BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25010

Title: Structural Characterization of the Hypertrophic Cardiomyopathy-Related R502W Mutant of the C3 Domain of Cardiac Myosin Binding Protein-C   PubMed: 25058872

Deposition date: 2014-06-12 Original release date: 2014-07-28

Authors: Zhang, Xiaolu Linda; De, Soumya; McIntosh, Lawrence; Paetzel, Mark

Citation: Zhang, Xiaolu Linda; De, Soumya; McIntosh, Lawrence; Paetzel, Mark. "Structural Characterization of the C3 Domain of Cardiac Myosin Binding Protein C and Its Hypertrophic Cardiomyopathy-Related R502W Mutant."  Biochemistry 53, 5332-5342 (2014).

Assembly members:
entity, polymer, 95 residues, 10856.431 Da.

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

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

Entity Sequences (FASTA):
entity: GSHMPVLITRPLEDQLVMVG QRVEFECEVSEEGAQVKWLK DGVELTREETFKYWFKKDGQ RHHLIINEAMLEDAGHYALC TSGGQALAELIVQEK

Data sets:
Data typeCount
1H chemical shifts670
13C chemical shifts326
15N chemical shifts100

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 95 residues - 10856.431 Da.

1   GLYSERHISMETPROVALLEUILETHRARG
2   PROLEUGLUASPGLNLEUVALMETVALGLY
3   GLNARGVALGLUPHEGLUCYSGLUVALSER
4   GLUGLUGLYALAGLNVALLYSTRPLEULYS
5   ASPGLYVALGLULEUTHRARGGLUGLUTHR
6   PHELYSTYRTRPPHELYSLYSASPGLYGLN
7   ARGHISHISLEUILEILEASNGLUALAMET
8   LEUGLUASPALAGLYHISTYRALALEUCYS
9   THRSERGLYGLYGLNALALEUALAGLULEU
10   ILEVALGLNGLULYS

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; entity, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 298 K; pH: 6.5; pressure: 1 atm; ionic strength: 0.4 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 25007
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts