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 15557

Title: 1H, 13C, and 15N Chemical Shift Assignment for actin depolymerizing and dynamics regulatory protein from Leishmania donovani   PubMed: 19844807

Deposition date: 2007-11-17 Original release date: 2009-11-20

Authors: Pathak, Prem Prakash; Pulavarti, S.V.S.R. Krishna; Jain, Anupam; Sahasrabuddhe, Amogh Anant; Gupta, Chhitar Mal; Arora, Ashish

Citation: Pathak, Prem Prakash; Pulavarti, S V S R Krishna; Jain, Anupam; Sahasrabuddhe, Amogh Anant; Gupta, Chittar Mal; Arora, Ashish. "NMR assignment of actin depolymerizing and dynamics regulatory protein from Leishmania donovani."  Biomol. NMR Assignments 3, 265-267 (2009).

Assembly members:
Actin_Depolymerzing_Factor, polymer, 150 residues, Formula weight is not available

Natural source:   Common Name: Leishmania donovani   Taxonomy ID: 5661   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Leishmania donovani

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

Entity Sequences (FASTA):
Actin_Depolymerzing_Factor: MAISGVTLEESVRGAIDDLR MKKSRYVMMCIGADGKKIEV TEVGERSVNYTDLKEKFSTE KPCYVAFDFEYNDAGSKREK LILIQWIPDTARPREKMMYS ASRDALSSVSEGYLPIQAND ESGLDAEEIIRKVRLHRSVA AALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts571
15N chemical shifts141
1H chemical shifts886

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ADF monomer1

Entities:

Entity 1, ADF monomer 150 residues - Formula weight is not available

1   METALAILESERGLYVALTHRLEUGLUGLU
2   SERVALARGGLYALAILEASPASPLEUARG
3   METLYSLYSSERARGTYRVALMETMETCYS
4   ILEGLYALAASPGLYLYSLYSILEGLUVAL
5   THRGLUVALGLYGLUARGSERVALASNTYR
6   THRASPLEULYSGLULYSPHESERTHRGLU
7   LYSPROCYSTYRVALALAPHEASPPHEGLU
8   TYRASNASPALAGLYSERLYSARGGLULYS
9   LEUILELEUILEGLNTRPILEPROASPTHR
10   ALAARGPROARGGLULYSMETMETTYRSER
11   ALASERARGASPALALEUSERSERVALSER
12   GLUGLYTYRLEUPROILEGLNALAASNASP
13   GLUSERGLYLEUASPALAGLUGLUILEILE
14   ARGLYSVALARGLEUHISARGSERVALALA
15   ALAALALEUGLUHISHISHISHISHISHIS

Samples:

sample_1: Actin Depolymerzing Factor, [U-13C; U-15N], 1.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.1%; DTT 1 mM; D2O 5%; AEBSF protease inhibitor 1 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 HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CARA vCara_1.8.3_linux [4], Bartels et al., Cornilescu, Delaglio and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Keller and Wuthrich - chemical shift assignment, chemical shift assignment, processing

NMR spectrometers:

  • Varian UnityINOVA 600 MHz

Related Database Links:

PDB
EMBL CAM69611 CBZ12381 CBZ35776
GB AAY99389
REF XP_001466572 XP_003722124 XP_003862469

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