BMRB Entry 50174

Name: Rab1b bound to GTP (AMPylation at Y77)
Published: 2020-05-30

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50174

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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:

Rab1b bound to GTP (AMPylation at Y77)

Deposition date:

2020-01-28

Original release date:

2020-05-30

Authors:

Kang, Hyun-Seo; Barthelmes, Katja; Sattler, Michael

Citation:

Citation: Barthelmes, Katja; Ramcke, Evelyn; Kang, Hyun-Seo; Sattler, Michael; Itzen, Aymelt. "Conformational Control of Small GTPases by AMPylation" Proc. Natl. Acad. Sci. U.S.A. 117, 5772-5781 (2020).
PubMed: 32123090

Assembly members:

Assembly members:
entity_1_Rab1b, polymer, 173 residues, Formula weight is not available
entity_GTP, non-polymer, 523.180 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: pMAL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1_Rab1b: MPEYDYLFKLLLIGDSGVGK SCLLLRFADDTYTESYISTI GVDFKIRTIELDGKTIKLQI WDTAGAERFRTITSSYYRGA HGIIVVYDVTDQESYANVKQ WLQEIDRYASENVNKLLVGN KSDLTTKKVVDNTTAKEFAD SLGIPFLETSAKNATNVEQA FMTMAAEIKKRMG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1_Rab1b-GTP

Data type	Count
13C chemical shifts	378
15N chemical shifts	145
1H chemical shifts	159

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rab1b	1
2	GTP	2

Entities:

Entity 1, Rab1b 173 residues - Formula weight is not available

AMPylation at Y77

1

MET

PRO

GLU

TYR

ASP

TYR

LEU

PHE

LYS

LEU

2

LEU

ILE

GLY

ASP

SER

GLY

VAL

GLY

LYS

3

SER

CYS

LEU

ARG

PHE

ALA

ASP

4

THR

TYR

THR

GLU

SER

TYR

ILE

SER

THR

ILE

5

GLY

VAL

ASP

PHE

LYS

ILE

ARG

THR

ILE

GLU

6

LEU

ASP

GLY

LYS

THR

ILE

LYS

LEU

GLN

ILE

7

TRP

ASP

THR

ALA

GLY

ALA

GLU

ARG

PHE

ARG

8

THR

ILE

THR

SER

TYR

ARG

GLY

ALA

9

HIS

GLY

ILE

VAL

TYR

ASP

VAL

THR

10

ASP

GLN

GLU

SER

TYR

ALA

ASN

VAL

LYS

GLN

11

TRP

LEU

GLN

GLU

ILE

ASP

ARG

TYR

ALA

SER

12

GLU

ASN

VAL

ASN

LYS

LEU

VAL

GLY

ASN

13

LYS

SER

ASP

LEU

THR

LYS

VAL

14

ASP

ASN

THR

ALA

LYS

GLU

PHE

ALA

ASP

15

SER

LEU

GLY

ILE

PRO

PHE

LEU

GLU

THR

SER

16

ALA

LYS

ASN

ALA

THR

ASN

VAL

GLU

GLN

ALA

17

PHE

MET

THR

MET

ALA

GLU

ILE

LYS

18

ARG

MET

GLY

Entity 2, GTP - C10 H16 N5 O14 P3 - 523.180 Da.

1

GTP

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.3 mM; HEPES 20 mM; DTE 2 mM; sodium chloride 50 mM; MgCl2 1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CcpNMR, CCPN - chemical shift assignment

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