BMRB Entry 19324

Title:
Human FKBP12.6-Minor Form
Deposition date:
2013-06-26
Original release date:
2014-02-13
Authors:
Mustafi, Sourajit; Chen, Hui; Li, Hongmin; LeMaster, David; Hernandez, Griselda; Li, Zhong; Heroux, Annie
Citation:

Citation: Mustafi, Sourajit; Chen, Hui; Li, Hongmin; Lemaster, David; Hernandez, Griselda. "Analysing the visible conformational substates of the FK506-binding protein FKBP12."  Biochem. J. 453, 371-380 (2013).
PubMed: 23688288

Assembly members:

Assembly members:
FKBP12.6, polymer, 107 residues, 11657.3 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 shifts307
15N chemical shifts98
1H chemical shifts217

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FKBP12.61

Entities:

Entity 1, FKBP12.6 107 residues - 11657.3 Da.

1   GLYVALGLUILEGLUTHRILESERPROGLY
2   ASPGLYARGTHRPHEPROLYSLYSGLYGLN
3   THRCYSVALVALHISTYRTHRGLYMETLEU
4   GLNASNGLYLYSLYSPHEASPSERSERARG
5   ASPARGASNLYSPROPHELYSPHEARGILE
6   GLYLYSGLNGLUVALILELYSGLYPHEGLU
7   GLUGLYALAALAGLNMETSERLEUGLYGLN
8   ARGALALYSLEUTHRCYSTHRPROASPVAL
9   ALATYRGLYALATHRGLYHISPROGLYVAL
10   ILEPROPROASNALATHRLEUILEPHEASP
11   VALGLULEULEUASNLEUGLU

Samples:

sample_1: FKBP12.6, [U-99% 13C; U-99% 15N], 1.5 mM; sodium phosphate 25 mM; DTT 2 mM; TCEP 2 mM; H2O 93%; D2O 7%

sample_2: FKBP12.6, [U-98% 15N], 1.5 mM; sodium phosphate 25 mM; DTT 2 mM; TCEP 2 mM; H2O, [U-98% 15N], 93%; D2O, [U-98% 15N], 7%

sample_conditions_1: ionic strength: 25 mM; pH: 7.00; pressure: 1 atm; temperature: 298.15 K

sample_condition_2: ionic strength: 25 mM; pH: 7.00; 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
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_condition_2
2D DQF-COSYsample_2isotropicsample_condition_2

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16931 19240 19241 19323 19323
PDB
DBJ BAA07232 BAA13154 BAB23879 BAE44300 BAF93934
EMBL CAH92123
GB AAB30684 AAB30685 AAC37581 AAC64923 AAH02614
PRF 2201446A
REF NP_001075614 NP_001091627 NP_001126241 NP_001253652 NP_004107
SP P68106 P68107 P97534 Q8HYX6 Q9Z2I2
TPG DAA24446
AlphaFold P97534 P68106 P68107 Q8HYX6 Q9Z2I2

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