BMRB Entry 50180

Name: Cdc42 bound to GTP (AMPylation at T35)
Published: 2020-05-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50180

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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:

Cdc42 bound to GTP (AMPylation at T35)

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_Cdc42, polymer, 188 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: pOPINM

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1_Cdc42: HMQTIKCVVVGDGAVGKTCL LISYTTNKFPSEYVPTVFDN YAVTVMIGGEPYTLGLFDTA GLEDYDRLRPLSYPQTDVFL VCFSVVSPSSFENVKEKWVP EITHHCPKTPFLLVGTQIDL RDDPSTIEKLAKNKQKPITP ETAEKLARDLKAVKYVECSA LTQKGLKNVFDEAILAALEP PEPKKPKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1_AMP-T35-Cdc42:GTP

Data type	Count
15N chemical shifts	162
1H chemical shifts	171

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cdc42	1
2	GTP	2

Entities:

Entity 1, Cdc42 188 residues - Formula weight is not available

AMPylation at T35

1

HIS

MET

GLN

THR

ILE

LYS

CYS

VAL

2

GLY

ASP

GLY

ALA

VAL

GLY

LYS

THR

CYS

LEU

3

LEU

ILE

SER

TYR

THR

ASN

LYS

PHE

PRO

4

SER

GLU

TYR

VAL

PRO

THR

VAL

PHE

ASP

ASN

5

TYR

ALA

VAL

THR

VAL

MET

ILE

GLY

GLU

6

PRO

TYR

THR

LEU

GLY

LEU

PHE

ASP

THR

ALA

7

GLY

LEU

GLU

ASP

TYR

ASP

ARG

LEU

ARG

PRO

8

LEU

SER

TYR

PRO

GLN

THR

ASP

VAL

PHE

LEU

9

VAL

CYS

PHE

SER

VAL

SER

PRO

SER

10

PHE

GLU

ASN

VAL

LYS

GLU

LYS

TRP

VAL

PRO

11

GLU

ILE

THR

HIS

CYS

PRO

LYS

THR

PRO

12

PHE

LEU

VAL

GLY

THR

GLN

ILE

ASP

LEU

13

ARG

ASP

PRO

SER

THR

ILE

GLU

LYS

LEU

14

ALA

LYS

ASN

LYS

GLN

LYS

PRO

ILE

THR

PRO

15

GLU

THR

ALA

GLU

LYS

LEU

ALA

ARG

ASP

LEU

16

LYS

ALA

VAL

LYS

TYR

VAL

GLU

CYS

SER

ALA

17

LEU

THR

GLN

LYS

GLY

LEU

LYS

ASN

VAL

PHE

18

ASP

GLU

ALA

ILE

LEU

ALA

LEU

GLU

PRO

19

PRO

GLU

PRO

LYS

PRO

LYS

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