BMRB Entry 16374

Name: Solution Structure of C-terminal domain of reduced NleG2-3 (residue 90-191) from Pathogenic E. coli O157:H7. Northeast Structural Genomics Consortium and Midwest Center for Structural Genomics target ET109A
Published: 2009-09-15

Click here to enlarge.

PDB ID: 2kkx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16374
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution Structure of C-terminal domain of reduced NleG2-3 (residue 90-191) from Pathogenic E. coli O157:H7. Northeast Structural Genomics Consortium and Midwest Center for Structural Genomics target ET109A

Deposition date:

2009-06-29

Original release date:

2009-09-15

Authors:

Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Semest, Anthony; Claude, Marie; Singer, Alexander; Edwards, Aled; Savchenko, Alexei; Arrowsmith, Cheryl

Citation:

Citation: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Semest, Anthony; Claude, Marie; Coomes, Brian; Edwards, Aled; Singer, Alexander; Arrowsmith, Cheryl; Savchenko, Alexei. "Pathogenic E. coli O157:H7 NleG family of Type 3 secretion effectors features a common C-terminal U-box domain and E3 ubiquitin ligase activity" .

Assembly members:

Assembly members:
NleG2-3, polymer, 102 residues, 11290.936 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NleG2-3: SQESIQNKISQCKFSVCPER LQCPLEAIQCPITLEQPEKG IFVKNSDGSDVCTLFDAAAF SRLVGEGLPHPLTREPITAS IIVKHEECIYDDTRGNFIIK GN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	432
15N chemical shifts	104
1H chemical shifts	721
residual dipolar couplings	186

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NleG2-3	1

Entities:

Entity 1, NleG2-3 102 residues - 11290.936 Da.

1

SER

GLN

GLU

SER

ILE

GLN

ASN

LYS

ILE

SER

2

GLN

CYS

LYS

PHE

SER

VAL

CYS

PRO

GLU

ARG

3

LEU

GLN

CYS

PRO

LEU

GLU

ALA

ILE

GLN

CYS

4

PRO

ILE

THR

LEU

GLU

GLN

PRO

GLU

LYS

GLY

5

ILE

PHE

VAL

LYS

ASN

SER

ASP

GLY

SER

ASP

6

VAL

CYS

THR

LEU

PHE

ASP

ALA

PHE

7

SER

ARG

LEU

VAL

GLY

GLU

GLY

LEU

PRO

HIS

8

PRO

LEU

THR

ARG

GLU

PRO

ILE

THR

ALA

SER

9

ILE

VAL

LYS

HIS

GLU

CYS

ILE

TYR

10

ASP

THR

ARG

GLY

ASN

PHE

ILE

LYS

11

GLY

ASN

Samples:

sample_1: NleG, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; H2O 90%; D2O 10%

sample_2: NleG, [U-7% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D IPAP-J HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

MDDGUI v1.0, Gutmanas and Arrowsmith - processing

SPARKY v3.95, Goddard - data analysis, peak picking

FAWN v1.0, Lemak and Arrowsmith - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment

PSVS, Bhattacharya and Montelione - NMR structure quality assessment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

BMRB	16375
PDB	2KKX 2KKY
DBJ	BAB35417 BAB35579 BAI25254 BAI35676
EMBL	CTT86631 CTZ63346 CTZ65248 CTZ72681 CTZ98837
GB	AAG56215 AAG56388 ACI35420 ACT71854 ADD56326
REF	NP_310021 NP_310183 WP_001131656 WP_001131657 WP_001131658