BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34114

Title: NMR Structural Characterisation of Pharmaceutically Relevant Proteins Obtained Through a Novel Recombinant Production: The Case of The Pulmonary Surfactant Polypeptide C Analogue rSP-C33Leu.   PubMed: 28534479

Deposition date: 2017-03-08 Original release date: 2017-06-02

Authors: Venturi, L.; Pioselli, B.; Johansson, J.; Rising, A.; Kronqvist, N.; Nordling, K.

Citation: Kronqvist, N.; Sarr, M.; Lindqvist, A.; Nordling, K.; Otikovs, M.; Venturi, L.; Pioselli, B.; Purhonen, P.; Landreh, M.; Biverstal, H.; Toleikis, Z.; Sjoberg, L.; Robinson, C.; Pelizzi, N.; Jornvall, H.; Hebert, H.; Jaudzems, K.; Curstedt, T.; Rising, A.; Johansson, J.. "Efficient protein production inspired by how spiders make silk"  Nat. Commun. 8, 15504-15504 (2017).

Assembly members:
entity_1, polymer, 33 residues, 3600.728 Da.

Natural source:   Common Name: Pig   Taxonomy ID: 9823   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Sus scrofa

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: IPSSPVHLKRLKLLLLLLLL ILLLILGALLLGL

Data sets:
Data typeCount
13C chemical shifts41
15N chemical shifts31
1H chemical shifts295

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 33 residues - 3600.728 Da.

1   ILEPROSERSERPROVALHISLEULYSARG
2   LEULYSLEULEULEULEULEULEULEULEU
3   ILELEULEULEUILELEUGLYALALEULEU
4   LEUGLYLEU

Samples:

sample_1: entity_1 1.7 mM

sample_conditions_1: pH: 1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

OPAL v3.97, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker A 600 MHz

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