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 15038

Title: 1H, 13C, and 15N resonance assignments of FK506-binding domain of Plasmodium falciparum FKBP35   PubMed: 19636818

Deposition date: 2006-11-19 Original release date: 2007-06-27

Authors: Kang, Congbao; Ye, Hong; Yoon, Hye Rim; Yoon, Ho Sup

Citation: Kang, Cong Bao; Ye, Hong; Yoon, Hye Rim; Yoon, Ho Sup. "1H, 13C, and 15N resonance assignments of FK506-binding domain of Plasmodium falciparum FKBP35"  Biomol. NMR Assignments 1, 27-28 (2007).

Assembly members:
pfFKBP35FKBD, polymer, 135 residues, 14141 Da.

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

Experimental source:   Production method: purified from the natural source

Entity Sequences (FASTA):
pfFKBP35FKBD: MTTEQEFEKVELTADGGVIK TILKKGDEGEENIPKKGNEV TVHYVGKLESTGKVFDSSFD RNVPFKFHLEQGEVIKGWDI CVSSMRKNEKCLVRIESMYG YGDEGCGESIPGNSVLLFEI ELLSFRELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts514
15N chemical shifts129
1H chemical shifts883

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pfFKBP35FKBD1

Entities:

Entity 1, pfFKBP35FKBD 135 residues - 14141 Da.

1   METTHRTHRGLUGLNGLUPHEGLULYSVAL
2   GLULEUTHRALAASPGLYGLYVALILELYS
3   THRILELEULYSLYSGLYASPGLUGLYGLU
4   GLUASNILEPROLYSLYSGLYASNGLUVAL
5   THRVALHISTYRVALGLYLYSLEUGLUSER
6   THRGLYLYSVALPHEASPSERSERPHEASP
7   ARGASNVALPROPHELYSPHEHISLEUGLU
8   GLNGLYGLUVALILELYSGLYTRPASPILE
9   CYSVALSERSERMETARGLYSASNGLULYS
10   CYSLEUVALARGILEGLUSERMETTYRGLY
11   TYRGLYASPGLUGLYCYSGLYGLUSERILE
12   PROGLYASNSERVALLEULEUPHEGLUILE
13   GLULEULEUSERPHEARGGLULEUGLUHIS
14   HISHISHISHISHIS

Samples:

sample_1: pfFKBP35FKBD, [U-13C; U-15N], 0.5 mM; Na-PO4 20 mM; NaCl 50 mM; DTT 1 mM; EDTA 0.1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
(H)CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

NMRPipe v2.3, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing

NMRView v5.2.2, B Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

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