BMRB Entry 15430

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15430
MolProbity Validation Chart

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

Title:
The chemical shift assignment of gamma subunit of phosphodiesterase
Deposition date:
2007-08-14
Original release date:
2007-08-20
Authors:
Song, Jikui; Guo, Lian-Wang; Ruoho, Arnold; Markley, John
Citation:

Citation: Song, Jikui; Guo, Lian-Wang; Muradov, Hakim; Artemyev, Nikolai; Ruoho, Arnold; Markley, John. "Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure"  Proc. Natl. Acad. Sci. U. S. A. 105, 1505-1510 (2008).
PubMed: 18230733

Assembly members:

Assembly members:
PDEgamma, polymer, 87 residues, 13286.163 Da.

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: pTXBI

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PDEgamma: MNLEPPKAEIRSATRVMGGP VTPRKGPPKFKQRQTRQFKS KPPKKGVQGFGDDIPGMEGL GTDITVIAPWEAFNHLELHE LAQYGII

Data sets:
Data typeCount
13C chemical shifts325
15N chemical shifts77
1H chemical shifts443

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDEgamma1

Entities:

Entity 1, PDEgamma 87 residues - 13286.163 Da.

1   METASNLEUGLUPROPROLYSALAGLUILE
2   ARGSERALATHRARGVALMETGLYGLYPRO
3   VALTHRPROARGLYSGLYPROPROLYSPHE
4   LYSGLNARGGLNTHRARGGLNPHELYSSER
5   LYSPROPROLYSLYSGLYVALGLNGLYPHE
6   GLYASPASPILEPROGLYMETGLUGLYLEU
7   GLYTHRASPILETHRVALILEALAPROTRP
8   GLUALAPHEASNHISLEUGLULEUHISGLU
9   LEUALAGLNTYRGLYILEILE

Samples:

sample_1: PDEgamma, [U-100% 15N], 0.05 mM

sample_2: PDEgamma, [U-100% 13C; U-100% 15N], 0.09 mM

sample_3: PROXYL-PDEgamma, [U-15N], 0.05 mM

sample_4: PROXYL-PDEgamma, [U-100% 15N], 0.05 mM; Ascorbic Acid 5 mM

sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR, Varian - collection

SPARKY, Goddard - processing

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker DMX 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

EMBL CAA27821 CAA28507 CAA93815 CAD10146
GB AAA61950 AAB00116 AAB40379 EDM06834 EDM06835
PRF 1212259A
REF NP_001003235 NP_776846 XP_001081804 XP_001081805 XP_001488767
SP P04972 P54827 P61248
TPG DAA18226
AlphaFold P04972 P54827 P61248

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