BMRB Entry 25887

Name: Solution structure of the SLURP-2, a secreted isoform of Lynx1
Published: 2016-09-15

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PDB ID: 2n99
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25887
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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:

Solution structure of the SLURP-2, a secreted isoform of Lynx1

Deposition date:

2015-11-11

Original release date:

2016-09-15

Authors:

Paramonov, Alexander; Shenkarev, Zakhar; Lyukmanova, Ekaterina; Arseniev, Alexander

Citation:

Citation: Lyukmanova, E.; Shulepko, M.; Shenkarev, Z.; Bychkov, M.; Paramonov, A.; Chugunov, A.; Kulbatskii, D.; Arvaniti, M.; Dolejsi, E.; Schaer, T.; Arseniev, A.; Efremov, R.; Thomsen, M.; Dolezal, V.; Bertrand, D.; Dolgikh, D.; Kirpichnikov, M.. "Secreted Isoform of Human Lynx1 (SLURP-2): Spatial Structure and Pharmacology of Interactions with Different Types of Acetylcholine Receptors" Sci. Rep. 6, 30698-30698 (2016).
PubMed: 27485575

Assembly members:

Assembly members:
SLURP-2, polymer, 76 residues, 8163.446 Da.

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-22b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SLURP-2: MIWCHQCTGFGGCSHGSRCL RDSTHCVTTATRVLSNTEDL PLVTKMCHIGCPDIPSLGLG PYVSIACCQTSLCNHD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	300
15N chemical shifts	78
1H chemical shifts	488

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SLURP-2	1

Entities:

Entity 1, SLURP-2 76 residues - 8163.446 Da.

Residue M100 was added due to recombinant production

1

MET

ILE

TRP

CYS

HIS

GLN

CYS

THR

GLY

PHE

2

GLY

CYS

SER

HIS

GLY

SER

ARG

CYS

LEU

3

ARG

ASP

SER

THR

HIS

CYS

VAL

THR

ALA

4

THR

ARG

VAL

LEU

SER

ASN

THR

GLU

ASP

LEU

5

PRO

LEU

VAL

THR

LYS

MET

CYS

HIS

ILE

GLY

6

CYS

PRO

ASP

ILE

PRO

SER

LEU

GLY

LEU

GLY

7

PRO

TYR

VAL

SER

ILE

ALA

CYS

GLN

THR

8

SER

LEU

CYS

ASN

HIS

ASP

Samples:

sample_1: SLURP-2, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 95%; D2O 5%; dioxane-d6 5%

sample_conditions_1: ionic strength: 10 mM; pH: 5.0; pressure: 1 atm; temperature: 315 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

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