BMRB Entry 26300

Name: The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata
Published: 2020-12-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26300

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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: The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata PubMed: 33328520

Deposition date: 2020-10-01 Original release date: 2020-12-22

Authors: Kamata, Kenichi; Mizutani, Kenji; Takahashi, Katsuya; Marchetti, Roberta; Silipo, Alba; Addy, Christine; Park, Sam-Yong; Fujii, Yuki; Fujita, Hideaki; Konuma, Tsuyoshi; Ikegami, Takahisa; Ozeki, Yasuhiro; Tame, Jeremy

Citation: Kamata, Kenichi; Mizutani, Kenji; Takahashi, Katsuya; Marchetti, Roberta; Silipo, Alba; Addy, Christine; Park, Sam-Yong; Fujii, Yuki; Fujita, Hideaki; Konuma, Tsuyoshi; Ikegami, Takahisa; Ozeki, Yasuhiro; Tame, Jeremy. "The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata" Sci. Rep. 10, 22102-22102 (2020).

Assembly members:
entity_1, polymer, 132 residues, Formula weight is not available

Natural source: Common Name: not available Taxonomy ID: 2547956 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mytilisepta virgata

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):
entity_1: GSHMSSVTIGKCYIQNRENG GRAFYNLGRKDLGIFTGKMY DDQIWSFQKSDTPGYYTIGR ESKFLQYNGEQVIMSDIEQD TTLWSLEEVPEDKGFYRLLN KVHKAYLDYNGGDLVANKHQ TESEKWILFKAY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	351
15N chemical shifts	114
1H chemical shifts	114

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit 1	1

Entities:

Entity 1, subunit 1 132 residues - Formula weight is not available

The three N-terminal residues, GSH, represent the remaining non-native residues after cleaving the His-tag. The sequence number 1 starts with Met.

1

GLY

SER

HIS

MET

SER

VAL

THR

ILE

GLY

2

LYS

CYS

TYR

ILE

GLN

ASN

ARG

GLU

ASN

GLY

3

GLY

ARG

ALA

PHE

TYR

ASN

LEU

GLY

ARG

LYS

4

ASP

LEU

GLY

ILE

PHE

THR

GLY

LYS

MET

TYR

5

ASP

GLN

ILE

TRP

SER

PHE

GLN

LYS

SER

6

ASP

THR

PRO

GLY

TYR

THR

ILE

GLY

ARG

7

GLU

SER

LYS

PHE

LEU

GLN

TYR

ASN

GLY

GLU

8

GLN

VAL

ILE

MET

SER

ASP

ILE

GLU

GLN

ASP

9

THR

LEU

TRP

SER

LEU

GLU

VAL

PRO

10

GLU

ASP

LYS

GLY

PHE

TYR

ARG

LEU

ASN

11

LYS

VAL

HIS

LYS

ALA

TYR

LEU

ASP

TYR

ASN

12

GLY

ASP

LEU

VAL

ALA

ASN

LYS

HIS

GLN

13

THR

GLU

SER

GLU

LYS

TRP

ILE

LEU

PHE

LYS

14

ALA

TYR

Samples:

sample_1: SeviL dimer, [U-13C; U-15N; U-2H], 0.36 mM; sodium phosphate 50 mM; sodium chloride 20 mM; H2O 93%; D2O, [U-2H], 7%

sample_conditions_1: ionic strength: 0.07 M; pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

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

Software:

MagRO - peak picking

NMR spectrometers:

Bruker AVANCE III 500 MHz

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