BMRB Entry 27051

Title:
1H, 15N and 13C resonance assignments of the Ixolaris, a tissue factor pathway inhibitor from the tick salivary gland
Deposition date:
2017-03-19
Original release date:
2019-01-18
Authors:
de Paula, Viviane; Silva, Felipe; Francischette, Ivo; Monteiro, Robson; Valente, Ana Paula
Citation:

Citation: de Paula, Viviane; Silva, Felipe; Francischette, Ivo; Monteiro, Robson; Valente, Ana Paula. "1H, 15N and 13C resonance assignments of Ixolaris, a tissue factor pathway inhibitor from the tick salivary gland"  Biomol. NMR Assign. 11, 293-296 (2017).
PubMed: 28856584

Assembly members:

Assembly members:
Ixolaris, polymer, 142 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: black-legged tick   Taxonomy ID: 6945   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Ixodes scapularis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32a

Data sets:
Data typeCount
13C chemical shifts515
15N chemical shifts134
1H chemical shifts828

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ixolaris1

Entities:

Entity 1, Ixolaris 142 residues - Formula weight is not available

Residues 1-2 (A,M) represent a non-native affinity tag

1   ALAMETALAGLUARGVALSERGLUMETASP
2   ILETYRGLUPHEGLUSERTRPVALSERCYS
3   LEUASPPROGLUGLNVALTHRCYSGLUSER
4   GLNGLUGLYTHRHISALASERTYRASNARG
5   LYSTHRGLYGLNCYSGLUGLUGLNLYSGLY
6   THRGLUCYSGLYGLYGLYGLUASNHISPHE
7   GLUTHRLEULEULYSCYSASNGLUSERCYS
8   ASNASPALAPROLYSPROPROCYSSERLEU
9   GLUVALASPTYRGLYVALGLYARGALAASN
10   ILEPROARGTRPTYRTYRASPTHRASNASN
11   ALATHRCYSGLUMETPHETHRTYRGLYGLY
12   ILETHRGLYASNLYSASNASNPHEGLUSER
13   GLUGLUGLUCYSLYSGLUTHRCYSLYSGLY
14   PHESERLEULEULYSLYSVALASNVALTHR
15   ILEASN

Samples:

sample_1: Ixolaris, [U-99% 13C; U-99% 15N], 0.18 mM

sample_conditions_1: ionic strength: 0 M; pH: 6; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CS-Rosetta, Shen, Vernon, Baker and Bax - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

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