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 17822

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F   PubMed: 22383581

Deposition date: 2011-08-02 Original release date: 2012-08-29

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

Citation: Wong, Leo; Li, Yan; Pillay, Shubhadra; Frolova, Ludmila; Pervushin, Konstantin. "Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1"  Nucleic Acids Res. 40, 5751-5765 (2012).

Assembly members:
entity, polymer, 144 residues, 16079.768 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

Entity Sequences (FASTA):
entity: MADDPSAADRNVEIWKIKKL IKSLEAARGNGTSMISLIIP PKDQISRVAKMLADEFGTAS NIKSRVNRLSVLGAITSVQQ RLKLYNKVPPNGLVVYCGTI VTEEGKEKKVNIDFEPFKPI NQFMYFCDNKFHTEALTALL SDLE

Data sets:
Data typeCount
13C chemical shifts488
15N chemical shifts150
1H chemical shifts1026

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1QFMF1

Entities:

Entity 1, QFMF 144 residues - 16079.768 Da.

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   ASNGLNPHEMETTYRPHECYSASPASNLYS
14   PHEHISTHRGLUALALEUTHRALALEULEU
15   SERASPLEUGLU

Samples:

sample_1: DSS 0.1 mM; potassium chloride 100 mM; MES 20 mM; D2O, [U-2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 18092 19506
PDB
DBJ BAA85489 BAC33839 BAE37589 BAE41096 BAE41644
EMBL CAA37987 CAA57281 CAA57282 CAA78620 CAF90786
GB AAB49726 AAD43966 AAH44515 AAH61387 AAH66583
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