BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25899

Title: Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil

Deposition date: 2015-11-12 Original release date: 2016-06-08

Authors: Vavra, K.; Xia, Youlin; Rock, Ronald

Citation: Vavra, K.; Xia, Youlin; Rock, Ronald. "Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection"  Biophys. J. 110, 2517-2527 (2016).

Assembly members:
entity, polymer, 69 residues, 8200.371 Da.

Natural source:   Common Name: cow   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

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

Entity Sequences (FASTA):
entity: GSHENKQVEEILRLEKEIED LQRMKERQELSLTEASLQKL QLEDKVEELLSKNYHLENEV ARLKKLVGE

Data sets:
Data typeCount
13C chemical shifts620
15N chemical shifts148
1H chemical shifts946

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 69 residues - 8200.371 Da.

1   GLYSERHISGLUASNLYSGLNVALGLUGLU
2   ILELEUARGLEUGLULYSGLUILEGLUASP
3   LEUGLNARGMETLYSGLUARGGLNGLULEU
4   SERLEUTHRGLUALASERLEUGLNLYSLEU
5   GLNLEUGLUASPLYSVALGLUGLULEULEU
6   SERLYSASNTYRHISLEUGLUASNGLUVAL
7   ALAARGLEULYSLYSLEUVALGLYGLU

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.1 mM; potassium phosphate 100 mM; EDTA 1 mM; sodium azide 0.03%

sample_conditions_1: ionic strength: 0.6 M; pH: 6.5; pressure: 1 atm; temperature: 35 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

Xplor-NIH v2.38, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

CCPN v2.4.1, CCPN - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Varian INOVA 600 MHz

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