BMRB Entry 19241

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19241

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Title:
Human FKBP12-Minor Form
Deposition date:
2013-05-14
Original release date:
2013-07-15
Authors:
Mustafi, Sourajit; Chen, Hui; Li, Hongmin; LeMaster, David; Hernandez, Griselda
Citation:

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

Assembly members:

Assembly members:
FKBP12, polymer, 107 residues, 11819.5 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FKBP12: GVQVETISPGDGRTFPKRGQ TCVVHYTGMLEDGKKFDSSR DRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDY AYGATGHPGIIPPHATLVFD VELLKLE

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts105
1H chemical shifts736

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FKBP121

Entities:

Entity 1, FKBP12 107 residues - 11819.5 Da.

1   GLYVALGLNVALGLUTHRILESERPROGLY
2   ASPGLYARGTHRPHEPROLYSARGGLYGLN
3   THRCYSVALVALHISTYRTHRGLYMETLEU
4   GLUASPGLYLYSLYSPHEASPSERSERARG
5   ASPARGASNLYSPROPHELYSPHEMETLEU
6   GLYLYSGLNGLUVALILEARGGLYTRPGLU
7   GLUGLYVALALAGLNMETSERVALGLYGLN
8   ARGALALYSLEUTHRILESERPROASPTYR
9   ALATYRGLYALATHRGLYHISPROGLYILE
10   ILEPROPROHISALATHRLEUVALPHEASP
11   VALGLULEULEULYSLEUGLU

Samples:

sample_1: FKBP12, [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, [U-98% 15N], 1.5 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
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 900 MHz

Related Database Links:

BMRB 16931 11471 16925 16931 16933 19240
PDB
DBJ BAB22351 BAB27125 BAB31680 BAE32804 BAE40271
EMBL CAA36462 CAA39272 CAA42762 CAG28541 CAG46965
GB AAA19163 AAA31252 AAA35844 AAA58472 AAA58476
PRF 1613455A
REF NP_000792 NP_001030533 NP_001033089 NP_001164597 NP_001239119
SP P18203 P26883 P62942 P62943 Q62658
TPG DAA23300
AlphaFold P18203 P26883 P62942 P62943 Q62658

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