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 18504

Title: pfsub2 solution NMR structure   PubMed: 23011838

Deposition date: 2012-06-06 Original release date: 2012-10-01

Authors: HE, Yanan; CHEN, Yihong; RUAN, Biao; O'BROCHTA, David; BRYAN, Philip; ORBAN, John

Citation: He, Yanan; Chen, Yihong; Oganesyan, Natalia; Ruan, Biao; Bryan, David; Orban, Philip. "Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum."  Proteins 80, 2810-2817 (2012).

Assembly members:
pfsub2, polymer, 149 residues, 10570.397 Da.

Natural source:   Common Name: Malaria parasite P. falciparum   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):
pfsub2: TSNKKILLNVDKLVDQYLLN LKNNHTSKQELILVLKGELD LHSKNMKNVINNAKKNLEKY FKEHFKEFDKISYDISTPIN FLCIFIPTLFDMNNMDLLKQ ALLILHNDLHEYVENWSFSS TYHTYEADYIKEQDSVYDRS PKKKYIKAS

Data sets:
Data typeCount
13C chemical shifts471
15N chemical shifts118
1H chemical shifts562

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pfsub21

Entities:

Entity 1, pfsub2 149 residues - 10570.397 Da.

1   THRSERASNLYSLYSILELEULEUASNVAL
2   ASPLYSLEUVALASPGLNTYRLEULEUASN
3   LEULYSASNASNHISTHRSERLYSGLNGLU
4   LEUILELEUVALLEULYSGLYGLULEUASP
5   LEUHISSERLYSASNMETLYSASNVALILE
6   ASNASNALALYSLYSASNLEUGLULYSTYR
7   PHELYSGLUHISPHELYSGLUPHEASPLYS
8   ILESERTYRASPILESERTHRPROILEASN
9   PHELEUCYSILEPHEILEPROTHRLEUPHE
10   ASPMETASNASNMETASPLEULEULYSGLN
11   ALALEULEUILELEUHISASNASPLEUHIS
12   GLUTYRVALGLUASNTRPSERPHESERSER
13   THRTYRHISTHRTYRGLUALAASPTYRILE
14   LYSGLUGLNASPSERVALTYRASPARGSER
15   PROLYSLYSLYSTYRILELYSALASER

Samples:

sample_1: pfsub2, [U-13C; U-15N], 0.3 – 0.4 mM; potassium phosphate 100 mM; sodium azide 10 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CNS v1.21, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAB37326 CAB43592 CDO65172
GB AAN35964 AAY33847 ETW15317 ETW30319 ETW35903
REF XP_001348051 XP_012763770

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