BMRB Entry 19724
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19724
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Citation: Salavei, Pavel; Bentrop, Detlef; Reth, Michael; Fakler, Bernd. "A heterodimeric construct mimicking the cytoplasmic region of the B-cell antigen receptor complex-associated protein" .
Assembly members:
cytoplasmic_Ig-alpha_polypeptide, polymer, 99 residues, Formula weight is not available
cytoplasmic_Ig-beta_polypeptide, polymer, 86 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: pET23a
Entity Sequences (FASTA):
cytoplasmic_Ig-alpha_polypeptide: SGGVAQLRERVKTLRAQNYE
LESEVQRLREQVAQLSGGRK
RWQNEKLGLDAGDEYEDENL
YEGLNLDDCSMYEDISRGLQ
GTYQDVGSLNIGDVQLEKP
cytoplasmic_Ig-beta_polypeptide: SGGVDELQAEVDQLQDENYA
LKTKVAQLRKKVEKLSGGDK
DDSKAGMEEDHTYEGLDIDQ
TATYEDIVTLRTGEVKWSVG
EHPGQE
- assigned_chemical_shifts
- heteronucl_NOEs
| Data type | Count |
| 13C chemical shifts | 119 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 283 |
| heteronuclear NOE values | 79 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ig-alpha Ig-beta construct, subunit 1 | 1 |
| 2 | Ig-alpha Ig-beta construct, subunit 2 | 2 |
Entities:
Entity 1, Ig-alpha Ig-beta construct, subunit 1 99 residues - Formula weight is not available
Residues 1-3 represent a linker to an affinity tag that was removed by proteolysis. Residues 4-35 are a coiled-coil heterodimerization domain (A2, see citation 3 and 1, respectively). Residues 36-38 represent a linker. Residues 39-99 are the cytoplasmic region of human Ig-alpha and contain an immunoreceptor tyrosine-based activation motif (ITAM).
| 1 | SER | GLY | GLY | VAL | ALA | GLN | LEU | ARG | GLU | ARG | ||||
| 2 | VAL | LYS | THR | LEU | ARG | ALA | GLN | ASN | TYR | GLU | ||||
| 3 | LEU | GLU | SER | GLU | VAL | GLN | ARG | LEU | ARG | GLU | ||||
| 4 | GLN | VAL | ALA | GLN | LEU | SER | GLY | GLY | ARG | LYS | ||||
| 5 | ARG | TRP | GLN | ASN | GLU | LYS | LEU | GLY | LEU | ASP | ||||
| 6 | ALA | GLY | ASP | GLU | TYR | GLU | ASP | GLU | ASN | LEU | ||||
| 7 | TYR | GLU | GLY | LEU | ASN | LEU | ASP | ASP | CYS | SER | ||||
| 8 | MET | TYR | GLU | ASP | ILE | SER | ARG | GLY | LEU | GLN | ||||
| 9 | GLY | THR | TYR | GLN | ASP | VAL | GLY | SER | LEU | ASN | ||||
| 10 | ILE | GLY | ASP | VAL | GLN | LEU | GLU | LYS | PRO |
Entity 2, Ig-alpha Ig-beta construct, subunit 2 86 residues - Formula weight is not available
Residues 1-3 represent a linker to an affinity tag that was removed by proteolysis. Residues 4-35 are a coiled-coil heterodimerization domain (B1, see citation 3 and 1, respectively). Residues 36-38 represent a linker. Residues 39-86 are the cytoplasmic region of human Ig-beta and contain an immunoreceptor tyrosine-based activation motif (ITAM).
| 1 | SER | GLY | GLY | VAL | ASP | GLU | LEU | GLN | ALA | GLU | ||||
| 2 | VAL | ASP | GLN | LEU | GLN | ASP | GLU | ASN | TYR | ALA | ||||
| 3 | LEU | LYS | THR | LYS | VAL | ALA | GLN | LEU | ARG | LYS | ||||
| 4 | LYS | VAL | GLU | LYS | LEU | SER | GLY | GLY | ASP | LYS | ||||
| 5 | ASP | ASP | SER | LYS | ALA | GLY | MET | GLU | GLU | ASP | ||||
| 6 | HIS | THR | TYR | GLU | GLY | LEU | ASP | ILE | ASP | GLN | ||||
| 7 | THR | ALA | THR | TYR | GLU | ASP | ILE | VAL | THR | LEU | ||||
| 8 | ARG | THR | GLY | GLU | VAL | LYS | TRP | SER | VAL | GLY | ||||
| 9 | GLU | HIS | PRO | GLY | GLN | GLU |
Samples:
sample_1: cytoplasmic Ig-alpha polypeptide 0.5 mM; cytoplasmic Ig-beta polypeptide, [U-98% 13C; U-98% 15N], 0.5 mM; sodium phosphate 50 mM
sample_2: cytoplasmic Ig-alpha polypeptide 0.25 mM; cytoplasmic Ig-beta polypeptide, [U-98% 13C; U-98% 15N], 0.25 mM; sodium phosphate 50 mM
sample_3: cytoplasmic Ig-alpha polypeptide 0.3 mM; cytoplasmic Ig-beta polypeptide, [U-98% 15N], 0.3 mM; sodium phosphate 50 mM
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 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 HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N heteroNOE | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - NMR data acquisition
CARA vv1.8.4.2, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks