BMRB Entry 11291

Title:
Solution structure of the fibronectin type-III domain of mouse myosin-binding protein C, Fast-type homolog
Deposition date:
2010-08-09
Original release date:
2011-08-18
Authors:
Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the fibronectin type-III domain of mouse myosin-binding protein C, Fast-type homolog"  .

Assembly members:

Assembly members:
Fibronectin type-III domain, polymer, 111 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P041012-11

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts424
15N chemical shifts97
1H chemical shifts692

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fibronectin type-III domain1

Entities:

Entity 1, Fibronectin type-III domain 111 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROTHRSER
2   ALAPROGLNHISLEUTHRVALGLUASPVAL
3   THRASPTHRTHRTHRTHRLEULYSTRPARG
4   PROPROASPARGILEGLYALAGLYGLYILE
5   ASPGLYTYRLEUVALGLUTYRCYSLEUGLU
6   GLYSERGLUGLUTRPVALPROALAASNLYS
7   GLUPROVALGLUARGCYSGLYPHETHRVAL
8   LYSASPLEUPROTHRGLYALAARGILELEU
9   PHEARGVALVALGLYVALASNILEALAGLY
10   ARGSERGLUPROALATHRLEULEUGLNPRO
11   VALTHRILEARGGLUSERGLYPROSERSER
12   GLY

Samples:

sample_1: fn3 domain, [U-13C; U-15N], 1.47 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.9295, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 700 MHz

Related Database Links:

PDB

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