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N-terminal domain of the telomerase catalytic subunit Est2 from Ogataea polymorpha
Authors
Polshakov, V., Efimov, S., Petrova, O., Zvereva, M.
Assembly
N Est2
Entity
1. N Est2 (polymer, Thiol state: all free), 159 monomers, 18563.60 Da Detail

MRFDQYVDEN KSSDDFEPLI HDLFETRWHG TGREIWIERV KDRKIPSTLV KPNYSHEELI DMLIGYLADN RYENALINGL VTGDDLEIAN SYGFKGRNAV TNLLKSPEFR LVHTIIGTET FLDLLINYSA RMGNVYLWGE LNESNYKTQC KSSENLYFQ


Formula weight
18563.6 Da
Source organism
Ogataea polymorpha
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 89.9 %, Completeness: 73.8 %, Completeness (bb): 85.5 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All73.8 % (1410 of 1910)73.3 % (727 of 992)72.8 % (542 of 744)81.0 % (141 of 174)
Backbone85.5 % (809 of 946)84.9 % (275 of 324)86.7 % (405 of 467)83.2 % (129 of 155)
Sidechain65.9 % (733 of 1113)67.7 % (452 of 668)62.9 % (268 of 426)68.4 % (13 of 19)
Aromatic30.4 % (59 of 194)40.2 % (39 of 97)18.1 % (17 of 94)100.0 % (3 of 3)
Methyl89.5 % (154 of 172)91.9 % (79 of 86)87.2 % (75 of 86)

1. TEN

MRFDQYVDEN KSSDDFEPLI HDLFETRWHG TGREIWIERV KDRKIPSTLV KPNYSHEELI DMLIGYLADN RYENALINGL VTGDDLEIAN SYGFKGRNAV TNLLKSPEFR LVHTIIGTET FLDLLINYSA RMGNVYLWGE LNESNYKTQC KSSENLYFQ

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7


#NameIsotope labelingTypeConcentration
1TEN[U-99% 13C; U-99% 15N]protein0.5 mM
2sodium phosphatenatural abundancebuffer20 mM
3sodium chloridenatural abundancesalt50 mM
4DTTnatural abundance1 mM
5sodium azidenatural abundance0.02 % w/v
6H2Onatural abundancesolvent90 %
7D2O[U-2H]solvent10 %
Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7


#NameIsotope labelingTypeConcentration
8TEN[U-99% 15N]protein0.8 mM
9sodium phosphatenatural abundancebuffer20 mM
10sodium chloridenatural abundancesalt50 mM
11DTTnatural abundance1 mM
12sodium azidenatural abundance0.02 % w/v
13H2Onatural abundancesolvent90 %
14D2O[U-2H]solvent10 %
Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 303 K, pH 7


#NameIsotope labelingTypeConcentration
15TEN[U-99% 13C; U-99% 15N]protein0.5 mM
16sodium phosphatenatural abundancebuffer20 mM
17sodium chloridenatural abundancesalt50 mM
18DTTnatural abundance1 mM
19sodium azidenatural abundance0.02 % w/v
20D2O[U-2H]solvent100 %
Sample #4

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7


#NameIsotope labelingTypeConcentration
21TENnatural abundanceprotein1.0 mM
22sodium phosphatenatural abundancebuffer20 mM
23sodium chloridenatural abundancesalt50 mM
24DTTnatural abundance1 mM
25sodium azidenatural abundance0.02 % w/v
26H2Onatural abundancesolvent90 %
27D2O[U-2H]solvent10 %

LACS Plot; CA
Referencing offset: -0.18 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.18 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.02 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: 0.14 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 5LGF, Strand ID: A Detail


Release date
2016-10-27
Citation
NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase
Polshakov, V., Petrova, O., Parfenova, Y., Efimov, S., Klochkov, V., Zvereva, M., Dontsova, O.
Biomol. NMR Assign. (2015), 10, 183-187, PubMed 26721464 , DOI 10.1007/s12104-015-9663-6 ,
Experiments performed 19 experiments Detail
NMR combined restraints 4 contents Detail
Keywords Protein structure and dynamics, Telomerase, Telomerase reverse transcriptase