BMRB Entry 19551

Title:
1H, 13C, and 15N Chemical Shift Assignments for human FK506 binding Protein 25
Deposition date:
2013-10-12
Original release date:
2014-02-12
Authors:
Shin, Joon; Prakash, Ajit; Yoon, Ho Sup
Citation:

Citation: Prakash, Ajit; Shin, Joon; Yoon, Ho Sup. "(1)H, (13)C and (15)N resonance assignments of human FK506 binding protein 25."  Biomol. NMR Assignments ., .-. (2014).
PubMed: 24414276

Assembly members:

Assembly members:
hFKBP25, polymer, 224 residues, Formula weight is not available

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: pSUMO

Data sets:
Data typeCount
13C chemical shifts945
15N chemical shifts229
1H chemical shifts1630

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hFKBP251

Entities:

Entity 1, hFKBP25 224 residues - Formula weight is not available

1   METALAALAALAVALPROGLNARGALATRP
2   THRVALGLUGLNLEUARGSERGLUGLNLEU
3   PROLYSLYSASPILEILELYSPHELEUGLN
4   GLUHISGLYSERASPSERPHELEUALAGLU
5   HISLYSLEULEUGLYASNILELYSASNVAL
6   ALALYSTHRALAASNLYSASPHISLEUVAL
7   THRALATYRASNHISLEUPHEGLUTHRLYS
8   ARGPHELYSGLYTHRGLUSERILESERLYS
9   VALSERGLUGLNVALLYSASNVALLYSLEU
10   ASNGLUASPLYSPROLYSGLUTHRLYSSER
11   GLUGLUTHRLEUASPGLUGLYPROPROLYS
12   TYRTHRLYSSERVALLEULYSLYSGLYASP
13   LYSTHRASNPHEPROLYSLYSGLYASPVAL
14   VALHISCYSTRPTYRTHRGLYTHRLEUGLN
15   ASPGLYTHRVALPHEASPTHRASNILEGLN
16   THRSERALALYSLYSLYSLYSASNALALYS
17   PROLEUSERPHELYSVALGLYVALGLYLYS
18   VALILEARGGLYTRPASPGLUALALEULEU
19   THRMETSERLYSGLYGLULYSALAARGLEU
20   GLUILEGLUPROGLUTRPALATYRGLYLYS
21   LYSGLYGLNPROASPALALYSILEPROPRO
22   ASNALALYSLEUTHRPHEGLUVALGLULEU
23   VALASPILEASP

Samples:

sample_1: human FK506 binding protein 25 (hFKBP25), [U-13C; U-15N], 0.5 mM; D2O, [U-100% 2H], 10%; H2O 90%; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 0.001%

sample_2: human FK506 binding protein 25 (hFKBP25), [U-15N], 0.5 mM; D2O, [U-100% 2H], 10%; H2O 90%; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 0.001%

sample_3: human FK506 binding protein 25 (hFKBP25), [U-13C], 0.5 mM; D2O, [U-100% 2H], 100%; sodium chloride 50 mM; sodium phosphate 20 mM; sodium phosphate 0.001%

sample_conditions_1: ionic strength: 70 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAD96713 BAE01700 BAE87176 BAG34856 BAI46571
GB AAA30348 AAA58471 AAA58475 AAH16288 AAH20809
REF NP_001033201 NP_001270679 NP_002004 XP_001096116 XP_002753901
SP P26884 Q00688
TPG DAA17319
AlphaFold P26884 Q00688

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