CYS | GLU | HIS | ASP | ARG | PRO | THR | ALA | ||||
| 8 | LEU | ILE | ASN | GLY | GLY | SER | GLY | GLY | SER | GLY | ||||
| 9 | SER | ILE | ALA | PRO | PHE | PRO | GLU | ALA | ALA | LEU | ||||
| 10 | PRO | THR | SER | HIS | PRO | LYS |
Entity 2, Zn2+, 1 - Zn - 65.409 Da.
| 1 | ZN |
sample_LMO4-DEAF-1: LMO4-DEAF-1, [U-13C; U-15N], 0.5 ± 0.2 mM; LMO4-DEAF-1, [U-15N], 0.5 ± 0.2 mM; LMO4-DEAF-1 0.5 ± 0.2 mM; sodium acetate 20 ± 1 mM; sodium chloride 35 ± 1 mM; TCEP 1 ± 0.5 mM; H2O 55 ± 1 M; D2O 5 ± 1 M
condition_LMO4-DEAF-1: ionic strength: 0.1 M; pH: 5.0; pressure: 1 atm; temperature: 298 K
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 2D 1H-13C HSQC | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 2D 1H-1H TOCSY | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 2D DQF-COSY | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 2D 1H-1H NOESY | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 3D CBCA(CO)NH | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 3D HNCO | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 3D HNCACB | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 3D H(CCO)NH | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 3D HCCH-TOCSY | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 3D 1H-15N NOESY | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
| 3D 1H-13C NOESY aliphatic | sample_LMO4-DEAF-1 | isotropic | condition_LMO4-DEAF-1 |
SPARKY, Goddard - chemical shift assignment, data analysis
| BMRB | 19415 |
| PDB | |
| DBJ | BAC37938 BAE23609 BAE35210 BAF85267 BAF93844 |
| EMBL | CAF90424 CAJ82708 |
| GB | AAB51073 AAC62958 AAC83789 AAC98510 AAH03488 |
| REF | NP_001004922 NP_001009708 NP_001029923 NP_001087890 NP_001106156 |
| SP | P61968 P61969 Q3SWZ8 Q6DJ06 |
| TPG | DAA31414 |
| AlphaFold | P61968 P61969 Q3SWZ8 Q6DJ06 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks