BMRB Entry 27403

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27403

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Title:
1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of P188A human flap endonuclease-1
Deposition date:
2018-02-15
Original release date:
2018-03-02
Authors:
Bennet, Ian; Baxter, Nicola
Citation:

Citation: Bennet, Ian. "Evidence of dynamics and disorder using NMR-spectroscopic techniques applied to human Flap-Endonuclease-1"  Thesis University of Sheffield .

Assembly members:

Assembly members:
hFEN1-P188A, polymer, 341 residues, 38431.14 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: pET-29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hFEN1-P188A: GIQGLAKLIADVAPSAIREN DIKSYFGRKVAIDASMSIYQ FLIAVRQGGDVLQNEEGETT SHLMGMFYRTIRMMENGIKP VYVFDGKPPQLKSGELAKRS ERRAEAEKQLQQAQAAGAEQ EVEKFTKRLVKVTKQHNDEC KHLLSLMGIPYLDAPSEAEA SCAALVKAGKVYAAATEDMD CLTFGSAVLMRHLTASEAKK LPIQEFHLSRILQELGLNQE QFVDLCILLGSDYCESIRGI GPKRAVDLIQKHKSIEEIVR RLDPNKYPVPENWLHKEAHQ LFLEPEVLDPESVELKWSEP NEEELIKFMCGEKQFSEERI RSGVKRLSKSRQGSTLEVLF Q

Data sets:
Data typeCount
13C chemical shifts780
15N chemical shifts250
1H chemical shifts250

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hFEN1-336-P188A1

Entities:

Entity 1, hFEN1-336-P188A 341 residues - 38431.14 Da.

1   GLYILEGLNGLYLEUALALYSLEUILEALA
2   ASPVALALAPROSERALAILEARGGLUASN
3   ASPILELYSSERTYRPHEGLYARGLYSVAL
4   ALAILEASPALASERMETSERILETYRGLN
5   PHELEUILEALAVALARGGLNGLYGLYASP
6   VALLEUGLNASNGLUGLUGLYGLUTHRTHR
7   SERHISLEUMETGLYMETPHETYRARGTHR
8   ILEARGMETMETGLUASNGLYILELYSPRO
9   VALTYRVALPHEASPGLYLYSPROPROGLN
10   LEULYSSERGLYGLULEUALALYSARGSER
11   GLUARGARGALAGLUALAGLULYSGLNLEU
12   GLNGLNALAGLNALAALAGLYALAGLUGLN
13   GLUVALGLULYSPHETHRLYSARGLEUVAL
14   LYSVALTHRLYSGLNHISASNASPGLUCYS
15   LYSHISLEULEUSERLEUMETGLYILEPRO
16   TYRLEUASPALAPROSERGLUALAGLUALA
17   SERCYSALAALALEUVALLYSALAGLYLYS
18   VALTYRALAALAALATHRGLUASPMETASP
19   CYSLEUTHRPHEGLYSERALAVALLEUMET
20   ARGHISLEUTHRALASERGLUALALYSLYS
21   LEUPROILEGLNGLUPHEHISLEUSERARG
22   ILELEUGLNGLULEUGLYLEUASNGLNGLU
23   GLNPHEVALASPLEUCYSILELEULEUGLY
24   SERASPTYRCYSGLUSERILEARGGLYILE
25   GLYPROLYSARGALAVALASPLEUILEGLN
26   LYSHISLYSSERILEGLUGLUILEVALARG
27   ARGLEUASPPROASNLYSTYRPROVALPRO
28   GLUASNTRPLEUHISLYSGLUALAHISGLN
29   LEUPHELEUGLUPROGLUVALLEUASPPRO
30   GLUSERVALGLULEULYSTRPSERGLUPRO
31   ASNGLUGLUGLULEUILELYSPHEMETCYS
32   GLYGLULYSGLNPHESERGLUGLUARGILE
33   ARGSERGLYVALLYSARGLEUSERLYSSER
34   ARGGLNGLYSERTHRLEUGLUVALLEUPHE
35   GLN

Samples:

sample_1: hFEN1-P188A, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; HEPES 10 mM; potassium chloride 76 mM; EDTA 0.1 mM; sodium azide 4 mM; D2O, [U-99% 2H], 10%; H2O 90%; TSP, [U-99% 2H], 0.05 mM; beta-mercaptoethanol 100 mM

sample_conditions_1: ionic strength: 90 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

Felix, Accelrys Software Inc. - processing

CCPN_Analysis, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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