BMRB Entry 27531

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27531

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Title:
Backbone chemical shift assignment of Macrophage infectivity potentiator virulence factor of Trypanosoma cruzi
Deposition date:
2018-07-02
Original release date:
2019-01-10
Authors:
Antiparra, Ricardo; Lippens, Guy; Zimic, Mirko; Sheen, Patricia; Maruenda, Helena; Lopez, Juan
Citation:

Citation: Lopez, Juan; Antiparra, Ricardo; Lippens, Guy; Zimic, Mirko; Sheen, Patricia; Maruenda, Helena. "Backbone chemical shift assignment of macrophage infectivity potentiator virulence factor of Trypanosoma cruzi"  Biomol. NMR Assignments 13, 21-25 (2019).
PubMed: 30229449

Assembly members:

Assembly members:
TcMIP, polymer, 173 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Trypanosoma Cruzi   Taxonomy ID: 5693   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma Cruzi

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TcMIP: SGDAASHEERMNNYRKRVGR LFMEQKAAQPDAVKLPSGLV FQRIARGSGKRAPAIDDKCE VHYTGRLRDGTVFDSSRERG KPTTFRPNEVIKGWTEALQL MREGDRWRLFIPYDLAYGVT GGGGMIPPYSPLEFDVELIS IKDGGKGRTAEEVDEILRKA EEDREDMHHHHHH

Data sets:
Data typeCount
13C chemical shifts433
15N chemical shifts142
1H chemical shifts142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TcMIP1

Entities:

Entity 1, TcMIP 173 residues - Formula weight is not available

1   SERGLYASPALAALASERHISGLUGLUARG
2   METASNASNTYRARGLYSARGVALGLYARG
3   LEUPHEMETGLUGLNLYSALAALAGLNPRO
4   ASPALAVALLYSLEUPROSERGLYLEUVAL
5   PHEGLNARGILEALAARGGLYSERGLYLYS
6   ARGALAPROALAILEASPASPLYSCYSGLU
7   VALHISTYRTHRGLYARGLEUARGASPGLY
8   THRVALPHEASPSERSERARGGLUARGGLY
9   LYSPROTHRTHRPHEARGPROASNGLUVAL
10   ILELYSGLYTRPTHRGLUALALEUGLNLEU
11   METARGGLUGLYASPARGTRPARGLEUPHE
12   ILEPROTYRASPLEUALATYRGLYVALTHR
13   GLYGLYGLYGLYMETILEPROPROTYRSER
14   PROLEUGLUPHEASPVALGLULEUILESER
15   ILELYSASPGLYGLYLYSGLYARGTHRALA
16   GLUGLUVALASPGLUILELEUARGLYSALA
17   GLUGLUASPARGGLUASPMETHISHISHIS
18   HISHISHIS

Samples:

sample_1: TcMIP, [U-13C; U-15N], 0.75 mM; buffer phosphate 50 mM; EDTA 2.5 mM

sample_2: TcMIP, [U-13C; U-15N], 1 mM; buffer phosphate 50 mM; EDTA 2.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2

Software:

SPARKY, Goddard - chemical shift assignment

EKNAS, EKNAS - chemical shift assignment

SHIFTX2, SHIFTX2 - chemical shift calculation

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

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