BMRB Entry 30196

Title:
Solution structure of the CaM34 with the iNOS CaM binding domain peptide
Deposition date:
2016-10-19
Original release date:
2017-09-25
Authors:
Piazza, M.; Dieckmann, T.; Guillemette, J.
Citation:

Citation: Piazza, Michael; Taiakina, Valentina; Dieckmann, Thorsten; Guillemette, J Guy. "Structural Consequences of Calmodulin EF Hand Mutations."  Biochemistry 56, 944-956 (2017).
PubMed: 28121131

Assembly members:

Assembly members:
Calmodulin, polymer, 148 residues, 16633.330 Da.
Nitric oxide synthase, inducible, polymer, 29 residues, 3402.371 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

Data sets:
Data typeCount
13C chemical shifts438
15N chemical shifts161
1H chemical shifts1010

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 148 residues - 16633.330 Da.

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

Entity 2, entity_2 29 residues - 3402.371 Da.

1   ALAGLYHISMETARGPROLYSARGARGGLU
2   ILEPROLEULYSVALLEUVALLYSALAVAL
3   LEUPHEALACYSMETLEUMETARGLYS

Samples:

sample_1: CaM34, [U-99% 13C; U-99% 15N], 1 mM; Calcium chloride 10 mM; iNOS CaM binding domain peptide 1 mM; potassium chloride 100 mM; sodium azide 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
3D HNCAsample_1anisotropicsample_conditions_1
3D HCCH-TOCSYsample_1anisotropicsample_conditions_1
3D 1H-13C NOESYsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
2D 1H-15N double filtered NOESYsample_1anisotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

NMR spectrometers:

  • Bruker DRX 600 MHz

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