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 15000

Title: Solution structure of chicken villin headpiece subdomain containing a fluorinated side chain in the core   PubMed: 17123960

Authors: Cornilescu, Claudia; Cornilescu, Gabriel; Hadley, Erik; Gellman, Samuel; Markley, John

Citation: Cornilescu, Gabriel; Hadley, Erik; Woll, Matthew; Markley, John; Gellman, Samuel; Cornilescu, Claudia. "Solution structure of a small protein containing a fluorinated side chain in the core."  Protein Sci. 16, 14-19 (2007).

Assembly members:
F5-Phe-cVHP, polymer, 35 residues, 1302.497 Da.

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
F5-Phe-cVHP: LSDEDFRAVXGMTRSAFANL PLWRQQNLRRERGLF

Data sets:
Data typeCount
13C chemical shifts77
15N chemical shifts40
1H chemical shifts223

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1F5-Phe-cVHP1

Entities:

Entity 1, F5-Phe-cVHP 35 residues - 1302.497 Da.

1   LEUSERASPGLUASPPHEARGALAVALPHF
2   GLYMETTHRARGSERALAPHEALAASNLEU
3   PROLEUTRPARGGLNGLNASNLEUARGARG
4   GLUARGGLYLEUPHE

Samples:

unlabeled_sample: F5-Phe-cVHP 4 mM

selectively_labeled_sample: F5-Phe-cVHP, [15N]-Ala, Phe, Leu, 2 mM

sample_conditions: ionic strength: 10 mM; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCunlabeled_sampleisotropicsample_conditions
2D 1H-13C HSQCunlabeled_sampleisotropicsample_conditions
2D COSYunlabeled_sampleisotropicsample_conditions
2D TOCSYunlabeled_sampleisotropicsample_conditions
2D NOESYunlabeled_sampleisotropicsample_conditions
2D 1H-15N HSQCselectively_labeled_sampleisotropicsample_conditions
2D HNCOselectively_labeled_sampleisotropicsample_conditions
2D HNCACBselectively_labeled_sampleisotropicsample_conditions
2D HNHAselectively_labeled_sampleisotropicsample_conditions
2D HNHBselectively_labeled_sampleisotropicsample_conditions
19F-HOESYunlabeled_sampleisotropicsample_conditions

Software:

NMRPipe, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing

PIPP, D Garrett - chemical shift assignment, data analysis, peak picking

SPARKY, T Goddard - chemical shift assignment

CYANA, P Guntert, C Mumenthaler and K Wuthrich - structure solution

X-PLOR NIH, CD Schwieters, JJ Kuszewski, N Tjandra and GM Clore - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 750 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

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