BMRB Entry 17262
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17262
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Title: SOLUTION STRUCTURE OF CALCIUM BOUND S100A16 PubMed: 21046186
Deposition date: 2010-10-22 Original release date: 2010-11-15
Authors: Babini, Elena; Bertini, Ivano; Borsi, Valentina; Calderone, Vito; Hu, Xiaoyu; Luchinat, Claudio; Parigi, Giacomo
Citation: Babini, Elena; Bertini, Ivano; Borsi, Valentina; Calderone, Vito; Hu, Xiaoyu; Luchinat, Claudio; Parigi, Giacomo. "Structural characterization of human S100A16, a low-affinity calcium binder." J. Biol. Inorg. Chem. 16, 243-256 (2011).
Assembly members:
S100A16, polymer, 102 residues, 11686.296 Da.
CA, non-polymer, 40.078 Da.
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
Entity Sequences (FASTA):
S100A16: SDCYTELEKAVIVLVENFYK
YVSKYSLVKNKISKSSFREM
LQKELNHMLSDTGNRKAADK
LIQNLDANHDGRISFDEYWT
LIGGITGPIAKLIHEQEQQS
SS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 408 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 446 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1_1 | 1 |
| 2 | entity_1_2 | 1 |
| 3 | CALCIUM ION_1 | 2 |
| 4 | CALCIUM ION_2 | 2 |
| 5 | CALCIUM ION_3 | 2 |
| 6 | CALCIUM ION_4 | 2 |
Entities:
Entity 1, entity_1_1 102 residues - 11686.296 Da.
| 1 | SER | ASP | CYS | TYR | THR | GLU | LEU | GLU | LYS | ALA | ||||
| 2 | VAL | ILE | VAL | LEU | VAL | GLU | ASN | PHE | TYR | LYS | ||||
| 3 | TYR | VAL | SER | LYS | TYR | SER | LEU | VAL | LYS | ASN | ||||
| 4 | LYS | ILE | SER | LYS | SER | SER | PHE | ARG | GLU | MET | ||||
| 5 | LEU | GLN | LYS | GLU | LEU | ASN | HIS | MET | LEU | SER | ||||
| 6 | ASP | THR | GLY | ASN | ARG | LYS | ALA | ALA | ASP | LYS | ||||
| 7 | LEU | ILE | GLN | ASN | LEU | ASP | ALA | ASN | HIS | ASP | ||||
| 8 | GLY | ARG | ILE | SER | PHE | ASP | GLU | TYR | TRP | THR | ||||
| 9 | LEU | ILE | GLY | GLY | ILE | THR | GLY | PRO | ILE | ALA | ||||
| 10 | LYS | LEU | ILE | HIS | GLU | GLN | GLU | GLN | GLN | SER | ||||
| 11 | SER | SER |
Entity 2, CALCIUM ION_1 - Ca - 40.078 Da.
| 1 | CA |
Samples:
13C15N_Ca_II_S100A16: S100A16, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%; Ca ions 10 mM; KCl 200 mM
15N_Ca_II_S100A16: S100A16, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%; Ca ions 10 mM; KCl 200 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 13C15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | 15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 13C15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 3D HNCO | 13C15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 3D HNCA | 13C15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 13C15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | 13C15N_Ca_II_S100A16 | isotropic | sample_conditions_1 |
Software:
AMBER v10.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - data analysis, structure solution
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis, structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis
ProcheckNMR, Laskowski and MacArthur - structure solution
TALOS, Cornilescu, Delaglio and Bax - structure solution
TOPSPIN v2.0, Bruker Biospin - collection, processing
XEASY, Bartels et al. - chemical shift assignment, peak picking
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
WhatIF, Vriend - structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 700 MHz
- Bruker Avance 900 MHz
Related Database Links:
| BMRB | 17261 |
| PDB | |
| DBJ | BAF83493 |
| EMBL | CAE51865 |
| GB | AAH10541 AAH19099 AAH95462 AAP46152 AAW88319 |
| REF | NP_001303936 NP_001303937 NP_525127 XP_001103071 XP_002760028 |
| SP | Q96FQ6 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts