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 19660

Title: Structure determination of the salamander courtship pheromone Plethodontid Modulating Factor   PubMed: 24849290

Authors: Wilburn, Damien; Bowen, Kathleen; Doty, Kari; Arumugam, Sengodagounder; Lane, Andrew; Feldhoff, Pamela; Feldhoff, Richard

Citation: Wilburn, Damien; Bowen, Kathleen; Doty, Kari; Arumugam, Sengodagounder; Lane, Andrew; Feldhoff, Pamela; Feldhoff, Richard. "Structural Insights into the Evolution of a Sexy Protein: Novel Topology and Restricted Backbone Flexibility in a Hypervariable Pheromone from the Red-Legged Salamander, Plethodon shermani."  PLoS ONE 9, e96975-e96975 (2014).

Assembly members:
rPMF-G, polymer, 57 residues, 6267.869 Da.

Natural source:   Common Name: red-legged salamander   Taxonomy ID: 263671   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Plethodon shermani

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris

Entity Sequences (FASTA):
rPMF-G: LQCNTLDGGTEECIPGIYNV CVHYKSEDEEYKSCGIQEEC EDAEGATVLCCPEDLCN

Data sets:
Data typeCount
13C chemical shifts171
15N chemical shifts56
1H chemical shifts352
H exchange rates57

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 57 residues - 6267.869 Da.

1   LEUGLNCYSASNTHRLEUASPGLYGLYTHR
2   GLUGLUCYSILEPROGLYILETYRASNVAL
3   CYSVALHISTYRLYSSERGLUASPGLUGLU
4   TYRLYSSERCYSGLYILEGLNGLUGLUCYS
5   GLUASPALAGLUGLYALATHRVALLEUCYS
6   CYSPROGLUASPLEUCYSASN

Samples:

sample_1: rPMF-G, [U-98% 15N], 2.2 mM; KCl 50 mM; NaPO4 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

PDB
GB AAQ13904 ABI48553 ABI48555 ABI48566 ABI48567