BMRB Entry 26320

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26320

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for RRM2/3 in complex with Paip2A(25-83)
Deposition date:
2021-09-08
Original release date:
2022-05-11
Authors:
Sagae, Takeru; Yokogawa, Mariko; Osawa, Masanori
Citation:

Citation: Sagae, Takeru; Yokogawa, Mariko; Sawazaki, Ryoichi; Ishii, Yuichiro; Hosoda, Nao; Hoshino, Shin-ichi; Imai, Shunsuke; Shimada, Ichio; 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:
RRM2/3 of PABPC1, polymer, 195 residues, 22202 Da.
Paip2A(25-83), polymer, 64 residues, 7995 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):
RRM2/3 of PABPC1: GPLGSNIFIKNLDKSIDNKA LYDTFSAFGNILSCKVVCDE NGSKGYGFVHFETQEAAERA IEKMNGMLLNDRKVFVGRFK SRKEREAELGARAKEFTNVY IKNFGEDMDDERLKDLFGKF GPALSVKVMTDESGKSKGFG FVSFERHEDAQKAVDEMNGK ELNGKQIYVGRAQKKVERQT ELKRKFEQMKQDRIT
Paip2A(25-83): GPLGSHEDDNPFAEYMWMEN EEEFNRQIEEELWEEEFIER CFQEMLEEEEEHEWFIPARD LPQT

Data sets:
Data typeCount
13C chemical shifts110
15N chemical shifts104
1H chemical shifts104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM2/3 of PABPC11
2Paip2A(25-83)2

Entities:

Entity 1, RRM2/3 of PABPC1 195 residues - 22202 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

Entity 2, Paip2A(25-83) 64 residues - 7995 Da.

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

Samples:

sample_1: RRM2/3 of PABPC1, [U-100% 13C; U-100% 15N], 394 uM; Paip2A(25-83) 493 uM; sodium phosphate 18 mM; sodium chloride 135 mM; H2O 90%; D2O, [U-2H], 10%; DTT 0.9 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

SPARKY v3.190 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz

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