BMRB Entry 34354

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34354
MolProbity Validation Chart

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Title:
Truncated Evasin-3 (tEv3 17-56)
Deposition date:
2019-01-24
Original release date:
2019-10-03
Authors:
Denisov, S.; Ippel, J.; Heinzman, A.; Koenen, R.; Ortega-Gomez, A.; Soehnlein, O.; Hackeng, T.; Dijkgraaf, I.
Citation:

Citation: Denisov, S.; Ippel, J.; Heinzmann, A.; Koenen, R.; Ortega-Gomez, A.; Soehnlein, O.; Hackeng, T.; Dijkgraaf, I.. "Tick saliva protein Evasin-3 modulates chemotaxis by disrupting CXCL8 interactions with glycosaminoglycans and CXCR2."  J. Biol. Chem. 294, 12370-12379 (2019).
PubMed: 31235521

Assembly members:

Assembly members:
entity_1, polymer, 40 residues, 4314.924 Da.

Natural source:

Natural source:   Common Name: Brown dog tick   Taxonomy ID: 34632   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rhipicephalus sanguineus

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: FDVVSCNKNCTSGQNECPEG CFCGLLGQNKKGHCYKIIGN

Data sets:
Data typeCount
13C chemical shifts122
15N chemical shifts44
1H chemical shifts257

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 40 residues - 4314.924 Da.

1   PHEASPVALVALSERCYSASNLYSASNCYS
2   THRSERGLYGLNASNGLUCYSPROGLUGLY
3   CYSPHECYSGLYLEULEUGLYGLNASNLYS
4   LYSGLYHISCYSTYRLYSILEILEGLYASN

Samples:

sample_1: entity_1 mM; EDTA 100 mM; sodium azide 200 mM; sodium acetate, [U-2H], 25 mM

sample_conditions_1: ionic strength: 325 mM; pH: 4.5; pressure: 1 atm; temperature: 37 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
3D HNCOsample_1anisotropicsample_conditions_1
3D HNCACBsample_1anisotropicsample_conditions_1
3D CBCA(CO)NHsample_1anisotropicsample_conditions_1
2D 1H-13C HSQCsample_1anisotropicsample_conditions_1
2D 1H-1H NOESYsample_1anisotropicsample_conditions_1

Software:

NMRFAM-SPARKY, NMRFAM-SPARKY - chemical shift assignment

Xplor-NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMRe, Hyojung Ryu, GyuTae Lim, Bong Hyun Sung, Jinhyuk Lee - refinement

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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