BMRB Entry 17737

Name: Solution NMR structure of HopPmal_281_385 from Pseudomonas syringae pv. maculicola str. ES4326, Midwest Center for Structural Genomics target APC40104.5 and Northeast Structural Genomics Consortium target PsT2A
Published: 2011-07-18

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PDB ID: 2lf3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17737
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR structure of HopPmal_281_385 from Pseudomonas syringae pv. maculicola str. ES4326, Midwest Center for Structural Genomics target APC40104.5 and Northeast Structural Genomics Consortium target PsT2A PubMed: 22191472

Deposition date: 2011-06-28 Original release date: 2011-07-18

Authors: Wu, Bin; Yee, Adelinda; Houliston, Scott; Semesi, Anthony; Garcia, Maite; Singer, Alexander; Savchenko, Alexei; Arrowsmith, Cheryl

Citation: Singer, Alex; Wu, Bin; Yee, Adelinda; Houliston, Scott; Xu, Xiaohui; Cui, Hong; Skarina, Tatiana; Garcia, Maite; Semesi, Anthony; Arrowsmith, Cheryl; Savchenko, Alexei. "Structural analysis of HopPmaL reveals the presence of a second adaptor domain common to the HopAB family of Pseudomonas syringae type III effectors." Biochemistry 51, 1-3 (2012).

Assembly members:
entity, polymer, 105 residues, 11582.251 Da.

Natural source: Common Name: Pseudomonas syringae pv. maculicola str. ES4326 Taxonomy ID: 629265 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas Pseudomonas syringae group genomosp. 3

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

Entity Sequences (FASTA):
entity: SQRPVDRNPPRINLMPTGAN RVAMRNRGNNEADAALQALA QNGINMEDLRAALEAYIVWL RPIPLDIANALEGVGITPRF DNPEEAKVDNPLMNLSSALK RRLDA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	430
15N chemical shifts	108
1H chemical shifts	730

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HopPmal_281_385	1

Entities:

Entity 1, HopPmal_281_385 105 residues - 11582.251 Da.

1

SER

GLN

ARG

PRO

VAL

ASP

ARG

ASN

PRO

2

ARG

ILE

ASN

LEU

MET

PRO

THR

GLY

ALA

ASN

3

ARG

VAL

ALA

MET

ARG

ASN

ARG

GLY

ASN

4

GLU

ALA

ASP

ALA

LEU

GLN

ALA

LEU

ALA

5

GLN

ASN

GLY

ILE

ASN

MET

GLU

ASP

LEU

ARG

6

ALA

LEU

GLU

ALA

TYR

ILE

VAL

TRP

LEU

7

ARG

PRO

ILE

PRO

LEU

ASP

ILE

ALA

ASN

ALA

8

LEU

GLU

GLY

VAL

GLY

ILE

THR

PRO

ARG

PHE

9

ASP

ASN

PRO

GLU

ALA

LYS

VAL

ASP

ASN

10

PRO

LEU

MET

ASN

LEU

SER

ALA

LEU

LYS

11

ARG

LEU

ASP

ALA

Samples:

sample_1: HopPmal_281_385, [U-100% 13C; U-100% 15N], 0.3 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; NaN3 0.01%; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%

sample_2: HopPmal_281_385, [U-100% 13C; U-100% 15N], 1 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; NaN3 0.01%; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%

sample_3: HopPmal_281_385, [U-7% 13C; U-100% 15N], 0.2 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; NaN3 0.01%; benzamidine 10 mM; inhibitor cocktail 1 x; 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-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1

Software:

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

MDDGUI v1.0, Gutmanas, Arrowsmith - processing

SPARKY v3.95, Goddard - data analysis

FMCGUI v2.4, Lemak, Arrowsmith - chemical shift assignment

CYANA v3.0, 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

FAWN, Lemak, Arrowsmith - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2LF3
GB	AAL84252 EGH63218 KPB74312 KPW15450
REF	WP_042911960
SP	Q8RP04

Biological Magnetic Resonance Data Bank