BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25020

Title: Solution structure of E55Q mutant of eRF1 N-domain

Deposition date: 2014-06-13 Original release date: 2015-06-29

Authors: Pillay, Shubhadra; Li, Yan; Wong, Leo E; Pervushin, Konstantin

Citation: Pillay, Shubhadra; Li, Yan; Wong, Leo E; Pervushin, Konstantin. "Structural insights of eRF1 mutants and their correlation with stop codon recognition"  ACS Chemical Biology ., .-..

Assembly members:
entity, polymer, 142 residues, 15697.333 Da.

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   Vector: pET23(+)

Entity Sequences (FASTA):
entity: MADDPSAADRNVEIWKIKKL IKSLEAARGNGTSMISLIIP PKDQISRVAKMLADQFGTAS NIKSRVNRLSVLGAITSVQQ RLKLYNKVPPNGLVVYCGTI VTEEGKEKKVNIDFEPFKPI NTSLYLCDNKFHTEALTALL SD

Data sets:
Data typeCount
13C chemical shifts444
15N chemical shifts146
1H chemical shifts966

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E55Q mutant of eRF1 N-domain1

Entities:

Entity 1, E55Q mutant of eRF1 N-domain 142 residues - 15697.333 Da.

1   METALAASPASPPROSERALAALAASPARG
2   ASNVALGLUILETRPLYSILELYSLYSLEU
3   ILELYSSERLEUGLUALAALAARGGLYASN
4   GLYTHRSERMETILESERLEUILEILEPRO
5   PROLYSASPGLNILESERARGVALALALYS
6   METLEUALAASPGLNPHEGLYTHRALASER
7   ASNILELYSSERARGVALASNARGLEUSER
8   VALLEUGLYALAILETHRSERVALGLNGLN
9   ARGLEULYSLEUTYRASNLYSVALPROPRO
10   ASNGLYLEUVALVALTYRCYSGLYTHRILE
11   VALTHRGLUGLUGLYLYSGLULYSLYSVAL
12   ASNILEASPPHEGLUPROPHELYSPROILE
13   ASNTHRSERLEUTYRLEUCYSASPASNLYS
14   PHEHISTHRGLUALALEUTHRALALEULEU
15   SERASP

Samples:

sample_1: MES 20 mM; potassium chloride 100 mM; DTT 2 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Bruker Biospin, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, collection, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 18092 19506 25016
PDB
DBJ BAA85489 BAC33839 BAE31210 BAE31619 BAE37589
EMBL CAA37987 CAA57281 CAA57282 CAA78620 CAF90786
GB AAA36665 AAB49726 AAD43966 AAH13717 AAH14269
REF NP_001008345 NP_001069722 NP_001076236 NP_001084363 NP_001126989
SP P35615 P62495 P62496 P62497 P62498
TPG DAA27419
AlphaFold P62496 P62498 P62497 P35615 P62495

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