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 6892

Title: Structure and influence on stability and activity of the N-terminal propetide part of lung surfactant protein C   PubMed: 16478467

Authors: Li, J.; Liepinsh, E.; Almlen, A.; Thyberg, J.; Curstedt, T.; Jornvall, H.; Johansson, J.

Citation: Li, J.; Liepinsh, E.; Almlen, A.; Thyberg, J.; Curstedt, T.; Jornvall, H.; Johansson, J.. "Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C"  FEBS J. 273, 926-935 (2006).

Assembly members:
lung surfactant protein C, polymer, 31 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: chemical synthesis

Entity Sequences (FASTA):
lung surfactant protein C: SPPDYSAAPRGRFGIPFFPV HLKRLLILLLX

Data sets:
Data typeCount
1H chemical shifts197

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lung surfactant protein C1

Entities:

Entity 1, lung surfactant protein C 31 residues - Formula weight is not available

1   SERPROPROASPTYRSERALAALAPROARG
2   GLYARGPHEGLYILEPROPHEPHEPROVAL
3   HISLEULYSARGLEULEUILELEULEULEU
4   NLW

Samples:

sample_1: lung surfactant protein C 0.5 mM; [2H38]dodecylphosphocholine (DPC) 35 mM; sodium phosphate buffer 50 mM; H2O 90%; D2O 10%

sample_2: lung surfactant protein C 0.5 mM; [2H5]-ethanol 100%

sample_cond_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 297 K

sample_cond_2: ionic strength: 0 M; pH: 7; pressure: 1 atm; temperature: 287 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
DQF-COSYnot availablenot availablenot available

Software:

VNMR v1.1.D - collection

PROSA v3.2 - processing

XEASY v3.0 - data analysis

DYANA v2.6 - structure solution

OPAL v3.0 - refinement

NMR spectrometers:

  • Bruker DMX 600 MHz

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