BMRB Entry 7127

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PDB ID: 2h41
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7127
MolProbity Validation Chart

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Title:
Fibronectin 2F3 chemical shift assignments
Deposition date:
2006-05-22
Original release date:
2007-05-29
Authors:
Vakonakis, Ioannis; Campbell, Iain
Citation:

Citation: Vakonakis, Ioannis; Staunton, David; Rooney, Luke; Campbell, Iain. "Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis."  EMBO J. 26, 2575-2583 (2007).
PubMed: 17464288

Assembly members:

Assembly members:
2F3, polymer, 95 residues, 9833.7 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Vector: pGEX-6P-3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
2F3: GPLGSHLVATSESVTEITAS SFVVSWVSASDTVSGFRVEY ELSEEGDEPQYLDLPSTATS VNIPDLLPGRKYIVNVYQIS EDGEQSLILSTSQTT

Data sets:
Data typeCount
13C chemical shifts318
15N chemical shifts97
1H chemical shifts645

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
12F31

Entities:

Entity 1, 2F3 95 residues - 9833.7 Da.

The 2F3 sequence corresponds to that of the second type III domain of fibronectin with an additional 6 non-canonical amino-terminal residues from the expression system

1   GLYPROLEUGLYSERHISLEUVALALATHR
2   SERGLUSERVALTHRGLUILETHRALASER
3   SERPHEVALVALSERTRPVALSERALASER
4   ASPTHRVALSERGLYPHEARGVALGLUTYR
5   GLULEUSERGLUGLUGLYASPGLUPROGLN
6   TYRLEUASPLEUPROSERTHRALATHRSER
7   VALASNILEPROASPLEULEUPROGLYARG
8   LYSTYRILEVALASNVALTYRGLNILESER
9   GLUASPGLYGLUGLNSERLEUILELEUSER
10   THRSERGLNTHRTHR

Related Database Links:

BMRB 7128
PDB 2H41 2H45 2HA1

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