BMRB Entry 18231
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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/BMR18231
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Title: Solution structure of S100A1 Ca2+ PubMed: 23351007
Deposition date: 2012-01-31 Original release date: 2013-02-18
Authors: Budzinska, Monika; Ruszczynska-Bartnik, Katarzyna Ruszczynska-Bartnik; Belczyk-Ciesielska, Agnieszka; Bierzynski, Andrzej; Ejchart, Andrzej
Citation: Nowakowski, Micha; Ruszczyska-Bartnik, Katarzyna; Budziska, Monika; Jaremko, Lukasz; Jaremko, Mariusz; Zdanowski, Konrad; Bierzyski, Andrzej; Ejchart, Andrzej. "Impact of calcium binding and thionylation of S100A1 protein on its nuclear magnetic resonance-derived structure and backbone dynamics." Biochemistry 52, 1149-1159 (2013).
Assembly members:
S100A1_Ca2+, polymer, 93 residues, 10425.684 Da.
CALCIUM ION, non-polymer, 40.078 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
S100A1_Ca2+: GSELETAMETLINVFHAHSG
KEGDKYKLSKKELKELLQTE
LSGFLDAQKDVDAVDKVMKE
LDENGDGEVDFQEYVVLVAA
LTVACNNFFWENS
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 380 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 620 |
| heteronuclear NOE values | 199 |
| T1 relaxation values | 221 |
| T2 relaxation values | 224 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | S100A1 monomer, 1 | 1 |
| 2 | S100A1 monomer, 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, S100A1 monomer, 1 93 residues - 10425.684 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 | GLU | LEU | LEU | GLN | THR | GLU | ||||
| 5 | LEU | SER | GLY | PHE | LEU | ASP | ALA | GLN | LYS | ASP | ||||
| 6 | VAL | ASP | ALA | VAL | ASP | LYS | VAL | MET | LYS | GLU | ||||
| 7 | LEU | ASP | GLU | ASN | GLY | ASP | GLY | GLU | VAL | ASP | ||||
| 8 | PHE | GLN | GLU | TYR | VAL | VAL | LEU | VAL | ALA | ALA | ||||
| 9 | LEU | THR | VAL | ALA | CYS | ASN | ASN | PHE | PHE | TRP | ||||
| 10 | GLU | ASN | SER |
Entity 2, CALCIUM ION_1 - Ca - 40.078 Da.
Samples:
sample_1: D2O 10%; H2O 90%; sodium chloride 50 mM; CALCIUM ION 10 mM; S100A1, [U-99% 13C; U-99% 15N], 0.8 mM; TRIS-d11 50 mM
sample_2: D2O 100%; sodium chloride 50 mM; CALCIUM ION 10 mM; S100A1, [U-99% 13C; U-99% 15N], 0.8 mM; TRIS-d11 50 mM
sample_3: D2O 10%; H2O 90%; sodium chloride 50 mM; CALCIUM ION 10 mM; S100A1, [U-99% 15N], 0.8 mM; TRIS-d11 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 310 K
sample_conditions_2: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC NH2 only | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_2 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N heteronuclear NOE | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N heteronuclear NOE | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N heteronuclear NOE | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N T1 relaxation | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N T1 relaxation | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N T1 relaxation | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N T2 relaxation | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N T2 relaxation | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N T2 relaxation | sample_3 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - constraints assignment, data analysis, structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Varian INOVA 400 MHz
- Varian UnityPlus 500 MHz
- Varian Varian NMR System 700 MHz
- Varian Varian NMR System 800 MHz
Related Database Links:
| BMRB | 16360 17857 18087 18088 18089 18101 18230 18545 |
| PDB | |
| DBJ | BAE90380 BAG35086 BAG70130 BAG70260 |
| EMBL | CAA41107 CAH90674 |
| GB | AAH14392 AAI41992 AAI48020 AAP35584 AAP36328 |
| PRF | 2003367A |
| REF | NP_001092512 NP_001127319 NP_001270255 NP_006262 XP_001111015 |
| SP | P02639 P23297 Q5RC36 |
| TPG | DAA31796 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts