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 15758

Title: 1H, 13C and 15N backbone chemical shift assignments of the 4FNI-5FNI module pair from human fibronectin   PubMed: 19366708

Deposition date: 2008-05-06 Original release date: 2009-04-15

Authors: Vakonakis, Ioannis; Campbell, Iain

Citation: Vakonakis, Ioannis; Staunton, David; Ellis, Ian; Sarkies, Peter; Flanagan, Aleksandra; Schor, Ana; Schor, Seth; Campbell, Iain. "Motogenic sites in human fibronectin are masked by long range interactions"  J. Biol. Chem. 284, 15668-15675 (2009).

Assembly members:
4F15F1, polymer, 93 residues, 10519.6 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris   Vector: pPIC9K

Entity Sequences (FASTA):
4F15F1: AEKCFDHAAGTSYVVGETWE KPYQGWMMVDCTCLGEGSGR ITCTSRNRCNDQDTRTSYRI GDTWSKKDNRGNLLQCICTG NGRGEWKCERHTS

Data sets:
Data typeCount
13C chemical shifts175
15N chemical shifts96
1H chemical shifts98

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1protein1

Entities:

Entity 1, protein 93 residues - 10519.6 Da.

1   ALAGLULYSCYSPHEASPHISALAALAGLY
2   THRSERTYRVALVALGLYGLUTHRTRPGLU
3   LYSPROTYRGLNGLYTRPMETMETVALASP
4   CYSTHRCYSLEUGLYGLUGLYSERGLYARG
5   ILETHRCYSTHRSERARGASNARGCYSASN
6   ASPGLNASPTHRARGTHRSERTYRARGILE
7   GLYASPTHRTRPSERLYSLYSASPASNARG
8   GLYASNLEULEUGLNCYSILECYSTHRGLY
9   ASNGLYARGGLYGLUTRPLYSCYSGLUARG
10   HISTHRSER

Samples:

sample_1: 4F15F1, [U-98% 13C; U-98% 15N], 0.2 mM; D2O 5%; sodium azide 0.01%; sodium chloride 20 mM; sodium phosphate 20 mM; DSS 0.1 mM

sample_conditions_1: ionic strength: 115 mM; pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PIPP v4.3.7, Garrett - data analysis

TOPSPIN v1.3, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

PDB

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