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 16260

Title: NMR assignments of FK506 binding domain from Plasmodium vivax   PubMed: 19774494

Deposition date: 2009-04-19 Original release date: 2009-10-16

Authors: Alag, Reema; Yoon, Ho Sup; Shin, Joon

Citation: Alag, Reema; Shin, Joon; Yoon, Ho Sup. "NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax"  Biomol. NMR Assignments 3, 243-245 (2009).

Assembly members:
PvFKBD, polymer, 126 residues, 13971.799 Da.

Natural source:   Common Name: malaria parasite   Taxonomy ID: not available   Superkingdom: Eukaryota   Kingdom: Alveolata   Genus/species: Plasmodium vivax

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

Entity Sequences (FASTA):
PvFKBD: MEQETLEQVHLTEDGGVVKT ILRKGEGGEENAPKKGNEVT VHYVGKLESSGKVFDSSRER NVPFKFHLGQGEVIKGWDIC VASMTKNEKCSVRLDSKYGY GEEGCGESIPGNSVLIFEIE LISFRE

Data sets:
Data typeCount
13C chemical shifts497
15N chemical shifts127
1H chemical shifts850

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Domain1

Entities:

Entity 1, Domain 126 residues - 13971.799 Da.

1   METGLUGLNGLUTHRLEUGLUGLNVALHIS
2   LEUTHRGLUASPGLYGLYVALVALLYSTHR
3   ILELEUARGLYSGLYGLUGLYGLYGLUGLU
4   ASNALAPROLYSLYSGLYASNGLUVALTHR
5   VALHISTYRVALGLYLYSLEUGLUSERSER
6   GLYLYSVALPHEASPSERSERARGGLUARG
7   ASNVALPROPHELYSPHEHISLEUGLYGLN
8   GLYGLUVALILELYSGLYTRPASPILECYS
9   VALALASERMETTHRLYSASNGLULYSCYS
10   SERVALARGLEUASPSERLYSTYRGLYTYR
11   GLYGLUGLUGLYCYSGLYGLUSERILEPRO
12   GLYASNSERVALLEUILEPHEGLUILEGLU
13   LEUILESERPHEARGGLU

Samples:

sample_1: PvFKBD, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%; H2O 90%; D2O 10%

sample_2: PvFKBD, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%; D2O 100%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
GB EDL44272 KMZ77558 KMZ84718 KMZ89996 KMZ96554
REF XP_001613999

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