BMRB Entry 30005

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30005
MolProbity Validation Chart

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Title:
Solution structure of coiled coil domain of myosin binding subunit of myosin light chain phosphatase
Deposition date:
2016-01-27
Original release date:
2016-03-14
Authors:
Sharma, A.; Birrane, G.; Anklin, C.; Rigby, A.; Pollak, M.; Alper, S.
Citation:

Citation: Sharma, A.; Rigby, A.; Sharma, A.; Rigby, A.. "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).
PubMed: 24693955

Assembly members:

Assembly members:
entity_1, polymer, 47 residues, 5358.105 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DFKKLYEQILAENEKLKAQL HDTNMELTDLKLQLEKATQR QERFARS

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

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 47 residues - 5358.105 Da.

1   ASPPHELYSLYSLEUTYRGLUGLNILELEU
2   ALAGLUASNGLULYSLEULYSALAGLNLEU
3   HISASPTHRASNMETGLULEUTHRASPLEU
4   LYSLEUGLNLEUGLULYSALATHRGLNARG
5   GLNGLUARGPHEALAARGSER

Samples:

sample_1: coiled coil mbs-1, [U-99% 13C; U-99% 15N], 1.0 mM; coiled coil mbs-2, [U-99% 15N], 1.0 mM; coiled coil mbs-3 1.0 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 ONLYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO) NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
isotope filtered 3D 1H-13C NOESYsample_1anisotropicsample_conditions_1
isotope filtered 3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
isotope filtered 2D NOESYsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

ANSIG, Kraulis - chemical shift assignment

Analysis v2.4.0, CCPN - chemical shift assignment

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

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 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