BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17737

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:
Data typeCount
13C chemical shifts430
15N chemical shifts108
1H chemical shifts730

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HopPmal_281_3851

Entities:

Entity 1, HopPmal_281_385 105 residues - 11582.251 Da.

1   SERGLNARGPROVALASPARGASNPROPRO
2   ARGILEASNLEUMETPROTHRGLYALAASN
3   ARGVALALAMETARGASNARGGLYASNASN
4   GLUALAASPALAALALEUGLNALALEUALA
5   GLNASNGLYILEASNMETGLUASPLEUARG
6   ALAALALEUGLUALATYRILEVALTRPLEU
7   ARGPROILEPROLEUASPILEALAASNALA
8   LEUGLUGLYVALGLYILETHRPROARGPHE
9   ASPASNPROGLUGLUALALYSVALASPASN
10   PROLEUMETASNLEUSERSERALALEULYS
11   ARGARGLEUASPALA

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:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_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

Related Database Links:

PDB
GB AAL84252 EGH63218 KPB74312 KPW15450
REF WP_042911960
SP Q8RP04

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts