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Biological Magnetic Resonance Data Bank


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BMRB Entry 25770

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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/BMR25770
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Title: N-terminal domain of the telomerase catalytic subunit Est2 from Ogataea polymorpha   PubMed: 26721464

Deposition date: 2015-08-26 Original release date: 2016-10-28

Authors: Polshakov, Vladimir; Efimov, Sergey; Petrova, Olga; Zvereva, Maria

Citation: Polshakov, Vladimir; Petrova, Olga; Parfenova, Yulia; Efimov, Sergey; Klochkov, Vladimir; Zvereva, Maria; Dontsova, Olga. "NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase"  Biomol. NMR Assign. 10, 183-187 (2016).

Assembly members:
TEN, polymer, 159 residues, Formula weight is not available

Natural source:   Common Name: Ogataea polymorpha   Taxonomy ID: 460523   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Ogataea polymorpha

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

Entity Sequences (FASTA):
TEN: MRFDQYVDENKSSDDFEPLI HDLFETRWHGTGREIWIERV KDRKIPSTLVKPNYSHEELI DMLIGYLADNRYENALINGL VTGDDLEIANSYGFKGRNAV TNLLKSPEFRLVHTIIGTET FLDLLINYSARMGNVYLWGE LNESNYKTQCKSSENLYFQ

Data sets:
Data typeCount
13C chemical shifts521
15N chemical shifts138
1H chemical shifts836

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TEN1

Entities:

Entity 1, TEN 159 residues - Formula weight is not available

1   METARGPHEASPGLNTYRVALASPGLUASN
2   LYSSERSERASPASPPHEGLUPROLEUILE
3   HISASPLEUPHEGLUTHRARGTRPHISGLY
4   THRGLYARGGLUILETRPILEGLUARGVAL
5   LYSASPARGLYSILEPROSERTHRLEUVAL
6   LYSPROASNTYRSERHISGLUGLULEUILE
7   ASPMETLEUILEGLYTYRLEUALAASPASN
8   ARGTYRGLUASNALALEUILEASNGLYLEU
9   VALTHRGLYASPASPLEUGLUILEALAASN
10   SERTYRGLYPHELYSGLYARGASNALAVAL
11   THRASNLEULEULYSSERPROGLUPHEARG
12   LEUVALHISTHRILEILEGLYTHRGLUTHR
13   PHELEUASPLEULEUILEASNTYRSERALA
14   ARGMETGLYASNVALTYRLEUTRPGLYGLU
15   LEUASNGLUSERASNTYRLYSTHRGLNCYS
16   LYSSERSERGLUASNLEUTYRPHEGLN

Samples:

sample_1: TEN, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.02 % w/v; H2O 90%; D2O, [U-2H], 10%

sample_2: TEN, [U-99% 15N], 0.8 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.02 % w/v; H2O 90%; D2O, [U-2H], 10%

sample_3: TEN, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.02 % w/v; D2O, [U-2H], 100%

sample_4: TEN 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.02 % w/v; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
2D DQF-COSYsample_4isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

SPARKY, Goddard - chemical shift assignment, data analysis

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

NMRest, Vladimir Polshakov - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

GB AGC31420.1

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