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 4320

Title: 1H-15N and 1H-13C Dipolar Splittings and Calculated Dipolar Shifts for Reduced Clostridium Pasteurianum Rubredoxin

Authors: Volkman, Brian; Wilkens, Steven; Westler, William; Lee, Andrew; Beger, Richard; Xia, Bin; Markley, John

Citation: Volkman, Brian; Wilkens, Steven; Westler, William; Lee, Andrew; Beger, Richard; Xia, Bin; Markley, John. "Redox-dependent magnetic alignment of Clostridium pasterianum rubredoxin: measurement of magnetic susceptibility anisotropy and prediction of pseudocontact shift contributions"  J. Am. Chem. Soc. 121, 4677-4688 (1999).

Assembly members:
rubredoxin peptide, polymer, 54 residues, 6040 Da.
FE2, non-polymer, 55.845 Da.

Natural source:   Common Name: C. pasteurianum   Taxonomy ID: 1501   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Clostridium pasteurianum

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
rubredoxin peptide: MKKYTCTVCGYIYNPEDGDP DNGVNPGTDFKDIPDDWVCP LCGVGKDQFEEVEE

Data sets:
Data typeCount
coupling constants109
residual dipolar couplings53

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Reduced Rubredoxin1
2FE22

Entities:

Entity 1, Reduced Rubredoxin 54 residues - 6040 Da.

1   METLYSLYSTYRTHRCYSTHRVALCYSGLY
2   TYRILETYRASNPROGLUASPGLYASPPRO
3   ASPASNGLYVALASNPROGLYTHRASPPHE
4   LYSASPILEPROASPASPTRPVALCYSPRO
5   LEUCYSGLYVALGLYLYSASPGLNPHEGLU
6   GLUVALGLUGLU

Entity 2, FE2 - Fe - 55.845 Da.

1   FE2

Samples:

sample_one: rubredoxin peptide, [U-15N], 4 – 6 mM; phosphate buffer 50 mM

sample_two: rubredoxin peptide, [U-13C], 4 – 6 mM; phosphate buffer 50 mM

conditions_one: pH: 6.0; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
not availablesample_twonot availableconditions_one
not availablesample_onenot availableconditions_one

Software:

FELIX95, Molecular Simulations - process raw NMR spectral data from spectrometers

in-house FORTRAN program - Perform Levenberg-Marquart non-linear least-squares 2- 3- or 4-parameter fit of dipolar coupling data to extract one-bond NH or CH couplings.

NMR spectrometers:

  • Bruker DMX 750 MHz
  • Bruker DMX 400 MHz

Related Database Links:

BMRB 4050 4051 4066 4137 4182 4319
PDB
GB AAA23279 AJA49845 AJA53833 ELP57804 KER11884
REF WP_003447684
SP P00268