BMRB Entry 27033

Title:
1H, 13C and 15N Chemical Shift Assignments of cyclophilin 2 from Trichomonas vaginalis
Deposition date:
2017-02-12
Original release date:
2017-09-15
Authors:
Martin, Tesmine; Lou, Yuan-Chao; Chen, Chinpan
Citation:

Citation: Martin, Tesmine; Lou, Yuan-Chao; Aryal, Sarita; Tai, Jung-Hsiang; Chen, Chinpan. "1H, 13C and 15N resonance assignments and secondary structures of cyclophilin 2 from Trichomonas vaginalis"  Biomol. NMR Assignments 12, 27-30 (2018).
PubMed: 28875299

Assembly members:

Assembly members:
cyclophilin_2_from_Trichomonas_vaginalis, polymer, 194 residues, 20947 Da.

Natural source:

Natural source:   Common Name: Trichomonas vaginalis   Taxonomy ID: 5722   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trichomonas vaginalis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Data sets:
Data typeCount
13C chemical shifts750
15N chemical shifts175
1H chemical shifts1115

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TvCyP2 monomer1

Entities:

Entity 1, TvCyP2 monomer 194 residues - 20947 Da.

1   METLEUALAPHEPHEALATHRARGVALILE
2   SERALAPROLYSVALTHRLYSLYSVALPHE
3   PHELYSILESERILEASNGLYGLUASPALA
4   GLYTHRILELYSPHEGLYLEUPHEGLYASP
5   ASPVALPROLYSTHRALAGLUASNPHEARG
6   ALALEUCYSTHRGLYGLULYSGLYMETGLY
7   LYSLEUGLYLYSPROLEUHISTYRLYSGLY
8   SERPROPHEHISARGVALILEPROASNPHE
9   METILEGLNGLYGLYASPILETHRSERGLY
10   ASNGLYTYRGLYGLYGLUSERILETYRGLY
11   SERLYSPHEALAASPGLUSERPHELYSILE
12   THRHISASPGLYPROGLYLEULEUSERMET
13   ALAASNSERGLYPROASNTHRASNGLYSER
14   GLNPHEPHEILETHRTHRVALPROCYSPRO
15   TRPLEUASNGLYLYSHISVALVALPHEGLY
16   LYSVALILEGLUGLYMETGLUILEVALLYS
17   LYSILEGLUSERLEUGLYSERGLNSERGLY
18   THRPROLYSALALYSILEILEILEALAASP
19   CYSGLYGLUILETHRGLULEUGLUHISHIS
20   HISHISHISHIS

Samples:

sample_1: cyclophilin 2 from Trichomonas vaginalis, [U-100% 13C; U-100% 15N], 0.6 ± 0.01 mM

sample_conditions_1: ionic strength: 170 mM; pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 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