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 30017

Title: Solution Structure of human calcium-binding S100A9 (C3S) protein   PubMed: 27524699

Deposition date: 2016-02-19 Original release date: 2016-08-19

Authors: Chang, Chin-Chi; Chin, Yu

Citation: Chang, Chin-Chi; Khan, Imran; Tsai, Kun-Lin; Li, Hongchun; Yang, Lee-Wei; Chou, Ruey-Hwang; Yu, Chin. "Blocking the interaction between S100A9 and RAGE V domain using CHAPS molecule: A novel route to drug development against cell proliferation"  Biochim. Biophys. Acta 1864, 1558-1569 (2016).

Assembly members:
entity_1, polymer, 114 residues, 13247.955 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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
entity_1: MTSKMSQLERNIETIINTFH QYSVKLGHPDTLNQGEFKEL VRKDLQNFLKKENKNEKVIE HIMEDLDTNADKQLSFEEFI MLMARLTWASHEKMHEGDEG PGHHHKPGLGEGTP

Data sets:
Data typeCount
13C chemical shifts435
15N chemical shifts98
1H chemical shifts668

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 114 residues - 13247.955 Da.

1   METTHRSERLYSMETSERGLNLEUGLUARG
2   ASNILEGLUTHRILEILEASNTHRPHEHIS
3   GLNTYRSERVALLYSLEUGLYHISPROASP
4   THRLEUASNGLNGLYGLUPHELYSGLULEU
5   VALARGLYSASPLEUGLNASNPHELEULYS
6   LYSGLUASNLYSASNGLULYSVALILEGLU
7   HISILEMETGLUASPLEUASPTHRASNALA
8   ASPLYSGLNLEUSERPHEGLUGLUPHEILE
9   METLEUMETALAARGLEUTHRTRPALASER
10   HISGLULYSMETHISGLUGLYASPGLUGLY
11   PROGLYHISHISHISLYSPROGLYLEUGLY
12   GLUGLYTHRPRO

Samples:

sample_1: S100A9 protein (C3S), [U-13C; U-15N], 2 ± 0.2 mM; TRIS 50 ± 0.2 mM; calcium chloride 2 ± 0.2 mM; sodium chloride 100 ± 0.2 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_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 HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - peak picking, refinement, structure calculation

SPARKY v3.1, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

Vnmrj v2.3, Varian - processing

NMR spectrometers:

  • Varian VNMRS 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts