BMRB Entry 51281

Title:
Salp15 NMR backbone assignment
Deposition date:
2022-01-14
Original release date:
2022-03-22
Authors:
Persson, Cecilia; Chaves-Arquero, Belen; Blanco, Francisco
Citation:

Citation: Belen, Chaves-Arquero; Persson, Cecilia; Merino, Nekane; Tomas-Cortazar, Julen; Rojas, Adriana; Anguita, Juan; Blanco, Francisco. "Structural Analysis of the Black-Legged Tick Saliva Protein Salp15"  Int. J. Mol. Sci. 23, 3134-3134 (2022).

Assembly members:

Assembly members:
entity_1, polymer, 117 residues, 12668.2 Da.

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: pHIS-Parallel2

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts96
1H chemical shifts96

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1salp151

Entities:

Entity 1, salp15 117 residues - 12668.2 Da.

The initial 4 residues are non-native ones. The first native residue is E5, which corresponds to residue number 23 in the sequence of the full-length protein.

1   GLYALAMETGLYGLUSERGLYPROTHRLYS
2   ALAASPALASERTHRALAASPLYSASPTHR
3   LYSLYSASNASNVALGLNLEUARGPHEPRO
4   ASNTYRILESERASNHISGLNLYSLEUALA
5   LEULYSLEULEULYSILECYSLYSASPSER
6   LYSSERSERHISASNSERLEUSERSERARG
7   SERSERASPVALILEASNASPLYSTYRVAL
8   ASPPHELYSASNCYSTHRPHELEUCYSLYS
9   HISGLYASNASPVALASNVALTHRLEUASN
10   LEUPROGLUASPTHRPROCYSGLYPROASN
11   GLYGLNTHRCYSALAGLULYSASNLYSCYS
12   VALGLYHISILEPROGLYCYS

Samples:

sample_1: salp15, [U-98% 13C; U-98% 15N], 0.14 ± 0.01 mM; D2O, [U-2H], 5 ± 1 %; H2O 95 ± 1 5; DSS 30 ± 3 uM; sodium phosphate 10 ± 1 mM; sodium azide 0.01 ± 0.001 %; sodium chloride 50 ± 5 mM

sample_conditions_1: ionic strength: 75 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

UNP Q95WZ4
AlphaFold Q95WZ4

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