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Biological Magnetic Resonance Data Bank


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BMRB Entry 17525

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17525
MolProbity Validation Chart

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Title: ATR13 Chemical Shifts   PubMed: 22194684

Deposition date: 2011-03-15 Original release date: 2012-01-18

Authors: Leonelli, Lauriebeth; Pelton, Jeffrey; Wemmer, David; Staskawicz, Brian

Citation: Leonelli, Lauriebeth; Pelton, Jeffery; Schoeffler, Allyn; Dahlbeck, Douglas; Berger, James; Wemmer, David; Staskawicz, Brian. "Structural Elucidation and Functional Characterization of the Hyaloperonospora arabidopsidis Effector Protein ATR13"  Plos Pathog. 7, e1002428-e1002428 (2011).

Assembly members:
ATR13, polymer, 202 residues, 22593.979 Da.

Natural source:   Common Name: Hyaloperonospora parasitica   Taxonomy ID: 123356   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Hyaloperonospora parasitica

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

Entity Sequences (FASTA):
ATR13: SFGLGKAQDPLDKFFSKIIF SGKPIETSYSAKGIHEKIIE AHDLHVSKSKNAPIQYASVM EYLKKTYPGPDIERIVSTLE RHDEVGAKDLGAKLRDALDR QSFGLGKAQDPLDKFFSKII FSGKPIETSYSAKGIHEKII EAHDLHVSKSKNAPIQYASV MEYLKKTYPGPDIERIVSTL ERHDEVGAKDLGAKLRDALD RQ

Data sets:
Data typeCount
13C chemical shifts320
15N chemical shifts77
1H chemical shifts479

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ATR131

Entities:

Entity 1, ATR13 202 residues - 22593.979 Da.

1   SERPHEGLYLEUGLYLYSALAGLNASPPRO
2   LEUASPLYSPHEPHESERLYSILEILEPHE
3   SERGLYLYSPROILEGLUTHRSERTYRSER
4   ALALYSGLYILEHISGLULYSILEILEGLU
5   ALAHISASPLEUHISVALSERLYSSERLYS
6   ASNALAPROILEGLNTYRALASERVALMET
7   GLUTYRLEULYSLYSTHRTYRPROGLYPRO
8   ASPILEGLUARGILEVALSERTHRLEUGLU
9   ARGHISASPGLUVALGLYALALYSASPLEU
10   GLYALALYSLEUARGASPALALEUASPARG
11   GLNSERPHEGLYLEUGLYLYSALAGLNASP
12   PROLEUASPLYSPHEPHESERLYSILEILE
13   PHESERGLYLYSPROILEGLUTHRSERTYR
14   SERALALYSGLYILEHISGLULYSILEILE
15   GLUALAHISASPLEUHISVALSERLYSSER
16   LYSASNALAPROILEGLNTYRALASERVAL
17   METGLUTYRLEULYSLYSTHRTYRPROGLY
18   PROASPILEGLUARGILEVALSERTHRLEU
19   GLUARGHISASPGLUVALGLYALALYSASP
20   LEUGLYALALYSLEUARGASPALALEUASP
21   ARGGLN

Samples:

sample_1: ATR13, [U-100% 13C; U-100% 15N], 1 ± 0.1 mM; potassium phosphate 20 ± 1 mM; sodium chloride 150 ± 5 mM; D2O, [U-99% 2H], 10 ± 0.5 %; H2O 90%

sample_2: ATR13, [U-98% 15N], 1 ± 0.1 mM; potassium phosphate 20 ± 1 mM; sodium chloride 150 ± 5 mM; D2O, [U-99% 2H], 10 ± 1 %; H2O 90%

sample_3: ATR13, [U-10% 13C; U-99% 15N], 1 ± 0.1 mM; potassium phosphate 20 ± 1 mM; sodium chloride 150 ± 5 mM; D2O, [U-99% 2H], 10 ± 1 %; H2O 90%

sample_4: ATR13, [U-98% 15N], 1 ± 0.1 mM; potassium phosphate 20 ± 1 mM; sodium chloride 150 ± 5 mM; D2O, [U-99% 2H], 10 ± 1 %; Pf1 phage 12 ± 1 mg/ml; H2O 90%

sample_conditions_1: ionic strength: 210 mM; pH: 7.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D IPAPsample_4anisotropicsample_conditions_1
2D 15N Heteronuclear NOEsample_2isotropicsample_conditions_1

Software:

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment

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

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance II 900 MHz

Related Database Links:

PDB
GB AAW63765 AAW63767 AAW63768

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