BMRB Entry 34114

Name: NMR Structural Characterisation of Pharmaceutically Relevant Proteins Obtained Through a Novel Recombinant Production: The Case of The Pulmonary Surfactant Polypeptide C Analogue rSP-C33Leu.
Published: 2017-06-02

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PDB ID: 5nda
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34114
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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.

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:

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).
PubMed: 28534479

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IPSSPVHLKRLKLLLLLLLL ILLLILGALLLGL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	41
15N chemical shifts	31
1H chemical shifts	295

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 33 residues - 3600.728 Da.

1

ILE

PRO

SER

PRO

VAL

HIS

LEU

LYS

ARG

2

LEU

LYS

LEU

3

ILE

LEU

ILE

LEU

GLY

ALA

LEU

4

LEU

GLY

LEU

Samples:

sample_1: entity_1 1.7 mM

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks