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 27070

Title: human FKBP25   PubMed: 29036638

Deposition date: 2017-04-12 Original release date: 2017-11-10

Authors: Upadhyay, Santosh; Mackereth, Cameron

Citation: Dilworth, David; Upadhyay, Santosh; Bonnafous, Pierre; Edoo, Amiirah Bibi; Bourbigot, Sarah; Pesek-Jardim, Francy; Gudavicius, Geoff; Serpa, Jason; Petrotchenko, Evgeniy; Borchers, Christoph; Nelson, Christopher; Mackereth, Cameron. "The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module."  Nucleic Acids Res. 45, 11989-12004 (2017).

Assembly members:
FKBP25, polymer, 226 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
FKBP25: GAMAAAVPQRAWTVEQLRSE QLPKKDIIKFLQEHGSDSFL AEHKLLGNIKNVAKTANKDH LVTAYNHLFETKRFKGTESI SKVSEQVKNVKLNEDKPKET KSEETLDEGPPKYTKSVLKK GDKTNFPKKGDVVHCWYTGT LQDGTVFDTNIQTSAKKKKN AKPLSFKVGVGKVIRGWDEA LLTMSKGEKARLEIEPEWAY GKKGQPDAKIPPNAKLTFEV ELVDID

Data sets:
Data typeCount
13C chemical shifts632
15N chemical shifts207
1H chemical shifts207

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FKBP251

Entities:

Entity 1, FKBP25 226 residues - Formula weight is not available

1   GLYALAMETALAALAALAVALPROGLNARG
2   ALATRPTHRVALGLUGLNLEUARGSERGLU
3   GLNLEUPROLYSLYSASPILEILELYSPHE
4   LEUGLNGLUHISGLYSERASPSERPHELEU
5   ALAGLUHISLYSLEULEUGLYASNILELYS
6   ASNVALALALYSTHRALAASNLYSASPHIS
7   LEUVALTHRALATYRASNHISLEUPHEGLU
8   THRLYSARGPHELYSGLYTHRGLUSERILE
9   SERLYSVALSERGLUGLNVALLYSASNVAL
10   LYSLEUASNGLUASPLYSPROLYSGLUTHR
11   LYSSERGLUGLUTHRLEUASPGLUGLYPRO
12   PROLYSTYRTHRLYSSERVALLEULYSLYS
13   GLYASPLYSTHRASNPHEPROLYSLYSGLY
14   ASPVALVALHISCYSTRPTYRTHRGLYTHR
15   LEUGLNASPGLYTHRVALPHEASPTHRASN
16   ILEGLNTHRSERALALYSLYSLYSLYSASN
17   ALALYSPROLEUSERPHELYSVALGLYVAL
18   GLYLYSVALILEARGGLYTRPASPGLUALA
19   LEULEUTHRMETSERLYSGLYGLULYSALA
20   ARGLEUGLUILEGLUPROGLUTRPALATYR
21   GLYLYSLYSGLYGLNPROASPALALYSILE
22   PROPROASNALALYSLEUTHRPHEGLUVAL
23   GLULEUVALASPILEASP

Samples:

sample_1: FKBP25, [U-99% 13C; U-99% 15N], 200 uM; sodium phosphate 20 mM; sodium chloride 150 mM; D2O, [U-99% 2H], 10 % v/v

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

UNP Q00688

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