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 18879

Title: SP-B C-terminal (residues 59-80) peptide in DPC micelles

Deposition date: 2012-12-06 Original release date: 2013-12-16

Authors: Kuznetsova, Anna; Vanni, Julieann; Long, Joanna

Citation: Kuznetsova, Anna; Vanni, Julieann; Long, Joanna. "Solution NMR structures of the C-terminal segment of surfactant protein B (residues 59-80) in DPC detergent micelles and methanol."  Biochemistry ., .-..

Assembly members:
entity, polymer, 22 residues, 2500.072 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity: DTLLGRILPQLVCRLVLRCS ID

Data sets:
Data typeCount
15N chemical shifts24
1H chemical shifts173

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SP-B1

Entities:

Entity 1, SP-B 22 residues - 2500.072 Da.

there is homoserine lactone residue (HSL) at the end of the sequence after D80 that is left due to cyanogen bromide cleavage of the peptide from fusion construct at the methionines before D59 and after D80

1   ASPTHRLEULEUGLYARGILELEUPROGLN
2   LEUVALCYSARGLEUVALLEUARGCYSSER
3   ILEASP

Samples:

SP-B_residues_59-80_in_DPC_micelles: entity, [U-100% 15N], 1.2 mM; D2O, [U-100% 2H], 5%; DPC, [U-100% 2H], 80 mM; TSP 1 mM; sodium phosphate 50 mM; H2O 95%

315K: ionic strength: 130 mM; pH: 4.5; pressure: 1 atm; temperature: 315 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSP-B_residues_59-80_in_DPC_micellesisotropic315K
2D 1H-1H TOCSYSP-B_residues_59-80_in_DPC_micellesisotropic315K
2D 1H-1H NOESYSP-B_residues_59-80_in_DPC_micellesisotropic315K
3D 1H-15N TOCSYSP-B_residues_59-80_in_DPC_micellesisotropic315K
3D 1H-15N NOESYSP-B_residues_59-80_in_DPC_micellesisotropic315K

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

X-PLOR NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TOPSPIN, Bruker Biospin - collection, data analysis

MolProbity, Ian W. Davis, Vincent B. Chen, Robert M. Immormino et. al - evaluation of structure refinement, structure evaluation

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts