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 19815

Title: NMR Assignment of Coiled Coil Domain of Myosin Binding Subunit of Myosin Light Chain Phosphatase   PubMed: 24693955

Deposition date: 2014-02-24 Original release date: 2014-03-24

Authors: SHARMA, ALOK; RIGBY, ALAN

Citation: Sharma, Alok; Rigby, Alan. "NMR Assignment and Secondary Structure of Coiled Coil Domain of C-terminal Myosin Binding Subunit of Myosin Phosphatase."  Protein Pept. Lett. 21, 639-645 (2014).

Assembly members:
COILED_COIL_DOMAIN_OF_MLCP, polymer, 50 residues, Formula weight is not available

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):
COILED_COIL_DOMAIN_OF_MLCP: DFKKLYEQILAENEKLKAQL HDTNMELTDLKLQLEKATQR QERFADRSLL

Data sets:
Data typeCount
1H chemical shifts346
13C chemical shifts206
15N chemical shifts50

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SUBUNIT 12A, 11
2SUBUNIT 12A, 21

Entities:

Entity 1, SUBUNIT 12A, 1 50 residues - Formula weight is not available

1   ASPPHELYSLYSLEUTYRGLUGLNILELEU
2   ALAGLUASNGLULYSLEULYSALAGLNLEU
3   HISASPTHRASNMETGLULEUTHRASPLEU
4   LYSLEUGLNLEUGLULYSALATHRGLNARG
5   GLNGLUARGPHEALAASPARGSERLEULEU

Samples:

sample_1: COILED COIL DOMAIN OF MLCP, [U-13C; U-15N], 1.0 mM; H2O 92%; D2O 8%

sample_conditions_1: ionic strength: 0.01 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA07201 BAA07202 BAA22378 BAB23563 BAC28990
EMBL CAH91185
GB AAB32730 AAB32731 AAI11753 AAI25382 AAI37631
REF NP_001137357 NP_001137358 NP_001231921 NP_001253022 NP_002471
SP O14974 Q10728 Q90623 Q9DBR7

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