BMRB Entry 36021

Name: Solution structure of heterodimeric coiled-coil domain of Drosophila GABAB receptor 1 and 3
Published: 2017-09-11

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PDB ID: 5gwm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36021
MolProbity Validation Chart

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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 heterodimeric coiled-coil domain of Drosophila GABAB receptor 1 and 3

Deposition date:

2016-09-12

Original release date:

2017-09-11

Authors:

Liu, X.; Zhang, S.; Zhang, C.; Liu, J.

Citation:

Citation: Liu, X.; Zhang, S.; Zhang, C.; Liu, J.. "Solution structure of heterodimeric coiled-coil domain of Drosophila GABAB receptor 1 and 3" .

Assembly members:

Assembly members:
entity_1, polymer, 53 residues, 6327.121 Da.
entity_2, polymer, 50 residues, 5954.819 Da.

Natural source:

Natural source: Common Name: Fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDSAISKEDEERYQKLVTEN EQLQRLITQKEEKIRVLRQR LVERGDAKGTELN
entity_2: GPLGSRRFVVDDRRELQYRV EVQNRVYKKEIQALDAEIRK LERLLESGLT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	406
15N chemical shifts	109
1H chemical shifts	704

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 53 residues - 6327.121 Da.

1

MET

ASP

SER

ALA

ILE

SER

LYS

GLU

ASP

GLU

2

GLU

ARG

TYR

GLN

LYS

LEU

VAL

THR

GLU

ASN

3

GLU

GLN

LEU

GLN

ARG

LEU

ILE

THR

GLN

LYS

4

GLU

LYS

ILE

ARG

VAL

LEU

ARG

GLN

ARG

5

LEU

VAL

GLU

ARG

GLY

ASP

ALA

LYS

GLY

THR

6

GLU

LEU

ASN

Entity 2, entity_2 50 residues - 5954.819 Da.

1	GLY	PRO	LEU	GLY	SER	ARG	ARG	PHE	VAL	VAL
2	ASP	ASP	ARG	ARG	GLU	LEU	GLN	TYR	ARG	VAL
3	GLU	VAL	GLN	ASN	ARG	VAL	TYR	LYS	LYS	GLU
4	ILE	GLN	ALA	LEU	ASP	ALA	GLU	ILE	ARG	LYS
5	LEU	GLU	ARG	LEU	LEU	GLU	SER	GLY	LEU	THR

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

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

BMRB Entry 36021

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	GLY	PRO	LEU	GLY	SER	ARG	ARG	PHE	VAL	VAL
2	ASP	ASP	ARG	ARG	GLU	LEU	GLN	TYR	ARG	VAL
3	GLU	VAL	GLN	ASN	ARG	VAL	TYR	LYS	LYS	GLU
4	ILE	GLN	ALA	LEU	ASP	ALA	GLU	ILE	ARG	LYS
5	LEU	GLU	ARG	LEU	LEU	GLU	SER	GLY	LEU	THR

1	GLY	PRO	LEU	GLY	SER	ARG	ARG	PHE	VAL	VAL
2	ASP	ASP	ARG	ARG	GLU	LEU	GLN	TYR	ARG	VAL
3	GLU	VAL	GLN	ASN	ARG	VAL	TYR	LYS	LYS	GLU
4	ILE	GLN	ALA	LEU	ASP	ALA	GLU	ILE	ARG	LYS
5	LEU	GLU	ARG	LEU	LEU	GLU	SER	GLY	LEU	THR

1	GLY	PRO	LEU	GLY	SER	ARG	ARG	PHE	VAL	VAL
2	ASP	ASP	ARG	ARG	GLU	LEU	GLN	TYR	ARG	VAL
3	GLU	VAL	GLN	ASN	ARG	VAL	TYR	LYS	LYS	GLU
4	ILE	GLN	ALA	LEU	ASP	ALA	GLU	ILE	ARG	LYS
5	LEU	GLU	ARG	LEU	LEU	GLU	SER	GLY	LEU	THR