BMRB Entry 51281

Name: Salp15 NMR backbone assignment
Published: 2022-03-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51281

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGESGPTKADASTADKDT KKNNVQLRFPNYISNHQKLA LKLLKICKDSKSSHNSLSSR SSDVINDKYVDFKNCTFLCK HGNDVNVTLNLPEDTPCGPN GQTCAEKNKCVGHIPGC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	299
15N chemical shifts	96
1H chemical shifts	96

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	salp15	1

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

GLY

ALA

MET

GLY

GLU

SER

GLY

PRO

THR

LYS

2

ALA

ASP

ALA

SER

THR

ALA

ASP

LYS

ASP

THR

3

LYS

ASN

VAL

GLN

LEU

ARG

PHE

PRO

4

ASN

TYR

ILE

SER

ASN

HIS

GLN

LYS

LEU

ALA

5

LEU

LYS

LEU

LYS

ILE

CYS

LYS

ASP

SER

6

LYS

SER

HIS

ASN

SER

LEU

SER

ARG

7

SER

ASP

VAL

ILE

ASN

ASP

LYS

TYR

VAL

8

ASP

PHE

LYS

ASN

CYS

THR

PHE

LEU

CYS

LYS

9

HIS

GLY

ASN

ASP

VAL

ASN

VAL

THR

LEU

ASN

10

LEU

PRO

GLU

ASP

THR

PRO

CYS

GLY

PRO

ASN

11

GLY

GLN

THR

CYS

ALA

GLU

LYS

ASN

LYS

CYS

12

VAL

GLY

HIS

ILE

PRO

GLY

CYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCOCA	sample_1	isotropic	sample_conditions_1
3D HNCOCACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

UNP	Q95WZ4
AlphaFold	Q95WZ4