BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18307

Title: Human APOBEC2 chemical shifts   PubMed: 22339232

Deposition date: 2012-03-01 Original release date: 2012-03-28

Authors: Krzysiak, Troy; Jung, Jinwon; Thompson, James; Baker, David; Gronenborn, Angela

Citation: Krzysiak, Troy; Jung, Jinwon; Thompson, James; Baker, David; Gronenborn, Angela. "APOBEC2 is a Monomer in Solution: Implications for APOBEC3G Models"  Biochemistry 51, 2008-2017 (2012).

Assembly members:
APOBEC2_1-224, polymer, 227 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET41a modified

Entity Sequences (FASTA):
APOBEC2_1-224: SEFMAQKEEAAVATEAASQN GEDLENLDDPEKLKELIELP PFEIVTGERLPANFFKFQFR NVEYSSGRNKTFLCYVVEAQ GKGGQVQASRGYLEDEHAAA HAEEAFFNTILPAFDPALRY NVTWYVSSSPCAACADRIIK TLSKTKNLRLLILVGRLFMW EEPEIQAALKKLKEAGCKLR IMKPQDFEYVWQNFVEQEEG ESKAFQPWEDIQENFLYYEE KLADILK

Data sets:
Data typeCount
13C chemical shifts387
15N chemical shifts198
1H chemical shifts198

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1A2POBEC2 1-2241

Entities:

Entity 1, A2POBEC2 1-224 227 residues - Formula weight is not available

Start SEF are cloning artifacts

1   SERGLUPHEMETALAGLNLYSGLUGLUALA
2   ALAVALALATHRGLUALAALASERGLNASN
3   GLYGLUASPLEUGLUASNLEUASPASPPRO
4   GLULYSLEULYSGLULEUILEGLULEUPRO
5   PROPHEGLUILEVALTHRGLYGLUARGLEU
6   PROALAASNPHEPHELYSPHEGLNPHEARG
7   ASNVALGLUTYRSERSERGLYARGASNLYS
8   THRPHELEUCYSTYRVALVALGLUALAGLN
9   GLYLYSGLYGLYGLNVALGLNALASERARG
10   GLYTYRLEUGLUASPGLUHISALAALAALA
11   HISALAGLUGLUALAPHEPHEASNTHRILE
12   LEUPROALAPHEASPPROALALEUARGTYR
13   ASNVALTHRTRPTYRVALSERSERSERPRO
14   CYSALAALACYSALAASPARGILEILELYS
15   THRLEUSERLYSTHRLYSASNLEUARGLEU
16   LEUILELEUVALGLYARGLEUPHEMETTRP
17   GLUGLUPROGLUILEGLNALAALALEULYS
18   LYSLEULYSGLUALAGLYCYSLYSLEUARG
19   ILEMETLYSPROGLNASPPHEGLUTYRVAL
20   TRPGLNASNPHEVALGLUGLNGLUGLUGLY
21   GLUSERLYSALAPHEGLNPROTRPGLUASP
22   ILEGLNGLUASNPHELEUTYRTYRGLUGLU
23   LYSLEUALAASPILELEULYS

Samples:

sample_1: HEPES 20 mM; sodium chloride 50 mM; DTT 5 mM; APOBEC2 1-224, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 18306
PDB
DBJ BAD97181 BAG36096
EMBL CAH90732
GB AAD45360 AAH47767 AAH69688 AAH69764 AAT44388
REF NP_001125408 NP_006780 XP_001117195 XP_003266357 XP_003897628
SP Q694B4 Q9Y235

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts