BMRB Entry 16824

Name: Solution Structure of the GTPase Binding Domain of WASP in Complex with EspFU, an EHEC Effector
Published: 2010-05-05

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PDB ID: 2k42
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16824
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of the GTPase Binding Domain of WASP in Complex with EspFU, an EHEC Effector

Deposition date:

2010-04-01

Original release date:

2010-05-05

Authors:

Cheng, Hui-Chun; Skehan, Brian; Campellone, Kenneth; Leong, John; Rosen, Michael

Citation:

Citation: Cheng, Hui-Chun; Skehan, Brian; Campellone, Kenneth; Leong, John; Rosen, Michael. "Structural Mechanism of WASP Activation by the Enterohaemorrhagic E. coli Effector EspFU" Nature 454, 1009-1013 (2008).
PubMed: 18650809

Assembly members:

Assembly members:
GBD, polymer, 72 residues, 8128.980 Da.
R33, polymer, 36 residues, 4070.712 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: pGEX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GBD: GHMSGFKHVSHVGWDPQNGF DVNNLDPDLRSLFSRAGISE AQLTDAETSKLIYDFIEDQG GLEAVRQEMRRQ
R33: GHMLPDVAQRLMQHLAEHGI QPARNMAEHIPPAPNW

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	444
15N chemical shifts	111
1H chemical shifts	728

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GBD	1
2	R33	2

Entities:

Entity 1, GBD 72 residues - 8128.980 Da.

1

GLY

HIS

MET

SER

GLY

PHE

LYS

HIS

VAL

SER

2

HIS

VAL

GLY

TRP

ASP

PRO

GLN

ASN

GLY

PHE

3

ASP

VAL

ASN

LEU

ASP

PRO

ASP

LEU

ARG

4

SER

LEU

PHE

SER

ARG

ALA

GLY

ILE

SER

GLU

5

ALA

GLN

LEU

THR

ASP

ALA

GLU

THR

SER

LYS

6

LEU

ILE

TYR

ASP

PHE

ILE

GLU

ASP

GLN

GLY

7

GLY

LEU

GLU

ALA

VAL

ARG

GLN

GLU

MET

ARG

8

ARG

GLN

Entity 2, R33 36 residues - 4070.712 Da.

1

GLY

HIS

MET

LEU

PRO

ASP

VAL

ALA

GLN

ARG

2

LEU

MET

GLN

HIS

LEU

ALA

GLU

HIS

GLY

ILE

3

GLN

PRO

ALA

ARG

ASN

MET

ALA

GLU

HIS

ILE

4

PRO

ALA

PRO

ASN

TRP

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

PDB	1EJ5 1T84 2K42 2K42 2KXC 2LNH
DBJ	BAJ20379
GB	AAA62663 AAA85515 AAC50140 AAC52556 AAC99855 EHU63438 EHV07820 EIN75194 EIN98845 EIN98874
PRF	2112369A 2122283A
REF	NP_000368 NP_001101718 NP_033541 XP_002831654 XP_003276872 WP_000807599 WP_001451998 WP_001457107 WP_001473124 WP_032163511
SP	P42768 P70315
BMRB	18165
AlphaFold	P42768 P70315

BMRB Entry 16824

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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