BMRB Entry 50385

Title:
Proton solid-state NMR assignment of pRN1
Deposition date:
2020-07-10
Original release date:
2020-07-18
Authors:
Lacabanne, Denis; Boudet, Julien; Malar, Alexander A.; Wu, Pengzhi; Salmon, Loic; Allain, Frederic H.-T.; Meier, Beat H.; Wiegand, Thomas
Citation:

Citation: Lacabanne, Denis; Boudet, Julien; Malar, Alexander A.; Wu, Pengzhi; Cadalbert, Riccardo; Salmon, Loic; Allain, Frederic H.-T.; Meier, Beat H.; Wiegand, Thomas. "Protein Side-Chain-DNA Contacts Probed by Fast Magic-Angle Spinning NMR"  J. Phys. Chem. B 124, 11089-11097 (2020).
PubMed: 33238710

Assembly members:

Assembly members:
entity_1, polymer, 370 residues, Formula weight is not available
entity_ATP, non-polymer, 507.181 Da.

Natural source:

Natural source:   Common Name: Sulfolobus islandicus   Taxonomy ID: 43080   Superkingdom: Archaea   Kingdom: not available   Genus/species: Sulfolobus islandicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Data sets:
Data typeCount
13C chemical shifts169
15N chemical shifts172
1H chemical shifts303

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pRN11
2ATP2

Entities:

Entity 1, pRN1 370 residues - Formula weight is not available

1   METILEASNLYSARGSERLYSVALILELEU
2   HISGLYASNVALLYSLYSTHRARGARGTHR
3   GLYVALTYRMETILESERLEUASPASNSER
4   GLYASNLYSASPPHESERSERASNPHESER
5   SERGLUARGILEARGTYRALALYSTRPPHE
6   LEUGLUHISGLYPHEASNILEILEPROILE
7   ASPPROGLUSERLYSLYSPROVALLEULYS
8   GLUTRPGLNLYSTYRSERHISGLUMETPRO
9   SERASPGLUGLULYSGLNARGPHELEULYS
10   METILEGLUGLUGLYTYRASNTYRALAILE
11   PROGLYGLYGLNLYSGLYLEUVALILELEU
12   ASPPHEGLUSERLYSGLULYSLEULYSALA
13   TRPILEGLYGLUSERALALEUGLUGLULEU
14   CYSARGLYSTHRLEUCYSTHRASNTHRVAL
15   HISGLYGLYILEHISILETYRVALLEUSER
16   ASNASPILEPROPROHISLYSILEASNPRO
17   LEUPHEGLUGLUASNGLYLYSGLYILEILE
18   ASPLEUGLNSERTYRASNSERTYRVALLEU
19   GLYLEUGLYSERCYSVALASNHISLEUHIS
20   CYSTHRTHRASPLYSCYSPROTRPLYSGLU
21   GLNASNTYRTHRTHRCYSTYRTHRLEUTYR
22   ASNGLULEULYSGLUILESERLYSVALASP
23   LEULYSSERLEULEUARGPHELEUALAGLU
24   LYSGLYLYSARGLEUGLYILETHRLEUSER
25   LYSTHRALALYSGLUTRPLEUGLUGLYLYS
26   LYSGLUGLUGLUASPTHRVALVALGLUPHE
27   GLUGLULEUARGLYSGLULEUVALLYSARG
28   ASPSERGLYLYSPROVALGLULYSILELYS
29   GLUGLUILECYSTHRLYSSERPROPROLYS
30   LEUILELYSGLUILEILECYSGLUASNLYS
31   THRTYRALAASPVALASNILEASPARGSER
32   ARGGLYASPTRPHISVALILELEUTYRLEU
33   METLYSHISGLYVALTHRASPPROASPLYS
34   ILELEUGLULEULEUPROARGASPSERLYS
35   ALALYSGLUASNGLULYSTRPASNTHRGLN
36   LYSTYRPHEVALILETHRLEUSERLYSALA
37   TRPSERVALVALLYSLYSTYRLEUGLUALA

Entity 2, ATP - C10 H16 N5 O13 P3 - 507.181 Da.

1   ATP

Samples:

sample_1: pRN1, [U-100% 13C; U-100% 15N], 400 mg/mL; ATP 400 mg/mL; DNA 400 mg/uL

sample_conditions_1: pH: 7; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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