BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25796

Title: NMR solution structure of a complex of PEP-19 bound to the C-domain of apo calmodulin   PubMed: 27876793

Deposition date: 2015-09-04 Original release date: 2016-11-28

Authors: Wang, Xu; Putkey, John

Citation: Wang, Xu; Putkey, John. "PEP-19 Modulates Calcium Binding to Calmodulin by Electrostatic Steering"  Nat. Commun. 7, 13583-13583 (2016).

Assembly members:
C-CaM, polymer, 73 residues, 8416.260 Da.
PEP-19, polymer, 62 residues, 6775.41 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
C-CaM: MKDTDSEEEIREAFRVFDKD GNGYISAAELRHVMTNLGEK LTDEEVDEMIREADIDGDGQ VNYEEFVQMMTAK
PEP-19: MAERQGAGATNGKDKTSGEN DGQKKVQEEFDIDMDAPETE RAAVAIQSQFRKFQKKKAGS QS

Data sets:
Data typeCount
13C chemical shifts430
15N chemical shifts112
1H chemical shifts716

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 73 residues - 8416.260 Da.

Isolated C-domain of calmodulin from residue M76 to K148

1   METLYSASPTHRASPSERGLUGLUGLUILE
2   ARGGLUALAPHEARGVALPHEASPLYSASP
3   GLYASNGLYTYRILESERALAALAGLULEU
4   ARGHISVALMETTHRASNLEUGLYGLULYS
5   LEUTHRASPGLUGLUVALASPGLUMETILE
6   ARGGLUALAASPILEASPGLYASPGLYGLN
7   VALASNTYRGLUGLUPHEVALGLNMETMET
8   THRALALYS

Entity 2, entity_2 62 residues - 6775.41 Da.

1   METALAGLUARGGLNGLYALAGLYALATHR
2   ASNGLYLYSASPLYSTHRSERGLYGLUASN
3   ASPGLYGLNLYSLYSVALGLNGLUGLUPHE
4   ASPILEASPMETASPALAPROGLUTHRGLU
5   ARGALAALAVALALAILEGLNSERGLNPHE
6   ARGLYSPHEGLNLYSLYSLYSALAGLYSER
7   GLNSER

Samples:

sample_1: C-CaM, [U-100% 13C; U-100% 15N], 0.8 mM; PEP_19 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; H2O 95%; D2O 5%

sample_2: PEP_19, [U-100% 13C; U-100% 15N], 0.8 mM; C-CaM 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; H2O 95%; D2O 5%

sample_3: C-CaM, [U-100% 13C; U-100% 15N], 0.8 mM; PEP_19 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; D2O 100%

sample_4: PEP-19, [U-100% 13C; U-100% 15N], 0.8 mM; C-CaM 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D F1--filtered, F3-edited NOESY-HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_1
3D CCH-TOCSYsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
D F1--filtered, F3-edited NOESY-HSQCsample_4isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

Felix_2007, Accelrys Software Inc. - data analysis

TOPSPIN v2.1, Bruker Biospin - collection, data analysis

NMR spectrometers:

  • 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