BMRB Entry 36473

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36473
MolProbity Validation Chart

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Title:
Solution structure of Tetrahymena p75OB1-p50PBM
Deposition date:
2022-03-04
Original release date:
2023-03-16
Authors:
Wu, B.; Tang, T.; Xue, H.; Wu, J.; Lei, M.
Citation:

Citation: Ma, Y.; Tang, T.; Wu, B.; Xue, H.; Cao, Y.; Wu, J.; Wan, B.; Lei, M.. "Association of the CST complex and p50 in Tetrahymena is crucial for telomere maintenance"  .

Assembly members:

Assembly members:
Telomerase-associated protein p75OB1, polymer, 172 residues, 20128.947 Da.
Telomerase associated protein p50PBM, polymer, 14 residues, 1536.663 Da.

Natural source:

Natural source:   Common Name: Tetrahymena   Taxonomy ID: 5890   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Tetrahymena not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Telomerase-associated protein p75OB1: MEIEEDLNLKILEDVKKLYL QSFDYIKNGISSGGSGGSID LSRITFLYKFISVNPTLLLI NEKTQAKRRIFQGEYLYGKK KIQFNIIAKNLEIERELIQF FKKPYQCYIMHNVQVFQMLN KNKNNNVVEFMDSEDLQSSV DSQLYYLIDESSHVLEDDSM DFISTLTRLSDS
Telomerase associated protein p50PBM: QDDFGDGCLLQIVN

Data sets:
Data typeCount
13C chemical shifts802
15N chemical shifts195
1H chemical shifts1330

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 172 residues - 20128.947 Da.

1   METGLUILEGLUGLUASPLEUASNLEULYS
2   ILELEUGLUASPVALLYSLYSLEUTYRLEU
3   GLNSERPHEASPTYRILELYSASNGLYILE
4   SERSERGLYGLYSERGLYGLYSERILEASP
5   LEUSERARGILETHRPHELEUTYRLYSPHE
6   ILESERVALASNPROTHRLEULEULEUILE
7   ASNGLULYSTHRGLNALALYSARGARGILE
8   PHEGLNGLYGLUTYRLEUTYRGLYLYSLYS
9   LYSILEGLNPHEASNILEILEALALYSASN
10   LEUGLUILEGLUARGGLULEUILEGLNPHE
11   PHELYSLYSPROTYRGLNCYSTYRILEMET
12   HISASNVALGLNVALPHEGLNMETLEUASN
13   LYSASNLYSASNASNASNVALVALGLUPHE
14   METASPSERGLUASPLEUGLNSERSERVAL
15   ASPSERGLNLEUTYRTYRLEUILEASPGLU
16   SERSERHISVALLEUGLUASPASPSERMET
17   ASPPHEILESERTHRLEUTHRARGLEUSER
18   ASPSER

Entity 2, unit_2 14 residues - 1536.663 Da.

1   GLNASPASPPHEGLYASPGLYCYSLEULEU
2   GLNILEVALASN

Samples:

sample_1: DTT 2 mM; NaN3 0.03%; PMSF 0.5 mM; benzamidine 2 mM; inhibitor cocktail 1 % v/v; p75OB1, [U-100% 13C; U-100% 15N], 0.5 mM; p50PBM, [U-100% 13C; U-100% 15N], 0.5 mM; phosphate buffer 20 mM; sodium chloride 300 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_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 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

MddNMR, Orekhov, V.Y. - processing

NMRFAM-SPARKY, Lee,W., Tonelli, M., & Markley, J.L. - data analysis

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

VnmrJ v4.1, Agilent - collection

NMR spectrometers:

  • Agilent DD2 800 MHz
  • Agilent DD2 600 MHz

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