BMRB Entry 15553

Name: 1H, 13C and 15N resonance assignments from the Gal_lectin domain of mouse Latrophilin-1 GPCR
Published: 2008-04-21

Click here to enlarge.

PDB ID: 2jx9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15553
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H, 13C and 15N resonance assignments from the Gal_lectin domain of mouse Latrophilin-1 GPCR

Deposition date:

2007-11-10

Original release date:

2008-04-21

Authors:

Vakonakis, Ioannis; Campbell, Iain

Citation:

Citation: Vakonakis, Ioannis; Langenhan, Tobias; Promel, Simone; Russ, Andreas; Campbell, Iain. "Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain" Structure 16, 944-953 (2008).
PubMed: 18547526

Assembly members:

Assembly members:
Gal_lectin, polymer, 106 residues, 11979.6 Da.
NAG, non-polymer, 221.208 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Pichia pastoris Vector: N/A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Gal_lectin: GLPFGLMRRELACEGYPIEL RCPGSDVIMVENANYGRTDD KICDADPFQMENVQCYLPDA FKIMSQRCNNRTQCVVVAGS DAFPDPCPGTYKYLEVQYDC VPYKVE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	463
15N chemical shifts	112
1H chemical shifts	724

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1
2	carbohydrate	2

Entities:

Entity 1, protein 106 residues - 11979.6 Da.

This is the Gal_lectin-type extracellular domain of Latrophilin-1 GPCR

1

GLY

LEU

PRO

PHE

GLY

LEU

MET

ARG

GLU

2

LEU

ALA

CYS

GLU

GLY

TYR

PRO

ILE

GLU

LEU

3

ARG

CYS

PRO

GLY

SER

ASP

VAL

ILE

MET

VAL

4

GLU

ASN

ALA

ASN

TYR

GLY

ARG

THR

ASP

5

LYS

ILE

CYS

ASP

ALA

ASP

PRO

PHE

GLN

MET

6

GLU

ASN

VAL

GLN

CYS

TYR

LEU

PRO

ASP

ALA

7

PHE

LYS

ILE

MET

SER

GLN

ARG

CYS

ASN

8

ARG

THR

GLN

CYS

VAL

ALA

GLY

SER

9

ASP

ALA

PHE

PRO

ASP

PRO

CYS

PRO

GLY

THR

10

TYR

LYS

TYR

LEU

GLU

VAL

GLN

TYR

ASP

CYS

11

VAL

PRO

TYR

LYS

VAL

GLU

Entity 2, carbohydrate - C8 H15 N O6 - 221.208 Da.

1

NAG

Samples:

sample_1: Gal_lectin, [U-100% 15N], 1-2 ± 0.1 mM; carbohydrate, [U-100% 15N], 1-2 ± 0.1 mM; D2O 5%; sodium azide 0.02%; sodium phosphate 20 mM

sample_2: Gal_lectin, [U-100% 13C; U-100% 15N], 1-2 ± 0.1 mM; carbohydrate, [U-100% 13C; U-100% 15N], 1-2 ± 0.1 mM; D2O 5%; sodium phosphate 20 mM; sodium azide 0.02%

sample_3: Gal_lectin, [U-100% 13C; U-100% 15N], 1-2 ± 0.1 mM; carbohydrate, [U-100% 13C; U-100% 15N], 1-2 ± 0.1 mM; D2O 100%; sodium azide 0.02%; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 30 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
4D 13C-13C NOESY	sample_3	isotropic	sample_conditions_1
3D HACAHB	sample_3	isotropic	sample_conditions_1

Software:

Omega Spectrometer Operating Software vBeta 6.0.3b2, GE/Bruker - collection

NMRPipe v2.4 Rev 2006.095.11.35, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PIPP v4.3.7, Garrett - data analysis, peak picking

NMR spectrometers:

home-built N/A 600 MHz
home-built N/A 500 MHz

PDB	2JX9 2JXA
DBJ	BAA74844 BAC06134 BAC65662 BAG09856
GB	AAC53268 AAC62650 AAC62651 AAC62652 AAC62653
REF	NP_001008701 NP_001107200 NP_055736 NP_075251 NP_851382
SP	O88917 O94910 O97831 Q80TR1
TPG	DAA28096
AlphaFold	O88917 O88917 O94910 O94910 O97831 O97831 Q80TR1 Q80TR1