BMRB Entry 25314

Name: FBP28 WW2 mutant Y238R L453A DNDC
Published: 2014-11-24

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PDB ID: 2mwe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25314
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:

FBP28 WW2 mutant Y238R L453A DNDC

Deposition date:

2014-11-04

Original release date:

2014-11-24

Authors:

Macias, Maria; Scheraga, Harold; Sunol, David; Todorovski, Toni

Citation:

Citation: Zhou, Rui; Maisuradze, Gia; Sunol, David; Todorovski, Toni; Macias, Maria; Xiao, Yi; Scheraga, Harold; Czaplewski, Cezary; Liwo, Adam. "Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements" Proc. Natl. Acad. Sci. U.S.A. 111, 18243-18248 (2014).
PubMed: 25489078

Assembly members:

Assembly members:
entity, polymer, 28 residues, 3417.664 Da.

Natural source:

Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGAT2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SEWTERKTADGKTYYYNNRT AESTWEKP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	168

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 28 residues - 3417.664 Da.

1

SER

GLU

TRP

THR

GLU

ARG

LYS

THR

ALA

ASP

2

GLY

LYS

THR

TYR

ASN

ARG

THR

3

ALA

GLU

SER

THR

TRP

GLU

LYS

PRO

Samples:

sample_1: entity 0.7 mM; sodium chloride 100 mM; sodium phosphate 20 mM; sodium azide 1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

Bruker Avance 600 MHz