BMRB Entry 15107

Name: NMR structure of D4P/K7G mutant of GPM12
Published: 2008-06-25

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PDB ID: 2e4e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15107
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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 structure of D4P/K7G mutant of GPM12

Deposition date:

2007-01-22

Original release date:

2008-06-25

Authors:

Terada, T.; Satoh, D.; Mikawa, T.; Ito, Y.; Shimizu, K.

Citation:

Citation: Terada, Tohru; Satoh, Daisuke; Mikawa, Tsutomu; Ito, Yutaka; Shimizu, Kentaro. "Understanding the roles of amino acid residues in tertiary structure formation of chignolin by using molecular dynamics simulation" Proteins 73, 621-631 (2008).
PubMed: 18473359

Assembly members:

Assembly members:
GPM12, polymer, 10 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GPM12: GYDPATGTFG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	53

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GPM12	1

Entities:

Entity 1, GPM12 10 residues - Formula weight is not available

1

GLY

TYR

ASP

PRO

ALA

THR

GLY

THR

PHE

GLY

Samples:

sample: GPM12 2 mM; sodium phosphate 20 mM; D2O, [U-2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 277 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample	isotropic	sample_conditions_1
2D TOCSY	sample	isotropic	sample_conditions_1
2D ROESY	sample	isotropic	sample_conditions_1

Software:

xwinnmr v3.5, Bruker BioSpin Corporation - collection

AZARA v2.7, Wayne Boucher - processing

ANSIG v3.3 for OpenGL version 1.0.6, Per Kraulis, Takeshi Nishimura - data analysis

CNS v1.1, Axel T.Brunger et al. - refinement, structure solution

NMR spectrometers:

Bruker DRX 600 MHz