BMRB Entry 18082
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18082
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Title: SOLUTION NMR-DERIVED STRUCTURE OF CALMODULIN N-LOBE BOUND WITH ER alpha PEPTIDE PubMed: 22275375
Deposition date: 2011-11-15 Original release date: 2012-01-30
Authors: Zhang, Yonghong
Citation: Zhang, Yonghong; Li, Zhigang; Sacks, David; Ames, James. "Structural basis for Ca2+-induced activation and dimerization of estrogen receptor by calmodulin." J. Biol. Chem. 287, 9336-9344 (2012).
Assembly members:
Calmodulin N-Lobe, polymer, 80 residues, 8914.874 Da.
ER alpha peptide, polymer, 19 residues, 2202.663 Da.
CALCIUM ION, non-polymer, 40.078 Da.
Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus laevis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Calmodulin N-Lobe: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTD
ER alpha peptide: RAANLWPSPLMIKRSKKNS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 157 |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 295 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Calmodulin N-Lobe | 1 |
| 2 | ER alpha peptide | 2 |
| 3 | CA2_1 | 3 |
| 4 | CA2_2 | 3 |
Entities:
Entity 1, Calmodulin N-Lobe 80 residues - 8914.874 Da.
| 1 | ALA | ASP | GLN | LEU | THR | GLU | GLU | GLN | ILE | ALA | |
| 2 | GLU | PHE | LYS | GLU | ALA | PHE | SER | LEU | PHE | ASP | |
| 3 | LYS | ASP | GLY | ASP | GLY | THR | ILE | THR | THR | LYS | |
| 4 | GLU | LEU | GLY | THR | VAL | MET | ARG | SER | LEU | GLY | |
| 5 | GLN | ASN | PRO | THR | GLU | ALA | GLU | LEU | GLN | ASP | |
| 6 | MET | ILE | ASN | GLU | VAL | ASP | ALA | ASP | GLY | ASN | |
| 7 | GLY | THR | ILE | ASP | PHE | PRO | GLU | PHE | LEU | THR | |
| 8 | MET | MET | ALA | ARG | LYS | MET | LYS | ASP | THR | ASP |
Entity 2, ER alpha peptide 19 residues - 2202.663 Da.
| 1 | ARG | ALA | ALA | ASN | LEU | TRP | PRO | SER | PRO | LEU | ||||
| 2 | MET | ILE | LYS | ARG | SER | LYS | LYS | ASN | SER |
Entity 3, CA2_1 - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: Cal_N, [U-100% 13C; U-100% 15N], 1 mM; H20 90%; D20 10%; Tris-d11 20 mM; sodium chloride 50 mM; CaCl2 5 mM
sample_conditions_1: ionic strength: 0.02 M; pH: 7.0; pressure: 1 atm; temperature: 310 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 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 18302 4174 |
| PDB | |
| EMBL | CAA29381 CAB65357 CCD82979 CUA69889 |
| GB | AAH53790 ABY16748 ABY16749 ABY16752 ACH46202 |
| REF | XP_001869424 XP_001995129 XP_002772218 XP_006032607 XP_006137175 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts