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 5600 6659 6660 6661 6662 6663 6664 6667 6668 6669 6670 6673 6674 6675 6676 6677 6678
PDB 1B13 1B2J 1BE7 1BFY 1C09 1FHH 1FHM 1IRN 1IRO 1R0F 1R0G 1R0H 1R0I 1R0J 1SMM 1SMU 1SMW 1T9O 1T9Q 4MBS
GB AAA23279 ELP57804 KER11884
REF WP_003447684
SP P00268