BMRB Entry 50920

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50920

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Title:
1H, 13C, and 15N Chemical Shift Assignments of cAMP-Binding Domains A and B of the PKA Regulatory Subunit
Deposition date:
2021-05-04
Original release date:
2021-06-13
Authors:
McNicholl, Tyler; Das, Rahul; SilDas, Soumita; Byun, Jung Ah; Akimoto, Madoka; Jafari, Naeimeh; Melacini, Giuseppe
Citation:

Citation: McNicholl, Tyler; Das, Rahul; SilDas, Soumita; Byun, Jung Ah; Akimoto, Madoka; Jafari, Naeimeh; Melacini, Giuseppe. "Backbone resonance assignment of the cAMP-binding domains of the protein kinase A regulatory subunit Ia"  Biomol. NMR Assign. 15, 379-382 (2021).
PubMed: 34118011

Assembly members:

Assembly members:
entity_1, polymer, 261 residues, Formula weight is not available
entity_CMP, non-polymer, 329.206 Da.

Natural source:

Natural source:   Common Name: cow   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRSET-B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DYKTMAALAKAIEKNVLFSH LDDNERSDIFDAMFPVSFIA GETVIQQGDEGDNFYVIDQG EMDVYVNNEWATSVGEGGSF GELALIYGTPRAATVKAKTN VKLWGIDRDSYRRILMGSTL RKRKMYEEFLSKVSILESLD KWERLTVADALEPVQFEDGQ KIVVQGEPGDEFFIILEGSA AVLQRRSENEEFVEVGRLGP SDYFGEIALLMNRPRAATVV ARGPLKCVKLDRPRFERVLG PCSDILKRNIQQYNSFVSLS V

Data sets:
Data typeCount
13C chemical shifts760
15N chemical shifts249
1H chemical shifts249

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cAMP-binding domains of PKA1
2cAMP2

Entities:

Entity 1, cAMP-binding domains of PKA 261 residues - Formula weight is not available

1   ASPTYRLYSTHRMETALAALALEUALALYS
2   ALAILEGLULYSASNVALLEUPHESERHIS
3   LEUASPASPASNGLUARGSERASPILEPHE
4   ASPALAMETPHEPROVALSERPHEILEALA
5   GLYGLUTHRVALILEGLNGLNGLYASPGLU
6   GLYASPASNPHETYRVALILEASPGLNGLY
7   GLUMETASPVALTYRVALASNASNGLUTRP
8   ALATHRSERVALGLYGLUGLYGLYSERPHE
9   GLYGLULEUALALEUILETYRGLYTHRPRO
10   ARGALAALATHRVALLYSALALYSTHRASN
11   VALLYSLEUTRPGLYILEASPARGASPSER
12   TYRARGARGILELEUMETGLYSERTHRLEU
13   ARGLYSARGLYSMETTYRGLUGLUPHELEU
14   SERLYSVALSERILELEUGLUSERLEUASP
15   LYSTRPGLUARGLEUTHRVALALAASPALA
16   LEUGLUPROVALGLNPHEGLUASPGLYGLN
17   LYSILEVALVALGLNGLYGLUPROGLYASP
18   GLUPHEPHEILEILELEUGLUGLYSERALA
19   ALAVALLEUGLNARGARGSERGLUASNGLU
20   GLUPHEVALGLUVALGLYARGLEUGLYPRO
21   SERASPTYRPHEGLYGLUILEALALEULEU
22   METASNARGPROARGALAALATHRVALVAL
23   ALAARGGLYPROLEULYSCYSVALLYSLEU
24   ASPARGPROARGPHEGLUARGVALLEUGLY
25   PROCYSSERASPILELEULYSARGASNILE
26   GLNGLNTYRASNSERPHEVALSERLEUSER
27   VAL

Entity 2, cAMP - C10 H12 N5 O6 P - 329.206 Da.

1   CMP

Samples:

sample_1: PKA regulatory subunit, [U-13C; U-15N], 0.5 mM; TCEP 1 mM; sodium azide 0.02%; MES 50 mM; ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE 2 mM; DTT 5 mM; sodium chloride 100 mM

sample_conditions_1: pH: 6.5; temperature: 306 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment

NMRPipe - processing

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