BMRB Entry 19604

Title:
1H, 13C, and 15N chemical shift assignments for the complex of calmodulin with minimal binding domain from HIV-1 matrix protein   PubMed: 24500712
Deposition date:
2013-11-07
Original release date:
2013-11-07
Authors:
Vlach, Jiri; Samal, Alexandra; Saad, Jamil
Citation:

Citation: Vlach, Jiri; Samal, Alexandra; Saad, Jamil. "Solution Structure of Calmodulin Bound to the Binding Domain of the HIV-1 Matrix Protein."  J. Biol. Chem. 289, 8697-8705 (2014).

Assembly members:

Assembly members:
calmodulin, polymer, 148 residues, 16721.465 Da.
MA8-43, polymer, 36 residues, 4317.116 Da.
CALCIUM ION, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: Norway Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7-7

Experimental source:

Natural source:   Common Name: Norway Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7-7

Data sets:
Data typeCount
13C chemical shifts632
15N chemical shifts197
1H chemical shifts1251

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1calmodulin1
2MA8-432
3CALCIUM ION_13
4CALCIUM ION_23
5CALCIUM ION_33
6CALCIUM ION_43

Entities:

Entity 1, calmodulin 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, MA8-43 36 residues - 4317.116 Da.

1   LEUSERGLYGLYGLULEUASPLYSTRPGLU
2   LYSILEARGLEUARGPROGLYGLYLYSLYS
3   GLNTYRLYSLEULYSHISILEVALTRPALA
4   SERARGGLULEUGLUARG

Entity 3, CALCIUM ION_1 - 40.078 Da.

1   CA

Samples:

sample_1: calmodulin, [U-95% 13C; U-95% 15N], 0.1 – 1.2 mM; MA8-430.1 – 1.2 mM; CALCIUM ION 5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.015 M; pH: 6.3; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

ANALYSIS v2.2, CCPN - chemical shift assignment, data analysis

CYANA vany, Guntert, Mumenthaler and Wuthrich - structure solution

NMRDraw vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectrum display

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

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

UNP P0DP29

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