BMRB Entry 7128

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7128
MolProbity Validation Chart

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Title:
Fibronecting 1F3-2F3 backbone chemical shift assignments
Deposition date:
2006-05-23
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:
1F3-2F3, polymer, 201 residues, 22097 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):
1F3-2F3: SGPVEVFITETPSQPNSHPI QWNAPQPSHISKYILRWRPK NSVGRWKEATIPGHLNSYTI KGLKPGVVYEGQLISIQQYG HQEVTRFDFTTTSTSTPVTS NTVTGETTPFSPLVATSESV TEITASSFVVSWVSASDTVS GFRVEYELSEEGDEPQYLDL PSTATSVNIPDLLPGRKYIV NVYQISEDGEQSLILSTSQT T

Data sets:
Data typeCount
13C chemical shifts322
15N chemical shifts175
1H chemical shifts175

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
11F3-2F31

Entities:

Entity 1, 1F3-2F3 201 residues - 22097 Da.

This sequence corresponds to the first two type III domain on human Fibronectin and the connecting amino acid linker

1   SERGLYPROVALGLUVALPHEILETHRGLU
2   THRPROSERGLNPROASNSERHISPROILE
3   GLNTRPASNALAPROGLNPROSERHISILE
4   SERLYSTYRILELEUARGTRPARGPROLYS
5   ASNSERVALGLYARGTRPLYSGLUALATHR
6   ILEPROGLYHISLEUASNSERTYRTHRILE
7   LYSGLYLEULYSPROGLYVALVALTYRGLU
8   GLYGLNLEUILESERILEGLNGLNTYRGLY
9   HISGLNGLUVALTHRARGPHEASPPHETHR
10   THRTHRSERTHRSERTHRPROVALTHRSER
11   ASNTHRVALTHRGLYGLUTHRTHRPROPHE
12   SERPROLEUVALALATHRSERGLUSERVAL
13   THRGLUILETHRALASERSERPHEVALVAL
14   SERTRPVALSERALASERASPTHRVALSER
15   GLYPHEARGVALGLUTYRGLULEUSERGLU
16   GLUGLYASPGLUPROGLNTYRLEUASPLEU
17   PROSERTHRALATHRSERVALASNILEPRO
18   ASPLEULEUPROGLYARGLYSTYRILEVAL
19   ASNVALTYRGLNILESERGLUASPGLYGLU
20   GLNSERLEUILELEUSERTHRSERGLNTHR
21   THR

Samples:

sample_1: 1F3-2F3, [U-15N], 1.2 ± 0.2 mM; NaCl 150 mM; NaPi 20 mM; D2O 5%; H2O 95%

sample_2: 1F3-2F3, [U-13C; U-15N], 1 ± 0.1 ; NaCl 150 mM; NaPi 20 mM; D2O 5%; H2O 95%

conditions_1: ionic strength: 420 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
15N HSQCsample_1not availableconditions_1
CBCA(CO)NHsample_2not availableconditions_1
CBCANHsample_2not availableconditions_1
HNCAsample_2not availableconditions_1
HN(CO)CAsample_2not availableconditions_1

Software:

Omega Spectrometer Operating Software vBeta 6.0.3b2, GE/Bruker - Data collection

NMRPipe v2.3 Rev 2005.319.11.22, NIH/NIDDK - Data processing

PIPP v4.3.7, NIH - Data analysis

TOPSPIN v1.3, Bruker - Data collection

NMR spectrometers:

  • home build . 750 MHz
  • Bruker Avance II 500 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