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 11290

Title: Solution structure of the fibronectin type-III domain of human fibronectin type III domain containing protein 3

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: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the fibronectin type-III domain of human fibronectin type III domain containing protein 3"  . ., .-..

Assembly members:
Fibronectin type-III domain, polymer, 109 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: cell free synthesis   Host organism: E. coli - cell free

Entity Sequences (FASTA):
Fibronectin type-III domain: GSSGSSGPSMPASPVLTKAG ITWLSLQWSKPSGTPSDEGI SYILEMEEETSGYGFKPKYD GEDLAYTVKNLRRSTKYKFK VIAYNSEGKSNPSEVVEFTT CPDSGPSSG

Data sets:
Data typeCount
13C chemical shifts437
15N chemical shifts93
1H chemical shifts668

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Fibronectin type-III domain1

Entities:

Entity 1, Fibronectin type-III domain 109 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROSERMET
2   PROALASERPROVALLEUTHRLYSALAGLY
3   ILETHRTRPLEUSERLEUGLNTRPSERLYS
4   PROSERGLYTHRPROSERASPGLUGLYILE
5   SERTYRILELEUGLUMETGLUGLUGLUTHR
6   SERGLYTYRGLYPHELYSPROLYSTYRASP
7   GLYGLUASPLEUALATYRTHRVALLYSASN
8   LEUARGARGSERTHRLYSTYRLYSPHELYS
9   VALILEALATYRASNSERGLUGLYLYSSER
10   ASNPROSERGLUVALVALGLUPHETHRTHR
11   CYSPROASPSERGLYPROSERSERGLY

Samples:

sample_1: fn3 domain, [U-13C; U-15N], 1.06 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 v2.6, 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 800 MHz

Related Database Links:

PDB

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