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Biological Magnetic Resonance Data Bank


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BMRB Entry 17278

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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/BMR17278
MolProbity Validation Chart

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Title: NMR assignment of actin depolymerizing and dynamics regulatory protein from toxoplasma gondii

Deposition date: 2010-11-03 Original release date: 2010-11-15

Authors: Shukla, Vaibhav Kumar; Pathak, Prem Prakash; Yadav, Rahul; Srivastava, Shubhra; Jain, Anupam; Pulavarti, S.V.S.R. Krishna

Citation: Shukla, Vaibhav Kumar; Pathak, Prem Prakash; Yadav, Rahul; Srivastava, Shubhra; Jain, Anupam; Pulavarti, S.V.S.R. Krishna; Arora, Ashish. "NMR assignment of actin depolymerizing and dynamics regulatory protein from Toxoplasma gondii"  Biomol. NMR Assignments ., .-..

Assembly members:
TgADF, polymer, 118 residues, Formula weight is not available

Natural source:   Common Name: Toxoplasma gondii   Taxonomy ID: 5811   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Toxoplasma gondii

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

Entity Sequences (FASTA):
TgADF: MASGMGVDENCVARFNELKI RKTVKWIVFKIENTKIVVEK DGKGNADEFRGALPANDCRF GVYDCGNKIQFVLWCPDNAP VKPRMTYASSKDALLKKLDG ATAVALEAHEMGDLAPLA

Data sets:
Data typeCount
13C chemical shifts478
15N chemical shifts109
1H chemical shifts721

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Monomer1

Entities:

Entity 1, Monomer 118 residues - Formula weight is not available

1   METALASERGLYMETGLYVALASPGLUASN
2   CYSVALALAARGPHEASNGLULEULYSILE
3   ARGLYSTHRVALLYSTRPILEVALPHELYS
4   ILEGLUASNTHRLYSILEVALVALGLULYS
5   ASPGLYLYSGLYASNALAASPGLUPHEARG
6   GLYALALEUPROALAASNASPCYSARGPHE
7   GLYVALTYRASPCYSGLYASNLYSILEGLN
8   PHEVALLEUTRPCYSPROASPASNALAPRO
9   VALLYSPROARGMETTHRTYRALASERSER
10   LYSASPALALEULEULYSLYSLEUASPGLY
11   ALATHRALAVALALALEUGLUALAHISGLU
12   METGLYASPLEUALAPROLEUALA

Samples:

sample_1: potassium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.1%; DTT 1 mM; AEBSF protease inhibitor 1 mM; H2O 95%; D2O 5%; TgADF, [U-100% 13C; U-100% 15N], 0.8 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
HBCB(CGCD)HDsample_1isotropicsample_conditions_1
HBCB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAC47717 EPR57074 EPT31140 ESS28466 KFG28323
REF XP_002371565
TPE CEL72722

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