BMRB Entry 25852

Title:
Structure and 15N relaxation data of Calmodulin bound to the endothelial Nitric Oxide Synthase Calmodulin Binding Domain Peptide at Physiological Calcium Concentration
Deposition date:
2015-10-16
Original release date:
2016-10-06
Authors:
Piazza, Michael; Guillemette, Guy; Dieckmann, Thorsten
Citation:

Citation: Piazza, Michael; Guillemette, Guy; Dieckmann, Thorsten. "Structure of Calmodulin bound to the endothelial Nitric Oxide Synthase Calmodulin Binding Domain Peptide at Physiological Calcium Concentration"  Biochem. Biophys. Res. Commun. ., .-..

Assembly members:

Assembly members:
CaM, polymer, 148 residues, 16721.465 Da.
eNOS, polymer, 22 residues, 2385.864 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: pET28a

Data sets:
Data typeCount
13C chemical shifts415
15N chemical shifts144
1H chemical shifts966
T1 relaxation values134
T2 relaxation values135
heteronuclear NOE values146
order parameters125

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CaM1
2eNOS2

Entities:

Entity 1, CaM 148 residues - 16721.465 Da.

1   ALAASPGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHESERLEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEASNGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUTHR
8   METMETALAARGLYSMETLYSASPTHRASP
9   SERGLUGLUGLUILEARGGLUALAPHEARG
10   VALPHEASPLYSASPGLYASNGLYTYRILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPGLUGLU
13   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, eNOS 22 residues - 2385.864 Da.

1   THRARGLYSLYSTHRPHELYSGLUVALALA
2   ASNALAVALLYSILESERALASERLEUMET
3   GLYTHR

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