BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17616

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17616

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Title: Backbone Resonance assignment of 1H, 13C, 15N for P2 of plasmodium falciparum in 9M urea.   PubMed: 22567147

Deposition date: 2011-05-02 Original release date: 2012-05-09

Authors: Mishra, Pushpa

Citation: Mishra, Pushpa; Das, Sudipta; Panicker, Lata; Hosur, Madhusoodan; Sharma, Shobhona; Hosur, Ramakrishna. "NMR Insights into Folding and Self-Association of Plasmodium falciparum P2."  PLoS ONE 7, .-. (2012).

Assembly members:
plasmodium_falciparum_p2, polymer, 142 residues, 15664.3 Da.

Natural source:   Common Name: Malaria Parasite   Taxonomy ID: 5833   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium Falciparum

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

Entity Sequences (FASTA):
plasmodium_falciparum_p2: MSYYHHHHHHDYDIPTTENL YFQGAMDPEFMAMKYVAAYL MCVLGGNENPSTKEVKNVLG AVNADVEDEVLNNFIDSLKG KSCHELITDGLKKLQNIGGG VAAAPAGAAAVETAEAKKED KKEEKKEEEEEEEDDLGFSL FG

Data sets:
Data typeCount
13C chemical shifts342
15N chemical shifts124
1H chemical shifts546

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P21

Entities:

Entity 1, P2 142 residues - 15664.3 Da.

Residues 1-30 represent sequence coming from vector. 31 onwards P2 protein sequence starts.

1   METSERTYRTYRHISHISHISHISHISHIS
2   ASPTYRASPILEPROTHRTHRGLUASNLEU
3   TYRPHEGLNGLYALAMETASPPROGLUPHE
4   METALAMETLYSTYRVALALAALATYRLEU
5   METCYSVALLEUGLYGLYASNGLUASNPRO
6   SERTHRLYSGLUVALLYSASNVALLEUGLY
7   ALAVALASNALAASPVALGLUASPGLUVAL
8   LEUASNASNPHEILEASPSERLEULYSGLY
9   LYSSERCYSHISGLULEUILETHRASPGLY
10   LEULYSLYSLEUGLNASNILEGLYGLYGLY
11   VALALAALAALAPROALAGLYALAALAALA
12   VALGLUTHRALAGLUALALYSLYSGLUASP
13   LYSLYSGLUGLULYSLYSGLUGLUGLUGLU
14   GLUGLUGLUASPASPLEUGLYPHESERLEU
15   PHEGLY

Samples:

sample_1: plasmodium falciparum p2, [U-99% 15N], 1 mM; H2O 90%; D2O 10%; Urea 9 M; MES Buffer 0.1 M; NaCl 150 mM; DTT 5 mM

sample_2: plasmodium falciparum p2, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; Urea 9 M; MES Buffer 0.1 M; NaCl 150 mM; DTT 5 mM

sample_conditions_1: pH: 5.6; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNNsample_2isotropicsample_conditions_1
3D HN(C)Nsample_2isotropicsample_conditions_1
3D HNCANsample_2isotropicsample_conditions_1
3D HSQC-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - collection

CARA v1.9.1, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

EMBL CAB11115 CDO62522
GB AAB51131 AAF15361 ETW20710 ETW38756 ETW45178
REF XP_001351169 XP_012761169
SP O00806

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