BMRB Entry 17739

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PDB ID: 2lf6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17739
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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:

Solution NMR structure of HopABPph1448_220_320 from Pseudomonas syringae pv. phaseolicola str. 1448A, Midwest Center for Structural Genomics target APC40132.4 and Northeast Structural Genomics Consortium target PsT3A

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:

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).
PubMed: 22191472

Assembly members:

Assembly members:
HopAB1Pph1448_220_320, polymer, 101 residues, 11275.805 Da.

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 264730 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas Pseudomonas savastanoi

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p15Tv lic

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HopAB1Pph1448_220_320: QGLDLESARLASAARHNHSA NQTNEALRRLTQEGVDMERL RTSLGRYIMSLEPLPPDLRR ALESVGINPFIPEELSLVDH PVLNFSAALNRMLASRQTTT N

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	388
15N chemical shifts	90
1H chemical shifts	657

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HopABPph1448_220_320	1

Entities:

Entity 1, HopABPph1448_220_320 101 residues - 11275.805 Da.

1

GLN

GLY

LEU

ASP

LEU

GLU

SER

ALA

ARG

LEU

2

ALA

SER

ALA

ARG

HIS

ASN

HIS

SER

ALA

3

ASN

GLN

THR

ASN

GLU

ALA

LEU

ARG

LEU

4

THR

GLN

GLU

GLY

VAL

ASP

MET

GLU

ARG

LEU

5

ARG

THR

SER

LEU

GLY

ARG

TYR

ILE

MET

SER

6

LEU

GLU

PRO

LEU

PRO

ASP

LEU

ARG

7

ALA

LEU

GLU

SER

VAL

GLY

ILE

ASN

PRO

PHE

8

ILE

PRO

GLU

LEU

SER

LEU

VAL

ASP

HIS

9

PRO

VAL

LEU

ASN

PHE

SER

ALA

LEU

ASN

10

ARG

MET

LEU

ALA

SER

ARG

GLN

THR

11

ASN

Samples:

sample_1: HopAB1Pph1448_220_320, [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_2: HopAB1Pph1448_220_320, [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-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

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, data analysis

FAWN v1.0, 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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2LF6
EMBL	CAD29302 CAM12730
GB	AAD47203 AAV68746 AAZ37972 EFW77542 EGH05285
REF	WP_011282445 WP_032074514 WP_032701278 WP_032706902 WP_044320005
SP	Q48B61 Q8RK09 Q9RBW3
AlphaFold	Q48B61 Q8RK09 Q9RBW3