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Biological Magnetic Resonance Data Bank


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BMRB Entry 18435

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18435
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Title: Solution structure of the C-terminal domain of Tetrahymena telomerase protein p65   PubMed: 22705372

Deposition date: 2012-05-01 Original release date: 2012-06-18

Authors: Singh, Mahavir; Wang, Zhonghua; Koo, Bon-Kyung; Patel, Anooj; Cascio, Duilio; Collins, Kathleen; Feigon, Juli

Citation: Singh, Mahavir; Wang, Zhonghua; Koo, Bon-Kyung; Patel, Anooj; Cascio, Duilio; Collins, Kathleen; Feigon, Juli. "Structural basis for telomerase RNA recognition and RNP assembly by the holoenzyme La family protein p65."  Mol. Cell 47, 16-26 (2012).

Assembly members:
entity, polymer, 137 residues, 15231.342 Da.

Natural source:   Common Name: Tetrahymena thermophila   Taxonomy ID: 5911   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Tetrahymena thermophila

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

Entity Sequences (FASTA):
entity: MHHHHHHSVSIDVEIKQNCL IKIINIPQGTLKAEVVLAVR HLGYEFYCDYIDENSNQINS NLIQQDQHPQLNDLLKEGQA MIRFQNSDEQRLAIQKLLNH NNNKLQIEIRGQICDVISTI PEDEEKNYWNYIKFKKN

Data sets:
Data typeCount
13C chemical shifts532
15N chemical shifts121
1H chemical shifts796

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal domain of Tetrahymena telomerase protein p651

Entities:

Entity 1, C-terminal domain of Tetrahymena telomerase protein p65 137 residues - 15231.342 Da.

1   METHISHISHISHISHISHISSERVALSER
2   ILEASPVALGLUILELYSGLNASNCYSLEU
3   ILELYSILEILEASNILEPROGLNGLYTHR
4   LEULYSALAGLUVALVALLEUALAVALARG
5   HISLEUGLYTYRGLUPHETYRCYSASPTYR
6   ILEASPGLUASNSERASNGLNILEASNSER
7   ASNLEUILEGLNGLNASPGLNHISPROGLN
8   LEUASNASPLEULEULYSGLUGLYGLNALA
9   METILEARGPHEGLNASNSERASPGLUGLN
10   ARGLEUALAILEGLNLYSLEULEUASNHIS
11   ASNASNASNLYSLEUGLNILEGLUILEARG
12   GLYGLNILECYSASPVALILESERTHRILE
13   PROGLUASPGLUGLULYSASNTYRTRPASN
14   TYRILELYSPHELYSLYSASN

Samples:

sample_1: p65 1 mM; H2O 90%; D2O, [U-100% 2H], 10%; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%

sample_2: p65 1 mM; D2O, [U-100% 2H], 100%; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB

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