BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16824

Title: Solution Structure of the GTPase Binding Domain of WASP in Complex with EspFU, an EHEC Effector   PubMed: 18650809

Deposition date: 2010-04-01 Original release date: 2010-05-05

Authors: Cheng, Hui-Chun; Skehan, Brian; Campellone, Kenneth; Leong, John; Rosen, Michael

Citation: Cheng, Hui-Chun; Skehan, Brian; Campellone, Kenneth; Leong, John; Rosen, Michael. "Structural Mechanism of WASP Activation by the Enterohaemorrhagic E. coli Effector EspFU"  Nature 454, 1009-1013 (2008).

Assembly members:
GBD, polymer, 72 residues, 8128.980 Da.
R33, polymer, 36 residues, 4070.712 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):
GBD: GHMSGFKHVSHVGWDPQNGF DVNNLDPDLRSLFSRAGISE AQLTDAETSKLIYDFIEDQG GLEAVRQEMRRQ
R33: GHMLPDVAQRLMQHLAEHGI QPARNMAEHIPPAPNW

Data sets:
Data typeCount
13C chemical shifts444
15N chemical shifts111
1H chemical shifts728

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GBD1
2R332

Entities:

Entity 1, GBD 72 residues - 8128.980 Da.

1   GLYHISMETSERGLYPHELYSHISVALSER
2   HISVALGLYTRPASPPROGLNASNGLYPHE
3   ASPVALASNASNLEUASPPROASPLEUARG
4   SERLEUPHESERARGALAGLYILESERGLU
5   ALAGLNLEUTHRASPALAGLUTHRSERLYS
6   LEUILETYRASPPHEILEGLUASPGLNGLY
7   GLYLEUGLUALAVALARGGLNGLUMETARG
8   ARGGLN

Entity 2, R33 36 residues - 4070.712 Da.

1   GLYHISMETLEUPROASPVALALAGLNARG
2   LEUMETGLNHISLEUALAGLUHISGLYILE
3   GLNPROALAARGASNMETALAGLUHISILE
4   PROPROALAPROASNTRP

Samples:

sample_1: GBD/R33 complex, [U-100% 13C; U-100% 15N], 1 – 1.5 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_2: GBD/R33 complex, [U-100% 13C; U-100% 15N], 1 – 1.5 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; D2O 100%

sample_3: R33 1 mM; GBD, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; D2O 100%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
4D 13C-13C NOESYsample_2isotropicsample_conditions_1
3D 13C-filtered NOESYsample_3isotropicsample_conditions_1

Software:

ARIA v2.1, Linge, O, . - refinement, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMRView, Johnson, One Moon Scientific - peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAJ20379
GB AAA62663 AAA85515 AAC50140 AAC52556 AAC99855 EHU63438 EHV07820 EIN75194 EIN98845 EIN98874
PRF 2112369A 2122283A
REF NP_000368 NP_001101718 NP_033541 XP_002831654 XP_003276872 WP_000807599 WP_001451998 WP_001457107 WP_001473124 WP_032163511
SP P42768 P70315
BMRB 18165

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