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 18377

Title: MTIP(61-204) from Plasmodium falciparum bound to peptide MyoA(799-818)   PubMed: 22932904

Deposition date: 2012-04-03 Original release date: 2012-04-16

Authors: Douse, Christopher

Citation: Douse, Christopher; Green, Judith; Salgado, Paula; Simpson, Peter; Thomas, Jemima; Langsley, Gordon; Holder, Anthony; Tate, Edward; Cota, Ernesto. "Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA."  J. Biol. Chem. 287, 36968-36977 (2012).

Assembly members:
MTIP(61-204), polymer, 154 residues, 17605 Da.
MyoA(799-818)_peptide, polymer, 20 residues, 2372.91 Da.

Natural source:   Common Name: not available   Taxonomy ID: 5833   Superkingdom: not available   Kingdom: Plasmodium   Genus/species: falciparum not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
MTIP(61-204): RGSHHHHHHGSVADIQQLEE KVDESDVRIYFNEKSSGGKI SIDNASYNARKLGLAPSSID EKKIKELYGDNLTYEQYLEY LSICVHDKDNVEELIKMFAH FDNNCTGYLTKSQMKNILTT WGDALTDQEAIDALNAFSSE DNIDYKLFCEDILQ
MyoA(799-818)_peptide: KNIPSLLRVQAHIRKKMVAQ

Data sets:
Data typeCount
13C chemical shifts423
15N chemical shifts142
1H chemical shifts142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MTIP(61-204)1
2MyoA(799-818)2

Entities:

Entity 1, MTIP(61-204) 154 residues - 17605 Da.

1   ARGGLYSERHISHISHISHISHISHISGLY
2   SERVALALAASPILEGLNGLNLEUGLUGLU
3   LYSVALASPGLUSERASPVALARGILETYR
4   PHEASNGLULYSSERSERGLYGLYLYSILE
5   SERILEASPASNALASERTYRASNALAARG
6   LYSLEUGLYLEUALAPROSERSERILEASP
7   GLULYSLYSILELYSGLULEUTYRGLYASP
8   ASNLEUTHRTYRGLUGLNTYRLEUGLUTYR
9   LEUSERILECYSVALHISASPLYSASPASN
10   VALGLUGLULEUILELYSMETPHEALAHIS
11   PHEASPASNASNCYSTHRGLYTYRLEUTHR
12   LYSSERGLNMETLYSASNILELEUTHRTHR
13   TRPGLYASPALALEUTHRASPGLNGLUALA
14   ILEASPALALEUASNALAPHESERSERGLU
15   ASPASNILEASPTYRLYSLEUPHECYSGLU
16   ASPILELEUGLN

Entity 2, MyoA(799-818) 20 residues - 2372.91 Da.

1   LYSASNILEPROSERLEULEUARGVALGLN
2   ALAHISILEARGLYSLYSMETVALALAGLN

Samples:

sample_1: MTIP(61-204), [U-98% 13C; U-98% 15N], 0.5 mM; MOPS buffer' 'natural abundance; .; .; . %; . %; 2, $MyoA(799-818)_peptide, ; .

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18376
PDB
EMBL CDO65736
GB AAN36529 ETW17315 ETW29792 ETW35145 ETW41309
REF XP_001350849 XP_012764323

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