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 15756

Title: 1H, 13C and 15N backbone chemical shift assignments of the 2FNI-3FNI 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:
2F13F1, polymer, 89 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: recombinant technology   Host organism: Pichia pastoris   Vector: pPIC9K

Entity Sequences (FASTA):
2F13F1: EETCFDKYTGNTYRVGDTYE RPKDSMIWDCTCIGAGRGRI SCTIANRCHEGGQSYKIGDT WRRPHETGGYMLECVCLGNG KGEWTCKPI

Data sets:
Data typeCount
13C chemical shifts160
15N chemical shifts88
1H chemical shifts88

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1protein1

Entities:

Entity 1, protein 89 residues - Formula weight is not available

1   GLUGLUTHRCYSPHEASPLYSTYRTHRGLY
2   ASNTHRTYRARGVALGLYASPTHRTYRGLU
3   ARGPROLYSASPSERMETILETRPASPCYS
4   THRCYSILEGLYALAGLYARGGLYARGILE
5   SERCYSTHRILEALAASNARGCYSHISGLU
6   GLYGLYGLNSERTYRLYSILEGLYASPTHR
7   TRPARGARGPROHISGLUTHRGLYGLYTYR
8   METLEUGLUCYSVALCYSLEUGLYASNGLY
9   LYSGLYGLUTRPTHRCYSLYSPROILE

Samples:

sample_1: 2F13F1, [U-99% 13C; U-99% 15N], 0.3 mM; D2O 5%; DSS 0.1 mM; sodium azide 0.01%; sodium phosphate 20 mM; sodium chloride 20 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
2D 1H-13C 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

Omega Spectrometer Operating Software v6.0.3b2, Bruker Instruments - collection

NMR spectrometers:

  • N/A N/A 600 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