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 15938

Title: p190-A RhoGAP FF1 domain   PubMed: 19393245

Deposition date: 2008-09-02 Original release date: 2009-04-29

Authors: Bonet, Roman; Ruiz, Lidia; Martin-Malpartida, Pau; Macias, Maria

Citation: Bonet, Roman; Ruiz, Lidia; Aragon, E.; Martin-Malpartida, Pau; Macias, Maria. "NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding"  J. Mol. Biol. 389, 230-237 (2009).

Assembly members:
p190-A_RhoGAP_FF1_domain, polymer, 69 residues, 7857.032 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):
p190-A_RhoGAP_FF1_domain: GAMGSQQIATAKDKYEWLVS RIVKNHNENWLSVSRKMQAS PEYQDYVYLEGTQKAKKLFL QHIHRLKHE

Data sets:
Data typeCount
13C chemical shifts233
15N chemical shifts72
1H chemical shifts482

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p190-A_RhoGAP_FF1_domain1

Entities:

Entity 1, p190-A_RhoGAP_FF1_domain 69 residues - 7857.032 Da.

Residues 1-4 remain from the cloning after cleavage of the tag.

1   GLYALAMETGLYSERGLNGLNILEALATHR
2   ALALYSASPLYSTYRGLUTRPLEUVALSER
3   ARGILEVALLYSASNHISASNGLUASNTRP
4   LEUSERVALSERARGLYSMETGLNALASER
5   PROGLUTYRGLNASPTYRVALTYRLEUGLU
6   GLYTHRGLNLYSALALYSLYSLEUPHELEU
7   GLNHISILEHISARGLEULYSHISGLU

Samples:

sample_1: p190-A RhoGAP FF1 domain 1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.5 mM

sample_2: p190-A RhoGAP FF1 domain, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.5 mM

sample_3: p190-A RhoGAP FF1 domain, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

ARIA, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

XEASY, Bartels et al. - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker AMX 600 MHz

Related Database Links:

PDB
DBJ BAB21813 BAD32520 BAE27848 BAE28076 BAE36578
GB AAF80386 AAI31566 AAI39460 AAI39462 AAI50258
REF NP_001003022 NP_001179327 NP_001258061 NP_004482 NP_766327
SP P81128 P83509 Q91YM2 Q9NRY4
TPG DAA19691

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