BMRB Entry 26309

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26309

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Title:
Backbone 1H, 15N, and 13C resonance assignments of the Phafin2 PH domain
Deposition date:
2021-08-03
Original release date:
2022-05-12
Authors:
Ellena, Jeffrey; Tang, Tuo-Xian; Shanaiah, Narasimhamurthy; Capelluto, Daniel
Citation:

Citation: Ellena, Jeffrey; Tang, Tuo-Xian; Shanaiah, Narasimhamurthy; Capelluto, Daniel. "Backbone 1 H, 15 N, and 13 C resonance assignments of the Phafin2 pleckstrin homology domain"  Biomol. NMR Assign. 16, 27-30 (2022).

Assembly members:

Assembly members:
Human Phafin2 pleckstrin homology domain, polymer, 140 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: pGEX6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human Phafin2 pleckstrin homology domain: GPLGSMVDRLANSEANTRRI SIVENCFGAAGQPLTIPGRV LIGEGVLTKLCRKKPKARQF FLFNDILVYGNIVIQKKKYN KQHIIPLENVTIDSIKDEGD LRNGWLIKTPTKSFAVYAAT ATEKSEWMNHINKCVTDLLS

Data sets:
Data typeCount
13C chemical shifts407
15N chemical shifts132
1H chemical shifts132

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Phafin2 PH domain1

Entities:

Entity 1, Phafin2 PH domain 140 residues - Formula weight is not available

The first five residues of the sequence (GPLGS) are non-native amino acids that remained from HRV-3C protease cleavage of the GST tag. The remaining sequence belongs to the Phafin2 PH domain (residues 1-135).

1   GLYPROLEUGLYSERMETVALASPARGLEU
2   ALAASNSERGLUALAASNTHRARGARGILE
3   SERILEVALGLUASNCYSPHEGLYALAALA
4   GLYGLNPROLEUTHRILEPROGLYARGVAL
5   LEUILEGLYGLUGLYVALLEUTHRLYSLEU
6   CYSARGLYSLYSPROLYSALAARGGLNPHE
7   PHELEUPHEASNASPILELEUVALTYRGLY
8   ASNILEVALILEGLNLYSLYSLYSTYRASN
9   LYSGLNHISILEILEPROLEUGLUASNVAL
10   THRILEASPSERILELYSASPGLUGLYASP
11   LEUARGASNGLYTRPLEUILELYSTHRPRO
12   THRLYSSERPHEALAVALTYRALAALATHR
13   ALATHRGLULYSSERGLUTRPMETASNHIS
14   ILEASNLYSCYSVALTHRASPLEULEUSER

Samples:

sample_1: Human Phafin2 pleckstrin homology domain, [U-100% 13C; U-100% 15N], 300 uM; d4-citrate, [U-98% 2H], 5 mM; NaCl 100 mM; DTT, [U-2H], 5 mM; sodium acetate, [U-2H], 5 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D NHSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2.7 - collection

NMRPipe v10.9_rev2021.005.11.52 - data visualization, processing

SMILE v10.9_rev2021.005.11.52 - reconstruction of non-uniformly sampled data

NMRFAM-SPARKY vBuild_01-26-2021 - visualization and analysis of data

NMRbox v7/1/21 - provided all software used and server for software execution

NMR spectrometers:

  • Bruker AVANCE III 800 MHz MHz

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