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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 18165

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PDB ID:
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/BMR18165
MolProbity Validation Chart

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Title: Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to hijack host F-actin assembly   PubMed: 22921828

Deposition date: 2011-12-28 Original release date: 2012-08-27

Authors: Aitio, Olli; Hellman, Maarit; Skehan, Brian; Kesti, Tapio; Leong, John; Saksela, Kalle; Permi, Perttu

Citation: Aitio, Olli; Hellman, Maarit; Skehan, Brian; Kesti, Tapio; Leong, John; Saksela, Kalle; Permi, Perttu. "Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly."  Structure 20, 1692-1703 (2012).

Assembly members:
entity_1, polymer, 65 residues, 7262.089 Da.
entity_2, polymer, 67 residues, 7559.687 Da.
entity_3, polymer, 48 residues, 5244.970 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity_1: GSNFQHIGHVGWDPNTGFDL NNLDPELKNLFDMCGISEAQ LKDRETSKVIYDFIEKTGGV EAVKN
entity_2: GSHMKKQKVKTIFPHTAGSN KTLLSFAQGDVITLLIPEEK DGWLYGEHDVSKARGWFPSS YTKLLEE
entity_3: GLPDVAQRLMQHLAEHGIQP ARNMAEHIPPAPNWPAPTPP VQNEQSRP

Data sets:
Data typeCount
13C chemical shifts584
15N chemical shifts158
1H chemical shifts1179

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_33

Entities:

Entity 1, entity_1 65 residues - 7262.089 Da.

1   GLYSERASNPHEGLNHISILEGLYHISVAL
2   GLYTRPASPPROASNTHRGLYPHEASPLEU
3   ASNASNLEUASPPROGLULEULYSASNLEU
4   PHEASPMETCYSGLYILESERGLUALAGLN
5   LEULYSASPARGGLUTHRSERLYSVALILE
6   TYRASPPHEILEGLULYSTHRGLYGLYVAL
7   GLUALAVALLYSASN

Entity 2, entity_2 67 residues - 7559.687 Da.

1   GLYSERHISMETLYSLYSGLNLYSVALLYS
2   THRILEPHEPROHISTHRALAGLYSERASN
3   LYSTHRLEULEUSERPHEALAGLNGLYASP
4   VALILETHRLEULEUILEPROGLUGLULYS
5   ASPGLYTRPLEUTYRGLYGLUHISASPVAL
6   SERLYSALAARGGLYTRPPHEPROSERSER
7   TYRTHRLYSLEULEUGLUGLU

Entity 3, entity_3 48 residues - 5244.970 Da.

1   GLYLEUPROASPVALALAGLNARGLEUMET
2   GLNHISLEUALAGLUHISGLYILEGLNPRO
3   ALAARGASNMETALAGLUHISILEPROPRO
4   ALAPROASNTRPPROALAPROTHRPROPRO
5   VALGLNASNGLUGLNSERARGPRO

Samples:

sample_1: entity_1, [U-98% 13C; U-98% 15N], 0.3 mM; entity_2 0.3 mM; entity_3 0.3 mM; H2O 93%; D2O 7%; Na-PO4 20 mM; NaCl 50 mM

sample_2: entity_1 0.5 mM; entity_2, [U-98% 13C; U-98% 15N], 0.5 mM; entity_3 0.5 mM; H2O 93%; D2O 7%; Na-PO4 20 mM; NaCl 50 mM

sample_3: entity_1 0.5 mM; entity_2 0.5 mM; entity_3, [U-98% 13C; U-98% 15N], 0.5 mM; H2O 93%; D2O 7%; Na-PO4 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

SPARKY v3.110, Goddard - chemical shift assignment

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

AMBER v8.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 26643 16909 16824
PDB
DBJ BAA11082 BAA21534 BAE25143 BAE25639 BAE28201 BAB15671
EMBL CAC69994 CAH89371 CAH91010 CAL26602
GB AAH52955 AAH55045 AAI51608 AAQ96857 AAV38348 AAD20937 AAF17223 AAH13888 ACE87078 ACE87758 EHU63438 EHW64582 EIO83229 EKW91176 ELV28821
REF NP_001103835 NP_001128797 NP_001253726 NP_003932 NP_082735 NP_061330 XP_001110709 XP_002817749 XP_003278101 XP_003895772 WP_000807599 WP_001431335 WP_032163511 WP_032165213 WP_032271112
SP O00401 O08816 Q91YD9 Q95107 Q9UHR4
TPG DAA30422

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