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 19788

Title: Human FKBP52-FK506 binding domain 1   PubMed: 24749623

Deposition date: 2014-02-11 Original release date: 2014-08-06

Authors: Mustafi, Sourajit; LeMaster, David; Hernandez, Griselda

Citation: Mustafi, Sourajit; LeMaster, David; Hernandez, Griselda. "Differential Conformational Dynamics in the Closely Homologous FK506-binding Domains of FKBP51 and FKBP52"  Biochem J. 461, 115-123 (2014).

Assembly members:
FKBP52, polymer, 121 residues, 13387.38 Da.

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):
FKBP52: MEGVDISPKQDEGVLKVIKR EGTGTEMPMIGDRVFVHYTG WLLDGTKFDSSLDRKDKFSF DLGKGEVIKAWDIAIATMKV GEVCHITCKPEYAYGSAGSP PKIPPNATLVFEVELFEFKG E

Data sets:
Data typeCount
13C chemical shifts341
15N chemical shifts111
1H chemical shifts111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FKBP521

Entities:

Entity 1, FKBP52 121 residues - 13387.38 Da.

1   METGLUGLYVALASPILESERPROLYSGLN
2   ASPGLUGLYVALLEULYSVALILELYSARG
3   GLUGLYTHRGLYTHRGLUMETPROMETILE
4   GLYASPARGVALPHEVALHISTYRTHRGLY
5   TRPLEULEUASPGLYTHRLYSPHEASPSER
6   SERLEUASPARGLYSASPLYSPHESERPHE
7   ASPLEUGLYLYSGLYGLUVALILELYSALA
8   TRPASPILEALAILEALATHRMETLYSVAL
9   GLYGLUVALCYSHISILETHRCYSLYSPRO
10   GLUTYRALATYRGLYSERALAGLYSERPRO
11   PROLYSILEPROPROASNALATHRLEUVAL
12   PHEGLUVALGLULEUPHEGLUPHELYSGLY
13   GLU

Samples:

sample_1: FKBP52, [U-99% 13C; U-99% 15N], 1.0 mM; sodium phosphate 25 mM; DTT 2 mM; TCEP 2 mM; H2O 93%; D2O 7%

sample_2: FKBP52, [U-98% 15N], 1.0 mM; sodium phosphate 25 mM; DTT 2 mM; TCEP 2 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 25 mM; pH: 6.50; pressure: 1 atm; temperature: 298.15 K

sample_condition_2: ionic strength: 25 mM; pH: 6.50; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_condition_2
2D 1H-15N HSQCsample_2isotropicsample_condition_2
2D 1H-15N HSQCsample_2isotropicsample_condition_2
2D 1H-15N HSQCsample_2isotropicsample_condition_2
2D 1H-15N HSQCsample_2isotropicsample_condition_2
2D 1H-15N HSQCsample_2isotropicsample_condition_2

Software:

Felix v2007, Accelrys Software Inc. - chemical shift assignment, peak picking, processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAA34914
PIR S14538

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