BMRB Entry 19787

Title:
Human FKBP51-FK506 binding domain 1
Deposition date:
2014-02-11
Original release date:
2014-08-06
Authors:
Mustafi, Sourajit; LeMaster, David; Hernandez, Griselda
Citation:

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).
PubMed: 24749623

Assembly members:

Assembly members:
FKBP51, polymer, 122 residues, 13537.59 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11a

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts114
1H chemical shifts250

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FKBP511

Entities:

Entity 1, FKBP51 122 residues - 13537.59 Da.

1   METGLUGLNGLYGLUASPILETHRSERLYS
2   LYSASPARGGLYVALLEULYSILEVALLYS
3   ARGVALGLYASNGLYGLUGLUTHRPROMET
4   ILEGLYASPLYSVALTYRVALHISTYRLYS
5   GLYLYSLEUSERASNGLYLYSLYSPHEASP
6   SERSERHISASPARGASNGLUPROPHEVAL
7   PHESERLEUGLYLYSGLYGLNVALILELYS
8   ALATRPASPILEGLYVALALATHRMETLYS
9   LYSGLYGLUILECYSHISLEULEUCYSLYS
10   PROGLUTYRALATYRGLYSERALAGLYSER
11   LEUPROLYSILEPROSERASNALATHRLEU
12   PHEPHEGLUILEGLULEULEUASPPHELYS
13   GLYGLU

Samples:

sample_1: FKBP51, [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: FKBP51, [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 HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_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

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAD93130
GB AAI18470
REF NP_001139249 XP_003897552 XP_012387759 XP_013833287 XP_013833288

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks