BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18088

Title: Post-translational S-nitrosylation is an endogenous factor fine-tuning human S100A1 protein properties   PubMed: 22989881

Authors: Lenarcic Zivkovic, Martina; Zareba-Koziol, Monika; Zhukova, Lilia; Poznanski, Jarek; Zhukov, Igor; Wyslouch-Cieszynska, Aleksandra

Citation: Lenari ivkovic, Martina; Zarba-Kozio, Monika; Zhukova, Liliya; Poznaski, Jarosaw; Zhukov, Igor; Wysouch-Cieszyska, Aleksandra. "Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein."  J. Biol. Chem. 287, 40457-40470 (2012).

Assembly members:
S100A1 with post-translational S-nitrosylation, strand 1, polymer, 93 residues, 10454.682 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):
S100A1 with post-translational S-nitrosylation, strand 1: GSELETAMETLINVFHAHSG KEGDKYKLSKKELKELLQTE LSGFLDAQKDVDAVDKVMKE LDENGDGEVDFQEYVVLVAA LTVAXNNFFWENS

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts100
1H chemical shifts652

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1S100A1 with post-translational S-nitrosylation, strand 11
2S100A1 with post-translational S-nitrosylation, strand 21

Entities:

Entity 1, S100A1 with post-translational S-nitrosylation, strand 1 93 residues - 10454.682 Da.

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

Samples:

sample_1: S100A1_pt, [U-98% 13C; U-98% 15N], 0.8 mM; H2O 90%; D2O 10%; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz

Related Database Links:

BMRB 16360 17857 18087 18089 18101 18230 18231 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