BMRB Entry 50260

Name: 1H, 15N and 13C backbone assignments of GDP-bound Rab4a
Published: 2020-05-07

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50260

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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:

1H, 15N and 13C backbone assignments of GDP-bound Rab4a

Deposition date:

2020-05-05

Original release date:

2020-05-07

Authors:

Genier, Samuel; Letourneau, Danny; Parent, Jean-Luc; Lavigne, Pierre

Citation:

Citation: Genier, Samuel; Letourneau, Danny; Gauthier, Esther; Picard, Samuel; Boisvert, Marilou; Parent, Jean-Luc; Lavigne, Pierre. "In-depth NMR characterization of Rab4a structure, nucleotide exchange and hydrolysis kinetics reveals an atypical GTPase profile" J. Struct. Biol. 212, 107582-107582 (2020).
PubMed: 32707235

Assembly members:

Assembly members:
entity_1, polymer, . residues, Formula weight is not available
entity_GDP, non-polymer, 443.201 Da.
entity_MG, non-polymer, 24.305 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: pet3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSETYDFLFKFLVIGNAGTG KSCLLHQFIEKKFKDDSNHT IGVEFGSKIINVGGKYVKLQ IWDTAGQERFRSVTRSYYRG AAGALLVYDITSRETYNALT NWLTDARMLASQNIVIILCG NKKDLDADREVTFLEASRFA QENELMFLETSALTGEDVEE AFVQCARKILNKHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	397
15N chemical shifts	136
1H chemical shifts	136

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rab4a	1
2	GDP	2
3	MG	3

Entities:

Entity 1, Rab4a - Formula weight is not available

1

MET

SER

GLU

THR

TYR

ASP

PHE

LEU

PHE

LYS

2

PHE

LEU

VAL

ILE

GLY

ASN

ALA

GLY

THR

GLY

3

LYS

SER

CYS

LEU

HIS

GLN

PHE

ILE

GLU

4

LYS

PHE

LYS

ASP

SER

ASN

HIS

THR

5

ILE

GLY

VAL

GLU

PHE

GLY

SER

LYS

ILE

6

ASN

VAL

GLY

LYS

TYR

VAL

LYS

LEU

GLN

7

ILE

TRP

ASP

THR

ALA

GLY

GLN

GLU

ARG

PHE

8

ARG

SER

VAL

THR

ARG

SER

TYR

ARG

GLY

9

ALA

GLY

ALA

LEU

VAL

TYR

ASP

ILE

10

THR

SER

ARG

GLU

THR

TYR

ASN

ALA

LEU

THR

11

ASN

TRP

LEU

THR

ASP

ALA

ARG

MET

LEU

ALA

12

SER

GLN

ASN

ILE

VAL

ILE

LEU

CYS

GLY

13

ASN

LYS

ASP

LEU

ASP

ALA

ASP

ARG

GLU

14

VAL

THR

PHE

LEU

GLU

ALA

SER

ARG

PHE

ALA

15

GLN

GLU

ASN

GLU

LEU

MET

PHE

LEU

GLU

THR

16

SER

ALA

LEU

THR

GLY

GLU

ASP

VAL

GLU

17

ALA

PHE

VAL

GLN

CYS

ALA

ARG

LYS

ILE

LEU

18

ASN

LYS

HIS

Entity 2, GDP - C10 H15 N5 O11 P2 - 443.201 Da.

1

GDP

Entity 3, MG - Mg - 24.305 Da.

1

MG

Samples:

sample_1: GUANOSINE-5'-DIPHOSPHATE, [U-99% 15N], 1 mM; Rab4a, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis v2.4.2 - chemical shift assignment

TOPSPIN v3.6.2 - collection

NMR spectrometers:

Bruker Avance 600 MHz

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