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

Samples:

sample_1: GBD/R33 complex, [U-100% 13C; U-100% 15N], 1 – 1.5 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_2: GBD/R33 complex, [U-100% 13C; U-100% 15N], 1 – 1.5 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; D2O 100%

sample_3: R33 1 mM; GBD, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; D2O 100%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298.15 K

Experiments:

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

Software:

ARIA v2.1, Linge, O'Donoghue and Nilges - refinement, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMRView, Johnson, One Moon Scientific - peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 500 MHz

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