BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19506

Title: Human eukaryotic release factor eRF1   PubMed: 24452424

Deposition date: 2013-09-19 Original release date: 2014-02-12

Authors: Polshakov, Vladimir

Citation: Polshakov, Vladimir; Eliseev, Boris; Frolova, Ludmila Yu; Chang, Chi-Fon; Huang, Tai-Huang. "Backbone (1)H, (13)C and (15)N resonance assignments of the human eukaryotic release factor eRF1."  Biomol. NMR Assignments ., .-. (2014).

Assembly members:
eRF1, polymer, 445 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
eRF1: MADDPSAADRNVEIWKIKKL IKSLEAARGNGTSMISLIIP PKDQISRVAKMLADEFGTAS NIKSRVNRLSVLGAITSVQQ RLKLYNKVPPNGLVVYCGTI VTEEGKEKKVNIDFEPFKPI NTSLYLCDNKFHTEALTALL SDDSKFGFIVIDGSGALFGT LQGNTREVLHKFTVDLPKKH GRGGQSALRFARLRMEKRHN YVRKVAETAVQLFISGDKVN VAGLVLAGSADFKTELSQSD MFDQRLQSKVLKLVDISYGG ENGFNQAIELSTEVLSNVKF IQEKKLIGRYFDEISQDTGK YCFGVEDTLKALEMGAVEIL IVYENLDIMRYVLHCQGTEE EKILYLTPEQEKDKSHFTDK ETGQEHELIESMPLLEWFAN NYKKFGATLEIVTDKSQEGS QFVKGFGGIGGILRYRVDFQ GMEYQGGDDEFFDLDDYLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts516
15N chemical shifts299
1H chemical shifts305

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Human eRF11

Entities:

Entity 1, Human eRF1 445 residues - Formula weight is not available

1   METALAASPASPPROSERALAALAASPARG
2   ASNVALGLUILETRPLYSILELYSLYSLEU
3   ILELYSSERLEUGLUALAALAARGGLYASN
4   GLYTHRSERMETILESERLEUILEILEPRO
5   PROLYSASPGLNILESERARGVALALALYS
6   METLEUALAASPGLUPHEGLYTHRALASER
7   ASNILELYSSERARGVALASNARGLEUSER
8   VALLEUGLYALAILETHRSERVALGLNGLN
9   ARGLEULYSLEUTYRASNLYSVALPROPRO
10   ASNGLYLEUVALVALTYRCYSGLYTHRILE
11   VALTHRGLUGLUGLYLYSGLULYSLYSVAL
12   ASNILEASPPHEGLUPROPHELYSPROILE
13   ASNTHRSERLEUTYRLEUCYSASPASNLYS
14   PHEHISTHRGLUALALEUTHRALALEULEU
15   SERASPASPSERLYSPHEGLYPHEILEVAL
16   ILEASPGLYSERGLYALALEUPHEGLYTHR
17   LEUGLNGLYASNTHRARGGLUVALLEUHIS
18   LYSPHETHRVALASPLEUPROLYSLYSHIS
19   GLYARGGLYGLYGLNSERALALEUARGPHE
20   ALAARGLEUARGMETGLULYSARGHISASN
21   TYRVALARGLYSVALALAGLUTHRALAVAL
22   GLNLEUPHEILESERGLYASPLYSVALASN
23   VALALAGLYLEUVALLEUALAGLYSERALA
24   ASPPHELYSTHRGLULEUSERGLNSERASP
25   METPHEASPGLNARGLEUGLNSERLYSVAL
26   LEULYSLEUVALASPILESERTYRGLYGLY
27   GLUASNGLYPHEASNGLNALAILEGLULEU
28   SERTHRGLUVALLEUSERASNVALLYSPHE
29   ILEGLNGLULYSLYSLEUILEGLYARGTYR
30   PHEASPGLUILESERGLNASPTHRGLYLYS
31   TYRCYSPHEGLYVALGLUASPTHRLEULYS
32   ALALEUGLUMETGLYALAVALGLUILELEU
33   ILEVALTYRGLUASNLEUASPILEMETARG
34   TYRVALLEUHISCYSGLNGLYTHRGLUGLU
35   GLULYSILELEUTYRLEUTHRPROGLUGLN
36   GLULYSASPLYSSERHISPHETHRASPLYS
37   GLUTHRGLYGLNGLUHISGLULEUILEGLU
38   SERMETPROLEULEUGLUTRPPHEALAASN
39   ASNTYRLYSLYSPHEGLYALATHRLEUGLU
40   ILEVALTHRASPLYSSERGLNGLUGLYSER
41   GLNPHEVALLYSGLYPHEGLYGLYILEGLY
42   GLYILELEUARGTYRARGVALASPPHEGLN
43   GLYMETGLUTYRGLNGLYGLYASPASPGLU
44   PHEPHEASPLEUASPASPTYRLEUGLUHIS
45   HISHISHISHISHIS

Samples:

sample_1: eRF1, [U-13C; U-15N; U-2H], 0.2 ± 0.05 mM; sodium phosphate 25 ± 0.05 mM; sodium chloride 100 ± 0.05 mM; dithiothreitol 2.0 ± 0.05 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HCACOsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

PDB
DBJ BAA13439 BAA85489 BAC33839 BAE31210 BAE31619
EMBL CAA37987 CAA57281 CAA57282 CAA78620 CAH93389
GB AAB49726 AAD43966 AAH13717 AAH14269 AAH61387
REF NP_001008345 NP_001069722 NP_001076236 NP_001084363 NP_001126989
SP P35615 P62495 P62496 P62497 P62498
TPG DAA27419

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