BMRB Entry 25992

Title:
Backbone and Side Chain Chemical Shift Assignments for the myosin IIA fragment 1893-1937 (MPT)
Deposition date:
2016-03-11
Original release date:
2016-08-19
Authors:
Bodor, Andrea; Palfy, Gyula; Kiss, Bence; Nyitray, Laszlo
Citation:

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).
PubMed: 27418229

Assembly members:

Assembly members:
MPT, polymer, 45 residues, 5346.1 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pUBK

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts136
15N chemical shifts41
1H chemical shifts251

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MPT1

Entities:

Entity 1, MPT 45 residues - 5346.1 Da.

1   TYRARGLYSLEUGLNARGGLULEUGLUASP
2   ALATHRGLUTHRALAASPALAMETASNARG
3   GLUVALSERSERLEULYSASNLYSLEUARG
4   ARGGLYASPLEUPROPHEVALVALPROARG
5   ARGMETALAARGLYS

Samples:

sample_1: MPT, [U-100% 15N], 0.7 mM; CaCl2 1 mM; MES 20 mM; NaCl 20 mM; TCEP 10 mM; NaN3 10 mM; D2O, [U-100% 2H], 10%

sample_2: MPT, [U-100% 13C; U-100% 15N], 0.80 mM; CaCl2 1 mM; MES 20 mM; NaCl 20 mM; TCEP 10 mM; NaN3 10 mM; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.2; pressure: 1 atm; temperature: 283 K

sample_conditions_2: ionic strength: 0.1 M; pH: 5.4; pressure: 1 atm; temperature: 283 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 CC(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-15N TOCSYsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_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 700 MHz

Related Database Links:

UNP P35579
AlphaFold Q86T83

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