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Biological Magnetic Resonance Data Bank


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BMRB Entry 51784

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51784
MolProbity Validation Chart

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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments of a Metal-Free Retinal Guanylyl Cyclase Activating Protein 5 (GCAP5) in Zebrafish Photoreceptors   PubMed: 37129703

Deposition date: 2023-01-11 Original release date: 2023-05-24

Authors: Cudia, Diana; Ahoulou, Effibe; Ames, James

Citation: Cudia, Diana; Ahoulou, Effibe; Ames, James. "Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation"  Biomol. NMR Assignments 17, 115-119 (2023).

Assembly members:
entity_1, polymer, 197 residues, Formula weight is not available
entity_MYR, non-polymer, 228.371 Da.

Natural source:   Common Name: zebrafish   Taxonomy ID: 7955   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Danio rerio

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):
entity_1: GDSSSMSATELSACKCHQWY RKFMTECPSGQLTFYEFKKF FGLKNLSEKSNAYVNTMFKT FDIDDDGCIDFMEYVAALSL VLKGGVQQKLRWYFKLFDMD GSGCIDKDELLLIFKAVQAI NGAEPEISAEDLADIVFNKI DVNGDGELSLEEFMEGISAD EKISEMLTQSLDLTRIVSNI YNDSYIEQEAEIIEDQA

Data sets:
Data typeCount
13C chemical shifts547
15N chemical shifts190
1H chemical shifts684

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1apo-GCAP5 WT1
2myristic acid2

Entities:

Entity 1, apo-GCAP5 WT 197 residues - Formula weight is not available

1   GLYASPSERSERSERMETSERALATHRGLU
2   LEUSERALACYSLYSCYSHISGLNTRPTYR
3   ARGLYSPHEMETTHRGLUCYSPROSERGLY
4   GLNLEUTHRPHETYRGLUPHELYSLYSPHE
5   PHEGLYLEULYSASNLEUSERGLULYSSER
6   ASNALATYRVALASNTHRMETPHELYSTHR
7   PHEASPILEASPASPASPGLYCYSILEASP
8   PHEMETGLUTYRVALALAALALEUSERLEU
9   VALLEULYSGLYGLYVALGLNGLNLYSLEU
10   ARGTRPTYRPHELYSLEUPHEASPMETASP
11   GLYSERGLYCYSILEASPLYSASPGLULEU
12   LEULEUILEPHELYSALAVALGLNALAILE
13   ASNGLYALAGLUPROGLUILESERALAGLU
14   ASPLEUALAASPILEVALPHEASNLYSILE
15   ASPVALASNGLYASPGLYGLULEUSERLEU
16   GLUGLUPHEMETGLUGLYILESERALAASP
17   GLULYSILESERGLUMETLEUTHRGLNSER
18   LEUASPLEUTHRARGILEVALSERASNILE
19   TYRASNASPSERTYRILEGLUGLNGLUALA
20   GLUILEILEGLUASPGLNALA

Entity 2, myristic acid - C14 H28 O2 - 228.371 Da.

1   MYR

Samples:

sample_1: apo-GCAP5 WT, [U-99% 15N], 0.75 mM; Tris-d11, [U-99% 2H], 5 mM; DTT-d10, [U-99% 2H], 2 mM

sample_2: apo-GCAP5 WT, [U-99% 13C; U-99% 15N], 0.75 mM; Tris-d11, [U-99% 2H], 5 mM; DTT-d10, [U-99% 2H], 2 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
2D HBCBCGCDHDsample_2isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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