BMRB Entry 16050
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16050
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Ca-S100A1 interacting with TRTK12 PubMed: 19452629
Deposition date: 2008-12-02 Original release date: 2009-04-04
Authors: Wright, Nathan; Varney, Kristen; Cannon, Brian; Morgan, Michael; Weber, David
Citation: Wright, Nathan; Cannon, Brian; Wilder, P.; Morgan, Michael; Varney, Kristen; Zimmer, D.; Weber, David. "Solution structure of S100A1 bound to the CapZ peptide (TRTK12)" J. Mol. Biol. 386, 1265-1277 (2009).
Assembly members:
S100A1, polymer, 93 residues, 10439.711 Da.
TRTK12, polymer, 12 residues, 1477.742 Da.
CA, non-polymer, 40.078 Da.
Natural source: Common Name: 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):
S100A1: GSELETAMETLINVFHAHSG
KEGDKYKLSKKELKDLLQTE
LSSFLDVQKDADAVDKIMKE
LDENGDGEVDFQEFVVLVAA
LTVACNNFFWENS
TRTK12: TRTKIDWNKILS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 369 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 668 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1_1 | 1 |
| 2 | entity_1_2 | 1 |
| 3 | entity_2_1 | 2 |
| 4 | entity_2_2 | 2 |
| 5 | CALCIUM ION_1 | 3 |
| 6 | CALCIUM ION_2 | 3 |
| 7 | CALCIUM ION_3 | 3 |
Entities:
Entity 1, entity_1_1 93 residues - 10439.711 Da.
| 1 | GLY | SER | GLU | LEU | GLU | THR | ALA | MET | GLU | THR | ||||
| 2 | LEU | ILE | ASN | VAL | PHE | HIS | ALA | HIS | SER | GLY | ||||
| 3 | LYS | GLU | GLY | ASP | LYS | TYR | LYS | LEU | SER | LYS | ||||
| 4 | LYS | GLU | LEU | LYS | ASP | LEU | LEU | GLN | THR | GLU | ||||
| 5 | LEU | SER | SER | PHE | LEU | ASP | VAL | GLN | LYS | ASP | ||||
| 6 | ALA | ASP | ALA | VAL | ASP | LYS | ILE | MET | LYS | GLU | ||||
| 7 | LEU | ASP | GLU | ASN | GLY | ASP | GLY | GLU | VAL | ASP | ||||
| 8 | PHE | GLN | GLU | PHE | VAL | VAL | LEU | VAL | ALA | ALA | ||||
| 9 | LEU | THR | VAL | ALA | CYS | ASN | ASN | PHE | PHE | TRP | ||||
| 10 | GLU | ASN | SER |
Entity 2, entity_2_1 12 residues - 1477.742 Da.
| 1 | THR | ARG | THR | LYS | ILE | ASP | TRP | ASN | LYS | ILE | ||||
| 2 | LEU | SER |
Entity 3, CALCIUM ION_1 - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: D2O 10%; H2O 90%; CALCIUM ION 10 mM; DTT 10 mM; TRIS 10 mM; sodium chloride 25 mM; entity_1, [U-100% 13C; U-100% 15N], 500 uM; entity_2 1500 uM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; 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 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | anisotropic | sample_conditions_1 |
| IPAP-HSQC | sample_1 | anisotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 15296 4285 |
| PDB | |
| GB | AAB20539 AAB53657 EDM00555 |
| REF | NP_001007637 XP_006232665 |
| SP | P35467 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts