BMRB Entry 34532

Name: NMR structure of water-soluble domain of human Lynx2 (Lypd1) protein
Published: 2021-01-06

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PDB ID: 6zss
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34532
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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:

NMR structure of water-soluble domain of human Lynx2 (Lypd1) protein

Deposition date:

2020-07-16

Original release date:

2021-01-06

Authors:

Kocharovskaya, M.; Paramonov, A.; Lyukmanova, E.; Shenkarev, Z.

Citation:

Citation: Paramonov, Alexander; Kocharovskaya, Milita; Tsarev, Andrey; Kulbatskii, Dmitrii; Loktyushov, Eugene; Shulepko, Mikhail; Kirpichnikov, Mikhail; Lyukmanova, Ekaterina; Shenkarev, Zakhar. "Structural Diversity and Dynamics of Human Three-Finger Proteins Acting on Nicotinic Acetylcholine Receptors" Int. J. Mol. Sci. 21, 7280-7280 (2020).
PubMed: 33019770

Assembly members:

Assembly members:
entity_1, polymer, 86 residues, 9390.756 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):
entity_1: MIQCYQCEEFQLNNDCSSPE FIVNCTVNVQDMCQKEVMEQ SAGIMYRKSCASSAACLIAS AGYQSFCSPGKLNSVCISCC NTPLCN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	313
15N chemical shifts	86
1H chemical shifts	512

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 86 residues - 9390.756 Da.

1

MET

ILE

GLN

CYS

TYR

GLN

CYS

GLU

PHE

2

GLN

LEU

ASN

ASP

CYS

SER

PRO

GLU

3

PHE

ILE

VAL

ASN

CYS

THR

VAL

ASN

VAL

GLN

4

ASP

MET

CYS

GLN

LYS

GLU

VAL

MET

GLU

GLN

5

SER

ALA

GLY

ILE

MET

TYR

ARG

LYS

SER

CYS

6

ALA

SER

ALA

CYS

LEU

ILE

ALA

SER

7

ALA

GLY

TYR

GLN

SER

PHE

CYS

SER

PRO

GLY

8

LYS

LEU

ASN

SER

VAL

CYS

ILE

SER

CYS

9

ASN

THR

PRO

LEU

CYS

ASN

Samples:

sample_1: Lynx2, [U-98% 13C; U-98% 15N], 0.25 ± 0.03 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.7; pressure: 1 atm; temperature: 318 K

Experiments:

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

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement

TopSpin, Bruker Biospin - collection

CARA v1.8, Keller and Wuthrich - chemical shift assignment

MddNMR, V. Orekhov, V. Jaravine, M. Mayzel, K. Kazimierczuk, Swedish NMR Center, University of Gothenburg - processing

NMR spectrometers:

Bruker AVANCE III 800 MHz

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