BMRB Entry 25681

Name: FBP28 WW E454Y
Published: 2015-10-19

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PDB ID: 2n4u
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25681
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 WW E454Y

Deposition date:

2015-07-01

Original release date:

2015-10-19

Authors:

Medina, Jordi; Macias, Maria J; Martin-Malpartida, Pau; Scheraga, Harold

Citation:

Citation: Maisuradze, Gia; Medina, Jordi; Kachlishvili, Khatuna; Krupa, Pawel; Mozolewska, Magdalena; Martin-Malpartida, Pau; Maisuradze, Luka; Macias, Maria J; Scheraga, Harold. "Preventing fibril formation of a protein by selective mutation" Proc. Natl. Acad. Sci. U.S.A. 112, 13549-13554 (2015).
PubMed: 26483482

Assembly members:

Assembly members:
entity, polymer, 37 residues, 4398.818 Da.

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GATAVSEWTEYKTADGKTYY YNNRTLYSTWEKPQELK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	25
15N chemical shifts	4
1H chemical shifts	199

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 37 residues - 4398.818 Da.

1

GLY

ALA

THR

ALA

VAL

SER

GLU

TRP

THR

GLU

2

TYR

LYS

THR

ALA

ASP

GLY

LYS

THR

TYR

3

TYR

ASN

ARG

THR

LEU

TYR

SER

THR

TRP

4

GLU

LYS

PRO

GLN

GLU

LEU

LYS

Samples:

sample_1: entity500 – 1000 uM; sodium phosphate 25 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.8; 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:

ARIA, Linge, O'Donoghue and Nilges - data analysis

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

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks