BMRB Entry 27146

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27146
MolProbity Validation Chart

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Title:
Est3 Hansenula polymorpha telomerase subunit
Deposition date:
2017-06-17
Original release date:
2017-09-29
Authors:
Polshakov, Vladimir; Mariasina, Sofia; Efimov, Sergey; Petrova, Olga
Citation:

Citation: Mariasina, Sofia; Efimov, Sergey; Petrova, Olga; Rodina, Elena; Malyavko, Alexander; Zvereva, Maria; Klochkov, Vladimir; Dontsova, Olga; Polshakov, Vladimir. "Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha"  Biomol. NMR Assignments 12, 57-62 (2018).
PubMed: 28916982

Assembly members:

Assembly members:
Est3, polymer, 178 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: yeast   Taxonomy ID: 870730   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Hansenula polymorpha

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30aTEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Est3: GAMGPPSSRDAVRVTASAHM KHWLEPVLCEAGLGHNYKVD KVLKVLRIYPRSNTLSSLPL CLCDANYKILAFANYKAIAA FERKERRRVTQNLLNSEIMI HSFTIRFYNDDQVQGFFDGL KFKQKASLFPGYLVLEINDF SMFNRDQLILSNAGTIEFLY GTPRYIARFIEQEFSDEE

Data sets:
Data typeCount
13C chemical shifts676
15N chemical shifts183
1H chemical shifts1138

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hpEst31

Entities:

Entity 1, hpEst3 178 residues - Formula weight is not available

1   GLYALAMETGLYPROPROSERSERARGASP
2   ALAVALARGVALTHRALASERALAHISMET
3   LYSHISTRPLEUGLUPROVALLEUCYSGLU
4   ALAGLYLEUGLYHISASNTYRLYSVALASP
5   LYSVALLEULYSVALLEUARGILETYRPRO
6   ARGSERASNTHRLEUSERSERLEUPROLEU
7   CYSLEUCYSASPALAASNTYRLYSILELEU
8   ALAPHEALAASNTYRLYSALAILEALAALA
9   PHEGLUARGLYSGLUARGARGARGVALTHR
10   GLNASNLEULEUASNSERGLUILEMETILE
11   HISSERPHETHRILEARGPHETYRASNASP
12   ASPGLNVALGLNGLYPHEPHEASPGLYLEU
13   LYSPHELYSGLNLYSALASERLEUPHEPRO
14   GLYTYRLEUVALLEUGLUILEASNASPPHE
15   SERMETPHEASNARGASPGLNLEUILELEU
16   SERASNALAGLYTHRILEGLUPHELEUTYR
17   GLYTHRPROARGTYRILEALAARGPHEILE
18   GLUGLNGLUPHESERASPGLUGLU

Samples:

sample_CN: Est3, [U-99% 13C; U-99% 15N], 0.5 mM; potassium chloride 100 mM; sodium phosphate 50 mM; DTT 3 mM; sodium azide 0.02%

sample_CN_D2O: Est3, [U-99% 13C; U-99% 15N], 0.7 mM; potassium chloride 100 mM; sodium phosphate 50 mM; DTT 3 mM; sodium azide 0.02%

Sample_N: Est3, [U-99% 15N], 0.8 mM; potassium chloride 100 mM; sodium phosphate 50 mM; DTT 3 mM; sodium azide 0.02%

sample_unl: Est3 1.0 mM; potassium chloride 100 mM; sodium phosphate 50 mM; DTT 3 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSample_Nisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_CN_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_CN_D2Oisotropicsample_conditions_1
2D DQF-COSYsample_unlisotropicsample_conditions_2
2D 1H-1H NOESYsample_unlisotropicsample_conditions_2
3D HNCOsample_CNisotropicsample_conditions_1
3D HN(CA)COsample_CNisotropicsample_conditions_1
3D HNCAsample_CNisotropicsample_conditions_1
3D HN(CO)CAsample_CNisotropicsample_conditions_1
3D HNCACBsample_CNisotropicsample_conditions_1
3D CBCA(CO)NHsample_CNisotropicsample_conditions_1
3D HNHASample_Nisotropicsample_conditions_1
3D HNHBSample_Nisotropicsample_conditions_1
3D HCCH-TOCSYsample_CN_D2Oisotropicsample_conditions_1
3D 1H-13C NOESYsample_CN_D2Oisotropicsample_conditions_1
2D HBCB(CGCD)HDsample_CN_D2Oisotropicsample_conditions_1
2D HBCB(CGCDCE)HEsample_CN_D2Oisotropicsample_conditions_1
3D 1H-15N TOCSYSample_Nisotropicsample_conditions_1
3D 1H-15N NOESYSample_Nisotropicsample_conditions_1
2D 1H-15N HSQCSample_Nisotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection

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

SPARKY, Goddard - data analysis, peak picking

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMRest, Polshakov - chemical shift calculation, data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • 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