BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27705

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Guanylate Cyclase Activating Protein-5 (GCAP5) in Zebrafish Photoreceptors   PubMed: 30559291

Deposition date: 2018-11-26 Original release date: 2019-01-08

Authors: Cudia, Diana; Ames, James

Citation: Peshenko, Igor; Yu, Qinhong; Lim, Sunghyuk; Cudia, Diana; Dizhoor, Alexander; Ames, James. "Retinal degeneration 3 (RD3) protein, a retinal guanylyl cyclase regulator, forms a monomeric and elongated four helix bundle"  J. Biol. Chem. 94, 2318-2328 (2019).

Assembly members:
GCAP5, polymer, 198 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
GCAP5: MGDSSSMSATELSACKCHQW YRKFMTECPSGQLTFYEFKK FFGLKNLSEKSNAYVNTMFK TFDIDDDGCIDFMEYVAALS LVLKGGVQQKLRWYFKLFDM DGSGCIDKDELLLIFKAVQA INGAEPEISAEDLADIVFNK IDVNGDGELSLEEFMEGISA DEKISEMLTQSLDLTRIVSN IYNDSYIEQEAEIIEDQA

Data sets:
Data typeCount
13C chemical shifts579
15N chemical shifts160
1H chemical shifts812

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GCAP51

Entities:

Entity 1, GCAP5 198 residues - Formula weight is not available

1   METGLYASPSERSERSERMETSERALATHR
2   GLULEUSERALACYSLYSCYSHISGLNTRP
3   TYRARGLYSPHEMETTHRGLUCYSPROSER
4   GLYGLNLEUTHRPHETYRGLUPHELYSLYS
5   PHEPHEGLYLEULYSASNLEUSERGLULYS
6   SERASNALATYRVALASNTHRMETPHELYS
7   THRPHEASPILEASPASPASPGLYCYSILE
8   ASPPHEMETGLUTYRVALALAALALEUSER
9   LEUVALLEULYSGLYGLYVALGLNGLNLYS
10   LEUARGTRPTYRPHELYSLEUPHEASPMET
11   ASPGLYSERGLYCYSILEASPLYSASPGLU
12   LEULEULEUILEPHELYSALAVALGLNALA
13   ILEASNGLYALAGLUPROGLUILESERALA
14   GLUASPLEUALAASPILEVALPHEASNLYS
15   ILEASPVALASNGLYASPGLYGLULEUSER
16   LEUGLUGLUPHEMETGLUGLYILESERALA
17   ASPGLULYSILESERGLUMETLEUTHRGLN
18   SERLEUASPLEUTHRARGILEVALSERASN
19   ILETYRASNASPSERTYRILEGLUGLNGLU
20   ALAGLUILEILEGLUASPGLNALA

Samples:

GCAP5_sample: GCAP5, [U-100% 13C; U-100% 15N], 500 mM; magnesium chloride, [U-100% 13C; U-100% 15N], 5 mM; MES 5 mM; DTT, [U-99% 2H], 3.5 mM; sodium azide 0.04 % w/v; D2O, [U-99% 2H], 7.5%; H2O 92.5%

sample_conditions_1: pH: 6.5; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCGCAP5_sampleisotropicsample_conditions_1
3D HNCOGCAP5_sampleisotropicsample_conditions_1
3D HNCACBGCAP5_sampleisotropicsample_conditions_1
3D CBCA(CO)NHGCAP5_sampleisotropicsample_conditions_1
3D HBHA(CO)NHGCAP5_sampleisotropicsample_conditions_1
3D HNCAGCAP5_sampleisotropicsample_conditions_1
3D HN(CO)CAGCAP5_sampleisotropicsample_conditions_1

Software:

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing, refinement

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts