BMRB Entry 25177

Name: Solution Structure of a De Novo Designed Peptide that Sequesters Toxic Heavy Metals
Published: 2015-03-30

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PDB ID: 2mtq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25177
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of a De Novo Designed Peptide that Sequesters Toxic Heavy Metals PubMed: 25790102

Deposition date: 2014-08-28 Original release date: 2015-03-30

Authors: Plegaria, Jefferson; Zuiderweg, Erik; Stemmler, Timothy; Pecoraro, Vincent

Citation: Plegaria, Jefferson; Zuiderweg, Erik; Stemmler, Timothy; Pecoraro, Vincent. "Apoprotein Structure and Metal Binding Characterization of a De Novo Designed Peptide, alpha 3DIV, that Sequesters Toxic Heavy Metals" Biochemistry 54, 2858-2873 (2015).

Assembly members:
entity, polymer, 73 residues, 8090.151 Da.

Natural source: Common Name: E. coli Taxonomy ID: 469008 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: MGSWAEFKQRLAAIKTRCQA LGGSEAECAAFEKEIAAFES ELQAYKGKGNPEVEALRKEA AAIRDECQAYRHN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	298
15N chemical shifts	69
1H chemical shifts	457

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 73 residues - 8090.151 Da.

1

MET

GLY

SER

TRP

ALA

GLU

PHE

LYS

GLN

ARG

2

LEU

ALA

ILE

LYS

THR

ARG

CYS

GLN

ALA

3

LEU

GLY

SER

GLU

ALA

GLU

CYS

ALA

4

PHE

GLU

LYS

GLU

ILE

ALA

PHE

GLU

SER

5

GLU

LEU

GLN

ALA

TYR

LYS

GLY

LYS

GLY

ASN

6

PRO

GLU

VAL

GLU

ALA

LEU

ARG

LYS

GLU

ALA

7

ALA

ILE

ARG

ASP

GLU

CYS

GLN

ALA

TYR

8

ARG

HIS

ASN

Samples:

sample_1: sodium chloride 100 mM; sodium azide 0.5%; PMSF 0.05 mM; TCEP 0.8 mM; entity, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_2: sodium chloride 100 mM; sodium azide 0.5%; PMSF 0.05 mM; TCEP 0.8 mM; entity, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 273 K

sample_conditions_2: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_2

Software:

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

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

SPARKY, Goddard - data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

Agilent INOVA 800 MHz

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