BMRB Entry 26648

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26648

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
FVO Plasmodium falciparum AMA1
Deposition date:
2015-09-04
Original release date:
2018-06-27
Authors:
Krishnarjuna, Bankala; Lim, San Sui; Devine, Shane; Debono, Cael; Lam, Raymond; Chandrashekaran, Indu; Jaipuria, Garima; Yagi, Hiromasa; MacRaild, Christopher; Atreya, Hanudatta; Anders, Robin; Scanlon, Martin; Scammells, Peter; Norton, Raymond
Citation:

Citation: Krishnarjuna, Bankala; Lim, San Sui; Devine, Shane; Debono, Cael; Lam, Raymond; Chandrashekaran, Indu; Jaipuria, Garima; Yagi, Hiromasa; Atreya, Hanudatta; Scanlon, Martin; MacRaild, Christopher; Scammells, Peter; Norton, Raymond. "Solution NMR characterization of apical membrane antigen 1 and small molecule interactions as a basis for designing new antimalarials"  J. Mol. Recognit. 29, 281-291 (2016).
PubMed: 26804042

Assembly members:

Assembly members:
FVO_PfAMA1, polymer, 335 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: malaria parasite P. falciparum   Taxonomy ID: 5833   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pPROEX HTb

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FVO_PfAMA1: NYMGNPWTEYMAKYDIEEVH GSGIRVDLGEDAEVAGTQYR LPSGKCPVFGKGIIIENSNT TFLKPVATGNQDLKDGGFAF PPTNPLISPMTLNGMRDFYK NNEYVKNLDELTLCSRHAGN MNPDNDKNSNYKYPAVYDYN DKKCHILYIAAFRNNGPRYC NKDQSKRNSMFCFKPAKDKL FENYTYLSKNVVDNWEEVCP RKNLENAKFGLWVDGNCEDI PHVNEFSANNDFLCNKLVFE LSASDQPKQYEQHLTDYEKI KEGFKNKNASMIKSAFLPTG AFKADRYKSHGKGYNWGNYN RETQKCEIFNVKPTCLINNS SYIATTALSHPIEVE

Data sets:
Data typeCount
13C chemical shifts403
15N chemical shifts218
1H chemical shifts218

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hydrophobic cleft1

Entities:

Entity 1, Hydrophobic cleft 335 residues - Formula weight is not available

1   ASNTYRMETGLYASNPROTRPTHRGLUTYR
2   METALALYSTYRASPILEGLUGLUVALHIS
3   GLYSERGLYILEARGVALASPLEUGLYGLU
4   ASPALAGLUVALALAGLYTHRGLNTYRARG
5   LEUPROSERGLYLYSCYSPROVALPHEGLY
6   LYSGLYILEILEILEGLUASNSERASNTHR
7   THRPHELEULYSPROVALALATHRGLYASN
8   GLNASPLEULYSASPGLYGLYPHEALAPHE
9   PROPROTHRASNPROLEUILESERPROMET
10   THRLEUASNGLYMETARGASPPHETYRLYS
11   ASNASNGLUTYRVALLYSASNLEUASPGLU
12   LEUTHRLEUCYSSERARGHISALAGLYASN
13   METASNPROASPASNASPLYSASNSERASN
14   TYRLYSTYRPROALAVALTYRASPTYRASN
15   ASPLYSLYSCYSHISILELEUTYRILEALA
16   ALAPHEARGASNASNGLYPROARGTYRCYS
17   ASNLYSASPGLNSERLYSARGASNSERMET
18   PHECYSPHELYSPROALALYSASPLYSLEU
19   PHEGLUASNTYRTHRTYRLEUSERLYSASN
20   VALVALASPASNTRPGLUGLUVALCYSPRO
21   ARGLYSASNLEUGLUASNALALYSPHEGLY
22   LEUTRPVALASPGLYASNCYSGLUASPILE
23   PROHISVALASNGLUPHESERALAASNASN
24   ASPLEUGLUCYSASNLYSLEUVALPHEGLU
25   LEUSERALASERASPGLNPROLYSGLNTYR
26   GLUGLNHISLEUTHRASPTYRGLULYSILE
27   LYSGLUGLYPHELYSASNLYSASNALASER
28   METILELYSSERALAPHELEUPROTHRGLY
29   ALAPHELYSALAASPARGTYRLYSSERHIS
30   GLYLYSGLYTYRASNTRPGLYASNTYRASN
31   ARGGLUTHRGLNLYSCYSGLUILEPHEASN
32   VALLYSPROTHRCYSLEUILEASNASNSER
33   SERTYRILEALATHRTHRALALEUSERHIS
34   PROILEGLUVALGLU

Samples:

sample_1: FVO PfAMA1, [U-100% 13C; U-100% 15N; U-80% 2H], 250 uM; D2O, [U-2H], 10%; sodium azide 0.01%; sodium phosphate 20 mM; arginine 50 mM; glutamic acid 50 mM; protease inhibitor cocktail 0.2%; H2O 90%

sample_2: FVO PfAMA1, [U-15N]-Lys; [U-80%] 2H, 80 uM; D2O, [U-100% 2H], 10%; sodium phosphate 20 mM; glutamic acid 50 mM; arginine 50 mM; protease inhibitor cocktail 0.2%; sodium azide 0.01%; H2O 90%

sample_conditions_1: ionic strength: 120 mM; pH: 6.8; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks