BMRB Entry 30100

Title:
The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C
Deposition date:
2016-05-25
Original release date:
2016-11-04
Authors:
Michie, K.; Kwan, A.; Tung, C.; Guss, J.; Trewhella, J.
Citation:

Citation: Michie, K.; Kwan, A.; Tung, C.; Guss, J.; Trewhella, J.. "A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C"  Structure 24, 2000-2007 (2016).
PubMed: 27720588

Assembly members:

Assembly members:
Myosin-binding protein C, cardiac-type, polymer, 137 residues, 15497.698 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: pETM

Data typeCount
13C chemical shifts582
15N chemical shifts147
1H chemical shifts972

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 137 residues - 15497.698 Da.

1   GLYPROGLYSERGLUASPVALTRPGLUILE
2   LEUARGGLNALAPROPROSERGLUTYRGLU
3   ARGILEALAPHEGLNTYRGLYVALTHRASP
4   LEUARGGLYMETLEULYSARGLEULYSGLY
5   METARGARGASPGLULYSLYSSERTHRALA
6   PHEGLNLYSLYSLEUGLUPROALATYRGLN
7   VALSERLYSGLYHISLYSILEARGLEUTHR
8   VALGLULEUALAASPHISASPALAGLUVAL
9   LYSTRPLEULYSASNGLYGLNGLUILEGLN
10   METSERGLYSERLYSTYRILEPHEGLUSER
11   ILEGLYALALYSARGTHRLEUTHRILESER
12   GLNCYSSERLEUALAASPASPALAALATYR
13   GLNCYSVALVALGLYGLYGLULYSCYSSER
14   THRGLULEUPHEVALLYSGLU

Samples:

sample_2: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 412 uM; H2O 95%; D2O 5%

sample_3: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 920 uM; H2O 95%; D2O 5%

sample_4: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 550 uM; H2O 95%; D2O 5%

sample_5: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 500 uM; H2O 1%; D2O 99%

sample_6: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 800 uM; H2O 1%; D2O 99%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
HCC(CO)NH TOCSYsample_3isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_5isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
CC(CO)NH-TOCSYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D 13C NOESY aromaticsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_6isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1
3D 13C NOESY aliphaticsample_5isotropicsample_conditions_1
3D HCC TOCSY aromaticsample_6isotropicsample_conditions_1
2D HBCBCGCDHDsample_5isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D hCCH-TOCSYsample_6isotropicsample_conditions_1
3D HcCH-TOCSYsample_4isotropicsample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, peak picking

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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