BMRB Entry 51080

Title:
Assignment of 1H, 13C, 15N backbone chemical shifts of SERBP1 149-400
Deposition date:
2021-09-08
Original release date:
2021-09-09
Authors:
Baudin, Antoine; Moreno-Romero, Alma; Xu, Xiaoping; Selig, Emily; Penalva, Luiz; Libich, David
Citation:

Citation: Baudin, Antoine; Moreno-Romero, Alma; Xu, Xiaoping; Selig, Emily; Penalva, Luiz; Libich, David. "Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes"  Front. Mol. Biosci 8, 744707-744707 (2021).
PubMed: 34631798

Assembly members:

Assembly members:
entity_1, polymer, 252 residues, Formula weight is not available

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: pAG8HA

Data sets:
Data typeCount
13C chemical shifts619
15N chemical shifts179
1H chemical shifts179

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SERBP11

Entities:

Entity 1, SERBP1 252 residues - Formula weight is not available

1   GLYGLUPHESERVALASPARGPROILEILE
2   ASPARGPROILEARGGLYARGGLYGLYLEU
3   GLYARGGLYARGGLYGLYARGGLYARGGLY
4   METGLYARGGLYASPGLYPHEASPSERARG
5   GLYLYSARGGLUPHEASPARGHISSERGLY
6   SERASPARGSERSERPHESERHISTYRSER
7   GLYLEULYSHISGLUASPLYSARGGLYGLY
8   SERGLYSERHISASNTRPGLYTHRVALLYS
9   ASPGLULEUTHRGLUSERPROLYSTYRILE
10   GLNLYSGLNILESERTYRASNTYRSERASP
11   LEUASPGLNSERASNVALTHRGLUGLUTHR
12   PROGLUGLYGLUGLUHISHISPROVALALA
13   ASPTHRGLUASNLYSGLUASNGLUVALGLU
14   GLUVALLYSGLUGLUGLYPROLYSGLUMET
15   THRLEUASPGLUTRPLYSALAILEGLNASN
16   LYSASPARGALALYSVALGLUPHEASNILE
17   ARGLYSPROASNGLUGLYALAASPGLYGLN
18   TRPLYSLYSGLYPHEVALLEUHISLYSSER
19   LYSSERGLUGLUALAHISALAGLUASPSER
20   VALMETASPHISHISPHEARGLYSPROALA
21   ASNASPILETHRSERGLNLEUGLUILEASN
22   PHEGLYASPLEUGLYARGPROGLYARGGLY
23   GLYARGGLYGLYARGGLYGLYARGGLYARG
24   GLYGLYARGPROASNARGGLYSERARGTHR
25   ASPLYSSERSERALASERALAPROASPVAL
26   ASPASP

Samples:

sample_1: SERBP1, [U-100% 13C; U-100% 15N], 300 uM

sample_conditions_1: ionic strength: 60 mM; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.5 - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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