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 51713

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51713

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Title: Solution NMR assignment of RRM2 Cterminal of human La protein.   PubMed: 36768895

Deposition date: 2022-11-29 Original release date: 2023-01-31

Authors: Machaliotis, Georgios; Argyriou, Aikaterini; Makrynitsa, Garyfallia; Spyroulias, Georgios

Citation: Argyriou, Aikaterini; Machaliotis, Georgios; Makrynitsa, Garyfallia; Kaliatsi, Eleni; Stathopoulos, Constantinos; Spyroulias, Georgios. "NMR Analysis Suggests Synergy between the RRM2 and and the Carboxy-Terminal Segment of Human La Protein in the Recognition and Interaction with HCV IRES"  Int. J. Mol. Sci. 24, 2572-2572 (2023).

Assembly members:
entity_1, polymer, 185 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   Vector: pET20b(+)

Entity Sequences (FASTA):
entity_1: MSLEEKIGCLLKFSGDLDDQ TCREDLHILFSNHGEIKWID FVRGAKEGIILFKEKAKEAL GKAKDANNGNLQLRNKEVTW EVLEGEVEKEALKKIIEDQQ ESLNKWKSKGRRFKGKGKGN KAAQPGSGKGKVQFQGKKTK FASDDEHDEHDENGATGPVK RAREETDKEEPASKQQKTEN GAGDQ

Data sets:
Data typeCount
13C chemical shifts684
15N chemical shifts165
1H chemical shifts1041

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM2-Cterminal1

Entities:

Entity 1, RRM2-Cterminal 185 residues - Formula weight is not available

1   METSERLEUGLUGLULYSILEGLYCYSLEU
2   LEULYSPHESERGLYASPLEUASPASPGLN
3   THRCYSARGGLUASPLEUHISILELEUPHE
4   SERASNHISGLYGLUILELYSTRPILEASP
5   PHEVALARGGLYALALYSGLUGLYILEILE
6   LEUPHELYSGLULYSALALYSGLUALALEU
7   GLYLYSALALYSASPALAASNASNGLYASN
8   LEUGLNLEUARGASNLYSGLUVALTHRTRP
9   GLUVALLEUGLUGLYGLUVALGLULYSGLU
10   ALALEULYSLYSILEILEGLUASPGLNGLN
11   GLUSERLEUASNLYSTRPLYSSERLYSGLY
12   ARGARGPHELYSGLYLYSGLYLYSGLYASN
13   LYSALAALAGLNPROGLYSERGLYLYSGLY
14   LYSVALGLNPHEGLNGLYLYSLYSTHRLYS
15   PHEALASERASPASPGLUHISASPGLUHIS
16   ASPGLUASNGLYALATHRGLYPROVALLYS
17   ARGALAARGGLUGLUTHRASPLYSGLUGLU
18   PROALASERLYSGLNGLNLYSTHRGLUASN
19   GLYALAGLYASPGLN

Samples:

sample_1: D2O, 100%, 10% v/v; DTT 20 mM; H2O 90% v/v; potassium phosphate 50 mM; human La RRM2-Cterminal, [U-99% 13C; U-99% 15N], 0.74 mM; protease inhibitor + EDTA 1 uL; sodium azide 3 uL

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CARA v1.5.5 - chemical shift assignment, data analysis, peak picking

TOPSPIN v3.5 pl7 - Data collection, Data processing

NMR spectrometers:

  • Bruker AVANCE III 700MHz MHz

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