BMRB Entry 26323

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26323

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Paip2A(25-83) in complex with RRM2/3
Deposition date:
2022-01-04
Original release date:
2022-05-11
Authors:
Sagae, Takeru; Yokogawa, Mariko; Osawa, Masanori
Citation:

Citation: Sagae, Takeru; Yokogawa, Mariko; Osawa, Masanori. "Paip2 competitively dissociates PABPC1 from poly(A) by initial access to RRM2 of the poly(A)-bound PABPC1"  J. Biol. Chem. 298, 101844-101844 (2022).
PubMed: 35307347

Assembly members:

Assembly members:
Paip2A(25-83), polymer, 64 residues, 7994.58 Da.
RRM2/3 of PABPC1, polymer, 195 residues, 22202.22 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6p-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Paip2A(25-83): GPLGSHEDDNPFAEYMWMEN EEEFNRQIEEELWEEEFIER CFQEMLEEEEEHEWFIPARD LPQT
RRM2/3 of PABPC1: GPLGSNIFIKNLDKSIDNKA LYDTFSAFGNILSCKVVCDE NGSKGYGFVHFETQEAAERA IEKMNGMLLNDRKVFVGRFK SRKEREAELGARAKEFTNVY IKNFGEDMDDERLKDLFGKF GPALSVKVMTDESGKSKGFG FVSFERHEDAQKAVDEMNGK ELNGKQIYVGRAQKKVERQT ELKRKFEQMKQDRIT

Data sets:
Data typeCount
13C chemical shifts102
15N chemical shifts46
1H chemical shifts46

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11
2subunit 22

Entities:

Entity 1, subunit 1 64 residues - 7994.58 Da.

1   GLYPROLEUGLYSERHISGLUASPASPASN
2   PROPHEALAGLUTYRMETTRPMETGLUASN
3   GLUGLUGLUPHEASNARGGLNILEGLUGLU
4   GLULEUTRPGLUGLUGLUPHEILEGLUARG
5   CYSPHEGLNGLUMETLEUGLUGLUGLUGLU
6   GLUHISGLUTRPPHEILEPROALAARGASP
7   LEUPROGLNTHR

Entity 2, subunit 2 195 residues - 22202.22 Da.

1   GLYPROLEUGLYSERASNILEPHEILELYS
2   ASNLEUASPLYSSERILEASPASNLYSALA
3   LEUTYRASPTHRPHESERALAPHEGLYASN
4   ILELEUSERCYSLYSVALVALCYSASPGLU
5   ASNGLYSERLYSGLYTYRGLYPHEVALHIS
6   PHEGLUTHRGLNGLUALAALAGLUARGALA
7   ILEGLULYSMETASNGLYMETLEULEUASN
8   ASPARGLYSVALPHEVALGLYARGPHELYS
9   SERARGLYSGLUARGGLUALAGLULEUGLY
10   ALAARGALALYSGLUPHETHRASNVALTYR
11   ILELYSASNPHEGLYGLUASPMETASPASP
12   GLUARGLEULYSASPLEUPHEGLYLYSPHE
13   GLYPROALALEUSERVALLYSVALMETTHR
14   ASPGLUSERGLYLYSSERLYSGLYPHEGLY
15   PHEVALSERPHEGLUARGHISGLUASPALA
16   GLNLYSALAVALASPGLUMETASNGLYLYS
17   GLULEUASNGLYLYSGLNILETYRVALGLY
18   ARGALAGLNLYSLYSVALGLUARGGLNTHR
19   GLULEULYSARGLYSPHEGLUGLNMETLYS
20   GLNASPARGILETHR

Samples:

sample_1: Paip2A(25-83), [U-13C; U-15N; U-2H], 826 uM; RRM2/3 of PABPC1 1032.5 uM; potassium phosphate 18 mM; sodium chloride 90 mM; DTT 0.9 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: pH: 6.0; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

SPARKY v3.190 - chemical shift assignment

TOPSPIN v4.0.8 - processing

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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