BMRB Entry 19660

Name: Structure determination of the salamander courtship pheromone Plethodontid Modulating Factor
Published: 2014-01-02

Click here to enlarge.

PDB ID: 2mhy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19660
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Structure determination of the salamander courtship pheromone Plethodontid Modulating Factor

Deposition date:

2013-12-05

Original release date:

2014-01-02

Authors:

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

Citation:

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).
PubMed: 24849290

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
H_exch_rates
- H_exch_rate_list_1

Data type	Count
13C chemical shifts	171
15N chemical shifts	56
1H chemical shifts	352
H exchange rates	57

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 57 residues - 6267.869 Da.

1

LEU

GLN

CYS

ASN

THR

LEU

ASP

GLY

THR

2

GLU

CYS

ILE

PRO

GLY

ILE

TYR

ASN

VAL

3

CYS

VAL

HIS

TYR

LYS

SER

GLU

ASP

GLU

4

TYR

LYS

SER

CYS

GLY

ILE

GLN

GLU

CYS

5

GLU

ASP

ALA

GLU

GLY

ALA

THR

VAL

LEU

CYS

6

CYS

PRO

GLU

ASP

LEU

CYS

ASN

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_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

PDB	2MHY
GB	AAQ13904 ABI48553 ABI48555 ABI48566 ABI48567