BMRB Entry 34333

Name: Solution structure of the water-soluble LU-domain of human Lypd6 protein
Published: 2019-12-13

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34333

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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 water-soluble LU-domain of human Lypd6 protein

Deposition date: 2018-11-29 Original release date: 2019-12-13

Authors: Tsarev, A.; Kulbatskii, D.; Paramonov, A.; Lyukmanova, E.; Shenkarev, Z.

Citation: Kulbatskii, D.; Tsarev, A.; Paramonov, A.; Loktyushov, E.; Dolgikh, D.; Kirpichnikov, M.; Lyukmanova, E.; Shenkarev, Z.. "Human Neuromodulator Lypd6 Inhibits A7 type Nicotinic Acetylcholine Receptors and Suppresses the Long-Term Potentiation" to be published ., .-..

Assembly members:
Ly6/PLAUR domain-containing protein 6, polymer, 96 residues, 10941.329 Da.

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
Ly6/PLAUR domain-containing protein 6: MFKCFTCEKAADNYECNRWA PDIYCPRETRYCYTQHTMEV TGNSISVTKRCVPLEECLST GCRDSEHEGHKVCTSCCEGN ICNLPLPRNETDATFA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	354
15N chemical shifts	97
1H chemical shifts	603

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 96 residues - 10941.329 Da.

1

MET

PHE

LYS

CYS

PHE

THR

CYS

GLU

LYS

ALA

2

ALA

ASP

ASN

TYR

GLU

CYS

ASN

ARG

TRP

ALA

3

PRO

ASP

ILE

TYR

CYS

PRO

ARG

GLU

THR

ARG

4

TYR

CYS

TYR

THR

GLN

HIS

THR

MET

GLU

VAL

5

THR

GLY

ASN

SER

ILE

SER

VAL

THR

LYS

ARG

6

CYS

VAL

PRO

LEU

GLU

CYS

LEU

SER

THR

7

GLY

CYS

ARG

ASP

SER

GLU

HIS

GLU

GLY

HIS

8

LYS

VAL

CYS

THR

SER

CYS

GLU

GLY

ASN

9

ILE

CYS

ASN

LEU

PRO

LEU

PRO

ARG

ASN

GLU

10

THR

ASP

ALA

THR

PHE

ALA

Samples:

sample_1: Lypd6sh, [U-99% 13C; U-99% 15N], 0.1 mM

sample_2: Lypd6sh, [U-99% 15N], 0.1 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v3.97, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker AvanceIII 800 MHz
Bruker AvanceIII 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts