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 18614

Title: NMR solution structure of Myo10 anti-CC   PubMed: 23012428

Deposition date: 2012-07-25 Original release date: 2012-09-24

Authors: Ye, Fei; Lu, Qing; Zhang, Mingjie

Citation: Lu, Qing; Ye, Fei; Wei, Zhiyi; Wen, Zilong; Zhang, Mingjie. "Antiparallel coiled-coil-mediated dimerization of myosin X."  Proc. Natl. Acad. Sci. U.S.A. 109, 17388-17393 (2012).

Assembly members:
entity, polymer, 51 residues, 6339.12 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32

Entity Sequences (FASTA):
entity: ENKQVEEILRLEKEIEDLQR MKEQQELSLTEASLQKLQER RDQELRRLEEE

Data sets:
Data typeCount
13C chemical shifts155
15N chemical shifts51
1H chemical shifts329

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Myo10 anti-CC, 11
2Myo10 anti-CC, 21

Entities:

Entity 1, Myo10 anti-CC, 1 51 residues - 6339.12 Da.

1   GLUASNLYSGLNVALGLUGLUILELEUARG
2   LEUGLULYSGLUILEGLUASPLEUGLNARG
3   METLYSGLUGLNGLNGLULEUSERLEUTHR
4   GLUALASERLEUGLNLYSLEUGLNGLUARG
5   ARGASPGLNGLULEUARGARGLEUGLUGLU
6   GLU

Samples:

sample_1: Myo10_anti-CC, [U-100% 13C; U-100% 15N], 0.8 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; 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 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - chemical shift assignment

PIPP, Garrett - chemical shift assignment

Molmol, Koradi, Billeter and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAA34519 BAG10382 BAH12170 BAH14509
EMBL CAH10611
GB AAF36524 AAF37875 AAF68025 AAI37169 AAI50286
REF NP_036466 XP_001175408 XP_002745141 XP_002804360 XP_003263225
SP Q9HD67
AlphaFold Q9HD67

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