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 25208

Title: Backbone and Side Chain Chemical Shift Assignments for S100A4dC in complex with MPT   PubMed: 27418229

Deposition date: 2014-09-09 Original release date: 2016-08-19

Authors: Bodor, Andrea; Palfy, Gyula; Kiss, Bence; Nyitray, Laszlo

Citation: Palfy, Gyula; Kiss, Bence; Nyitray, Laszlo; Bodor, Andrea. "Multilevel Changes in Protein Dynamics upon Complex Formation of the Calcium-Loaded S100A4 with a Nonmuscle Myosin IIA Tail Fragment"  Chembiochem 17, 1829-1838 (2016).

Assembly members:
S100A4dC, polymer, 91 residues, 10403.9 Da.
MPT, polymer, 45 residues, 5346.1 Da.
entity_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   Vector: pEV

Entity Sequences (FASTA):
S100A4dC: GSHMACPLEKALDVMVSTFH KYSGKEGDKFKLNKSELKEL LTRELPSFLGKRTDEAAFQK LMSNLDSNRDNEVDFQEYCV FLSCIAMMCNE
MPT: YRKLQRELEDATETADAMNR EVSSLKNKLRRGDLPFVVPR RMARK

Data sets:
Data typeCount
13C chemical shifts526
15N chemical shifts178
1H chemical shifts174

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S100A4dC, 11
2S100A4dC, 21
3MPT2
4Ca, 13
5Ca, 23
6Ca, 33
7Ca, 43

Entities:

Entity 1, S100A4dC, 1 91 residues - 10403.9 Da.

1   GLYSERHISMETALACYSPROLEUGLULYS
2   ALALEUASPVALMETVALSERTHRPHEHIS
3   LYSTYRSERGLYLYSGLUGLYASPLYSPHE
4   LYSLEUASNLYSSERGLULEULYSGLULEU
5   LEUTHRARGGLULEUPROSERPHELEUGLY
6   LYSARGTHRASPGLUALAALAPHEGLNLYS
7   LEUMETSERASNLEUASPSERASNARGASP
8   ASNGLUVALASPPHEGLNGLUTYRCYSVAL
9   PHELEUSERCYSILEALAMETMETCYSASN
10   GLU

Entity 2, MPT 45 residues - 5346.1 Da.

1   TYRARGLYSLEUGLNARGGLULEUGLUASP
2   ALATHRGLUTHRALAASPALAMETASNARG
3   GLUVALSERSERLEULYSASNLYSLEUARG
4   ARGGLYASPLEUPROPHEVALVALPROARG
5   ARGMETALAARGLYS

Entity 3, Ca, 1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: S100A4dC, [U-100% 13C; U-100% 15N], 1.37 mM; MPT 6.44 mM; CaCl2 3.2 mM; MES 16 mM; NaCl 16 mM; TCEP 2 mM; DSS 3 uL; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.080 M; pH: 6; pressure: 1 atm; temperature: 300 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 HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D BEST-HNCACBsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
2D CBCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0.3, Bruker Biospin - collection, processing

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz

Related Database Links:

UNP P26447 P35579
AlphaFold Q6ICP8 Q86T83

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