BMRB Entry 16516

Title:
Backbone and 13Cb chemical shifts for human AP endonuclease 1 (APE1) residues 39-318
Deposition date:
2009-09-23
Original release date:
2009-11-20
Authors:
Manvilla, Brittney; Drohat, Alex
Citation:

Citation: Manvilla, Brittney; Varney, Kristen; Drohat, Alexander. "Chemical shift assignments for human apurinic/apyrimidinic endonuclease 1."  Biomol. NMR Assignments 4, 5-8 (2010).
PubMed: 19888678

Assembly members:

Assembly members:
APE1, polymer, 286 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: pET28a

Data sets:
Data typeCount
13C chemical shifts766
15N chemical shifts237
1H chemical shifts237

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1APE11

Entities:

Entity 1, APE1 286 residues - Formula weight is not available

The protein is comprised of six non-native N-terminal residues (GSHMAS)resulting from thrombin cleavage of a poly-His tag, followed by residues 39-318 of human APE1. Full length APE1 contains 318 residues.

1   GLYSERHISMETALASERGLYGLUGLYPRO
2   ALALEUTYRGLUASPPROPROASPGLNLYS
3   THRSERPROSERGLYLYSPROALATHRLEU
4   LYSILECYSSERTRPASNVALASPGLYLEU
5   ARGALATRPILELYSLYSLYSGLYLEUASP
6   TRPVALLYSGLUGLUALAPROASPILELEU
7   CYSLEUGLNGLUTHRLYSCYSSERGLUASN
8   LYSLEUPROALAGLULEUGLNGLULEUPRO
9   GLYLEUSERHISGLNTYRTRPSERALAPRO
10   SERASPLYSGLUGLYTYRSERGLYVALGLY
11   LEULEUSERARGGLNCYSPROLEULYSVAL
12   SERTYRGLYILEGLYASPGLUGLUHISASP
13   GLNGLUGLYARGVALILEVALALAGLUPHE
14   ASPSERPHEVALLEUVALTHRALATYRVAL
15   PROASNALAGLYARGGLYLEUVALARGLEU
16   GLUTYRARGGLNARGTRPASPGLUALAPHE
17   ARGLYSPHELEULYSGLYLEUALASERARG
18   LYSPROLEUVALLEUCYSGLYASPLEUASN
19   VALALAHISGLUGLUILEASPLEUARGASN
20   PROLYSGLYASNLYSLYSASNALAGLYPHE
21   THRPROGLNGLUARGGLNGLYPHEGLYGLU
22   LEULEUGLNALAVALPROLEUALAASPSER
23   PHEARGHISLEUTYRPROASNTHRPROTYR
24   ALATYRTHRPHETRPTHRTYRMETMETASN
25   ALAARGSERLYSASNVALGLYTRPARGLEU
26   ASPTYRPHELEULEUSERHISSERLEULEU
27   PROALALEUCYSASPSERLYSILEARGSER
28   LYSALALEUGLYSERASPHISCYSPROILE
29   THRLEUTYRLEUALALEU

Samples:

2H_13C_15N-APE1_delta_N38: APE1, [U-13C; U-15N; U-2H], 0.8 mM; D2O, [U-99% 2H], 10%; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY2H_13C_15N-APE1_delta_N38isotropicsample_conditions_1
3D TROSY HNCO2H_13C_15N-APE1_delta_N38isotropicsample_conditions_1
3D TROSY HNCACO2H_13C_15N-APE1_delta_N38isotropicsample_conditions_1
3D TROSY HNCA2H_13C_15N-APE1_delta_N38isotropicsample_conditions_1
3D TROSY HNCOCA2H_13C_15N-APE1_delta_N38isotropicsample_conditions_1
3D TROSY HNCACB2H_13C_15N-APE1_delta_N38isotropicsample_conditions_1
3D TROSY HNCOCACB2H_13C_15N-APE1_delta_N38isotropicsample_conditions_1
3D 1H-15N NOESY2H_13C_15N-APE1_delta_N38isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

SWS P27695
PDB
DBJ BAA02633 BAA07270 BAA14381 BAA14382 BAB28774
EMBL CAA42437 CAA46925 CAD61917
GB AAA58371 AAA58372 AAA58629 AAB22977 AAB26054
PRF 2019234A
REF NP_001074954 NP_001138591 NP_001231178 NP_001245038 NP_001277543
SP A1YES6 A1YFZ3 A2T6Y4 A2T7I6 P27695
AlphaFold A1YES6 A2T6Y4 A2T7I6 P27695 A1YFZ3

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