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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
MolProbity Validation Chart

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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

Data typeCount
13C chemical shifts380
15N chemical shifts91
1H chemical shifts620
heteronuclear NOE values199
T1 relaxation values221
T2 relaxation values224

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1S100A1 monomer, 11
2S100A1 monomer, 21
3CALCIUM ION_12
4CALCIUM ION_22
5CALCIUM ION_32
6CALCIUM ION_42

Entities:

Entity 1, S100A1 monomer, 1 93 residues - 10425.684 Da.

1   GLYSERGLULEUGLUTHRALAMETGLUTHR
2   LEUILEASNVALPHEHISALAHISSERGLY
3   LYSGLUGLYASPLYSTYRLYSLEUSERLYS
4   LYSGLULEULYSGLULEULEUGLNTHRGLU
5   LEUSERGLYPHELEUASPALAGLNLYSASP
6   VALASPALAVALASPLYSVALMETLYSGLU
7   LEUASPGLUASNGLYASPGLYGLUVALASP
8   PHEGLNGLUTYRVALVALLEUVALALAALA
9   LEUTHRVALALACYSASNASNPHEPHETRP
10   GLUASNSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N heteronuclear NOEsample_3isotropicsample_conditions_1
2D 1H-15N heteronuclear NOEsample_3isotropicsample_conditions_1
2D 1H-15N heteronuclear NOEsample_3isotropicsample_conditions_1
2D 1H-15N T1 relaxationsample_3isotropicsample_conditions_1
2D 1H-15N T1 relaxationsample_3isotropicsample_conditions_1
2D 1H-15N T1 relaxationsample_3isotropicsample_conditions_1
2D 1H-15N T2 relaxationsample_3isotropicsample_conditions_1
2D 1H-15N T2 relaxationsample_3isotropicsample_conditions_1
2D 1H-15N T2 relaxationsample_3isotropicsample_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