BMRB Entry 17867

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17867
MolProbity Validation Chart

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Title:
Structural Insight into the Unique Cardiac Myosin Binding Protein-C Motif: A Partially Folded Domain
Deposition date:
2011-08-18
Original release date:
2012-01-18
Authors:
Howarth, Jack; Rosevear, Paul; Ramisetti, Srini; Nolan, Kristof; Sadayappan, Sakthivel
Citation:

Citation: Howarth, Jack; Ramisetti, Srinivas; Nolan, Kristof; Sadayappan, Sakthivel; Rosevear, Paul. "Structural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAIN."  J. Biol. Chem. 287, 8254-8262 (2012).
PubMed: 22235120

Assembly members:

Assembly members:
Myosin Binding Protein-C Motif, polymer, 124 residues, 4189.856 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Myosin Binding Protein-C Motif: MGSSHHHHHHSSGLVPRGSH MHEAIGSGDLDLRSAFRRTS LAGAGRRTSDSHEDAGTLDF SSLLKKRDSFRRDSKLEAPA EEDVWEILRQAPPSEYERIA FQHGVTDLRGMLKRLKGMKQ DEKK

Data sets:
Data typeCount
13C chemical shifts298
15N chemical shifts100
1H chemical shifts210

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Myosin Binding Protein-C Motif1

Entities:

Entity 1, Myosin Binding Protein-C Motif 124 residues - 4189.856 Da.

Residues 1-20 represent a histidine tag.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METHISGLUALAILEGLYSERGLYASPLEU
4   ASPLEUARGSERALAPHEARGARGTHRSER
5   LEUALAGLYALAGLYARGARGTHRSERASP
6   SERHISGLUASPALAGLYTHRLEUASPPHE
7   SERSERLEULEULYSLYSARGASPSERPHE
8   ARGARGASPSERLYSLEUGLUALAPROALA
9   GLUGLUASPVALTRPGLUILELEUARGGLN
10   ALAPROPROSERGLUTYRGLUARGILEALA
11   PHEGLNHISGLYVALTHRASPLEUARGGLY
12   METLEULYSARGLEULYSGLYMETLYSGLN
13   ASPGLULYSLYS

Samples:

sample_1: myosin binding protein-C (255-357), [U-13C; U-15N], 1.0 mM; TRIS, [U-2H], 20.0 mM; sodium chloride 50.0 mM; TCEP 2.0 mM; EDTA 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

SPARKY, Goddard - chemical shift assignment

CS-Rosetta, Yang Shen, Robert Vernon, David Baker and Ad Bax - structure solution

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAE27506 BAE41061
GB AAC64202 AAI54409 EDL27527
PRF 2020397A
REF NP_032679 XP_006234565 XP_006234566 XP_006498945 XP_011237643

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