BMRB Entry 17878

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17878

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for La(4-325)
Deposition date:
2011-08-22
Original release date:
2011-12-09
Authors:
Martino, Luigi; Kelly, Geoff; Curry, Stephen; Conte, Maria
Citation:

Citation: Martino, Luigi; Pennell, Simon; Kelly, Geoff; Bui, Tam; Kotik-Kogan, Olga; Smerdon, Stephen; Drake, Alex; Curry, Stephen; Conte, Maria. "Analysis of the interaction with the hepatitis C virus mRNA reveals an alternative mode of RNA recognition by the human La protein."  Nucleic Acids Res. 40, 1381-1394 (2012).
PubMed: 22009680

Assembly members:

Assembly members:
human_La_protein, polymer, 322 residues, 37441.7 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human_La_protein: NGDNEKMAALEAKICHQIEY YFGDFNLPRDKFLKEQIKLD EGWVPLEIMIKFNRLNRLTT DFNVIVEALSKSKAELMEIS EDKTKIRRSPSKPLPEVTDE YKNDVKNRSVYIKGFPTDAT LDDIKEWLEDKGQVLNIQMR RTLHKAFKGSIFVVFDSIES AKKFVETPGQKYKETDLLIL FKDDYFAKKNEERKQNKVEA KLRAKQEQEAKQKLEEDAEM KSLEEKIGCLLKFSGDLDDQ TCREDLHILFSNHGEIKWID FVRGAKEGIILFKEKAKEAL GKAKDANNGNLQLRNKEVTW EVLEGEVEKEALKKIIEDQQ ES

Data sets:
Data typeCount
13C chemical shifts687
15N chemical shifts260
1H chemical shifts260

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1La(4-325)1

Entities:

Entity 1, La(4-325) 322 residues - 37441.7 Da.

1   ASNGLYASPASNGLULYSMETALAALALEU
2   GLUALALYSILECYSHISGLNILEGLUTYR
3   TYRPHEGLYASPPHEASNLEUPROARGASP
4   LYSPHELEULYSGLUGLNILELYSLEUASP
5   GLUGLYTRPVALPROLEUGLUILEMETILE
6   LYSPHEASNARGLEUASNARGLEUTHRTHR
7   ASPPHEASNVALILEVALGLUALALEUSER
8   LYSSERLYSALAGLULEUMETGLUILESER
9   GLUASPLYSTHRLYSILEARGARGSERPRO
10   SERLYSPROLEUPROGLUVALTHRASPGLU
11   TYRLYSASNASPVALLYSASNARGSERVAL
12   TYRILELYSGLYPHEPROTHRASPALATHR
13   LEUASPASPILELYSGLUTRPLEUGLUASP
14   LYSGLYGLNVALLEUASNILEGLNMETARG
15   ARGTHRLEUHISLYSALAPHELYSGLYSER
16   ILEPHEVALVALPHEASPSERILEGLUSER
17   ALALYSLYSPHEVALGLUTHRPROGLYGLN
18   LYSTYRLYSGLUTHRASPLEULEUILELEU
19   PHELYSASPASPTYRPHEALALYSLYSASN
20   GLUGLUARGLYSGLNASNLYSVALGLUALA
21   LYSLEUARGALALYSGLNGLUGLNGLUALA
22   LYSGLNLYSLEUGLUGLUASPALAGLUMET
23   LYSSERLEUGLUGLULYSILEGLYCYSLEU
24   LEULYSPHESERGLYASPLEUASPASPGLN
25   THRCYSARGGLUASPLEUHISILELEUPHE
26   SERASNHISGLYGLUILELYSTRPILEASP
27   PHEVALARGGLYALALYSGLUGLYILEILE
28   LEUPHELYSGLULYSALALYSGLUALALEU
29   GLYLYSALALYSASPALAASNASNGLYASN
30   LEUGLNLEUARGASNLYSGLUVALTHRTRP
31   GLUVALLEUGLUGLYGLUVALGLULYSGLU
32   ALALEULYSLYSILEILEGLUASPGLNGLN
33   GLUSER

Samples:

sample_La(4-325): La(4-325), [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; Tris 20 mM; KCl 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.25; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY-HSQCsample_La(4-325)isotropicsample_conditions_1
3D TROSY-HNCAsample_La(4-325)isotropicsample_conditions_1
3D TROSY-HNCACBsample_La(4-325)isotropicsample_conditions_1
3D TROSY-HN(COCA)CBsample_La(4-325)isotropicsample_conditions_1
3D TROSY-HNCOsample_La(4-325)isotropicsample_conditions_1

Software:

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

XEASY, Bartels et al. - chemical shift assignment

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 15726 15727
PDB
DBJ BAE87871 BAE87890 BAG70042 BAG70165 BAI45822
EMBL CAA31985 CAA32815
GB AAA36577 AAA51885 AAH01289 AAH20818 AAP88864
REF NP_001267347 NP_001270975 NP_001281074 NP_001296114 NP_003133
SP P05455
AlphaFold P05455

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