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Human eRF1 C-domain
Authors
Mantsyzov, A.B., Polshakov, V.I., Birdsall, B., Kisselev, L.L.
Assembly
Human eRF1 C-domain
Entity
1. Human eRF1 C-domain (polymer, Thiol state: all free), 171 monomers, 19954.10 Da Detail

MSNVKFIQEK KLIGRYFDEI SQDTGKYCFG VEDTLKALEM GAVEILIVYE NLDIMRYVLH CQGTEEEKIL YLTPEQEKDK SHFTDKETGQ EHELIESMPL LEWFANNYKK FGATLEIVTD KSQEGSQFVK GFGGIGGILR YRVDFQGMEY QGGDDEFFDL DDYLEHHHHH H


Formula weight
19954.1 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete1
Sequence coverage: 93.0 %, Completeness: 34.4 %, Completeness (bb): 62.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All34.4 % (708 of 2057)20.2 % (216 of 1070)42.4 % (341 of 804)82.5 % (151 of 183)
Backbone62.2 % (636 of 1022)46.3 % (165 of 356)64.4 % (320 of 497)89.3 % (151 of 169)
Sidechain 7.2 % (86 of 1190) 7.1 % (51 of 714) 7.6 % (35 of 462) 0.0 % (0 of 14)
Aromatic 3.5 % (8 of 230) 3.5 % (4 of 115) 3.5 % (4 of 114) 0.0 % (0 of 1)
Methyl13.8 % (22 of 160)15.0 % (12 of 80)12.5 % (10 of 80)

1. C-domain of human polypeptide release factor eRF1

MSNVKFIQEK KLIGRYFDEI SQDTGKYCFG VEDTLKALEM GAVEILIVYE NLDIMRYVLH CQGTEEEKIL YLTPEQEKDK SHFTDKETGQ EHELIESMPL LEWFANNYKK FGATLEIVTD KSQEGSQFVK GFGGIGGILR YRVDFQGMEY QGGDDEFFDL DDYLEHHHHH H

Sample #1

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0


#NameIsotope labelingTypeConcentration
1C-domain of human polypeptide release factor eRF1natural abundance1 mM
2potassium phosphatenatural abundance10 mM
3potassium chloridenatural abundance50 mM
Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0


#NameIsotope labelingTypeConcentration
4C-domain of human polypeptide release factor eRF1[U-99% 15N]1.1 mM
5potassium phosphatenatural abundance10 mM
6potassium chloridenatural abundance20 mM
Sample #3

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0


#NameIsotope labelingTypeConcentration
7C-domain of human polypeptide release factor eRF1[U-99% 13C; U-99% 15N]0.8 mM
8potassium phosphatenatural abundance10 mM
9potassium chloridenatural abundance20 mM

Chem. Shift Complete2
Sequence coverage: 17.0 %, Completeness: 20.9 %, Completeness (bb): 36.4 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All20.9 % (858 of 4114)13.8 % (295 of 2140)24.2 % (389 of 1608)47.5 % (174 of 366)
Backbone36.4 % (743 of 2044)29.4 % (209 of 712)36.2 % (360 of 994)51.5 % (174 of 338)
Sidechain 5.8 % (137 of 2380) 6.0 % (85 of 1428) 5.6 % (52 of 924) 0.0 % (0 of 28)
Aromatic 3.5 % (16 of 460) 3.5 % (8 of 230) 3.5 % (8 of 228) 0.0 % (0 of 2)
Methyl 9.7 % (31 of 320)11.2 % (18 of 160) 8.1 % (13 of 160)

1. C-domain of human polypeptide release factor eRF1

MSNVKFIQEK KLIGRYFDEI SQDTGKYCFG VEDTLKALEM GAVEILIVYE NLDIMRYVLH CQGTEEEKIL YLTPEQEKDK SHFTDKETGQ EHELIESMPL LEWFANNYKK FGATLEIVTD KSQEGSQFVK GFGGIGGILR YRVDFQGMEY QGGDDEFFDL DDYLEHHHHH H

Sample #1

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0


#NameIsotope labelingTypeConcentration
1C-domain of human polypeptide release factor eRF1natural abundance1 mM
2potassium phosphatenatural abundance10 mM
3potassium chloridenatural abundance50 mM
Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0


#NameIsotope labelingTypeConcentration
4C-domain of human polypeptide release factor eRF1[U-99% 15N]1.1 mM
5potassium phosphatenatural abundance10 mM
6potassium chloridenatural abundance20 mM
Sample #3

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0


#NameIsotope labelingTypeConcentration
7C-domain of human polypeptide release factor eRF1[U-99% 13C; U-99% 15N]0.8 mM
8potassium phosphatenatural abundance10 mM
9potassium chloridenatural abundance20 mM

Protein Blocks Logo
Calculated from 24 models in PDB: 2KTU, Strand ID: A Detail


Release date
2015-09-02
Citation
NMR assignments of the C-terminal domain of human polypeptide release factor eRF1
Mantsyzov, A.B., Ivanova, E.V., Birdsall, B., Kolosov, P.M., Kisselev, L.L., Polshakov, V.I.
Biomol. NMR Assign. (2007), 1, 183-185, PubMed 19636860 , DOI 10.1007/s12104-007-9050-z ,
Related entities 1. Human eRF1 C-domain, : 1 : 2 : 119 entities Detail
Interaction partners 1. Human eRF1 C-domain, : 3 interactors Detail
Experiments performed 13 experiments Detail
Chemical shift validation 4 contents Detail